data_9LHJ
# 
_entry.id   9LHJ 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9LHJ         pdb_00009lhj 10.2210/pdb9lhj/pdb 
WWPDB D_1300055605 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-05-14 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9LHJ 
_pdbx_database_status.recvd_initial_deposition_date   2025-01-12 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBC 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.email              zhoulu@fudan.edu.cn 
_pdbx_contact_author.name_first         Lu 
_pdbx_contact_author.name_last          Zhou 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-6807-2647 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Li, S.'   1 ? 
'Wu, X.'   2 ? 
'Zhou, L.' 3 ? 
'Lu, X.'   4 ? 
# 
_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                   GE 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Angew.Chem.Int.Ed.Engl. 
_citation.journal_id_ASTM           ACIEAY 
_citation.journal_id_CSD            0179 
_citation.journal_id_ISSN           1521-3773 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                e202505581 
_citation.page_last                 e202505581 
_citation.title                     
'Proteome-Wide Data Guides the Discovery of Lysine-Targeting Covalent Inhibitors Using DNA-Encoded Chemical Libraries.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1002/anie.202505581 
_citation.pdbx_database_id_PubMed   40223230 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Wu, X.'     1  ? 
primary 'Li, S.'     2  ? 
primary 'Liang, T.'  3  ? 
primary 'Yu, Q.'     4  ? 
primary 'Zhang, Y.'  5  ? 
primary 'Liu, J.'    6  ? 
primary 'Li, K.'     7  ? 
primary 'Liu, Z.'    8  ? 
primary 'Cui, M.'    9  ? 
primary 'Zhao, Y.'   10 ? 
primary 'Han, X.'    11 ? 
primary 'Jin, R.'    12 ? 
primary 'Tan, M.'    13 ? 
primary 'Chen, X.H.' 14 ? 
primary 'Zhao, Y.'   15 ? 
primary 'Zheng, M.'  16 ? 
primary 'Sun, Y.'    17 ? 
primary 'Zhou, L.'   18 ? 
primary 'Lu, X.'     19 ? 
# 
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 'Ubiquitin-conjugating enzyme E2 N'         17682.254 2   2.3.2.23 ? ? ? 
2 polymer man 'Ubiquitin-conjugating enzyme E2 variant 2' 16380.731 2   ?        ? ? ? 
3 water   nat water                                       18.015    592 ?        ? ? ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 
;Bendless-like ubiquitin-conjugating enzyme,E2 ubiquitin-conjugating enzyme N,Ubc13,UbcH13,Ubiquitin carrier protein N,Ubiquitin-protein ligase N
;
2 
;DDVit 1,Enterocyte differentiation-associated factor 1,EDAF-1,Enterocyte differentiation-promoting factor 1,EDPF-1,MMS2 homolog,Vitamin D3-inducible 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 yes 
;MAGLPRRIIKETQRLLAEPVPGIKAEPDESNARYFHVVIAGPQDSPFEGGTFKLELFLPEEYPMAAPKVRFMT(A1EJS)
IYHPNVDKLGRICLDILKDKWSPALQIRTVLLSIQALLSAPNPDDPLANDVAEQWKTNEAQAIETARAWTRLYAMNNI
;
;MAGLPRRIIKETQRLLAEPVPGIKAEPDESNARYFHVVIAGPQDSPFEGGTFKLELFLPEEYPMAAPKVRFMTXIYHPNV
DKLGRICLDILKDKWSPALQIRTVLLSIQALLSAPNPDDPLANDVAEQWKTNEAQAIETARAWTRLYAMNNI
;
A,B ? 
2 'polypeptide(L)' no no  
;MAVSTGVKVPRNFRLLEELEEGQKGVGDGTVSWGLEDDEDMTLTRWTGMIIGPPRTNYENRIYSLKVECGPKYPEAPPSV
RFVTKINMNGINNSSGMVDARSIPVLAKWQNSYSIKVVLQELRRLMMSKENMKLPQPPEGQTYNN
;
;MAVSTGVKVPRNFRLLEELEEGQKGVGDGTVSWGLEDDEDMTLTRWTGMIIGPPRTNYENRIYSLKVECGPKYPEAPPSV
RFVTKINMNGINNSSGMVDARSIPVLAKWQNSYSIKVVLQELRRLMMSKENMKLPQPPEGQTYNN
;
C,D ? 
# 
_pdbx_entity_nonpoly.entity_id   3 
_pdbx_entity_nonpoly.name        water 
_pdbx_entity_nonpoly.comp_id     HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET   n 
1 2   ALA   n 
1 3   GLY   n 
1 4   LEU   n 
1 5   PRO   n 
1 6   ARG   n 
1 7   ARG   n 
1 8   ILE   n 
1 9   ILE   n 
1 10  LYS   n 
1 11  GLU   n 
1 12  THR   n 
1 13  GLN   n 
1 14  ARG   n 
1 15  LEU   n 
1 16  LEU   n 
1 17  ALA   n 
1 18  GLU   n 
1 19  PRO   n 
1 20  VAL   n 
1 21  PRO   n 
1 22  GLY   n 
1 23  ILE   n 
1 24  LYS   n 
1 25  ALA   n 
1 26  GLU   n 
1 27  PRO   n 
1 28  ASP   n 
1 29  GLU   n 
1 30  SER   n 
1 31  ASN   n 
1 32  ALA   n 
1 33  ARG   n 
1 34  TYR   n 
1 35  PHE   n 
1 36  HIS   n 
1 37  VAL   n 
1 38  VAL   n 
1 39  ILE   n 
1 40  ALA   n 
1 41  GLY   n 
1 42  PRO   n 
1 43  GLN   n 
1 44  ASP   n 
1 45  SER   n 
1 46  PRO   n 
1 47  PHE   n 
1 48  GLU   n 
1 49  GLY   n 
1 50  GLY   n 
1 51  THR   n 
1 52  PHE   n 
1 53  LYS   n 
1 54  LEU   n 
1 55  GLU   n 
1 56  LEU   n 
1 57  PHE   n 
1 58  LEU   n 
1 59  PRO   n 
1 60  GLU   n 
1 61  GLU   n 
1 62  TYR   n 
1 63  PRO   n 
1 64  MET   n 
1 65  ALA   n 
1 66  ALA   n 
1 67  PRO   n 
1 68  LYS   n 
1 69  VAL   n 
1 70  ARG   n 
1 71  PHE   n 
1 72  MET   n 
1 73  THR   n 
1 74  A1EJS n 
1 75  ILE   n 
1 76  TYR   n 
1 77  HIS   n 
1 78  PRO   n 
1 79  ASN   n 
1 80  VAL   n 
1 81  ASP   n 
1 82  LYS   n 
1 83  LEU   n 
1 84  GLY   n 
1 85  ARG   n 
1 86  ILE   n 
1 87  CYS   n 
1 88  LEU   n 
1 89  ASP   n 
1 90  ILE   n 
1 91  LEU   n 
1 92  LYS   n 
1 93  ASP   n 
1 94  LYS   n 
1 95  TRP   n 
1 96  SER   n 
1 97  PRO   n 
1 98  ALA   n 
1 99  LEU   n 
1 100 GLN   n 
1 101 ILE   n 
1 102 ARG   n 
1 103 THR   n 
1 104 VAL   n 
1 105 LEU   n 
1 106 LEU   n 
1 107 SER   n 
1 108 ILE   n 
1 109 GLN   n 
1 110 ALA   n 
1 111 LEU   n 
1 112 LEU   n 
1 113 SER   n 
1 114 ALA   n 
1 115 PRO   n 
1 116 ASN   n 
1 117 PRO   n 
1 118 ASP   n 
1 119 ASP   n 
1 120 PRO   n 
1 121 LEU   n 
1 122 ALA   n 
1 123 ASN   n 
1 124 ASP   n 
1 125 VAL   n 
1 126 ALA   n 
1 127 GLU   n 
1 128 GLN   n 
1 129 TRP   n 
1 130 LYS   n 
1 131 THR   n 
1 132 ASN   n 
1 133 GLU   n 
1 134 ALA   n 
1 135 GLN   n 
1 136 ALA   n 
1 137 ILE   n 
1 138 GLU   n 
1 139 THR   n 
1 140 ALA   n 
1 141 ARG   n 
1 142 ALA   n 
1 143 TRP   n 
1 144 THR   n 
1 145 ARG   n 
1 146 LEU   n 
1 147 TYR   n 
1 148 ALA   n 
1 149 MET   n 
1 150 ASN   n 
1 151 ASN   n 
1 152 ILE   n 
2 1   MET   n 
2 2   ALA   n 
2 3   VAL   n 
2 4   SER   n 
2 5   THR   n 
2 6   GLY   n 
2 7   VAL   n 
2 8   LYS   n 
2 9   VAL   n 
2 10  PRO   n 
2 11  ARG   n 
2 12  ASN   n 
2 13  PHE   n 
2 14  ARG   n 
2 15  LEU   n 
2 16  LEU   n 
2 17  GLU   n 
2 18  GLU   n 
2 19  LEU   n 
2 20  GLU   n 
2 21  GLU   n 
2 22  GLY   n 
2 23  GLN   n 
2 24  LYS   n 
2 25  GLY   n 
2 26  VAL   n 
2 27  GLY   n 
2 28  ASP   n 
2 29  GLY   n 
2 30  THR   n 
2 31  VAL   n 
2 32  SER   n 
2 33  TRP   n 
2 34  GLY   n 
2 35  LEU   n 
2 36  GLU   n 
2 37  ASP   n 
2 38  ASP   n 
2 39  GLU   n 
2 40  ASP   n 
2 41  MET   n 
2 42  THR   n 
2 43  LEU   n 
2 44  THR   n 
2 45  ARG   n 
2 46  TRP   n 
2 47  THR   n 
2 48  GLY   n 
2 49  MET   n 
2 50  ILE   n 
2 51  ILE   n 
2 52  GLY   n 
2 53  PRO   n 
2 54  PRO   n 
2 55  ARG   n 
2 56  THR   n 
2 57  ASN   n 
2 58  TYR   n 
2 59  GLU   n 
2 60  ASN   n 
2 61  ARG   n 
2 62  ILE   n 
2 63  TYR   n 
2 64  SER   n 
2 65  LEU   n 
2 66  LYS   n 
2 67  VAL   n 
2 68  GLU   n 
2 69  CYS   n 
2 70  GLY   n 
2 71  PRO   n 
2 72  LYS   n 
2 73  TYR   n 
2 74  PRO   n 
2 75  GLU   n 
2 76  ALA   n 
2 77  PRO   n 
2 78  PRO   n 
2 79  SER   n 
2 80  VAL   n 
2 81  ARG   n 
2 82  PHE   n 
2 83  VAL   n 
2 84  THR   n 
2 85  LYS   n 
2 86  ILE   n 
2 87  ASN   n 
2 88  MET   n 
2 89  ASN   n 
2 90  GLY   n 
2 91  ILE   n 
2 92  ASN   n 
2 93  ASN   n 
2 94  SER   n 
2 95  SER   n 
2 96  GLY   n 
2 97  MET   n 
2 98  VAL   n 
2 99  ASP   n 
2 100 ALA   n 
2 101 ARG   n 
2 102 SER   n 
2 103 ILE   n 
2 104 PRO   n 
2 105 VAL   n 
2 106 LEU   n 
2 107 ALA   n 
2 108 LYS   n 
2 109 TRP   n 
2 110 GLN   n 
2 111 ASN   n 
2 112 SER   n 
2 113 TYR   n 
2 114 SER   n 
2 115 ILE   n 
2 116 LYS   n 
2 117 VAL   n 
2 118 VAL   n 
2 119 LEU   n 
2 120 GLN   n 
2 121 GLU   n 
2 122 LEU   n 
2 123 ARG   n 
2 124 ARG   n 
2 125 LEU   n 
2 126 MET   n 
2 127 MET   n 
2 128 SER   n 
2 129 LYS   n 
2 130 GLU   n 
2 131 ASN   n 
2 132 MET   n 
2 133 LYS   n 
2 134 LEU   n 
2 135 PRO   n 
2 136 GLN   n 
2 137 PRO   n 
2 138 PRO   n 
2 139 GLU   n 
2 140 GLY   n 
2 141 GLN   n 
2 142 THR   n 
2 143 TYR   n 
2 144 ASN   n 
2 145 ASN   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' 1 152 human ? 'UBE2N, BLU'         ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 
'Escherichia coli' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 145 human ? 'UBE2V2, MMS2, UEV2' ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? 
'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 
A1EJS 'L-peptide linking' n 
;(2S)-2-azanyl-6-[[2-[[4-[(5-fluoranyl-2-methoxycarbonyl-phenyl)amino]-2-[[3-(1-methylimidazol-2-yl)phenyl]methylamino]pyrimidin-5-yl]amino]-3,4-bis(oxidanylidene)cyclobuten-1-yl]amino]hexanoic acid
;
? 'C33 H34 F N9 O6' 671.678 
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 
CYS   'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S'    121.158 
GLN   'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3'    146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'      147.129 
GLY   'peptide linking'   y GLYCINE ? 'C2 H5 N O2'      75.067  
HIS   'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1'  156.162 
HOH   non-polymer         . WATER ? 'H2 O'            18.015  
ILE   'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2'     131.173 
LEU   'L-peptide linking' y LEUCINE ? 'C6 H13 N O2'     131.173 
LYS   'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1'  147.195 
MET   'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S'   149.211 
PHE   'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2'     165.189 
PRO   'L-peptide linking' y PROLINE ? 'C5 H9 N O2'      115.130 
SER   'L-peptide linking' y SERINE ? 'C3 H7 N O3'      105.093 
THR   'L-peptide linking' y THREONINE ? 'C4 H9 N O3'      119.119 
TRP   'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2'   204.225 
TYR   'L-peptide linking' y TYROSINE ? 'C9 H11 N O3'     181.189 
VAL   'L-peptide linking' y VALINE ? 'C5 H11 N O2'     117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET   1   1   ?   ?     ?   A . n 
A 1 2   ALA   2   2   ?   ?     ?   A . n 
A 1 3   GLY   3   3   3   GLY   GLY A . n 
A 1 4   LEU   4   4   4   LEU   LEU A . n 
A 1 5   PRO   5   5   5   PRO   PRO A . n 
A 1 6   ARG   6   6   6   ARG   ARG A . n 
A 1 7   ARG   7   7   7   ARG   ARG A . n 
A 1 8   ILE   8   8   8   ILE   ILE A . n 
A 1 9   ILE   9   9   9   ILE   ILE A . n 
A 1 10  LYS   10  10  10  LYS   LYS A . n 
A 1 11  GLU   11  11  11  GLU   GLU A . n 
A 1 12  THR   12  12  12  THR   THR A . n 
A 1 13  GLN   13  13  13  GLN   GLN A . n 
A 1 14  ARG   14  14  14  ARG   ARG A . n 
A 1 15  LEU   15  15  15  LEU   LEU A . n 
A 1 16  LEU   16  16  16  LEU   LEU A . n 
A 1 17  ALA   17  17  17  ALA   ALA A . n 
A 1 18  GLU   18  18  18  GLU   GLU A . n 
A 1 19  PRO   19  19  19  PRO   PRO A . n 
A 1 20  VAL   20  20  20  VAL   VAL A . n 
A 1 21  PRO   21  21  21  PRO   PRO A . n 
A 1 22  GLY   22  22  22  GLY   GLY A . n 
A 1 23  ILE   23  23  23  ILE   ILE A . n 
A 1 24  LYS   24  24  24  LYS   LYS A . n 
A 1 25  ALA   25  25  25  ALA   ALA A . n 
A 1 26  GLU   26  26  26  GLU   GLU A . n 
A 1 27  PRO   27  27  27  PRO   PRO A . n 
A 1 28  ASP   28  28  28  ASP   ASP A . n 
A 1 29  GLU   29  29  29  GLU   GLU A . n 
A 1 30  SER   30  30  30  SER   SER A . n 
A 1 31  ASN   31  31  31  ASN   ASN A . n 
A 1 32  ALA   32  32  32  ALA   ALA A . n 
A 1 33  ARG   33  33  33  ARG   ARG A . n 
A 1 34  TYR   34  34  34  TYR   TYR A . n 
A 1 35  PHE   35  35  35  PHE   PHE A . n 
A 1 36  HIS   36  36  36  HIS   HIS A . n 
A 1 37  VAL   37  37  37  VAL   VAL A . n 
A 1 38  VAL   38  38  38  VAL   VAL A . n 
A 1 39  ILE   39  39  39  ILE   ILE A . n 
A 1 40  ALA   40  40  40  ALA   ALA A . n 
A 1 41  GLY   41  41  41  GLY   GLY A . n 
A 1 42  PRO   42  42  42  PRO   PRO A . n 
A 1 43  GLN   43  43  43  GLN   GLN A . n 
A 1 44  ASP   44  44  44  ASP   ASP A . n 
A 1 45  SER   45  45  45  SER   SER A . n 
A 1 46  PRO   46  46  46  PRO   PRO A . n 
A 1 47  PHE   47  47  47  PHE   PHE A . n 
A 1 48  GLU   48  48  48  GLU   GLU A . n 
A 1 49  GLY   49  49  49  GLY   GLY A . n 
A 1 50  GLY   50  50  50  GLY   GLY A . n 
A 1 51  THR   51  51  51  THR   THR A . n 
A 1 52  PHE   52  52  52  PHE   PHE A . n 
A 1 53  LYS   53  53  53  LYS   LYS A . n 
A 1 54  LEU   54  54  54  LEU   LEU A . n 
A 1 55  GLU   55  55  55  GLU   GLU A . n 
A 1 56  LEU   56  56  56  LEU   LEU A . n 
A 1 57  PHE   57  57  57  PHE   PHE A . n 
A 1 58  LEU   58  58  58  LEU   LEU A . n 
A 1 59  PRO   59  59  59  PRO   PRO A . n 
A 1 60  GLU   60  60  60  GLU   GLU A . n 
A 1 61  GLU   61  61  61  GLU   GLU A . n 
A 1 62  TYR   62  62  62  TYR   TYR A . n 
A 1 63  PRO   63  63  63  PRO   PRO A . n 
A 1 64  MET   64  64  64  MET   MET A . n 
A 1 65  ALA   65  65  65  ALA   ALA A . n 
A 1 66  ALA   66  66  66  ALA   ALA A . n 
A 1 67  PRO   67  67  67  PRO   PRO A . n 
A 1 68  LYS   68  68  68  LYS   LYS A . n 
A 1 69  VAL   69  69  69  VAL   VAL A . n 
A 1 70  ARG   70  70  70  ARG   ARG A . n 
A 1 71  PHE   71  71  71  PHE   PHE A . n 
A 1 72  MET   72  72  72  MET   MET A . n 
A 1 73  THR   73  73  73  THR   THR A . n 
A 1 74  A1EJS 74  74  74  A1EJS UBE A . n 
A 1 75  ILE   75  75  75  ILE   ILE A . n 
A 1 76  TYR   76  76  76  TYR   TYR A . n 
A 1 77  HIS   77  77  77  HIS   HIS A . n 
A 1 78  PRO   78  78  78  PRO   PRO A . n 
A 1 79  ASN   79  79  79  ASN   ASN A . n 
A 1 80  VAL   80  80  80  VAL   VAL A . n 
A 1 81  ASP   81  81  81  ASP   ASP A . n 
A 1 82  LYS   82  82  82  LYS   LYS A . n 
A 1 83  LEU   83  83  83  LEU   LEU A . n 
A 1 84  GLY   84  84  84  GLY   GLY A . n 
A 1 85  ARG   85  85  85  ARG   ARG A . n 
A 1 86  ILE   86  86  86  ILE   ILE A . n 
A 1 87  CYS   87  87  87  CYS   CYS A . n 
A 1 88  LEU   88  88  88  LEU   LEU A . n 
A 1 89  ASP   89  89  89  ASP   ASP A . n 
A 1 90  ILE   90  90  90  ILE   ILE A . n 
A 1 91  LEU   91  91  91  LEU   LEU A . n 
A 1 92  LYS   92  92  92  LYS   LYS A . n 
A 1 93  ASP   93  93  93  ASP   ASP A . n 
A 1 94  LYS   94  94  94  LYS   LYS A . n 
A 1 95  TRP   95  95  95  TRP   TRP A . n 
A 1 96  SER   96  96  96  SER   SER A . n 
A 1 97  PRO   97  97  97  PRO   PRO A . n 
A 1 98  ALA   98  98  98  ALA   ALA A . n 
A 1 99  LEU   99  99  99  LEU   LEU A . n 
A 1 100 GLN   100 100 100 GLN   GLN A . n 
A 1 101 ILE   101 101 101 ILE   ILE A . n 
A 1 102 ARG   102 102 102 ARG   ARG A . n 
A 1 103 THR   103 103 103 THR   THR A . n 
A 1 104 VAL   104 104 104 VAL   VAL A . n 
A 1 105 LEU   105 105 105 LEU   LEU A . n 
A 1 106 LEU   106 106 106 LEU   LEU A . n 
A 1 107 SER   107 107 107 SER   SER A . n 
A 1 108 ILE   108 108 108 ILE   ILE A . n 
A 1 109 GLN   109 109 109 GLN   GLN A . n 
A 1 110 ALA   110 110 110 ALA   ALA A . n 
A 1 111 LEU   111 111 111 LEU   LEU A . n 
A 1 112 LEU   112 112 112 LEU   LEU A . n 
A 1 113 SER   113 113 113 SER   SER A . n 
A 1 114 ALA   114 114 114 ALA   ALA A . n 
A 1 115 PRO   115 115 115 PRO   PRO A . n 
A 1 116 ASN   116 116 116 ASN   ASN A . n 
A 1 117 PRO   117 117 117 PRO   PRO A . n 
A 1 118 ASP   118 118 118 ASP   ASP A . n 
A 1 119 ASP   119 119 119 ASP   ASP A . n 
A 1 120 PRO   120 120 ?   ?     ?   A . n 
A 1 121 LEU   121 121 ?   ?     ?   A . n 
A 1 122 ALA   122 122 122 ALA   ALA A . n 
A 1 123 ASN   123 123 123 ASN   ASN A . n 
A 1 124 ASP   124 124 124 ASP   ASP A . n 
A 1 125 VAL   125 125 125 VAL   VAL A . n 
A 1 126 ALA   126 126 126 ALA   ALA A . n 
A 1 127 GLU   127 127 127 GLU   GLU A . n 
A 1 128 GLN   128 128 128 GLN   GLN A . n 
A 1 129 TRP   129 129 129 TRP   TRP A . n 
A 1 130 LYS   130 130 130 LYS   LYS A . n 
A 1 131 THR   131 131 131 THR   THR A . n 
A 1 132 ASN   132 132 132 ASN   ASN A . n 
A 1 133 GLU   133 133 133 GLU   GLU A . n 
A 1 134 ALA   134 134 134 ALA   ALA A . n 
A 1 135 GLN   135 135 135 GLN   GLN A . n 
A 1 136 ALA   136 136 136 ALA   ALA A . n 
A 1 137 ILE   137 137 137 ILE   ILE A . n 
A 1 138 GLU   138 138 138 GLU   GLU A . n 
A 1 139 THR   139 139 139 THR   THR A . n 
A 1 140 ALA   140 140 140 ALA   ALA A . n 
A 1 141 ARG   141 141 141 ARG   ARG A . n 
A 1 142 ALA   142 142 142 ALA   ALA A . n 
A 1 143 TRP   143 143 143 TRP   TRP A . n 
A 1 144 THR   144 144 144 THR   THR A . n 
A 1 145 ARG   145 145 145 ARG   ARG A . n 
A 1 146 LEU   146 146 146 LEU   LEU A . n 
A 1 147 TYR   147 147 147 TYR   TYR A . n 
A 1 148 ALA   148 148 148 ALA   ALA A . n 
A 1 149 MET   149 149 149 MET   MET A . n 
A 1 150 ASN   150 150 150 ASN   ASN A . n 
A 1 151 ASN   151 151 ?   ?     ?   A . n 
A 1 152 ILE   152 152 ?   ?     ?   A . n 
B 1 1   MET   1   1   ?   ?     ?   B . n 
B 1 2   ALA   2   2   ?   ?     ?   B . n 
B 1 3   GLY   3   3   3   GLY   GLY B . n 
B 1 4   LEU   4   4   4   LEU   LEU B . n 
B 1 5   PRO   5   5   5   PRO   PRO B . n 
B 1 6   ARG   6   6   6   ARG   ARG B . n 
B 1 7   ARG   7   7   7   ARG   ARG B . n 
B 1 8   ILE   8   8   8   ILE   ILE B . n 
B 1 9   ILE   9   9   9   ILE   ILE B . n 
B 1 10  LYS   10  10  10  LYS   LYS B . n 
B 1 11  GLU   11  11  11  GLU   GLU B . n 
B 1 12  THR   12  12  12  THR   THR B . n 
B 1 13  GLN   13  13  13  GLN   GLN B . n 
B 1 14  ARG   14  14  14  ARG   ARG B . n 
B 1 15  LEU   15  15  15  LEU   LEU B . n 
B 1 16  LEU   16  16  16  LEU   LEU B . n 
B 1 17  ALA   17  17  17  ALA   ALA B . n 
B 1 18  GLU   18  18  18  GLU   GLU B . n 
B 1 19  PRO   19  19  19  PRO   PRO B . n 
B 1 20  VAL   20  20  20  VAL   VAL B . n 
B 1 21  PRO   21  21  21  PRO   PRO B . n 
B 1 22  GLY   22  22  22  GLY   GLY B . n 
B 1 23  ILE   23  23  23  ILE   ILE B . n 
B 1 24  LYS   24  24  24  LYS   LYS B . n 
B 1 25  ALA   25  25  25  ALA   ALA B . n 
B 1 26  GLU   26  26  26  GLU   GLU B . n 
B 1 27  PRO   27  27  27  PRO   PRO B . n 
B 1 28  ASP   28  28  28  ASP   ASP B . n 
B 1 29  GLU   29  29  29  GLU   GLU B . n 
B 1 30  SER   30  30  30  SER   SER B . n 
B 1 31  ASN   31  31  31  ASN   ASN B . n 
B 1 32  ALA   32  32  32  ALA   ALA B . n 
B 1 33  ARG   33  33  33  ARG   ARG B . n 
B 1 34  TYR   34  34  34  TYR   TYR B . n 
B 1 35  PHE   35  35  35  PHE   PHE B . n 
B 1 36  HIS   36  36  36  HIS   HIS B . n 
B 1 37  VAL   37  37  37  VAL   VAL B . n 
B 1 38  VAL   38  38  38  VAL   VAL B . n 
B 1 39  ILE   39  39  39  ILE   ILE B . n 
B 1 40  ALA   40  40  40  ALA   ALA B . n 
B 1 41  GLY   41  41  41  GLY   GLY B . n 
B 1 42  PRO   42  42  42  PRO   PRO B . n 
B 1 43  GLN   43  43  43  GLN   GLN B . n 
B 1 44  ASP   44  44  44  ASP   ASP B . n 
B 1 45  SER   45  45  45  SER   SER B . n 
B 1 46  PRO   46  46  46  PRO   PRO B . n 
B 1 47  PHE   47  47  47  PHE   PHE B . n 
B 1 48  GLU   48  48  48  GLU   GLU B . n 
B 1 49  GLY   49  49  49  GLY   GLY B . n 
B 1 50  GLY   50  50  50  GLY   GLY B . n 
B 1 51  THR   51  51  51  THR   THR B . n 
B 1 52  PHE   52  52  52  PHE   PHE B . n 
B 1 53  LYS   53  53  53  LYS   LYS B . n 
B 1 54  LEU   54  54  54  LEU   LEU B . n 
B 1 55  GLU   55  55  55  GLU   GLU B . n 
B 1 56  LEU   56  56  56  LEU   LEU B . n 
B 1 57  PHE   57  57  57  PHE   PHE B . n 
B 1 58  LEU   58  58  58  LEU   LEU B . n 
B 1 59  PRO   59  59  59  PRO   PRO B . n 
B 1 60  GLU   60  60  60  GLU   GLU B . n 
B 1 61  GLU   61  61  61  GLU   GLU B . n 
B 1 62  TYR   62  62  62  TYR   TYR B . n 
B 1 63  PRO   63  63  63  PRO   PRO B . n 
B 1 64  MET   64  64  64  MET   MET B . n 
B 1 65  ALA   65  65  65  ALA   ALA B . n 
B 1 66  ALA   66  66  66  ALA   ALA B . n 
B 1 67  PRO   67  67  67  PRO   PRO B . n 
B 1 68  LYS   68  68  68  LYS   LYS B . n 
B 1 69  VAL   69  69  69  VAL   VAL B . n 
B 1 70  ARG   70  70  70  ARG   ARG B . n 
B 1 71  PHE   71  71  71  PHE   PHE B . n 
B 1 72  MET   72  72  72  MET   MET B . n 
B 1 73  THR   73  73  73  THR   THR B . n 
B 1 74  A1EJS 74  74  74  A1EJS UBE B . n 
B 1 75  ILE   75  75  75  ILE   ILE B . n 
B 1 76  TYR   76  76  76  TYR   TYR B . n 
B 1 77  HIS   77  77  77  HIS   HIS B . n 
B 1 78  PRO   78  78  78  PRO   PRO B . n 
B 1 79  ASN   79  79  79  ASN   ASN B . n 
B 1 80  VAL   80  80  80  VAL   VAL B . n 
B 1 81  ASP   81  81  81  ASP   ASP B . n 
B 1 82  LYS   82  82  82  LYS   LYS B . n 
B 1 83  LEU   83  83  83  LEU   LEU B . n 
B 1 84  GLY   84  84  84  GLY   GLY B . n 
B 1 85  ARG   85  85  85  ARG   ARG B . n 
B 1 86  ILE   86  86  86  ILE   ILE B . n 
B 1 87  CYS   87  87  87  CYS   CYS B . n 
B 1 88  LEU   88  88  88  LEU   LEU B . n 
B 1 89  ASP   89  89  89  ASP   ASP B . n 
B 1 90  ILE   90  90  90  ILE   ILE B . n 
B 1 91  LEU   91  91  91  LEU   LEU B . n 
B 1 92  LYS   92  92  92  LYS   LYS B . n 
B 1 93  ASP   93  93  93  ASP   ASP B . n 
B 1 94  LYS   94  94  94  LYS   LYS B . n 
B 1 95  TRP   95  95  95  TRP   TRP B . n 
B 1 96  SER   96  96  96  SER   SER B . n 
B 1 97  PRO   97  97  97  PRO   PRO B . n 
B 1 98  ALA   98  98  98  ALA   ALA B . n 
B 1 99  LEU   99  99  99  LEU   LEU B . n 
B 1 100 GLN   100 100 100 GLN   GLN B . n 
B 1 101 ILE   101 101 101 ILE   ILE B . n 
B 1 102 ARG   102 102 102 ARG   ARG B . n 
B 1 103 THR   103 103 103 THR   THR B . n 
B 1 104 VAL   104 104 104 VAL   VAL B . n 
B 1 105 LEU   105 105 105 LEU   LEU B . n 
B 1 106 LEU   106 106 106 LEU   LEU B . n 
B 1 107 SER   107 107 107 SER   SER B . n 
B 1 108 ILE   108 108 108 ILE   ILE B . n 
B 1 109 GLN   109 109 109 GLN   GLN B . n 
B 1 110 ALA   110 110 110 ALA   ALA B . n 
B 1 111 LEU   111 111 111 LEU   LEU B . n 
B 1 112 LEU   112 112 112 LEU   LEU B . n 
B 1 113 SER   113 113 113 SER   SER B . n 
B 1 114 ALA   114 114 114 ALA   ALA B . n 
B 1 115 PRO   115 115 115 PRO   PRO B . n 
B 1 116 ASN   116 116 116 ASN   ASN B . n 
B 1 117 PRO   117 117 117 PRO   PRO B . n 
B 1 118 ASP   118 118 118 ASP   ASP B . n 
B 1 119 ASP   119 119 119 ASP   ASP B . n 
B 1 120 PRO   120 120 120 PRO   PRO B . n 
B 1 121 LEU   121 121 ?   ?     ?   B . n 
B 1 122 ALA   122 122 122 ALA   ALA B . n 
B 1 123 ASN   123 123 123 ASN   ASN B . n 
B 1 124 ASP   124 124 124 ASP   ASP B . n 
B 1 125 VAL   125 125 125 VAL   VAL B . n 
B 1 126 ALA   126 126 126 ALA   ALA B . n 
B 1 127 GLU   127 127 127 GLU   GLU B . n 
B 1 128 GLN   128 128 128 GLN   GLN B . n 
B 1 129 TRP   129 129 129 TRP   TRP B . n 
B 1 130 LYS   130 130 130 LYS   LYS B . n 
B 1 131 THR   131 131 131 THR   THR B . n 
B 1 132 ASN   132 132 132 ASN   ASN B . n 
B 1 133 GLU   133 133 133 GLU   GLU B . n 
B 1 134 ALA   134 134 134 ALA   ALA B . n 
B 1 135 GLN   135 135 135 GLN   GLN B . n 
B 1 136 ALA   136 136 136 ALA   ALA B . n 
B 1 137 ILE   137 137 137 ILE   ILE B . n 
B 1 138 GLU   138 138 138 GLU   GLU B . n 
B 1 139 THR   139 139 139 THR   THR B . n 
B 1 140 ALA   140 140 140 ALA   ALA B . n 
B 1 141 ARG   141 141 141 ARG   ARG B . n 
B 1 142 ALA   142 142 142 ALA   ALA B . n 
B 1 143 TRP   143 143 143 TRP   TRP B . n 
B 1 144 THR   144 144 144 THR   THR B . n 
B 1 145 ARG   145 145 145 ARG   ARG B . n 
B 1 146 LEU   146 146 146 LEU   LEU B . n 
B 1 147 TYR   147 147 147 TYR   TYR B . n 
B 1 148 ALA   148 148 148 ALA   ALA B . n 
B 1 149 MET   149 149 149 MET   MET B . n 
B 1 150 ASN   150 150 150 ASN   ASN B . n 
B 1 151 ASN   151 151 ?   ?     ?   B . n 
B 1 152 ILE   152 152 ?   ?     ?   B . n 
C 2 1   MET   1   1   ?   ?     ?   C . n 
C 2 2   ALA   2   2   ?   ?     ?   C . n 
C 2 3   VAL   3   3   ?   ?     ?   C . n 
C 2 4   SER   4   4   ?   ?     ?   C . n 
C 2 5   THR   5   5   ?   ?     ?   C . n 
C 2 6   GLY   6   6   ?   ?     ?   C . n 
C 2 7   VAL   7   7   7   VAL   VAL C . n 
C 2 8   LYS   8   8   8   LYS   LYS C . n 
C 2 9   VAL   9   9   9   VAL   VAL C . n 
C 2 10  PRO   10  10  10  PRO   PRO C . n 
C 2 11  ARG   11  11  11  ARG   ARG C . n 
C 2 12  ASN   12  12  12  ASN   ASN C . n 
C 2 13  PHE   13  13  13  PHE   PHE C . n 
C 2 14  ARG   14  14  14  ARG   ARG C . n 
C 2 15  LEU   15  15  15  LEU   LEU C . n 
C 2 16  LEU   16  16  16  LEU   LEU C . n 
C 2 17  GLU   17  17  17  GLU   GLU C . n 
C 2 18  GLU   18  18  18  GLU   GLU C . n 
C 2 19  LEU   19  19  19  LEU   LEU C . n 
C 2 20  GLU   20  20  20  GLU   GLU C . n 
C 2 21  GLU   21  21  21  GLU   GLU C . n 
C 2 22  GLY   22  22  22  GLY   GLY C . n 
C 2 23  GLN   23  23  23  GLN   GLN C . n 
C 2 24  LYS   24  24  24  LYS   LYS C . n 
C 2 25  GLY   25  25  25  GLY   GLY C . n 
C 2 26  VAL   26  26  26  VAL   VAL C . n 
C 2 27  GLY   27  27  27  GLY   GLY C . n 
C 2 28  ASP   28  28  28  ASP   ASP C . n 
C 2 29  GLY   29  29  29  GLY   GLY C . n 
C 2 30  THR   30  30  30  THR   THR C . n 
C 2 31  VAL   31  31  31  VAL   VAL C . n 
C 2 32  SER   32  32  32  SER   SER C . n 
C 2 33  TRP   33  33  33  TRP   TRP C . n 
C 2 34  GLY   34  34  34  GLY   GLY C . n 
C 2 35  LEU   35  35  35  LEU   LEU C . n 
C 2 36  GLU   36  36  36  GLU   GLU C . n 
C 2 37  ASP   37  37  37  ASP   ASP C . n 
C 2 38  ASP   38  38  38  ASP   ASP C . n 
C 2 39  GLU   39  39  39  GLU   GLU C . n 
C 2 40  ASP   40  40  40  ASP   ASP C . n 
C 2 41  MET   41  41  41  MET   MET C . n 
C 2 42  THR   42  42  42  THR   THR C . n 
C 2 43  LEU   43  43  43  LEU   LEU C . n 
C 2 44  THR   44  44  44  THR   THR C . n 
C 2 45  ARG   45  45  45  ARG   ARG C . n 
C 2 46  TRP   46  46  46  TRP   TRP C . n 
C 2 47  THR   47  47  47  THR   THR C . n 
C 2 48  GLY   48  48  48  GLY   GLY C . n 
C 2 49  MET   49  49  49  MET   MET C . n 
C 2 50  ILE   50  50  50  ILE   ILE C . n 
C 2 51  ILE   51  51  51  ILE   ILE C . n 
C 2 52  GLY   52  52  52  GLY   GLY C . n 
C 2 53  PRO   53  53  53  PRO   PRO C . n 
C 2 54  PRO   54  54  54  PRO   PRO C . n 
C 2 55  ARG   55  55  55  ARG   ARG C . n 
C 2 56  THR   56  56  56  THR   THR C . n 
C 2 57  ASN   57  57  57  ASN   ASN C . n 
C 2 58  TYR   58  58  58  TYR   TYR C . n 
C 2 59  GLU   59  59  59  GLU   GLU C . n 
C 2 60  ASN   60  60  60  ASN   ASN C . n 
C 2 61  ARG   61  61  61  ARG   ARG C . n 
C 2 62  ILE   62  62  62  ILE   ILE C . n 
C 2 63  TYR   63  63  63  TYR   TYR C . n 
C 2 64  SER   64  64  64  SER   SER C . n 
C 2 65  LEU   65  65  65  LEU   LEU C . n 
C 2 66  LYS   66  66  66  LYS   LYS C . n 
C 2 67  VAL   67  67  67  VAL   VAL C . n 
C 2 68  GLU   68  68  68  GLU   GLU C . n 
C 2 69  CYS   69  69  69  CYS   CYS C . n 
C 2 70  GLY   70  70  70  GLY   GLY C . n 
C 2 71  PRO   71  71  71  PRO   PRO C . n 
C 2 72  LYS   72  72  72  LYS   LYS C . n 
C 2 73  TYR   73  73  73  TYR   TYR C . n 
C 2 74  PRO   74  74  74  PRO   PRO C . n 
C 2 75  GLU   75  75  75  GLU   GLU C . n 
C 2 76  ALA   76  76  76  ALA   ALA C . n 
C 2 77  PRO   77  77  77  PRO   PRO C . n 
C 2 78  PRO   78  78  78  PRO   PRO C . n 
C 2 79  SER   79  79  79  SER   SER C . n 
C 2 80  VAL   80  80  80  VAL   VAL C . n 
C 2 81  ARG   81  81  81  ARG   ARG C . n 
C 2 82  PHE   82  82  82  PHE   PHE C . n 
C 2 83  VAL   83  83  83  VAL   VAL C . n 
C 2 84  THR   84  84  84  THR   THR C . n 
C 2 85  LYS   85  85  85  LYS   LYS C . n 
C 2 86  ILE   86  86  86  ILE   ILE C . n 
C 2 87  ASN   87  87  87  ASN   ASN C . n 
C 2 88  MET   88  88  88  MET   MET C . n 
C 2 89  ASN   89  89  89  ASN   ASN C . n 
C 2 90  GLY   90  90  90  GLY   GLY C . n 
C 2 91  ILE   91  91  91  ILE   ILE C . n 
C 2 92  ASN   92  92  92  ASN   ASN C . n 
C 2 93  ASN   93  93  93  ASN   ASN C . n 
C 2 94  SER   94  94  94  SER   SER C . n 
C 2 95  SER   95  95  95  SER   SER C . n 
C 2 96  GLY   96  96  96  GLY   GLY C . n 
C 2 97  MET   97  97  97  MET   MET C . n 
C 2 98  VAL   98  98  98  VAL   VAL C . n 
C 2 99  ASP   99  99  99  ASP   ASP C . n 
C 2 100 ALA   100 100 100 ALA   ALA C . n 
C 2 101 ARG   101 101 101 ARG   ARG C . n 
C 2 102 SER   102 102 102 SER   SER C . n 
C 2 103 ILE   103 103 103 ILE   ILE C . n 
C 2 104 PRO   104 104 104 PRO   PRO C . n 
C 2 105 VAL   105 105 105 VAL   VAL C . n 
C 2 106 LEU   106 106 106 LEU   LEU C . n 
C 2 107 ALA   107 107 107 ALA   ALA C . n 
C 2 108 LYS   108 108 108 LYS   LYS C . n 
C 2 109 TRP   109 109 109 TRP   TRP C . n 
C 2 110 GLN   110 110 110 GLN   GLN C . n 
C 2 111 ASN   111 111 111 ASN   ASN C . n 
C 2 112 SER   112 112 112 SER   SER C . n 
C 2 113 TYR   113 113 113 TYR   TYR C . n 
C 2 114 SER   114 114 114 SER   SER C . n 
C 2 115 ILE   115 115 115 ILE   ILE C . n 
C 2 116 LYS   116 116 116 LYS   LYS C . n 
C 2 117 VAL   117 117 117 VAL   VAL C . n 
C 2 118 VAL   118 118 118 VAL   VAL C . n 
C 2 119 LEU   119 119 119 LEU   LEU C . n 
C 2 120 GLN   120 120 120 GLN   GLN C . n 
C 2 121 GLU   121 121 121 GLU   GLU C . n 
C 2 122 LEU   122 122 122 LEU   LEU C . n 
C 2 123 ARG   123 123 123 ARG   ARG C . n 
C 2 124 ARG   124 124 124 ARG   ARG C . n 
C 2 125 LEU   125 125 125 LEU   LEU C . n 
C 2 126 MET   126 126 126 MET   MET C . n 
C 2 127 MET   127 127 127 MET   MET C . n 
C 2 128 SER   128 128 128 SER   SER C . n 
C 2 129 LYS   129 129 129 LYS   LYS C . n 
C 2 130 GLU   130 130 130 GLU   GLU C . n 
C 2 131 ASN   131 131 131 ASN   ASN C . n 
C 2 132 MET   132 132 132 MET   MET C . n 
C 2 133 LYS   133 133 133 LYS   LYS C . n 
C 2 134 LEU   134 134 134 LEU   LEU C . n 
C 2 135 PRO   135 135 135 PRO   PRO C . n 
C 2 136 GLN   136 136 136 GLN   GLN C . n 
C 2 137 PRO   137 137 137 PRO   PRO C . n 
C 2 138 PRO   138 138 138 PRO   PRO C . n 
C 2 139 GLU   139 139 139 GLU   GLU C . n 
C 2 140 GLY   140 140 140 GLY   GLY C . n 
C 2 141 GLN   141 141 141 GLN   GLN C . n 
C 2 142 THR   142 142 142 THR   THR C . n 
C 2 143 TYR   143 143 143 TYR   TYR C . n 
C 2 144 ASN   144 144 144 ASN   ASN C . n 
C 2 145 ASN   145 145 ?   ?     ?   C . n 
D 2 1   MET   1   1   ?   ?     ?   D . n 
D 2 2   ALA   2   2   ?   ?     ?   D . n 
D 2 3   VAL   3   3   ?   ?     ?   D . n 
D 2 4   SER   4   4   ?   ?     ?   D . n 
D 2 5   THR   5   5   ?   ?     ?   D . n 
D 2 6   GLY   6   6   ?   ?     ?   D . n 
D 2 7   VAL   7   7   7   VAL   VAL D . n 
D 2 8   LYS   8   8   8   LYS   LYS D . n 
D 2 9   VAL   9   9   9   VAL   VAL D . n 
D 2 10  PRO   10  10  10  PRO   PRO D . n 
D 2 11  ARG   11  11  11  ARG   ARG D . n 
D 2 12  ASN   12  12  12  ASN   ASN D . n 
D 2 13  PHE   13  13  13  PHE   PHE D . n 
D 2 14  ARG   14  14  14  ARG   ARG D . n 
D 2 15  LEU   15  15  15  LEU   LEU D . n 
D 2 16  LEU   16  16  16  LEU   LEU D . n 
D 2 17  GLU   17  17  17  GLU   GLU D . n 
D 2 18  GLU   18  18  18  GLU   GLU D . n 
D 2 19  LEU   19  19  19  LEU   LEU D . n 
D 2 20  GLU   20  20  20  GLU   GLU D . n 
D 2 21  GLU   21  21  21  GLU   GLU D . n 
D 2 22  GLY   22  22  22  GLY   GLY D . n 
D 2 23  GLN   23  23  23  GLN   GLN D . n 
D 2 24  LYS   24  24  24  LYS   LYS D . n 
D 2 25  GLY   25  25  25  GLY   GLY D . n 
D 2 26  VAL   26  26  26  VAL   VAL D . n 
D 2 27  GLY   27  27  27  GLY   GLY D . n 
D 2 28  ASP   28  28  28  ASP   ASP D . n 
D 2 29  GLY   29  29  29  GLY   GLY D . n 
D 2 30  THR   30  30  30  THR   THR D . n 
D 2 31  VAL   31  31  31  VAL   VAL D . n 
D 2 32  SER   32  32  32  SER   SER D . n 
D 2 33  TRP   33  33  33  TRP   TRP D . n 
D 2 34  GLY   34  34  34  GLY   GLY D . n 
D 2 35  LEU   35  35  35  LEU   LEU D . n 
D 2 36  GLU   36  36  36  GLU   GLU D . n 
D 2 37  ASP   37  37  37  ASP   ASP D . n 
D 2 38  ASP   38  38  38  ASP   ASP D . n 
D 2 39  GLU   39  39  39  GLU   GLU D . n 
D 2 40  ASP   40  40  40  ASP   ASP D . n 
D 2 41  MET   41  41  41  MET   MET D . n 
D 2 42  THR   42  42  42  THR   THR D . n 
D 2 43  LEU   43  43  43  LEU   LEU D . n 
D 2 44  THR   44  44  44  THR   THR D . n 
D 2 45  ARG   45  45  45  ARG   ARG D . n 
D 2 46  TRP   46  46  46  TRP   TRP D . n 
D 2 47  THR   47  47  47  THR   THR D . n 
D 2 48  GLY   48  48  48  GLY   GLY D . n 
D 2 49  MET   49  49  49  MET   MET D . n 
D 2 50  ILE   50  50  50  ILE   ILE D . n 
D 2 51  ILE   51  51  51  ILE   ILE D . n 
D 2 52  GLY   52  52  52  GLY   GLY D . n 
D 2 53  PRO   53  53  53  PRO   PRO D . n 
D 2 54  PRO   54  54  54  PRO   PRO D . n 
D 2 55  ARG   55  55  55  ARG   ARG D . n 
D 2 56  THR   56  56  56  THR   THR D . n 
D 2 57  ASN   57  57  57  ASN   ASN D . n 
D 2 58  TYR   58  58  58  TYR   TYR D . n 
D 2 59  GLU   59  59  59  GLU   GLU D . n 
D 2 60  ASN   60  60  60  ASN   ASN D . n 
D 2 61  ARG   61  61  61  ARG   ARG D . n 
D 2 62  ILE   62  62  62  ILE   ILE D . n 
D 2 63  TYR   63  63  63  TYR   TYR D . n 
D 2 64  SER   64  64  64  SER   SER D . n 
D 2 65  LEU   65  65  65  LEU   LEU D . n 
D 2 66  LYS   66  66  66  LYS   LYS D . n 
D 2 67  VAL   67  67  67  VAL   VAL D . n 
D 2 68  GLU   68  68  68  GLU   GLU D . n 
D 2 69  CYS   69  69  69  CYS   CYS D . n 
D 2 70  GLY   70  70  70  GLY   GLY D . n 
D 2 71  PRO   71  71  71  PRO   PRO D . n 
D 2 72  LYS   72  72  72  LYS   LYS D . n 
D 2 73  TYR   73  73  73  TYR   TYR D . n 
D 2 74  PRO   74  74  74  PRO   PRO D . n 
D 2 75  GLU   75  75  75  GLU   GLU D . n 
D 2 76  ALA   76  76  76  ALA   ALA D . n 
D 2 77  PRO   77  77  77  PRO   PRO D . n 
D 2 78  PRO   78  78  78  PRO   PRO D . n 
D 2 79  SER   79  79  79  SER   SER D . n 
D 2 80  VAL   80  80  80  VAL   VAL D . n 
D 2 81  ARG   81  81  81  ARG   ARG D . n 
D 2 82  PHE   82  82  82  PHE   PHE D . n 
D 2 83  VAL   83  83  83  VAL   VAL D . n 
D 2 84  THR   84  84  84  THR   THR D . n 
D 2 85  LYS   85  85  85  LYS   LYS D . n 
D 2 86  ILE   86  86  86  ILE   ILE D . n 
D 2 87  ASN   87  87  87  ASN   ASN D . n 
D 2 88  MET   88  88  88  MET   MET D . n 
D 2 89  ASN   89  89  89  ASN   ASN D . n 
D 2 90  GLY   90  90  90  GLY   GLY D . n 
D 2 91  ILE   91  91  91  ILE   ILE D . n 
D 2 92  ASN   92  92  92  ASN   ASN D . n 
D 2 93  ASN   93  93  93  ASN   ASN D . n 
D 2 94  SER   94  94  94  SER   SER D . n 
D 2 95  SER   95  95  95  SER   SER D . n 
D 2 96  GLY   96  96  96  GLY   GLY D . n 
D 2 97  MET   97  97  97  MET   MET D . n 
D 2 98  VAL   98  98  98  VAL   VAL D . n 
D 2 99  ASP   99  99  99  ASP   ASP D . n 
D 2 100 ALA   100 100 100 ALA   ALA D . n 
D 2 101 ARG   101 101 101 ARG   ARG D . n 
D 2 102 SER   102 102 102 SER   SER D . n 
D 2 103 ILE   103 103 103 ILE   ILE D . n 
D 2 104 PRO   104 104 104 PRO   PRO D . n 
D 2 105 VAL   105 105 105 VAL   VAL D . n 
D 2 106 LEU   106 106 106 LEU   LEU D . n 
D 2 107 ALA   107 107 107 ALA   ALA D . n 
D 2 108 LYS   108 108 108 LYS   LYS D . n 
D 2 109 TRP   109 109 109 TRP   TRP D . n 
D 2 110 GLN   110 110 110 GLN   GLN D . n 
D 2 111 ASN   111 111 111 ASN   ASN D . n 
D 2 112 SER   112 112 112 SER   SER D . n 
D 2 113 TYR   113 113 113 TYR   TYR D . n 
D 2 114 SER   114 114 114 SER   SER D . n 
D 2 115 ILE   115 115 115 ILE   ILE D . n 
D 2 116 LYS   116 116 116 LYS   LYS D . n 
D 2 117 VAL   117 117 117 VAL   VAL D . n 
D 2 118 VAL   118 118 118 VAL   VAL D . n 
D 2 119 LEU   119 119 119 LEU   LEU D . n 
D 2 120 GLN   120 120 120 GLN   GLN D . n 
D 2 121 GLU   121 121 121 GLU   GLU D . n 
D 2 122 LEU   122 122 122 LEU   LEU D . n 
D 2 123 ARG   123 123 123 ARG   ARG D . n 
D 2 124 ARG   124 124 124 ARG   ARG D . n 
D 2 125 LEU   125 125 125 LEU   LEU D . n 
D 2 126 MET   126 126 126 MET   MET D . n 
D 2 127 MET   127 127 127 MET   MET D . n 
D 2 128 SER   128 128 128 SER   SER D . n 
D 2 129 LYS   129 129 129 LYS   LYS D . n 
D 2 130 GLU   130 130 130 GLU   GLU D . n 
D 2 131 ASN   131 131 131 ASN   ASN D . n 
D 2 132 MET   132 132 132 MET   MET D . n 
D 2 133 LYS   133 133 133 LYS   LYS D . n 
D 2 134 LEU   134 134 134 LEU   LEU D . n 
D 2 135 PRO   135 135 135 PRO   PRO D . n 
D 2 136 GLN   136 136 136 GLN   GLN D . n 
D 2 137 PRO   137 137 137 PRO   PRO D . n 
D 2 138 PRO   138 138 138 PRO   PRO D . n 
D 2 139 GLU   139 139 139 GLU   GLU D . n 
D 2 140 GLY   140 140 140 GLY   GLY D . n 
D 2 141 GLN   141 141 141 GLN   GLN D . n 
D 2 142 THR   142 142 142 THR   THR D . n 
D 2 143 TYR   143 143 143 TYR   TYR D . n 
D 2 144 ASN   144 144 144 ASN   ASN D . n 
D 2 145 ASN   145 145 ?   ?     ?   D . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1EJS 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1EJS 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
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 
E 3 HOH 1   201 307 HOH HOH A . 
E 3 HOH 2   202 56  HOH HOH A . 
E 3 HOH 3   203 244 HOH HOH A . 
E 3 HOH 4   204 298 HOH HOH A . 
E 3 HOH 5   205 429 HOH HOH A . 
E 3 HOH 6   206 135 HOH HOH A . 
E 3 HOH 7   207 114 HOH HOH A . 
E 3 HOH 8   208 19  HOH HOH A . 
E 3 HOH 9   209 75  HOH HOH A . 
E 3 HOH 10  210 362 HOH HOH A . 
E 3 HOH 11  211 29  HOH HOH A . 
E 3 HOH 12  212 673 HOH HOH A . 
E 3 HOH 13  213 107 HOH HOH A . 
E 3 HOH 14  214 289 HOH HOH A . 
E 3 HOH 15  215 172 HOH HOH A . 
E 3 HOH 16  216 32  HOH HOH A . 
E 3 HOH 17  217 392 HOH HOH A . 
E 3 HOH 18  218 383 HOH HOH A . 
E 3 HOH 19  219 157 HOH HOH A . 
E 3 HOH 20  220 282 HOH HOH A . 
E 3 HOH 21  221 297 HOH HOH A . 
E 3 HOH 22  222 645 HOH HOH A . 
E 3 HOH 23  223 20  HOH HOH A . 
E 3 HOH 24  224 153 HOH HOH A . 
E 3 HOH 25  225 2   HOH HOH A . 
E 3 HOH 26  226 72  HOH HOH A . 
E 3 HOH 27  227 324 HOH HOH A . 
E 3 HOH 28  228 287 HOH HOH A . 
E 3 HOH 29  229 159 HOH HOH A . 
E 3 HOH 30  230 181 HOH HOH A . 
E 3 HOH 31  231 449 HOH HOH A . 
E 3 HOH 32  232 625 HOH HOH A . 
E 3 HOH 33  233 131 HOH HOH A . 
E 3 HOH 34  234 129 HOH HOH A . 
E 3 HOH 35  235 666 HOH HOH A . 
E 3 HOH 36  236 257 HOH HOH A . 
E 3 HOH 37  237 78  HOH HOH A . 
E 3 HOH 38  238 500 HOH HOH A . 
E 3 HOH 39  239 162 HOH HOH A . 
E 3 HOH 40  240 77  HOH HOH A . 
E 3 HOH 41  241 404 HOH HOH A . 
E 3 HOH 42  242 564 HOH HOH A . 
E 3 HOH 43  243 176 HOH HOH A . 
E 3 HOH 44  244 371 HOH HOH A . 
E 3 HOH 45  245 320 HOH HOH A . 
E 3 HOH 46  246 169 HOH HOH A . 
E 3 HOH 47  247 659 HOH HOH A . 
E 3 HOH 48  248 403 HOH HOH A . 
E 3 HOH 49  249 134 HOH HOH A . 
E 3 HOH 50  250 568 HOH HOH A . 
E 3 HOH 51  251 405 HOH HOH A . 
E 3 HOH 52  252 263 HOH HOH A . 
E 3 HOH 53  253 124 HOH HOH A . 
E 3 HOH 54  254 236 HOH HOH A . 
E 3 HOH 55  255 549 HOH HOH A . 
E 3 HOH 56  256 240 HOH HOH A . 
E 3 HOH 57  257 300 HOH HOH A . 
E 3 HOH 58  258 675 HOH HOH A . 
E 3 HOH 59  259 355 HOH HOH A . 
E 3 HOH 60  260 165 HOH HOH A . 
E 3 HOH 61  261 179 HOH HOH A . 
E 3 HOH 62  262 190 HOH HOH A . 
E 3 HOH 63  263 10  HOH HOH A . 
E 3 HOH 64  264 61  HOH HOH A . 
E 3 HOH 65  265 69  HOH HOH A . 
E 3 HOH 66  266 402 HOH HOH A . 
E 3 HOH 67  267 127 HOH HOH A . 
E 3 HOH 68  268 590 HOH HOH A . 
E 3 HOH 69  269 504 HOH HOH A . 
E 3 HOH 70  270 512 HOH HOH A . 
E 3 HOH 71  271 277 HOH HOH A . 
E 3 HOH 72  272 260 HOH HOH A . 
E 3 HOH 73  273 407 HOH HOH A . 
E 3 HOH 74  274 39  HOH HOH A . 
E 3 HOH 75  275 566 HOH HOH A . 
E 3 HOH 76  276 518 HOH HOH A . 
E 3 HOH 77  277 467 HOH HOH A . 
E 3 HOH 78  278 149 HOH HOH A . 
E 3 HOH 79  279 641 HOH HOH A . 
E 3 HOH 80  280 430 HOH HOH A . 
E 3 HOH 81  281 667 HOH HOH A . 
E 3 HOH 82  282 672 HOH HOH A . 
E 3 HOH 83  283 417 HOH HOH A . 
E 3 HOH 84  284 440 HOH HOH A . 
E 3 HOH 85  285 420 HOH HOH A . 
E 3 HOH 86  286 418 HOH HOH A . 
E 3 HOH 87  287 132 HOH HOH A . 
E 3 HOH 88  288 447 HOH HOH A . 
E 3 HOH 89  289 389 HOH HOH A . 
E 3 HOH 90  290 218 HOH HOH A . 
E 3 HOH 91  291 327 HOH HOH A . 
E 3 HOH 92  292 250 HOH HOH A . 
E 3 HOH 93  293 295 HOH HOH A . 
E 3 HOH 94  294 539 HOH HOH A . 
E 3 HOH 95  295 534 HOH HOH A . 
E 3 HOH 96  296 290 HOH HOH A . 
E 3 HOH 97  297 488 HOH HOH A . 
E 3 HOH 98  298 419 HOH HOH A . 
E 3 HOH 99  299 570 HOH HOH A . 
E 3 HOH 100 300 191 HOH HOH A . 
E 3 HOH 101 301 519 HOH HOH A . 
E 3 HOH 102 302 396 HOH HOH A . 
E 3 HOH 103 303 387 HOH HOH A . 
E 3 HOH 104 304 458 HOH HOH A . 
E 3 HOH 105 305 346 HOH HOH A . 
E 3 HOH 106 306 482 HOH HOH A . 
E 3 HOH 107 307 479 HOH HOH A . 
E 3 HOH 108 308 532 HOH HOH A . 
E 3 HOH 109 309 555 HOH HOH A . 
E 3 HOH 110 310 652 HOH HOH A . 
E 3 HOH 111 311 547 HOH HOH A . 
E 3 HOH 112 312 444 HOH HOH A . 
E 3 HOH 113 313 632 HOH HOH A . 
F 3 HOH 1   201 99  HOH HOH B . 
F 3 HOH 2   202 158 HOH HOH B . 
F 3 HOH 3   203 489 HOH HOH B . 
F 3 HOH 4   204 187 HOH HOH B . 
F 3 HOH 5   205 436 HOH HOH B . 
F 3 HOH 6   206 209 HOH HOH B . 
F 3 HOH 7   207 178 HOH HOH B . 
F 3 HOH 8   208 214 HOH HOH B . 
F 3 HOH 9   209 139 HOH HOH B . 
F 3 HOH 10  210 173 HOH HOH B . 
F 3 HOH 11  211 537 HOH HOH B . 
F 3 HOH 12  212 491 HOH HOH B . 
F 3 HOH 13  213 548 HOH HOH B . 
F 3 HOH 14  214 95  HOH HOH B . 
F 3 HOH 15  215 278 HOH HOH B . 
F 3 HOH 16  216 262 HOH HOH B . 
F 3 HOH 17  217 288 HOH HOH B . 
F 3 HOH 18  218 599 HOH HOH B . 
F 3 HOH 19  219 448 HOH HOH B . 
F 3 HOH 20  220 195 HOH HOH B . 
F 3 HOH 21  221 84  HOH HOH B . 
F 3 HOH 22  222 636 HOH HOH B . 
F 3 HOH 23  223 51  HOH HOH B . 
F 3 HOH 24  224 3   HOH HOH B . 
F 3 HOH 25  225 471 HOH HOH B . 
F 3 HOH 26  226 47  HOH HOH B . 
F 3 HOH 27  227 23  HOH HOH B . 
F 3 HOH 28  228 168 HOH HOH B . 
F 3 HOH 29  229 15  HOH HOH B . 
F 3 HOH 30  230 145 HOH HOH B . 
F 3 HOH 31  231 46  HOH HOH B . 
F 3 HOH 32  232 104 HOH HOH B . 
F 3 HOH 33  233 21  HOH HOH B . 
F 3 HOH 34  234 13  HOH HOH B . 
F 3 HOH 35  235 94  HOH HOH B . 
F 3 HOH 36  236 194 HOH HOH B . 
F 3 HOH 37  237 183 HOH HOH B . 
F 3 HOH 38  238 86  HOH HOH B . 
F 3 HOH 39  239 211 HOH HOH B . 
F 3 HOH 40  240 248 HOH HOH B . 
F 3 HOH 41  241 206 HOH HOH B . 
F 3 HOH 42  242 533 HOH HOH B . 
F 3 HOH 43  243 17  HOH HOH B . 
F 3 HOH 44  244 163 HOH HOH B . 
F 3 HOH 45  245 589 HOH HOH B . 
F 3 HOH 46  246 152 HOH HOH B . 
F 3 HOH 47  247 617 HOH HOH B . 
F 3 HOH 48  248 57  HOH HOH B . 
F 3 HOH 49  249 494 HOH HOH B . 
F 3 HOH 50  250 322 HOH HOH B . 
F 3 HOH 51  251 378 HOH HOH B . 
F 3 HOH 52  252 372 HOH HOH B . 
F 3 HOH 53  253 607 HOH HOH B . 
F 3 HOH 54  254 71  HOH HOH B . 
F 3 HOH 55  255 510 HOH HOH B . 
F 3 HOH 56  256 43  HOH HOH B . 
F 3 HOH 57  257 197 HOH HOH B . 
F 3 HOH 58  258 101 HOH HOH B . 
F 3 HOH 59  259 474 HOH HOH B . 
F 3 HOH 60  260 45  HOH HOH B . 
F 3 HOH 61  261 27  HOH HOH B . 
F 3 HOH 62  262 182 HOH HOH B . 
F 3 HOH 63  263 338 HOH HOH B . 
F 3 HOH 64  264 609 HOH HOH B . 
F 3 HOH 65  265 16  HOH HOH B . 
F 3 HOH 66  266 7   HOH HOH B . 
F 3 HOH 67  267 28  HOH HOH B . 
F 3 HOH 68  268 6   HOH HOH B . 
F 3 HOH 69  269 301 HOH HOH B . 
F 3 HOH 70  270 321 HOH HOH B . 
F 3 HOH 71  271 170 HOH HOH B . 
F 3 HOH 72  272 382 HOH HOH B . 
F 3 HOH 73  273 630 HOH HOH B . 
F 3 HOH 74  274 386 HOH HOH B . 
F 3 HOH 75  275 202 HOH HOH B . 
F 3 HOH 76  276 414 HOH HOH B . 
F 3 HOH 77  277 35  HOH HOH B . 
F 3 HOH 78  278 73  HOH HOH B . 
F 3 HOH 79  279 126 HOH HOH B . 
F 3 HOH 80  280 453 HOH HOH B . 
F 3 HOH 81  281 221 HOH HOH B . 
F 3 HOH 82  282 140 HOH HOH B . 
F 3 HOH 83  283 254 HOH HOH B . 
F 3 HOH 84  284 59  HOH HOH B . 
F 3 HOH 85  285 513 HOH HOH B . 
F 3 HOH 86  286 26  HOH HOH B . 
F 3 HOH 87  287 664 HOH HOH B . 
F 3 HOH 88  288 226 HOH HOH B . 
F 3 HOH 89  289 224 HOH HOH B . 
F 3 HOH 90  290 413 HOH HOH B . 
F 3 HOH 91  291 348 HOH HOH B . 
F 3 HOH 92  292 219 HOH HOH B . 
F 3 HOH 93  293 96  HOH HOH B . 
F 3 HOH 94  294 143 HOH HOH B . 
F 3 HOH 95  295 193 HOH HOH B . 
F 3 HOH 96  296 318 HOH HOH B . 
F 3 HOH 97  297 508 HOH HOH B . 
F 3 HOH 98  298 540 HOH HOH B . 
F 3 HOH 99  299 141 HOH HOH B . 
F 3 HOH 100 300 150 HOH HOH B . 
F 3 HOH 101 301 105 HOH HOH B . 
F 3 HOH 102 302 472 HOH HOH B . 
F 3 HOH 103 303 379 HOH HOH B . 
F 3 HOH 104 304 485 HOH HOH B . 
F 3 HOH 105 305 354 HOH HOH B . 
F 3 HOH 106 306 399 HOH HOH B . 
F 3 HOH 107 307 52  HOH HOH B . 
F 3 HOH 108 308 5   HOH HOH B . 
F 3 HOH 109 309 243 HOH HOH B . 
F 3 HOH 110 310 118 HOH HOH B . 
F 3 HOH 111 311 146 HOH HOH B . 
F 3 HOH 112 312 66  HOH HOH B . 
F 3 HOH 113 313 353 HOH HOH B . 
F 3 HOH 114 314 220 HOH HOH B . 
F 3 HOH 115 315 470 HOH HOH B . 
F 3 HOH 116 316 352 HOH HOH B . 
F 3 HOH 117 317 586 HOH HOH B . 
F 3 HOH 118 318 25  HOH HOH B . 
F 3 HOH 119 319 496 HOH HOH B . 
F 3 HOH 120 320 111 HOH HOH B . 
F 3 HOH 121 321 90  HOH HOH B . 
F 3 HOH 122 322 546 HOH HOH B . 
F 3 HOH 123 323 18  HOH HOH B . 
F 3 HOH 124 324 74  HOH HOH B . 
F 3 HOH 125 325 598 HOH HOH B . 
F 3 HOH 126 326 161 HOH HOH B . 
F 3 HOH 127 327 454 HOH HOH B . 
F 3 HOH 128 328 366 HOH HOH B . 
F 3 HOH 129 329 477 HOH HOH B . 
F 3 HOH 130 330 164 HOH HOH B . 
F 3 HOH 131 331 154 HOH HOH B . 
F 3 HOH 132 332 237 HOH HOH B . 
F 3 HOH 133 333 268 HOH HOH B . 
F 3 HOH 134 334 270 HOH HOH B . 
F 3 HOH 135 335 375 HOH HOH B . 
F 3 HOH 136 336 592 HOH HOH B . 
F 3 HOH 137 337 439 HOH HOH B . 
F 3 HOH 138 338 363 HOH HOH B . 
F 3 HOH 139 339 503 HOH HOH B . 
F 3 HOH 140 340 648 HOH HOH B . 
F 3 HOH 141 341 217 HOH HOH B . 
F 3 HOH 142 342 147 HOH HOH B . 
F 3 HOH 143 343 640 HOH HOH B . 
F 3 HOH 144 344 462 HOH HOH B . 
F 3 HOH 145 345 225 HOH HOH B . 
F 3 HOH 146 346 428 HOH HOH B . 
F 3 HOH 147 347 271 HOH HOH B . 
F 3 HOH 148 348 279 HOH HOH B . 
F 3 HOH 149 349 385 HOH HOH B . 
F 3 HOH 150 350 520 HOH HOH B . 
F 3 HOH 151 351 480 HOH HOH B . 
F 3 HOH 152 352 443 HOH HOH B . 
F 3 HOH 153 353 619 HOH HOH B . 
F 3 HOH 154 354 614 HOH HOH B . 
F 3 HOH 155 355 680 HOH HOH B . 
F 3 HOH 156 356 358 HOH HOH B . 
F 3 HOH 157 357 579 HOH HOH B . 
F 3 HOH 158 358 561 HOH HOH B . 
F 3 HOH 159 359 461 HOH HOH B . 
F 3 HOH 160 360 523 HOH HOH B . 
F 3 HOH 161 361 347 HOH HOH B . 
F 3 HOH 162 362 535 HOH HOH B . 
F 3 HOH 163 363 269 HOH HOH B . 
F 3 HOH 164 364 473 HOH HOH B . 
F 3 HOH 165 365 656 HOH HOH B . 
F 3 HOH 166 366 478 HOH HOH B . 
F 3 HOH 167 367 249 HOH HOH B . 
F 3 HOH 168 368 408 HOH HOH B . 
F 3 HOH 169 369 650 HOH HOH B . 
F 3 HOH 170 370 323 HOH HOH B . 
F 3 HOH 171 371 550 HOH HOH B . 
F 3 HOH 172 372 83  HOH HOH B . 
F 3 HOH 173 373 557 HOH HOH B . 
F 3 HOH 174 374 401 HOH HOH B . 
F 3 HOH 175 375 38  HOH HOH B . 
F 3 HOH 176 376 665 HOH HOH B . 
F 3 HOH 177 377 273 HOH HOH B . 
F 3 HOH 178 378 186 HOH HOH B . 
F 3 HOH 179 379 445 HOH HOH B . 
F 3 HOH 180 380 315 HOH HOH B . 
F 3 HOH 181 381 463 HOH HOH B . 
F 3 HOH 182 382 267 HOH HOH B . 
F 3 HOH 183 383 345 HOH HOH B . 
F 3 HOH 184 384 651 HOH HOH B . 
F 3 HOH 185 385 662 HOH HOH B . 
F 3 HOH 186 386 647 HOH HOH B . 
F 3 HOH 187 387 276 HOH HOH B . 
F 3 HOH 188 388 530 HOH HOH B . 
F 3 HOH 189 389 334 HOH HOH B . 
F 3 HOH 190 390 674 HOH HOH B . 
F 3 HOH 191 391 272 HOH HOH B . 
F 3 HOH 192 392 501 HOH HOH B . 
F 3 HOH 193 393 456 HOH HOH B . 
G 3 HOH 1   201 205 HOH HOH C . 
G 3 HOH 2   202 44  HOH HOH C . 
G 3 HOH 3   203 384 HOH HOH C . 
G 3 HOH 4   204 312 HOH HOH C . 
G 3 HOH 5   205 424 HOH HOH C . 
G 3 HOH 6   206 670 HOH HOH C . 
G 3 HOH 7   207 200 HOH HOH C . 
G 3 HOH 8   208 291 HOH HOH C . 
G 3 HOH 9   209 328 HOH HOH C . 
G 3 HOH 10  210 184 HOH HOH C . 
G 3 HOH 11  211 633 HOH HOH C . 
G 3 HOH 12  212 155 HOH HOH C . 
G 3 HOH 13  213 171 HOH HOH C . 
G 3 HOH 14  214 509 HOH HOH C . 
G 3 HOH 15  215 63  HOH HOH C . 
G 3 HOH 16  216 336 HOH HOH C . 
G 3 HOH 17  217 148 HOH HOH C . 
G 3 HOH 18  218 196 HOH HOH C . 
G 3 HOH 19  219 223 HOH HOH C . 
G 3 HOH 20  220 264 HOH HOH C . 
G 3 HOH 21  221 1   HOH HOH C . 
G 3 HOH 22  222 365 HOH HOH C . 
G 3 HOH 23  223 9   HOH HOH C . 
G 3 HOH 24  224 596 HOH HOH C . 
G 3 HOH 25  225 610 HOH HOH C . 
G 3 HOH 26  226 33  HOH HOH C . 
G 3 HOH 27  227 121 HOH HOH C . 
G 3 HOH 28  228 109 HOH HOH C . 
G 3 HOH 29  229 437 HOH HOH C . 
G 3 HOH 30  230 24  HOH HOH C . 
G 3 HOH 31  231 339 HOH HOH C . 
G 3 HOH 32  232 416 HOH HOH C . 
G 3 HOH 33  233 235 HOH HOH C . 
G 3 HOH 34  234 41  HOH HOH C . 
G 3 HOH 35  235 466 HOH HOH C . 
G 3 HOH 36  236 562 HOH HOH C . 
G 3 HOH 37  237 246 HOH HOH C . 
G 3 HOH 38  238 639 HOH HOH C . 
G 3 HOH 39  239 286 HOH HOH C . 
G 3 HOH 40  240 70  HOH HOH C . 
G 3 HOH 41  241 442 HOH HOH C . 
G 3 HOH 42  242 370 HOH HOH C . 
G 3 HOH 43  243 40  HOH HOH C . 
G 3 HOH 44  244 122 HOH HOH C . 
G 3 HOH 45  245 433 HOH HOH C . 
G 3 HOH 46  246 234 HOH HOH C . 
G 3 HOH 47  247 258 HOH HOH C . 
G 3 HOH 48  248 68  HOH HOH C . 
G 3 HOH 49  249 203 HOH HOH C . 
G 3 HOH 50  250 198 HOH HOH C . 
G 3 HOH 51  251 595 HOH HOH C . 
G 3 HOH 52  252 364 HOH HOH C . 
G 3 HOH 53  253 137 HOH HOH C . 
G 3 HOH 54  254 671 HOH HOH C . 
G 3 HOH 55  255 113 HOH HOH C . 
G 3 HOH 56  256 37  HOH HOH C . 
G 3 HOH 57  257 502 HOH HOH C . 
G 3 HOH 58  258 48  HOH HOH C . 
G 3 HOH 59  259 80  HOH HOH C . 
G 3 HOH 60  260 160 HOH HOH C . 
G 3 HOH 61  261 280 HOH HOH C . 
G 3 HOH 62  262 597 HOH HOH C . 
G 3 HOH 63  263 304 HOH HOH C . 
G 3 HOH 64  264 238 HOH HOH C . 
G 3 HOH 65  265 76  HOH HOH C . 
G 3 HOH 66  266 542 HOH HOH C . 
G 3 HOH 67  267 14  HOH HOH C . 
G 3 HOH 68  268 128 HOH HOH C . 
G 3 HOH 69  269 475 HOH HOH C . 
G 3 HOH 70  270 81  HOH HOH C . 
G 3 HOH 71  271 120 HOH HOH C . 
G 3 HOH 72  272 432 HOH HOH C . 
G 3 HOH 73  273 11  HOH HOH C . 
G 3 HOH 74  274 12  HOH HOH C . 
G 3 HOH 75  275 514 HOH HOH C . 
G 3 HOH 76  276 110 HOH HOH C . 
G 3 HOH 77  277 174 HOH HOH C . 
G 3 HOH 78  278 678 HOH HOH C . 
G 3 HOH 79  279 229 HOH HOH C . 
G 3 HOH 80  280 136 HOH HOH C . 
G 3 HOH 81  281 438 HOH HOH C . 
G 3 HOH 82  282 58  HOH HOH C . 
G 3 HOH 83  283 360 HOH HOH C . 
G 3 HOH 84  284 531 HOH HOH C . 
G 3 HOH 85  285 251 HOH HOH C . 
G 3 HOH 86  286 180 HOH HOH C . 
G 3 HOH 87  287 233 HOH HOH C . 
G 3 HOH 88  288 658 HOH HOH C . 
G 3 HOH 89  289 50  HOH HOH C . 
G 3 HOH 90  290 87  HOH HOH C . 
G 3 HOH 91  291 67  HOH HOH C . 
G 3 HOH 92  292 55  HOH HOH C . 
G 3 HOH 93  293 119 HOH HOH C . 
G 3 HOH 94  294 343 HOH HOH C . 
G 3 HOH 95  295 138 HOH HOH C . 
G 3 HOH 96  296 359 HOH HOH C . 
G 3 HOH 97  297 529 HOH HOH C . 
G 3 HOH 98  298 427 HOH HOH C . 
G 3 HOH 99  299 64  HOH HOH C . 
G 3 HOH 100 300 517 HOH HOH C . 
G 3 HOH 101 301 242 HOH HOH C . 
G 3 HOH 102 302 215 HOH HOH C . 
G 3 HOH 103 303 42  HOH HOH C . 
G 3 HOH 104 304 284 HOH HOH C . 
G 3 HOH 105 305 22  HOH HOH C . 
G 3 HOH 106 306 79  HOH HOH C . 
G 3 HOH 107 307 604 HOH HOH C . 
G 3 HOH 108 308 634 HOH HOH C . 
G 3 HOH 109 309 507 HOH HOH C . 
G 3 HOH 110 310 451 HOH HOH C . 
G 3 HOH 111 311 102 HOH HOH C . 
G 3 HOH 112 312 274 HOH HOH C . 
G 3 HOH 113 313 600 HOH HOH C . 
G 3 HOH 114 314 620 HOH HOH C . 
G 3 HOH 115 315 239 HOH HOH C . 
G 3 HOH 116 316 349 HOH HOH C . 
G 3 HOH 117 317 4   HOH HOH C . 
G 3 HOH 118 318 668 HOH HOH C . 
G 3 HOH 119 319 395 HOH HOH C . 
G 3 HOH 120 320 522 HOH HOH C . 
G 3 HOH 121 321 313 HOH HOH C . 
G 3 HOH 122 322 649 HOH HOH C . 
G 3 HOH 123 323 551 HOH HOH C . 
G 3 HOH 124 324 390 HOH HOH C . 
G 3 HOH 125 325 374 HOH HOH C . 
G 3 HOH 126 326 342 HOH HOH C . 
G 3 HOH 127 327 293 HOH HOH C . 
G 3 HOH 128 328 455 HOH HOH C . 
G 3 HOH 129 329 677 HOH HOH C . 
G 3 HOH 130 330 412 HOH HOH C . 
G 3 HOH 131 331 623 HOH HOH C . 
G 3 HOH 132 332 228 HOH HOH C . 
G 3 HOH 133 333 621 HOH HOH C . 
G 3 HOH 134 334 151 HOH HOH C . 
G 3 HOH 135 335 185 HOH HOH C . 
G 3 HOH 136 336 361 HOH HOH C . 
G 3 HOH 137 337 459 HOH HOH C . 
G 3 HOH 138 338 661 HOH HOH C . 
G 3 HOH 139 339 679 HOH HOH C . 
G 3 HOH 140 340 369 HOH HOH C . 
G 3 HOH 141 341 669 HOH HOH C . 
G 3 HOH 142 342 357 HOH HOH C . 
G 3 HOH 143 343 285 HOH HOH C . 
G 3 HOH 144 344 310 HOH HOH C . 
G 3 HOH 145 345 642 HOH HOH C . 
G 3 HOH 146 346 594 HOH HOH C . 
G 3 HOH 147 347 526 HOH HOH C . 
G 3 HOH 148 348 329 HOH HOH C . 
G 3 HOH 149 349 435 HOH HOH C . 
G 3 HOH 150 350 125 HOH HOH C . 
G 3 HOH 151 351 423 HOH HOH C . 
G 3 HOH 152 352 660 HOH HOH C . 
G 3 HOH 153 353 377 HOH HOH C . 
G 3 HOH 154 354 283 HOH HOH C . 
G 3 HOH 155 355 624 HOH HOH C . 
G 3 HOH 156 356 545 HOH HOH C . 
G 3 HOH 157 357 256 HOH HOH C . 
G 3 HOH 158 358 331 HOH HOH C . 
G 3 HOH 159 359 230 HOH HOH C . 
G 3 HOH 160 360 411 HOH HOH C . 
G 3 HOH 161 361 367 HOH HOH C . 
G 3 HOH 162 362 593 HOH HOH C . 
G 3 HOH 163 363 261 HOH HOH C . 
H 3 HOH 1   201 177 HOH HOH D . 
H 3 HOH 2   202 317 HOH HOH D . 
H 3 HOH 3   203 89  HOH HOH D . 
H 3 HOH 4   204 305 HOH HOH D . 
H 3 HOH 5   205 115 HOH HOH D . 
H 3 HOH 6   206 231 HOH HOH D . 
H 3 HOH 7   207 368 HOH HOH D . 
H 3 HOH 8   208 210 HOH HOH D . 
H 3 HOH 9   209 524 HOH HOH D . 
H 3 HOH 10  210 376 HOH HOH D . 
H 3 HOH 11  211 208 HOH HOH D . 
H 3 HOH 12  212 296 HOH HOH D . 
H 3 HOH 13  213 97  HOH HOH D . 
H 3 HOH 14  214 8   HOH HOH D . 
H 3 HOH 15  215 82  HOH HOH D . 
H 3 HOH 16  216 615 HOH HOH D . 
H 3 HOH 17  217 100 HOH HOH D . 
H 3 HOH 18  218 292 HOH HOH D . 
H 3 HOH 19  219 332 HOH HOH D . 
H 3 HOH 20  220 212 HOH HOH D . 
H 3 HOH 21  221 521 HOH HOH D . 
H 3 HOH 22  222 30  HOH HOH D . 
H 3 HOH 23  223 394 HOH HOH D . 
H 3 HOH 24  224 201 HOH HOH D . 
H 3 HOH 25  225 93  HOH HOH D . 
H 3 HOH 26  226 156 HOH HOH D . 
H 3 HOH 27  227 608 HOH HOH D . 
H 3 HOH 28  228 53  HOH HOH D . 
H 3 HOH 29  229 98  HOH HOH D . 
H 3 HOH 30  230 553 HOH HOH D . 
H 3 HOH 31  231 167 HOH HOH D . 
H 3 HOH 32  232 388 HOH HOH D . 
H 3 HOH 33  233 601 HOH HOH D . 
H 3 HOH 34  234 232 HOH HOH D . 
H 3 HOH 35  235 222 HOH HOH D . 
H 3 HOH 36  236 166 HOH HOH D . 
H 3 HOH 37  237 65  HOH HOH D . 
H 3 HOH 38  238 62  HOH HOH D . 
H 3 HOH 39  239 31  HOH HOH D . 
H 3 HOH 40  240 207 HOH HOH D . 
H 3 HOH 41  241 49  HOH HOH D . 
H 3 HOH 42  242 144 HOH HOH D . 
H 3 HOH 43  243 216 HOH HOH D . 
H 3 HOH 44  244 133 HOH HOH D . 
H 3 HOH 45  245 85  HOH HOH D . 
H 3 HOH 46  246 142 HOH HOH D . 
H 3 HOH 47  247 54  HOH HOH D . 
H 3 HOH 48  248 247 HOH HOH D . 
H 3 HOH 49  249 627 HOH HOH D . 
H 3 HOH 50  250 356 HOH HOH D . 
H 3 HOH 51  251 189 HOH HOH D . 
H 3 HOH 52  252 299 HOH HOH D . 
H 3 HOH 53  253 36  HOH HOH D . 
H 3 HOH 54  254 425 HOH HOH D . 
H 3 HOH 55  255 393 HOH HOH D . 
H 3 HOH 56  256 612 HOH HOH D . 
H 3 HOH 57  257 490 HOH HOH D . 
H 3 HOH 58  258 265 HOH HOH D . 
H 3 HOH 59  259 213 HOH HOH D . 
H 3 HOH 60  260 116 HOH HOH D . 
H 3 HOH 61  261 487 HOH HOH D . 
H 3 HOH 62  262 108 HOH HOH D . 
H 3 HOH 63  263 255 HOH HOH D . 
H 3 HOH 64  264 241 HOH HOH D . 
H 3 HOH 65  265 400 HOH HOH D . 
H 3 HOH 66  266 611 HOH HOH D . 
H 3 HOH 67  267 227 HOH HOH D . 
H 3 HOH 68  268 259 HOH HOH D . 
H 3 HOH 69  269 398 HOH HOH D . 
H 3 HOH 70  270 441 HOH HOH D . 
H 3 HOH 71  271 175 HOH HOH D . 
H 3 HOH 72  272 397 HOH HOH D . 
H 3 HOH 73  273 303 HOH HOH D . 
H 3 HOH 74  274 188 HOH HOH D . 
H 3 HOH 75  275 34  HOH HOH D . 
H 3 HOH 76  276 60  HOH HOH D . 
H 3 HOH 77  277 91  HOH HOH D . 
H 3 HOH 78  278 88  HOH HOH D . 
H 3 HOH 79  279 493 HOH HOH D . 
H 3 HOH 80  280 340 HOH HOH D . 
H 3 HOH 81  281 123 HOH HOH D . 
H 3 HOH 82  282 380 HOH HOH D . 
H 3 HOH 83  283 130 HOH HOH D . 
H 3 HOH 84  284 516 HOH HOH D . 
H 3 HOH 85  285 92  HOH HOH D . 
H 3 HOH 86  286 391 HOH HOH D . 
H 3 HOH 87  287 536 HOH HOH D . 
H 3 HOH 88  288 569 HOH HOH D . 
H 3 HOH 89  289 335 HOH HOH D . 
H 3 HOH 90  290 192 HOH HOH D . 
H 3 HOH 91  291 117 HOH HOH D . 
H 3 HOH 92  292 506 HOH HOH D . 
H 3 HOH 93  293 330 HOH HOH D . 
H 3 HOH 94  294 199 HOH HOH D . 
H 3 HOH 95  295 676 HOH HOH D . 
H 3 HOH 96  296 381 HOH HOH D . 
H 3 HOH 97  297 106 HOH HOH D . 
H 3 HOH 98  298 481 HOH HOH D . 
H 3 HOH 99  299 613 HOH HOH D . 
H 3 HOH 100 300 333 HOH HOH D . 
H 3 HOH 101 301 484 HOH HOH D . 
H 3 HOH 102 302 311 HOH HOH D . 
H 3 HOH 103 303 302 HOH HOH D . 
H 3 HOH 104 304 452 HOH HOH D . 
H 3 HOH 105 305 406 HOH HOH D . 
H 3 HOH 106 306 326 HOH HOH D . 
H 3 HOH 107 307 325 HOH HOH D . 
H 3 HOH 108 308 281 HOH HOH D . 
H 3 HOH 109 309 351 HOH HOH D . 
H 3 HOH 110 310 410 HOH HOH D . 
H 3 HOH 111 311 476 HOH HOH D . 
H 3 HOH 112 312 341 HOH HOH D . 
H 3 HOH 113 313 591 HOH HOH D . 
H 3 HOH 114 314 308 HOH HOH D . 
H 3 HOH 115 315 492 HOH HOH D . 
H 3 HOH 116 316 421 HOH HOH D . 
H 3 HOH 117 317 635 HOH HOH D . 
H 3 HOH 118 318 605 HOH HOH D . 
H 3 HOH 119 319 204 HOH HOH D . 
H 3 HOH 120 320 584 HOH HOH D . 
H 3 HOH 121 321 112 HOH HOH D . 
H 3 HOH 122 322 316 HOH HOH D . 
H 3 HOH 123 323 505 HOH HOH D . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement        ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? '(1.20.1_4487: ???)' 1 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? HKL-3000 ? ? ? .                    2 
? phasing           ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .                    3 
? 'data processing' ? ? ? ? ? ? ? ? ? ? ? HKL-3000 ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   93.10 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9LHJ 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     62.415 
_cell.length_a_esd                 ? 
_cell.length_b                     71.603 
_cell.length_b_esd                 ? 
_cell.length_c                     68.560 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9LHJ 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9LHJ 
_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             2.25 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          45.22 
_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, HANGING 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    '0.1 M BIS-TRIS pH 6.5, 20% w/v PEG 5,000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            289.15 
# 
_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 PILATUS3 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-07-21 
_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   0.96183 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SSRF BEAMLINE BL18U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.96183 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL18U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9LHJ 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.68 
_reflns.d_resolution_low                               50.00 
_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                                     68847 
_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                           100.0 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.6 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          4.0 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.657 
_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                                0.117 
_reflns.pdbx_Rpim_I_all                                0.045 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       455503 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.983 
_reflns.pdbx_CC_star                                   0.996 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.108 
_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                        ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.meanI_over_sigI_gt 
_reflns_shell.meanI_over_uI_all 
_reflns_shell.meanI_over_uI_gt 
_reflns_shell.number_measured_gt 
_reflns_shell.number_unique_gt 
_reflns_shell.percent_possible_gt 
_reflns_shell.Rmerge_F_gt 
_reflns_shell.Rmerge_I_gt 
_reflns_shell.pdbx_redundancy 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_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 
_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 
1.68 1.74  ? ? ? ? ? ? 6854 ? ? ? ? ? ? ? ? ? ? ? 5.9 0.488 ? ? 0.716 0.292 ? 1  1 0.784 0.938 ? 99.9  ? 0.652 ? ? ? ? ? ? ? ? ? 
1.74 1.81  ? ? ? ? ? ? 6826 ? ? ? ? ? ? ? ? ? ? ? 6.6 0.505 ? ? 0.620 0.239 ? 2  1 0.877 0.967 ? 100.0 ? 0.571 ? ? ? ? ? ? ? ? ? 
1.81 1.89  ? ? ? ? ? ? 6883 ? ? ? ? ? ? ? ? ? ? ? 6.7 0.540 ? ? 0.486 0.185 ? 3  1 0.925 0.980 ? 100.0 ? 0.448 ? ? ? ? ? ? ? ? ? 
1.89 1.99  ? ? ? ? ? ? 6827 ? ? ? ? ? ? ? ? ? ? ? 6.6 0.594 ? ? 0.371 0.143 ? 4  1 0.949 0.987 ? 100.0 ? 0.342 ? ? ? ? ? ? ? ? ? 
1.99 2.12  ? ? ? ? ? ? 6863 ? ? ? ? ? ? ? ? ? ? ? 6.6 0.658 ? ? 0.271 0.104 ? 5  1 0.969 0.992 ? 100.0 ? 0.250 ? ? ? ? ? ? ? ? ? 
2.12 2.28  ? ? ? ? ? ? 6866 ? ? ? ? ? ? ? ? ? ? ? 6.9 0.714 ? ? 0.201 0.075 ? 6  1 0.981 0.995 ? 100.0 ? 0.187 ? ? ? ? ? ? ? ? ? 
2.28 2.51  ? ? ? ? ? ? 6891 ? ? ? ? ? ? ? ? ? ? ? 6.7 0.733 ? ? 0.154 0.059 ? 7  1 0.986 0.997 ? 100.0 ? 0.142 ? ? ? ? ? ? ? ? ? 
2.51 2.87  ? ? ? ? ? ? 6899 ? ? ? ? ? ? ? ? ? ? ? 6.8 0.723 ? ? 0.118 0.044 ? 8  1 0.992 0.998 ? 100.0 ? 0.109 ? ? ? ? ? ? ? ? ? 
2.87 3.62  ? ? ? ? ? ? 6907 ? ? ? ? ? ? ? ? ? ? ? 6.8 0.778 ? ? 0.085 0.032 ? 9  1 0.994 0.999 ? 100.0 ? 0.078 ? ? ? ? ? ? ? ? ? 
3.62 50.00 ? ? ? ? ? ? 7031 ? ? ? ? ? ? ? ? ? ? ? 6.5 0.806 ? ? 0.067 0.026 ? 10 1 0.996 0.999 ? 100.0 ? 0.062 ? ? ? ? ? ? ? ? ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9LHJ 
_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                            1.68 
_refine.ls_d_res_low                             35.80 
_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                     68806 
_refine.ls_number_reflns_R_free                  3640 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.88 
_refine.ls_percent_reflns_R_free                 5.29 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1847 
_refine.ls_R_factor_R_free                       0.2283 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1824 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 22.18 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.21 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.68 
_refine_hist.d_res_low                        35.80 
_refine_hist.number_atoms_solvent             592 
_refine_hist.number_atoms_total               5201 
_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        4609 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_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' ? 0.008  ? 4784 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.009  ? 6500 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 11.620 ? 652  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.062  ? 692  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.010  ? 850  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.68 1.70  . . 119 2449 97.00  . . . . 0.2283 . . . . . . . . . . . 0.2877 
'X-RAY DIFFRACTION' 1.70 1.72  . . 150 2465 100.00 . . . . 0.2242 . . . . . . . . . . . 0.2894 
'X-RAY DIFFRACTION' 1.72 1.75  . . 123 2522 100.00 . . . . 0.2242 . . . . . . . . . . . 0.2752 
'X-RAY DIFFRACTION' 1.75 1.77  . . 145 2497 100.00 . . . . 0.2311 . . . . . . . . . . . 0.3089 
'X-RAY DIFFRACTION' 1.77 1.80  . . 148 2499 100.00 . . . . 0.2288 . . . . . . . . . . . 0.2639 
'X-RAY DIFFRACTION' 1.80 1.83  . . 171 2453 100.00 . . . . 0.2443 . . . . . . . . . . . 0.3071 
'X-RAY DIFFRACTION' 1.83 1.86  . . 149 2500 100.00 . . . . 0.2175 . . . . . . . . . . . 0.2619 
'X-RAY DIFFRACTION' 1.86 1.90  . . 126 2496 100.00 . . . . 0.1995 . . . . . . . . . . . 0.2466 
'X-RAY DIFFRACTION' 1.90 1.93  . . 165 2450 100.00 . . . . 0.2011 . . . . . . . . . . . 0.2399 
'X-RAY DIFFRACTION' 1.93 1.97  . . 122 2525 100.00 . . . . 0.1950 . . . . . . . . . . . 0.2627 
'X-RAY DIFFRACTION' 1.97 2.02  . . 167 2519 100.00 . . . . 0.1930 . . . . . . . . . . . 0.2628 
'X-RAY DIFFRACTION' 2.02 2.06  . . 165 2457 100.00 . . . . 0.1886 . . . . . . . . . . . 0.2515 
'X-RAY DIFFRACTION' 2.06 2.12  . . 139 2488 100.00 . . . . 0.1899 . . . . . . . . . . . 0.1951 
'X-RAY DIFFRACTION' 2.12 2.17  . . 120 2545 100.00 . . . . 0.1927 . . . . . . . . . . . 0.2604 
'X-RAY DIFFRACTION' 2.17 2.24  . . 134 2491 100.00 . . . . 0.1908 . . . . . . . . . . . 0.2387 
'X-RAY DIFFRACTION' 2.24 2.31  . . 146 2516 100.00 . . . . 0.1893 . . . . . . . . . . . 0.2727 
'X-RAY DIFFRACTION' 2.31 2.39  . . 162 2479 100.00 . . . . 0.1898 . . . . . . . . . . . 0.2504 
'X-RAY DIFFRACTION' 2.39 2.49  . . 130 2510 100.00 . . . . 0.1958 . . . . . . . . . . . 0.2608 
'X-RAY DIFFRACTION' 2.49 2.60  . . 133 2511 100.00 . . . . 0.1902 . . . . . . . . . . . 0.2264 
'X-RAY DIFFRACTION' 2.60 2.74  . . 125 2544 100.00 . . . . 0.1917 . . . . . . . . . . . 0.2442 
'X-RAY DIFFRACTION' 2.74 2.91  . . 115 2524 100.00 . . . . 0.1854 . . . . . . . . . . . 0.2422 
'X-RAY DIFFRACTION' 2.91 3.13  . . 156 2514 100.00 . . . . 0.1839 . . . . . . . . . . . 0.2318 
'X-RAY DIFFRACTION' 3.13 3.45  . . 150 2499 100.00 . . . . 0.1775 . . . . . . . . . . . 0.2012 
'X-RAY DIFFRACTION' 3.45 3.95  . . 116 2567 100.00 . . . . 0.1563 . . . . . . . . . . . 0.1969 
'X-RAY DIFFRACTION' 3.95 4.97  . . 131 2556 100.00 . . . . 0.1409 . . . . . . . . . . . 0.1746 
'X-RAY DIFFRACTION' 4.97 35.80 . . 133 2590 100.00 . . . . 0.1739 . . . . . . . . . . . 0.1879 
# 
_struct.entry_id                     9LHJ 
_struct.title                        'UBE2N/UBE2V2 complexed with a covalent inhibitor' 
_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        9LHJ 
_struct_keywords.text            'Covalent inhibitor, LIGASE' 
_struct_keywords.pdbx_keywords   LIGASE 
# 
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 2 ? 
E N N 3 ? 
F N N 3 ? 
G N N 3 ? 
H N N 3 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP UBE2N_HUMAN P61088 ? 1 
;MAGLPRRIIKETQRLLAEPVPGIKAEPDESNARYFHVVIAGPQDSPFEGGTFKLELFLPEEYPMAAPKVRFMTKIYHPNV
DKLGRICLDILKDKWSPALQIRTVLLSIQALLSAPNPDDPLANDVAEQWKTNEAQAIETARAWTRLYAMNNI
;
1 
2 UNP UB2V2_HUMAN Q15819 ? 2 
;MAVSTGVKVPRNFRLLEELEEGQKGVGDGTVSWGLEDDEDMTLTRWTGMIIGPPRTNYENRIYSLKVECGPKYPEAPPSV
RFVTKINMNGINNSSGMVDARSIPVLAKWQNSYSIKVVLQELRRLMMSKENMKLPQPPEGQTYNN
;
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 9LHJ A 1 ? 152 ? P61088 1 ? 152 ? 1 152 
2 1 9LHJ B 1 ? 152 ? P61088 1 ? 152 ? 1 152 
3 2 9LHJ C 1 ? 145 ? Q15819 1 ? 145 ? 1 145 
4 2 9LHJ D 1 ? 145 ? Q15819 1 ? 145 ? 1 145 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA dimeric 2 
2 author_and_software_defined_assembly PISA dimeric 2 
# 
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)' 1560  ? 
1 MORE         -9    ? 
1 'SSA (A^2)'  15020 ? 
2 'ABSA (A^2)' 1230  ? 
2 MORE         -10   ? 
2 'SSA (A^2)'  14930 ? 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,E 
1 2 D,H 
2 1 B,F 
2 3 C,G 
# 
_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' 1_655 x+1,y,z     1.0000000000  0.0000000000 0.0000000000 62.4150000000 0.0000000000 1.0000000000 
0.0000000000 0.0000000000  0.0000000000 0.0000000000 1.0000000000  0.0000000000 
3 'crystal symmetry operation' 2_555 -x,y+1/2,-z -1.0000000000 0.0000000000 0.0000000000 0.0000000000  0.0000000000 1.0000000000 
0.0000000000 35.8015000000 0.0000000000 0.0000000000 -1.0000000000 0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 PRO A 5   ? GLU A 18  ? PRO A 5   GLU A 18  1 ? 14 
HELX_P HELX_P2  AA2 LEU A 88  ? LYS A 92  ? LEU A 88  LYS A 92  5 ? 5  
HELX_P HELX_P3  AA3 GLN A 100 ? ALA A 114 ? GLN A 100 ALA A 114 1 ? 15 
HELX_P HELX_P4  AA4 ASN A 123 ? ASN A 132 ? ASN A 123 ASN A 132 1 ? 10 
HELX_P HELX_P5  AA5 ASN A 132 ? ALA A 148 ? ASN A 132 ALA A 148 1 ? 17 
HELX_P HELX_P6  AA6 PRO B 5   ? GLU B 18  ? PRO B 5   GLU B 18  1 ? 14 
HELX_P HELX_P7  AA7 LEU B 88  ? LYS B 92  ? LEU B 88  LYS B 92  5 ? 5  
HELX_P HELX_P8  AA8 GLN B 100 ? ALA B 114 ? GLN B 100 ALA B 114 1 ? 15 
HELX_P HELX_P9  AA9 ASN B 123 ? ASN B 132 ? ASN B 123 ASN B 132 1 ? 10 
HELX_P HELX_P10 AB1 ASN B 132 ? MET B 149 ? ASN B 132 MET B 149 1 ? 18 
HELX_P HELX_P11 AB2 PRO C 10  ? GLY C 25  ? PRO C 10  GLY C 25  1 ? 16 
HELX_P HELX_P12 AB3 ASP C 99  ? SER C 102 ? ASP C 99  SER C 102 5 ? 4  
HELX_P HELX_P13 AB4 ILE C 103 ? LYS C 108 ? ILE C 103 LYS C 108 1 ? 6  
HELX_P HELX_P14 AB5 SER C 114 ? MET C 126 ? SER C 114 MET C 126 1 ? 13 
HELX_P HELX_P15 AB6 PRO D 10  ? GLY D 25  ? PRO D 10  GLY D 25  1 ? 16 
HELX_P HELX_P16 AB7 ASP D 99  ? SER D 102 ? ASP D 99  SER D 102 5 ? 4  
HELX_P HELX_P17 AB8 ILE D 103 ? LYS D 108 ? ILE D 103 LYS D 108 1 ? 6  
HELX_P HELX_P18 AB9 SER D 114 ? MET D 126 ? SER D 114 MET D 126 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
covale1 covale one ? A THR   73 C ? ? ? 1_555 A A1EJS 74 N ? ? A THR   73 A A1EJS 74 1_555 ? ? ? ? ? ? ? 1.429 ? ? 
covale2 covale one ? A A1EJS 74 C ? ? ? 1_555 A ILE   75 N ? ? A A1EJS 74 A ILE   75 1_555 ? ? ? ? ? ? ? 1.424 ? ? 
covale3 covale one ? B THR   73 C ? ? ? 1_555 B A1EJS 74 N ? ? B THR   73 B A1EJS 74 1_555 ? ? ? ? ? ? ? 1.429 ? ? 
covale4 covale one ? B A1EJS 74 C ? ? ? 1_555 B ILE   75 N ? ? B A1EJS 74 B ILE   75 1_555 ? ? ? ? ? ? ? 1.424 ? ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 A1EJS A 74 ? . . . . A1EJS A 74 ? 1_555 . . . . . . . LYS 1 A1EJS None 'Non-standard residue' 
2 A1EJS B 74 ? . . . . A1EJS B 74 ? 1_555 . . . . . . . LYS 1 A1EJS None 'Non-standard residue' 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 TYR 62 A . ? TYR 62 A PRO 63 A ? PRO 63 A 1 2.94  
2 TYR 62 B . ? TYR 62 B PRO 63 B ? PRO 63 B 1 7.52  
3 TYR 73 C . ? TYR 73 C PRO 74 C ? PRO 74 C 1 -2.27 
4 TYR 73 D . ? TYR 73 D PRO 74 D ? PRO 74 D 1 -0.64 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 4 ? 
AA3 ? 4 ? 
AA4 ? 4 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ILE A 23 ? ASP A 28 ? ILE A 23 ASP A 28 
AA1 2 ASN A 31 ? ALA A 40 ? ASN A 31 ALA A 40 
AA1 3 THR A 51 ? PHE A 57 ? THR A 51 PHE A 57 
AA1 4 LYS A 68 ? PHE A 71 ? LYS A 68 PHE A 71 
AA2 1 ILE B 23 ? ASP B 28 ? ILE B 23 ASP B 28 
AA2 2 ASN B 31 ? ALA B 40 ? ASN B 31 ALA B 40 
AA2 3 THR B 51 ? PHE B 57 ? THR B 51 PHE B 57 
AA2 4 LYS B 68 ? PHE B 71 ? LYS B 68 PHE B 71 
AA3 1 VAL C 31 ? LEU C 35 ? VAL C 31 LEU C 35 
AA3 2 ARG C 45 ? ILE C 51 ? ARG C 45 ILE C 51 
AA3 3 ILE C 62 ? GLU C 68 ? ILE C 62 GLU C 68 
AA3 4 SER C 79 ? PHE C 82 ? SER C 79 PHE C 82 
AA4 1 VAL D 31 ? LEU D 35 ? VAL D 31 LEU D 35 
AA4 2 ARG D 45 ? ILE D 51 ? ARG D 45 ILE D 51 
AA4 3 ILE D 62 ? GLU D 68 ? ILE D 62 GLU D 68 
AA4 4 SER D 79 ? PHE D 82 ? SER D 79 PHE D 82 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N ASP A 28 ? N ASP A 28 O TYR A 34 ? O TYR A 34 
AA1 2 3 N PHE A 35 ? N PHE A 35 O LEU A 56 ? O LEU A 56 
AA1 3 4 N PHE A 57 ? N PHE A 57 O LYS A 68 ? O LYS A 68 
AA2 1 2 N GLU B 26 ? N GLU B 26 O HIS B 36 ? O HIS B 36 
AA2 2 3 N PHE B 35 ? N PHE B 35 O LEU B 56 ? O LEU B 56 
AA2 3 4 N PHE B 57 ? N PHE B 57 O LYS B 68 ? O LYS B 68 
AA3 1 2 N GLY C 34 ? N GLY C 34 O THR C 47 ? O THR C 47 
AA3 2 3 N ILE C 50 ? N ILE C 50 O TYR C 63 ? O TYR C 63 
AA3 3 4 N LYS C 66 ? N LYS C 66 O ARG C 81 ? O ARG C 81 
AA4 1 2 N GLY D 34 ? N GLY D 34 O THR D 47 ? O THR D 47 
AA4 2 3 N TRP D 46 ? N TRP D 46 O VAL D 67 ? O VAL D 67 
AA4 3 4 N LYS D 66 ? N LYS D 66 O ARG D 81 ? O ARG D 81 
# 
_pdbx_entry_details.entry_id                   9LHJ 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 O   C HOH 278 ? ? O C HOH 329 ? ? 1.92 
2  1 O   B HOH 287 ? ? O B HOH 376 ? ? 1.95 
3  1 O   D HOH 204 ? ? O D HOH 211 ? ? 1.99 
4  1 O   C HOH 308 ? ? O C HOH 331 ? ? 2.00 
5  1 O   D HOH 230 ? ? O D HOH 287 ? ? 2.05 
6  1 O   B HOH 337 ? ? O B HOH 357 ? ? 2.05 
7  1 O   B HOH 285 ? ? O B HOH 368 ? ? 2.08 
8  1 OE2 D GLU 21  ? ? O D HOH 201 ? ? 2.09 
9  1 O   C HOH 328 ? ? O C HOH 347 ? ? 2.10 
10 1 O   C HOH 310 ? ? O C HOH 324 ? ? 2.11 
11 1 O   B HOH 292 ? ? O B HOH 319 ? ? 2.11 
12 1 O   B HOH 305 ? ? O B HOH 331 ? ? 2.12 
13 1 O   D HOH 270 ? ? O D HOH 302 ? ? 2.13 
14 1 O   B HOH 222 ? ? O B HOH 249 ? ? 2.14 
15 1 O   B HOH 350 ? ? O B HOH 358 ? ? 2.14 
16 1 O   B HOH 338 ? ? O B HOH 354 ? ? 2.19 
17 1 O   A HOH 311 ? ? O A HOH 313 ? ? 2.19 
18 1 O   C HOH 225 ? ? O C HOH 259 ? ? 2.19 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O B HOH 353 ? ? 1_555 O C HOH 333 ? ? 2_555 1.95 
2 1 O B HOH 217 ? ? 1_555 O C HOH 350 ? ? 2_655 2.09 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 CA A A1EJS 74 ? ? C A A1EJS 74 ? ? N A ILE 75 ? ? 100.42 117.20 -16.78 2.20 Y 
2 1 O  A A1EJS 74 ? ? C A A1EJS 74 ? ? N A ILE 75 ? ? 132.88 122.70 10.18  1.60 Y 
3 1 O  B A1EJS 74 ? ? C B A1EJS 74 ? ? N B ILE 75 ? ? 134.29 122.70 11.59  1.60 Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 LYS A 92  ? ? -131.72 -109.72 
2 1 ALA A 114 ? ? -154.67 79.70   
3 1 ASN B 31  ? ? -164.06 100.86  
4 1 LYS B 92  ? ? -130.10 -115.36 
5 1 ASP D 38  ? ? -68.43  5.29    
6 1 ASN D 60  ? ? 81.72   -20.37  
# 
_pdbx_validate_main_chain_plane.id                       1 
_pdbx_validate_main_chain_plane.PDB_model_num            1 
_pdbx_validate_main_chain_plane.auth_comp_id             A1EJS 
_pdbx_validate_main_chain_plane.auth_asym_id             A 
_pdbx_validate_main_chain_plane.auth_seq_id              74 
_pdbx_validate_main_chain_plane.PDB_ins_code             ? 
_pdbx_validate_main_chain_plane.label_alt_id             ? 
_pdbx_validate_main_chain_plane.improper_torsion_angle   11.96 
# 
loop_
_pdbx_struct_mod_residue.id 
_pdbx_struct_mod_residue.label_asym_id 
_pdbx_struct_mod_residue.label_comp_id 
_pdbx_struct_mod_residue.label_seq_id 
_pdbx_struct_mod_residue.auth_asym_id 
_pdbx_struct_mod_residue.auth_comp_id 
_pdbx_struct_mod_residue.auth_seq_id 
_pdbx_struct_mod_residue.PDB_ins_code 
_pdbx_struct_mod_residue.parent_comp_id 
_pdbx_struct_mod_residue.details 
1 A A1EJS 74 A A1EJS 74 ? LYS 'modified residue' 
2 B A1EJS 74 B A1EJS 74 ? LYS 'modified residue' 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       313 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   6.14 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 1   ? A MET 1   
2  1 Y 1 A ALA 2   ? A ALA 2   
3  1 Y 1 A PRO 120 ? A PRO 120 
4  1 Y 1 A LEU 121 ? A LEU 121 
5  1 Y 1 A ASN 151 ? A ASN 151 
6  1 Y 1 A ILE 152 ? A ILE 152 
7  1 Y 1 B MET 1   ? B MET 1   
8  1 Y 1 B ALA 2   ? B ALA 2   
9  1 Y 1 B LEU 121 ? B LEU 121 
10 1 Y 1 B ASN 151 ? B ASN 151 
11 1 Y 1 B ILE 152 ? B ILE 152 
12 1 Y 1 C MET 1   ? C MET 1   
13 1 Y 1 C ALA 2   ? C ALA 2   
14 1 Y 1 C VAL 3   ? C VAL 3   
15 1 Y 1 C SER 4   ? C SER 4   
16 1 Y 1 C THR 5   ? C THR 5   
17 1 Y 1 C GLY 6   ? C GLY 6   
18 1 Y 1 C ASN 145 ? C ASN 145 
19 1 Y 1 D MET 1   ? D MET 1   
20 1 Y 1 D ALA 2   ? D ALA 2   
21 1 Y 1 D VAL 3   ? D VAL 3   
22 1 Y 1 D SER 4   ? D SER 4   
23 1 Y 1 D THR 5   ? D THR 5   
24 1 Y 1 D GLY 6   ? D GLY 6   
25 1 Y 1 D ASN 145 ? D ASN 145 
# 
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 
A1EJS C22  C Y N 1   
A1EJS C25  C Y N 2   
A1EJS C30  C Y N 3   
A1EJS C29  C Y N 4   
A1EJS C28  C Y N 5   
A1EJS C27  C Y N 6   
A1EJS C26  C Y N 7   
A1EJS C18  C Y N 8   
A1EJS C17  C Y N 9   
A1EJS O15  O N N 10  
A1EJS O14  O N N 11  
A1EJS C13  C N N 12  
A1EJS C10  C N N 13  
A1EJS CE   C N N 14  
A1EJS CD   C N N 15  
A1EJS CG   C N N 16  
A1EJS CB   C N N 17  
A1EJS CA   C N S 18  
A1EJS C    C N N 19  
A1EJS C11  C N N 20  
A1EJS C12  C N N 21  
A1EJS C20  C Y N 22  
A1EJS C31  C N N 23  
A1EJS C34  C N N 24  
A1EJS C35  C N N 25  
A1EJS C36  C Y N 26  
A1EJS C37  C Y N 27  
A1EJS C38  C Y N 28  
A1EJS C39  C Y N 29  
A1EJS C40  C Y N 30  
A1EJS C41  C Y N 31  
A1EJS C42  C Y N 32  
A1EJS C44  C Y N 33  
A1EJS C45  C Y N 34  
A1EJS C47  C N N 35  
A1EJS F48  F N N 36  
A1EJS NZ   N N N 37  
A1EJS N    N N N 38  
A1EJS N16  N N N 39  
A1EJS N19  N Y N 40  
A1EJS N21  N Y N 41  
A1EJS N23  N N N 42  
A1EJS N24  N N N 43  
A1EJS N43  N Y N 44  
A1EJS N46  N Y N 45  
A1EJS O    O N N 46  
A1EJS O32  O N N 47  
A1EJS O33  O N N 48  
A1EJS H301 H N N 49  
A1EJS H281 H N N 50  
A1EJS H271 H N N 51  
A1EJS H181 H N N 52  
A1EJS HE2  H N N 53  
A1EJS HE3  H N N 54  
A1EJS HD3  H N N 55  
A1EJS HD2  H N N 56  
A1EJS HG2  H N N 57  
A1EJS HG3  H N N 58  
A1EJS HB2  H N N 59  
A1EJS HB3  H N N 60  
A1EJS HA   H N N 61  
A1EJS H341 H N N 62  
A1EJS H343 H N N 63  
A1EJS H342 H N N 64  
A1EJS H352 H N N 65  
A1EJS H351 H N N 66  
A1EJS H371 H N N 67  
A1EJS H381 H N N 68  
A1EJS H391 H N N 69  
A1EJS H411 H N N 70  
A1EJS H441 H N N 71  
A1EJS H451 H N N 72  
A1EJS H472 H N N 73  
A1EJS H473 H N N 74  
A1EJS H471 H N N 75  
A1EJS HZ1  H N N 76  
A1EJS H    H N N 77  
A1EJS H2   H N N 78  
A1EJS H161 H N N 79  
A1EJS H231 H N N 80  
A1EJS H241 H N N 81  
A1EJS OXT  O N N 82  
A1EJS H1   H N N 83  
ALA   N    N N N 84  
ALA   CA   C N S 85  
ALA   C    C N N 86  
ALA   O    O N N 87  
ALA   CB   C N N 88  
ALA   OXT  O N N 89  
ALA   H    H N N 90  
ALA   H2   H N N 91  
ALA   HA   H N N 92  
ALA   HB1  H N N 93  
ALA   HB2  H N N 94  
ALA   HB3  H N N 95  
ALA   HXT  H N N 96  
ARG   N    N N N 97  
ARG   CA   C N S 98  
ARG   C    C N N 99  
ARG   O    O N N 100 
ARG   CB   C N N 101 
ARG   CG   C N N 102 
ARG   CD   C N N 103 
ARG   NE   N N N 104 
ARG   CZ   C N N 105 
ARG   NH1  N N N 106 
ARG   NH2  N N N 107 
ARG   OXT  O N N 108 
ARG   H    H N N 109 
ARG   H2   H N N 110 
ARG   HA   H N N 111 
ARG   HB2  H N N 112 
ARG   HB3  H N N 113 
ARG   HG2  H N N 114 
ARG   HG3  H N N 115 
ARG   HD2  H N N 116 
ARG   HD3  H N N 117 
ARG   HE   H N N 118 
ARG   HH11 H N N 119 
ARG   HH12 H N N 120 
ARG   HH21 H N N 121 
ARG   HH22 H N N 122 
ARG   HXT  H N N 123 
ASN   N    N N N 124 
ASN   CA   C N S 125 
ASN   C    C N N 126 
ASN   O    O N N 127 
ASN   CB   C N N 128 
ASN   CG   C N N 129 
ASN   OD1  O N N 130 
ASN   ND2  N N N 131 
ASN   OXT  O N N 132 
ASN   H    H N N 133 
ASN   H2   H N N 134 
ASN   HA   H N N 135 
ASN   HB2  H N N 136 
ASN   HB3  H N N 137 
ASN   HD21 H N N 138 
ASN   HD22 H N N 139 
ASN   HXT  H N N 140 
ASP   N    N N N 141 
ASP   CA   C N S 142 
ASP   C    C N N 143 
ASP   O    O N N 144 
ASP   CB   C N N 145 
ASP   CG   C N N 146 
ASP   OD1  O N N 147 
ASP   OD2  O N N 148 
ASP   OXT  O N N 149 
ASP   H    H N N 150 
ASP   H2   H N N 151 
ASP   HA   H N N 152 
ASP   HB2  H N N 153 
ASP   HB3  H N N 154 
ASP   HD2  H N N 155 
ASP   HXT  H N N 156 
CYS   N    N N N 157 
CYS   CA   C N R 158 
CYS   C    C N N 159 
CYS   O    O N N 160 
CYS   CB   C N N 161 
CYS   SG   S N N 162 
CYS   OXT  O N N 163 
CYS   H    H N N 164 
CYS   H2   H N N 165 
CYS   HA   H N N 166 
CYS   HB2  H N N 167 
CYS   HB3  H N N 168 
CYS   HG   H N N 169 
CYS   HXT  H N N 170 
GLN   N    N N N 171 
GLN   CA   C N S 172 
GLN   C    C N N 173 
GLN   O    O N N 174 
GLN   CB   C N N 175 
GLN   CG   C N N 176 
GLN   CD   C N N 177 
GLN   OE1  O N N 178 
GLN   NE2  N N N 179 
GLN   OXT  O N N 180 
GLN   H    H N N 181 
GLN   H2   H N N 182 
GLN   HA   H N N 183 
GLN   HB2  H N N 184 
GLN   HB3  H N N 185 
GLN   HG2  H N N 186 
GLN   HG3  H N N 187 
GLN   HE21 H N N 188 
GLN   HE22 H N N 189 
GLN   HXT  H N N 190 
GLU   N    N N N 191 
GLU   CA   C N S 192 
GLU   C    C N N 193 
GLU   O    O N N 194 
GLU   CB   C N N 195 
GLU   CG   C N N 196 
GLU   CD   C N N 197 
GLU   OE1  O N N 198 
GLU   OE2  O N N 199 
GLU   OXT  O N N 200 
GLU   H    H N N 201 
GLU   H2   H N N 202 
GLU   HA   H N N 203 
GLU   HB2  H N N 204 
GLU   HB3  H N N 205 
GLU   HG2  H N N 206 
GLU   HG3  H N N 207 
GLU   HE2  H N N 208 
GLU   HXT  H N N 209 
GLY   N    N N N 210 
GLY   CA   C N N 211 
GLY   C    C N N 212 
GLY   O    O N N 213 
GLY   OXT  O N N 214 
GLY   H    H N N 215 
GLY   H2   H N N 216 
GLY   HA2  H N N 217 
GLY   HA3  H N N 218 
GLY   HXT  H N N 219 
HIS   N    N N N 220 
HIS   CA   C N S 221 
HIS   C    C N N 222 
HIS   O    O N N 223 
HIS   CB   C N N 224 
HIS   CG   C Y N 225 
HIS   ND1  N Y N 226 
HIS   CD2  C Y N 227 
HIS   CE1  C Y N 228 
HIS   NE2  N Y N 229 
HIS   OXT  O N N 230 
HIS   H    H N N 231 
HIS   H2   H N N 232 
HIS   HA   H N N 233 
HIS   HB2  H N N 234 
HIS   HB3  H N N 235 
HIS   HD1  H N N 236 
HIS   HD2  H N N 237 
HIS   HE1  H N N 238 
HIS   HE2  H N N 239 
HIS   HXT  H N N 240 
HOH   O    O N N 241 
HOH   H1   H N N 242 
HOH   H2   H N N 243 
ILE   N    N N N 244 
ILE   CA   C N S 245 
ILE   C    C N N 246 
ILE   O    O N N 247 
ILE   CB   C N S 248 
ILE   CG1  C N N 249 
ILE   CG2  C N N 250 
ILE   CD1  C N N 251 
ILE   OXT  O N N 252 
ILE   H    H N N 253 
ILE   H2   H N N 254 
ILE   HA   H N N 255 
ILE   HB   H N N 256 
ILE   HG12 H N N 257 
ILE   HG13 H N N 258 
ILE   HG21 H N N 259 
ILE   HG22 H N N 260 
ILE   HG23 H N N 261 
ILE   HD11 H N N 262 
ILE   HD12 H N N 263 
ILE   HD13 H N N 264 
ILE   HXT  H N N 265 
LEU   N    N N N 266 
LEU   CA   C N S 267 
LEU   C    C N N 268 
LEU   O    O N N 269 
LEU   CB   C N N 270 
LEU   CG   C N N 271 
LEU   CD1  C N N 272 
LEU   CD2  C N N 273 
LEU   OXT  O N N 274 
LEU   H    H N N 275 
LEU   H2   H N N 276 
LEU   HA   H N N 277 
LEU   HB2  H N N 278 
LEU   HB3  H N N 279 
LEU   HG   H N N 280 
LEU   HD11 H N N 281 
LEU   HD12 H N N 282 
LEU   HD13 H N N 283 
LEU   HD21 H N N 284 
LEU   HD22 H N N 285 
LEU   HD23 H N N 286 
LEU   HXT  H N N 287 
LYS   N    N N N 288 
LYS   CA   C N S 289 
LYS   C    C N N 290 
LYS   O    O N N 291 
LYS   CB   C N N 292 
LYS   CG   C N N 293 
LYS   CD   C N N 294 
LYS   CE   C N N 295 
LYS   NZ   N N N 296 
LYS   OXT  O N N 297 
LYS   H    H N N 298 
LYS   H2   H N N 299 
LYS   HA   H N N 300 
LYS   HB2  H N N 301 
LYS   HB3  H N N 302 
LYS   HG2  H N N 303 
LYS   HG3  H N N 304 
LYS   HD2  H N N 305 
LYS   HD3  H N N 306 
LYS   HE2  H N N 307 
LYS   HE3  H N N 308 
LYS   HZ1  H N N 309 
LYS   HZ2  H N N 310 
LYS   HZ3  H N N 311 
LYS   HXT  H N N 312 
MET   N    N N N 313 
MET   CA   C N S 314 
MET   C    C N N 315 
MET   O    O N N 316 
MET   CB   C N N 317 
MET   CG   C N N 318 
MET   SD   S N N 319 
MET   CE   C N N 320 
MET   OXT  O N N 321 
MET   H    H N N 322 
MET   H2   H N N 323 
MET   HA   H N N 324 
MET   HB2  H N N 325 
MET   HB3  H N N 326 
MET   HG2  H N N 327 
MET   HG3  H N N 328 
MET   HE1  H N N 329 
MET   HE2  H N N 330 
MET   HE3  H N N 331 
MET   HXT  H N N 332 
PHE   N    N N N 333 
PHE   CA   C N S 334 
PHE   C    C N N 335 
PHE   O    O N N 336 
PHE   CB   C N N 337 
PHE   CG   C Y N 338 
PHE   CD1  C Y N 339 
PHE   CD2  C Y N 340 
PHE   CE1  C Y N 341 
PHE   CE2  C Y N 342 
PHE   CZ   C Y N 343 
PHE   OXT  O N N 344 
PHE   H    H N N 345 
PHE   H2   H N N 346 
PHE   HA   H N N 347 
PHE   HB2  H N N 348 
PHE   HB3  H N N 349 
PHE   HD1  H N N 350 
PHE   HD2  H N N 351 
PHE   HE1  H N N 352 
PHE   HE2  H N N 353 
PHE   HZ   H N N 354 
PHE   HXT  H N N 355 
PRO   N    N N N 356 
PRO   CA   C N S 357 
PRO   C    C N N 358 
PRO   O    O N N 359 
PRO   CB   C N N 360 
PRO   CG   C N N 361 
PRO   CD   C N N 362 
PRO   OXT  O N N 363 
PRO   H    H N N 364 
PRO   HA   H N N 365 
PRO   HB2  H N N 366 
PRO   HB3  H N N 367 
PRO   HG2  H N N 368 
PRO   HG3  H N N 369 
PRO   HD2  H N N 370 
PRO   HD3  H N N 371 
PRO   HXT  H N N 372 
SER   N    N N N 373 
SER   CA   C N S 374 
SER   C    C N N 375 
SER   O    O N N 376 
SER   CB   C N N 377 
SER   OG   O N N 378 
SER   OXT  O N N 379 
SER   H    H N N 380 
SER   H2   H N N 381 
SER   HA   H N N 382 
SER   HB2  H N N 383 
SER   HB3  H N N 384 
SER   HG   H N N 385 
SER   HXT  H N N 386 
THR   N    N N N 387 
THR   CA   C N S 388 
THR   C    C N N 389 
THR   O    O N N 390 
THR   CB   C N R 391 
THR   OG1  O N N 392 
THR   CG2  C N N 393 
THR   OXT  O N N 394 
THR   H    H N N 395 
THR   H2   H N N 396 
THR   HA   H N N 397 
THR   HB   H N N 398 
THR   HG1  H N N 399 
THR   HG21 H N N 400 
THR   HG22 H N N 401 
THR   HG23 H N N 402 
THR   HXT  H N N 403 
TRP   N    N N N 404 
TRP   CA   C N S 405 
TRP   C    C N N 406 
TRP   O    O N N 407 
TRP   CB   C N N 408 
TRP   CG   C Y N 409 
TRP   CD1  C Y N 410 
TRP   CD2  C Y N 411 
TRP   NE1  N Y N 412 
TRP   CE2  C Y N 413 
TRP   CE3  C Y N 414 
TRP   CZ2  C Y N 415 
TRP   CZ3  C Y N 416 
TRP   CH2  C Y N 417 
TRP   OXT  O N N 418 
TRP   H    H N N 419 
TRP   H2   H N N 420 
TRP   HA   H N N 421 
TRP   HB2  H N N 422 
TRP   HB3  H N N 423 
TRP   HD1  H N N 424 
TRP   HE1  H N N 425 
TRP   HE3  H N N 426 
TRP   HZ2  H N N 427 
TRP   HZ3  H N N 428 
TRP   HH2  H N N 429 
TRP   HXT  H N N 430 
TYR   N    N N N 431 
TYR   CA   C N S 432 
TYR   C    C N N 433 
TYR   O    O N N 434 
TYR   CB   C N N 435 
TYR   CG   C Y N 436 
TYR   CD1  C Y N 437 
TYR   CD2  C Y N 438 
TYR   CE1  C Y N 439 
TYR   CE2  C Y N 440 
TYR   CZ   C Y N 441 
TYR   OH   O N N 442 
TYR   OXT  O N N 443 
TYR   H    H N N 444 
TYR   H2   H N N 445 
TYR   HA   H N N 446 
TYR   HB2  H N N 447 
TYR   HB3  H N N 448 
TYR   HD1  H N N 449 
TYR   HD2  H N N 450 
TYR   HE1  H N N 451 
TYR   HE2  H N N 452 
TYR   HH   H N N 453 
TYR   HXT  H N N 454 
VAL   N    N N N 455 
VAL   CA   C N S 456 
VAL   C    C N N 457 
VAL   O    O N N 458 
VAL   CB   C N N 459 
VAL   CG1  C N N 460 
VAL   CG2  C N N 461 
VAL   OXT  O N N 462 
VAL   H    H N N 463 
VAL   H2   H N N 464 
VAL   HA   H N N 465 
VAL   HB   H N N 466 
VAL   HG11 H N N 467 
VAL   HG12 H N N 468 
VAL   HG13 H N N 469 
VAL   HG21 H N N 470 
VAL   HG22 H N N 471 
VAL   HG23 H N N 472 
VAL   HXT  H N N 473 
# 
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 
A1EJS C34 O32  sing N N 1   
A1EJS N   CA   sing N N 2   
A1EJS O32 C31  sing N N 3   
A1EJS O   C    doub N N 4   
A1EJS C27 C28  doub Y N 5   
A1EJS C27 C26  sing Y N 6   
A1EJS CA  CB   sing N N 7   
A1EJS CA  C    sing N N 8   
A1EJS CB  CG   sing N N 9   
A1EJS C28 C29  sing Y N 10  
A1EJS C31 C26  sing N N 11  
A1EJS C31 O33  doub N N 12  
A1EJS C26 C25  doub Y N 13  
A1EJS CD  CG   sing N N 14  
A1EJS CD  CE   sing N N 15  
A1EJS C29 F48  sing N N 16  
A1EJS C29 C30  doub Y N 17  
A1EJS O14 C11  doub N N 18  
A1EJS C25 C30  sing Y N 19  
A1EJS C25 N24  sing N N 20  
A1EJS C11 C12  sing N N 21  
A1EJS C11 C10  sing N N 22  
A1EJS CE  NZ   sing N N 23  
A1EJS O15 C12  doub N N 24  
A1EJS N24 C22  sing N N 25  
A1EJS C12 C13  sing N N 26  
A1EJS C10 NZ   sing N N 27  
A1EJS C10 C13  doub N N 28  
A1EJS C13 N16  sing N N 29  
A1EJS C22 N21  doub Y N 30  
A1EJS C22 C17  sing Y N 31  
A1EJS N16 C17  sing N N 32  
A1EJS N21 C20  sing Y N 33  
A1EJS C17 C18  doub Y N 34  
A1EJS C20 N23  sing N N 35  
A1EJS C20 N19  doub Y N 36  
A1EJS C18 N19  sing Y N 37  
A1EJS N23 C35  sing N N 38  
A1EJS C35 C36  sing N N 39  
A1EJS C41 C36  doub Y N 40  
A1EJS C41 C40  sing Y N 41  
A1EJS C36 C37  sing Y N 42  
A1EJS C47 N46  sing N N 43  
A1EJS N46 C45  sing Y N 44  
A1EJS N46 C42  sing Y N 45  
A1EJS C45 C44  doub Y N 46  
A1EJS C42 C40  sing N N 47  
A1EJS C42 N43  doub Y N 48  
A1EJS C40 C39  doub Y N 49  
A1EJS C37 C38  doub Y N 50  
A1EJS C44 N43  sing Y N 51  
A1EJS C39 C38  sing Y N 52  
A1EJS C30 H301 sing N N 53  
A1EJS C28 H281 sing N N 54  
A1EJS C27 H271 sing N N 55  
A1EJS C18 H181 sing N N 56  
A1EJS CE  HE2  sing N N 57  
A1EJS CE  HE3  sing N N 58  
A1EJS CD  HD3  sing N N 59  
A1EJS CD  HD2  sing N N 60  
A1EJS CG  HG2  sing N N 61  
A1EJS CG  HG3  sing N N 62  
A1EJS CB  HB2  sing N N 63  
A1EJS CB  HB3  sing N N 64  
A1EJS CA  HA   sing N N 65  
A1EJS C34 H341 sing N N 66  
A1EJS C34 H343 sing N N 67  
A1EJS C34 H342 sing N N 68  
A1EJS C35 H352 sing N N 69  
A1EJS C35 H351 sing N N 70  
A1EJS C37 H371 sing N N 71  
A1EJS C38 H381 sing N N 72  
A1EJS C39 H391 sing N N 73  
A1EJS C41 H411 sing N N 74  
A1EJS C44 H441 sing N N 75  
A1EJS C45 H451 sing N N 76  
A1EJS C47 H472 sing N N 77  
A1EJS C47 H473 sing N N 78  
A1EJS C47 H471 sing N N 79  
A1EJS NZ  HZ1  sing N N 80  
A1EJS N   H    sing N N 81  
A1EJS N   H2   sing N N 82  
A1EJS N16 H161 sing N N 83  
A1EJS N23 H231 sing N N 84  
A1EJS N24 H241 sing N N 85  
A1EJS C   OXT  sing N N 86  
A1EJS OXT H1   sing N N 87  
ALA   N   CA   sing N N 88  
ALA   N   H    sing N N 89  
ALA   N   H2   sing N N 90  
ALA   CA  C    sing N N 91  
ALA   CA  CB   sing N N 92  
ALA   CA  HA   sing N N 93  
ALA   C   O    doub N N 94  
ALA   C   OXT  sing N N 95  
ALA   CB  HB1  sing N N 96  
ALA   CB  HB2  sing N N 97  
ALA   CB  HB3  sing N N 98  
ALA   OXT HXT  sing N N 99  
ARG   N   CA   sing N N 100 
ARG   N   H    sing N N 101 
ARG   N   H2   sing N N 102 
ARG   CA  C    sing N N 103 
ARG   CA  CB   sing N N 104 
ARG   CA  HA   sing N N 105 
ARG   C   O    doub N N 106 
ARG   C   OXT  sing N N 107 
ARG   CB  CG   sing N N 108 
ARG   CB  HB2  sing N N 109 
ARG   CB  HB3  sing N N 110 
ARG   CG  CD   sing N N 111 
ARG   CG  HG2  sing N N 112 
ARG   CG  HG3  sing N N 113 
ARG   CD  NE   sing N N 114 
ARG   CD  HD2  sing N N 115 
ARG   CD  HD3  sing N N 116 
ARG   NE  CZ   sing N N 117 
ARG   NE  HE   sing N N 118 
ARG   CZ  NH1  sing N N 119 
ARG   CZ  NH2  doub N N 120 
ARG   NH1 HH11 sing N N 121 
ARG   NH1 HH12 sing N N 122 
ARG   NH2 HH21 sing N N 123 
ARG   NH2 HH22 sing N N 124 
ARG   OXT HXT  sing N N 125 
ASN   N   CA   sing N N 126 
ASN   N   H    sing N N 127 
ASN   N   H2   sing N N 128 
ASN   CA  C    sing N N 129 
ASN   CA  CB   sing N N 130 
ASN   CA  HA   sing N N 131 
ASN   C   O    doub N N 132 
ASN   C   OXT  sing N N 133 
ASN   CB  CG   sing N N 134 
ASN   CB  HB2  sing N N 135 
ASN   CB  HB3  sing N N 136 
ASN   CG  OD1  doub N N 137 
ASN   CG  ND2  sing N N 138 
ASN   ND2 HD21 sing N N 139 
ASN   ND2 HD22 sing N N 140 
ASN   OXT HXT  sing N N 141 
ASP   N   CA   sing N N 142 
ASP   N   H    sing N N 143 
ASP   N   H2   sing N N 144 
ASP   CA  C    sing N N 145 
ASP   CA  CB   sing N N 146 
ASP   CA  HA   sing N N 147 
ASP   C   O    doub N N 148 
ASP   C   OXT  sing N N 149 
ASP   CB  CG   sing N N 150 
ASP   CB  HB2  sing N N 151 
ASP   CB  HB3  sing N N 152 
ASP   CG  OD1  doub N N 153 
ASP   CG  OD2  sing N N 154 
ASP   OD2 HD2  sing N N 155 
ASP   OXT HXT  sing N N 156 
CYS   N   CA   sing N N 157 
CYS   N   H    sing N N 158 
CYS   N   H2   sing N N 159 
CYS   CA  C    sing N N 160 
CYS   CA  CB   sing N N 161 
CYS   CA  HA   sing N N 162 
CYS   C   O    doub N N 163 
CYS   C   OXT  sing N N 164 
CYS   CB  SG   sing N N 165 
CYS   CB  HB2  sing N N 166 
CYS   CB  HB3  sing N N 167 
CYS   SG  HG   sing N N 168 
CYS   OXT HXT  sing N N 169 
GLN   N   CA   sing N N 170 
GLN   N   H    sing N N 171 
GLN   N   H2   sing N N 172 
GLN   CA  C    sing N N 173 
GLN   CA  CB   sing N N 174 
GLN   CA  HA   sing N N 175 
GLN   C   O    doub N N 176 
GLN   C   OXT  sing N N 177 
GLN   CB  CG   sing N N 178 
GLN   CB  HB2  sing N N 179 
GLN   CB  HB3  sing N N 180 
GLN   CG  CD   sing N N 181 
GLN   CG  HG2  sing N N 182 
GLN   CG  HG3  sing N N 183 
GLN   CD  OE1  doub N N 184 
GLN   CD  NE2  sing N N 185 
GLN   NE2 HE21 sing N N 186 
GLN   NE2 HE22 sing N N 187 
GLN   OXT HXT  sing N N 188 
GLU   N   CA   sing N N 189 
GLU   N   H    sing N N 190 
GLU   N   H2   sing N N 191 
GLU   CA  C    sing N N 192 
GLU   CA  CB   sing N N 193 
GLU   CA  HA   sing N N 194 
GLU   C   O    doub N N 195 
GLU   C   OXT  sing N N 196 
GLU   CB  CG   sing N N 197 
GLU   CB  HB2  sing N N 198 
GLU   CB  HB3  sing N N 199 
GLU   CG  CD   sing N N 200 
GLU   CG  HG2  sing N N 201 
GLU   CG  HG3  sing N N 202 
GLU   CD  OE1  doub N N 203 
GLU   CD  OE2  sing N N 204 
GLU   OE2 HE2  sing N N 205 
GLU   OXT HXT  sing N N 206 
GLY   N   CA   sing N N 207 
GLY   N   H    sing N N 208 
GLY   N   H2   sing N N 209 
GLY   CA  C    sing N N 210 
GLY   CA  HA2  sing N N 211 
GLY   CA  HA3  sing N N 212 
GLY   C   O    doub N N 213 
GLY   C   OXT  sing N N 214 
GLY   OXT HXT  sing N N 215 
HIS   N   CA   sing N N 216 
HIS   N   H    sing N N 217 
HIS   N   H2   sing N N 218 
HIS   CA  C    sing N N 219 
HIS   CA  CB   sing N N 220 
HIS   CA  HA   sing N N 221 
HIS   C   O    doub N N 222 
HIS   C   OXT  sing N N 223 
HIS   CB  CG   sing N N 224 
HIS   CB  HB2  sing N N 225 
HIS   CB  HB3  sing N N 226 
HIS   CG  ND1  sing Y N 227 
HIS   CG  CD2  doub Y N 228 
HIS   ND1 CE1  doub Y N 229 
HIS   ND1 HD1  sing N N 230 
HIS   CD2 NE2  sing Y N 231 
HIS   CD2 HD2  sing N N 232 
HIS   CE1 NE2  sing Y N 233 
HIS   CE1 HE1  sing N N 234 
HIS   NE2 HE2  sing N N 235 
HIS   OXT HXT  sing N N 236 
HOH   O   H1   sing N N 237 
HOH   O   H2   sing N N 238 
ILE   N   CA   sing N N 239 
ILE   N   H    sing N N 240 
ILE   N   H2   sing N N 241 
ILE   CA  C    sing N N 242 
ILE   CA  CB   sing N N 243 
ILE   CA  HA   sing N N 244 
ILE   C   O    doub N N 245 
ILE   C   OXT  sing N N 246 
ILE   CB  CG1  sing N N 247 
ILE   CB  CG2  sing N N 248 
ILE   CB  HB   sing N N 249 
ILE   CG1 CD1  sing N N 250 
ILE   CG1 HG12 sing N N 251 
ILE   CG1 HG13 sing N N 252 
ILE   CG2 HG21 sing N N 253 
ILE   CG2 HG22 sing N N 254 
ILE   CG2 HG23 sing N N 255 
ILE   CD1 HD11 sing N N 256 
ILE   CD1 HD12 sing N N 257 
ILE   CD1 HD13 sing N N 258 
ILE   OXT HXT  sing N N 259 
LEU   N   CA   sing N N 260 
LEU   N   H    sing N N 261 
LEU   N   H2   sing N N 262 
LEU   CA  C    sing N N 263 
LEU   CA  CB   sing N N 264 
LEU   CA  HA   sing N N 265 
LEU   C   O    doub N N 266 
LEU   C   OXT  sing N N 267 
LEU   CB  CG   sing N N 268 
LEU   CB  HB2  sing N N 269 
LEU   CB  HB3  sing N N 270 
LEU   CG  CD1  sing N N 271 
LEU   CG  CD2  sing N N 272 
LEU   CG  HG   sing N N 273 
LEU   CD1 HD11 sing N N 274 
LEU   CD1 HD12 sing N N 275 
LEU   CD1 HD13 sing N N 276 
LEU   CD2 HD21 sing N N 277 
LEU   CD2 HD22 sing N N 278 
LEU   CD2 HD23 sing N N 279 
LEU   OXT HXT  sing N N 280 
LYS   N   CA   sing N N 281 
LYS   N   H    sing N N 282 
LYS   N   H2   sing N N 283 
LYS   CA  C    sing N N 284 
LYS   CA  CB   sing N N 285 
LYS   CA  HA   sing N N 286 
LYS   C   O    doub N N 287 
LYS   C   OXT  sing N N 288 
LYS   CB  CG   sing N N 289 
LYS   CB  HB2  sing N N 290 
LYS   CB  HB3  sing N N 291 
LYS   CG  CD   sing N N 292 
LYS   CG  HG2  sing N N 293 
LYS   CG  HG3  sing N N 294 
LYS   CD  CE   sing N N 295 
LYS   CD  HD2  sing N N 296 
LYS   CD  HD3  sing N N 297 
LYS   CE  NZ   sing N N 298 
LYS   CE  HE2  sing N N 299 
LYS   CE  HE3  sing N N 300 
LYS   NZ  HZ1  sing N N 301 
LYS   NZ  HZ2  sing N N 302 
LYS   NZ  HZ3  sing N N 303 
LYS   OXT HXT  sing N N 304 
MET   N   CA   sing N N 305 
MET   N   H    sing N N 306 
MET   N   H2   sing N N 307 
MET   CA  C    sing N N 308 
MET   CA  CB   sing N N 309 
MET   CA  HA   sing N N 310 
MET   C   O    doub N N 311 
MET   C   OXT  sing N N 312 
MET   CB  CG   sing N N 313 
MET   CB  HB2  sing N N 314 
MET   CB  HB3  sing N N 315 
MET   CG  SD   sing N N 316 
MET   CG  HG2  sing N N 317 
MET   CG  HG3  sing N N 318 
MET   SD  CE   sing N N 319 
MET   CE  HE1  sing N N 320 
MET   CE  HE2  sing N N 321 
MET   CE  HE3  sing N N 322 
MET   OXT HXT  sing N N 323 
PHE   N   CA   sing N N 324 
PHE   N   H    sing N N 325 
PHE   N   H2   sing N N 326 
PHE   CA  C    sing N N 327 
PHE   CA  CB   sing N N 328 
PHE   CA  HA   sing N N 329 
PHE   C   O    doub N N 330 
PHE   C   OXT  sing N N 331 
PHE   CB  CG   sing N N 332 
PHE   CB  HB2  sing N N 333 
PHE   CB  HB3  sing N N 334 
PHE   CG  CD1  doub Y N 335 
PHE   CG  CD2  sing Y N 336 
PHE   CD1 CE1  sing Y N 337 
PHE   CD1 HD1  sing N N 338 
PHE   CD2 CE2  doub Y N 339 
PHE   CD2 HD2  sing N N 340 
PHE   CE1 CZ   doub Y N 341 
PHE   CE1 HE1  sing N N 342 
PHE   CE2 CZ   sing Y N 343 
PHE   CE2 HE2  sing N N 344 
PHE   CZ  HZ   sing N N 345 
PHE   OXT HXT  sing N N 346 
PRO   N   CA   sing N N 347 
PRO   N   CD   sing N N 348 
PRO   N   H    sing N N 349 
PRO   CA  C    sing N N 350 
PRO   CA  CB   sing N N 351 
PRO   CA  HA   sing N N 352 
PRO   C   O    doub N N 353 
PRO   C   OXT  sing N N 354 
PRO   CB  CG   sing N N 355 
PRO   CB  HB2  sing N N 356 
PRO   CB  HB3  sing N N 357 
PRO   CG  CD   sing N N 358 
PRO   CG  HG2  sing N N 359 
PRO   CG  HG3  sing N N 360 
PRO   CD  HD2  sing N N 361 
PRO   CD  HD3  sing N N 362 
PRO   OXT HXT  sing N N 363 
SER   N   CA   sing N N 364 
SER   N   H    sing N N 365 
SER   N   H2   sing N N 366 
SER   CA  C    sing N N 367 
SER   CA  CB   sing N N 368 
SER   CA  HA   sing N N 369 
SER   C   O    doub N N 370 
SER   C   OXT  sing N N 371 
SER   CB  OG   sing N N 372 
SER   CB  HB2  sing N N 373 
SER   CB  HB3  sing N N 374 
SER   OG  HG   sing N N 375 
SER   OXT HXT  sing N N 376 
THR   N   CA   sing N N 377 
THR   N   H    sing N N 378 
THR   N   H2   sing N N 379 
THR   CA  C    sing N N 380 
THR   CA  CB   sing N N 381 
THR   CA  HA   sing N N 382 
THR   C   O    doub N N 383 
THR   C   OXT  sing N N 384 
THR   CB  OG1  sing N N 385 
THR   CB  CG2  sing N N 386 
THR   CB  HB   sing N N 387 
THR   OG1 HG1  sing N N 388 
THR   CG2 HG21 sing N N 389 
THR   CG2 HG22 sing N N 390 
THR   CG2 HG23 sing N N 391 
THR   OXT HXT  sing N N 392 
TRP   N   CA   sing N N 393 
TRP   N   H    sing N N 394 
TRP   N   H2   sing N N 395 
TRP   CA  C    sing N N 396 
TRP   CA  CB   sing N N 397 
TRP   CA  HA   sing N N 398 
TRP   C   O    doub N N 399 
TRP   C   OXT  sing N N 400 
TRP   CB  CG   sing N N 401 
TRP   CB  HB2  sing N N 402 
TRP   CB  HB3  sing N N 403 
TRP   CG  CD1  doub Y N 404 
TRP   CG  CD2  sing Y N 405 
TRP   CD1 NE1  sing Y N 406 
TRP   CD1 HD1  sing N N 407 
TRP   CD2 CE2  doub Y N 408 
TRP   CD2 CE3  sing Y N 409 
TRP   NE1 CE2  sing Y N 410 
TRP   NE1 HE1  sing N N 411 
TRP   CE2 CZ2  sing Y N 412 
TRP   CE3 CZ3  doub Y N 413 
TRP   CE3 HE3  sing N N 414 
TRP   CZ2 CH2  doub Y N 415 
TRP   CZ2 HZ2  sing N N 416 
TRP   CZ3 CH2  sing Y N 417 
TRP   CZ3 HZ3  sing N N 418 
TRP   CH2 HH2  sing N N 419 
TRP   OXT HXT  sing N N 420 
TYR   N   CA   sing N N 421 
TYR   N   H    sing N N 422 
TYR   N   H2   sing N N 423 
TYR   CA  C    sing N N 424 
TYR   CA  CB   sing N N 425 
TYR   CA  HA   sing N N 426 
TYR   C   O    doub N N 427 
TYR   C   OXT  sing N N 428 
TYR   CB  CG   sing N N 429 
TYR   CB  HB2  sing N N 430 
TYR   CB  HB3  sing N N 431 
TYR   CG  CD1  doub Y N 432 
TYR   CG  CD2  sing Y N 433 
TYR   CD1 CE1  sing Y N 434 
TYR   CD1 HD1  sing N N 435 
TYR   CD2 CE2  doub Y N 436 
TYR   CD2 HD2  sing N N 437 
TYR   CE1 CZ   doub Y N 438 
TYR   CE1 HE1  sing N N 439 
TYR   CE2 CZ   sing Y N 440 
TYR   CE2 HE2  sing N N 441 
TYR   CZ  OH   sing N N 442 
TYR   OH  HH   sing N N 443 
TYR   OXT HXT  sing N N 444 
VAL   N   CA   sing N N 445 
VAL   N   H    sing N N 446 
VAL   N   H2   sing N N 447 
VAL   CA  C    sing N N 448 
VAL   CA  CB   sing N N 449 
VAL   CA  HA   sing N N 450 
VAL   C   O    doub N N 451 
VAL   C   OXT  sing N N 452 
VAL   CB  CG1  sing N N 453 
VAL   CB  CG2  sing N N 454 
VAL   CB  HB   sing N N 455 
VAL   CG1 HG11 sing N N 456 
VAL   CG1 HG12 sing N N 457 
VAL   CG1 HG13 sing N N 458 
VAL   CG2 HG21 sing N N 459 
VAL   CG2 HG22 sing N N 460 
VAL   CG2 HG23 sing N N 461 
VAL   OXT HXT  sing N N 462 
# 
_pdbx_audit_support.funding_organization   'National Natural Science Foundation of China (NSFC)' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           22077019 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   1J7D 
_pdbx_initial_refinement_model.details          'heterodimer in PDB was seperated into 2 monomer used in ensemble search' 
# 
_atom_sites.entry_id                    9LHJ 
_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]   0.016022 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000868 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.013966 
_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]   0.014607 
_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 
F 
H 
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    . GLY   A 1 3   ? 26.674  -30.512 -47.167 1.00 43.55 ?  3   GLY   A N    1 
ATOM   2    C CA   . GLY   A 1 3   ? 25.662  -29.849 -47.975 1.00 45.93 ?  3   GLY   A CA   1 
ATOM   3    C C    . GLY   A 1 3   ? 24.810  -28.828 -47.233 1.00 50.16 ?  3   GLY   A C    1 
ATOM   4    O O    . GLY   A 1 3   ? 24.412  -29.052 -46.090 1.00 43.21 ?  3   GLY   A O    1 
ATOM   5    N N    . LEU   A 1 4   ? 24.527  -27.704 -47.886 1.00 43.77 ?  4   LEU   A N    1 
ATOM   6    C CA   . LEU   A 1 4   ? 23.671  -26.686 -47.294 1.00 42.24 ?  4   LEU   A CA   1 
ATOM   7    C C    . LEU   A 1 4   ? 22.305  -27.282 -46.968 1.00 30.81 ?  4   LEU   A C    1 
ATOM   8    O O    . LEU   A 1 4   ? 21.615  -27.766 -47.880 1.00 35.93 ?  4   LEU   A O    1 
ATOM   9    C CB   . LEU   A 1 4   ? 23.509  -25.497 -48.236 1.00 48.53 ?  4   LEU   A CB   1 
ATOM   10   C CG   . LEU   A 1 4   ? 22.752  -24.318 -47.619 1.00 41.44 ?  4   LEU   A CG   1 
ATOM   11   C CD1  . LEU   A 1 4   ? 23.412  -23.852 -46.327 1.00 41.02 ?  4   LEU   A CD1  1 
ATOM   12   C CD2  . LEU   A 1 4   ? 22.616  -23.175 -48.615 1.00 45.90 ?  4   LEU   A CD2  1 
ATOM   13   N N    . PRO   A 1 5   ? 21.876  -27.266 -45.707 1.00 29.24 ?  5   PRO   A N    1 
ATOM   14   C CA   . PRO   A 1 5   ? 20.612  -27.925 -45.349 1.00 33.13 ?  5   PRO   A CA   1 
ATOM   15   C C    . PRO   A 1 5   ? 19.428  -27.323 -46.087 1.00 36.53 ?  5   PRO   A C    1 
ATOM   16   O O    . PRO   A 1 5   ? 19.300  -26.101 -46.207 1.00 29.00 ?  5   PRO   A O    1 
ATOM   17   C CB   . PRO   A 1 5   ? 20.500  -27.693 -43.840 1.00 35.72 ?  5   PRO   A CB   1 
ATOM   18   C CG   . PRO   A 1 5   ? 21.888  -27.362 -43.389 1.00 30.16 ?  5   PRO   A CG   1 
ATOM   19   C CD   . PRO   A 1 5   ? 22.592  -26.733 -44.537 1.00 36.43 ?  5   PRO   A CD   1 
ATOM   20   N N    . ARG   A 1 6   ? 18.557  -28.212 -46.579 1.00 28.96 ?  6   ARG   A N    1 
ATOM   21   C CA   . ARG   A 1 6   ? 17.339  -27.799 -47.276 1.00 29.02 ?  6   ARG   A CA   1 
ATOM   22   C C    . ARG   A 1 6   ? 16.513  -26.821 -46.442 1.00 28.22 ?  6   ARG   A C    1 
ATOM   23   O O    . ARG   A 1 6   ? 15.899  -25.889 -46.983 1.00 26.90 ?  6   ARG   A O    1 
ATOM   24   C CB   . ARG   A 1 6   ? 16.521  -29.044 -47.640 1.00 32.70 ?  6   ARG   A CB   1 
ATOM   25   C CG   . ARG   A 1 6   ? 15.186  -28.773 -48.316 1.00 36.57 ?  6   ARG   A CG   1 
ATOM   26   C CD   . ARG   A 1 6   ? 14.304  -30.025 -48.347 1.00 46.18 ?  6   ARG   A CD   1 
ATOM   27   N NE   . ARG   A 1 6   ? 12.877  -29.711 -48.387 1.00 56.98 ?  6   ARG   A NE   1 
ATOM   28   C CZ   . ARG   A 1 6   ? 12.170  -29.271 -47.354 1.00 53.23 ?  6   ARG   A CZ   1 
ATOM   29   N NH1  . ARG   A 1 6   ? 12.721  -29.086 -46.162 1.00 57.42 ?  6   ARG   A NH1  1 
ATOM   30   N NH2  . ARG   A 1 6   ? 10.874  -29.021 -47.516 1.00 54.80 ?  6   ARG   A NH2  1 
ATOM   31   N N    . ARG   A 1 7   ? 16.488  -27.016 -45.122 1.00 32.77 ?  7   ARG   A N    1 
ATOM   32   C CA   . ARG   A 1 7   ? 15.716  -26.126 -44.257 1.00 26.41 ?  7   ARG   A CA   1 
ATOM   33   C C    . ARG   A 1 7   ? 16.178  -24.675 -44.386 1.00 29.52 ?  7   ARG   A C    1 
ATOM   34   O O    . ARG   A 1 7   ? 15.354  -23.754 -44.400 1.00 27.16 ?  7   ARG   A O    1 
ATOM   35   C CB   . ARG   A 1 7   ? 15.813  -26.596 -42.809 1.00 33.95 ?  7   ARG   A CB   1 
ATOM   36   C CG   . ARG   A 1 7   ? 15.598  -25.477 -41.822 1.00 33.32 ?  7   ARG   A CG   1 
ATOM   37   C CD   . ARG   A 1 7   ? 14.762  -25.927 -40.671 1.00 34.39 ?  7   ARG   A CD   1 
ATOM   38   N NE   . ARG   A 1 7   ? 14.554  -24.831 -39.735 1.00 29.45 ?  7   ARG   A NE   1 
ATOM   39   C CZ   . ARG   A 1 7   ? 14.032  -24.978 -38.528 1.00 30.73 ?  7   ARG   A CZ   1 
ATOM   40   N NH1  . ARG   A 1 7   ? 13.591  -26.154 -38.104 1.00 30.51 ?  7   ARG   A NH1  1 
ATOM   41   N NH2  . ARG   A 1 7   ? 13.964  -23.925 -37.723 1.00 25.94 ?  7   ARG   A NH2  1 
ATOM   42   N N    . ILE   A 1 8   ? 17.492  -24.450 -44.481 1.00 26.14 ?  8   ILE   A N    1 
ATOM   43   C CA   . ILE   A 1 8   ? 17.991  -23.085 -44.635 1.00 25.08 ?  8   ILE   A CA   1 
ATOM   44   C C    . ILE   A 1 8   ? 17.561  -22.495 -45.979 1.00 27.79 ?  8   ILE   A C    1 
ATOM   45   O O    . ILE   A 1 8   ? 17.140  -21.332 -46.058 1.00 25.93 ?  8   ILE   A O    1 
ATOM   46   C CB   . ILE   A 1 8   ? 19.517  -23.055 -44.443 1.00 28.64 ?  8   ILE   A CB   1 
ATOM   47   C CG1  . ILE   A 1 8   ? 19.852  -23.371 -42.988 1.00 25.29 ?  8   ILE   A CG1  1 
ATOM   48   C CG2  . ILE   A 1 8   ? 20.078  -21.701 -44.824 1.00 29.25 ?  8   ILE   A CG2  1 
ATOM   49   C CD1  . ILE   A 1 8   ? 21.340  -23.278 -42.666 1.00 24.23 ?  8   ILE   A CD1  1 
ATOM   50   N N    . ILE   A 1 9   ? 17.625  -23.293 -47.053 1.00 24.88 ?  9   ILE   A N    1 
ATOM   51   C CA   . ILE   A 1 9   ? 17.186  -22.809 -48.362 1.00 29.51 ?  9   ILE   A CA   1 
ATOM   52   C C    . ILE   A 1 9   ? 15.713  -22.408 -48.321 1.00 22.42 ?  9   ILE   A C    1 
ATOM   53   O O    . ILE   A 1 9   ? 15.316  -21.343 -48.824 1.00 24.58 ?  9   ILE   A O    1 
ATOM   54   C CB   . ILE   A 1 9   ? 17.453  -23.877 -49.441 1.00 27.30 ?  9   ILE   A CB   1 
ATOM   55   C CG1  . ILE   A 1 9   ? 18.943  -23.932 -49.779 1.00 33.91 ?  9   ILE   A CG1  1 
ATOM   56   C CG2  . ILE   A 1 9   ? 16.649  -23.596 -50.702 1.00 32.16 ?  9   ILE   A CG2  1 
ATOM   57   C CD1  . ILE   A 1 9   ? 19.457  -25.330 -49.913 1.00 34.52 ?  9   ILE   A CD1  1 
ATOM   58   N N    . LYS   A 1 10  ? 14.880  -23.250 -47.708 1.00 25.28 ?  10  LYS   A N    1 
ATOM   59   C CA   . LYS   A 1 10  ? 13.446  -22.978 -47.683 1.00 29.05 ?  10  LYS   A CA   1 
ATOM   60   C C    . LYS   A 1 10  ? 13.130  -21.758 -46.819 1.00 29.09 ?  10  LYS   A C    1 
ATOM   61   O O    . LYS   A 1 10  ? 12.313  -20.914 -47.206 1.00 23.47 ?  10  LYS   A O    1 
ATOM   62   C CB   . LYS   A 1 10  ? 12.683  -24.210 -47.192 1.00 29.26 ?  10  LYS   A CB   1 
ATOM   63   C CG   . LYS   A 1 10  ? 12.809  -25.409 -48.135 1.00 41.34 ?  10  LYS   A CG   1 
ATOM   64   C CD   . LYS   A 1 10  ? 12.329  -25.085 -49.553 1.00 47.93 ?  10  LYS   A CD   1 
ATOM   65   C CE   . LYS   A 1 10  ? 12.014  -26.351 -50.357 1.00 49.23 ?  10  LYS   A CE   1 
ATOM   66   N NZ   . LYS   A 1 10  ? 10.699  -26.272 -51.071 1.00 51.66 ?  10  LYS   A NZ   1 
ATOM   67   N N    . GLU   A 1 11  ? 13.777  -21.634 -45.654 1.00 25.60 ?  11  GLU   A N    1 
ATOM   68   C CA   . GLU   A 1 11  ? 13.575  -20.438 -44.839 1.00 22.60 ?  11  GLU   A CA   1 
ATOM   69   C C    . GLU   A 1 11  ? 13.984  -19.180 -45.588 1.00 22.32 ?  11  GLU   A C    1 
ATOM   70   O O    . GLU   A 1 11  ? 13.306  -18.145 -45.494 1.00 28.61 ?  11  GLU   A O    1 
ATOM   71   C CB   . GLU   A 1 11  ? 14.352  -20.551 -43.520 1.00 22.48 ?  11  GLU   A CB   1 
ATOM   72   C CG   . GLU   A 1 11  ? 13.665  -21.403 -42.470 1.00 27.19 ?  11  GLU   A CG   1 
ATOM   73   C CD   . GLU   A 1 11  ? 14.205  -21.177 -41.058 1.00 23.40 ?  11  GLU   A CD   1 
ATOM   74   O OE1  . GLU   A 1 11  ? 13.947  -20.099 -40.482 1.00 21.22 ?  11  GLU   A OE1  1 
ATOM   75   O OE2  . GLU   A 1 11  ? 14.889  -22.078 -40.526 1.00 25.21 -1 11  GLU   A OE2  1 
ATOM   76   N N    . THR   A 1 12  ? 15.090  -19.238 -46.338 1.00 20.78 ?  12  THR   A N    1 
ATOM   77   C CA   . THR   A 1 12  ? 15.536  -18.063 -47.079 1.00 21.07 ?  12  THR   A CA   1 
ATOM   78   C C    . THR   A 1 12  ? 14.517  -17.672 -48.137 1.00 23.29 ?  12  THR   A C    1 
ATOM   79   O O    . THR   A 1 12  ? 14.179  -16.488 -48.299 1.00 25.30 ?  12  THR   A O    1 
ATOM   80   C CB   . THR   A 1 12  ? 16.899  -18.337 -47.720 1.00 24.18 ?  12  THR   A CB   1 
ATOM   81   O OG1  . THR   A 1 12  ? 17.823  -18.769 -46.718 1.00 27.25 ?  12  THR   A OG1  1 
ATOM   82   C CG2  . THR   A 1 12  ? 17.435  -17.090 -48.409 1.00 26.38 ?  12  THR   A CG2  1 
ATOM   83   N N    . GLN   A 1 13  ? 14.032  -18.667 -48.888 1.00 23.25 ?  13  GLN   A N    1 
ATOM   84   C CA   . GLN   A 1 13  ? 12.988  -18.397 -49.871 1.00 23.43 ?  13  GLN   A CA   1 
ATOM   85   C C    . GLN   A 1 13  ? 11.768  -17.761 -49.218 1.00 25.62 ?  13  GLN   A C    1 
ATOM   86   O O    . GLN   A 1 13  ? 11.168  -16.825 -49.772 1.00 23.82 ?  13  GLN   A O    1 
ATOM   87   C CB   . GLN   A 1 13  ? 12.589  -19.687 -50.590 1.00 28.62 ?  13  GLN   A CB   1 
ATOM   88   C CG   . GLN   A 1 13  ? 13.367  -20.000 -51.856 1.00 42.59 ?  13  GLN   A CG   1 
ATOM   89   C CD   . GLN   A 1 13  ? 13.489  -21.494 -52.119 1.00 42.34 ?  13  GLN   A CD   1 
ATOM   90   O OE1  . GLN   A 1 13  ? 12.646  -22.288 -51.683 1.00 42.32 ?  13  GLN   A OE1  1 
ATOM   91   N NE2  . GLN   A 1 13  ? 14.470  -21.869 -52.932 1.00 29.80 ?  13  GLN   A NE2  1 
ATOM   92   N N    . ARG   A 1 14  ? 11.378  -18.270 -48.044 1.00 24.78 ?  14  ARG   A N    1 
ATOM   93   C CA   . ARG   A 1 14  ? 10.199  -17.755 -47.354 1.00 25.30 ?  14  ARG   A CA   1 
ATOM   94   C C    . ARG   A 1 14  ? 10.404  -16.317 -46.905 1.00 31.27 ?  14  ARG   A C    1 
ATOM   95   O O    . ARG   A 1 14  ? 9.463   -15.513 -46.934 1.00 28.30 ?  14  ARG   A O    1 
ATOM   96   C CB   . ARG   A 1 14  ? 9.859   -18.635 -46.149 1.00 37.42 ?  14  ARG   A CB   1 
ATOM   97   C CG   . ARG   A 1 14  ? 9.507   -20.078 -46.474 1.00 36.89 ?  14  ARG   A CG   1 
ATOM   98   C CD   . ARG   A 1 14  ? 8.398   -20.614 -45.564 1.00 53.45 ?  14  ARG   A CD   1 
ATOM   99   N NE   . ARG   A 1 14  ? 7.141   -20.806 -46.284 1.00 69.34 ?  14  ARG   A NE   1 
ATOM   100  C CZ   . ARG   A 1 14  ? 6.073   -21.422 -45.792 1.00 70.19 ?  14  ARG   A CZ   1 
ATOM   101  N NH1  . ARG   A 1 14  ? 6.072   -21.942 -44.574 1.00 70.18 ?  14  ARG   A NH1  1 
ATOM   102  N NH2  . ARG   A 1 14  ? 4.980   -21.526 -46.544 1.00 67.54 ?  14  ARG   A NH2  1 
ATOM   103  N N    . LEU   A 1 15  ? 11.616  -15.987 -46.442 1.00 28.00 ?  15  LEU   A N    1 
ATOM   104  C CA   . LEU   A 1 15  ? 11.896  -14.615 -46.029 1.00 27.20 ?  15  LEU   A CA   1 
ATOM   105  C C    . LEU   A 1 15  ? 11.777  -13.663 -47.209 1.00 29.33 ?  15  LEU   A C    1 
ATOM   106  O O    . LEU   A 1 15  ? 11.307  -12.527 -47.061 1.00 27.91 ?  15  LEU   A O    1 
ATOM   107  C CB   . LEU   A 1 15  ? 13.295  -14.518 -45.417 1.00 28.19 ?  15  LEU   A CB   1 
ATOM   108  C CG   . LEU   A 1 15  ? 13.498  -14.988 -43.981 1.00 31.37 ?  15  LEU   A CG   1 
ATOM   109  C CD1  . LEU   A 1 15  ? 14.953  -14.851 -43.602 1.00 31.97 ?  15  LEU   A CD1  1 
ATOM   110  C CD2  . LEU   A 1 15  ? 12.605  -14.206 -43.026 1.00 24.48 ?  15  LEU   A CD2  1 
ATOM   111  N N    . LEU   A 1 16  ? 12.215  -14.108 -48.392 1.00 24.50 ?  16  LEU   A N    1 
ATOM   112  C CA   . LEU   A 1 16  ? 12.126  -13.242 -49.565 1.00 24.28 ?  16  LEU   A CA   1 
ATOM   113  C C    . LEU   A 1 16  ? 10.682  -13.102 -50.040 1.00 27.79 ?  16  LEU   A C    1 
ATOM   114  O O    . LEU   A 1 16  ? 10.262  -12.018 -50.466 1.00 33.25 ?  16  LEU   A O    1 
ATOM   115  C CB   . LEU   A 1 16  ? 13.020  -13.786 -50.687 1.00 30.34 ?  16  LEU   A CB   1 
ATOM   116  C CG   . LEU   A 1 16  ? 12.787  -13.223 -52.091 1.00 41.11 ?  16  LEU   A CG   1 
ATOM   117  C CD1  . LEU   A 1 16  ? 13.084  -11.733 -52.110 1.00 36.41 ?  16  LEU   A CD1  1 
ATOM   118  C CD2  . LEU   A 1 16  ? 13.636  -13.965 -53.134 1.00 37.62 ?  16  LEU   A CD2  1 
ATOM   119  N N    . ALA   A 1 17  ? 9.907   -14.185 -49.959 1.00 26.23 ?  17  ALA   A N    1 
ATOM   120  C CA   . ALA   A 1 17  ? 8.546   -14.202 -50.496 1.00 36.37 ?  17  ALA   A CA   1 
ATOM   121  C C    . ALA   A 1 17  ? 7.528   -13.568 -49.550 1.00 39.72 ?  17  ALA   A C    1 
ATOM   122  O O    . ALA   A 1 17  ? 6.574   -12.926 -50.008 1.00 33.53 ?  17  ALA   A O    1 
ATOM   123  C CB   . ALA   A 1 17  ? 8.128   -15.641 -50.813 1.00 31.93 ?  17  ALA   A CB   1 
ATOM   124  N N    . GLU   A 1 18  ? 7.671   -13.774 -48.239 1.00 27.74 ?  18  GLU   A N    1 
ATOM   125  C CA   . GLU   A 1 18  ? 6.719   -13.258 -47.252 1.00 25.80 ?  18  GLU   A CA   1 
ATOM   126  C C    . GLU   A 1 18  ? 7.482   -12.560 -46.136 1.00 31.76 ?  18  GLU   A C    1 
ATOM   127  O O    . GLU   A 1 18  ? 7.688   -13.130 -45.059 1.00 28.88 ?  18  GLU   A O    1 
ATOM   128  C CB   . GLU   A 1 18  ? 5.825   -14.362 -46.675 1.00 38.49 ?  18  GLU   A CB   1 
ATOM   129  C CG   . GLU   A 1 18  ? 5.559   -15.542 -47.603 1.00 44.91 ?  18  GLU   A CG   1 
ATOM   130  C CD   . GLU   A 1 18  ? 5.034   -16.778 -46.871 1.00 58.69 ?  18  GLU   A CD   1 
ATOM   131  O OE1  . GLU   A 1 18  ? 4.574   -16.649 -45.713 1.00 53.53 ?  18  GLU   A OE1  1 
ATOM   132  O OE2  . GLU   A 1 18  ? 5.073   -17.881 -47.464 1.00 61.51 -1 18  GLU   A OE2  1 
ATOM   133  N N    . PRO   A 1 19  ? 7.908   -11.321 -46.352 1.00 33.04 ?  19  PRO   A N    1 
ATOM   134  C CA   . PRO   A 1 19  ? 8.662   -10.620 -45.307 1.00 34.58 ?  19  PRO   A CA   1 
ATOM   135  C C    . PRO   A 1 19  ? 7.779   -10.282 -44.113 1.00 40.76 ?  19  PRO   A C    1 
ATOM   136  O O    . PRO   A 1 19  ? 6.549   -10.245 -44.196 1.00 33.25 ?  19  PRO   A O    1 
ATOM   137  C CB   . PRO   A 1 19  ? 9.165   -9.352  -46.005 1.00 34.21 ?  19  PRO   A CB   1 
ATOM   138  C CG   . PRO   A 1 19  ? 8.295   -9.175  -47.216 1.00 38.33 ?  19  PRO   A CG   1 
ATOM   139  C CD   . PRO   A 1 19  ? 7.714   -10.516 -47.572 1.00 35.87 ?  19  PRO   A CD   1 
ATOM   140  N N    . VAL   A 1 20  ? 8.435   -10.065 -42.980 1.00 32.11 ?  20  VAL   A N    1 
ATOM   141  C CA   . VAL   A 1 20  ? 7.741   -9.608  -41.773 1.00 28.77 ?  20  VAL   A CA   1 
ATOM   142  C C    . VAL   A 1 20  ? 7.515   -8.102  -41.874 1.00 34.83 ?  20  VAL   A C    1 
ATOM   143  O O    . VAL   A 1 20  ? 8.469   -7.361  -42.144 1.00 28.43 ?  20  VAL   A O    1 
ATOM   144  C CB   . VAL   A 1 20  ? 8.551   -9.958  -40.531 1.00 32.93 ?  20  VAL   A CB   1 
ATOM   145  C CG1  . VAL   A 1 20  ? 7.785   -9.562  -39.295 1.00 33.47 ?  20  VAL   A CG1  1 
ATOM   146  C CG2  . VAL   A 1 20  ? 8.882   -11.458 -40.512 1.00 33.97 ?  20  VAL   A CG2  1 
ATOM   147  N N    . PRO   A 1 21  ? 6.293   -7.610  -41.666 1.00 30.36 ?  21  PRO   A N    1 
ATOM   148  C CA   . PRO   A 1 21  ? 6.060   -6.158  -41.706 1.00 26.28 ?  21  PRO   A CA   1 
ATOM   149  C C    . PRO   A 1 21  ? 6.988   -5.417  -40.745 1.00 20.01 ?  21  PRO   A C    1 
ATOM   150  O O    . PRO   A 1 21  ? 7.175   -5.835  -39.604 1.00 20.56 ?  21  PRO   A O    1 
ATOM   151  C CB   . PRO   A 1 21  ? 4.595   -6.019  -41.279 1.00 33.32 ?  21  PRO   A CB   1 
ATOM   152  C CG   . PRO   A 1 21  ? 3.998   -7.369  -41.439 1.00 34.19 ?  21  PRO   A CG   1 
ATOM   153  C CD   . PRO   A 1 21  ? 5.086   -8.374  -41.311 1.00 36.95 ?  21  PRO   A CD   1 
ATOM   154  N N    . GLY   A 1 22  ? 7.552   -4.300  -41.210 1.00 20.45 ?  22  GLY   A N    1 
ATOM   155  C CA   . GLY   A 1 22  ? 8.517   -3.540  -40.438 1.00 20.94 ?  22  GLY   A CA   1 
ATOM   156  C C    . GLY   A 1 22  ? 9.929   -4.103  -40.390 1.00 19.42 ?  22  GLY   A C    1 
ATOM   157  O O    . GLY   A 1 22  ? 10.791  -3.497  -39.733 1.00 18.22 ?  22  GLY   A O    1 
ATOM   158  N N    . ILE   A 1 23  ? 10.196  -5.239  -41.038 1.00 14.47 ?  23  ILE   A N    1 
ATOM   159  C CA   . ILE   A 1 23  ? 11.493  -5.914  -40.968 1.00 12.60 ?  23  ILE   A CA   1 
ATOM   160  C C    . ILE   A 1 23  ? 11.978  -6.229  -42.370 1.00 21.32 ?  23  ILE   A C    1 
ATOM   161  O O    . ILE   A 1 23  ? 11.252  -6.846  -43.158 1.00 22.16 ?  23  ILE   A O    1 
ATOM   162  C CB   . ILE   A 1 23  ? 11.420  -7.219  -40.149 1.00 14.89 ?  23  ILE   A CB   1 
ATOM   163  C CG1  . ILE   A 1 23  ? 10.797  -6.944  -38.785 1.00 15.92 ?  23  ILE   A CG1  1 
ATOM   164  C CG2  . ILE   A 1 23  ? 12.838  -7.840  -40.023 1.00 15.58 ?  23  ILE   A CG2  1 
ATOM   165  C CD1  . ILE   A 1 23  ? 10.824  -8.134  -37.827 1.00 20.58 ?  23  ILE   A CD1  1 
ATOM   166  N N    . LYS   A 1 24  ? 13.205  -5.829  -42.673 1.00 16.32 ?  24  LYS   A N    1 
ATOM   167  C CA   . LYS   A 1 24  ? 13.903  -6.287  -43.867 1.00 19.27 ?  24  LYS   A CA   1 
ATOM   168  C C    . LYS   A 1 24  ? 14.940  -7.325  -43.467 1.00 19.21 ?  24  LYS   A C    1 
ATOM   169  O O    . LYS   A 1 24  ? 15.646  -7.161  -42.468 1.00 19.01 ?  24  LYS   A O    1 
ATOM   170  C CB   . LYS   A 1 24  ? 14.605  -5.145  -44.611 1.00 24.57 ?  24  LYS   A CB   1 
ATOM   171  C CG   . LYS   A 1 24  ? 13.693  -4.128  -45.271 1.00 37.06 ?  24  LYS   A CG   1 
ATOM   172  C CD   . LYS   A 1 24  ? 14.484  -2.886  -45.652 1.00 43.10 ?  24  LYS   A CD   1 
ATOM   173  C CE   . LYS   A 1 24  ? 15.760  -3.263  -46.403 1.00 44.06 ?  24  LYS   A CE   1 
ATOM   174  N NZ   . LYS   A 1 24  ? 16.917  -2.387  -46.030 1.00 54.81 ?  24  LYS   A NZ   1 
ATOM   175  N N    . ALA   A 1 25  ? 15.040  -8.394  -44.248 1.00 21.07 ?  25  ALA   A N    1 
ATOM   176  C CA   . ALA   A 1 25  ? 16.012  -9.434  -43.924 1.00 18.45 ?  25  ALA   A CA   1 
ATOM   177  C C    . ALA   A 1 25  ? 16.487  -10.066 -45.218 1.00 19.88 ?  25  ALA   A C    1 
ATOM   178  O O    . ALA   A 1 25  ? 15.680  -10.641 -45.956 1.00 26.12 ?  25  ALA   A O    1 
ATOM   179  C CB   . ALA   A 1 25  ? 15.395  -10.488 -43.008 1.00 16.92 ?  25  ALA   A CB   1 
ATOM   180  N N    . GLU   A 1 26  ? 17.780  -9.937  -45.495 1.00 18.81 ?  26  GLU   A N    1 
ATOM   181  C CA   . GLU   A 1 26  ? 18.340  -10.360 -46.766 1.00 27.71 ?  26  GLU   A CA   1 
ATOM   182  C C    . GLU   A 1 26  ? 19.599  -11.173 -46.515 1.00 27.83 ?  26  GLU   A C    1 
ATOM   183  O O    . GLU   A 1 26  ? 20.396  -10.816 -45.644 1.00 22.73 ?  26  GLU   A O    1 
ATOM   184  C CB   . GLU   A 1 26  ? 18.684  -9.139  -47.615 1.00 28.07 ?  26  GLU   A CB   1 
ATOM   185  C CG   . GLU   A 1 26  ? 17.649  -8.038  -47.474 1.00 43.68 ?  26  GLU   A CG   1 
ATOM   186  C CD   . GLU   A 1 26  ? 17.688  -7.048  -48.605 1.00 46.54 ?  26  GLU   A CD   1 
ATOM   187  O OE1  . GLU   A 1 26  ? 17.673  -7.494  -49.770 1.00 46.16 ?  26  GLU   A OE1  1 
ATOM   188  O OE2  . GLU   A 1 26  ? 17.741  -5.829  -48.327 1.00 59.20 -1 26  GLU   A OE2  1 
ATOM   189  N N    . PRO   A 1 27  ? 19.810  -12.264 -47.245 1.00 24.00 ?  27  PRO   A N    1 
ATOM   190  C CA   . PRO   A 1 27  ? 21.070  -12.998 -47.092 1.00 22.73 ?  27  PRO   A CA   1 
ATOM   191  C C    . PRO   A 1 27  ? 22.234  -12.237 -47.715 1.00 23.09 ?  27  PRO   A C    1 
ATOM   192  O O    . PRO   A 1 27  ? 22.068  -11.446 -48.644 1.00 28.03 ?  27  PRO   A O    1 
ATOM   193  C CB   . PRO   A 1 27  ? 20.806  -14.324 -47.815 1.00 29.97 ?  27  PRO   A CB   1 
ATOM   194  C CG   . PRO   A 1 27  ? 19.733  -14.015 -48.795 1.00 34.73 ?  27  PRO   A CG   1 
ATOM   195  C CD   . PRO   A 1 27  ? 18.888  -12.923 -48.186 1.00 31.24 ?  27  PRO   A CD   1 
ATOM   196  N N    . ASP   A 1 28  ? 23.418  -12.467 -47.146 1.00 21.09 ?  28  ASP   A N    1 
ATOM   197  C CA   . ASP   A 1 28  ? 24.657  -11.878 -47.633 1.00 28.92 ?  28  ASP   A CA   1 
ATOM   198  C C    . ASP   A 1 28  ? 25.063  -12.548 -48.940 1.00 27.73 ?  28  ASP   A C    1 
ATOM   199  O O    . ASP   A 1 28  ? 25.050  -13.781 -49.045 1.00 29.25 ?  28  ASP   A O    1 
ATOM   200  C CB   . ASP   A 1 28  ? 25.755  -12.056 -46.582 1.00 21.14 ?  28  ASP   A CB   1 
ATOM   201  C CG   . ASP   A 1 28  ? 27.055  -11.366 -46.953 1.00 24.59 ?  28  ASP   A CG   1 
ATOM   202  O OD1  . ASP   A 1 28  ? 27.208  -10.158 -46.676 1.00 25.10 ?  28  ASP   A OD1  1 
ATOM   203  O OD2  . ASP   A 1 28  ? 27.939  -12.057 -47.503 1.00 29.71 -1 28  ASP   A OD2  1 
ATOM   204  N N    . GLU   A 1 29  ? 25.454  -11.734 -49.930 1.00 28.09 ?  29  GLU   A N    1 
ATOM   205  C CA   . GLU   A 1 29  ? 25.777  -12.294 -51.246 1.00 38.99 ?  29  GLU   A CA   1 
ATOM   206  C C    . GLU   A 1 29  ? 26.871  -13.350 -51.163 1.00 33.40 ?  29  GLU   A C    1 
ATOM   207  O O    . GLU   A 1 29  ? 26.872  -14.308 -51.947 1.00 33.67 ?  29  GLU   A O    1 
ATOM   208  C CB   . GLU   A 1 29  ? 26.224  -11.213 -52.234 1.00 38.57 ?  29  GLU   A CB   1 
ATOM   209  C CG   . GLU   A 1 29  ? 26.892  -9.991  -51.639 1.00 41.53 ?  29  GLU   A CG   1 
ATOM   210  C CD   . GLU   A 1 29  ? 27.002  -8.849  -52.641 1.00 57.25 ?  29  GLU   A CD   1 
ATOM   211  O OE1  . GLU   A 1 29  ? 27.839  -7.947  -52.421 1.00 59.22 ?  29  GLU   A OE1  1 
ATOM   212  O OE2  . GLU   A 1 29  ? 26.262  -8.856  -53.653 1.00 59.05 -1 29  GLU   A OE2  1 
ATOM   213  N N    . SER   A 1 30  ? 27.814  -13.190 -50.239 1.00 25.07 ?  30  SER   A N    1 
ATOM   214  C CA   . SER   A 1 30  ? 28.941  -14.105 -50.144 1.00 27.02 ?  30  SER   A CA   1 
ATOM   215  C C    . SER   A 1 30  ? 28.728  -15.227 -49.150 1.00 30.64 ?  30  SER   A C    1 
ATOM   216  O O    . SER   A 1 30  ? 29.575  -16.123 -49.080 1.00 31.84 ?  30  SER   A O    1 
ATOM   217  C CB   . SER   A 1 30  ? 30.223  -13.360 -49.748 1.00 34.76 ?  30  SER   A CB   1 
ATOM   218  O OG   . SER   A 1 30  ? 30.264  -12.066 -50.316 1.00 48.31 ?  30  SER   A OG   1 
ATOM   219  N N    . ASN   A 1 31  ? 27.651  -15.205 -48.363 1.00 26.01 ?  31  ASN   A N    1 
ATOM   220  C CA   . ASN   A 1 31  ? 27.563  -16.160 -47.259 1.00 17.68 ?  31  ASN   A CA   1 
ATOM   221  C C    . ASN   A 1 31  ? 26.100  -16.477 -47.004 1.00 26.68 ?  31  ASN   A C    1 
ATOM   222  O O    . ASN   A 1 31  ? 25.384  -15.657 -46.429 1.00 23.97 ?  31  ASN   A O    1 
ATOM   223  C CB   . ASN   A 1 31  ? 28.235  -15.609 -46.003 1.00 21.25 ?  31  ASN   A CB   1 
ATOM   224  C CG   . ASN   A 1 31  ? 28.414  -16.653 -44.919 1.00 19.72 ?  31  ASN   A CG   1 
ATOM   225  O OD1  . ASN   A 1 31  ? 27.672  -17.628 -44.843 1.00 22.54 ?  31  ASN   A OD1  1 
ATOM   226  N ND2  . ASN   A 1 31  ? 29.418  -16.443 -44.053 1.00 23.50 ?  31  ASN   A ND2  1 
ATOM   227  N N    . ALA   A 1 32  ? 25.671  -17.666 -47.429 1.00 26.02 ?  32  ALA   A N    1 
ATOM   228  C CA   . ALA   A 1 32  ? 24.265  -18.037 -47.336 1.00 23.53 ?  32  ALA   A CA   1 
ATOM   229  C C    . ALA   A 1 32  ? 23.775  -18.198 -45.902 1.00 22.08 ?  32  ALA   A C    1 
ATOM   230  O O    . ALA   A 1 32  ? 22.560  -18.284 -45.691 1.00 27.22 ?  32  ALA   A O    1 
ATOM   231  C CB   . ALA   A 1 32  ? 24.019  -19.329 -48.115 1.00 32.88 ?  32  ALA   A CB   1 
ATOM   232  N N    . ARG   A 1 33  ? 24.671  -18.230 -44.916 1.00 22.09 ?  33  ARG   A N    1 
ATOM   233  C CA   . ARG   A 1 33  ? 24.286  -18.377 -43.522 1.00 20.73 ?  33  ARG   A CA   1 
ATOM   234  C C    . ARG   A 1 33  ? 24.189  -17.036 -42.807 1.00 17.33 ?  33  ARG   A C    1 
ATOM   235  O O    . ARG   A 1 33  ? 23.875  -17.000 -41.617 1.00 20.43 ?  33  ARG   A O    1 
ATOM   236  C CB   . ARG   A 1 33  ? 25.295  -19.291 -42.799 1.00 21.06 ?  33  ARG   A CB   1 
ATOM   237  C CG   . ARG   A 1 33  ? 25.131  -20.759 -43.174 1.00 23.53 ?  33  ARG   A CG   1 
ATOM   238  C CD   . ARG   A 1 33  ? 26.233  -21.641 -42.618 1.00 23.52 ?  33  ARG   A CD   1 
ATOM   239  N NE   . ARG   A 1 33  ? 25.951  -23.054 -42.861 1.00 29.81 ?  33  ARG   A NE   1 
ATOM   240  C CZ   . ARG   A 1 33  ? 25.181  -23.819 -42.095 1.00 28.80 ?  33  ARG   A CZ   1 
ATOM   241  N NH1  . ARG   A 1 33  ? 24.647  -23.367 -40.973 1.00 26.83 ?  33  ARG   A NH1  1 
ATOM   242  N NH2  . ARG   A 1 33  ? 24.941  -25.075 -42.464 1.00 35.18 ?  33  ARG   A NH2  1 
ATOM   243  N N    . TYR   A 1 34  ? 24.459  -15.943 -43.514 1.00 18.46 ?  34  TYR   A N    1 
ATOM   244  C CA   . TYR   A 1 34  ? 24.645  -14.618 -42.939 1.00 19.62 ?  34  TYR   A CA   1 
ATOM   245  C C    . TYR   A 1 34  ? 23.561  -13.699 -43.481 1.00 17.19 ?  34  TYR   A C    1 
ATOM   246  O O    . TYR   A 1 34  ? 23.378  -13.604 -44.698 1.00 21.14 ?  34  TYR   A O    1 
ATOM   247  C CB   . TYR   A 1 34  ? 26.047  -14.120 -43.316 1.00 14.93 ?  34  TYR   A CB   1 
ATOM   248  C CG   . TYR   A 1 34  ? 26.545  -12.807 -42.743 1.00 17.83 ?  34  TYR   A CG   1 
ATOM   249  C CD1  . TYR   A 1 34  ? 26.106  -12.313 -41.525 1.00 19.06 ?  34  TYR   A CD1  1 
ATOM   250  C CD2  . TYR   A 1 34  ? 27.501  -12.083 -43.435 1.00 19.01 ?  34  TYR   A CD2  1 
ATOM   251  C CE1  . TYR   A 1 34  ? 26.611  -11.099 -41.024 1.00 19.32 ?  34  TYR   A CE1  1 
ATOM   252  C CE2  . TYR   A 1 34  ? 28.013  -10.899 -42.950 1.00 23.33 ?  34  TYR   A CE2  1 
ATOM   253  C CZ   . TYR   A 1 34  ? 27.563  -10.400 -41.753 1.00 24.31 ?  34  TYR   A CZ   1 
ATOM   254  O OH   . TYR   A 1 34  ? 28.113  -9.210  -41.313 1.00 26.32 ?  34  TYR   A OH   1 
ATOM   255  N N    . PHE   A 1 35  ? 22.826  -13.046 -42.582 1.00 18.10 ?  35  PHE   A N    1 
ATOM   256  C CA   . PHE   A 1 35  ? 21.695  -12.214 -42.955 1.00 19.01 ?  35  PHE   A CA   1 
ATOM   257  C C    . PHE   A 1 35  ? 21.884  -10.807 -42.415 1.00 16.92 ?  35  PHE   A C    1 
ATOM   258  O O    . PHE   A 1 35  ? 22.331  -10.620 -41.277 1.00 19.12 ?  35  PHE   A O    1 
ATOM   259  C CB   . PHE   A 1 35  ? 20.384  -12.803 -42.431 1.00 15.30 ?  35  PHE   A CB   1 
ATOM   260  C CG   . PHE   A 1 35  ? 19.976  -14.085 -43.115 1.00 21.99 ?  35  PHE   A CG   1 
ATOM   261  C CD1  . PHE   A 1 35  ? 18.987  -14.076 -44.084 1.00 27.92 ?  35  PHE   A CD1  1 
ATOM   262  C CD2  . PHE   A 1 35  ? 20.573  -15.294 -42.782 1.00 17.12 ?  35  PHE   A CD2  1 
ATOM   263  C CE1  . PHE   A 1 35  ? 18.604  -15.252 -44.728 1.00 31.70 ?  35  PHE   A CE1  1 
ATOM   264  C CE2  . PHE   A 1 35  ? 20.198  -16.471 -43.421 1.00 23.69 ?  35  PHE   A CE2  1 
ATOM   265  C CZ   . PHE   A 1 35  ? 19.214  -16.446 -44.394 1.00 27.50 ?  35  PHE   A CZ   1 
ATOM   266  N N    . HIS   A 1 36  ? 21.547  -9.827  -43.255 1.00 17.03 ?  36  HIS   A N    1 
ATOM   267  C CA   . HIS   A 1 36  ? 21.514  -8.424  -42.874 1.00 16.49 ?  36  HIS   A CA   1 
ATOM   268  C C    . HIS   A 1 36  ? 20.069  -8.024  -42.657 1.00 18.29 ?  36  HIS   A C    1 
ATOM   269  O O    . HIS   A 1 36  ? 19.243  -8.181  -43.561 1.00 18.67 ?  36  HIS   A O    1 
ATOM   270  C CB   . HIS   A 1 36  ? 22.164  -7.565  -43.953 1.00 17.58 ?  36  HIS   A CB   1 
ATOM   271  C CG   . HIS   A 1 36  ? 23.583  -7.953  -44.202 1.00 22.43 ?  36  HIS   A CG   1 
ATOM   272  N ND1  . HIS   A 1 36  ? 24.628  -7.436  -43.467 1.00 20.99 ?  36  HIS   A ND1  1 
ATOM   273  C CD2  . HIS   A 1 36  ? 24.125  -8.872  -45.036 1.00 26.14 ?  36  HIS   A CD2  1 
ATOM   274  C CE1  . HIS   A 1 36  ? 25.761  -7.991  -43.866 1.00 25.94 ?  36  HIS   A CE1  1 
ATOM   275  N NE2  . HIS   A 1 36  ? 25.485  -8.868  -44.815 1.00 23.17 ?  36  HIS   A NE2  1 
ATOM   276  N N    . VAL   A 1 37  ? 19.770  -7.505  -41.470 1.00 15.84 ?  37  VAL   A N    1 
ATOM   277  C CA   . VAL   A 1 37  ? 18.402  -7.258  -41.031 1.00 15.48 ?  37  VAL   A CA   1 
ATOM   278  C C    . VAL   A 1 37  ? 18.260  -5.782  -40.697 1.00 16.11 ?  37  VAL   A C    1 
ATOM   279  O O    . VAL   A 1 37  ? 19.193  -5.174  -40.168 1.00 15.51 ?  37  VAL   A O    1 
ATOM   280  C CB   . VAL   A 1 37  ? 18.064  -8.130  -39.799 1.00 16.51 ?  37  VAL   A CB   1 
ATOM   281  C CG1  . VAL   A 1 37  ? 16.675  -7.807  -39.285 1.00 15.25 ?  37  VAL   A CG1  1 
ATOM   282  C CG2  . VAL   A 1 37  ? 18.155  -9.607  -40.147 1.00 18.64 ?  37  VAL   A CG2  1 
ATOM   283  N N    . VAL   A 1 38  ? 17.106  -5.198  -41.020 1.00 13.93 ?  38  VAL   A N    1 
ATOM   284  C CA   . VAL   A 1 38  ? 16.769  -3.857  -40.556 1.00 15.71 ?  38  VAL   A CA   1 
ATOM   285  C C    . VAL   A 1 38  ? 15.389  -3.904  -39.921 1.00 13.22 ?  38  VAL   A C    1 
ATOM   286  O O    . VAL   A 1 38  ? 14.433  -4.356  -40.553 1.00 17.16 ?  38  VAL   A O    1 
ATOM   287  C CB   . VAL   A 1 38  ? 16.803  -2.816  -41.695 1.00 17.37 ?  38  VAL   A CB   1 
ATOM   288  C CG1  . VAL   A 1 38  ? 16.468  -1.441  -41.124 1.00 20.61 ?  38  VAL   A CG1  1 
ATOM   289  C CG2  . VAL   A 1 38  ? 18.191  -2.787  -42.351 1.00 20.30 ?  38  VAL   A CG2  1 
ATOM   290  N N    . ILE   A 1 39  ? 15.274  -3.420  -38.679 1.00 13.01 ?  39  ILE   A N    1 
ATOM   291  C CA   . ILE   A 1 39  ? 13.980  -3.340  -37.998 1.00 13.85 ?  39  ILE   A CA   1 
ATOM   292  C C    . ILE   A 1 39  ? 13.617  -1.873  -37.794 1.00 15.15 ?  39  ILE   A C    1 
ATOM   293  O O    . ILE   A 1 39  ? 14.421  -1.088  -37.272 1.00 17.06 ?  39  ILE   A O    1 
ATOM   294  C CB   . ILE   A 1 39  ? 13.982  -4.115  -36.672 1.00 14.18 ?  39  ILE   A CB   1 
ATOM   295  C CG1  . ILE   A 1 39  ? 14.270  -5.594  -36.949 1.00 16.16 ?  39  ILE   A CG1  1 
ATOM   296  C CG2  . ILE   A 1 39  ? 12.621  -3.960  -35.953 1.00 16.34 ?  39  ILE   A CG2  1 
ATOM   297  C CD1  . ILE   A 1 39  ? 14.537  -6.458  -35.690 1.00 19.42 ?  39  ILE   A CD1  1 
ATOM   298  N N    . ALA   A 1 40  ? 12.414  -1.497  -38.233 1.00 15.87 ?  40  ALA   A N    1 
ATOM   299  C CA   . ALA   A 1 40  ? 11.936  -0.146  -37.993 1.00 19.48 ?  40  ALA   A CA   1 
ATOM   300  C C    . ALA   A 1 40  ? 11.511  -0.013  -36.541 1.00 16.77 ?  40  ALA   A C    1 
ATOM   301  O O    . ALA   A 1 40  ? 10.912  -0.927  -35.973 1.00 16.39 ?  40  ALA   A O    1 
ATOM   302  C CB   . ALA   A 1 40  ? 10.755  0.181   -38.911 1.00 20.47 ?  40  ALA   A CB   1 
ATOM   303  N N    . GLY   A 1 41  ? 11.825  1.132   -35.935 1.00 16.01 ?  41  GLY   A N    1 
ATOM   304  C CA   . GLY   A 1 41  ? 11.393  1.402   -34.586 1.00 15.40 ?  41  GLY   A CA   1 
ATOM   305  C C    . GLY   A 1 41  ? 9.880   1.366   -34.520 1.00 15.91 ?  41  GLY   A C    1 
ATOM   306  O O    . GLY   A 1 41  ? 9.199   2.036   -35.301 1.00 20.38 ?  41  GLY   A O    1 
ATOM   307  N N    . PRO   A 1 42  ? 9.321   0.564   -33.615 1.00 16.38 ?  42  PRO   A N    1 
ATOM   308  C CA   . PRO   A 1 42  ? 7.855   0.451   -33.566 1.00 18.88 ?  42  PRO   A CA   1 
ATOM   309  C C    . PRO   A 1 42  ? 7.167   1.767   -33.211 1.00 22.25 ?  42  PRO   A C    1 
ATOM   310  O O    . PRO   A 1 42  ? 7.647   2.554   -32.394 1.00 18.89 ?  42  PRO   A O    1 
ATOM   311  C CB   . PRO   A 1 42  ? 7.617   -0.620  -32.498 1.00 19.43 ?  42  PRO   A CB   1 
ATOM   312  C CG   . PRO   A 1 42  ? 8.858   -1.486  -32.590 1.00 19.88 ?  42  PRO   A CG   1 
ATOM   313  C CD   . PRO   A 1 42  ? 9.976   -0.501  -32.833 1.00 16.34 ?  42  PRO   A CD   1 
ATOM   314  N N    . GLN   A 1 43  ? 6.016   1.993   -33.845 1.00 22.88 ?  43  GLN   A N    1 
ATOM   315  C CA   . GLN   A 1 43  ? 5.163   3.123   -33.496 1.00 21.85 ?  43  GLN   A CA   1 
ATOM   316  C C    . GLN   A 1 43  ? 4.852   3.136   -32.006 1.00 22.25 ?  43  GLN   A C    1 
ATOM   317  O O    . GLN   A 1 43  ? 4.590   2.093   -31.402 1.00 23.38 ?  43  GLN   A O    1 
ATOM   318  C CB   . GLN   A 1 43  ? 3.853   3.040   -34.280 1.00 29.02 ?  43  GLN   A CB   1 
ATOM   319  C CG   . GLN   A 1 43  ? 3.036   4.325   -34.276 1.00 33.73 ?  43  GLN   A CG   1 
ATOM   320  C CD   . GLN   A 1 43  ? 1.821   4.228   -35.184 1.00 44.00 ?  43  GLN   A CD   1 
ATOM   321  O OE1  . GLN   A 1 43  ? 0.756   4.769   -34.877 1.00 48.45 ?  43  GLN   A OE1  1 
ATOM   322  N NE2  . GLN   A 1 43  ? 1.970   3.520   -36.300 1.00 48.93 ?  43  GLN   A NE2  1 
ATOM   323  N N    . ASP   A 1 44  ? 4.871   4.330   -31.409 1.00 24.25 ?  44  ASP   A N    1 
ATOM   324  C CA   . ASP   A 1 44  ? 4.553   4.568   -30.000 1.00 22.19 ?  44  ASP   A CA   1 
ATOM   325  C C    . ASP   A 1 44  ? 5.622   4.068   -29.033 1.00 28.64 ?  44  ASP   A C    1 
ATOM   326  O O    . ASP   A 1 44  ? 5.444   4.203   -27.815 1.00 29.77 ?  44  ASP   A O    1 
ATOM   327  C CB   . ASP   A 1 44  ? 3.198   3.959   -29.597 1.00 28.69 ?  44  ASP   A CB   1 
ATOM   328  C CG   . ASP   A 1 44  ? 2.018   4.661   -30.250 1.00 33.04 ?  44  ASP   A CG   1 
ATOM   329  O OD1  . ASP   A 1 44  ? 2.195   5.758   -30.824 1.00 31.45 ?  44  ASP   A OD1  1 
ATOM   330  O OD2  . ASP   A 1 44  ? 0.899   4.106   -30.190 1.00 41.16 -1 44  ASP   A OD2  1 
ATOM   331  N N    . SER   A 1 45  ? 6.721   3.503   -29.516 1.00 22.17 ?  45  SER   A N    1 
ATOM   332  C CA   . SER   A 1 45  ? 7.809   3.087   -28.643 1.00 19.97 ?  45  SER   A CA   1 
ATOM   333  C C    . SER   A 1 45  ? 8.862   4.172   -28.574 1.00 17.76 ?  45  SER   A C    1 
ATOM   334  O O    . SER   A 1 45  ? 8.864   5.114   -29.368 1.00 17.96 ?  45  SER   A O    1 
ATOM   335  C CB   . SER   A 1 45  ? 8.426   1.786   -29.152 1.00 20.71 ?  45  SER   A CB   1 
ATOM   336  O OG   . SER   A 1 45  ? 9.301   2.053   -30.236 1.00 18.03 ?  45  SER   A OG   1 
ATOM   337  N N    . PRO   A 1 46  ? 9.798   4.056   -27.630 1.00 19.32 ?  46  PRO   A N    1 
ATOM   338  C CA   . PRO   A 1 46  ? 10.896  5.026   -27.571 1.00 21.95 ?  46  PRO   A CA   1 
ATOM   339  C C    . PRO   A 1 46  ? 11.736  5.039   -28.829 1.00 19.88 ?  46  PRO   A C    1 
ATOM   340  O O    . PRO   A 1 46  ? 12.473  6.005   -29.063 1.00 22.10 ?  46  PRO   A O    1 
ATOM   341  C CB   . PRO   A 1 46  ? 11.715  4.571   -26.347 1.00 17.44 ?  46  PRO   A CB   1 
ATOM   342  C CG   . PRO   A 1 46  ? 10.813  3.661   -25.577 1.00 22.20 ?  46  PRO   A CG   1 
ATOM   343  C CD   . PRO   A 1 46  ? 9.844   3.062   -26.543 1.00 18.19 ?  46  PRO   A CD   1 
ATOM   344  N N    . PHE   A 1 47  ? 11.637  4.004   -29.659 1.00 17.28 ?  47  PHE   A N    1 
ATOM   345  C CA   . PHE   A 1 47  ? 12.481  3.856   -30.834 1.00 16.76 ?  47  PHE   A CA   1 
ATOM   346  C C    . PHE   A 1 47  ? 11.777  4.286   -32.112 1.00 17.10 ?  47  PHE   A C    1 
ATOM   347  O O    . PHE   A 1 47  ? 12.335  4.136   -33.193 1.00 19.33 ?  47  PHE   A O    1 
ATOM   348  C CB   . PHE   A 1 47  ? 12.956  2.408   -30.928 1.00 14.88 ?  47  PHE   A CB   1 
ATOM   349  C CG   . PHE   A 1 47  ? 13.447  1.877   -29.608 1.00 15.70 ?  47  PHE   A CG   1 
ATOM   350  C CD1  . PHE   A 1 47  ? 14.708  2.225   -29.151 1.00 15.71 ?  47  PHE   A CD1  1 
ATOM   351  C CD2  . PHE   A 1 47  ? 12.625  1.110   -28.787 1.00 16.13 ?  47  PHE   A CD2  1 
ATOM   352  C CE1  . PHE   A 1 47  ? 15.170  1.793   -27.900 1.00 16.81 ?  47  PHE   A CE1  1 
ATOM   353  C CE2  . PHE   A 1 47  ? 13.082  0.653   -27.558 1.00 15.03 ?  47  PHE   A CE2  1 
ATOM   354  C CZ   . PHE   A 1 47  ? 14.343  1.005   -27.102 1.00 16.04 ?  47  PHE   A CZ   1 
ATOM   355  N N    . GLU   A 1 48  ? 10.580  4.851   -31.994 1.00 18.18 ?  48  GLU   A N    1 
ATOM   356  C CA   . GLU   A 1 48  ? 9.843   5.319   -33.155 1.00 15.84 ?  48  GLU   A CA   1 
ATOM   357  C C    . GLU   A 1 48  ? 10.684  6.258   -34.008 1.00 21.08 ?  48  GLU   A C    1 
ATOM   358  O O    . GLU   A 1 48  ? 11.380  7.143   -33.497 1.00 22.58 ?  48  GLU   A O    1 
ATOM   359  C CB   . GLU   A 1 48  ? 8.569   6.025   -32.717 1.00 19.12 ?  48  GLU   A CB   1 
ATOM   360  C CG   . GLU   A 1 48  ? 7.667   6.412   -33.873 1.00 20.78 ?  48  GLU   A CG   1 
ATOM   361  C CD   . GLU   A 1 48  ? 6.492   7.249   -33.394 1.00 32.35 ?  48  GLU   A CD   1 
ATOM   362  O OE1  . GLU   A 1 48  ? 5.716   6.732   -32.570 1.00 24.65 ?  48  GLU   A OE1  1 
ATOM   363  O OE2  . GLU   A 1 48  ? 6.333   8.406   -33.844 1.00 39.28 -1 48  GLU   A OE2  1 
ATOM   364  N N    . GLY   A 1 49  ? 10.578  6.081   -35.324 1.00 17.64 ?  49  GLY   A N    1 
ATOM   365  C CA   . GLY   A 1 49  ? 11.293  6.897   -36.270 1.00 27.10 ?  49  GLY   A CA   1 
ATOM   366  C C    . GLY   A 1 49  ? 12.680  6.404   -36.608 1.00 30.02 ?  49  GLY   A C    1 
ATOM   367  O O    . GLY   A 1 49  ? 13.269  6.887   -37.585 1.00 29.68 ?  49  GLY   A O    1 
ATOM   368  N N    . GLY   A 1 50  ? 13.226  5.459   -35.827 1.00 17.05 ?  50  GLY   A N    1 
ATOM   369  C CA   . GLY   A 1 50  ? 14.550  4.944   -36.087 1.00 17.56 ?  50  GLY   A CA   1 
ATOM   370  C C    . GLY   A 1 50  ? 14.558  3.711   -36.990 1.00 17.54 ?  50  GLY   A C    1 
ATOM   371  O O    . GLY   A 1 50  ? 13.552  3.037   -37.173 1.00 19.52 ?  50  GLY   A O    1 
ATOM   372  N N    . THR   A 1 51  ? 15.730  3.432   -37.566 1.00 15.14 ?  51  THR   A N    1 
ATOM   373  C CA   . THR   A 1 51  ? 15.954  2.218   -38.342 1.00 15.93 ?  51  THR   A CA   1 
ATOM   374  C C    . THR   A 1 51  ? 17.156  1.523   -37.725 1.00 15.76 ?  51  THR   A C    1 
ATOM   375  O O    . THR   A 1 51  ? 18.216  2.140   -37.591 1.00 20.48 ?  51  THR   A O    1 
ATOM   376  C CB   . THR   A 1 51  ? 16.226  2.539   -39.826 1.00 20.44 ?  51  THR   A CB   1 
ATOM   377  O OG1  . THR   A 1 51  ? 17.260  3.519   -39.908 1.00 29.49 ?  51  THR   A OG1  1 
ATOM   378  C CG2  . THR   A 1 51  ? 14.980  3.109   -40.477 1.00 30.28 ?  51  THR   A CG2  1 
ATOM   379  N N    . PHE   A 1 52  ? 17.006  0.255   -37.348 1.00 14.86 ?  52  PHE   A N    1 
ATOM   380  C CA   . PHE   A 1 52  ? 18.036  -0.444  -36.585 1.00 13.83 ?  52  PHE   A CA   1 
ATOM   381  C C    . PHE   A 1 52  ? 18.592  -1.607  -37.389 1.00 15.47 ?  52  PHE   A C    1 
ATOM   382  O O    . PHE   A 1 52  ? 17.842  -2.487  -37.830 1.00 14.58 ?  52  PHE   A O    1 
ATOM   383  C CB   . PHE   A 1 52  ? 17.462  -0.917  -35.232 1.00 14.36 ?  52  PHE   A CB   1 
ATOM   384  C CG   . PHE   A 1 52  ? 16.989  0.231   -34.365 1.00 12.91 ?  52  PHE   A CG   1 
ATOM   385  C CD1  . PHE   A 1 52  ? 15.707  0.735   -34.513 1.00 14.12 ?  52  PHE   A CD1  1 
ATOM   386  C CD2  . PHE   A 1 52  ? 17.852  0.860   -33.482 1.00 16.91 ?  52  PHE   A CD2  1 
ATOM   387  C CE1  . PHE   A 1 52  ? 15.272  1.817   -33.769 1.00 15.62 ?  52  PHE   A CE1  1 
ATOM   388  C CE2  . PHE   A 1 52  ? 17.423  1.939   -32.724 1.00 16.05 ?  52  PHE   A CE2  1 
ATOM   389  C CZ   . PHE   A 1 52  ? 16.124  2.418   -32.867 1.00 14.82 ?  52  PHE   A CZ   1 
ATOM   390  N N    . LYS   A 1 53  ? 19.913  -1.614  -37.557 1.00 15.61 ?  53  LYS   A N    1 
ATOM   391  C CA   . LYS   A 1 53  ? 20.613  -2.672  -38.264 1.00 13.16 ?  53  LYS   A CA   1 
ATOM   392  C C    . LYS   A 1 53  ? 20.974  -3.793  -37.301 1.00 14.35 ?  53  LYS   A C    1 
ATOM   393  O O    . LYS   A 1 53  ? 21.451  -3.537  -36.192 1.00 16.12 ?  53  LYS   A O    1 
ATOM   394  C CB   . LYS   A 1 53  ? 21.897  -2.137  -38.902 1.00 15.38 ?  53  LYS   A CB   1 
ATOM   395  C CG   . LYS   A 1 53  ? 21.676  -1.245  -40.103 1.00 21.16 ?  53  LYS   A CG   1 
ATOM   396  C CD   . LYS   A 1 53  ? 23.011  -0.626  -40.479 1.00 35.20 ?  53  LYS   A CD   1 
ATOM   397  C CE   . LYS   A 1 53  ? 23.614  -1.284  -41.697 1.00 44.13 ?  53  LYS   A CE   1 
ATOM   398  N NZ   . LYS   A 1 53  ? 24.868  -0.578  -42.108 1.00 42.12 ?  53  LYS   A NZ   1 
ATOM   399  N N    . LEU   A 1 54  ? 20.738  -5.031  -37.738 1.00 13.44 ?  54  LEU   A N    1 
ATOM   400  C CA   . LEU   A 1 54  ? 21.143  -6.227  -37.017 1.00 14.78 ?  54  LEU   A CA   1 
ATOM   401  C C    . LEU   A 1 54  ? 21.803  -7.183  -37.997 1.00 17.08 ?  54  LEU   A C    1 
ATOM   402  O O    . LEU   A 1 54  ? 21.574  -7.119  -39.208 1.00 17.52 ?  54  LEU   A O    1 
ATOM   403  C CB   . LEU   A 1 54  ? 19.944  -6.939  -36.370 1.00 16.29 ?  54  LEU   A CB   1 
ATOM   404  C CG   . LEU   A 1 54  ? 19.166  -6.194  -35.296 1.00 15.33 ?  54  LEU   A CG   1 
ATOM   405  C CD1  . LEU   A 1 54  ? 18.076  -5.323  -35.918 1.00 20.28 ?  54  LEU   A CD1  1 
ATOM   406  C CD2  . LEU   A 1 54  ? 18.540  -7.248  -34.339 1.00 15.03 ?  54  LEU   A CD2  1 
ATOM   407  N N    . GLU   A 1 55  ? 22.600  -8.092  -37.455 1.00 15.19 ?  55  GLU   A N    1 
ATOM   408  C CA   . GLU   A 1 55  ? 23.155  -9.191  -38.228 1.00 12.54 ?  55  GLU   A CA   1 
ATOM   409  C C    . GLU   A 1 55  ? 22.754  -10.513 -37.600 1.00 13.78 ?  55  GLU   A C    1 
ATOM   410  O O    . GLU   A 1 55  ? 22.623  -10.626 -36.381 1.00 14.59 ?  55  GLU   A O    1 
ATOM   411  C CB   . GLU   A 1 55  ? 24.693  -9.077  -38.324 1.00 17.51 ?  55  GLU   A CB   1 
ATOM   412  C CG   . GLU   A 1 55  ? 25.083  -7.799  -39.033 1.00 23.04 ?  55  GLU   A CG   1 
ATOM   413  C CD   . GLU   A 1 55  ? 26.578  -7.609  -39.197 1.00 26.35 ?  55  GLU   A CD   1 
ATOM   414  O OE1  . GLU   A 1 55  ? 27.362  -8.492  -38.776 1.00 23.09 ?  55  GLU   A OE1  1 
ATOM   415  O OE2  . GLU   A 1 55  ? 26.959  -6.560  -39.762 1.00 34.20 -1 55  GLU   A OE2  1 
ATOM   416  N N    . LEU   A 1 56  ? 22.543  -11.516 -38.447 1.00 15.99 ?  56  LEU   A N    1 
ATOM   417  C CA   . LEU   A 1 56  ? 22.123  -12.828 -37.985 1.00 15.95 ?  56  LEU   A CA   1 
ATOM   418  C C    . LEU   A 1 56  ? 22.971  -13.881 -38.682 1.00 19.43 ?  56  LEU   A C    1 
ATOM   419  O O    . LEU   A 1 56  ? 23.321  -13.724 -39.852 1.00 19.24 ?  56  LEU   A O    1 
ATOM   420  C CB   . LEU   A 1 56  ? 20.612  -13.043 -38.265 1.00 16.60 ?  56  LEU   A CB   1 
ATOM   421  C CG   . LEU   A 1 56  ? 19.967  -14.361 -37.816 1.00 18.95 ?  56  LEU   A CG   1 
ATOM   422  C CD1  . LEU   A 1 56  ? 18.474  -14.168 -37.401 1.00 17.81 ?  56  LEU   A CD1  1 
ATOM   423  C CD2  . LEU   A 1 56  ? 20.077  -15.375 -38.933 1.00 19.51 ?  56  LEU   A CD2  1 
ATOM   424  N N    . PHE   A 1 57  ? 23.328  -14.934 -37.951 1.00 16.91 ?  57  PHE   A N    1 
ATOM   425  C CA   . PHE   A 1 57  ? 24.205  -15.971 -38.483 1.00 17.91 ?  57  PHE   A CA   1 
ATOM   426  C C    . PHE   A 1 57  ? 23.671  -17.334 -38.076 1.00 13.81 ?  57  PHE   A C    1 
ATOM   427  O O    . PHE   A 1 57  ? 23.300  -17.534 -36.916 1.00 18.00 ?  57  PHE   A O    1 
ATOM   428  C CB   . PHE   A 1 57  ? 25.640  -15.794 -37.982 1.00 18.39 ?  57  PHE   A CB   1 
ATOM   429  C CG   . PHE   A 1 57  ? 26.556  -16.848 -38.483 1.00 18.91 ?  57  PHE   A CG   1 
ATOM   430  C CD1  . PHE   A 1 57  ? 26.810  -16.949 -39.837 1.00 21.12 ?  57  PHE   A CD1  1 
ATOM   431  C CD2  . PHE   A 1 57  ? 27.127  -17.758 -37.609 1.00 21.37 ?  57  PHE   A CD2  1 
ATOM   432  C CE1  . PHE   A 1 57  ? 27.654  -17.938 -40.334 1.00 24.82 ?  57  PHE   A CE1  1 
ATOM   433  C CE2  . PHE   A 1 57  ? 27.973  -18.750 -38.101 1.00 25.77 ?  57  PHE   A CE2  1 
ATOM   434  C CZ   . PHE   A 1 57  ? 28.213  -18.836 -39.468 1.00 19.54 ?  57  PHE   A CZ   1 
ATOM   435  N N    . LEU   A 1 58  ? 23.600  -18.262 -39.049 1.00 17.95 ?  58  LEU   A N    1 
ATOM   436  C CA   . LEU   A 1 58  ? 23.141  -19.616 -38.796 1.00 22.52 ?  58  LEU   A CA   1 
ATOM   437  C C    . LEU   A 1 58  ? 24.350  -20.515 -38.589 1.00 21.43 ?  58  LEU   A C    1 
ATOM   438  O O    . LEU   A 1 58  ? 25.045  -20.828 -39.566 1.00 22.47 ?  58  LEU   A O    1 
ATOM   439  C CB   . LEU   A 1 58  ? 22.292  -20.122 -39.960 1.00 18.39 ?  58  LEU   A CB   1 
ATOM   440  C CG   . LEU   A 1 58  ? 21.128  -19.181 -40.300 1.00 16.71 ?  58  LEU   A CG   1 
ATOM   441  C CD1  . LEU   A 1 58  ? 20.421  -19.639 -41.578 1.00 17.33 ?  58  LEU   A CD1  1 
ATOM   442  C CD2  . LEU   A 1 58  ? 20.136  -19.085 -39.139 1.00 23.95 ?  58  LEU   A CD2  1 
ATOM   443  N N    . PRO   A 1 59  ? 24.634  -20.949 -37.363 1.00 20.53 ?  59  PRO   A N    1 
ATOM   444  C CA   . PRO   A 1 59  ? 25.849  -21.730 -37.109 1.00 27.92 ?  59  PRO   A CA   1 
ATOM   445  C C    . PRO   A 1 59  ? 25.732  -23.146 -37.650 1.00 29.47 ?  59  PRO   A C    1 
ATOM   446  O O    . PRO   A 1 59  ? 24.676  -23.595 -38.102 1.00 25.93 ?  59  PRO   A O    1 
ATOM   447  C CB   . PRO   A 1 59  ? 25.972  -21.727 -35.583 1.00 28.33 ?  59  PRO   A CB   1 
ATOM   448  C CG   . PRO   A 1 59  ? 24.614  -21.396 -35.067 1.00 26.44 ?  59  PRO   A CG   1 
ATOM   449  C CD   . PRO   A 1 59  ? 23.783  -20.816 -36.167 1.00 22.89 ?  59  PRO   A CD   1 
ATOM   450  N N    . GLU   A 1 60  ? 26.864  -23.855 -37.580 1.00 28.29 ?  60  GLU   A N    1 
ATOM   451  C CA   . GLU   A 1 60  ? 26.973  -25.189 -38.166 1.00 35.38 ?  60  GLU   A CA   1 
ATOM   452  C C    . GLU   A 1 60  ? 25.785  -26.077 -37.821 1.00 29.10 ?  60  GLU   A C    1 
ATOM   453  O O    . GLU   A 1 60  ? 25.232  -26.756 -38.693 1.00 32.39 ?  60  GLU   A O    1 
ATOM   454  C CB   . GLU   A 1 60  ? 28.264  -25.858 -37.698 1.00 37.52 ?  60  GLU   A CB   1 
ATOM   455  C CG   . GLU   A 1 60  ? 28.815  -26.873 -38.679 1.00 45.49 ?  60  GLU   A CG   1 
ATOM   456  C CD   . GLU   A 1 60  ? 30.326  -26.861 -38.715 1.00 52.77 ?  60  GLU   A CD   1 
ATOM   457  O OE1  . GLU   A 1 60  ? 30.937  -26.929 -37.627 1.00 52.34 ?  60  GLU   A OE1  1 
ATOM   458  O OE2  . GLU   A 1 60  ? 30.900  -26.764 -39.820 1.00 56.15 -1 60  GLU   A OE2  1 
ATOM   459  N N    . GLU   A 1 61  ? 25.403  -26.116 -36.548 1.00 33.36 ?  61  GLU   A N    1 
ATOM   460  C CA   . GLU   A 1 61  ? 24.395  -27.052 -36.071 1.00 32.52 ?  61  GLU   A CA   1 
ATOM   461  C C    . GLU   A 1 61  ? 22.967  -26.530 -36.174 1.00 35.51 ?  61  GLU   A C    1 
ATOM   462  O O    . GLU   A 1 61  ? 22.055  -27.176 -35.647 1.00 28.32 ?  61  GLU   A O    1 
ATOM   463  C CB   . GLU   A 1 61  ? 24.681  -27.450 -34.620 1.00 37.48 ?  61  GLU   A CB   1 
ATOM   464  C CG   . GLU   A 1 61  ? 25.536  -28.703 -34.483 1.00 53.91 ?  61  GLU   A CG   1 
ATOM   465  C CD   . GLU   A 1 61  ? 24.693  -29.965 -34.314 1.00 66.42 ?  61  GLU   A CD   1 
ATOM   466  O OE1  . GLU   A 1 61  ? 24.307  -30.280 -33.165 1.00 62.88 ?  61  GLU   A OE1  1 
ATOM   467  O OE2  . GLU   A 1 61  ? 24.412  -30.638 -35.333 1.00 63.42 -1 61  GLU   A OE2  1 
ATOM   468  N N    . TYR   A 1 62  ? 22.745  -25.392 -36.825 1.00 28.16 ?  62  TYR   A N    1 
ATOM   469  C CA   . TYR   A 1 62  ? 21.379  -24.955 -37.064 1.00 26.52 ?  62  TYR   A CA   1 
ATOM   470  C C    . TYR   A 1 62  ? 20.646  -26.025 -37.880 1.00 28.73 ?  62  TYR   A C    1 
ATOM   471  O O    . TYR   A 1 62  ? 21.221  -26.573 -38.830 1.00 29.05 ?  62  TYR   A O    1 
ATOM   472  C CB   . TYR   A 1 62  ? 21.363  -23.610 -37.805 1.00 24.49 ?  62  TYR   A CB   1 
ATOM   473  C CG   . TYR   A 1 62  ? 19.972  -23.030 -37.963 1.00 24.91 ?  62  TYR   A CG   1 
ATOM   474  C CD1  . TYR   A 1 62  ? 19.383  -22.320 -36.926 1.00 23.81 ?  62  TYR   A CD1  1 
ATOM   475  C CD2  . TYR   A 1 62  ? 19.246  -23.205 -39.137 1.00 21.24 ?  62  TYR   A CD2  1 
ATOM   476  C CE1  . TYR   A 1 62  ? 18.109  -21.802 -37.048 1.00 26.01 ?  62  TYR   A CE1  1 
ATOM   477  C CE2  . TYR   A 1 62  ? 17.962  -22.683 -39.270 1.00 21.33 ?  62  TYR   A CE2  1 
ATOM   478  C CZ   . TYR   A 1 62  ? 17.405  -21.977 -38.214 1.00 22.34 ?  62  TYR   A CZ   1 
ATOM   479  O OH   . TYR   A 1 62  ? 16.124  -21.458 -38.311 1.00 21.16 ?  62  TYR   A OH   1 
ATOM   480  N N    . PRO   A 1 63  ? 19.369  -26.348 -37.549 1.00 29.00 ?  63  PRO   A N    1 
ATOM   481  C CA   . PRO   A 1 63  ? 18.515  -25.758 -36.506 1.00 26.09 ?  63  PRO   A CA   1 
ATOM   482  C C    . PRO   A 1 63  ? 18.571  -26.409 -35.120 1.00 30.69 ?  63  PRO   A C    1 
ATOM   483  O O    . PRO   A 1 63  ? 17.740  -26.080 -34.279 1.00 29.47 ?  63  PRO   A O    1 
ATOM   484  C CB   . PRO   A 1 63  ? 17.111  -25.919 -37.108 1.00 28.33 ?  63  PRO   A CB   1 
ATOM   485  C CG   . PRO   A 1 63  ? 17.203  -27.248 -37.796 1.00 27.96 ?  63  PRO   A CG   1 
ATOM   486  C CD   . PRO   A 1 63  ? 18.575  -27.227 -38.439 1.00 25.68 ?  63  PRO   A CD   1 
ATOM   487  N N    . MET   A 1 64  ? 19.493  -27.331 -34.822 1.00 25.12 ?  64  MET   A N    1 
ATOM   488  C CA   . MET   A 1 64  ? 19.588  -27.825 -33.451 1.00 26.95 ?  64  MET   A CA   1 
ATOM   489  C C    . MET   A 1 64  ? 20.111  -26.747 -32.509 1.00 28.71 ?  64  MET   A C    1 
ATOM   490  O O    . MET   A 1 64  ? 19.672  -26.659 -31.360 1.00 33.00 ?  64  MET   A O    1 
ATOM   491  C CB   . MET   A 1 64  ? 20.479  -29.067 -33.390 1.00 41.13 ?  64  MET   A CB   1 
ATOM   492  C CG   . MET   A 1 64  ? 19.869  -30.317 -34.013 1.00 45.74 ?  64  MET   A CG   1 
ATOM   493  S SD   . MET   A 1 64  ? 18.182  -30.626 -33.452 1.00 54.81 ?  64  MET   A SD   1 
ATOM   494  C CE   . MET   A 1 64  ? 18.446  -30.993 -31.721 1.00 34.59 ?  64  MET   A CE   1 
ATOM   495  N N    . ALA   A 1 65  ? 21.045  -25.925 -32.975 1.00 31.83 ?  65  ALA   A N    1 
ATOM   496  C CA   . ALA   A 1 65  ? 21.522  -24.767 -32.234 1.00 29.75 ?  65  ALA   A CA   1 
ATOM   497  C C    . ALA   A 1 65  ? 20.808  -23.508 -32.720 1.00 29.79 ?  65  ALA   A C    1 
ATOM   498  O O    . ALA   A 1 65  ? 20.392  -23.420 -33.878 1.00 27.78 ?  65  ALA   A O    1 
ATOM   499  C CB   . ALA   A 1 65  ? 23.033  -24.603 -32.397 1.00 31.27 ?  65  ALA   A CB   1 
ATOM   500  N N    . ALA   A 1 66  ? 20.682  -22.524 -31.831 1.00 23.12 ?  66  ALA   A N    1 
ATOM   501  C CA   . ALA   A 1 66  ? 19.942  -21.313 -32.164 1.00 21.24 ?  66  ALA   A CA   1 
ATOM   502  C C    . ALA   A 1 66  ? 20.702  -20.436 -33.168 1.00 20.79 ?  66  ALA   A C    1 
ATOM   503  O O    . ALA   A 1 66  ? 21.931  -20.475 -33.246 1.00 23.02 ?  66  ALA   A O    1 
ATOM   504  C CB   . ALA   A 1 66  ? 19.671  -20.499 -30.902 1.00 20.84 ?  66  ALA   A CB   1 
ATOM   505  N N    . PRO   A 1 67  ? 19.995  -19.597 -33.923 1.00 18.10 ?  67  PRO   A N    1 
ATOM   506  C CA   . PRO   A 1 67  ? 20.693  -18.545 -34.672 1.00 18.32 ?  67  PRO   A CA   1 
ATOM   507  C C    . PRO   A 1 67  ? 21.392  -17.595 -33.702 1.00 15.72 ?  67  PRO   A C    1 
ATOM   508  O O    . PRO   A 1 67  ? 20.975  -17.427 -32.554 1.00 19.46 ?  67  PRO   A O    1 
ATOM   509  C CB   . PRO   A 1 67  ? 19.574  -17.845 -35.463 1.00 20.99 ?  67  PRO   A CB   1 
ATOM   510  C CG   . PRO   A 1 67  ? 18.286  -18.568 -35.126 1.00 19.75 ?  67  PRO   A CG   1 
ATOM   511  C CD   . PRO   A 1 67  ? 18.528  -19.446 -33.945 1.00 19.29 ?  67  PRO   A CD   1 
ATOM   512  N N    . LYS   A 1 68  ? 22.491  -16.997 -34.157 1.00 17.57 ?  68  LYS   A N    1 
ATOM   513  C CA   . LYS   A 1 68  ? 23.150  -15.939 -33.405 1.00 19.36 ?  68  LYS   A CA   1 
ATOM   514  C C    . LYS   A 1 68  ? 22.771  -14.594 -33.999 1.00 15.13 ?  68  LYS   A C    1 
ATOM   515  O O    . LYS   A 1 68  ? 22.689  -14.454 -35.221 1.00 17.56 ?  68  LYS   A O    1 
ATOM   516  C CB   . LYS   A 1 68  ? 24.674  -16.103 -33.404 1.00 20.45 ?  68  LYS   A CB   1 
ATOM   517  C CG   . LYS   A 1 68  ? 25.106  -17.482 -32.992 1.00 23.83 ?  68  LYS   A CG   1 
ATOM   518  C CD   . LYS   A 1 68  ? 26.585  -17.692 -33.099 1.00 30.29 ?  68  LYS   A CD   1 
ATOM   519  C CE   . LYS   A 1 68  ? 26.973  -18.776 -32.109 1.00 36.28 ?  68  LYS   A CE   1 
ATOM   520  N NZ   . LYS   A 1 68  ? 27.005  -18.226 -30.714 1.00 37.55 ?  68  LYS   A NZ   1 
ATOM   521  N N    . VAL   A 1 69  ? 22.499  -13.613 -33.134 1.00 16.28 ?  69  VAL   A N    1 
ATOM   522  C CA   . VAL   A 1 69  ? 21.993  -12.324 -33.598 1.00 17.90 ?  69  VAL   A CA   1 
ATOM   523  C C    . VAL   A 1 69  ? 22.667  -11.215 -32.810 1.00 18.34 ?  69  VAL   A C    1 
ATOM   524  O O    . VAL   A 1 69  ? 22.817  -11.312 -31.590 1.00 24.08 ?  69  VAL   A O    1 
ATOM   525  C CB   . VAL   A 1 69  ? 20.458  -12.202 -33.456 1.00 19.03 ?  69  VAL   A CB   1 
ATOM   526  C CG1  . VAL   A 1 69  ? 19.950  -10.961 -34.207 1.00 19.50 ?  69  VAL   A CG1  1 
ATOM   527  C CG2  . VAL   A 1 69  ? 19.765  -13.462 -33.954 1.00 22.36 ?  69  VAL   A CG2  1 
ATOM   528  N N    . ARG   A 1 70  ? 23.034  -10.143 -33.510 1.00 16.68 ?  70  ARG   A N    1 
ATOM   529  C CA   . ARG   A 1 70  ? 23.733  -9.002  -32.924 1.00 20.43 ?  70  ARG   A CA   1 
ATOM   530  C C    . ARG   A 1 70  ? 23.096  -7.713  -33.427 1.00 16.58 ?  70  ARG   A C    1 
ATOM   531  O O    . ARG   A 1 70  ? 22.935  -7.536  -34.636 1.00 17.54 ?  70  ARG   A O    1 
ATOM   532  C CB   . ARG   A 1 70  ? 25.223  -9.018  -33.317 1.00 18.20 ?  70  ARG   A CB   1 
ATOM   533  C CG   . ARG   A 1 70  ? 26.155  -8.341  -32.342 1.00 31.06 ?  70  ARG   A CG   1 
ATOM   534  C CD   . ARG   A 1 70  ? 27.567  -8.294  -32.877 1.00 27.58 ?  70  ARG   A CD   1 
ATOM   535  N NE   . ARG   A 1 70  ? 28.300  -7.187  -32.276 1.00 35.67 ?  70  ARG   A NE   1 
ATOM   536  C CZ   . ARG   A 1 70  ? 29.560  -6.877  -32.553 1.00 33.84 ?  70  ARG   A CZ   1 
ATOM   537  N NH1  . ARG   A 1 70  ? 30.239  -7.514  -33.495 1.00 31.73 ?  70  ARG   A NH1  1 
ATOM   538  N NH2  . ARG   A 1 70  ? 30.153  -5.900  -31.866 1.00 27.28 ?  70  ARG   A NH2  1 
ATOM   539  N N    . PHE   A 1 71  ? 22.728  -6.813  -32.511 1.00 16.85 ?  71  PHE   A N    1 
ATOM   540  C CA   . PHE   A 1 71  ? 22.412  -5.448  -32.916 1.00 16.97 ?  71  PHE   A CA   1 
ATOM   541  C C    . PHE   A 1 71  ? 23.685  -4.768  -33.380 1.00 18.04 ?  71  PHE   A C    1 
ATOM   542  O O    . PHE   A 1 71  ? 24.708  -4.822  -32.689 1.00 22.33 ?  71  PHE   A O    1 
ATOM   543  C CB   . PHE   A 1 71  ? 21.835  -4.630  -31.760 1.00 20.44 ?  71  PHE   A CB   1 
ATOM   544  C CG   . PHE   A 1 71  ? 20.337  -4.534  -31.754 1.00 13.94 ?  71  PHE   A CG   1 
ATOM   545  C CD1  . PHE   A 1 71  ? 19.681  -3.527  -32.446 1.00 25.89 ?  71  PHE   A CD1  1 
ATOM   546  C CD2  . PHE   A 1 71  ? 19.590  -5.441  -31.030 1.00 22.73 ?  71  PHE   A CD2  1 
ATOM   547  C CE1  . PHE   A 1 71  ? 18.285  -3.443  -32.417 1.00 18.24 ?  71  PHE   A CE1  1 
ATOM   548  C CE2  . PHE   A 1 71  ? 18.219  -5.369  -31.003 1.00 23.38 ?  71  PHE   A CE2  1 
ATOM   549  C CZ   . PHE   A 1 71  ? 17.558  -4.377  -31.703 1.00 20.06 ?  71  PHE   A CZ   1 
ATOM   550  N N    . MET   A 1 72  ? 23.626  -4.108  -34.523 1.00 15.22 ?  72  MET   A N    1 
ATOM   551  C CA   . MET   A 1 72  ? 24.772  -3.330  -34.969 1.00 17.85 ?  72  MET   A CA   1 
ATOM   552  C C    . MET   A 1 72  ? 24.576  -1.847  -34.735 1.00 20.60 ?  72  MET   A C    1 
ATOM   553  O O    . MET   A 1 72  ? 25.544  -1.139  -34.444 1.00 22.52 ?  72  MET   A O    1 
ATOM   554  C CB   . MET   A 1 72  ? 25.063  -3.583  -36.445 1.00 23.05 ?  72  MET   A CB   1 
ATOM   555  C CG   . MET   A 1 72  ? 25.368  -5.043  -36.706 1.00 22.31 ?  72  MET   A CG   1 
ATOM   556  S SD   . MET   A 1 72  ? 26.791  -5.673  -35.761 1.00 33.95 ?  72  MET   A SD   1 
ATOM   557  C CE   . MET   A 1 72  ? 28.018  -4.394  -36.074 1.00 35.75 ?  72  MET   A CE   1 
ATOM   558  N N    . THR   A 1 73  ? 23.345  -1.365  -34.826 1.00 16.64 ?  73  THR   A N    1 
ATOM   559  C CA   . THR   A 1 73  ? 23.037  0.028   -34.511 1.00 17.48 ?  73  THR   A CA   1 
ATOM   560  C C    . THR   A 1 73  ? 23.009  0.261   -33.015 1.00 17.56 ?  73  THR   A C    1 
ATOM   561  O O    . THR   A 1 73  ? 22.424  -0.516  -32.258 1.00 17.63 ?  73  THR   A O    1 
ATOM   562  C CB   . THR   A 1 73  ? 21.666  0.436   -35.112 1.00 17.30 ?  73  THR   A CB   1 
ATOM   563  O OG1  . THR   A 1 73  ? 21.698  0.248   -36.530 1.00 18.33 ?  73  THR   A OG1  1 
ATOM   564  C CG2  . THR   A 1 73  ? 21.327  1.889   -34.797 1.00 19.74 ?  73  THR   A CG2  1 
HETATM 565  C C22  . A1EJS A 1 74  ? 26.691  1.000   -26.330 1.00 28.69 ?  74  A1EJS A C22  1 
HETATM 566  C C25  . A1EJS A 1 74  ? 26.283  -0.025  -28.662 1.00 26.92 ?  74  A1EJS A C25  1 
HETATM 567  C C30  . A1EJS A 1 74  ? 25.241  -0.879  -28.313 1.00 19.97 ?  74  A1EJS A C30  1 
HETATM 568  C C29  . A1EJS A 1 74  ? 24.604  -1.608  -29.307 1.00 22.68 ?  74  A1EJS A C29  1 
HETATM 569  C C28  . A1EJS A 1 74  ? 24.988  -1.480  -30.638 1.00 23.35 ?  74  A1EJS A C28  1 
HETATM 570  C C27  . A1EJS A 1 74  ? 26.028  -0.620  -30.974 1.00 24.09 ?  74  A1EJS A C27  1 
HETATM 571  C C26  . A1EJS A 1 74  ? 26.679  0.084   -29.981 1.00 22.67 ?  74  A1EJS A C26  1 
HETATM 572  C C18  . A1EJS A 1 74  ? 27.306  1.912   -24.188 1.00 31.26 ?  74  A1EJS A C18  1 
HETATM 573  C C17  . A1EJS A 1 74  ? 27.604  1.662   -25.509 1.00 30.68 ?  74  A1EJS A C17  1 
HETATM 574  O O15  . A1EJS A 1 74  ? 31.316  3.671   -27.803 1.00 44.08 ?  74  A1EJS A O15  1 
HETATM 575  O O14  . A1EJS A 1 74  ? 29.158  5.672   -29.114 1.00 36.32 ?  74  A1EJS A O14  1 
HETATM 576  C C13  . A1EJS A 1 74  ? 29.026  3.250   -26.849 1.00 26.28 ?  74  A1EJS A C13  1 
HETATM 577  C C10  . A1EJS A 1 74  ? 28.047  4.278   -27.364 1.00 30.67 ?  74  A1EJS A C10  1 
HETATM 578  C CE   . A1EJS A 1 74  ? 25.969  5.356   -28.182 1.00 33.56 ?  74  A1EJS A CE   1 
HETATM 579  C CD   . A1EJS A 1 74  ? 25.333  4.717   -29.422 1.00 27.97 ?  74  A1EJS A CD   1 
HETATM 580  C CG   . A1EJS A 1 74  ? 24.835  3.269   -29.288 1.00 21.68 ?  74  A1EJS A CG   1 
HETATM 581  C CB   . A1EJS A 1 74  ? 24.565  2.823   -30.723 1.00 16.33 ?  74  A1EJS A CB   1 
HETATM 582  C CA   . A1EJS A 1 74  ? 23.603  1.661   -30.947 1.00 16.23 ?  74  A1EJS A CA   1 
HETATM 583  C C    . A1EJS A 1 74  ? 22.191  2.087   -30.584 1.00 17.80 ?  74  A1EJS A C    1 
HETATM 584  C C11  . A1EJS A 1 74  ? 29.132  4.829   -28.286 1.00 33.32 ?  74  A1EJS A C11  1 
HETATM 585  C C12  . A1EJS A 1 74  ? 30.148  3.864   -27.682 1.00 36.03 ?  74  A1EJS A C12  1 
HETATM 586  C C20  . A1EJS A 1 74  ? 25.290  0.877   -24.573 1.00 27.34 ?  74  A1EJS A C20  1 
HETATM 587  C C31  . A1EJS A 1 74  ? 27.787  1.050   -30.373 1.00 27.95 ?  74  A1EJS A C31  1 
HETATM 588  C C34  . A1EJS A 1 74  ? 29.068  1.216   -32.371 1.00 46.13 ?  74  A1EJS A C34  1 
HETATM 589  C C35  . A1EJS A 1 74  ? 23.671  1.049   -22.776 1.00 22.07 ?  74  A1EJS A C35  1 
HETATM 590  C C36  . A1EJS A 1 74  ? 24.070  0.150   -21.600 1.00 24.85 ?  74  A1EJS A C36  1 
HETATM 591  C C37  . A1EJS A 1 74  ? 24.565  0.750   -20.452 1.00 25.42 ?  74  A1EJS A C37  1 
HETATM 592  C C38  . A1EJS A 1 74  ? 24.895  -0.030  -19.360 1.00 23.35 ?  74  A1EJS A C38  1 
HETATM 593  C C39  . A1EJS A 1 74  ? 24.736  -1.402  -19.413 1.00 24.66 ?  74  A1EJS A C39  1 
HETATM 594  C C40  . A1EJS A 1 74  ? 24.245  -2.007  -20.566 1.00 26.36 ?  74  A1EJS A C40  1 
HETATM 595  C C41  . A1EJS A 1 74  ? 23.911  -1.223  -21.662 1.00 18.89 ?  74  A1EJS A C41  1 
HETATM 596  C C42  . A1EJS A 1 74  ? 24.064  -3.522  -20.576 1.00 25.63 ?  74  A1EJS A C42  1 
HETATM 597  C C44  . A1EJS A 1 74  ? 24.440  -5.604  -20.339 1.00 23.96 ?  74  A1EJS A C44  1 
HETATM 598  C C45  . A1EJS A 1 74  ? 23.135  -5.438  -20.764 1.00 25.50 ?  74  A1EJS A C45  1 
HETATM 599  C C47  . A1EJS A 1 74  ? 21.673  -3.550  -21.313 1.00 20.19 ?  74  A1EJS A C47  1 
HETATM 600  F F48  . A1EJS A 1 74  ? 23.564  -2.425  -28.974 1.00 23.12 ?  74  A1EJS A F48  1 
HETATM 601  N NZ   . A1EJS A 1 74  ? 26.609  4.366   -27.341 1.00 27.60 ?  74  A1EJS A NZ   1 
HETATM 602  N N    . A1EJS A 1 74  ? 23.705  1.314   -32.345 1.00 16.70 ?  74  A1EJS A N    1 
HETATM 603  N N16  . A1EJS A 1 74  ? 28.890  2.064   -26.042 1.00 30.74 ?  74  A1EJS A N16  1 
HETATM 604  N N19  . A1EJS A 1 74  ? 26.135  1.502   -23.765 1.00 32.10 ?  74  A1EJS A N19  1 
HETATM 605  N N21  . A1EJS A 1 74  ? 25.539  0.622   -25.829 1.00 19.67 ?  74  A1EJS A N21  1 
HETATM 606  N N23  . A1EJS A 1 74  ? 24.032  0.454   -24.038 1.00 21.63 ?  74  A1EJS A N23  1 
HETATM 607  N N24  . A1EJS A 1 74  ? 27.046  0.772   -27.712 1.00 30.14 ?  74  A1EJS A N24  1 
HETATM 608  N N43  . A1EJS A 1 74  ? 24.990  -4.404  -20.234 1.00 25.80 ?  74  A1EJS A N43  1 
HETATM 609  N N46  . A1EJS A 1 74  ? 22.932  -4.142  -20.889 1.00 24.74 ?  74  A1EJS A N46  1 
HETATM 610  O O    . A1EJS A 1 74  ? 21.517  2.613   -31.378 1.00 20.41 ?  74  A1EJS A O    1 
HETATM 611  O O32  . A1EJS A 1 74  ? 27.858  1.454   -31.713 1.00 33.36 ?  74  A1EJS A O32  1 
HETATM 612  O O33  . A1EJS A 1 74  ? 28.500  1.518   -29.548 1.00 29.97 ?  74  A1EJS A O33  1 
HETATM 613  H H301 . A1EJS A 1 74  ? 24.931  -0.972  -27.278 1.00 23.96 ?  74  A1EJS A H301 1 
HETATM 614  H H281 . A1EJS A 1 74  ? 24.479  -2.047  -31.409 1.00 28.02 ?  74  A1EJS A H281 1 
HETATM 615  H H271 . A1EJS A 1 74  ? 26.326  -0.504  -32.010 1.00 28.90 ?  74  A1EJS A H271 1 
HETATM 616  H H181 . A1EJS A 1 74  ? 28.002  2.421   -23.534 1.00 37.52 ?  74  A1EJS A H181 1 
HETATM 617  H HE2  . A1EJS A 1 74  ? 25.196  5.859   -27.609 1.00 40.28 ?  74  A1EJS A HE2  1 
HETATM 618  H HE3  . A1EJS A 1 74  ? 26.710  6.082   -28.499 1.00 40.28 ?  74  A1EJS A HE3  1 
HETATM 619  H HD3  . A1EJS A 1 74  ? 24.486  5.331   -29.711 1.00 33.57 ?  74  A1EJS A HD3  1 
HETATM 620  H HD2  . A1EJS A 1 74  ? 26.071  4.739   -30.217 1.00 33.57 ?  74  A1EJS A HD2  1 
HETATM 621  H HG2  . A1EJS A 1 74  ? 25.590  2.642   -28.824 1.00 26.01 ?  74  A1EJS A HG2  1 
HETATM 622  H HG3  . A1EJS A 1 74  ? 23.927  3.226   -28.693 1.00 26.01 ?  74  A1EJS A HG3  1 
HETATM 623  H HB2  . A1EJS A 1 74  ? 24.171  3.677   -31.259 1.00 19.59 ?  74  A1EJS A HB2  1 
HETATM 624  H HB3  . A1EJS A 1 74  ? 25.517  2.543   -31.159 1.00 19.59 ?  74  A1EJS A HB3  1 
HETATM 625  H HA   . A1EJS A 1 74  ? 23.847  0.808   -30.326 1.00 19.47 ?  74  A1EJS A HA   1 
HETATM 626  H H341 . A1EJS A 1 74  ? 29.181  1.923   -33.189 1.00 55.36 ?  74  A1EJS A H341 1 
HETATM 627  H H343 . A1EJS A 1 74  ? 29.072  0.203   -32.766 1.00 55.36 ?  74  A1EJS A H343 1 
HETATM 628  H H342 . A1EJS A 1 74  ? 29.891  1.335   -31.672 1.00 55.36 ?  74  A1EJS A H342 1 
HETATM 629  H H352 . A1EJS A 1 74  ? 22.596  1.206   -22.753 1.00 26.49 ?  74  A1EJS A H352 1 
HETATM 630  H H351 . A1EJS A 1 74  ? 24.176  2.006   -22.678 1.00 26.49 ?  74  A1EJS A H351 1 
HETATM 631  H H371 . A1EJS A 1 74  ? 24.692  1.825   -20.411 1.00 30.50 ?  74  A1EJS A H371 1 
HETATM 632  H H381 . A1EJS A 1 74  ? 25.280  0.436   -18.459 1.00 28.02 ?  74  A1EJS A H381 1 
HETATM 633  H H391 . A1EJS A 1 74  ? 24.995  -2.009  -18.554 1.00 29.59 ?  74  A1EJS A H391 1 
HETATM 634  H H411 . A1EJS A 1 74  ? 23.527  -1.685  -22.563 1.00 22.67 ?  74  A1EJS A H411 1 
HETATM 635  H H441 . A1EJS A 1 74  ? 24.926  -6.550  -20.129 1.00 28.75 ?  74  A1EJS A H441 1 
HETATM 636  H H451 . A1EJS A 1 74  ? 22.415  -6.225  -20.958 1.00 30.60 ?  74  A1EJS A H451 1 
HETATM 637  H H472 . A1EJS A 1 74  ? 20.937  -4.334  -21.463 1.00 24.23 ?  74  A1EJS A H472 1 
HETATM 638  H H473 . A1EJS A 1 74  ? 21.822  -3.011  -22.243 1.00 24.23 ?  74  A1EJS A H473 1 
HETATM 639  H H471 . A1EJS A 1 74  ? 21.321  -2.864  -20.550 1.00 24.23 ?  74  A1EJS A H471 1 
HETATM 640  H HZ1  . A1EJS A 1 74  ? 26.067  3.758   -26.760 1.00 33.13 ?  74  A1EJS A HZ1  1 
HETATM 641  H H    . A1EJS A 1 74  ? 23.648  2.145   -32.905 1.00 20.04 ?  74  A1EJS A H    1 
HETATM 642  H H161 . A1EJS A 1 74  ? 29.698  1.507   -25.846 1.00 36.89 ?  74  A1EJS A H161 1 
HETATM 643  H H231 . A1EJS A 1 74  ? 23.447  -0.204  -24.505 1.00 25.96 ?  74  A1EJS A H231 1 
HETATM 644  H H241 . A1EJS A 1 74  ? 27.888  1.198   -28.044 1.00 36.16 ?  74  A1EJS A H241 1 
ATOM   645  N N    . ILE   A 1 75  ? 21.911  1.176   -29.526 1.00 15.32 ?  75  ILE   A N    1 
ATOM   646  C CA   . ILE   A 1 75  ? 20.530  1.299   -29.044 1.00 14.63 ?  75  ILE   A CA   1 
ATOM   647  C C    . ILE   A 1 75  ? 20.541  1.227   -27.523 1.00 16.29 ?  75  ILE   A C    1 
ATOM   648  O O    . ILE   A 1 75  ? 21.396  0.552   -26.944 1.00 21.05 ?  75  ILE   A O    1 
ATOM   649  C CB   . ILE   A 1 75  ? 19.623  0.195   -29.662 1.00 17.62 ?  75  ILE   A CB   1 
ATOM   650  C CG1  . ILE   A 1 75  ? 18.153  0.346   -29.232 1.00 15.88 ?  75  ILE   A CG1  1 
ATOM   651  C CG2  . ILE   A 1 75  ? 20.124  -1.200  -29.314 1.00 19.34 ?  75  ILE   A CG2  1 
ATOM   652  C CD1  . ILE   A 1 75  ? 17.196  -0.588  -30.005 1.00 19.29 ?  75  ILE   A CD1  1 
ATOM   653  N N    . TYR   A 1 76  ? 19.597  1.915   -26.876 1.00 13.53 ?  76  TYR   A N    1 
ATOM   654  C CA   . TYR   A 1 76  ? 19.466  1.917   -25.415 1.00 17.50 ?  76  TYR   A CA   1 
ATOM   655  C C    . TYR   A 1 76  ? 18.276  1.032   -25.037 1.00 17.25 ?  76  TYR   A C    1 
ATOM   656  O O    . TYR   A 1 76  ? 17.115  1.430   -25.181 1.00 15.87 ?  76  TYR   A O    1 
ATOM   657  C CB   . TYR   A 1 76  ? 19.286  3.338   -24.891 1.00 17.94 ?  76  TYR   A CB   1 
ATOM   658  C CG   . TYR   A 1 76  ? 19.528  3.473   -23.390 1.00 16.98 ?  76  TYR   A CG   1 
ATOM   659  C CD1  . TYR   A 1 76  ? 20.817  3.443   -22.880 1.00 22.66 ?  76  TYR   A CD1  1 
ATOM   660  C CD2  . TYR   A 1 76  ? 18.471  3.632   -22.505 1.00 18.00 ?  76  TYR   A CD2  1 
ATOM   661  C CE1  . TYR   A 1 76  ? 21.053  3.574   -21.513 1.00 24.06 ?  76  TYR   A CE1  1 
ATOM   662  C CE2  . TYR   A 1 76  ? 18.691  3.757   -21.125 1.00 19.10 ?  76  TYR   A CE2  1 
ATOM   663  C CZ   . TYR   A 1 76  ? 19.996  3.723   -20.646 1.00 22.26 ?  76  TYR   A CZ   1 
ATOM   664  O OH   . TYR   A 1 76  ? 20.254  3.850   -19.296 1.00 26.69 ?  76  TYR   A OH   1 
ATOM   665  N N    . HIS   A 1 77  ? 18.568  -0.182  -24.549 1.00 15.80 ?  77  HIS   A N    1 
ATOM   666  C CA   . HIS   A 1 77  ? 17.511  -1.167  -24.338 1.00 16.76 ?  77  HIS   A CA   1 
ATOM   667  C C    . HIS   A 1 77  ? 17.889  -2.181  -23.259 1.00 16.82 ?  77  HIS   A C    1 
ATOM   668  O O    . HIS   A 1 77  ? 19.035  -2.634  -23.224 1.00 16.55 ?  77  HIS   A O    1 
ATOM   669  C CB   . HIS   A 1 77  ? 17.202  -1.887  -25.664 1.00 19.19 ?  77  HIS   A CB   1 
ATOM   670  C CG   . HIS   A 1 77  ? 15.948  -2.707  -25.623 1.00 14.97 ?  77  HIS   A CG   1 
ATOM   671  N ND1  . HIS   A 1 77  ? 15.898  -3.952  -25.032 1.00 14.31 ?  77  HIS   A ND1  1 
ATOM   672  C CD2  . HIS   A 1 77  ? 14.697  -2.447  -26.068 1.00 16.67 ?  77  HIS   A CD2  1 
ATOM   673  C CE1  . HIS   A 1 77  ? 14.671  -4.426  -25.125 1.00 15.52 ?  77  HIS   A CE1  1 
ATOM   674  N NE2  . HIS   A 1 77  ? 13.922  -3.532  -25.750 1.00 16.95 ?  77  HIS   A NE2  1 
ATOM   675  N N    . PRO   A 1 78  ? 16.948  -2.574  -22.394 1.00 16.92 ?  78  PRO   A N    1 
ATOM   676  C CA   . PRO   A 1 78  ? 17.284  -3.508  -21.305 1.00 16.10 ?  78  PRO   A CA   1 
ATOM   677  C C    . PRO   A 1 78  ? 17.882  -4.820  -21.774 1.00 20.90 ?  78  PRO   A C    1 
ATOM   678  O O    . PRO   A 1 78  ? 18.616  -5.467  -21.014 1.00 23.12 ?  78  PRO   A O    1 
ATOM   679  C CB   . PRO   A 1 78  ? 15.925  -3.756  -20.633 1.00 19.83 ?  78  PRO   A CB   1 
ATOM   680  C CG   . PRO   A 1 78  ? 15.082  -2.635  -21.002 1.00 26.18 ?  78  PRO   A CG   1 
ATOM   681  C CD   . PRO   A 1 78  ? 15.547  -2.132  -22.336 1.00 17.32 ?  78  PRO   A CD   1 
ATOM   682  N N    . ASN   A 1 79  ? 17.564  -5.248  -22.993 1.00 15.17 ?  79  ASN   A N    1 
ATOM   683  C CA   . ASN   A 1 79  ? 17.937  -6.565  -23.494 1.00 16.80 ?  79  ASN   A CA   1 
ATOM   684  C C    . ASN   A 1 79  ? 19.168  -6.570  -24.395 1.00 15.92 ?  79  ASN   A C    1 
ATOM   685  O O    . ASN   A 1 79  ? 19.508  -7.628  -24.921 1.00 17.29 ?  79  ASN   A O    1 
ATOM   686  C CB   . ASN   A 1 79  ? 16.759  -7.173  -24.279 1.00 18.04 ?  79  ASN   A CB   1 
ATOM   687  C CG   . ASN   A 1 79  ? 15.579  -7.564  -23.397 1.00 23.12 ?  79  ASN   A CG   1 
ATOM   688  O OD1  . ASN   A 1 79  ? 14.780  -6.717  -22.970 1.00 19.69 ?  79  ASN   A OD1  1 
ATOM   689  N ND2  . ASN   A 1 79  ? 15.422  -8.863  -23.175 1.00 24.61 ?  79  ASN   A ND2  1 
ATOM   690  N N    . VAL   A 1 80  ? 19.834  -5.433  -24.605 1.00 16.19 ?  80  VAL   A N    1 
ATOM   691  C CA   . VAL   A 1 80  ? 20.927  -5.331  -25.573 1.00 14.54 ?  80  VAL   A CA   1 
ATOM   692  C C    . VAL   A 1 80  ? 22.159  -4.776  -24.863 1.00 17.14 ?  80  VAL   A C    1 
ATOM   693  O O    . VAL   A 1 80  ? 22.138  -3.632  -24.395 1.00 17.22 ?  80  VAL   A O    1 
ATOM   694  C CB   . VAL   A 1 80  ? 20.559  -4.442  -26.776 1.00 12.86 ?  80  VAL   A CB   1 
ATOM   695  C CG1  . VAL   A 1 80  ? 21.670  -4.492  -27.837 1.00 15.52 ?  80  VAL   A CG1  1 
ATOM   696  C CG2  . VAL   A 1 80  ? 19.184  -4.878  -27.384 1.00 12.45 ?  80  VAL   A CG2  1 
ATOM   697  N N    . ASP   A 1 81  ? 23.238  -5.566  -24.806 1.00 19.17 ?  81  ASP   A N    1 
ATOM   698  C CA   . ASP   A 1 81  ? 24.419  -5.118  -24.076 1.00 22.03 ?  81  ASP   A CA   1 
ATOM   699  C C    . ASP   A 1 81  ? 25.277  -4.199  -24.956 1.00 19.70 ?  81  ASP   A C    1 
ATOM   700  O O    . ASP   A 1 81  ? 24.885  -3.799  -26.059 1.00 17.92 ?  81  ASP   A O    1 
ATOM   701  C CB   . ASP   A 1 81  ? 25.185  -6.314  -23.489 1.00 20.81 ?  81  ASP   A CB   1 
ATOM   702  C CG   . ASP   A 1 81  ? 25.980  -7.120  -24.521 1.00 23.96 ?  81  ASP   A CG   1 
ATOM   703  O OD1  . ASP   A 1 81  ? 26.242  -6.645  -25.644 1.00 19.83 ?  81  ASP   A OD1  1 
ATOM   704  O OD2  . ASP   A 1 81  ? 26.397  -8.245  -24.168 1.00 24.93 -1 81  ASP   A OD2  1 
ATOM   705  N N    . LYS   A 1 82  ? 26.453  -3.801  -24.450 1.00 18.44 ?  82  LYS   A N    1 
ATOM   706  C CA   . LYS   A 1 82  ? 27.220  -2.739  -25.098 1.00 21.75 ?  82  LYS   A CA   1 
ATOM   707  C C    . LYS   A 1 82  ? 27.947  -3.214  -26.352 1.00 21.25 ?  82  LYS   A C    1 
ATOM   708  O O    . LYS   A 1 82  ? 28.509  -2.384  -27.078 1.00 21.06 ?  82  LYS   A O    1 
ATOM   709  C CB   . LYS   A 1 82  ? 28.238  -2.134  -24.116 1.00 24.98 ?  82  LYS   A CB   1 
ATOM   710  C CG   . LYS   A 1 82  ? 27.631  -1.252  -23.058 1.00 24.15 ?  82  LYS   A CG   1 
ATOM   711  C CD   . LYS   A 1 82  ? 28.665  -0.843  -22.001 1.00 29.17 ?  82  LYS   A CD   1 
ATOM   712  C CE   . LYS   A 1 82  ? 28.009  -0.308  -20.738 1.00 32.86 ?  82  LYS   A CE   1 
ATOM   713  N NZ   . LYS   A 1 82  ? 28.954  0.492   -19.911 1.00 35.10 ?  82  LYS   A NZ   1 
ATOM   714  N N    . LEU   A 1 83  ? 27.971  -4.518  -26.605 1.00 21.12 ?  83  LEU   A N    1 
ATOM   715  C CA   . LEU   A 1 83  ? 28.489  -5.071  -27.844 1.00 21.46 ?  83  LEU   A CA   1 
ATOM   716  C C    . LEU   A 1 83  ? 27.368  -5.514  -28.771 1.00 17.60 ?  83  LEU   A C    1 
ATOM   717  O O    . LEU   A 1 83  ? 27.627  -6.185  -29.776 1.00 19.46 ?  83  LEU   A O    1 
ATOM   718  C CB   . LEU   A 1 83  ? 29.426  -6.249  -27.550 1.00 21.03 ?  83  LEU   A CB   1 
ATOM   719  C CG   . LEU   A 1 83  ? 30.656  -5.841  -26.738 1.00 25.59 ?  83  LEU   A CG   1 
ATOM   720  C CD1  . LEU   A 1 83  ? 31.571  -7.047  -26.559 1.00 31.47 ?  83  LEU   A CD1  1 
ATOM   721  C CD2  . LEU   A 1 83  ? 31.409  -4.676  -27.380 1.00 28.51 ?  83  LEU   A CD2  1 
ATOM   722  N N    . GLY   A 1 84  ? 26.127  -5.170  -28.442 1.00 15.03 ?  84  GLY   A N    1 
ATOM   723  C CA   . GLY   A 1 84  ? 25.002  -5.542  -29.281 1.00 18.17 ?  84  GLY   A CA   1 
ATOM   724  C C    . GLY   A 1 84  ? 24.449  -6.932  -29.052 1.00 21.32 ?  84  GLY   A C    1 
ATOM   725  O O    . GLY   A 1 84  ? 23.570  -7.367  -29.813 1.00 17.90 ?  84  GLY   A O    1 
ATOM   726  N N    . ARG   A 1 85  ? 24.933  -7.660  -28.047 1.00 18.50 ?  85  ARG   A N    1 
ATOM   727  C CA   . ARG   A 1 85  ? 24.385  -8.987  -27.816 1.00 21.10 ?  85  ARG   A CA   1 
ATOM   728  C C    . ARG   A 1 85  ? 22.996  -8.891  -27.192 1.00 17.76 ?  85  ARG   A C    1 
ATOM   729  O O    . ARG   A 1 85  ? 22.701  -7.973  -26.419 1.00 18.81 ?  85  ARG   A O    1 
ATOM   730  C CB   . ARG   A 1 85  ? 25.338  -9.811  -26.953 1.00 21.12 ?  85  ARG   A CB   1 
ATOM   731  C CG   . ARG   A 1 85  ? 26.605  -10.197 -27.739 1.00 28.00 ?  85  ARG   A CG   1 
ATOM   732  C CD   . ARG   A 1 85  ? 27.623  -10.905 -26.868 1.00 31.71 ?  85  ARG   A CD   1 
ATOM   733  N NE   . ARG   A 1 85  ? 28.047  -10.037 -25.782 1.00 32.26 ?  85  ARG   A NE   1 
ATOM   734  C CZ   . ARG   A 1 85  ? 29.149  -10.204 -25.070 1.00 38.29 ?  85  ARG   A CZ   1 
ATOM   735  N NH1  . ARG   A 1 85  ? 30.011  -11.172 -25.345 1.00 38.24 ?  85  ARG   A NH1  1 
ATOM   736  N NH2  . ARG   A 1 85  ? 29.401  -9.370  -24.068 1.00 33.68 ?  85  ARG   A NH2  1 
ATOM   737  N N    . ILE   A 1 86  ? 22.126  -9.828  -27.568 1.00 17.87 ?  86  ILE   A N    1 
ATOM   738  C CA   . ILE   A 1 86  ? 20.710  -9.774  -27.233 1.00 13.96 ?  86  ILE   A CA   1 
ATOM   739  C C    . ILE   A 1 86  ? 20.403  -10.844 -26.196 1.00 19.70 ?  86  ILE   A C    1 
ATOM   740  O O    . ILE   A 1 86  ? 20.736  -12.019 -26.389 1.00 26.20 ?  86  ILE   A O    1 
ATOM   741  C CB   . ILE   A 1 86  ? 19.830  -9.952  -28.485 1.00 19.04 ?  86  ILE   A CB   1 
ATOM   742  C CG1  . ILE   A 1 86  ? 20.093  -8.823  -29.479 1.00 13.79 ?  86  ILE   A CG1  1 
ATOM   743  C CG2  . ILE   A 1 86  ? 18.363  -9.962  -28.117 1.00 19.25 ?  86  ILE   A CG2  1 
ATOM   744  C CD1  . ILE   A 1 86  ? 19.482  -9.095  -30.843 1.00 20.15 ?  86  ILE   A CD1  1 
ATOM   745  N N    . CYS   A 1 87  ? 19.766  -10.439 -25.101 1.00 19.60 ?  87  CYS   A N    1 
ATOM   746  C CA   . CYS   A 1 87  ? 19.325  -11.375 -24.069 1.00 19.17 ?  87  CYS   A CA   1 
ATOM   747  C C    . CYS   A 1 87  ? 17.866  -11.720 -24.349 1.00 19.46 ?  87  CYS   A C    1 
ATOM   748  O O    . CYS   A 1 87  ? 16.967  -10.921 -24.096 1.00 21.45 ?  87  CYS   A O    1 
ATOM   749  C CB   . CYS   A 1 87  ? 19.501  -10.778 -22.679 1.00 19.20 ?  87  CYS   A CB   1 
ATOM   750  S SG   . CYS   A 1 87  ? 18.938  -11.891 -21.342 1.00 32.00 ?  87  CYS   A SG   1 
ATOM   751  N N    . LEU   A 1 88  ? 17.642  -12.926 -24.859 1.00 18.43 ?  88  LEU   A N    1 
ATOM   752  C CA   . LEU   A 1 88  ? 16.335  -13.408 -25.264 1.00 17.66 ?  88  LEU   A CA   1 
ATOM   753  C C    . LEU   A 1 88  ? 16.316  -14.912 -25.046 1.00 18.18 ?  88  LEU   A C    1 
ATOM   754  O O    . LEU   A 1 88  ? 17.201  -15.618 -25.534 1.00 17.77 ?  88  LEU   A O    1 
ATOM   755  C CB   . LEU   A 1 88  ? 16.079  -13.065 -26.738 1.00 20.59 ?  88  LEU   A CB   1 
ATOM   756  C CG   . LEU   A 1 88  ? 14.754  -13.460 -27.379 1.00 20.29 ?  88  LEU   A CG   1 
ATOM   757  C CD1  . LEU   A 1 88  ? 13.586  -12.894 -26.580 1.00 21.16 ?  88  LEU   A CD1  1 
ATOM   758  C CD2  . LEU   A 1 88  ? 14.751  -12.957 -28.828 1.00 22.65 ?  88  LEU   A CD2  1 
ATOM   759  N N    . ASP   A 1 89  ? 15.306  -15.412 -24.331 1.00 18.16 ?  89  ASP   A N    1 
ATOM   760  C CA   . ASP   A 1 89  ? 15.363  -16.818 -23.932 1.00 21.72 ?  89  ASP   A CA   1 
ATOM   761  C C    . ASP   A 1 89  ? 15.441  -17.762 -25.135 1.00 22.01 ?  89  ASP   A C    1 
ATOM   762  O O    . ASP   A 1 89  ? 16.158  -18.771 -25.094 1.00 22.33 ?  89  ASP   A O    1 
ATOM   763  C CB   . ASP   A 1 89  ? 14.182  -17.176 -23.011 1.00 22.05 ?  89  ASP   A CB   1 
ATOM   764  C CG   . ASP   A 1 89  ? 12.808  -16.836 -23.591 1.00 30.92 ?  89  ASP   A CG   1 
ATOM   765  O OD1  . ASP   A 1 89  ? 12.686  -16.323 -24.722 1.00 24.81 ?  89  ASP   A OD1  1 
ATOM   766  O OD2  . ASP   A 1 89  ? 11.828  -17.088 -22.862 1.00 36.94 -1 89  ASP   A OD2  1 
ATOM   767  N N    . ILE   A 1 90  ? 14.720  -17.472 -26.216 1.00 19.95 ?  90  ILE   A N    1 
ATOM   768  C CA   . ILE   A 1 90  ? 14.751  -18.411 -27.333 1.00 18.96 ?  90  ILE   A CA   1 
ATOM   769  C C    . ILE   A 1 90  ? 16.062  -18.350 -28.119 1.00 24.53 ?  90  ILE   A C    1 
ATOM   770  O O    . ILE   A 1 90  ? 16.257  -19.133 -29.055 1.00 22.71 ?  90  ILE   A O    1 
ATOM   771  C CB   . ILE   A 1 90  ? 13.560  -18.214 -28.292 1.00 19.12 ?  90  ILE   A CB   1 
ATOM   772  C CG1  . ILE   A 1 90  ? 13.560  -16.796 -28.892 1.00 22.00 ?  90  ILE   A CG1  1 
ATOM   773  C CG2  . ILE   A 1 90  ? 12.264  -18.538 -27.580 1.00 21.82 ?  90  ILE   A CG2  1 
ATOM   774  C CD1  . ILE   A 1 90  ? 12.649  -16.664 -30.113 1.00 21.72 ?  90  ILE   A CD1  1 
ATOM   775  N N    . LEU   A 1 91  ? 16.960  -17.421 -27.779 1.00 18.28 ?  91  LEU   A N    1 
ATOM   776  C CA   . LEU   A 1 91  ? 18.304  -17.443 -28.346 1.00 21.37 ?  91  LEU   A CA   1 
ATOM   777  C C    . LEU   A 1 91  ? 19.273  -18.219 -27.461 1.00 21.73 ?  91  LEU   A C    1 
ATOM   778  O O    . LEU   A 1 91  ? 20.439  -18.392 -27.838 1.00 26.10 ?  91  LEU   A O    1 
ATOM   779  C CB   . LEU   A 1 91  ? 18.823  -16.015 -28.580 1.00 19.62 ?  91  LEU   A CB   1 
ATOM   780  C CG   . LEU   A 1 91  ? 18.095  -15.182 -29.650 1.00 19.83 ?  91  LEU   A CG   1 
ATOM   781  C CD1  . LEU   A 1 91  ? 18.671  -13.769 -29.724 1.00 23.99 ?  91  LEU   A CD1  1 
ATOM   782  C CD2  . LEU   A 1 91  ? 18.118  -15.847 -31.023 1.00 19.33 ?  91  LEU   A CD2  1 
ATOM   783  N N    . LYS   A 1 92  ? 18.808  -18.688 -26.300 1.00 24.55 ?  92  LYS   A N    1 
ATOM   784  C CA   . LYS   A 1 92  ? 19.597  -19.538 -25.415 1.00 27.43 ?  92  LYS   A CA   1 
ATOM   785  C C    . LYS   A 1 92  ? 18.800  -20.761 -24.968 1.00 28.51 ?  92  LYS   A C    1 
ATOM   786  O O    . LYS   A 1 92  ? 18.523  -21.659 -25.772 1.00 34.73 ?  92  LYS   A O    1 
ATOM   787  C CB   . LYS   A 1 92  ? 20.101  -18.753 -24.197 1.00 32.04 ?  92  LYS   A CB   1 
ATOM   788  C CG   . LYS   A 1 92  ? 19.382  -17.453 -23.858 1.00 35.57 ?  92  LYS   A CG   1 
ATOM   789  C CD   . LYS   A 1 92  ? 20.082  -16.744 -22.684 1.00 44.65 ?  92  LYS   A CD   1 
ATOM   790  C CE   . LYS   A 1 92  ? 19.403  -15.435 -22.260 1.00 44.64 ?  92  LYS   A CE   1 
ATOM   791  N NZ   . LYS   A 1 92  ? 18.024  -15.621 -21.701 1.00 42.82 ?  92  LYS   A NZ   1 
ATOM   792  N N    . ASP   A 1 93  ? 18.425  -20.789 -23.685 1.00 32.32 ?  93  ASP   A N    1 
ATOM   793  C CA   . ASP   A 1 93  ? 17.775  -21.952 -23.083 1.00 35.55 ?  93  ASP   A CA   1 
ATOM   794  C C    . ASP   A 1 93  ? 16.603  -22.474 -23.901 1.00 33.02 ?  93  ASP   A C    1 
ATOM   795  O O    . ASP   A 1 93  ? 16.418  -23.690 -24.029 1.00 31.09 ?  93  ASP   A O    1 
ATOM   796  C CB   . ASP   A 1 93  ? 17.275  -21.593 -21.682 1.00 49.34 ?  93  ASP   A CB   1 
ATOM   797  C CG   . ASP   A 1 93  ? 18.287  -21.887 -20.612 1.00 61.97 ?  93  ASP   A CG   1 
ATOM   798  O OD1  . ASP   A 1 93  ? 19.489  -21.976 -20.947 1.00 66.81 ?  93  ASP   A OD1  1 
ATOM   799  O OD2  . ASP   A 1 93  ? 17.879  -22.033 -19.438 1.00 65.46 -1 93  ASP   A OD2  1 
ATOM   800  N N    . LYS   A 1 94  ? 15.768  -21.578 -24.414 1.00 28.01 ?  94  LYS   A N    1 
ATOM   801  C CA   . LYS   A 1 94  ? 14.459  -21.966 -24.909 1.00 27.96 ?  94  LYS   A CA   1 
ATOM   802  C C    . LYS   A 1 94  ? 14.425  -22.143 -26.419 1.00 22.68 ?  94  LYS   A C    1 
ATOM   803  O O    . LYS   A 1 94  ? 13.337  -22.273 -26.986 1.00 26.42 ?  94  LYS   A O    1 
ATOM   804  C CB   . LYS   A 1 94  ? 13.398  -20.947 -24.467 1.00 24.70 ?  94  LYS   A CB   1 
ATOM   805  C CG   . LYS   A 1 94  ? 13.315  -20.729 -22.960 1.00 35.50 ?  94  LYS   A CG   1 
ATOM   806  C CD   . LYS   A 1 94  ? 12.842  -21.988 -22.237 1.00 37.13 ?  94  LYS   A CD   1 
ATOM   807  C CE   . LYS   A 1 94  ? 12.745  -21.757 -20.733 1.00 39.92 ?  94  LYS   A CE   1 
ATOM   808  N NZ   . LYS   A 1 94  ? 13.535  -22.761 -19.966 1.00 52.95 ?  94  LYS   A NZ   1 
ATOM   809  N N    . TRP   A 1 95  ? 15.575  -22.148 -27.094 1.00 22.53 ?  95  TRP   A N    1 
ATOM   810  C CA   . TRP   A 1 95  ? 15.539  -22.431 -28.521 1.00 19.37 ?  95  TRP   A CA   1 
ATOM   811  C C    . TRP   A 1 95  ? 15.084  -23.866 -28.756 1.00 27.31 ?  95  TRP   A C    1 
ATOM   812  O O    . TRP   A 1 95  ? 15.333  -24.764 -27.946 1.00 29.48 ?  95  TRP   A O    1 
ATOM   813  C CB   . TRP   A 1 95  ? 16.905  -22.206 -29.179 1.00 23.55 ?  95  TRP   A CB   1 
ATOM   814  C CG   . TRP   A 1 95  ? 16.889  -22.642 -30.606 1.00 23.15 ?  95  TRP   A CG   1 
ATOM   815  C CD1  . TRP   A 1 95  ? 17.375  -23.826 -31.118 1.00 23.91 ?  95  TRP   A CD1  1 
ATOM   816  C CD2  . TRP   A 1 95  ? 16.303  -21.941 -31.706 1.00 22.84 ?  95  TRP   A CD2  1 
ATOM   817  N NE1  . TRP   A 1 95  ? 17.132  -23.889 -32.468 1.00 24.92 ?  95  TRP   A NE1  1 
ATOM   818  C CE2  . TRP   A 1 95  ? 16.479  -22.745 -32.857 1.00 26.54 ?  95  TRP   A CE2  1 
ATOM   819  C CE3  . TRP   A 1 95  ? 15.644  -20.709 -31.833 1.00 18.92 ?  95  TRP   A CE3  1 
ATOM   820  C CZ2  . TRP   A 1 95  ? 16.023  -22.353 -34.121 1.00 29.87 ?  95  TRP   A CZ2  1 
ATOM   821  C CZ3  . TRP   A 1 95  ? 15.199  -20.320 -33.085 1.00 17.66 ?  95  TRP   A CZ3  1 
ATOM   822  C CH2  . TRP   A 1 95  ? 15.388  -21.138 -34.217 1.00 23.45 ?  95  TRP   A CH2  1 
ATOM   823  N N    . SER   A 1 96  ? 14.396  -24.075 -29.871 1.00 22.48 ?  96  SER   A N    1 
ATOM   824  C CA   . SER   A 1 96  ? 14.136  -25.422 -30.355 1.00 24.28 ?  96  SER   A CA   1 
ATOM   825  C C    . SER   A 1 96  ? 13.987  -25.368 -31.866 1.00 30.57 ?  96  SER   A C    1 
ATOM   826  O O    . SER   A 1 96  ? 13.683  -24.307 -32.432 1.00 23.97 ?  96  SER   A O    1 
ATOM   827  C CB   . SER   A 1 96  ? 12.895  -26.037 -29.692 1.00 28.51 ?  96  SER   A CB   1 
ATOM   828  O OG   . SER   A 1 96  ? 11.750  -25.918 -30.502 1.00 28.95 ?  96  SER   A OG   1 
ATOM   829  N N    . PRO   A 1 97  ? 14.223  -26.487 -32.553 1.00 28.65 ?  97  PRO   A N    1 
ATOM   830  C CA   . PRO   A 1 97  ? 14.079  -26.498 -34.014 1.00 28.89 ?  97  PRO   A CA   1 
ATOM   831  C C    . PRO   A 1 97  ? 12.652  -26.280 -34.477 1.00 27.10 ?  97  PRO   A C    1 
ATOM   832  O O    . PRO   A 1 97  ? 12.441  -26.057 -35.673 1.00 33.84 ?  97  PRO   A O    1 
ATOM   833  C CB   . PRO   A 1 97  ? 14.590  -27.889 -34.419 1.00 36.79 ?  97  PRO   A CB   1 
ATOM   834  C CG   . PRO   A 1 97  ? 15.241  -28.460 -33.221 1.00 32.88 ?  97  PRO   A CG   1 
ATOM   835  C CD   . PRO   A 1 97  ? 14.691  -27.777 -32.019 1.00 35.29 ?  97  PRO   A CD   1 
ATOM   836  N N    . ALA   A 1 98  ? 11.670  -26.344 -33.575 1.00 25.37 ?  98  ALA   A N    1 
ATOM   837  C CA   . ALA   A 1 98  ? 10.309  -25.953 -33.934 1.00 24.09 ?  98  ALA   A CA   1 
ATOM   838  C C    . ALA   A 1 98  ? 10.226  -24.478 -34.295 1.00 28.30 ?  98  ALA   A C    1 
ATOM   839  O O    . ALA   A 1 98  ? 9.361   -24.078 -35.083 1.00 30.03 ?  98  ALA   A O    1 
ATOM   840  C CB   . ALA   A 1 98  ? 9.350   -26.263 -32.783 1.00 33.56 ?  98  ALA   A CB   1 
ATOM   841  N N    . LEU   A 1 99  ? 11.118  -23.659 -33.743 1.00 26.27 ?  99  LEU   A N    1 
ATOM   842  C CA   . LEU   A 1 99  ? 11.147  -22.235 -34.026 1.00 19.80 ?  99  LEU   A CA   1 
ATOM   843  C C    . LEU   A 1 99  ? 11.965  -21.960 -35.288 1.00 22.61 ?  99  LEU   A C    1 
ATOM   844  O O    . LEU   A 1 99  ? 12.661  -22.830 -35.818 1.00 24.50 ?  99  LEU   A O    1 
ATOM   845  C CB   . LEU   A 1 99  ? 11.723  -21.475 -32.833 1.00 19.14 ?  99  LEU   A CB   1 
ATOM   846  C CG   . LEU   A 1 99  ? 11.163  -21.847 -31.459 1.00 21.52 ?  99  LEU   A CG   1 
ATOM   847  C CD1  . LEU   A 1 99  ? 11.793  -21.009 -30.347 1.00 24.88 ?  99  LEU   A CD1  1 
ATOM   848  C CD2  . LEU   A 1 99  ? 9.644   -21.669 -31.481 1.00 23.69 ?  99  LEU   A CD2  1 
ATOM   849  N N    . GLN   A 1 100 ? 11.877  -20.733 -35.787 1.00 19.36 ?  100 GLN   A N    1 
ATOM   850  C CA   . GLN   A 1 100 ? 12.580  -20.418 -37.024 1.00 21.38 ?  100 GLN   A CA   1 
ATOM   851  C C    . GLN   A 1 100 ? 13.001  -18.959 -37.024 1.00 20.84 ?  100 GLN   A C    1 
ATOM   852  O O    . GLN   A 1 100 ? 12.702  -18.202 -36.097 1.00 19.79 ?  100 GLN   A O    1 
ATOM   853  C CB   . GLN   A 1 100 ? 11.718  -20.759 -38.233 1.00 26.34 ?  100 GLN   A CB   1 
ATOM   854  C CG   . GLN   A 1 100 ? 10.427  -20.015 -38.261 1.00 23.76 ?  100 GLN   A CG   1 
ATOM   855  C CD   . GLN   A 1 100 ? 9.566   -20.461 -39.408 1.00 42.30 ?  100 GLN   A CD   1 
ATOM   856  O OE1  . GLN   A 1 100 ? 10.021  -20.518 -40.558 1.00 38.94 ?  100 GLN   A OE1  1 
ATOM   857  N NE2  . GLN   A 1 100 ? 8.319   -20.797 -39.111 1.00 36.95 ?  100 GLN   A NE2  1 
ATOM   858  N N    . ILE   A 1 101 ? 13.749  -18.587 -38.069 1.00 19.43 ?  101 ILE   A N    1 
ATOM   859  C CA   . ILE   A 1 101 ? 14.297  -17.235 -38.177 1.00 15.41 ?  101 ILE   A CA   1 
ATOM   860  C C    . ILE   A 1 101 ? 13.195  -16.194 -38.017 1.00 14.06 ?  101 ILE   A C    1 
ATOM   861  O O    . ILE   A 1 101 ? 13.353  -15.190 -37.304 1.00 17.97 ?  101 ILE   A O    1 
ATOM   862  C CB   . ILE   A 1 101 ? 15.031  -17.071 -39.521 1.00 19.75 ?  101 ILE   A CB   1 
ATOM   863  C CG1  . ILE   A 1 101 ? 16.273  -17.971 -39.564 1.00 20.50 ?  101 ILE   A CG1  1 
ATOM   864  C CG2  . ILE   A 1 101 ? 15.443  -15.612 -39.726 1.00 17.62 ?  101 ILE   A CG2  1 
ATOM   865  C CD1  . ILE   A 1 101 ? 16.936  -18.040 -40.967 1.00 18.81 ?  101 ILE   A CD1  1 
ATOM   866  N N    . ARG   A 1 102 ? 12.064  -16.415 -38.683 1.00 18.00 ?  102 ARG   A N    1 
ATOM   867  C CA   . ARG   A 1 102 ? 10.988  -15.434 -38.634 1.00 22.75 ?  102 ARG   A CA   1 
ATOM   868  C C    . ARG   A 1 102 ? 10.512  -15.208 -37.196 1.00 18.79 ?  102 ARG   A C    1 
ATOM   869  O O    . ARG   A 1 102 ? 10.193  -14.070 -36.817 1.00 16.88 ?  102 ARG   A O    1 
ATOM   870  C CB   . ARG   A 1 102 ? 9.856   -15.880 -39.565 1.00 23.12 ?  102 ARG   A CB   1 
ATOM   871  C CG   . ARG   A 1 102 ? 8.517   -15.155 -39.392 1.00 29.56 ?  102 ARG   A CG   1 
ATOM   872  C CD   . ARG   A 1 102 ? 7.465   -15.828 -40.262 1.00 28.50 ?  102 ARG   A CD   1 
ATOM   873  N NE   . ARG   A 1 102 ? 8.107   -16.270 -41.489 1.00 34.81 ?  102 ARG   A NE   1 
ATOM   874  C CZ   . ARG   A 1 102 ? 8.123   -15.571 -42.616 1.00 39.30 ?  102 ARG   A CZ   1 
ATOM   875  N NH1  . ARG   A 1 102 ? 7.412   -14.463 -42.751 1.00 34.04 ?  102 ARG   A NH1  1 
ATOM   876  N NH2  . ARG   A 1 102 ? 8.885   -15.986 -43.627 1.00 35.86 ?  102 ARG   A NH2  1 
ATOM   877  N N    . THR   A 1 103 ? 10.492  -16.271 -36.372 1.00 17.38 ?  103 THR   A N    1 
ATOM   878  C CA   . THR   A 1 103 ? 10.127  -16.136 -34.962 1.00 17.28 ?  103 THR   A CA   1 
ATOM   879  C C    . THR   A 1 103 ? 11.100  -15.235 -34.221 1.00 17.67 ?  103 THR   A C    1 
ATOM   880  O O    . THR   A 1 103 ? 10.699  -14.421 -33.381 1.00 17.15 ?  103 THR   A O    1 
ATOM   881  C CB   . THR   A 1 103 ? 10.120  -17.496 -34.263 1.00 22.50 ?  103 THR   A CB   1 
ATOM   882  O OG1  . THR   A 1 103 ? 9.606   -18.509 -35.135 1.00 32.23 ?  103 THR   A OG1  1 
ATOM   883  C CG2  . THR   A 1 103 ? 9.283   -17.418 -32.978 1.00 18.01 ?  103 THR   A CG2  1 
ATOM   884  N N    . VAL   A 1 104 ? 12.396  -15.384 -34.508 1.00 14.82 ?  104 VAL   A N    1 
ATOM   885  C CA   . VAL   A 1 104 ? 13.409  -14.588 -33.820 1.00 17.25 ?  104 VAL   A CA   1 
ATOM   886  C C    . VAL   A 1 104 ? 13.264  -13.120 -34.189 1.00 17.24 ?  104 VAL   A C    1 
ATOM   887  O O    . VAL   A 1 104 ? 13.362  -12.230 -33.333 1.00 15.46 ?  104 VAL   A O    1 
ATOM   888  C CB   . VAL   A 1 104 ? 14.820  -15.100 -34.161 1.00 16.25 ?  104 VAL   A CB   1 
ATOM   889  C CG1  . VAL   A 1 104 ? 15.860  -14.190 -33.562 1.00 16.82 ?  104 VAL   A CG1  1 
ATOM   890  C CG2  . VAL   A 1 104 ? 15.004  -16.546 -33.656 1.00 19.51 ?  104 VAL   A CG2  1 
ATOM   891  N N    . LEU   A 1 105 ? 13.081  -12.850 -35.484 1.00 17.11 ?  105 LEU   A N    1 
ATOM   892  C CA   . LEU   A 1 105 ? 12.944  -11.470 -35.939 1.00 14.53 ?  105 LEU   A CA   1 
ATOM   893  C C    . LEU   A 1 105 ? 11.699  -10.819 -35.333 1.00 14.66 ?  105 LEU   A C    1 
ATOM   894  O O    . LEU   A 1 105 ? 11.744  -9.671  -34.858 1.00 14.68 ?  105 LEU   A O    1 
ATOM   895  C CB   . LEU   A 1 105 ? 12.891  -11.443 -37.467 1.00 19.84 ?  105 LEU   A CB   1 
ATOM   896  C CG   . LEU   A 1 105 ? 14.113  -11.971 -38.222 1.00 20.59 ?  105 LEU   A CG   1 
ATOM   897  C CD1  . LEU   A 1 105 ? 13.856  -11.959 -39.716 1.00 20.37 ?  105 LEU   A CD1  1 
ATOM   898  C CD2  . LEU   A 1 105 ? 15.319  -11.129 -37.882 1.00 25.22 ?  105 LEU   A CD2  1 
ATOM   899  N N    . LEU   A 1 106 ? 10.567  -11.539 -35.349 1.00 16.42 ?  106 LEU   A N    1 
ATOM   900  C CA   . LEU   A 1 106 ? 9.352   -11.003 -34.737 1.00 14.04 ?  106 LEU   A CA   1 
ATOM   901  C C    . LEU   A 1 106 ? 9.532   -10.776 -33.241 1.00 15.71 ?  106 LEU   A C    1 
ATOM   902  O O    . LEU   A 1 106 ? 9.009   -9.798  -32.688 1.00 15.80 ?  106 LEU   A O    1 
ATOM   903  C CB   . LEU   A 1 106 ? 8.188   -11.956 -35.001 1.00 14.21 ?  106 LEU   A CB   1 
ATOM   904  C CG   . LEU   A 1 106 ? 7.676   -11.910 -36.436 1.00 25.14 ?  106 LEU   A CG   1 
ATOM   905  C CD1  . LEU   A 1 106 ? 6.770   -13.113 -36.721 1.00 28.20 ?  106 LEU   A CD1  1 
ATOM   906  C CD2  . LEU   A 1 106 ? 6.922   -10.608 -36.637 1.00 29.88 ?  106 LEU   A CD2  1 
ATOM   907  N N    . SER   A 1 107 ? 10.268  -11.671 -32.565 1.00 15.19 ?  107 SER   A N    1 
ATOM   908  C CA   . SER   A 1 107 ? 10.507  -11.490 -31.133 1.00 15.56 ?  107 SER   A CA   1 
ATOM   909  C C    . SER   A 1 107 ? 11.325  -10.239 -30.842 1.00 14.62 ?  107 SER   A C    1 
ATOM   910  O O    . SER   A 1 107 ? 11.064  -9.538  -29.857 1.00 13.14 ?  107 SER   A O    1 
ATOM   911  C CB   . SER   A 1 107 ? 11.215  -12.717 -30.549 1.00 14.22 ?  107 SER   A CB   1 
ATOM   912  O OG   . SER   A 1 107 ? 10.410  -13.866 -30.627 1.00 18.06 ?  107 SER   A OG   1 
ATOM   913  N N    . ILE   A 1 108 ? 12.359  -9.967  -31.647 1.00 15.09 ?  108 ILE   A N    1 
ATOM   914  C CA   . ILE   A 1 108 ? 13.170  -8.775  -31.401 1.00 13.47 ?  108 ILE   A CA   1 
ATOM   915  C C    . ILE   A 1 108 ? 12.346  -7.512  -31.628 1.00 15.03 ?  108 ILE   A C    1 
ATOM   916  O O    . ILE   A 1 108 ? 12.395  -6.554  -30.833 1.00 14.22 ?  108 ILE   A O    1 
ATOM   917  C CB   . ILE   A 1 108 ? 14.437  -8.807  -32.282 1.00 11.47 ?  108 ILE   A CB   1 
ATOM   918  C CG1  . ILE   A 1 108 ? 15.298  -9.997  -31.866 1.00 14.45 ?  108 ILE   A CG1  1 
ATOM   919  C CG2  . ILE   A 1 108 ? 15.197  -7.490  -32.169 1.00 14.50 ?  108 ILE   A CG2  1 
ATOM   920  C CD1  . ILE   A 1 108 ? 16.419  -10.356 -32.888 1.00 13.88 ?  108 ILE   A CD1  1 
ATOM   921  N N    . GLN   A 1 109 ? 11.559  -7.492  -32.716 1.00 12.81 ?  109 GLN   A N    1 
ATOM   922  C CA   . GLN   A 1 109 ? 10.643  -6.375  -32.928 1.00 16.42 ?  109 GLN   A CA   1 
ATOM   923  C C    . GLN   A 1 109 ? 9.735   -6.180  -31.719 1.00 16.32 ?  109 GLN   A C    1 
ATOM   924  O O    . GLN   A 1 109 ? 9.498   -5.043  -31.272 1.00 14.91 ?  109 GLN   A O    1 
ATOM   925  C CB   . GLN   A 1 109 ? 9.804   -6.641  -34.175 1.00 14.45 ?  109 GLN   A CB   1 
ATOM   926  C CG   . GLN   A 1 109 ? 8.891   -5.513  -34.589 1.00 15.28 ?  109 GLN   A CG   1 
ATOM   927  C CD   . GLN   A 1 109 ? 8.081   -5.900  -35.811 1.00 17.87 ?  109 GLN   A CD   1 
ATOM   928  O OE1  . GLN   A 1 109 ? 7.352   -6.893  -35.799 1.00 20.96 ?  109 GLN   A OE1  1 
ATOM   929  N NE2  . GLN   A 1 109 ? 8.247   -5.146  -36.892 1.00 15.98 ?  109 GLN   A NE2  1 
ATOM   930  N N    . ALA   A 1 110 ? 9.210   -7.284  -31.186 1.00 15.69 ?  110 ALA   A N    1 
ATOM   931  C CA   . ALA   A 1 110 ? 8.328   -7.197  -30.029 1.00 13.73 ?  110 ALA   A CA   1 
ATOM   932  C C    . ALA   A 1 110 ? 9.067   -6.661  -28.804 1.00 16.62 ?  110 ALA   A C    1 
ATOM   933  O O    . ALA   A 1 110 ? 8.490   -5.910  -28.008 1.00 18.26 ?  110 ALA   A O    1 
ATOM   934  C CB   . ALA   A 1 110 ? 7.713   -8.563  -29.728 1.00 15.87 ?  110 ALA   A CB   1 
ATOM   935  N N    . LEU   A 1 111 ? 10.346  -7.033  -28.647 1.00 16.70 ?  111 LEU   A N    1 
ATOM   936  C CA   . LEU   A 1 111 ? 11.159  -6.505  -27.549 1.00 16.62 ?  111 LEU   A CA   1 
ATOM   937  C C    . LEU   A 1 111 ? 11.270  -4.984  -27.623 1.00 19.79 ?  111 LEU   A C    1 
ATOM   938  O O    . LEU   A 1 111 ? 11.239  -4.295  -26.589 1.00 19.07 ?  111 LEU   A O    1 
ATOM   939  C CB   . LEU   A 1 111 ? 12.551  -7.148  -27.586 1.00 16.14 ?  111 LEU   A CB   1 
ATOM   940  C CG   . LEU   A 1 111 ? 12.825  -8.468  -26.876 1.00 21.23 ?  111 LEU   A CG   1 
ATOM   941  C CD1  . LEU   A 1 111 ? 14.349  -8.736  -26.909 1.00 19.95 ?  111 LEU   A CD1  1 
ATOM   942  C CD2  . LEU   A 1 111 ? 12.325  -8.472  -25.446 1.00 23.82 ?  111 LEU   A CD2  1 
ATOM   943  N N    . LEU   A 1 112 ? 11.416  -4.443  -28.841 1.00 14.82 ?  112 LEU   A N    1 
ATOM   944  C CA   . LEU   A 1 112 ? 11.531  -2.994  -28.999 1.00 17.32 ?  112 LEU   A CA   1 
ATOM   945  C C    . LEU   A 1 112 ? 10.193  -2.303  -28.750 1.00 18.58 ?  112 LEU   A C    1 
ATOM   946  O O    . LEU   A 1 112 ? 10.144  -1.213  -28.167 1.00 18.98 ?  112 LEU   A O    1 
ATOM   947  C CB   . LEU   A 1 112 ? 12.030  -2.644  -30.405 1.00 16.78 ?  112 LEU   A CB   1 
ATOM   948  C CG   . LEU   A 1 112 ? 13.378  -3.210  -30.857 1.00 19.53 ?  112 LEU   A CG   1 
ATOM   949  C CD1  . LEU   A 1 112 ? 13.799  -2.535  -32.160 1.00 24.74 ?  112 LEU   A CD1  1 
ATOM   950  C CD2  . LEU   A 1 112 ? 14.456  -3.050  -29.804 1.00 21.28 ?  112 LEU   A CD2  1 
ATOM   951  N N    . SER   A 1 113 ? 9.099   -2.914  -29.209 1.00 18.06 ?  113 SER   A N    1 
ATOM   952  C CA   . SER   A 1 113 ? 7.792   -2.257  -29.135 1.00 20.21 ?  113 SER   A CA   1 
ATOM   953  C C    . SER   A 1 113 ? 7.356   -1.989  -27.704 1.00 29.60 ?  113 SER   A C    1 
ATOM   954  O O    . SER   A 1 113 ? 6.665   -0.995  -27.434 1.00 31.38 ?  113 SER   A O    1 
ATOM   955  C CB   . SER   A 1 113 ? 6.741   -3.122  -29.821 1.00 21.70 ?  113 SER   A CB   1 
ATOM   956  O OG   . SER   A 1 113 ? 5.434   -2.688  -29.460 1.00 29.41 ?  113 SER   A OG   1 
ATOM   957  N N    . ALA   A 1 114 ? 7.699   -2.869  -26.794 1.00 20.73 ?  114 ALA   A N    1 
ATOM   958  C CA   . ALA   A 1 114 ? 7.196   -2.782  -25.439 1.00 23.81 ?  114 ALA   A CA   1 
ATOM   959  C C    . ALA   A 1 114 ? 8.202   -3.479  -24.536 1.00 27.26 ?  114 ALA   A C    1 
ATOM   960  O O    . ALA   A 1 114 ? 8.006   -4.643  -24.171 1.00 24.84 ?  114 ALA   A O    1 
ATOM   961  C CB   . ALA   A 1 114 ? 5.811   -3.424  -25.321 1.00 35.89 ?  114 ALA   A CB   1 
ATOM   962  N N    . PRO   A 1 115 ? 9.299   -2.804  -24.189 1.00 26.34 ?  115 PRO   A N    1 
ATOM   963  C CA   . PRO   A 1 115 ? 10.349  -3.449  -23.397 1.00 25.61 ?  115 PRO   A CA   1 
ATOM   964  C C    . PRO   A 1 115 ? 9.841   -3.868  -22.021 1.00 32.48 ?  115 PRO   A C    1 
ATOM   965  O O    . PRO   A 1 115 ? 9.052   -3.164  -21.381 1.00 33.62 ?  115 PRO   A O    1 
ATOM   966  C CB   . PRO   A 1 115 ? 11.429  -2.361  -23.280 1.00 31.70 ?  115 PRO   A CB   1 
ATOM   967  C CG   . PRO   A 1 115 ? 11.123  -1.375  -24.362 1.00 29.39 ?  115 PRO   A CG   1 
ATOM   968  C CD   . PRO   A 1 115 ? 9.618   -1.409  -24.523 1.00 25.59 ?  115 PRO   A CD   1 
ATOM   969  N N    . ASN   A 1 116 ? 10.319  -5.022  -21.571 1.00 25.73 ?  116 ASN   A N    1 
ATOM   970  C CA   . ASN   A 1 116 ? 10.033  -5.564  -20.241 1.00 35.11 ?  116 ASN   A CA   1 
ATOM   971  C C    . ASN   A 1 116 ? 11.331  -5.730  -19.455 1.00 35.68 ?  116 ASN   A C    1 
ATOM   972  O O    . ASN   A 1 116 ? 12.124  -6.642  -19.763 1.00 39.90 ?  116 ASN   A O    1 
ATOM   973  C CB   . ASN   A 1 116 ? 9.309   -6.904  -20.361 1.00 36.42 ?  116 ASN   A CB   1 
ATOM   974  C CG   . ASN   A 1 116 ? 8.548   -7.259  -19.111 1.00 38.78 ?  116 ASN   A CG   1 
ATOM   975  O OD1  . ASN   A 1 116 ? 8.940   -6.880  -18.000 1.00 42.39 ?  116 ASN   A OD1  1 
ATOM   976  N ND2  . ASN   A 1 116 ? 7.449   -7.985  -19.277 1.00 49.79 ?  116 ASN   A ND2  1 
ATOM   977  N N    . PRO   A 1 117 ? 11.595  -4.901  -18.441 1.00 28.98 ?  117 PRO   A N    1 
ATOM   978  C CA   . PRO   A 1 117 ? 12.932  -4.851  -17.827 1.00 40.63 ?  117 PRO   A CA   1 
ATOM   979  C C    . PRO   A 1 117 ? 13.253  -5.940  -16.808 1.00 49.83 ?  117 PRO   A C    1 
ATOM   980  O O    . PRO   A 1 117 ? 14.309  -5.862  -16.175 1.00 40.10 ?  117 PRO   A O    1 
ATOM   981  C CB   . PRO   A 1 117 ? 12.933  -3.470  -17.150 1.00 36.43 ?  117 PRO   A CB   1 
ATOM   982  C CG   . PRO   A 1 117 ? 11.510  -3.219  -16.808 1.00 32.69 ?  117 PRO   A CG   1 
ATOM   983  C CD   . PRO   A 1 117 ? 10.718  -3.818  -17.956 1.00 32.81 ?  117 PRO   A CD   1 
ATOM   984  N N    . ASP   A 1 118 ? 12.440  -6.973  -16.610 1.00 52.85 ?  118 ASP   A N    1 
ATOM   985  C CA   . ASP   A 1 118 ? 12.770  -7.997  -15.619 1.00 46.68 ?  118 ASP   A CA   1 
ATOM   986  C C    . ASP   A 1 118 ? 13.644  -9.087  -16.231 1.00 57.73 ?  118 ASP   A C    1 
ATOM   987  O O    . ASP   A 1 118 ? 13.348  -9.597  -17.317 1.00 60.36 ?  118 ASP   A O    1 
ATOM   988  C CB   . ASP   A 1 118 ? 11.496  -8.587  -15.025 1.00 53.01 ?  118 ASP   A CB   1 
ATOM   989  C CG   . ASP   A 1 118 ? 10.535  -7.515  -14.566 1.00 59.57 ?  118 ASP   A CG   1 
ATOM   990  O OD1  . ASP   A 1 118 ? 10.802  -6.888  -13.516 1.00 55.88 ?  118 ASP   A OD1  1 
ATOM   991  O OD2  . ASP   A 1 118 ? 9.529   -7.278  -15.269 1.00 68.32 -1 118 ASP   A OD2  1 
ATOM   992  N N    . ASP   A 1 119 ? 14.721  -9.437  -15.524 1.00 65.07 ?  119 ASP   A N    1 
ATOM   993  C CA   . ASP   A 1 119 ? 15.709  -10.413 -15.995 1.00 60.33 ?  119 ASP   A CA   1 
ATOM   994  C C    . ASP   A 1 119 ? 15.931  -11.541 -14.986 1.00 59.54 ?  119 ASP   A C    1 
ATOM   995  O O    . ASP   A 1 119 ? 17.071  -11.828 -14.604 1.00 53.63 ?  119 ASP   A O    1 
ATOM   996  C CB   . ASP   A 1 119 ? 17.050  -9.731  -16.285 1.00 37.33 ?  119 ASP   A CB   1 
ATOM   997  C CG   . ASP   A 1 119 ? 17.062  -8.987  -17.605 1.00 59.10 ?  119 ASP   A CG   1 
ATOM   998  O OD1  . ASP   A 1 119 ? 16.482  -9.492  -18.594 1.00 58.39 -1 119 ASP   A OD1  1 
ATOM   999  O OD2  . ASP   A 1 119 ? 17.664  -7.892  -17.654 1.00 50.56 ?  119 ASP   A OD2  1 
ATOM   1000 N N    . ALA   A 1 122 ? 19.810  -8.970  -15.710 1.00 50.21 ?  122 ALA   A N    1 
ATOM   1001 C CA   . ALA   A 1 122 ? 19.874  -7.883  -14.738 1.00 42.71 ?  122 ALA   A CA   1 
ATOM   1002 C C    . ALA   A 1 122 ? 21.087  -6.999  -15.025 1.00 40.08 ?  122 ALA   A C    1 
ATOM   1003 O O    . ALA   A 1 122 ? 22.228  -7.474  -15.049 1.00 39.46 ?  122 ALA   A O    1 
ATOM   1004 C CB   . ALA   A 1 122 ? 19.923  -8.432  -13.321 1.00 45.34 ?  122 ALA   A CB   1 
ATOM   1005 N N    . ASN   A 1 123 ? 20.837  -5.709  -15.240 1.00 27.08 ?  123 ASN   A N    1 
ATOM   1006 C CA   . ASN   A 1 123 ? 21.857  -4.809  -15.762 1.00 29.84 ?  123 ASN   A CA   1 
ATOM   1007 C C    . ASN   A 1 123 ? 21.405  -3.379  -15.513 1.00 21.77 ?  123 ASN   A C    1 
ATOM   1008 O O    . ASN   A 1 123 ? 20.253  -3.136  -15.143 1.00 24.62 ?  123 ASN   A O    1 
ATOM   1009 C CB   . ASN   A 1 123 ? 22.082  -5.046  -17.257 1.00 27.41 ?  123 ASN   A CB   1 
ATOM   1010 C CG   . ASN   A 1 123 ? 20.835  -4.788  -18.067 1.00 28.10 ?  123 ASN   A CG   1 
ATOM   1011 O OD1  . ASN   A 1 123 ? 20.442  -3.647  -18.247 1.00 24.55 ?  123 ASN   A OD1  1 
ATOM   1012 N ND2  . ASN   A 1 123 ? 20.210  -5.843  -18.556 1.00 23.38 ?  123 ASN   A ND2  1 
ATOM   1013 N N    . ASP   A 1 124 ? 22.319  -2.426  -15.759 1.00 22.17 ?  124 ASP   A N    1 
ATOM   1014 C CA   . ASP   A 1 124 ? 22.047  -1.032  -15.400 1.00 24.98 ?  124 ASP   A CA   1 
ATOM   1015 C C    . ASP   A 1 124 ? 20.838  -0.480  -16.146 1.00 24.48 ?  124 ASP   A C    1 
ATOM   1016 O O    . ASP   A 1 124 ? 20.057  0.302   -15.590 1.00 25.22 ?  124 ASP   A O    1 
ATOM   1017 C CB   . ASP   A 1 124 ? 23.262  -0.148  -15.688 1.00 23.41 ?  124 ASP   A CB   1 
ATOM   1018 C CG   . ASP   A 1 124 ? 24.402  -0.339  -14.688 1.00 36.22 ?  124 ASP   A CG   1 
ATOM   1019 O OD1  . ASP   A 1 124 ? 24.257  -1.106  -13.712 1.00 38.09 ?  124 ASP   A OD1  1 
ATOM   1020 O OD2  . ASP   A 1 124 ? 25.453  0.304   -14.883 1.00 46.64 -1 124 ASP   A OD2  1 
ATOM   1021 N N    . VAL   A 1 125 ? 20.682  -0.844  -17.422 1.00 24.20 ?  125 VAL   A N    1 
ATOM   1022 C CA   . VAL   A 1 125 ? 19.576  -0.278  -18.190 1.00 20.70 ?  125 VAL   A CA   1 
ATOM   1023 C C    . VAL   A 1 125 ? 18.246  -0.857  -17.722 1.00 19.73 ?  125 VAL   A C    1 
ATOM   1024 O O    . VAL   A 1 125 ? 17.253  -0.134  -17.600 1.00 19.49 ?  125 VAL   A O    1 
ATOM   1025 C CB   . VAL   A 1 125 ? 19.790  -0.492  -19.700 1.00 21.89 ?  125 VAL   A CB   1 
ATOM   1026 C CG1  . VAL   A 1 125 ? 18.586  0.060   -20.495 1.00 20.03 ?  125 VAL   A CG1  1 
ATOM   1027 C CG2  . VAL   A 1 125 ? 21.112  0.154   -20.139 1.00 20.18 ?  125 VAL   A CG2  1 
ATOM   1028 N N    . ALA   A 1 126 ? 18.195  -2.169  -17.477 1.00 21.72 ?  126 ALA   A N    1 
ATOM   1029 C CA   . ALA   A 1 126 ? 16.979  -2.765  -16.937 1.00 22.46 ?  126 ALA   A CA   1 
ATOM   1030 C C    . ALA   A 1 126 ? 16.609  -2.136  -15.600 1.00 26.30 ?  126 ALA   A C    1 
ATOM   1031 O O    . ALA   A 1 126 ? 15.431  -1.861  -15.333 1.00 22.02 ?  126 ALA   A O    1 
ATOM   1032 C CB   . ALA   A 1 126 ? 17.163  -4.274  -16.783 1.00 26.81 ?  126 ALA   A CB   1 
ATOM   1033 N N    . GLU   A 1 127 ? 17.606  -1.901  -14.744 1.00 26.38 ?  127 GLU   A N    1 
ATOM   1034 C CA   . GLU   A 1 127 ? 17.336  -1.272  -13.450 1.00 26.53 ?  127 GLU   A CA   1 
ATOM   1035 C C    . GLU   A 1 127 ? 16.753  0.128   -13.630 1.00 23.77 ?  127 GLU   A C    1 
ATOM   1036 O O    . GLU   A 1 127 ? 15.775  0.502   -12.966 1.00 23.46 ?  127 GLU   A O    1 
ATOM   1037 C CB   . GLU   A 1 127 ? 18.618  -1.222  -12.612 1.00 28.96 ?  127 GLU   A CB   1 
ATOM   1038 C CG   . GLU   A 1 127 ? 19.030  -2.541  -11.958 1.00 31.55 ?  127 GLU   A CG   1 
ATOM   1039 C CD   . GLU   A 1 127 ? 17.895  -3.196  -11.167 1.00 36.34 ?  127 GLU   A CD   1 
ATOM   1040 O OE1  . GLU   A 1 127 ? 17.276  -2.511  -10.325 1.00 39.26 ?  127 GLU   A OE1  1 
ATOM   1041 O OE2  . GLU   A 1 127 ? 17.628  -4.396  -11.390 1.00 43.51 -1 127 GLU   A OE2  1 
ATOM   1042 N N    . GLN   A 1 128 ? 17.351  0.926   -14.523 1.00 24.24 ?  128 GLN   A N    1 
ATOM   1043 C CA   . GLN   A 1 128 ? 16.804  2.253   -14.797 1.00 25.21 ?  128 GLN   A CA   1 
ATOM   1044 C C    . GLN   A 1 128 ? 15.373  2.174   -15.310 1.00 24.79 ?  128 GLN   A C    1 
ATOM   1045 O O    . GLN   A 1 128 ? 14.521  2.993   -14.941 1.00 23.47 ?  128 GLN   A O    1 
ATOM   1046 C CB   . GLN   A 1 128 ? 17.693  2.992   -15.808 1.00 20.67 ?  128 GLN   A CB   1 
ATOM   1047 C CG   . GLN   A 1 128 ? 17.654  4.486   -15.641 1.00 26.66 ?  128 GLN   A CG   1 
ATOM   1048 C CD   . GLN   A 1 128 ? 18.257  5.234   -16.806 1.00 34.80 ?  128 GLN   A CD   1 
ATOM   1049 O OE1  . GLN   A 1 128 ? 18.276  4.752   -17.944 1.00 24.84 ?  128 GLN   A OE1  1 
ATOM   1050 N NE2  . GLN   A 1 128 ? 18.804  6.405   -16.518 1.00 38.07 ?  128 GLN   A NE2  1 
ATOM   1051 N N    . TRP   A 1 129 ? 15.096  1.211   -16.189 1.00 21.33 ?  129 TRP   A N    1 
ATOM   1052 C CA   . TRP   A 1 129 ? 13.755  1.091   -16.745 1.00 23.97 ?  129 TRP   A CA   1 
ATOM   1053 C C    . TRP   A 1 129 ? 12.750  0.762   -15.653 1.00 26.28 ?  129 TRP   A C    1 
ATOM   1054 O O    . TRP   A 1 129 ? 11.602  1.215   -15.708 1.00 26.83 ?  129 TRP   A O    1 
ATOM   1055 C CB   . TRP   A 1 129 ? 13.729  0.018   -17.848 1.00 29.00 ?  129 TRP   A CB   1 
ATOM   1056 C CG   . TRP   A 1 129 ? 12.888  0.385   -19.054 1.00 27.11 ?  129 TRP   A CG   1 
ATOM   1057 C CD1  . TRP   A 1 129 ? 11.520  0.364   -19.142 1.00 29.06 ?  129 TRP   A CD1  1 
ATOM   1058 C CD2  . TRP   A 1 129 ? 13.363  0.826   -20.341 1.00 27.61 ?  129 TRP   A CD2  1 
ATOM   1059 N NE1  . TRP   A 1 129 ? 11.116  0.765   -20.402 1.00 25.65 ?  129 TRP   A NE1  1 
ATOM   1060 C CE2  . TRP   A 1 129 ? 12.227  1.059   -21.152 1.00 31.92 ?  129 TRP   A CE2  1 
ATOM   1061 C CE3  . TRP   A 1 129 ? 14.638  1.055   -20.882 1.00 29.64 ?  129 TRP   A CE3  1 
ATOM   1062 C CZ2  . TRP   A 1 129 ? 12.329  1.507   -22.475 1.00 30.08 ?  129 TRP   A CZ2  1 
ATOM   1063 C CZ3  . TRP   A 1 129 ? 14.735  1.495   -22.202 1.00 23.36 ?  129 TRP   A CZ3  1 
ATOM   1064 C CH2  . TRP   A 1 129 ? 13.588  1.719   -22.975 1.00 25.30 ?  129 TRP   A CH2  1 
ATOM   1065 N N    . LYS   A 1 130 ? 13.176  -0.021  -14.654 1.00 27.77 ?  130 LYS   A N    1 
ATOM   1066 C CA   . LYS   A 1 130 ? 12.276  -0.403  -13.567 1.00 28.59 ?  130 LYS   A CA   1 
ATOM   1067 C C    . LYS   A 1 130 ? 12.012  0.768   -12.628 1.00 29.35 ?  130 LYS   A C    1 
ATOM   1068 O O    . LYS   A 1 130 ? 10.855  1.083   -12.318 1.00 28.53 ?  130 LYS   A O    1 
ATOM   1069 C CB   . LYS   A 1 130 ? 12.872  -1.582  -12.800 1.00 28.20 ?  130 LYS   A CB   1 
ATOM   1070 C CG   . LYS   A 1 130 ? 13.150  -2.801  -13.654 1.00 31.70 ?  130 LYS   A CG   1 
ATOM   1071 C CD   . LYS   A 1 130 ? 12.876  -4.089  -12.904 1.00 42.27 ?  130 LYS   A CD   1 
ATOM   1072 C CE   . LYS   A 1 130 ? 13.943  -4.309  -11.833 1.00 46.49 ?  130 LYS   A CE   1 
ATOM   1073 N NZ   . LYS   A 1 130 ? 14.614  -5.637  -11.923 1.00 43.26 ?  130 LYS   A NZ   1 
ATOM   1074 N N    . THR   A 1 131 ? 13.069  1.434   -12.163 1.00 29.31 ?  131 THR   A N    1 
ATOM   1075 C CA   . THR   A 1 131 ? 12.893  2.414   -11.101 1.00 32.06 ?  131 THR   A CA   1 
ATOM   1076 C C    . THR   A 1 131 ? 12.972  3.860   -11.572 1.00 34.79 ?  131 THR   A C    1 
ATOM   1077 O O    . THR   A 1 131 ? 12.673  4.762   -10.786 1.00 33.63 ?  131 THR   A O    1 
ATOM   1078 C CB   . THR   A 1 131 ? 13.922  2.173   -9.979  1.00 24.63 ?  131 THR   A CB   1 
ATOM   1079 O OG1  . THR   A 1 131 ? 15.241  2.414   -10.473 1.00 37.76 ?  131 THR   A OG1  1 
ATOM   1080 C CG2  . THR   A 1 131 ? 13.861  0.728   -9.543  1.00 23.62 ?  131 THR   A CG2  1 
ATOM   1081 N N    . ASN   A 1 132 ? 13.358  4.114   -12.818 1.00 29.00 ?  132 ASN   A N    1 
ATOM   1082 C CA   . ASN   A 1 132 ? 13.396  5.480   -13.330 1.00 29.42 ?  132 ASN   A CA   1 
ATOM   1083 C C    . ASN   A 1 132 ? 13.009  5.449   -14.808 1.00 30.18 ?  132 ASN   A C    1 
ATOM   1084 O O    . ASN   A 1 132 ? 13.778  5.834   -15.690 1.00 29.48 ?  132 ASN   A O    1 
ATOM   1085 C CB   . ASN   A 1 132 ? 14.772  6.102   -13.104 1.00 28.42 ?  132 ASN   A CB   1 
ATOM   1086 C CG   . ASN   A 1 132 ? 14.774  7.605   -13.319 1.00 37.55 ?  132 ASN   A CG   1 
ATOM   1087 O OD1  . ASN   A 1 132 ? 13.721  8.228   -13.471 1.00 38.04 ?  132 ASN   A OD1  1 
ATOM   1088 N ND2  . ASN   A 1 132 ? 15.964  8.195   -13.329 1.00 38.15 ?  132 ASN   A ND2  1 
ATOM   1089 N N    . GLU   A 1 133 ? 11.779  5.000   -15.073 1.00 29.67 ?  133 GLU   A N    1 
ATOM   1090 C CA   . GLU   A 1 133 ? 11.361  4.720   -16.442 1.00 25.98 ?  133 GLU   A CA   1 
ATOM   1091 C C    . GLU   A 1 133 ? 11.414  5.971   -17.309 1.00 33.03 ?  133 GLU   A C    1 
ATOM   1092 O O    . GLU   A 1 133 ? 11.826  5.904   -18.471 1.00 25.19 ?  133 GLU   A O    1 
ATOM   1093 C CB   . GLU   A 1 133 ? 9.955   4.117   -16.447 1.00 27.52 ?  133 GLU   A CB   1 
ATOM   1094 C CG   . GLU   A 1 133 ? 9.348   3.909   -17.839 1.00 32.27 ?  133 GLU   A CG   1 
ATOM   1095 C CD   . GLU   A 1 133 ? 8.063   3.090   -17.799 1.00 40.27 ?  133 GLU   A CD   1 
ATOM   1096 O OE1  . GLU   A 1 133 ? 7.513   2.910   -16.693 1.00 42.77 ?  133 GLU   A OE1  1 
ATOM   1097 O OE2  . GLU   A 1 133 ? 7.603   2.620   -18.866 1.00 44.39 -1 133 GLU   A OE2  1 
ATOM   1098 N N    . ALA   A 1 134 ? 10.993  7.120   -16.770 1.00 33.55 ?  134 ALA   A N    1 
ATOM   1099 C CA   . ALA   A 1 134 ? 10.947  8.337   -17.576 1.00 29.05 ?  134 ALA   A CA   1 
ATOM   1100 C C    . ALA   A 1 134 ? 12.311  8.657   -18.174 1.00 27.85 ?  134 ALA   A C    1 
ATOM   1101 O O    . ALA   A 1 134 ? 12.421  8.978   -19.368 1.00 29.33 ?  134 ALA   A O    1 
ATOM   1102 C CB   . ALA   A 1 134 ? 10.440  9.503   -16.728 1.00 41.81 ?  134 ALA   A CB   1 
ATOM   1103 N N    . GLN   A 1 135 ? 13.364  8.552   -17.360 1.00 28.20 ?  135 GLN   A N    1 
ATOM   1104 C CA   . GLN   A 1 135 ? 14.714  8.833   -17.833 1.00 28.76 ?  135 GLN   A CA   1 
ATOM   1105 C C    . GLN   A 1 135 ? 15.180  7.781   -18.833 1.00 29.28 ?  135 GLN   A C    1 
ATOM   1106 O O    . GLN   A 1 135 ? 15.852  8.112   -19.818 1.00 26.25 ?  135 GLN   A O    1 
ATOM   1107 C CB   . GLN   A 1 135 ? 15.679  8.911   -16.647 1.00 30.08 ?  135 GLN   A CB   1 
ATOM   1108 C CG   . GLN   A 1 135 ? 17.122  9.269   -16.984 1.00 31.43 ?  135 GLN   A CG   1 
ATOM   1109 C CD   . GLN   A 1 135 ? 17.281  10.334  -18.075 1.00 48.32 ?  135 GLN   A CD   1 
ATOM   1110 O OE1  . GLN   A 1 135 ? 16.313  10.772  -18.703 1.00 54.59 ?  135 GLN   A OE1  1 
ATOM   1111 N NE2  . GLN   A 1 135 ? 18.524  10.726  -18.324 1.00 53.87 ?  135 GLN   A NE2  1 
ATOM   1112 N N    . ALA   A 1 136 ? 14.854  6.508   -18.587 1.00 23.81 ?  136 ALA   A N    1 
ATOM   1113 C CA   . ALA   A 1 136 ? 15.249  5.464   -19.529 1.00 23.05 ?  136 ALA   A CA   1 
ATOM   1114 C C    . ALA   A 1 136 ? 14.613  5.705   -20.887 1.00 17.98 ?  136 ALA   A C    1 
ATOM   1115 O O    . ALA   A 1 136 ? 15.271  5.563   -21.929 1.00 20.01 ?  136 ALA   A O    1 
ATOM   1116 C CB   . ALA   A 1 136 ? 14.864  4.085   -18.984 1.00 20.97 ?  136 ALA   A CB   1 
ATOM   1117 N N    . ILE   A 1 137 ? 13.328  6.057   -20.895 1.00 20.74 ?  137 ILE   A N    1 
ATOM   1118 C CA   . ILE   A 1 137 ? 12.638  6.314   -22.157 1.00 23.23 ?  137 ILE   A CA   1 
ATOM   1119 C C    . ILE   A 1 137 ? 13.241  7.521   -22.863 1.00 24.52 ?  137 ILE   A C    1 
ATOM   1120 O O    . ILE   A 1 137 ? 13.444  7.503   -24.087 1.00 19.03 ?  137 ILE   A O    1 
ATOM   1121 C CB   . ILE   A 1 137 ? 11.126  6.496   -21.919 1.00 23.87 ?  137 ILE   A CB   1 
ATOM   1122 C CG1  . ILE   A 1 137 ? 10.480  5.176   -21.507 1.00 24.26 ?  137 ILE   A CG1  1 
ATOM   1123 C CG2  . ILE   A 1 137 ? 10.452  7.042   -23.182 1.00 24.42 ?  137 ILE   A CG2  1 
ATOM   1124 C CD1  . ILE   A 1 137 ? 9.075   5.340   -20.979 1.00 32.81 ?  137 ILE   A CD1  1 
ATOM   1125 N N    . GLU   A 1 138 ? 13.535  8.596   -22.111 1.00 22.91 ?  138 GLU   A N    1 
ATOM   1126 C CA   . GLU   A 1 138 ? 14.149  9.767   -22.734 1.00 24.83 ?  138 GLU   A CA   1 
ATOM   1127 C C    . GLU   A 1 138 ? 15.506  9.422   -23.342 1.00 20.59 ?  138 GLU   A C    1 
ATOM   1128 O O    . GLU   A 1 138 ? 15.839  9.880   -24.441 1.00 20.44 ?  138 GLU   A O    1 
ATOM   1129 C CB   . GLU   A 1 138 ? 14.307  10.901  -21.715 1.00 30.51 ?  138 GLU   A CB   1 
ATOM   1130 C CG   . GLU   A 1 138 ? 14.501  12.320  -22.316 1.00 34.69 ?  138 GLU   A CG   1 
ATOM   1131 C CD   . GLU   A 1 138 ? 13.886  12.500  -23.703 1.00 32.86 ?  138 GLU   A CD   1 
ATOM   1132 O OE1  . GLU   A 1 138 ? 12.652  12.332  -23.818 1.00 31.18 ?  138 GLU   A OE1  1 
ATOM   1133 O OE2  . GLU   A 1 138 ? 14.612  12.867  -24.662 1.00 33.76 -1 138 GLU   A OE2  1 
ATOM   1134 N N    . THR   A 1 139 ? 16.301  8.600   -22.654 1.00 22.71 ?  139 THR   A N    1 
ATOM   1135 C CA   . THR   A 1 139 ? 17.606  8.228   -23.195 1.00 19.22 ?  139 THR   A CA   1 
ATOM   1136 C C    . THR   A 1 139 ? 17.463  7.367   -24.441 1.00 20.51 ?  139 THR   A C    1 
ATOM   1137 O O    . THR   A 1 139 ? 18.228  7.523   -25.402 1.00 20.11 ?  139 THR   A O    1 
ATOM   1138 C CB   . THR   A 1 139 ? 18.423  7.489   -22.136 1.00 22.54 ?  139 THR   A CB   1 
ATOM   1139 O OG1  . THR   A 1 139 ? 18.524  8.307   -20.958 1.00 27.36 ?  139 THR   A OG1  1 
ATOM   1140 C CG2  . THR   A 1 139 ? 19.806  7.129   -22.660 1.00 19.07 ?  139 THR   A CG2  1 
ATOM   1141 N N    . ALA   A 1 140 ? 16.513  6.424   -24.430 1.00 18.90 ?  140 ALA   A N    1 
ATOM   1142 C CA   . ALA   A 1 140 ? 16.269  5.622   -25.627 1.00 18.28 ?  140 ALA   A CA   1 
ATOM   1143 C C    . ALA   A 1 140 ? 15.837  6.504   -26.796 1.00 18.27 ?  140 ALA   A C    1 
ATOM   1144 O O    . ALA   A 1 140 ? 16.249  6.280   -27.942 1.00 17.79 ?  140 ALA   A O    1 
ATOM   1145 C CB   . ALA   A 1 140 ? 15.202  4.555   -25.343 1.00 16.32 ?  140 ALA   A CB   1 
ATOM   1146 N N    . ARG   A 1 141 ? 14.999  7.511   -26.524 1.00 17.51 ?  141 ARG   A N    1 
ATOM   1147 C CA   . ARG   A 1 141 ? 14.600  8.447   -27.575 1.00 20.30 ?  141 ARG   A CA   1 
ATOM   1148 C C    . ARG   A 1 141 ? 15.795  9.246   -28.080 1.00 19.65 ?  141 ARG   A C    1 
ATOM   1149 O O    . ARG   A 1 141 ? 15.946  9.461   -29.294 1.00 18.01 ?  141 ARG   A O    1 
ATOM   1150 C CB   . ARG   A 1 141 ? 13.523  9.403   -27.064 1.00 18.55 ?  141 ARG   A CB   1 
ATOM   1151 C CG   . ARG   A 1 141 ? 12.166  8.762   -26.961 1.00 20.21 ?  141 ARG   A CG   1 
ATOM   1152 C CD   . ARG   A 1 141 ? 11.124  9.792   -26.560 1.00 29.07 ?  141 ARG   A CD   1 
ATOM   1153 N NE   . ARG   A 1 141 ? 9.848   9.173   -26.230 1.00 31.23 ?  141 ARG   A NE   1 
ATOM   1154 C CZ   . ARG   A 1 141 ? 9.055   9.577   -25.248 1.00 40.74 ?  141 ARG   A CZ   1 
ATOM   1155 N NH1  . ARG   A 1 141 ? 9.398   10.579  -24.453 1.00 37.18 ?  141 ARG   A NH1  1 
ATOM   1156 N NH2  . ARG   A 1 141 ? 7.887   8.965   -25.064 1.00 39.03 ?  141 ARG   A NH2  1 
ATOM   1157 N N    . ALA   A 1 142 ? 16.640  9.717   -27.159 1.00 18.28 ?  142 ALA   A N    1 
ATOM   1158 C CA   . ALA   A 1 142 ? 17.805  10.498  -27.558 1.00 19.65 ?  142 ALA   A CA   1 
ATOM   1159 C C    . ALA   A 1 142 ? 18.721  9.680   -28.452 1.00 21.60 ?  142 ALA   A C    1 
ATOM   1160 O O    . ALA   A 1 142 ? 19.200  10.168  -29.486 1.00 18.39 ?  142 ALA   A O    1 
ATOM   1161 C CB   . ALA   A 1 142 ? 18.564  11.000  -26.325 1.00 20.12 ?  142 ALA   A CB   1 
ATOM   1162 N N    . TRP   A 1 143 ? 18.981  8.426   -28.066 1.00 16.80 ?  143 TRP   A N    1 
ATOM   1163 C CA   . TRP   A 1 143 ? 19.866  7.582   -28.862 1.00 18.07 ?  143 TRP   A CA   1 
ATOM   1164 C C    . TRP   A 1 143 ? 19.228  7.204   -30.194 1.00 17.74 ?  143 TRP   A C    1 
ATOM   1165 O O    . TRP   A 1 143 ? 19.940  7.013   -31.185 1.00 16.84 ?  143 TRP   A O    1 
ATOM   1166 C CB   . TRP   A 1 143 ? 20.253  6.321   -28.087 1.00 15.59 ?  143 TRP   A CB   1 
ATOM   1167 C CG   . TRP   A 1 143 ? 21.258  6.556   -26.994 1.00 20.22 ?  143 TRP   A CG   1 
ATOM   1168 C CD1  . TRP   A 1 143 ? 21.450  7.714   -26.287 1.00 21.91 ?  143 TRP   A CD1  1 
ATOM   1169 C CD2  . TRP   A 1 143 ? 22.176  5.601   -26.460 1.00 19.64 ?  143 TRP   A CD2  1 
ATOM   1170 N NE1  . TRP   A 1 143 ? 22.455  7.535   -25.359 1.00 24.76 ?  143 TRP   A NE1  1 
ATOM   1171 C CE2  . TRP   A 1 143 ? 22.908  6.245   -25.439 1.00 24.53 ?  143 TRP   A CE2  1 
ATOM   1172 C CE3  . TRP   A 1 143 ? 22.448  4.259   -26.738 1.00 19.33 ?  143 TRP   A CE3  1 
ATOM   1173 C CZ2  . TRP   A 1 143 ? 23.898  5.589   -24.709 1.00 23.27 ?  143 TRP   A CZ2  1 
ATOM   1174 C CZ3  . TRP   A 1 143 ? 23.427  3.614   -26.019 1.00 24.57 ?  143 TRP   A CZ3  1 
ATOM   1175 C CH2  . TRP   A 1 143 ? 24.142  4.280   -25.012 1.00 24.89 ?  143 TRP   A CH2  1 
ATOM   1176 N N    . THR   A 1 144 ? 17.897  7.105   -30.251 1.00 16.28 ?  144 THR   A N    1 
ATOM   1177 C CA   . THR   A 1 144 ? 17.262  6.906   -31.552 1.00 16.16 ?  144 THR   A CA   1 
ATOM   1178 C C    . THR   A 1 144 ? 17.516  8.104   -32.465 1.00 18.43 ?  144 THR   A C    1 
ATOM   1179 O O    . THR   A 1 144 ? 17.910  7.939   -33.628 1.00 16.97 ?  144 THR   A O    1 
ATOM   1180 C CB   . THR   A 1 144 ? 15.765  6.671   -31.381 1.00 15.22 ?  144 THR   A CB   1 
ATOM   1181 O OG1  . THR   A 1 144 ? 15.551  5.491   -30.600 1.00 16.13 ?  144 THR   A OG1  1 
ATOM   1182 C CG2  . THR   A 1 144 ? 15.116  6.477   -32.739 1.00 18.67 ?  144 THR   A CG2  1 
ATOM   1183 N N    . ARG   A 1 145 ? 17.290  9.325   -31.947 1.00 17.71 ?  145 ARG   A N    1 
ATOM   1184 C CA   . ARG   A 1 145 ? 17.605  10.541  -32.709 1.00 23.93 ?  145 ARG   A CA   1 
ATOM   1185 C C    . ARG   A 1 145 ? 19.069  10.583  -33.166 1.00 24.39 ?  145 ARG   A C    1 
ATOM   1186 O O    . ARG   A 1 145 ? 19.373  11.080  -34.265 1.00 23.40 ?  145 ARG   A O    1 
ATOM   1187 C CB   . ARG   A 1 145 ? 17.304  11.792  -31.873 1.00 22.85 ?  145 ARG   A CB   1 
ATOM   1188 C CG   . ARG   A 1 145 ? 15.843  12.066  -31.592 1.00 23.18 ?  145 ARG   A CG   1 
ATOM   1189 C CD   . ARG   A 1 145 ? 15.701  13.193  -30.561 1.00 31.33 ?  145 ARG   A CD   1 
ATOM   1190 N NE   . ARG   A 1 145 ? 14.328  13.328  -30.083 1.00 29.40 ?  145 ARG   A NE   1 
ATOM   1191 C CZ   . ARG   A 1 145 ? 13.971  13.292  -28.806 1.00 33.49 ?  145 ARG   A CZ   1 
ATOM   1192 N NH1  . ARG   A 1 145 ? 14.861  13.109  -27.841 1.00 24.16 ?  145 ARG   A NH1  1 
ATOM   1193 N NH2  . ARG   A 1 145 ? 12.687  13.427  -28.488 1.00 29.29 ?  145 ARG   A NH2  1 
ATOM   1194 N N    . LEU   A 1 146 ? 19.995  10.120  -32.317 1.00 19.19 ?  146 LEU   A N    1 
ATOM   1195 C CA   . LEU   A 1 146 ? 21.425  10.303  -32.575 1.00 20.13 ?  146 LEU   A CA   1 
ATOM   1196 C C    . LEU   A 1 146 ? 21.992  9.245   -33.508 1.00 27.14 ?  146 LEU   A C    1 
ATOM   1197 O O    . LEU   A 1 146 ? 22.885  9.538   -34.304 1.00 24.38 ?  146 LEU   A O    1 
ATOM   1198 C CB   . LEU   A 1 146 ? 22.214  10.273  -31.268 1.00 20.29 ?  146 LEU   A CB   1 
ATOM   1199 C CG   . LEU   A 1 146 ? 22.145  11.447  -30.289 1.00 23.88 ?  146 LEU   A CG   1 
ATOM   1200 C CD1  . LEU   A 1 146 ? 22.694  11.020  -28.949 1.00 22.51 ?  146 LEU   A CD1  1 
ATOM   1201 C CD2  . LEU   A 1 146 ? 22.897  12.676  -30.824 1.00 22.68 ?  146 LEU   A CD2  1 
ATOM   1202 N N    . TYR   A 1 147 ? 21.517  8.005   -33.410 1.00 20.55 ?  147 TYR   A N    1 
ATOM   1203 C CA   . TYR   A 1 147 ? 22.222  6.881   -34.004 1.00 20.00 ?  147 TYR   A CA   1 
ATOM   1204 C C    . TYR   A 1 147 ? 21.385  6.059   -34.961 1.00 20.93 ?  147 TYR   A C    1 
ATOM   1205 O O    . TYR   A 1 147 ? 21.952  5.280   -35.739 1.00 22.31 ?  147 TYR   A O    1 
ATOM   1206 C CB   . TYR   A 1 147 ? 22.765  5.973   -32.894 1.00 19.62 ?  147 TYR   A CB   1 
ATOM   1207 C CG   . TYR   A 1 147 ? 23.588  6.732   -31.876 1.00 21.43 ?  147 TYR   A CG   1 
ATOM   1208 C CD1  . TYR   A 1 147 ? 24.793  7.326   -32.240 1.00 21.33 ?  147 TYR   A CD1  1 
ATOM   1209 C CD2  . TYR   A 1 147 ? 23.128  6.924   -30.577 1.00 21.17 ?  147 TYR   A CD2  1 
ATOM   1210 C CE1  . TYR   A 1 147 ? 25.550  8.035   -31.326 1.00 25.71 ?  147 TYR   A CE1  1 
ATOM   1211 C CE2  . TYR   A 1 147 ? 23.895  7.651   -29.640 1.00 23.34 ?  147 TYR   A CE2  1 
ATOM   1212 C CZ   . TYR   A 1 147 ? 25.101  8.188   -30.029 1.00 30.08 ?  147 TYR   A CZ   1 
ATOM   1213 O OH   . TYR   A 1 147 ? 25.857  8.901   -29.123 1.00 29.15 ?  147 TYR   A OH   1 
ATOM   1214 N N    . ALA   A 1 148 ? 20.064  6.214   -34.948 1.00 17.27 ?  148 ALA   A N    1 
ATOM   1215 C CA   . ALA   A 1 148 ? 19.186  5.374   -35.738 1.00 18.16 ?  148 ALA   A CA   1 
ATOM   1216 C C    . ALA   A 1 148 ? 18.485  6.156   -36.834 1.00 21.39 ?  148 ALA   A C    1 
ATOM   1217 O O    . ALA   A 1 148 ? 17.499  5.678   -37.381 1.00 18.77 ?  148 ALA   A O    1 
ATOM   1218 C CB   . ALA   A 1 148 ? 18.157  4.683   -34.833 1.00 15.68 ?  148 ALA   A CB   1 
ATOM   1219 N N    . MET   A 1 149 ? 18.980  7.353   -37.178 1.00 24.20 ?  149 MET   A N    1 
ATOM   1220 C CA   . MET   A 1 149 ? 18.322  8.161   -38.197 1.00 27.50 ?  149 MET   A CA   1 
ATOM   1221 C C    . MET   A 1 149 ? 19.140  8.358   -39.465 1.00 36.82 ?  149 MET   A C    1 
ATOM   1222 O O    . MET   A 1 149 ? 18.568  8.767   -40.480 1.00 43.78 ?  149 MET   A O    1 
ATOM   1223 C CB   . MET   A 1 149 ? 17.954  9.552   -37.649 1.00 33.00 ?  149 MET   A CB   1 
ATOM   1224 C CG   . MET   A 1 149 ? 17.061  9.568   -36.421 1.00 29.10 ?  149 MET   A CG   1 
ATOM   1225 S SD   . MET   A 1 149 ? 15.359  9.090   -36.713 1.00 44.98 ?  149 MET   A SD   1 
ATOM   1226 C CE   . MET   A 1 149 ? 14.623  9.502   -35.128 1.00 34.69 ?  149 MET   A CE   1 
ATOM   1227 N N    . ASN   A 1 150 ? 20.444  8.099   -39.438 1.00 38.76 ?  150 ASN   A N    1 
ATOM   1228 C CA   . ASN   A 1 150 ? 21.281  8.340   -40.613 1.00 43.84 ?  150 ASN   A CA   1 
ATOM   1229 C C    . ASN   A 1 150 ? 22.202  7.156   -40.902 1.00 42.18 ?  150 ASN   A C    1 
ATOM   1230 O O    . ASN   A 1 150 ? 21.758  6.005   -40.941 1.00 44.78 ?  150 ASN   A O    1 
ATOM   1231 C CB   . ASN   A 1 150 ? 22.106  9.622   -40.426 1.00 39.43 ?  150 ASN   A CB   1 
ATOM   1232 C CG   . ASN   A 1 150 ? 21.236  10.877  -40.355 1.00 41.73 ?  150 ASN   A CG   1 
ATOM   1233 O OD1  . ASN   A 1 150 ? 21.129  11.520  -39.307 1.00 40.14 ?  150 ASN   A OD1  1 
ATOM   1234 N ND2  . ASN   A 1 150 ? 20.599  11.219  -41.472 1.00 38.00 ?  150 ASN   A ND2  1 
ATOM   1235 N N    . GLY   B 1 3   ? 8.296   -5.247  13.906  1.00 43.05 ?  3   GLY   B N    1 
ATOM   1236 C CA   . GLY   B 1 3   ? 9.334   -4.424  14.508  1.00 48.84 ?  3   GLY   B CA   1 
ATOM   1237 C C    . GLY   B 1 3   ? 10.278  -3.817  13.482  1.00 39.65 ?  3   GLY   B C    1 
ATOM   1238 O O    . GLY   B 1 3   ? 10.214  -4.154  12.297  1.00 49.04 ?  3   GLY   B O    1 
ATOM   1239 N N    . LEU   B 1 4   ? 11.166  -2.911  13.938  1.00 42.18 ?  4   LEU   B N    1 
ATOM   1240 C CA   . LEU   B 1 4   ? 12.102  -2.264  13.024  1.00 33.34 ?  4   LEU   B CA   1 
ATOM   1241 C C    . LEU   B 1 4   ? 13.245  -3.215  12.673  1.00 38.25 ?  4   LEU   B C    1 
ATOM   1242 O O    . LEU   B 1 4   ? 13.789  -3.880  13.557  1.00 39.45 ?  4   LEU   B O    1 
ATOM   1243 C CB   . LEU   B 1 4   ? 12.677  -0.994  13.642  1.00 35.06 ?  4   LEU   B CB   1 
ATOM   1244 C CG   . LEU   B 1 4   ? 12.132  0.357   13.196  1.00 39.91 ?  4   LEU   B CG   1 
ATOM   1245 C CD1  . LEU   B 1 4   ? 13.043  1.464   13.685  1.00 39.70 ?  4   LEU   B CD1  1 
ATOM   1246 C CD2  . LEU   B 1 4   ? 11.998  0.397   11.686  1.00 32.65 ?  4   LEU   B CD2  1 
ATOM   1247 N N    . PRO   B 1 5   ? 13.630  -3.292  11.398  1.00 36.43 ?  5   PRO   B N    1 
ATOM   1248 C CA   . PRO   B 1 5   ? 14.797  -4.104  11.031  1.00 33.43 ?  5   PRO   B CA   1 
ATOM   1249 C C    . PRO   B 1 5   ? 16.046  -3.655  11.774  1.00 32.68 ?  5   PRO   B C    1 
ATOM   1250 O O    . PRO   B 1 5   ? 16.301  -2.459  11.942  1.00 27.82 ?  5   PRO   B O    1 
ATOM   1251 C CB   . PRO   B 1 5   ? 14.933  -3.875  9.522   1.00 34.68 ?  5   PRO   B CB   1 
ATOM   1252 C CG   . PRO   B 1 5   ? 13.605  -3.415  9.072   1.00 35.04 ?  5   PRO   B CG   1 
ATOM   1253 C CD   . PRO   B 1 5   ? 12.932  -2.741  10.225  1.00 36.99 ?  5   PRO   B CD   1 
ATOM   1254 N N    . ARG   B 1 6   ? 16.836  -4.638  12.215  1.00 27.42 ?  6   ARG   B N    1 
ATOM   1255 C CA   . ARG   B 1 6   ? 18.080  -4.343  12.917  1.00 27.69 ?  6   ARG   B CA   1 
ATOM   1256 C C    . ARG   B 1 6   ? 18.943  -3.361  12.132  1.00 24.90 ?  6   ARG   B C    1 
ATOM   1257 O O    . ARG   B 1 6   ? 19.629  -2.514  12.715  1.00 28.36 ?  6   ARG   B O    1 
ATOM   1258 C CB   . ARG   B 1 6   ? 18.843  -5.648  13.174  1.00 31.09 ?  6   ARG   B CB   1 
ATOM   1259 C CG   . ARG   B 1 6   ? 20.271  -5.467  13.686  1.00 45.31 ?  6   ARG   B CG   1 
ATOM   1260 C CD   . ARG   B 1 6   ? 21.304  -6.177  12.802  1.00 50.38 ?  6   ARG   B CD   1 
ATOM   1261 N NE   . ARG   B 1 6   ? 21.471  -5.529  11.503  1.00 58.51 ?  6   ARG   B NE   1 
ATOM   1262 C CZ   . ARG   B 1 6   ? 22.321  -5.927  10.565  1.00 49.22 ?  6   ARG   B CZ   1 
ATOM   1263 N NH1  . ARG   B 1 6   ? 23.073  -7.004  10.726  1.00 51.62 ?  6   ARG   B NH1  1 
ATOM   1264 N NH2  . ARG   B 1 6   ? 22.422  -5.224  9.438   1.00 43.16 ?  6   ARG   B NH2  1 
ATOM   1265 N N    . ARG   B 1 7   ? 18.931  -3.470  10.805  1.00 26.07 ?  7   ARG   B N    1 
ATOM   1266 C CA   . ARG   B 1 7   ? 19.746  -2.580  9.984   1.00 29.59 ?  7   ARG   B CA   1 
ATOM   1267 C C    . ARG   B 1 7   ? 19.402  -1.119  10.241  1.00 20.46 ?  7   ARG   B C    1 
ATOM   1268 O O    . ARG   B 1 7   ? 20.300  -0.271  10.354  1.00 22.99 ?  7   ARG   B O    1 
ATOM   1269 C CB   . ARG   B 1 7   ? 19.562  -2.927  8.511   1.00 25.46 ?  7   ARG   B CB   1 
ATOM   1270 C CG   . ARG   B 1 7   ? 19.825  -1.771  7.573   1.00 31.11 ?  7   ARG   B CG   1 
ATOM   1271 C CD   . ARG   B 1 7   ? 21.140  -1.944  6.868   1.00 28.45 ?  7   ARG   B CD   1 
ATOM   1272 N NE   . ARG   B 1 7   ? 21.450  -0.789  6.034   1.00 28.61 ?  7   ARG   B NE   1 
ATOM   1273 C CZ   . ARG   B 1 7   ? 21.918  -0.866  4.797   1.00 24.90 ?  7   ARG   B CZ   1 
ATOM   1274 N NH1  . ARG   B 1 7   ? 22.198  -2.034  4.235   1.00 27.08 ?  7   ARG   B NH1  1 
ATOM   1275 N NH2  . ARG   B 1 7   ? 22.091  0.252   4.098   1.00 22.37 ?  7   ARG   B NH2  1 
ATOM   1276 N N    . ILE   B 1 8   ? 18.110  -0.804  10.346  1.00 24.79 ?  8   ILE   B N    1 
ATOM   1277 C CA   . ILE   B 1 8   ? 17.728  0.590   10.546  1.00 23.00 ?  8   ILE   B CA   1 
ATOM   1278 C C    . ILE   B 1 8   ? 18.108  1.052   11.948  1.00 21.76 ?  8   ILE   B C    1 
ATOM   1279 O O    . ILE   B 1 8   ? 18.564  2.185   12.145  1.00 20.73 ?  8   ILE   B O    1 
ATOM   1280 C CB   . ILE   B 1 8   ? 16.230  0.774   10.263  1.00 22.22 ?  8   ILE   B CB   1 
ATOM   1281 C CG1  . ILE   B 1 8   ? 15.942  0.502   8.782   1.00 20.59 ?  8   ILE   B CG1  1 
ATOM   1282 C CG2  . ILE   B 1 8   ? 15.787  2.181   10.637  1.00 22.78 ?  8   ILE   B CG2  1 
ATOM   1283 C CD1  . ILE   B 1 8   ? 14.460  0.556   8.401   1.00 23.63 ?  8   ILE   B CD1  1 
ATOM   1284 N N    . ILE   B 1 9   ? 17.917  0.183   12.945  1.00 26.02 ?  9   ILE   B N    1 
ATOM   1285 C CA   . ILE   B 1 9   ? 18.301  0.509   14.316  1.00 25.45 ?  9   ILE   B CA   1 
ATOM   1286 C C    . ILE   B 1 9   ? 19.783  0.855   14.382  1.00 23.49 ?  9   ILE   B C    1 
ATOM   1287 O O    . ILE   B 1 9   ? 20.188  1.866   14.978  1.00 21.46 ?  9   ILE   B O    1 
ATOM   1288 C CB   . ILE   B 1 9   ? 17.956  -0.669  15.248  1.00 29.95 ?  9   ILE   B CB   1 
ATOM   1289 C CG1  . ILE   B 1 9   ? 16.436  -0.804  15.399  1.00 35.51 ?  9   ILE   B CG1  1 
ATOM   1290 C CG2  . ILE   B 1 9   ? 18.619  -0.475  16.594  1.00 29.83 ?  9   ILE   B CG2  1 
ATOM   1291 C CD1  . ILE   B 1 9   ? 16.008  -1.910  16.342  1.00 39.78 ?  9   ILE   B CD1  1 
ATOM   1292 N N    . LYS   B 1 10  ? 20.616  0.026   13.747  1.00 25.81 ?  10  LYS   B N    1 
ATOM   1293 C CA   . LYS   B 1 10  ? 22.058  0.233   13.806  1.00 28.41 ?  10  LYS   B CA   1 
ATOM   1294 C C    . LYS   B 1 10  ? 22.453  1.505   13.063  1.00 23.71 ?  10  LYS   B C    1 
ATOM   1295 O O    . LYS   B 1 10  ? 23.263  2.301   13.554  1.00 24.23 ?  10  LYS   B O    1 
ATOM   1296 C CB   . LYS   B 1 10  ? 22.789  -0.983  13.221  1.00 29.04 ?  10  LYS   B CB   1 
ATOM   1297 C CG   . LYS   B 1 10  ? 22.472  -2.331  13.894  1.00 34.93 ?  10  LYS   B CG   1 
ATOM   1298 C CD   . LYS   B 1 10  ? 21.821  -2.190  15.277  1.00 42.83 ?  10  LYS   B CD   1 
ATOM   1299 C CE   . LYS   B 1 10  ? 22.823  -2.330  16.425  1.00 51.74 ?  10  LYS   B CE   1 
ATOM   1300 N NZ   . LYS   B 1 10  ? 22.197  -2.021  17.750  1.00 48.34 ?  10  LYS   B NZ   1 
ATOM   1301 N N    . GLU   B 1 11  ? 21.883  1.719   11.870  1.00 21.36 ?  11  GLU   B N    1 
ATOM   1302 C CA   . GLU   B 1 11  ? 22.208  2.932   11.132  1.00 20.35 ?  11  GLU   B CA   1 
ATOM   1303 C C    . GLU   B 1 11  ? 21.826  4.170   11.921  1.00 19.37 ?  11  GLU   B C    1 
ATOM   1304 O O    . GLU   B 1 11  ? 22.572  5.148   11.948  1.00 20.10 ?  11  GLU   B O    1 
ATOM   1305 C CB   . GLU   B 1 11  ? 21.501  2.933   9.776   1.00 24.25 ?  11  GLU   B CB   1 
ATOM   1306 C CG   . GLU   B 1 11  ? 22.264  2.257   8.694   1.00 24.76 ?  11  GLU   B CG   1 
ATOM   1307 C CD   . GLU   B 1 11  ? 21.800  2.685   7.315   1.00 21.99 ?  11  GLU   B CD   1 
ATOM   1308 O OE1  . GLU   B 1 11  ? 22.186  3.788   6.863   1.00 19.11 ?  11  GLU   B OE1  1 
ATOM   1309 O OE2  . GLU   B 1 11  ? 21.072  1.897   6.674   1.00 22.78 -1 11  GLU   B OE2  1 
ATOM   1310 N N    . THR   B 1 12  ? 20.643  4.163   12.536  1.00 20.93 ?  12  THR   B N    1 
ATOM   1311 C CA   . THR   B 1 12  ? 20.209  5.322   13.303  1.00 21.85 ?  12  THR   B CA   1 
ATOM   1312 C C    . THR   B 1 12  ? 21.151  5.594   14.468  1.00 19.86 ?  12  THR   B C    1 
ATOM   1313 O O    . THR   B 1 12  ? 21.530  6.749   14.725  1.00 21.09 ?  12  THR   B O    1 
ATOM   1314 C CB   . THR   B 1 12  ? 18.788  5.093   13.811  1.00 19.76 ?  12  THR   B CB   1 
ATOM   1315 O OG1  . THR   B 1 12  ? 17.929  4.826   12.702  1.00 20.80 ?  12  THR   B OG1  1 
ATOM   1316 C CG2  . THR   B 1 12  ? 18.290  6.302   14.563  1.00 17.48 ?  12  THR   B CG2  1 
ATOM   1317 N N    . GLN   B 1 13  ? 21.532  4.539   15.195  1.00 21.35 ?  13  GLN   B N    1 
ATOM   1318 C CA   . GLN   B 1 13  ? 22.461  4.728   16.311  1.00 25.92 ?  13  GLN   B CA   1 
ATOM   1319 C C    . GLN   B 1 13  ? 23.792  5.314   15.846  1.00 22.12 ?  13  GLN   B C    1 
ATOM   1320 O O    . GLN   B 1 13  ? 24.329  6.229   16.485  1.00 22.73 ?  13  GLN   B O    1 
ATOM   1321 C CB   . GLN   B 1 13  ? 22.678  3.404   17.046  1.00 25.40 ?  13  GLN   B CB   1 
ATOM   1322 C CG   . GLN   B 1 13  ? 21.465  2.948   17.828  1.00 30.28 ?  13  GLN   B CG   1 
ATOM   1323 C CD   . GLN   B 1 13  ? 21.607  1.533   18.348  1.00 41.97 ?  13  GLN   B CD   1 
ATOM   1324 O OE1  . GLN   B 1 13  ? 22.432  0.758   17.858  1.00 36.48 ?  13  GLN   B OE1  1 
ATOM   1325 N NE2  . GLN   B 1 13  ? 20.804  1.188   19.351  1.00 39.74 ?  13  GLN   B NE2  1 
ATOM   1326 N N    . ARG   B 1 14  ? 24.335  4.814   14.726  1.00 22.79 ?  14  ARG   B N    1 
ATOM   1327 C CA   . ARG   B 1 14  ? 25.592  5.363   14.208  1.00 26.06 ?  14  ARG   B CA   1 
ATOM   1328 C C    . ARG   B 1 14  ? 25.430  6.809   13.736  1.00 24.74 ?  14  ARG   B C    1 
ATOM   1329 O O    . ARG   B 1 14  ? 26.327  7.638   13.934  1.00 25.89 ?  14  ARG   B O    1 
ATOM   1330 C CB   . ARG   B 1 14  ? 26.129  4.487   13.074  1.00 31.35 ?  14  ARG   B CB   1 
ATOM   1331 C CG   . ARG   B 1 14  ? 26.001  2.987   13.307  1.00 43.03 ?  14  ARG   B CG   1 
ATOM   1332 C CD   . ARG   B 1 14  ? 26.313  2.609   14.748  1.00 51.89 ?  14  ARG   B CD   1 
ATOM   1333 N NE   . ARG   B 1 14  ? 25.617  1.408   15.207  1.00 52.13 ?  14  ARG   B NE   1 
ATOM   1334 C CZ   . ARG   B 1 14  ? 25.960  0.162   14.899  1.00 57.65 ?  14  ARG   B CZ   1 
ATOM   1335 N NH1  . ARG   B 1 14  ? 26.901  -0.096  14.004  1.00 57.83 ?  14  ARG   B NH1  1 
ATOM   1336 N NH2  . ARG   B 1 14  ? 25.340  -0.851  15.503  1.00 59.19 ?  14  ARG   B NH2  1 
ATOM   1337 N N    . LEU   B 1 15  ? 24.300  7.137   13.103  1.00 24.84 ?  15  LEU   B N    1 
ATOM   1338 C CA   . LEU   B 1 15  ? 24.094  8.511   12.652  1.00 20.75 ?  15  LEU   B CA   1 
ATOM   1339 C C    . LEU   B 1 15  ? 24.062  9.479   13.824  1.00 26.44 ?  15  LEU   B C    1 
ATOM   1340 O O    . LEU   B 1 15  ? 24.552  10.612  13.725  1.00 26.40 ?  15  LEU   B O    1 
ATOM   1341 C CB   . LEU   B 1 15  ? 22.793  8.611   11.856  1.00 25.48 ?  15  LEU   B CB   1 
ATOM   1342 C CG   . LEU   B 1 15  ? 22.909  8.232   10.389  1.00 32.29 ?  15  LEU   B CG   1 
ATOM   1343 C CD1  . LEU   B 1 15  ? 21.509  8.117   9.801   1.00 30.98 ?  15  LEU   B CD1  1 
ATOM   1344 C CD2  . LEU   B 1 15  ? 23.770  9.252   9.614   1.00 28.47 ?  15  LEU   B CD2  1 
ATOM   1345 N N    . LEU   B 1 16  ? 23.455  9.069   14.939  1.00 25.16 ?  16  LEU   B N    1 
ATOM   1346 C CA   . LEU   B 1 16  ? 23.404  9.990   16.069  1.00 24.33 ?  16  LEU   B CA   1 
ATOM   1347 C C    . LEU   B 1 16  ? 24.708  9.991   16.868  1.00 22.41 ?  16  LEU   B C    1 
ATOM   1348 O O    . LEU   B 1 16  ? 25.065  11.017  17.460  1.00 29.31 ?  16  LEU   B O    1 
ATOM   1349 C CB   . LEU   B 1 16  ? 22.196  9.670   16.958  1.00 30.34 ?  16  LEU   B CB   1 
ATOM   1350 C CG   . LEU   B 1 16  ? 20.839  9.838   16.245  1.00 32.82 ?  16  LEU   B CG   1 
ATOM   1351 C CD1  . LEU   B 1 16  ? 19.673  9.214   17.030  1.00 30.96 ?  16  LEU   B CD1  1 
ATOM   1352 C CD2  . LEU   B 1 16  ? 20.533  11.315  15.903  1.00 32.82 ?  16  LEU   B CD2  1 
ATOM   1353 N N    . ALA   B 1 17  ? 25.457  8.888   16.847  1.00 21.28 ?  17  ALA   B N    1 
ATOM   1354 C CA   . ALA   B 1 17  ? 26.729  8.833   17.566  1.00 24.65 ?  17  ALA   B CA   1 
ATOM   1355 C C    . ALA   B 1 17  ? 27.828  9.594   16.835  1.00 28.78 ?  17  ALA   B C    1 
ATOM   1356 O O    . ALA   B 1 17  ? 28.732  10.154  17.469  1.00 29.25 ?  17  ALA   B O    1 
ATOM   1357 C CB   . ALA   B 1 17  ? 27.152  7.377   17.773  1.00 21.21 ?  17  ALA   B CB   1 
ATOM   1358 N N    . GLU   B 1 18  ? 27.783  9.593   15.505  1.00 21.74 ?  18  GLU   B N    1 
ATOM   1359 C CA   . GLU   B 1 18  ? 28.820  10.176  14.657  1.00 20.04 ?  18  GLU   B CA   1 
ATOM   1360 C C    . GLU   B 1 18  ? 28.146  11.038  13.611  1.00 23.61 ?  18  GLU   B C    1 
ATOM   1361 O O    . GLU   B 1 18  ? 28.072  10.656  12.437  1.00 26.23 ?  18  GLU   B O    1 
ATOM   1362 C CB   . GLU   B 1 18  ? 29.662  9.100   13.975  1.00 20.38 ?  18  GLU   B CB   1 
ATOM   1363 C CG   . GLU   B 1 18  ? 30.306  8.111   14.934  1.00 41.94 ?  18  GLU   B CG   1 
ATOM   1364 C CD   . GLU   B 1 18  ? 30.986  6.954   14.213  1.00 51.31 ?  18  GLU   B CD   1 
ATOM   1365 O OE1  . GLU   B 1 18  ? 30.392  5.856   14.137  1.00 50.31 ?  18  GLU   B OE1  1 
ATOM   1366 O OE2  . GLU   B 1 18  ? 32.114  7.148   13.719  1.00 55.69 -1 18  GLU   B OE2  1 
ATOM   1367 N N    . PRO   B 1 19  ? 27.652  12.211  13.997  1.00 26.51 ?  19  PRO   B N    1 
ATOM   1368 C CA   . PRO   B 1 19  ? 26.905  13.044  13.047  1.00 26.33 ?  19  PRO   B CA   1 
ATOM   1369 C C    . PRO   B 1 19  ? 27.813  13.593  11.959  1.00 24.98 ?  19  PRO   B C    1 
ATOM   1370 O O    . PRO   B 1 19  ? 29.031  13.702  12.121  1.00 28.62 ?  19  PRO   B O    1 
ATOM   1371 C CB   . PRO   B 1 19  ? 26.339  14.179  13.916  1.00 29.96 ?  19  PRO   B CB   1 
ATOM   1372 C CG   . PRO   B 1 19  ? 26.803  13.909  15.318  1.00 36.63 ?  19  PRO   B CG   1 
ATOM   1373 C CD   . PRO   B 1 19  ? 27.881  12.888  15.283  1.00 33.15 ?  19  PRO   B CD   1 
ATOM   1374 N N    . VAL   B 1 20  ? 27.191  13.912  10.823  1.00 27.10 ?  20  VAL   B N    1 
ATOM   1375 C CA   . VAL   B 1 20  ? 27.862  14.548  9.687   1.00 25.40 ?  20  VAL   B CA   1 
ATOM   1376 C C    . VAL   B 1 20  ? 27.963  16.044  9.967   1.00 27.20 ?  20  VAL   B C    1 
ATOM   1377 O O    . VAL   B 1 20  ? 26.944  16.693  10.233  1.00 20.94 ?  20  VAL   B O    1 
ATOM   1378 C CB   . VAL   B 1 20  ? 27.110  14.297  8.364   1.00 28.35 ?  20  VAL   B CB   1 
ATOM   1379 C CG1  . VAL   B 1 20  ? 27.864  14.923  7.194   1.00 25.77 ?  20  VAL   B CG1  1 
ATOM   1380 C CG2  . VAL   B 1 20  ? 26.839  12.797  8.124   1.00 25.50 ?  20  VAL   B CG2  1 
ATOM   1381 N N    . PRO   B 1 21  ? 29.149  16.633  9.927   1.00 23.01 ?  21  PRO   B N    1 
ATOM   1382 C CA   . PRO   B 1 21  ? 29.268  18.081  10.129  1.00 21.25 ?  21  PRO   B CA   1 
ATOM   1383 C C    . PRO   B 1 21  ? 28.387  18.835  9.138   1.00 19.04 ?  21  PRO   B C    1 
ATOM   1384 O O    . PRO   B 1 21  ? 28.373  18.525  7.947   1.00 20.23 ?  21  PRO   B O    1 
ATOM   1385 C CB   . PRO   B 1 21  ? 30.757  18.355  9.881   1.00 30.16 ?  21  PRO   B CB   1 
ATOM   1386 C CG   . PRO   B 1 21  ? 31.446  17.028  9.919   1.00 28.11 ?  21  PRO   B CG   1 
ATOM   1387 C CD   . PRO   B 1 21  ? 30.444  15.934  9.864   1.00 38.52 ?  21  PRO   B CD   1 
ATOM   1388 N N    . GLY   B 1 22  ? 27.643  19.813  9.651   1.00 18.33 ?  22  GLY   B N    1 
ATOM   1389 C CA   . GLY   B 1 22  ? 26.721  20.624  8.869   1.00 17.78 ?  22  GLY   B CA   1 
ATOM   1390 C C    . GLY   B 1 22  ? 25.366  19.996  8.619   1.00 14.95 ?  22  GLY   B C    1 
ATOM   1391 O O    . GLY   B 1 22  ? 24.539  20.607  7.914   1.00 14.01 ?  22  GLY   B O    1 
ATOM   1392 N N    . ILE   B 1 23  ? 25.110  18.802  9.161   1.00 15.32 ?  23  ILE   B N    1 
ATOM   1393 C CA   . ILE   B 1 23  ? 23.879  18.056  8.906   1.00 12.45 ?  23  ILE   B CA   1 
ATOM   1394 C C    . ILE   B 1 23  ? 23.291  17.568  10.222  1.00 14.82 ?  23  ILE   B C    1 
ATOM   1395 O O    . ILE   B 1 23  ? 23.969  16.877  10.994  1.00 17.72 ?  23  ILE   B O    1 
ATOM   1396 C CB   . ILE   B 1 23  ? 24.132  16.862  7.973   1.00 12.87 ?  23  ILE   B CB   1 
ATOM   1397 C CG1  . ILE   B 1 23  ? 24.832  17.339  6.700   1.00 14.87 ?  23  ILE   B CG1  1 
ATOM   1398 C CG2  . ILE   B 1 23  ? 22.818  16.171  7.648   1.00 16.99 ?  23  ILE   B CG2  1 
ATOM   1399 C CD1  . ILE   B 1 23  ? 24.926  16.255  5.661   1.00 17.68 ?  23  ILE   B CD1  1 
ATOM   1400 N N    . LYS   B 1 24  ? 22.026  17.906  10.470  1.00 12.96 ?  24  LYS   B N    1 
ATOM   1401 C CA   . LYS   B 1 24  ? 21.252  17.346  11.569  1.00 17.72 ?  24  LYS   B CA   1 
ATOM   1402 C C    . LYS   B 1 24  ? 20.244  16.355  10.999  1.00 19.60 ?  24  LYS   B C    1 
ATOM   1403 O O    . LYS   B 1 24  ? 19.544  16.668  10.030  1.00 17.44 ?  24  LYS   B O    1 
ATOM   1404 C CB   . LYS   B 1 24  ? 20.539  18.455  12.351  1.00 19.66 ?  24  LYS   B CB   1 
ATOM   1405 C CG   . LYS   B 1 24  ? 19.886  17.984  13.647  1.00 27.58 ?  24  LYS   B CG   1 
ATOM   1406 C CD   . LYS   B 1 24  ? 19.643  19.146  14.604  1.00 44.33 ?  24  LYS   B CD   1 
ATOM   1407 C CE   . LYS   B 1 24  ? 18.164  19.460  14.741  1.00 44.83 ?  24  LYS   B CE   1 
ATOM   1408 N NZ   . LYS   B 1 24  ? 17.876  20.932  14.686  1.00 47.13 ?  24  LYS   B NZ   1 
ATOM   1409 N N    . ALA   B 1 25  ? 20.178  15.153  11.580  1.00 13.73 ?  25  ALA   B N    1 
ATOM   1410 C CA   . ALA   B 1 25  ? 19.206  14.159  11.125  1.00 15.58 ?  25  ALA   B CA   1 
ATOM   1411 C C    . ALA   B 1 25  ? 18.645  13.435  12.334  1.00 21.52 ?  25  ALA   B C    1 
ATOM   1412 O O    . ALA   B 1 25  ? 19.395  12.747  13.037  1.00 22.45 ?  25  ALA   B O    1 
ATOM   1413 C CB   . ALA   B 1 25  ? 19.851  13.166  10.158  1.00 16.39 ?  25  ALA   B CB   1 
ATOM   1414 N N    . GLU   B 1 26  ? 17.338  13.583  12.561  1.00 18.57 ?  26  GLU   B N    1 
ATOM   1415 C CA   . GLU   B 1 26  ? 16.682  13.092  13.769  1.00 20.00 ?  26  GLU   B CA   1 
ATOM   1416 C C    . GLU   B 1 26  ? 15.474  12.234  13.416  1.00 17.39 ?  26  GLU   B C    1 
ATOM   1417 O O    . GLU   B 1 26  ? 14.551  12.712  12.742  1.00 16.50 ?  26  GLU   B O    1 
ATOM   1418 C CB   . GLU   B 1 26  ? 16.222  14.256  14.656  1.00 21.72 ?  26  GLU   B CB   1 
ATOM   1419 C CG   . GLU   B 1 26  ? 17.326  15.171  15.100  1.00 26.17 ?  26  GLU   B CG   1 
ATOM   1420 C CD   . GLU   B 1 26  ? 16.792  16.441  15.701  1.00 28.47 ?  26  GLU   B CD   1 
ATOM   1421 O OE1  . GLU   B 1 26  ? 15.744  16.941  15.220  1.00 33.97 ?  26  GLU   B OE1  1 
ATOM   1422 O OE2  . GLU   B 1 26  ? 17.424  16.941  16.649  1.00 37.64 -1 26  GLU   B OE2  1 
ATOM   1423 N N    . PRO   B 1 27  ? 15.393  11.003  13.916  1.00 16.55 ?  27  PRO   B N    1 
ATOM   1424 C CA   . PRO   B 1 27  ? 14.191  10.201  13.673  1.00 15.77 ?  27  PRO   B CA   1 
ATOM   1425 C C    . PRO   B 1 27  ? 12.982  10.732  14.431  1.00 18.08 ?  27  PRO   B C    1 
ATOM   1426 O O    . PRO   B 1 27  ? 13.097  11.305  15.516  1.00 17.66 ?  27  PRO   B O    1 
ATOM   1427 C CB   . PRO   B 1 27  ? 14.595  8.810   14.174  1.00 18.27 ?  27  PRO   B CB   1 
ATOM   1428 C CG   . PRO   B 1 27  ? 15.570  9.093   15.245  1.00 19.20 ?  27  PRO   B CG   1 
ATOM   1429 C CD   . PRO   B 1 27  ? 16.377  10.273  14.738  1.00 15.79 ?  27  PRO   B CD   1 
ATOM   1430 N N    . ASP   B 1 28  ? 11.809  10.519  13.846  1.00 15.12 ?  28  ASP   B N    1 
ATOM   1431 C CA   . ASP   B 1 28  ? 10.558  11.022  14.416  1.00 16.19 ?  28  ASP   B CA   1 
ATOM   1432 C C    . ASP   B 1 28  ? 10.047  10.101  15.520  1.00 17.67 ?  28  ASP   B C    1 
ATOM   1433 O O    . ASP   B 1 28  ? 10.013  8.874   15.360  1.00 17.83 ?  28  ASP   B O    1 
ATOM   1434 C CB   . ASP   B 1 28  ? 9.512   11.176  13.314  1.00 14.00 ?  28  ASP   B CB   1 
ATOM   1435 C CG   . ASP   B 1 28  ? 8.260   11.906  13.782  1.00 18.50 ?  28  ASP   B CG   1 
ATOM   1436 O OD1  . ASP   B 1 28  ? 7.341   11.243  14.297  1.00 20.21 ?  28  ASP   B OD1  1 
ATOM   1437 O OD2  . ASP   B 1 28  ? 8.209   13.150  13.636  1.00 18.25 -1 28  ASP   B OD2  1 
ATOM   1438 N N    . GLU   B 1 29  ? 9.623   10.701  16.644  1.00 16.77 ?  29  GLU   B N    1 
ATOM   1439 C CA   . GLU   B 1 29  ? 9.188   9.886   17.775  1.00 20.98 ?  29  GLU   B CA   1 
ATOM   1440 C C    . GLU   B 1 29  ? 8.023   8.966   17.410  1.00 16.89 ?  29  GLU   B C    1 
ATOM   1441 O O    . GLU   B 1 29  ? 7.871   7.893   18.016  1.00 18.29 ?  29  GLU   B O    1 
ATOM   1442 C CB   . GLU   B 1 29  ? 8.816   10.785  18.955  1.00 20.47 ?  29  GLU   B CB   1 
ATOM   1443 C CG   . GLU   B 1 29  ? 7.466   11.432  18.826  1.00 25.25 ?  29  GLU   B CG   1 
ATOM   1444 C CD   . GLU   B 1 29  ? 7.094   12.253  20.059  1.00 19.42 ?  29  GLU   B CD   1 
ATOM   1445 O OE1  . GLU   B 1 29  ? 7.170   11.721  21.187  1.00 26.48 ?  29  GLU   B OE1  1 
ATOM   1446 O OE2  . GLU   B 1 29  ? 6.756   13.434  19.878  1.00 30.28 -1 29  GLU   B OE2  1 
ATOM   1447 N N    . SER   B 1 30  ? 7.190   9.345   16.431  1.00 16.17 ?  30  SER   B N    1 
ATOM   1448 C CA   . SER   B 1 30  ? 6.039   8.531   16.036  1.00 17.80 ?  30  SER   B CA   1 
ATOM   1449 C C    . SER   B 1 30  ? 6.289   7.659   14.810  1.00 17.07 ?  30  SER   B C    1 
ATOM   1450 O O    . SER   B 1 30  ? 5.376   6.937   14.388  1.00 18.98 ?  30  SER   B O    1 
ATOM   1451 C CB   . SER   B 1 30  ? 4.817   9.417   15.765  1.00 19.85 ?  30  SER   B CB   1 
ATOM   1452 O OG   . SER   B 1 30  ? 4.420   10.120  16.935  1.00 24.03 ?  30  SER   B OG   1 
ATOM   1453 N N    . ASN   B 1 31  ? 7.478   7.723   14.201  1.00 15.16 ?  31  ASN   B N    1 
ATOM   1454 C CA   . ASN   B 1 31  ? 7.776   6.819   13.086  1.00 16.37 ?  31  ASN   B CA   1 
ATOM   1455 C C    . ASN   B 1 31  ? 9.290   6.856   12.889  1.00 16.70 ?  31  ASN   B C    1 
ATOM   1456 O O    . ASN   B 1 31  ? 9.809   7.799   12.287  1.00 16.78 ?  31  ASN   B O    1 
ATOM   1457 C CB   . ASN   B 1 31  ? 7.047   7.200   11.803  1.00 19.96 ?  31  ASN   B CB   1 
ATOM   1458 C CG   . ASN   B 1 31  ? 7.188   6.123   10.704  1.00 20.21 ?  31  ASN   B CG   1 
ATOM   1459 O OD1  . ASN   B 1 31  ? 8.154   5.362   10.679  1.00 19.69 ?  31  ASN   B OD1  1 
ATOM   1460 N ND2  . ASN   B 1 31  ? 6.205   6.048   9.815   1.00 24.10 ?  31  ASN   B ND2  1 
ATOM   1461 N N    . ALA   B 1 32  ? 9.968   5.830   13.400  1.00 15.28 ?  32  ALA   B N    1 
ATOM   1462 C CA   . ALA   B 1 32  ? 11.419  5.706   13.330  1.00 19.18 ?  32  ALA   B CA   1 
ATOM   1463 C C    . ALA   B 1 32  ? 11.957  5.603   11.901  1.00 16.99 ?  32  ALA   B C    1 
ATOM   1464 O O    . ALA   B 1 32  ? 13.181  5.704   11.712  1.00 18.60 ?  32  ALA   B O    1 
ATOM   1465 C CB   . ALA   B 1 32  ? 11.850  4.483   14.150  1.00 22.58 ?  32  ALA   B CB   1 
ATOM   1466 N N    . ARG   B 1 33  ? 11.094  5.413   10.899  1.00 18.42 ?  33  ARG   B N    1 
ATOM   1467 C CA   . ARG   B 1 33  ? 11.525  5.419   9.505   1.00 16.48 ?  33  ARG   B CA   1 
ATOM   1468 C C    . ARG   B 1 33  ? 11.601  6.820   8.913   1.00 13.30 ?  33  ARG   B C    1 
ATOM   1469 O O    . ARG   B 1 33  ? 12.128  6.980   7.803   1.00 13.92 ?  33  ARG   B O    1 
ATOM   1470 C CB   . ARG   B 1 33  ? 10.560  4.568   8.664   1.00 15.54 ?  33  ARG   B CB   1 
ATOM   1471 C CG   . ARG   B 1 33  ? 10.623  3.097   8.984   1.00 15.88 ?  33  ARG   B CG   1 
ATOM   1472 C CD   . ARG   B 1 33  ? 9.558   2.356   8.198   1.00 14.08 ?  33  ARG   B CD   1 
ATOM   1473 N NE   . ARG   B 1 33  ? 9.701   0.921   8.411   1.00 22.51 ?  33  ARG   B NE   1 
ATOM   1474 C CZ   . ARG   B 1 33  ? 10.564  0.160   7.752   1.00 25.79 ?  33  ARG   B CZ   1 
ATOM   1475 N NH1  . ARG   B 1 33  ? 11.277  0.638   6.742   1.00 20.77 ?  33  ARG   B NH1  1 
ATOM   1476 N NH2  . ARG   B 1 33  ? 10.711  -1.115  8.109   1.00 27.22 ?  33  ARG   B NH2  1 
ATOM   1477 N N    . TYR   B 1 34  ? 11.108  7.825   9.634   1.00 11.79 ?  34  TYR   B N    1 
ATOM   1478 C CA   . TYR   B 1 34  ? 11.029  9.203   9.164   1.00 14.46 ?  34  TYR   B CA   1 
ATOM   1479 C C    . TYR   B 1 34  ? 12.067  10.047  9.886   1.00 15.30 ?  34  TYR   B C    1 
ATOM   1480 O O    . TYR   B 1 34  ? 12.140  10.026  11.123  1.00 15.94 ?  34  TYR   B O    1 
ATOM   1481 C CB   . TYR   B 1 34  ? 9.637   9.783   9.431   1.00 13.01 ?  34  TYR   B CB   1 
ATOM   1482 C CG   . TYR   B 1 34  ? 9.482   11.221  8.966   1.00 15.81 ?  34  TYR   B CG   1 
ATOM   1483 C CD1  . TYR   B 1 34  ? 9.089   11.513  7.694   1.00 17.39 ?  34  TYR   B CD1  1 
ATOM   1484 C CD2  . TYR   B 1 34  ? 9.803   12.286  9.809   1.00 24.62 ?  34  TYR   B CD2  1 
ATOM   1485 C CE1  . TYR   B 1 34  ? 8.935   12.827  7.267   1.00 16.42 ?  34  TYR   B CE1  1 
ATOM   1486 C CE2  . TYR   B 1 34  ? 9.665   13.603  9.389   1.00 24.04 ?  34  TYR   B CE2  1 
ATOM   1487 C CZ   . TYR   B 1 34  ? 9.213   13.859  8.108   1.00 20.60 ?  34  TYR   B CZ   1 
ATOM   1488 O OH   . TYR   B 1 34  ? 9.060   15.160  7.645   1.00 24.42 ?  34  TYR   B OH   1 
ATOM   1489 N N    . PHE   B 1 35  ? 12.839  10.819  9.126   1.00 11.99 ?  35  PHE   B N    1 
ATOM   1490 C CA   . PHE   B 1 35  ? 13.911  11.632  9.677   1.00 13.17 ?  35  PHE   B CA   1 
ATOM   1491 C C    . PHE   B 1 35  ? 13.694  13.085  9.287   1.00 16.87 ?  35  PHE   B C    1 
ATOM   1492 O O    . PHE   B 1 35  ? 13.490  13.394  8.100   1.00 15.01 ?  35  PHE   B O    1 
ATOM   1493 C CB   . PHE   B 1 35  ? 15.283  11.193  9.149   1.00 15.06 ?  35  PHE   B CB   1 
ATOM   1494 C CG   . PHE   B 1 35  ? 15.770  9.886   9.710   1.00 14.77 ?  35  PHE   B CG   1 
ATOM   1495 C CD1  . PHE   B 1 35  ? 15.252  8.684   9.250   1.00 15.67 ?  35  PHE   B CD1  1 
ATOM   1496 C CD2  . PHE   B 1 35  ? 16.767  9.873   10.680  1.00 18.23 ?  35  PHE   B CD2  1 
ATOM   1497 C CE1  . PHE   B 1 35  ? 15.708  7.473   9.772   1.00 18.40 ?  35  PHE   B CE1  1 
ATOM   1498 C CE2  . PHE   B 1 35  ? 17.218  8.673   11.215  1.00 16.22 ?  35  PHE   B CE2  1 
ATOM   1499 C CZ   . PHE   B 1 35  ? 16.694  7.478   10.757  1.00 17.00 ?  35  PHE   B CZ   1 
ATOM   1500 N N    . HIS   B 1 36  ? 13.750  13.964  10.294  1.00 14.15 ?  36  HIS   B N    1 
ATOM   1501 C CA   . HIS   B 1 36  ? 13.780  15.406  10.069  1.00 11.46 ?  36  HIS   B CA   1 
ATOM   1502 C C    . HIS   B 1 36  ? 15.227  15.819  9.848   1.00 13.12 ?  36  HIS   B C    1 
ATOM   1503 O O    . HIS   B 1 36  ? 16.081  15.557  10.703  1.00 16.33 ?  36  HIS   B O    1 
ATOM   1504 C CB   . HIS   B 1 36  ? 13.207  16.149  11.273  1.00 14.37 ?  36  HIS   B CB   1 
ATOM   1505 C CG   . HIS   B 1 36  ? 11.829  15.720  11.654  1.00 20.56 ?  36  HIS   B CG   1 
ATOM   1506 N ND1  . HIS   B 1 36  ? 10.707  16.369  11.188  1.00 27.91 ?  36  HIS   B ND1  1 
ATOM   1507 C CD2  . HIS   B 1 36  ? 11.387  14.714  12.446  1.00 22.35 ?  36  HIS   B CD2  1 
ATOM   1508 C CE1  . HIS   B 1 36  ? 9.631   15.786  11.686  1.00 32.68 ?  36  HIS   B CE1  1 
ATOM   1509 N NE2  . HIS   B 1 36  ? 10.017  14.785  12.456  1.00 18.95 ?  36  HIS   B NE2  1 
ATOM   1510 N N    . VAL   B 1 37  ? 15.522  16.456  8.712   1.00 10.98 ?  37  VAL   B N    1 
ATOM   1511 C CA   . VAL   B 1 37  ? 16.897  16.738  8.313   1.00 12.31 ?  37  VAL   B CA   1 
ATOM   1512 C C    . VAL   B 1 37  ? 17.087  18.235  8.142   1.00 12.51 ?  37  VAL   B C    1 
ATOM   1513 O O    . VAL   B 1 37  ? 16.211  18.917  7.611   1.00 12.66 ?  37  VAL   B O    1 
ATOM   1514 C CB   . VAL   B 1 37  ? 17.250  16.016  6.999   1.00 11.20 ?  37  VAL   B CB   1 
ATOM   1515 C CG1  . VAL   B 1 37  ? 18.649  16.417  6.510   1.00 10.54 ?  37  VAL   B CG1  1 
ATOM   1516 C CG2  . VAL   B 1 37  ? 17.143  14.487  7.214   1.00 15.74 ?  37  VAL   B CG2  1 
ATOM   1517 N N    . VAL   B 1 38  ? 18.235  18.751  8.594   1.00 11.30 ?  38  VAL   B N    1 
ATOM   1518 C CA   . VAL   B 1 38  ? 18.601  20.145  8.327   1.00 9.29  ?  38  VAL   B CA   1 
ATOM   1519 C C    . VAL   B 1 38  ? 20.025  20.136  7.789   1.00 11.87 ?  38  VAL   B C    1 
ATOM   1520 O O    . VAL   B 1 38  ? 20.897  19.506  8.388   1.00 13.73 ?  38  VAL   B O    1 
ATOM   1521 C CB   . VAL   B 1 38  ? 18.510  21.027  9.598   1.00 13.87 ?  38  VAL   B CB   1 
ATOM   1522 C CG1  . VAL   B 1 38  ? 18.849  22.490  9.291   1.00 17.32 ?  38  VAL   B CG1  1 
ATOM   1523 C CG2  . VAL   B 1 38  ? 17.122  20.931  10.237  1.00 19.19 ?  38  VAL   B CG2  1 
ATOM   1524 N N    . ILE   B 1 39  ? 20.255  20.812  6.662   1.00 10.48 ?  39  ILE   B N    1 
ATOM   1525 C CA   . ILE   B 1 39  ? 21.601  20.955  6.093   1.00 9.28  ?  39  ILE   B CA   1 
ATOM   1526 C C    . ILE   B 1 39  ? 21.946  22.439  5.982   1.00 10.28 ?  39  ILE   B C    1 
ATOM   1527 O O    . ILE   B 1 39  ? 21.175  23.226  5.421   1.00 12.41 ?  39  ILE   B O    1 
ATOM   1528 C CB   . ILE   B 1 39  ? 21.708  20.263  4.725   1.00 11.91 ?  39  ILE   B CB   1 
ATOM   1529 C CG1  . ILE   B 1 39  ? 21.403  18.768  4.875   1.00 12.30 ?  39  ILE   B CG1  1 
ATOM   1530 C CG2  . ILE   B 1 39  ? 23.097  20.481  4.122   1.00 17.66 ?  39  ILE   B CG2  1 
ATOM   1531 C CD1  . ILE   B 1 39  ? 21.377  17.985  3.566   1.00 13.06 ?  39  ILE   B CD1  1 
ATOM   1532 N N    . ALA   B 1 40  ? 23.098  22.827  6.535   1.00 13.61 ?  40  ALA   B N    1 
ATOM   1533 C CA   . ALA   B 1 40  ? 23.560  24.199  6.367   1.00 14.07 ?  40  ALA   B CA   1 
ATOM   1534 C C    . ALA   B 1 40  ? 24.104  24.406  4.958   1.00 13.21 ?  40  ALA   B C    1 
ATOM   1535 O O    . ALA   B 1 40  ? 24.788  23.541  4.407   1.00 12.90 ?  40  ALA   B O    1 
ATOM   1536 C CB   . ALA   B 1 40  ? 24.650  24.523  7.392   1.00 19.85 ?  40  ALA   B CB   1 
ATOM   1537 N N    . GLY   B 1 41  ? 23.791  25.560  4.357   1.00 15.44 ?  41  GLY   B N    1 
ATOM   1538 C CA   . GLY   B 1 41  ? 24.363  25.885  3.072   1.00 14.24 ?  41  GLY   B CA   1 
ATOM   1539 C C    . GLY   B 1 41  ? 25.877  25.869  3.184   1.00 11.38 ?  41  GLY   B C    1 
ATOM   1540 O O    . GLY   B 1 41  ? 26.445  26.462  4.103   1.00 15.67 ?  41  GLY   B O    1 
ATOM   1541 N N    . PRO   B 1 42  ? 26.558  25.153  2.293   1.00 11.79 ?  42  PRO   B N    1 
ATOM   1542 C CA   . PRO   B 1 42  ? 28.018  25.071  2.414   1.00 11.58 ?  42  PRO   B CA   1 
ATOM   1543 C C    . PRO   B 1 42  ? 28.692  26.421  2.232   1.00 15.69 ?  42  PRO   B C    1 
ATOM   1544 O O    . PRO   B 1 42  ? 28.236  27.289  1.486   1.00 14.08 ?  42  PRO   B O    1 
ATOM   1545 C CB   . PRO   B 1 42  ? 28.419  24.097  1.299   1.00 14.98 ?  42  PRO   B CB   1 
ATOM   1546 C CG   . PRO   B 1 42  ? 27.216  23.192  1.161   1.00 14.11 ?  42  PRO   B CG   1 
ATOM   1547 C CD   . PRO   B 1 42  ? 26.022  24.126  1.377   1.00 10.56 ?  42  PRO   B CD   1 
ATOM   1548 N N    . GLN   B 1 43  ? 29.803  26.593  2.943   1.00 17.66 ?  43  GLN   B N    1 
ATOM   1549 C CA   . GLN   B 1 43  ? 30.603  27.795  2.765   1.00 19.45 ?  43  GLN   B CA   1 
ATOM   1550 C C    . GLN   B 1 43  ? 31.135  27.859  1.338   1.00 19.53 ?  43  GLN   B C    1 
ATOM   1551 O O    . GLN   B 1 43  ? 31.453  26.836  0.730   1.00 21.77 ?  43  GLN   B O    1 
ATOM   1552 C CB   . GLN   B 1 43  ? 31.740  27.793  3.784   1.00 20.32 ?  43  GLN   B CB   1 
ATOM   1553 C CG   . GLN   B 1 43  ? 32.919  28.643  3.423   1.00 31.47 ?  43  GLN   B CG   1 
ATOM   1554 C CD   . GLN   B 1 43  ? 33.975  28.619  4.510   1.00 47.64 ?  43  GLN   B CD   1 
ATOM   1555 O OE1  . GLN   B 1 43  ? 33.705  28.218  5.646   1.00 47.73 ?  43  GLN   B OE1  1 
ATOM   1556 N NE2  . GLN   B 1 43  ? 35.187  29.039  4.167   1.00 47.05 ?  43  GLN   B NE2  1 
ATOM   1557 N N    . ASP   B 1 44  ? 31.179  29.064  0.774   1.00 19.83 ?  44  ASP   B N    1 
ATOM   1558 C CA   . ASP   B 1 44  ? 31.673  29.255  -0.592  1.00 23.62 ?  44  ASP   B CA   1 
ATOM   1559 C C    . ASP   B 1 44  ? 30.829  28.474  -1.599  1.00 26.85 ?  44  ASP   B C    1 
ATOM   1560 O O    . ASP   B 1 44  ? 31.345  27.877  -2.546  1.00 29.87 ?  44  ASP   B O    1 
ATOM   1561 C CB   . ASP   B 1 44  ? 33.151  28.856  -0.721  1.00 27.43 ?  44  ASP   B CB   1 
ATOM   1562 C CG   . ASP   B 1 44  ? 34.066  29.624  0.233   1.00 38.41 ?  44  ASP   B CG   1 
ATOM   1563 O OD1  . ASP   B 1 44  ? 33.784  30.796  0.555   1.00 37.13 -1 44  ASP   B OD1  1 
ATOM   1564 O OD2  . ASP   B 1 44  ? 35.088  29.047  0.662   1.00 43.49 ?  44  ASP   B OD2  1 
ATOM   1565 N N    . SER   B 1 45  ? 29.531  28.411  -1.356  1.00 18.63 ?  45  SER   B N    1 
ATOM   1566 C CA   . SER   B 1 45  ? 28.568  27.920  -2.329  1.00 16.64 ?  45  SER   B CA   1 
ATOM   1567 C C    . SER   B 1 45  ? 27.507  28.991  -2.481  1.00 16.92 ?  45  SER   B C    1 
ATOM   1568 O O    . SER   B 1 45  ? 27.434  29.917  -1.670  1.00 14.16 ?  45  SER   B O    1 
ATOM   1569 C CB   . SER   B 1 45  ? 27.920  26.602  -1.878  1.00 16.23 ?  45  SER   B CB   1 
ATOM   1570 O OG   . SER   B 1 45  ? 26.899  26.833  -0.912  1.00 14.74 ?  45  SER   B OG   1 
ATOM   1571 N N    . PRO   B 1 46  ? 26.650  28.881  -3.505  1.00 13.14 ?  46  PRO   B N    1 
ATOM   1572 C CA   . PRO   B 1 46  ? 25.575  29.877  -3.661  1.00 13.96 ?  46  PRO   B CA   1 
ATOM   1573 C C    . PRO   B 1 46  ? 24.603  29.866  -2.522  1.00 18.65 ?  46  PRO   B C    1 
ATOM   1574 O O    . PRO   B 1 46  ? 23.785  30.785  -2.431  1.00 15.16 ?  46  PRO   B O    1 
ATOM   1575 C CB   . PRO   B 1 46  ? 24.888  29.475  -4.976  1.00 15.47 ?  46  PRO   B CB   1 
ATOM   1576 C CG   . PRO   B 1 46  ? 25.949  28.640  -5.714  1.00 17.46 ?  46  PRO   B CG   1 
ATOM   1577 C CD   . PRO   B 1 46  ? 26.658  27.907  -4.613  1.00 15.71 ?  46  PRO   B CD   1 
ATOM   1578 N N    . PHE   B 1 47  ? 24.660  28.854  -1.663  1.00 14.59 ?  47  PHE   B N    1 
ATOM   1579 C CA   . PHE   B 1 47  ? 23.695  28.670  -0.593  1.00 13.36 ?  47  PHE   B CA   1 
ATOM   1580 C C    . PHE   B 1 47  ? 24.262  29.050  0.757   1.00 12.73 ?  47  PHE   B C    1 
ATOM   1581 O O    . PHE   B 1 47  ? 23.616  28.804  1.774   1.00 12.66 ?  47  PHE   B O    1 
ATOM   1582 C CB   . PHE   B 1 47  ? 23.181  27.221  -0.630  1.00 12.89 ?  47  PHE   B CB   1 
ATOM   1583 C CG   . PHE   B 1 47  ? 22.730  26.808  -2.005  1.00 9.92  ?  47  PHE   B CG   1 
ATOM   1584 C CD1  . PHE   B 1 47  ? 21.495  27.239  -2.503  1.00 12.11 ?  47  PHE   B CD1  1 
ATOM   1585 C CD2  . PHE   B 1 47  ? 23.561  26.074  -2.839  1.00 10.67 ?  47  PHE   B CD2  1 
ATOM   1586 C CE1  . PHE   B 1 47  ? 21.115  26.920  -3.781  1.00 11.50 ?  47  PHE   B CE1  1 
ATOM   1587 C CE2  . PHE   B 1 47  ? 23.196  25.750  -4.106  1.00 13.14 ?  47  PHE   B CE2  1 
ATOM   1588 C CZ   . PHE   B 1 47  ? 21.960  26.156  -4.604  1.00 13.97 ?  47  PHE   B CZ   1 
ATOM   1589 N N    . GLU   B 1 48  ? 25.457  29.672  0.776   1.00 13.86 ?  48  GLU   B N    1 
ATOM   1590 C CA   . GLU   B 1 48  ? 26.091  30.090  2.020   1.00 15.98 ?  48  GLU   B CA   1 
ATOM   1591 C C    . GLU   B 1 48  ? 25.178  31.029  2.800   1.00 17.14 ?  48  GLU   B C    1 
ATOM   1592 O O    . GLU   B 1 48  ? 24.544  31.924  2.229   1.00 16.89 ?  48  GLU   B O    1 
ATOM   1593 C CB   . GLU   B 1 48  ? 27.423  30.794  1.711   1.00 16.75 ?  48  GLU   B CB   1 
ATOM   1594 C CG   . GLU   B 1 48  ? 28.130  31.293  2.939   1.00 24.63 ?  48  GLU   B CG   1 
ATOM   1595 C CD   . GLU   B 1 48  ? 29.605  31.482  2.695   1.00 32.23 ?  48  GLU   B CD   1 
ATOM   1596 O OE1  . GLU   B 1 48  ? 29.991  31.538  1.515   1.00 30.77 ?  48  GLU   B OE1  1 
ATOM   1597 O OE2  . GLU   B 1 48  ? 30.372  31.533  3.678   1.00 42.23 -1 48  GLU   B OE2  1 
ATOM   1598 N N    . GLY   B 1 49  ? 25.098  30.811  4.112   1.00 15.55 ?  49  GLY   B N    1 
ATOM   1599 C CA   . GLY   B 1 49  ? 24.195  31.560  4.962   1.00 19.70 ?  49  GLY   B CA   1 
ATOM   1600 C C    . GLY   B 1 49  ? 22.829  30.934  5.153   1.00 17.29 ?  49  GLY   B C    1 
ATOM   1601 O O    . GLY   B 1 49  ? 22.112  31.302  6.099   1.00 16.50 ?  49  GLY   B O    1 
ATOM   1602 N N    . GLY   B 1 50  ? 22.444  29.991  4.290   1.00 13.48 ?  50  GLY   B N    1 
ATOM   1603 C CA   . GLY   B 1 50  ? 21.120  29.405  4.367   1.00 12.52 ?  50  GLY   B CA   1 
ATOM   1604 C C    . GLY   B 1 50  ? 21.054  28.173  5.243   1.00 13.36 ?  50  GLY   B C    1 
ATOM   1605 O O    . GLY   B 1 50  ? 22.057  27.502  5.491   1.00 15.51 ?  50  GLY   B O    1 
ATOM   1606 N N    . THR   B 1 51  ? 19.843  27.896  5.723   1.00 12.29 ?  51  THR   B N    1 
ATOM   1607 C CA   . THR   B 1 51  ? 19.555  26.691  6.495   1.00 12.13 ?  51  THR   B CA   1 
ATOM   1608 C C    . THR   B 1 51  ? 18.428  25.977  5.758   1.00 11.63 ?  51  THR   B C    1 
ATOM   1609 O O    . THR   B 1 51  ? 17.357  26.561  5.558   1.00 17.59 ?  51  THR   B O    1 
ATOM   1610 C CB   . THR   B 1 51  ? 19.135  27.045  7.932   1.00 17.31 ?  51  THR   B CB   1 
ATOM   1611 O OG1  . THR   B 1 51  ? 20.213  27.734  8.604   1.00 20.03 ?  51  THR   B OG1  1 
ATOM   1612 C CG2  . THR   B 1 51  ? 18.766  25.811  8.711   1.00 23.98 ?  51  THR   B CG2  1 
ATOM   1613 N N    . PHE   B 1 52  ? 18.636  24.719  5.386   1.00 12.39 ?  52  PHE   B N    1 
ATOM   1614 C CA   . PHE   B 1 52  ? 17.683  24.030  4.516   1.00 11.70 ?  52  PHE   B CA   1 
ATOM   1615 C C    . PHE   B 1 52  ? 17.074  22.840  5.237   1.00 10.53 ?  52  PHE   B C    1 
ATOM   1616 O O    . PHE   B 1 52  ? 17.801  21.963  5.715   1.00 13.32 ?  52  PHE   B O    1 
ATOM   1617 C CB   . PHE   B 1 52  ? 18.389  23.593  3.213   1.00 9.80  ?  52  PHE   B CB   1 
ATOM   1618 C CG   . PHE   B 1 52  ? 18.890  24.754  2.411   1.00 10.28 ?  52  PHE   B CG   1 
ATOM   1619 C CD1  . PHE   B 1 52  ? 20.137  25.325  2.678   1.00 13.29 ?  52  PHE   B CD1  1 
ATOM   1620 C CD2  . PHE   B 1 52  ? 18.079  25.340  1.446   1.00 14.73 ?  52  PHE   B CD2  1 
ATOM   1621 C CE1  . PHE   B 1 52  ? 20.577  26.439  1.962   1.00 13.05 ?  52  PHE   B CE1  1 
ATOM   1622 C CE2  . PHE   B 1 52  ? 18.514  26.448  0.729   1.00 12.71 ?  52  PHE   B CE2  1 
ATOM   1623 C CZ   . PHE   B 1 52  ? 19.766  26.999  0.989   1.00 12.50 ?  52  PHE   B CZ   1 
ATOM   1624 N N    . LYS   B 1 53  ? 15.736  22.803  5.283   1.00 11.14 ?  53  LYS   B N    1 
ATOM   1625 C CA   . LYS   B 1 53  ? 14.996  21.698  5.887   1.00 10.04 ?  53  LYS   B CA   1 
ATOM   1626 C C    . LYS   B 1 53  ? 14.684  20.664  4.817   1.00 11.44 ?  53  LYS   B C    1 
ATOM   1627 O O    . LYS   B 1 53  ? 14.282  21.019  3.715   1.00 12.47 ?  53  LYS   B O    1 
ATOM   1628 C CB   . LYS   B 1 53  ? 13.702  22.214  6.527   1.00 16.67 ?  53  LYS   B CB   1 
ATOM   1629 C CG   . LYS   B 1 53  ? 13.913  23.056  7.788   1.00 19.09 ?  53  LYS   B CG   1 
ATOM   1630 C CD   . LYS   B 1 53  ? 12.623  23.140  8.623   1.00 30.92 ?  53  LYS   B CD   1 
ATOM   1631 C CE   . LYS   B 1 53  ? 11.590  22.078  8.250   1.00 34.20 ?  53  LYS   B CE   1 
ATOM   1632 N NZ   . LYS   B 1 53  ? 10.320  22.266  9.030   1.00 44.35 ?  53  LYS   B NZ   1 
ATOM   1633 N N    . LEU   B 1 54  ? 14.881  19.386  5.147   1.00 9.24  ?  54  LEU   B N    1 
ATOM   1634 C CA   . LEU   B 1 54  ? 14.549  18.260  4.288   1.00 10.78 ?  54  LEU   B CA   1 
ATOM   1635 C C    . LEU   B 1 54  ? 13.850  17.190  5.112   1.00 10.87 ?  54  LEU   B C    1 
ATOM   1636 O O    . LEU   B 1 54  ? 13.868  17.206  6.347   1.00 12.36 ?  54  LEU   B O    1 
ATOM   1637 C CB   . LEU   B 1 54  ? 15.798  17.635  3.653   1.00 10.48 ?  54  LEU   B CB   1 
ATOM   1638 C CG   . LEU   B 1 54  ? 16.592  18.531  2.697   1.00 12.02 ?  54  LEU   B CG   1 
ATOM   1639 C CD1  . LEU   B 1 54  ? 17.679  19.349  3.431   1.00 13.29 ?  54  LEU   B CD1  1 
ATOM   1640 C CD2  . LEU   B 1 54  ? 17.220  17.671  1.596   1.00 14.67 ?  54  LEU   B CD2  1 
ATOM   1641 N N    . GLU   B 1 55  ? 13.212  16.251  4.419   1.00 11.56 ?  55  GLU   B N    1 
ATOM   1642 C CA   . GLU   B 1 55  ? 12.665  15.083  5.097   1.00 11.88 ?  55  GLU   B CA   1 
ATOM   1643 C C    . GLU   B 1 55  ? 13.094  13.839  4.345   1.00 9.32  ?  55  GLU   B C    1 
ATOM   1644 O O    . GLU   B 1 55  ? 13.328  13.877  3.132   1.00 11.04 ?  55  GLU   B O    1 
ATOM   1645 C CB   . GLU   B 1 55  ? 11.138  15.124  5.233   1.00 15.77 ?  55  GLU   B CB   1 
ATOM   1646 C CG   . GLU   B 1 55  ? 10.456  15.601  4.004   1.00 15.18 ?  55  GLU   B CG   1 
ATOM   1647 C CD   . GLU   B 1 55  ? 8.978   15.932  4.234   1.00 21.57 ?  55  GLU   B CD   1 
ATOM   1648 O OE1  . GLU   B 1 55  ? 8.379   15.522  5.262   1.00 18.68 ?  55  GLU   B OE1  1 
ATOM   1649 O OE2  . GLU   B 1 55  ? 8.419   16.615  3.360   1.00 18.91 -1 55  GLU   B OE2  1 
ATOM   1650 N N    . LEU   B 1 56  ? 13.288  12.757  5.112   1.00 12.63 ?  56  LEU   B N    1 
ATOM   1651 C CA   . LEU   B 1 56  ? 13.807  11.494  4.602   1.00 9.82  ?  56  LEU   B CA   1 
ATOM   1652 C C    . LEU   B 1 56  ? 12.958  10.356  5.165   1.00 14.89 ?  56  LEU   B C    1 
ATOM   1653 O O    . LEU   B 1 56  ? 12.559  10.385  6.331   1.00 13.98 ?  56  LEU   B O    1 
ATOM   1654 C CB   . LEU   B 1 56  ? 15.301  11.318  4.997   1.00 11.30 ?  56  LEU   B CB   1 
ATOM   1655 C CG   . LEU   B 1 56  ? 16.003  10.060  4.498   1.00 9.83  ?  56  LEU   B CG   1 
ATOM   1656 C CD1  . LEU   B 1 56  ? 17.471  10.350  4.193   1.00 11.52 ?  56  LEU   B CD1  1 
ATOM   1657 C CD2  . LEU   B 1 56  ? 15.885  8.917   5.502   1.00 12.18 ?  56  LEU   B CD2  1 
ATOM   1658 N N    . PHE   B 1 57  ? 12.651  9.363   4.339   1.00 11.80 ?  57  PHE   B N    1 
ATOM   1659 C CA   . PHE   B 1 57  ? 11.801  8.269   4.784   1.00 11.47 ?  57  PHE   B CA   1 
ATOM   1660 C C    . PHE   B 1 57  ? 12.371  6.957   4.276   1.00 13.48 ?  57  PHE   B C    1 
ATOM   1661 O O    . PHE   B 1 57  ? 12.711  6.846   3.090   1.00 14.35 ?  57  PHE   B O    1 
ATOM   1662 C CB   . PHE   B 1 57  ? 10.359  8.439   4.275   1.00 14.34 ?  57  PHE   B CB   1 
ATOM   1663 C CG   . PHE   B 1 57  ? 9.420   7.384   4.786   1.00 16.60 ?  57  PHE   B CG   1 
ATOM   1664 C CD1  . PHE   B 1 57  ? 9.061   7.363   6.125   1.00 17.95 ?  57  PHE   B CD1  1 
ATOM   1665 C CD2  . PHE   B 1 57  ? 8.909   6.413   3.937   1.00 23.52 ?  57  PHE   B CD2  1 
ATOM   1666 C CE1  . PHE   B 1 57  ? 8.188   6.389   6.615   1.00 20.01 ?  57  PHE   B CE1  1 
ATOM   1667 C CE2  . PHE   B 1 57  ? 8.033   5.436   4.425   1.00 21.16 ?  57  PHE   B CE2  1 
ATOM   1668 C CZ   . PHE   B 1 57  ? 7.691   5.428   5.757   1.00 23.79 ?  57  PHE   B CZ   1 
ATOM   1669 N N    . LEU   B 1 58  ? 12.449  5.960   5.157   1.00 11.91 ?  58  LEU   B N    1 
ATOM   1670 C CA   . LEU   B 1 58  ? 12.919  4.630   4.763   1.00 10.55 ?  58  LEU   B CA   1 
ATOM   1671 C C    . LEU   B 1 58  ? 11.721  3.754   4.421   1.00 14.24 ?  58  LEU   B C    1 
ATOM   1672 O O    . LEU   B 1 58  ? 10.985  3.350   5.337   1.00 18.66 ?  58  LEU   B O    1 
ATOM   1673 C CB   . LEU   B 1 58  ? 13.716  3.999   5.879   1.00 14.73 ?  58  LEU   B CB   1 
ATOM   1674 C CG   . LEU   B 1 58  ? 14.851  4.865   6.415   1.00 13.67 ?  58  LEU   B CG   1 
ATOM   1675 C CD1  . LEU   B 1 58  ? 15.460  4.201   7.629   1.00 13.49 ?  58  LEU   B CD1  1 
ATOM   1676 C CD2  . LEU   B 1 58  ? 15.897  5.055   5.311   1.00 12.80 ?  58  LEU   B CD2  1 
ATOM   1677 N N    . PRO   B 1 59  ? 11.504  3.410   3.154   1.00 14.65 ?  59  PRO   B N    1 
ATOM   1678 C CA   . PRO   B 1 59  ? 10.337  2.590   2.794   1.00 19.18 ?  59  PRO   B CA   1 
ATOM   1679 C C    . PRO   B 1 59  ? 10.436  1.179   3.363   1.00 18.55 ?  59  PRO   B C    1 
ATOM   1680 O O    . PRO   B 1 59  ? 11.472  0.733   3.855   1.00 18.66 ?  59  PRO   B O    1 
ATOM   1681 C CB   . PRO   B 1 59  ? 10.350  2.565   1.261   1.00 21.85 ?  59  PRO   B CB   1 
ATOM   1682 C CG   . PRO   B 1 59  ? 11.541  3.321   0.816   1.00 22.11 ?  59  PRO   B CG   1 
ATOM   1683 C CD   . PRO   B 1 59  ? 12.348  3.748   1.992   1.00 14.03 ?  59  PRO   B CD   1 
ATOM   1684 N N    . GLU   B 1 60  ? 9.307   0.462   3.262   1.00 19.78 ?  60  GLU   B N    1 
ATOM   1685 C CA   . GLU   B 1 60  ? 9.229   -0.904  3.780   1.00 22.61 ?  60  GLU   B CA   1 
ATOM   1686 C C    . GLU   B 1 60  ? 10.344  -1.796  3.233   1.00 20.66 ?  60  GLU   B C    1 
ATOM   1687 O O    . GLU   B 1 60  ? 10.874  -2.643  3.954   1.00 25.08 ?  60  GLU   B O    1 
ATOM   1688 C CB   . GLU   B 1 60  ? 7.867   -1.514  3.436   1.00 25.91 ?  60  GLU   B CB   1 
ATOM   1689 C CG   . GLU   B 1 60  ? 6.702   -1.097  4.342   1.00 48.06 ?  60  GLU   B CG   1 
ATOM   1690 C CD   . GLU   B 1 60  ? 7.043   -1.085  5.836   1.00 50.64 ?  60  GLU   B CD   1 
ATOM   1691 O OE1  . GLU   B 1 60  ? 6.741   -2.081  6.529   1.00 51.89 ?  60  GLU   B OE1  1 
ATOM   1692 O OE2  . GLU   B 1 60  ? 7.567   -0.059  6.327   1.00 48.98 -1 60  GLU   B OE2  1 
ATOM   1693 N N    . GLU   B 1 61  ? 10.701  -1.632  1.962   1.00 23.10 ?  61  GLU   B N    1 
ATOM   1694 C CA   . GLU   B 1 61  ? 11.691  -2.491  1.317   1.00 24.50 ?  61  GLU   B CA   1 
ATOM   1695 C C    . GLU   B 1 61  ? 13.136  -2.089  1.637   1.00 22.48 ?  61  GLU   B C    1 
ATOM   1696 O O    . GLU   B 1 61  ? 14.072  -2.781  1.205   1.00 24.32 ?  61  GLU   B O    1 
ATOM   1697 C CB   . GLU   B 1 61  ? 11.463  -2.479  -0.197  1.00 27.92 ?  61  GLU   B CB   1 
ATOM   1698 C CG   . GLU   B 1 61  ? 10.375  -3.431  -0.702  1.00 40.11 ?  61  GLU   B CG   1 
ATOM   1699 C CD   . GLU   B 1 61  ? 10.517  -4.843  -0.163  1.00 53.56 ?  61  GLU   B CD   1 
ATOM   1700 O OE1  . GLU   B 1 61  ? 11.279  -5.640  -0.759  1.00 58.66 ?  61  GLU   B OE1  1 
ATOM   1701 O OE2  . GLU   B 1 61  ? 9.851   -5.161  0.846   1.00 57.77 -1 61  GLU   B OE2  1 
ATOM   1702 N N    . TYR   B 1 62  ? 13.348  -1.016  2.401   1.00 18.12 ?  62  TYR   B N    1 
ATOM   1703 C CA   . TYR   B 1 62  ? 14.705  -0.602  2.749   1.00 18.08 ?  62  TYR   B CA   1 
ATOM   1704 C C    . TYR   B 1 62  ? 15.406  -1.729  3.509   1.00 17.74 ?  62  TYR   B C    1 
ATOM   1705 O O    . TYR   B 1 62  ? 14.812  -2.325  4.412   1.00 22.02 ?  62  TYR   B O    1 
ATOM   1706 C CB   . TYR   B 1 62  ? 14.688  0.672   3.605   1.00 17.04 ?  62  TYR   B CB   1 
ATOM   1707 C CG   . TYR   B 1 62  ? 16.080  1.223   3.871   1.00 16.54 ?  62  TYR   B CG   1 
ATOM   1708 C CD1  . TYR   B 1 62  ? 16.732  2.016   2.919   1.00 16.51 ?  62  TYR   B CD1  1 
ATOM   1709 C CD2  . TYR   B 1 62  ? 16.760  0.944   5.067   1.00 16.63 ?  62  TYR   B CD2  1 
ATOM   1710 C CE1  . TYR   B 1 62  ? 18.019  2.509   3.145   1.00 14.19 ?  62  TYR   B CE1  1 
ATOM   1711 C CE2  . TYR   B 1 62  ? 18.044  1.442   5.302   1.00 15.87 ?  62  TYR   B CE2  1 
ATOM   1712 C CZ   . TYR   B 1 62  ? 18.670  2.230   4.349   1.00 17.67 ?  62  TYR   B CZ   1 
ATOM   1713 O OH   . TYR   B 1 62  ? 19.967  2.701   4.577   1.00 18.08 ?  62  TYR   B OH   1 
ATOM   1714 N N    . PRO   B 1 63  ? 16.677  -2.038  3.195   1.00 19.44 ?  63  PRO   B N    1 
ATOM   1715 C CA   . PRO   B 1 63  ? 17.598  -1.341  2.290   1.00 18.66 ?  63  PRO   B CA   1 
ATOM   1716 C C    . PRO   B 1 63  ? 17.673  -1.850  0.847   1.00 17.78 ?  63  PRO   B C    1 
ATOM   1717 O O    . PRO   B 1 63  ? 18.631  -1.512  0.141   1.00 18.92 ?  63  PRO   B O    1 
ATOM   1718 C CB   . PRO   B 1 63  ? 18.940  -1.555  2.987   1.00 18.42 ?  63  PRO   B CB   1 
ATOM   1719 C CG   . PRO   B 1 63  ? 18.818  -2.960  3.516   1.00 20.60 ?  63  PRO   B CG   1 
ATOM   1720 C CD   . PRO   B 1 63  ? 17.379  -3.087  3.963   1.00 22.16 ?  63  PRO   B CD   1 
ATOM   1721 N N    . MET   B 1 64  ? 16.730  -2.648  0.348   1.00 18.74 ?  64  MET   B N    1 
ATOM   1722 C CA   . MET   B 1 64  ? 16.777  -2.962  -1.076  1.00 21.31 ?  64  MET   B CA   1 
ATOM   1723 C C    . MET   B 1 64  ? 16.224  -1.849  -1.950  1.00 21.23 ?  64  MET   B C    1 
ATOM   1724 O O    . MET   B 1 64  ? 16.568  -1.786  -3.141  1.00 24.61 ?  64  MET   B O    1 
ATOM   1725 C CB   . MET   B 1 64  ? 16.053  -4.273  -1.379  1.00 27.89 ?  64  MET   B CB   1 
ATOM   1726 C CG   . MET   B 1 64  ? 16.251  -5.299  -0.315  1.00 27.07 ?  64  MET   B CG   1 
ATOM   1727 S SD   . MET   B 1 64  ? 17.943  -5.910  -0.508  1.00 41.83 ?  64  MET   B SD   1 
ATOM   1728 C CE   . MET   B 1 64  ? 18.064  -5.969  -2.290  1.00 37.32 ?  64  MET   B CE   1 
ATOM   1729 N N    . ALA   B 1 65  ? 15.394  -0.972  -1.394  1.00 21.78 ?  65  ALA   B N    1 
ATOM   1730 C CA   . ALA   B 1 65  ? 14.947  0.226   -2.081  1.00 22.32 ?  65  ALA   B CA   1 
ATOM   1731 C C    . ALA   B 1 65  ? 15.516  1.444   -1.371  1.00 16.81 ?  65  ALA   B C    1 
ATOM   1732 O O    . ALA   B 1 65  ? 15.791  1.408   -0.165  1.00 15.25 ?  65  ALA   B O    1 
ATOM   1733 C CB   . ALA   B 1 65  ? 13.423  0.311   -2.130  1.00 21.43 ?  65  ALA   B CB   1 
ATOM   1734 N N    . ALA   B 1 66  ? 15.725  2.505   -2.143  1.00 18.78 ?  66  ALA   B N    1 
ATOM   1735 C CA   . ALA   B 1 66  ? 16.400  3.688   -1.635  1.00 16.64 ?  66  ALA   B CA   1 
ATOM   1736 C C    . ALA   B 1 66  ? 15.525  4.433   -0.630  1.00 12.96 ?  66  ALA   B C    1 
ATOM   1737 O O    . ALA   B 1 66  ? 14.295  4.368   -0.706  1.00 15.60 ?  66  ALA   B O    1 
ATOM   1738 C CB   . ALA   B 1 66  ? 16.729  4.641   -2.775  1.00 17.53 ?  66  ALA   B CB   1 
ATOM   1739 N N    . PRO   B 1 67  ? 16.133  5.196   0.276   1.00 11.89 ?  67  PRO   B N    1 
ATOM   1740 C CA   . PRO   B 1 67  ? 15.346  6.170   1.036   1.00 12.42 ?  67  PRO   B CA   1 
ATOM   1741 C C    . PRO   B 1 67  ? 14.669  7.134   0.075   1.00 12.24 ?  67  PRO   B C    1 
ATOM   1742 O O    . PRO   B 1 67  ? 15.174  7.418   -1.014  1.00 17.45 ?  67  PRO   B O    1 
ATOM   1743 C CB   . PRO   B 1 67  ? 16.389  6.893   1.907   1.00 15.66 ?  67  PRO   B CB   1 
ATOM   1744 C CG   . PRO   B 1 67  ? 17.635  6.032   1.834   1.00 15.01 ?  67  PRO   B CG   1 
ATOM   1745 C CD   . PRO   B 1 67  ? 17.586  5.331   0.521   1.00 11.73 ?  67  PRO   B CD   1 
ATOM   1746 N N    . LYS   B 1 68  ? 13.528  7.660   0.508   1.00 14.46 ?  68  LYS   B N    1 
ATOM   1747 C CA   . LYS   B 1 68  ? 12.872  8.773   -0.156  1.00 13.25 ?  68  LYS   B CA   1 
ATOM   1748 C C    . LYS   B 1 68  ? 13.340  10.051  0.517   1.00 10.63 ?  68  LYS   B C    1 
ATOM   1749 O O    . LYS   B 1 68  ? 13.440  10.101  1.742   1.00 12.47 ?  68  LYS   B O    1 
ATOM   1750 C CB   . LYS   B 1 68  ? 11.349  8.634   -0.054  1.00 13.88 ?  68  LYS   B CB   1 
ATOM   1751 C CG   . LYS   B 1 68  ? 10.826  7.255   -0.462  1.00 22.75 ?  68  LYS   B CG   1 
ATOM   1752 C CD   . LYS   B 1 68  ? 9.349   7.297   -0.870  1.00 30.46 ?  68  LYS   B CD   1 
ATOM   1753 C CE   . LYS   B 1 68  ? 9.002   6.066   -1.699  1.00 32.43 ?  68  LYS   B CE   1 
ATOM   1754 N NZ   . LYS   B 1 68  ? 9.500   6.227   -3.096  1.00 35.05 ?  68  LYS   B NZ   1 
ATOM   1755 N N    . VAL   B 1 69  ? 13.656  11.073  -0.275  1.00 12.45 ?  69  VAL   B N    1 
ATOM   1756 C CA   . VAL   B 1 69  ? 14.149  12.322  0.298   1.00 11.68 ?  69  VAL   B CA   1 
ATOM   1757 C C    . VAL   B 1 69  ? 13.577  13.499  -0.475  1.00 13.76 ?  69  VAL   B C    1 
ATOM   1758 O O    . VAL   B 1 69  ? 13.510  13.465  -1.708  1.00 17.12 ?  69  VAL   B O    1 
ATOM   1759 C CB   . VAL   B 1 69  ? 15.693  12.403  0.286   1.00 12.93 ?  69  VAL   B CB   1 
ATOM   1760 C CG1  . VAL   B 1 69  ? 16.145  13.576  1.169   1.00 13.43 ?  69  VAL   B CG1  1 
ATOM   1761 C CG2  . VAL   B 1 69  ? 16.304  11.118  0.742   1.00 18.33 ?  69  VAL   B CG2  1 
ATOM   1762 N N    . ARG   B 1 70  ? 13.219  14.571  0.235   1.00 9.98  ?  70  ARG   B N    1 
ATOM   1763 C CA   . ARG   B 1 70  ? 12.843  15.783  -0.490  1.00 11.62 ?  70  ARG   B CA   1 
ATOM   1764 C C    . ARG   B 1 70  ? 13.225  17.029  0.302   1.00 12.43 ?  70  ARG   B C    1 
ATOM   1765 O O    . ARG   B 1 70  ? 13.316  16.992  1.535   1.00 12.39 ?  70  ARG   B O    1 
ATOM   1766 C CB   . ARG   B 1 70  ? 11.344  15.804  -0.812  1.00 14.99 ?  70  ARG   B CB   1 
ATOM   1767 C CG   . ARG   B 1 70  ? 10.458  15.900  0.396   1.00 14.74 ?  70  ARG   B CG   1 
ATOM   1768 C CD   . ARG   B 1 70  ? 8.965   16.034  -0.014  1.00 18.22 ?  70  ARG   B CD   1 
ATOM   1769 N NE   . ARG   B 1 70  ? 8.653   17.311  -0.655  1.00 19.54 ?  70  ARG   B NE   1 
ATOM   1770 C CZ   . ARG   B 1 70  ? 8.246   18.400  -0.014  1.00 15.66 ?  70  ARG   B CZ   1 
ATOM   1771 N NH1  . ARG   B 1 70  ? 8.123   18.427  1.307   1.00 18.87 ?  70  ARG   B NH1  1 
ATOM   1772 N NH2  . ARG   B 1 70  ? 7.957   19.501  -0.715  1.00 19.53 ?  70  ARG   B NH2  1 
ATOM   1773 N N    . PHE   B 1 71  ? 13.498  18.126  -0.421  1.00 11.91 ?  71  PHE   B N    1 
ATOM   1774 C CA   . PHE   B 1 71  ? 13.637  19.429  0.220   1.00 9.13  ?  71  PHE   B CA   1 
ATOM   1775 C C    . PHE   B 1 71  ? 12.268  19.948  0.639   1.00 15.91 ?  71  PHE   B C    1 
ATOM   1776 O O    . PHE   B 1 71  ? 11.322  19.929  -0.159  1.00 15.33 ?  71  PHE   B O    1 
ATOM   1777 C CB   . PHE   B 1 71  ? 14.270  20.452  -0.735  1.00 13.76 ?  71  PHE   B CB   1 
ATOM   1778 C CG   . PHE   B 1 71  ? 15.775  20.427  -0.776  1.00 12.28 ?  71  PHE   B CG   1 
ATOM   1779 C CD1  . PHE   B 1 71  ? 16.447  19.552  -1.620  1.00 13.33 ?  71  PHE   B CD1  1 
ATOM   1780 C CD2  . PHE   B 1 71  ? 16.528  21.317  0.002   1.00 13.29 ?  71  PHE   B CD2  1 
ATOM   1781 C CE1  . PHE   B 1 71  ? 17.827  19.535  -1.670  1.00 10.81 ?  71  PHE   B CE1  1 
ATOM   1782 C CE2  . PHE   B 1 71  ? 17.931  21.299  -0.052  1.00 14.71 ?  71  PHE   B CE2  1 
ATOM   1783 C CZ   . PHE   B 1 71  ? 18.570  20.404  -0.888  1.00 12.67 ?  71  PHE   B CZ   1 
ATOM   1784 N N    . MET   B 1 72  ? 12.166  20.452  1.868   1.00 10.27 ?  72  MET   B N    1 
ATOM   1785 C CA   . MET   B 1 72  ? 10.977  21.238  2.188   1.00 12.04 ?  72  MET   B CA   1 
ATOM   1786 C C    . MET   B 1 72  ? 11.199  22.737  2.034   1.00 15.59 ?  72  MET   B C    1 
ATOM   1787 O O    . MET   B 1 72  ? 10.286  23.435  1.577   1.00 18.59 ?  72  MET   B O    1 
ATOM   1788 C CB   . MET   B 1 72  ? 10.389  20.882  3.571   1.00 20.26 ?  72  MET   B CB   1 
ATOM   1789 C CG   . MET   B 1 72  ? 10.607  19.444  4.046   1.00 18.77 ?  72  MET   B CG   1 
ATOM   1790 S SD   . MET   B 1 72  ? 10.413  19.070  5.809   1.00 23.45 ?  72  MET   B SD   1 
ATOM   1791 C CE   . MET   B 1 72  ? 8.668   19.396  6.027   1.00 26.95 ?  72  MET   B CE   1 
ATOM   1792 N N    . THR   B 1 73  ? 12.401  23.228  2.315   1.00 13.05 ?  73  THR   B N    1 
ATOM   1793 C CA   . THR   B 1 73  ? 12.762  24.606  2.014   1.00 10.95 ?  73  THR   B CA   1 
ATOM   1794 C C    . THR   B 1 73  ? 12.856  24.814  0.515   1.00 13.82 ?  73  THR   B C    1 
ATOM   1795 O O    . THR   B 1 73  ? 13.494  24.031  -0.185  1.00 16.77 ?  73  THR   B O    1 
ATOM   1796 C CB   . THR   B 1 73  ? 14.112  24.970  2.672   1.00 11.41 ?  73  THR   B CB   1 
ATOM   1797 O OG1  . THR   B 1 73  ? 13.994  24.734  4.068   1.00 12.58 ?  73  THR   B OG1  1 
ATOM   1798 C CG2  . THR   B 1 73  ? 14.490  26.434  2.437   1.00 14.78 ?  73  THR   B CG2  1 
HETATM 1799 C C22  . A1EJS B 1 74  ? 9.580   25.490  -6.466  1.00 26.35 ?  74  A1EJS B C22  1 
HETATM 1800 C C25  . A1EJS B 1 74  ? 9.827   23.933  -4.413  1.00 22.12 ?  74  A1EJS B C25  1 
HETATM 1801 C C30  . A1EJS B 1 74  ? 11.205  23.894  -4.429  1.00 17.60 ?  74  A1EJS B C30  1 
HETATM 1802 C C29  . A1EJS B 1 74  ? 11.856  23.095  -3.504  1.00 18.54 ?  74  A1EJS B C29  1 
HETATM 1803 C C28  . A1EJS B 1 74  ? 11.187  22.341  -2.565  1.00 22.86 ?  74  A1EJS B C28  1 
HETATM 1804 C C27  . A1EJS B 1 74  ? 9.809   22.363  -2.549  1.00 24.81 ?  74  A1EJS B C27  1 
HETATM 1805 C C26  . A1EJS B 1 74  ? 9.157   23.162  -3.466  1.00 22.96 ?  74  A1EJS B C26  1 
HETATM 1806 C C18  . A1EJS B 1 74  ? 9.181   27.119  -8.201  1.00 26.24 ?  74  A1EJS B C18  1 
HETATM 1807 C C17  . A1EJS B 1 74  ? 8.744   26.398  -7.108  1.00 25.27 ?  74  A1EJS B C17  1 
HETATM 1808 O O15  . A1EJS B 1 74  ? 4.626   27.820  -5.241  1.00 45.56 ?  74  A1EJS B O15  1 
HETATM 1809 O O14  . A1EJS B 1 74  ? 6.385   29.795  -3.325  1.00 42.21 ?  74  A1EJS B O14  1 
HETATM 1810 C C13  . A1EJS B 1 74  ? 7.037   27.763  -5.874  1.00 28.98 ?  74  A1EJS B C13  1 
HETATM 1811 C C10  . A1EJS B 1 74  ? 7.792   28.868  -5.163  1.00 40.35 ?  74  A1EJS B C10  1 
HETATM 1812 C CE   . A1EJS B 1 74  ? 10.229  29.310  -4.765  1.00 33.38 ?  74  A1EJS B CE   1 
HETATM 1813 C CD   . A1EJS B 1 74  ? 10.066  28.921  -3.299  1.00 31.46 ?  74  A1EJS B CD   1 
HETATM 1814 C CG   . A1EJS B 1 74  ? 10.939  27.681  -3.077  1.00 27.75 ?  74  A1EJS B CG   1 
HETATM 1815 C CB   . A1EJS B 1 74  ? 11.536  27.588  -1.681  1.00 21.60 ?  74  A1EJS B CB   1 
HETATM 1816 C CA   . A1EJS B 1 74  ? 12.451  26.369  -1.488  1.00 14.51 ?  74  A1EJS B CA   1 
HETATM 1817 C C    . A1EJS B 1 74  ? 13.921  26.754  -1.688  1.00 12.00 ?  74  A1EJS B C    1 
HETATM 1818 C C11  . A1EJS B 1 74  ? 6.576   29.125  -4.282  1.00 40.48 ?  74  A1EJS B C11  1 
HETATM 1819 C C12  . A1EJS B 1 74  ? 5.759   28.159  -5.146  1.00 46.16 ?  74  A1EJS B C12  1 
HETATM 1820 C C20  . A1EJS B 1 74  ? 11.176  26.014  -7.990  1.00 22.00 ?  74  A1EJS B C20  1 
HETATM 1821 C C31  . A1EJS B 1 74  ? 7.653   23.109  -3.379  1.00 29.82 ?  74  A1EJS B C31  1 
HETATM 1822 C C34  . A1EJS B 1 74  ? 5.784   21.716  -2.968  1.00 32.84 ?  74  A1EJS B C34  1 
HETATM 1823 C C35  . A1EJS B 1 74  ? 12.874  26.454  -9.716  1.00 18.04 ?  74  A1EJS B C35  1 
HETATM 1824 C C36  . A1EJS B 1 74  ? 12.586  25.613  -10.962 1.00 21.56 ?  74  A1EJS B C36  1 
HETATM 1825 C C37  . A1EJS B 1 74  ? 12.073  26.261  -12.079 1.00 25.27 ?  74  A1EJS B C37  1 
HETATM 1826 C C38  . A1EJS B 1 74  ? 11.835  25.532  -13.229 1.00 22.45 ?  74  A1EJS B C38  1 
HETATM 1827 C C39  . A1EJS B 1 74  ? 12.091  24.171  -13.266 1.00 25.71 ?  74  A1EJS B C39  1 
HETATM 1828 C C40  . A1EJS B 1 74  ? 12.596  23.520  -12.149 1.00 24.60 ?  74  A1EJS B C40  1 
HETATM 1829 C C41  . A1EJS B 1 74  ? 12.844  24.250  -10.995 1.00 22.17 ?  74  A1EJS B C41  1 
HETATM 1830 C C42  . A1EJS B 1 74  ? 12.900  22.020  -12.219 1.00 23.15 ?  74  A1EJS B C42  1 
HETATM 1831 C C44  . A1EJS B 1 74  ? 12.711  19.923  -12.607 1.00 26.39 ?  74  A1EJS B C44  1 
HETATM 1832 C C45  . A1EJS B 1 74  ? 13.973  20.167  -12.072 1.00 28.12 ?  74  A1EJS B C45  1 
HETATM 1833 C C47  . A1EJS B 1 74  ? 15.212  22.144  -11.301 1.00 20.91 ?  74  A1EJS B C47  1 
HETATM 1834 F F48  . A1EJS B 1 74  ? 13.199  23.035  -3.527  1.00 20.09 ?  74  A1EJS B F48  1 
HETATM 1835 N NZ   . A1EJS B 1 74  ? 8.990   29.618  -5.441  1.00 38.09 ?  74  A1EJS B NZ   1 
HETATM 1836 N N    . A1EJS B 1 74  ? 12.271  25.950  -0.124  1.00 13.89 ?  74  A1EJS B N    1 
HETATM 1837 N N16  . A1EJS B 1 74  ? 7.400   26.574  -6.594  1.00 24.91 ?  74  A1EJS B N16  1 
HETATM 1838 N N19  . A1EJS B 1 74  ? 10.411  26.887  -8.620  1.00 24.75 ?  74  A1EJS B N19  1 
HETATM 1839 N N21  . A1EJS B 1 74  ? 10.793  25.325  -6.937  1.00 19.31 ?  74  A1EJS B N21  1 
HETATM 1840 N N23  . A1EJS B 1 74  ? 12.505  25.804  -8.484  1.00 20.29 ?  74  A1EJS B N23  1 
HETATM 1841 N N24  . A1EJS B 1 74  ? 9.050   24.758  -5.335  1.00 26.11 ?  74  A1EJS B N24  1 
HETATM 1842 N N43  . A1EJS B 1 74  ? 12.083  21.091  -12.685 1.00 27.63 ?  74  A1EJS B N43  1 
HETATM 1843 N N46  . A1EJS B 1 74  ? 14.052  21.467  -11.847 1.00 23.26 ?  74  A1EJS B N46  1 
HETATM 1844 O O    . A1EJS B 1 74  ? 14.488  27.431  -0.905  1.00 15.71 ?  74  A1EJS B O    1 
HETATM 1845 O O32  . A1EJS B 1 74  ? 7.152   21.958  -2.752  1.00 25.91 ?  74  A1EJS B O32  1 
HETATM 1846 O O33  . A1EJS B 1 74  ? 6.980   23.962  -3.849  1.00 30.38 ?  74  A1EJS B O33  1 
HETATM 1847 H H301 . A1EJS B 1 74  ? 11.768  24.476  -5.150  1.00 21.12 ?  74  A1EJS B H301 1 
HETATM 1848 H H281 . A1EJS B 1 74  ? 11.736  21.740  -1.849  1.00 27.43 ?  74  A1EJS B H281 1 
HETATM 1849 H H271 . A1EJS B 1 74  ? 9.251   21.766  -1.834  1.00 29.77 ?  74  A1EJS B H271 1 
HETATM 1850 H H181 . A1EJS B 1 74  ? 8.543   27.841  -8.693  1.00 31.49 ?  74  A1EJS B H181 1 
HETATM 1851 H HE2  . A1EJS B 1 74  ? 10.705  28.485  -5.285  1.00 40.06 ?  74  A1EJS B HE2  1 
HETATM 1852 H HE3  . A1EJS B 1 74  ? 10.871  30.183  -4.816  1.00 40.06 ?  74  A1EJS B HE3  1 
HETATM 1853 H HD3  . A1EJS B 1 74  ? 10.392  29.731  -2.655  1.00 37.75 ?  74  A1EJS B HD3  1 
HETATM 1854 H HD2  . A1EJS B 1 74  ? 9.027   28.694  -3.082  1.00 37.75 ?  74  A1EJS B HD2  1 
HETATM 1855 H HG2  . A1EJS B 1 74  ? 11.751  27.698  -3.798  1.00 33.30 ?  74  A1EJS B HG2  1 
HETATM 1856 H HG3  . A1EJS B 1 74  ? 10.333  26.797  -3.252  1.00 33.30 ?  74  A1EJS B HG3  1 
HETATM 1857 H HB2  . A1EJS B 1 74  ? 12.112  28.485  -1.491  1.00 25.92 ?  74  A1EJS B HB2  1 
HETATM 1858 H HB3  . A1EJS B 1 74  ? 10.728  27.531  -0.962  1.00 25.92 ?  74  A1EJS B HB3  1 
HETATM 1859 H HA   . A1EJS B 1 74  ? 12.204  25.593  -2.201  1.00 17.41 ?  74  A1EJS B HA   1 
HETATM 1860 H H341 . A1EJS B 1 74  ? 5.574   20.660  -2.817  1.00 39.40 ?  74  A1EJS B H341 1 
HETATM 1861 H H343 . A1EJS B 1 74  ? 5.522   21.995  -3.985  1.00 39.40 ?  74  A1EJS B H343 1 
HETATM 1862 H H342 . A1EJS B 1 74  ? 5.196   22.305  -2.268  1.00 39.40 ?  74  A1EJS B H342 1 
HETATM 1863 H H352 . A1EJS B 1 74  ? 13.939  26.670  -9.686  1.00 21.65 ?  74  A1EJS B H352 1 
HETATM 1864 H H351 . A1EJS B 1 74  ? 12.320  27.386  -9.794  1.00 21.65 ?  74  A1EJS B H351 1 
HETATM 1865 H H371 . A1EJS B 1 74  ? 11.861  27.323  -12.049 1.00 30.32 ?  74  A1EJS B H371 1 
HETATM 1866 H H381 . A1EJS B 1 74  ? 11.445  26.030  -14.111 1.00 26.94 ?  74  A1EJS B H381 1 
HETATM 1867 H H391 . A1EJS B 1 74  ? 11.896  23.610  -14.173 1.00 30.85 ?  74  A1EJS B H391 1 
HETATM 1868 H H411 . A1EJS B 1 74  ? 13.240  23.754  -10.117 1.00 26.60 ?  74  A1EJS B H411 1 
HETATM 1869 H H441 . A1EJS B 1 74  ? 12.314  18.959  -12.903 1.00 31.67 ?  74  A1EJS B H441 1 
HETATM 1870 H H451 . A1EJS B 1 74  ? 14.744  19.431  -11.878 1.00 33.74 ?  74  A1EJS B H451 1 
HETATM 1871 H H472 . A1EJS B 1 74  ? 16.020  21.431  -11.175 1.00 25.09 ?  74  A1EJS B H472 1 
HETATM 1872 H H473 . A1EJS B 1 74  ? 15.526  22.929  -11.981 1.00 25.09 ?  74  A1EJS B H473 1 
HETATM 1873 H H471 . A1EJS B 1 74  ? 14.959  22.578  -10.340 1.00 25.09 ?  74  A1EJS B H471 1 
HETATM 1874 H HZ1  . A1EJS B 1 74  ? 8.964   30.362  -6.110  1.00 45.70 ?  74  A1EJS B HZ1  1 
HETATM 1875 H H    . A1EJS B 1 74  ? 12.506  26.715  0.485   1.00 16.67 ?  74  A1EJS B H    1 
HETATM 1876 H H161 . A1EJS B 1 74  ? 6.717   25.857  -6.742  1.00 29.89 ?  74  A1EJS B H161 1 
HETATM 1877 H H231 . A1EJS B 1 74  ? 13.153  25.227  -7.992  1.00 24.34 ?  74  A1EJS B H231 1 
HETATM 1878 H H241 . A1EJS B 1 74  ? 8.065   24.822  -5.171  1.00 31.33 ?  74  A1EJS B H241 1 
ATOM   1879 N N    . ILE   B 1 75  ? 14.318  26.029  -2.847  1.00 13.36 ?  75  ILE   B N    1 
ATOM   1880 C CA   . ILE   B 1 75  ? 15.717  26.229  -3.243  1.00 13.44 ?  75  ILE   B CA   1 
ATOM   1881 C C    . ILE   B 1 75  ? 15.768  26.279  -4.763  1.00 16.33 ?  75  ILE   B C    1 
ATOM   1882 O O    . ILE   B 1 75  ? 14.940  25.651  -5.429  1.00 15.92 ?  75  ILE   B O    1 
ATOM   1883 C CB   . ILE   B 1 75  ? 16.634  25.110  -2.678  1.00 17.59 ?  75  ILE   B CB   1 
ATOM   1884 C CG1  . ILE   B 1 75  ? 18.108  25.401  -2.980  1.00 13.93 ?  75  ILE   B CG1  1 
ATOM   1885 C CG2  . ILE   B 1 75  ? 16.282  23.769  -3.303  1.00 17.55 ?  75  ILE   B CG2  1 
ATOM   1886 C CD1  . ILE   B 1 75  ? 19.076  24.326  -2.417  1.00 18.46 ?  75  ILE   B CD1  1 
ATOM   1887 N N    . TYR   B 1 76  ? 16.745  27.010  -5.319  1.00 14.17 ?  76  TYR   B N    1 
ATOM   1888 C CA   . TYR   B 1 76  ? 16.934  27.118  -6.761  1.00 14.96 ?  76  TYR   B CA   1 
ATOM   1889 C C    . TYR   B 1 76  ? 18.188  26.320  -7.127  1.00 11.60 ?  76  TYR   B C    1 
ATOM   1890 O O    . TYR   B 1 76  ? 19.304  26.748  -6.835  1.00 13.79 ?  76  TYR   B O    1 
ATOM   1891 C CB   . TYR   B 1 76  ? 17.037  28.590  -7.154  1.00 14.26 ?  76  TYR   B CB   1 
ATOM   1892 C CG   . TYR   B 1 76  ? 17.121  28.863  -8.645  1.00 17.32 ?  76  TYR   B CG   1 
ATOM   1893 C CD1  . TYR   B 1 76  ? 15.959  29.020  -9.387  1.00 23.65 ?  76  TYR   B CD1  1 
ATOM   1894 C CD2  . TYR   B 1 76  ? 18.347  29.087  -9.281  1.00 17.46 ?  76  TYR   B CD2  1 
ATOM   1895 C CE1  . TYR   B 1 76  ? 16.002  29.300  -10.741 1.00 22.82 ?  76  TYR   B CE1  1 
ATOM   1896 C CE2  . TYR   B 1 76  ? 18.403  29.382  -10.636 1.00 20.86 ?  76  TYR   B CE2  1 
ATOM   1897 C CZ   . TYR   B 1 76  ? 17.227  29.487  -11.362 1.00 29.22 ?  76  TYR   B CZ   1 
ATOM   1898 O OH   . TYR   B 1 76  ? 17.259  29.785  -12.712 1.00 27.91 ?  76  TYR   B OH   1 
ATOM   1899 N N    . HIS   B 1 77  ? 17.994  25.152  -7.738  1.00 12.91 ?  77  HIS   B N    1 
ATOM   1900 C CA   . HIS   B 1 77  ? 19.098  24.202  -7.896  1.00 13.21 ?  77  HIS   B CA   1 
ATOM   1901 C C    . HIS   B 1 77  ? 18.788  23.286  -9.065  1.00 14.93 ?  77  HIS   B C    1 
ATOM   1902 O O    . HIS   B 1 77  ? 17.657  22.809  -9.159  1.00 12.31 ?  77  HIS   B O    1 
ATOM   1903 C CB   . HIS   B 1 77  ? 19.288  23.365  -6.614  1.00 15.51 ?  77  HIS   B CB   1 
ATOM   1904 C CG   . HIS   B 1 77  ? 20.550  22.558  -6.606  1.00 14.15 ?  77  HIS   B CG   1 
ATOM   1905 N ND1  . HIS   B 1 77  ? 20.738  21.465  -7.426  1.00 15.52 ?  77  HIS   B ND1  1 
ATOM   1906 C CD2  . HIS   B 1 77  ? 21.709  22.723  -5.929  1.00 12.87 ?  77  HIS   B CD2  1 
ATOM   1907 C CE1  . HIS   B 1 77  ? 21.952  20.975  -7.238  1.00 11.81 ?  77  HIS   B CE1  1 
ATOM   1908 N NE2  . HIS   B 1 77  ? 22.559  21.714  -6.326  1.00 12.86 ?  77  HIS   B NE2  1 
ATOM   1909 N N    . PRO   B 1 78  ? 19.760  22.979  -9.930  1.00 15.08 ?  78  PRO   B N    1 
ATOM   1910 C CA   . PRO   B 1 78  ? 19.451  22.151  -11.108 1.00 18.16 ?  78  PRO   B CA   1 
ATOM   1911 C C    . PRO   B 1 78  ? 18.930  20.772  -10.772 1.00 18.77 ?  78  PRO   B C    1 
ATOM   1912 O O    . PRO   B 1 78  ? 18.265  20.161  -11.618 1.00 19.92 ?  78  PRO   B O    1 
ATOM   1913 C CB   . PRO   B 1 78  ? 20.790  22.059  -11.855 1.00 17.17 ?  78  PRO   B CB   1 
ATOM   1914 C CG   . PRO   B 1 78  ? 21.792  22.764  -11.056 1.00 20.48 ?  78  PRO   B CG   1 
ATOM   1915 C CD   . PRO   B 1 78  ? 21.168  23.407  -9.863  1.00 12.60 ?  78  PRO   B CD   1 
ATOM   1916 N N    . ASN   B 1 79  ? 19.215  20.237  -9.578  1.00 14.34 ?  79  ASN   B N    1 
ATOM   1917 C CA   . ASN   B 1 79  ? 18.783  18.886  -9.241  1.00 14.45 ?  79  ASN   B CA   1 
ATOM   1918 C C    . ASN   B 1 79  ? 17.535  18.836  -8.369  1.00 16.68 ?  79  ASN   B C    1 
ATOM   1919 O O    . ASN   B 1 79  ? 17.200  17.763  -7.857  1.00 18.61 ?  79  ASN   B O    1 
ATOM   1920 C CB   . ASN   B 1 79  ? 19.902  18.119  -8.526  1.00 15.95 ?  79  ASN   B CB   1 
ATOM   1921 C CG   . ASN   B 1 79  ? 21.130  17.921  -9.402  1.00 16.97 ?  79  ASN   B CG   1 
ATOM   1922 O OD1  . ASN   B 1 79  ? 21.843  18.883  -9.719  1.00 20.06 ?  79  ASN   B OD1  1 
ATOM   1923 N ND2  . ASN   B 1 79  ? 21.402  16.675  -9.775  1.00 22.14 ?  79  ASN   B ND2  1 
ATOM   1924 N N    . VAL   B 1 80  ? 16.841  19.950  -8.165  1.00 14.89 ?  80  VAL   B N    1 
ATOM   1925 C CA   . VAL   B 1 80  ? 15.703  19.955  -7.252  1.00 13.26 ?  80  VAL   B CA   1 
ATOM   1926 C C    . VAL   B 1 80  ? 14.486  20.522  -7.965  1.00 14.39 ?  80  VAL   B C    1 
ATOM   1927 O O    . VAL   B 1 80  ? 14.475  21.693  -8.361  1.00 14.26 ?  80  VAL   B O    1 
ATOM   1928 C CB   . VAL   B 1 80  ? 16.004  20.738  -5.966  1.00 13.13 ?  80  VAL   B CB   1 
ATOM   1929 C CG1  . VAL   B 1 80  ? 14.796  20.676  -5.008  1.00 11.92 ?  80  VAL   B CG1  1 
ATOM   1930 C CG2  . VAL   B 1 80  ? 17.304  20.202  -5.308  1.00 13.47 ?  80  VAL   B CG2  1 
ATOM   1931 N N    . ASP   B 1 81  ? 13.440  19.708  -8.077  1.00 15.05 ?  81  ASP   B N    1 
ATOM   1932 C CA   . ASP   B 1 81  ? 12.286  20.113  -8.865  1.00 16.50 ?  81  ASP   B CA   1 
ATOM   1933 C C    . ASP   B 1 81  ? 11.292  20.930  -8.021  1.00 20.71 ?  81  ASP   B C    1 
ATOM   1934 O O    . ASP   B 1 81  ? 11.534  21.271  -6.857  1.00 19.39 ?  81  ASP   B O    1 
ATOM   1935 C CB   . ASP   B 1 81  ? 11.688  18.875  -9.553  1.00 17.25 ?  81  ASP   B CB   1 
ATOM   1936 C CG   . ASP   B 1 81  ? 10.823  17.994  -8.644  1.00 27.01 ?  81  ASP   B CG   1 
ATOM   1937 O OD1  . ASP   B 1 81  ? 10.474  18.379  -7.514  1.00 17.07 ?  81  ASP   B OD1  1 
ATOM   1938 O OD2  . ASP   B 1 81  ? 10.452  16.885  -9.109  1.00 26.56 -1 81  ASP   B OD2  1 
ATOM   1939 N N    . LYS   B 1 82  ? 10.167  21.306  -8.631  1.00 20.27 ?  82  LYS   B N    1 
ATOM   1940 C CA   . LYS   B 1 82  ? 9.292   22.242  -7.944  1.00 15.83 ?  82  LYS   B CA   1 
ATOM   1941 C C    . LYS   B 1 82  ? 8.538   21.616  -6.785  1.00 21.18 ?  82  LYS   B C    1 
ATOM   1942 O O    . LYS   B 1 82  ? 7.840   22.336  -6.068  1.00 22.85 ?  82  LYS   B O    1 
ATOM   1943 C CB   . LYS   B 1 82  ? 8.285   22.852  -8.924  1.00 22.59 ?  82  LYS   B CB   1 
ATOM   1944 C CG   . LYS   B 1 82  ? 8.957   23.786  -9.910  1.00 24.51 ?  82  LYS   B CG   1 
ATOM   1945 C CD   . LYS   B 1 82  ? 8.012   24.244  -11.012 1.00 27.12 ?  82  LYS   B CD   1 
ATOM   1946 C CE   . LYS   B 1 82  ? 8.236   25.715  -11.318 1.00 37.17 ?  82  LYS   B CE   1 
ATOM   1947 N NZ   . LYS   B 1 82  ? 7.530   26.150  -12.558 1.00 32.98 ?  82  LYS   B NZ   1 
ATOM   1948 N N    . LEU   B 1 83  ? 8.637   20.307  -6.602  1.00 18.09 ?  83  LEU   B N    1 
ATOM   1949 C CA   . LEU   B 1 83  ? 8.065   19.654  -5.439  1.00 19.51 ?  83  LEU   B CA   1 
ATOM   1950 C C    . LEU   B 1 83  ? 9.127   19.276  -4.420  1.00 16.26 ?  83  LEU   B C    1 
ATOM   1951 O O    . LEU   B 1 83  ? 8.822   18.576  -3.453  1.00 16.92 ?  83  LEU   B O    1 
ATOM   1952 C CB   . LEU   B 1 83  ? 7.284   18.417  -5.873  1.00 23.64 ?  83  LEU   B CB   1 
ATOM   1953 C CG   . LEU   B 1 83  ? 6.117   18.768  -6.798  1.00 30.48 ?  83  LEU   B CG   1 
ATOM   1954 C CD1  . LEU   B 1 83  ? 5.679   17.543  -7.580  1.00 29.75 ?  83  LEU   B CD1  1 
ATOM   1955 C CD2  . LEU   B 1 83  ? 4.968   19.352  -6.000  1.00 28.77 ?  83  LEU   B CD2  1 
ATOM   1956 N N    . GLY   B 1 84  ? 10.367  19.710  -4.634  1.00 15.88 ?  84  GLY   B N    1 
ATOM   1957 C CA   . GLY   B 1 84  ? 11.454  19.360  -3.737  1.00 16.17 ?  84  GLY   B CA   1 
ATOM   1958 C C    . GLY   B 1 84  ? 12.114  18.022  -4.008  1.00 14.74 ?  84  GLY   B C    1 
ATOM   1959 O O    . GLY   B 1 84  ? 13.022  17.635  -3.265  1.00 14.96 ?  84  GLY   B O    1 
ATOM   1960 N N    . ARG   B 1 85  ? 11.673  17.284  -5.025  1.00 15.25 ?  85  ARG   B N    1 
ATOM   1961 C CA   . ARG   B 1 85  ? 12.273  15.992  -5.294  1.00 14.18 ?  85  ARG   B CA   1 
ATOM   1962 C C    . ARG   B 1 85  ? 13.658  16.189  -5.879  1.00 17.74 ?  85  ARG   B C    1 
ATOM   1963 O O    . ARG   B 1 85  ? 13.928  17.180  -6.568  1.00 18.54 ?  85  ARG   B O    1 
ATOM   1964 C CB   . ARG   B 1 85  ? 11.379  15.168  -6.224  1.00 18.73 ?  85  ARG   B CB   1 
ATOM   1965 C CG   . ARG   B 1 85  ? 9.985   15.027  -5.666  1.00 21.17 ?  85  ARG   B CG   1 
ATOM   1966 C CD   . ARG   B 1 85  ? 9.055   14.269  -6.611  1.00 30.39 ?  85  ARG   B CD   1 
ATOM   1967 N NE   . ARG   B 1 85  ? 8.734   15.057  -7.791  1.00 36.75 ?  85  ARG   B NE   1 
ATOM   1968 C CZ   . ARG   B 1 85  ? 7.589   14.967  -8.455  1.00 40.95 ?  85  ARG   B CZ   1 
ATOM   1969 N NH1  . ARG   B 1 85  ? 6.666   14.081  -8.122  1.00 46.13 ?  85  ARG   B NH1  1 
ATOM   1970 N NH2  . ARG   B 1 85  ? 7.367   15.784  -9.481  1.00 45.55 ?  85  ARG   B NH2  1 
ATOM   1971 N N    . ILE   B 1 86  ? 14.550  15.253  -5.569  1.00 14.23 ?  86  ILE   B N    1 
ATOM   1972 C CA   . ILE   B 1 86  ? 15.981  15.413  -5.800  1.00 15.32 ?  86  ILE   B CA   1 
ATOM   1973 C C    . ILE   B 1 86  ? 16.423  14.457  -6.896  1.00 19.89 ?  86  ILE   B C    1 
ATOM   1974 O O    . ILE   B 1 86  ? 16.293  13.233  -6.753  1.00 19.25 ?  86  ILE   B O    1 
ATOM   1975 C CB   . ILE   B 1 86  ? 16.769  15.180  -4.507  1.00 14.30 ?  86  ILE   B CB   1 
ATOM   1976 C CG1  . ILE   B 1 86  ? 16.250  16.154  -3.441  1.00 14.31 ?  86  ILE   B CG1  1 
ATOM   1977 C CG2  . ILE   B 1 86  ? 18.239  15.363  -4.753  1.00 17.28 ?  86  ILE   B CG2  1 
ATOM   1978 C CD1  . ILE   B 1 86  ? 16.743  15.837  -2.007  1.00 17.18 ?  86  ILE   B CD1  1 
ATOM   1979 N N    . CYS   B 1 87  ? 16.977  15.015  -7.969  1.00 21.41 ?  87  CYS   B N    1 
ATOM   1980 C CA   . CYS   B 1 87  ? 17.545  14.221  -9.063  1.00 23.27 ?  87  CYS   B CA   1 
ATOM   1981 C C    . CYS   B 1 87  ? 18.934  13.748  -8.666  1.00 24.00 ?  87  CYS   B C    1 
ATOM   1982 O O    . CYS   B 1 87  ? 19.947  14.418  -8.888  1.00 24.83 ?  87  CYS   B O    1 
ATOM   1983 C CB   . CYS   B 1 87  ? 17.596  15.013  -10.362 1.00 30.44 ?  87  CYS   B CB   1 
ATOM   1984 S SG   . CYS   B 1 87  ? 18.146  13.969  -11.745 1.00 42.24 ?  87  CYS   B SG   1 
ATOM   1985 N N    . LEU   B 1 88  ? 18.977  12.552  -8.089  1.00 19.69 ?  88  LEU   B N    1 
ATOM   1986 C CA   . LEU   B 1 88  ? 20.198  11.910  -7.647  1.00 19.15 ?  88  LEU   B CA   1 
ATOM   1987 C C    . LEU   B 1 88  ? 20.064  10.435  -7.979  1.00 15.87 ?  88  LEU   B C    1 
ATOM   1988 O O    . LEU   B 1 88  ? 19.073  9.802   -7.594  1.00 17.26 ?  88  LEU   B O    1 
ATOM   1989 C CB   . LEU   B 1 88  ? 20.399  12.134  -6.137  1.00 23.05 ?  88  LEU   B CB   1 
ATOM   1990 C CG   . LEU   B 1 88  ? 21.619  11.564  -5.442  1.00 23.16 ?  88  LEU   B CG   1 
ATOM   1991 C CD1  . LEU   B 1 88  ? 22.914  12.149  -6.038  1.00 25.85 ?  88  LEU   B CD1  1 
ATOM   1992 C CD2  . LEU   B 1 88  ? 21.546  11.862  -3.935  1.00 21.79 ?  88  LEU   B CD2  1 
ATOM   1993 N N    . ASP   B 1 89  ? 21.042  9.885   -8.696  1.00 18.26 ?  89  ASP   B N    1 
ATOM   1994 C CA   . ASP   B 1 89  ? 20.850  8.536   -9.222  1.00 18.83 ?  89  ASP   B CA   1 
ATOM   1995 C C    . ASP   B 1 89  ? 20.769  7.494   -8.110  1.00 17.21 ?  89  ASP   B C    1 
ATOM   1996 O O    . ASP   B 1 89  ? 20.045  6.505   -8.248  1.00 16.70 ?  89  ASP   B O    1 
ATOM   1997 C CB   . ASP   B 1 89  ? 21.941  8.175   -10.253 1.00 19.61 ?  89  ASP   B CB   1 
ATOM   1998 C CG   . ASP   B 1 89  ? 23.377  8.448   -9.773  1.00 30.31 ?  89  ASP   B CG   1 
ATOM   1999 O OD1  . ASP   B 1 89  ? 23.598  8.793   -8.590  1.00 26.31 ?  89  ASP   B OD1  1 
ATOM   2000 O OD2  . ASP   B 1 89  ? 24.303  8.273   -10.610 1.00 29.76 -1 89  ASP   B OD2  1 
ATOM   2001 N N    . ILE   B 1 90  ? 21.472  7.694   -6.994  1.00 16.89 ?  90  ILE   B N    1 
ATOM   2002 C CA   . ILE   B 1 90  ? 21.389  6.717   -5.913  1.00 13.62 ?  90  ILE   B CA   1 
ATOM   2003 C C    . ILE   B 1 90  ? 20.056  6.754   -5.162  1.00 15.75 ?  90  ILE   B C    1 
ATOM   2004 O O    . ILE   B 1 90  ? 19.809  5.898   -4.307  1.00 19.43 ?  90  ILE   B O    1 
ATOM   2005 C CB   . ILE   B 1 90  ? 22.567  6.858   -4.930  1.00 17.48 ?  90  ILE   B CB   1 
ATOM   2006 C CG1  . ILE   B 1 90  ? 22.661  8.261   -4.331  1.00 15.38 ?  90  ILE   B CG1  1 
ATOM   2007 C CG2  . ILE   B 1 90  ? 23.893  6.470   -5.589  1.00 18.38 ?  90  ILE   B CG2  1 
ATOM   2008 C CD1  . ILE   B 1 90  ? 23.491  8.263   -3.002  1.00 18.50 ?  90  ILE   B CD1  1 
ATOM   2009 N N    . LEU   B 1 91  ? 19.174  7.711   -5.473  1.00 14.47 ?  91  LEU   B N    1 
ATOM   2010 C CA   . LEU   B 1 91  ? 17.814  7.672   -4.935  1.00 13.56 ?  91  LEU   B CA   1 
ATOM   2011 C C    . LEU   B 1 91  ? 16.887  6.879   -5.832  1.00 17.27 ?  91  LEU   B C    1 
ATOM   2012 O O    . LEU   B 1 91  ? 15.707  6.698   -5.495  1.00 19.02 ?  91  LEU   B O    1 
ATOM   2013 C CB   . LEU   B 1 91  ? 17.248  9.085   -4.768  1.00 13.30 ?  91  LEU   B CB   1 
ATOM   2014 C CG   . LEU   B 1 91  ? 18.054  9.934   -3.796  1.00 15.63 ?  91  LEU   B CG   1 
ATOM   2015 C CD1  . LEU   B 1 91  ? 17.454  11.311  -3.643  1.00 15.62 ?  91  LEU   B CD1  1 
ATOM   2016 C CD2  . LEU   B 1 91  ? 18.123  9.222   -2.434  1.00 16.80 ?  91  LEU   B CD2  1 
ATOM   2017 N N    . LYS   B 1 92  ? 17.410  6.410   -6.962  1.00 17.97 ?  92  LYS   B N    1 
ATOM   2018 C CA   . LYS   B 1 92  ? 16.631  5.640   -7.917  1.00 19.68 ?  92  LYS   B CA   1 
ATOM   2019 C C    . LYS   B 1 92  ? 17.389  4.372   -8.275  1.00 24.39 ?  92  LYS   B C    1 
ATOM   2020 O O    . LYS   B 1 92  ? 17.630  3.521   -7.406  1.00 24.78 ?  92  LYS   B O    1 
ATOM   2021 C CB   . LYS   B 1 92  ? 16.328  6.485   -9.152  1.00 21.17 ?  92  LYS   B CB   1 
ATOM   2022 C CG   . LYS   B 1 92  ? 15.875  7.914   -8.852  1.00 34.98 ?  92  LYS   B CG   1 
ATOM   2023 C CD   . LYS   B 1 92  ? 15.555  8.668   -10.145 1.00 39.13 ?  92  LYS   B CD   1 
ATOM   2024 C CE   . LYS   B 1 92  ? 16.334  9.977   -10.267 1.00 39.86 ?  92  LYS   B CE   1 
ATOM   2025 N NZ   . LYS   B 1 92  ? 15.463  11.138  -10.632 1.00 43.37 ?  92  LYS   B NZ   1 
ATOM   2026 N N    . ASP   B 1 93  ? 17.797  4.243   -9.541  1.00 19.49 ?  93  ASP   B N    1 
ATOM   2027 C CA   . ASP   B 1 93  ? 18.285  2.949   -9.995  1.00 26.67 ?  93  ASP   B CA   1 
ATOM   2028 C C    . ASP   B 1 93  ? 19.692  2.646   -9.515  1.00 28.92 ?  93  ASP   B C    1 
ATOM   2029 O O    . ASP   B 1 93  ? 20.076  1.470   -9.501  1.00 22.84 ?  93  ASP   B O    1 
ATOM   2030 C CB   . ASP   B 1 93  ? 18.242  2.861   -11.521 1.00 28.88 ?  93  ASP   B CB   1 
ATOM   2031 C CG   . ASP   B 1 93  ? 18.874  4.054   -12.188 1.00 28.62 ?  93  ASP   B CG   1 
ATOM   2032 O OD1  . ASP   B 1 93  ? 18.343  5.178   -12.025 1.00 31.55 ?  93  ASP   B OD1  1 
ATOM   2033 O OD2  . ASP   B 1 93  ? 19.894  3.862   -12.895 1.00 28.99 -1 93  ASP   B OD2  1 
ATOM   2034 N N    . LYS   B 1 94  ? 20.472  3.654   -9.126  1.00 20.52 ?  94  LYS   B N    1 
ATOM   2035 C CA   . LYS   B 1 94  ? 21.827  3.379   -8.666  1.00 18.99 ?  94  LYS   B CA   1 
ATOM   2036 C C    . LYS   B 1 94  ? 21.909  3.139   -7.160  1.00 19.60 ?  94  LYS   B C    1 
ATOM   2037 O O    . LYS   B 1 94  ? 23.014  3.015   -6.624  1.00 18.64 ?  94  LYS   B O    1 
ATOM   2038 C CB   . LYS   B 1 94  ? 22.770  4.515   -9.072  1.00 24.46 ?  94  LYS   B CB   1 
ATOM   2039 C CG   . LYS   B 1 94  ? 23.076  4.583   -10.570 1.00 29.16 ?  94  LYS   B CG   1 
ATOM   2040 C CD   . LYS   B 1 94  ? 23.168  3.193   -11.180 1.00 37.03 ?  94  LYS   B CD   1 
ATOM   2041 C CE   . LYS   B 1 94  ? 24.303  3.111   -12.196 1.00 36.26 ?  94  LYS   B CE   1 
ATOM   2042 N NZ   . LYS   B 1 94  ? 23.869  3.546   -13.547 1.00 42.96 ?  94  LYS   B NZ   1 
ATOM   2043 N N    . TRP   B 1 95  ? 20.770  3.034   -6.469  1.00 17.60 ?  95  TRP   B N    1 
ATOM   2044 C CA   . TRP   B 1 95  ? 20.790  2.580   -5.089  1.00 16.77 ?  95  TRP   B CA   1 
ATOM   2045 C C    . TRP   B 1 95  ? 21.255  1.126   -5.018  1.00 20.78 ?  95  TRP   B C    1 
ATOM   2046 O O    . TRP   B 1 95  ? 21.041  0.336   -5.943  1.00 18.48 ?  95  TRP   B O    1 
ATOM   2047 C CB   . TRP   B 1 95  ? 19.389  2.720   -4.434  1.00 13.96 ?  95  TRP   B CB   1 
ATOM   2048 C CG   . TRP   B 1 95  ? 19.405  2.195   -3.019  1.00 15.37 ?  95  TRP   B CG   1 
ATOM   2049 C CD1  . TRP   B 1 95  ? 18.950  0.981   -2.582  1.00 15.52 ?  95  TRP   B CD1  1 
ATOM   2050 C CD2  . TRP   B 1 95  ? 19.969  2.847   -1.866  1.00 14.35 ?  95  TRP   B CD2  1 
ATOM   2051 N NE1  . TRP   B 1 95  ? 19.179  0.842   -1.238  1.00 16.40 ?  95  TRP   B NE1  1 
ATOM   2052 C CE2  . TRP   B 1 95  ? 19.801  1.969   -0.768  1.00 17.35 ?  95  TRP   B CE2  1 
ATOM   2053 C CE3  . TRP   B 1 95  ? 20.590  4.082   -1.656  1.00 14.79 ?  95  TRP   B CE3  1 
ATOM   2054 C CZ2  . TRP   B 1 95  ? 20.233  2.288   0.530   1.00 17.50 ?  95  TRP   B CZ2  1 
ATOM   2055 C CZ3  . TRP   B 1 95  ? 21.032  4.402   -0.351  1.00 15.57 ?  95  TRP   B CZ3  1 
ATOM   2056 C CH2  . TRP   B 1 95  ? 20.842  3.509   0.715   1.00 14.81 ?  95  TRP   B CH2  1 
ATOM   2057 N N    . SER   B 1 96  ? 21.934  0.783   -3.923  1.00 17.99 ?  96  SER   B N    1 
ATOM   2058 C CA   . SER   B 1 96  ? 22.230  -0.603  -3.590  1.00 20.05 ?  96  SER   B CA   1 
ATOM   2059 C C    . SER   B 1 96  ? 22.273  -0.734  -2.077  1.00 20.70 ?  96  SER   B C    1 
ATOM   2060 O O    . SER   B 1 96  ? 22.547  0.251   -1.380  1.00 17.50 ?  96  SER   B O    1 
ATOM   2061 C CB   . SER   B 1 96  ? 23.561  -1.072  -4.208  1.00 21.23 ?  96  SER   B CB   1 
ATOM   2062 O OG   . SER   B 1 96  ? 24.650  -0.537  -3.493  1.00 26.61 ?  96  SER   B OG   1 
ATOM   2063 N N    . PRO   B 1 97  ? 21.978  -1.920  -1.534  1.00 16.27 ?  97  PRO   B N    1 
ATOM   2064 C CA   . PRO   B 1 97  ? 21.967  -2.067  -0.074  1.00 19.68 ?  97  PRO   B CA   1 
ATOM   2065 C C    . PRO   B 1 97  ? 23.311  -1.803  0.550   1.00 17.30 ?  97  PRO   B C    1 
ATOM   2066 O O    . PRO   B 1 97  ? 23.382  -1.616  1.767   1.00 26.87 ?  97  PRO   B O    1 
ATOM   2067 C CB   . PRO   B 1 97  ? 21.522  -3.519  0.152   1.00 27.23 ?  97  PRO   B CB   1 
ATOM   2068 C CG   . PRO   B 1 97  ? 21.080  -4.032  -1.170  1.00 32.48 ?  97  PRO   B CG   1 
ATOM   2069 C CD   . PRO   B 1 97  ? 21.589  -3.149  -2.248  1.00 20.21 ?  97  PRO   B CD   1 
ATOM   2070 N N    . ALA   B 1 98  ? 24.377  -1.776  -0.243  1.00 21.45 ?  98  ALA   B N    1 
ATOM   2071 C CA   . ALA   B 1 98  ? 25.692  -1.445  0.289   1.00 26.50 ?  98  ALA   B CA   1 
ATOM   2072 C C    . ALA   B 1 98  ? 25.802  0.022   0.695   1.00 25.70 ?  98  ALA   B C    1 
ATOM   2073 O O    . ALA   B 1 98  ? 26.658  0.360   1.525   1.00 27.69 ?  98  ALA   B O    1 
ATOM   2074 C CB   . ALA   B 1 98  ? 26.768  -1.776  -0.745  1.00 28.43 ?  98  ALA   B CB   1 
ATOM   2075 N N    . LEU   B 1 99  ? 24.983  0.898   0.115   1.00 18.51 ?  99  LEU   B N    1 
ATOM   2076 C CA   . LEU   B 1 99  ? 25.017  2.306   0.477   1.00 16.76 ?  99  LEU   B CA   1 
ATOM   2077 C C    . LEU   B 1 99  ? 24.255  2.522   1.778   1.00 18.61 ?  99  LEU   B C    1 
ATOM   2078 O O    . LEU   B 1 99  ? 23.580  1.627   2.286   1.00 21.08 ?  99  LEU   B O    1 
ATOM   2079 C CB   . LEU   B 1 99  ? 24.420  3.165   -0.637  1.00 16.67 ?  99  LEU   B CB   1 
ATOM   2080 C CG   . LEU   B 1 99  ? 24.946  2.947   -2.045  1.00 16.94 ?  99  LEU   B CG   1 
ATOM   2081 C CD1  . LEU   B 1 99  ? 24.211  3.862   -3.002  1.00 18.06 ?  99  LEU   B CD1  1 
ATOM   2082 C CD2  . LEU   B 1 99  ? 26.450  3.173   -2.085  1.00 22.52 ?  99  LEU   B CD2  1 
ATOM   2083 N N    . GLN   B 1 100 ? 24.355  3.729   2.333   1.00 15.75 ?  100 GLN   B N    1 
ATOM   2084 C CA   . GLN   B 1 100 ? 23.648  3.977   3.578   1.00 19.71 ?  100 GLN   B CA   1 
ATOM   2085 C C    . GLN   B 1 100 ? 23.094  5.385   3.607   1.00 16.92 ?  100 GLN   B C    1 
ATOM   2086 O O    . GLN   B 1 100 ? 23.365  6.210   2.729   1.00 16.01 ?  100 GLN   B O    1 
ATOM   2087 C CB   . GLN   B 1 100 ? 24.537  3.764   4.798   1.00 23.93 ?  100 GLN   B CB   1 
ATOM   2088 C CG   . GLN   B 1 100 ? 25.977  3.984   4.527   1.00 28.10 ?  100 GLN   B CG   1 
ATOM   2089 C CD   . GLN   B 1 100 ? 26.825  3.583   5.703   1.00 39.15 ?  100 GLN   B CD   1 
ATOM   2090 O OE1  . GLN   B 1 100 ? 26.538  3.958   6.841   1.00 46.51 ?  100 GLN   B OE1  1 
ATOM   2091 N NE2  . GLN   B 1 100 ? 27.894  2.839   5.438   1.00 46.59 ?  100 GLN   B NE2  1 
ATOM   2092 N N    . ILE   B 1 101 ? 22.281  5.630   4.639   1.00 14.45 ?  101 ILE   B N    1 
ATOM   2093 C CA   . ILE   B 1 101 ? 21.678  6.946   4.826   1.00 13.02 ?  101 ILE   B CA   1 
ATOM   2094 C C    . ILE   B 1 101 ? 22.761  8.020   4.833   1.00 13.53 ?  101 ILE   B C    1 
ATOM   2095 O O    . ILE   B 1 101 ? 22.608  9.082   4.211   1.00 15.73 ?  101 ILE   B O    1 
ATOM   2096 C CB   . ILE   B 1 101 ? 20.839  6.960   6.121   1.00 14.95 ?  101 ILE   B CB   1 
ATOM   2097 C CG1  . ILE   B 1 101 ? 19.702  5.939   6.012   1.00 16.74 ?  101 ILE   B CG1  1 
ATOM   2098 C CG2  . ILE   B 1 101 ? 20.308  8.371   6.429   1.00 15.89 ?  101 ILE   B CG2  1 
ATOM   2099 C CD1  . ILE   B 1 101 ? 19.081  5.553   7.351   1.00 19.34 ?  101 ILE   B CD1  1 
ATOM   2100 N N    . ARG   B 1 102 ? 23.879  7.749   5.513   1.00 14.69 ?  102 ARG   B N    1 
ATOM   2101 C CA   . ARG   B 1 102 ? 24.937  8.748   5.605   1.00 14.54 ?  102 ARG   B CA   1 
ATOM   2102 C C    . ARG   B 1 102 ? 25.391  9.194   4.223   1.00 14.86 ?  102 ARG   B C    1 
ATOM   2103 O O    . ARG   B 1 102 ? 25.678  10.381  4.011   1.00 14.34 ?  102 ARG   B O    1 
ATOM   2104 C CB   . ARG   B 1 102 ? 26.115  8.207   6.431   1.00 14.37 ?  102 ARG   B CB   1 
ATOM   2105 C CG   . ARG   B 1 102 ? 27.273  9.180   6.563   1.00 23.75 ?  102 ARG   B CG   1 
ATOM   2106 C CD   . ARG   B 1 102 ? 28.431  8.517   7.292   1.00 24.12 ?  102 ARG   B CD   1 
ATOM   2107 N NE   . ARG   B 1 102 ? 27.896  7.771   8.425   1.00 35.33 ?  102 ARG   B NE   1 
ATOM   2108 C CZ   . ARG   B 1 102 ? 27.719  8.287   9.635   1.00 39.37 ?  102 ARG   B CZ   1 
ATOM   2109 N NH1  . ARG   B 1 102 ? 28.114  9.517   9.923   1.00 27.41 ?  102 ARG   B NH1  1 
ATOM   2110 N NH2  . ARG   B 1 102 ? 27.119  7.555   10.572  1.00 30.10 ?  102 ARG   B NH2  1 
ATOM   2111 N N    . THR   B 1 103 ? 25.487  8.251   3.275   1.00 12.88 ?  103 THR   B N    1 
ATOM   2112 C CA   . THR   B 1 103 ? 25.929  8.586   1.923   1.00 14.89 ?  103 THR   B CA   1 
ATOM   2113 C C    . THR   B 1 103 ? 24.916  9.466   1.197   1.00 13.53 ?  103 THR   B C    1 
ATOM   2114 O O    . THR   B 1 103 ? 25.302  10.362  0.443   1.00 13.37 ?  103 THR   B O    1 
ATOM   2115 C CB   . THR   B 1 103 ? 26.211  7.292   1.160   1.00 22.21 ?  103 THR   B CB   1 
ATOM   2116 O OG1  . THR   B 1 103 ? 27.207  6.565   1.890   1.00 27.88 ?  103 THR   B OG1  1 
ATOM   2117 C CG2  . THR   B 1 103 ? 26.759  7.567   -0.246  1.00 17.94 ?  103 THR   B CG2  1 
ATOM   2118 N N    . VAL   B 1 104 ? 23.619  9.243   1.428   1.00 13.06 ?  104 VAL   B N    1 
ATOM   2119 C CA   . VAL   B 1 104 ? 22.587  10.104  0.843   1.00 10.78 ?  104 VAL   B CA   1 
ATOM   2120 C C    . VAL   B 1 104 ? 22.710  11.523  1.394   1.00 13.15 ?  104 VAL   B C    1 
ATOM   2121 O O    . VAL   B 1 104 ? 22.670  12.511  0.649   1.00 13.54 ?  104 VAL   B O    1 
ATOM   2122 C CB   . VAL   B 1 104 ? 21.191  9.514   1.109   1.00 16.00 ?  104 VAL   B CB   1 
ATOM   2123 C CG1  . VAL   B 1 104 ? 20.102  10.489  0.682   1.00 13.22 ?  104 VAL   B CG1  1 
ATOM   2124 C CG2  . VAL   B 1 104 ? 21.048  8.137   0.373   1.00 14.78 ?  104 VAL   B CG2  1 
ATOM   2125 N N    . LEU   B 1 105 ? 22.874  11.637  2.713   1.00 11.78 ?  105 LEU   B N    1 
ATOM   2126 C CA   . LEU   B 1 105 ? 23.016  12.966  3.321   1.00 10.76 ?  105 LEU   B CA   1 
ATOM   2127 C C    . LEU   B 1 105 ? 24.258  13.679  2.777   1.00 9.71  ?  105 LEU   B C    1 
ATOM   2128 O O    . LEU   B 1 105 ? 24.196  14.855  2.381   1.00 11.34 ?  105 LEU   B O    1 
ATOM   2129 C CB   . LEU   B 1 105 ? 23.075  12.835  4.849   1.00 13.35 ?  105 LEU   B CB   1 
ATOM   2130 C CG   . LEU   B 1 105 ? 21.805  12.252  5.472   1.00 12.70 ?  105 LEU   B CG   1 
ATOM   2131 C CD1  . LEU   B 1 105 ? 22.012  12.069  6.984   1.00 16.54 ?  105 LEU   B CD1  1 
ATOM   2132 C CD2  . LEU   B 1 105 ? 20.623  13.163  5.186   1.00 15.75 ?  105 LEU   B CD2  1 
ATOM   2133 N N    . LEU   B 1 106 ? 25.403  12.980  2.747   1.00 12.09 ?  106 LEU   B N    1 
ATOM   2134 C CA   . LEU   B 1 106 ? 26.613  13.594  2.211   1.00 15.06 ?  106 LEU   B CA   1 
ATOM   2135 C C    . LEU   B 1 106 ? 26.434  13.983  0.746   1.00 12.19 ?  106 LEU   B C    1 
ATOM   2136 O O    . LEU   B 1 106 ? 26.949  15.022  0.306   1.00 12.80 ?  106 LEU   B O    1 
ATOM   2137 C CB   . LEU   B 1 106 ? 27.801  12.635  2.375   1.00 12.05 ?  106 LEU   B CB   1 
ATOM   2138 C CG   . LEU   B 1 106 ? 28.292  12.451  3.808   1.00 18.43 ?  106 LEU   B CG   1 
ATOM   2139 C CD1  . LEU   B 1 106 ? 29.135  11.159  3.968   1.00 17.08 ?  106 LEU   B CD1  1 
ATOM   2140 C CD2  . LEU   B 1 106 ? 29.090  13.690  4.246   1.00 19.62 ?  106 LEU   B CD2  1 
ATOM   2141 N N    . SER   B 1 107 ? 25.705  13.165  -0.027  1.00 12.17 ?  107 SER   B N    1 
ATOM   2142 C CA   . SER   B 1 107 ? 25.480  13.478  -1.436  1.00 14.07 ?  107 SER   B CA   1 
ATOM   2143 C C    . SER   B 1 107 ? 24.683  14.762  -1.596  1.00 11.25 ?  107 SER   B C    1 
ATOM   2144 O O    . SER   B 1 107 ? 24.960  15.569  -2.489  1.00 11.40 ?  107 SER   B O    1 
ATOM   2145 C CB   . SER   B 1 107 ? 24.769  12.305  -2.131  1.00 13.29 ?  107 SER   B CB   1 
ATOM   2146 O OG   . SER   B 1 107 ? 25.647  11.195  -2.223  1.00 14.13 ?  107 SER   B OG   1 
ATOM   2147 N N    . ILE   B 1 108 ? 23.653  14.957  -0.768  1.00 11.74 ?  108 ILE   B N    1 
ATOM   2148 C CA   . ILE   B 1 108 ? 22.873  16.186  -0.911  1.00 12.80 ?  108 ILE   B CA   1 
ATOM   2149 C C    . ILE   B 1 108 ? 23.712  17.405  -0.520  1.00 14.51 ?  108 ILE   B C    1 
ATOM   2150 O O    . ILE   B 1 108 ? 23.690  18.448  -1.197  1.00 13.61 ?  108 ILE   B O    1 
ATOM   2151 C CB   . ILE   B 1 108 ? 21.573  16.079  -0.095  1.00 11.36 ?  108 ILE   B CB   1 
ATOM   2152 C CG1  . ILE   B 1 108 ? 20.702  14.967  -0.684  1.00 13.88 ?  108 ILE   B CG1  1 
ATOM   2153 C CG2  . ILE   B 1 108 ? 20.806  17.411  -0.121  1.00 13.13 ?  108 ILE   B CG2  1 
ATOM   2154 C CD1  . ILE   B 1 108 ? 19.518  14.506  0.210   1.00 13.96 ?  108 ILE   B CD1  1 
ATOM   2155 N N    . GLN   B 1 109 ? 24.475  17.292  0.570   1.00 11.14 ?  109 GLN   B N    1 
ATOM   2156 C CA   . GLN   B 1 109 ? 25.393  18.380  0.927   1.00 11.43 ?  109 GLN   B CA   1 
ATOM   2157 C C    . GLN   B 1 109 ? 26.341  18.689  -0.230  1.00 13.66 ?  109 GLN   B C    1 
ATOM   2158 O O    . GLN   B 1 109 ? 26.617  19.859  -0.538  1.00 12.70 ?  109 GLN   B O    1 
ATOM   2159 C CB   . GLN   B 1 109 ? 26.175  17.991  2.177   1.00 12.05 ?  109 GLN   B CB   1 
ATOM   2160 C CG   . GLN   B 1 109 ? 27.088  19.086  2.772   1.00 13.84 ?  109 GLN   B CG   1 
ATOM   2161 C CD   . GLN   B 1 109 ? 27.727  18.606  4.068   1.00 16.81 ?  109 GLN   B CD   1 
ATOM   2162 O OE1  . GLN   B 1 109 ? 27.616  19.253  5.108   1.00 19.78 ?  109 GLN   B OE1  1 
ATOM   2163 N NE2  . GLN   B 1 109 ? 28.386  17.468  4.010   1.00 15.45 ?  109 GLN   B NE2  1 
ATOM   2164 N N    . ALA   B 1 110 ? 26.816  17.642  -0.906  1.00 11.09 ?  110 ALA   B N    1 
ATOM   2165 C CA   . ALA   B 1 110 ? 27.714  17.815  -2.042  1.00 11.40 ?  110 ALA   B CA   1 
ATOM   2166 C C    . ALA   B 1 110 ? 27.016  18.500  -3.221  1.00 13.03 ?  110 ALA   B C    1 
ATOM   2167 O O    . ALA   B 1 110 ? 27.630  19.313  -3.930  1.00 14.19 ?  110 ALA   B O    1 
ATOM   2168 C CB   . ALA   B 1 110 ? 28.272  16.448  -2.460  1.00 12.05 ?  110 ALA   B CB   1 
ATOM   2169 N N    . LEU   B 1 111 ? 25.742  18.181  -3.447  1.00 12.94 ?  111 LEU   B N    1 
ATOM   2170 C CA   . LEU   B 1 111 ? 24.977  18.876  -4.486  1.00 13.71 ?  111 LEU   B CA   1 
ATOM   2171 C C    . LEU   B 1 111 ? 24.935  20.374  -4.209  1.00 14.67 ?  111 LEU   B C    1 
ATOM   2172 O O    . LEU   B 1 111 ? 25.096  21.189  -5.128  1.00 16.44 ?  111 LEU   B O    1 
ATOM   2173 C CB   . LEU   B 1 111 ? 23.554  18.317  -4.567  1.00 13.13 ?  111 LEU   B CB   1 
ATOM   2174 C CG   . LEU   B 1 111 ? 23.282  16.944  -5.162  1.00 15.87 ?  111 LEU   B CG   1 
ATOM   2175 C CD1  . LEU   B 1 111 ? 21.777  16.680  -5.140  1.00 15.10 ?  111 LEU   B CD1  1 
ATOM   2176 C CD2  . LEU   B 1 111 ? 23.802  16.871  -6.596  1.00 21.57 ?  111 LEU   B CD2  1 
ATOM   2177 N N    . LEU   B 1 112 ? 24.703  20.754  -2.947  1.00 14.27 ?  112 LEU   B N    1 
ATOM   2178 C CA   . LEU   B 1 112 ? 24.653  22.182  -2.616  1.00 13.21 ?  112 LEU   B CA   1 
ATOM   2179 C C    . LEU   B 1 112 ? 26.035  22.844  -2.729  1.00 14.56 ?  112 LEU   B C    1 
ATOM   2180 O O    . LEU   B 1 112 ? 26.146  24.013  -3.126  1.00 13.26 ?  112 LEU   B O    1 
ATOM   2181 C CB   . LEU   B 1 112 ? 24.098  22.373  -1.209  1.00 14.02 ?  112 LEU   B CB   1 
ATOM   2182 C CG   . LEU   B 1 112 ? 22.688  21.831  -0.969  1.00 20.11 ?  112 LEU   B CG   1 
ATOM   2183 C CD1  . LEU   B 1 112 ? 22.279  21.975  0.492   1.00 24.89 ?  112 LEU   B CD1  1 
ATOM   2184 C CD2  . LEU   B 1 112 ? 21.748  22.580  -1.858  1.00 19.74 ?  112 LEU   B CD2  1 
ATOM   2185 N N    . SER   B 1 113 ? 27.099  22.118  -2.376  1.00 12.46 ?  113 SER   B N    1 
ATOM   2186 C CA   . SER   B 1 113 ? 28.433  22.719  -2.367  1.00 15.22 ?  113 SER   B CA   1 
ATOM   2187 C C    . SER   B 1 113 ? 28.885  23.177  -3.753  1.00 15.90 ?  113 SER   B C    1 
ATOM   2188 O O    . SER   B 1 113 ? 29.553  24.215  -3.879  1.00 19.45 ?  113 SER   B O    1 
ATOM   2189 C CB   . SER   B 1 113 ? 29.453  21.732  -1.789  1.00 17.58 ?  113 SER   B CB   1 
ATOM   2190 O OG   . SER   B 1 113 ? 30.764  22.280  -1.892  1.00 21.41 ?  113 SER   B OG   1 
ATOM   2191 N N    . ALA   B 1 114 ? 28.610  22.391  -4.796  1.00 13.65 ?  114 ALA   B N    1 
ATOM   2192 C CA   . ALA   B 1 114 ? 29.072  22.710  -6.151  1.00 17.38 ?  114 ALA   B CA   1 
ATOM   2193 C C    . ALA   B 1 114 ? 28.040  22.241  -7.166  1.00 15.48 ?  114 ALA   B C    1 
ATOM   2194 O O    . ALA   B 1 114 ? 28.190  21.192  -7.798  1.00 16.53 ?  114 ALA   B O    1 
ATOM   2195 C CB   . ALA   B 1 114 ? 30.443  22.083  -6.432  1.00 23.04 ?  114 ALA   B CB   1 
ATOM   2196 N N    . PRO   B 1 115 ? 26.957  22.997  -7.340  1.00 14.98 ?  115 PRO   B N    1 
ATOM   2197 C CA   . PRO   B 1 115 ? 25.901  22.577  -8.276  1.00 13.69 ?  115 PRO   B CA   1 
ATOM   2198 C C    . PRO   B 1 115 ? 26.473  22.272  -9.658  1.00 13.52 ?  115 PRO   B C    1 
ATOM   2199 O O    . PRO   B 1 115 ? 27.324  23.005  -10.178 1.00 19.15 ?  115 PRO   B O    1 
ATOM   2200 C CB   . PRO   B 1 115 ? 24.953  23.785  -8.307  1.00 17.08 ?  115 PRO   B CB   1 
ATOM   2201 C CG   . PRO   B 1 115 ? 25.250  24.541  -7.034  1.00 14.68 ?  115 PRO   B CG   1 
ATOM   2202 C CD   . PRO   B 1 115 ? 26.684  24.294  -6.697  1.00 16.87 ?  115 PRO   B CD   1 
ATOM   2203 N N    . ASN   B 1 116 ? 25.989  21.186  -10.254 1.00 14.89 ?  116 ASN   B N    1 
ATOM   2204 C CA   . ASN   B 1 116 ? 26.485  20.699  -11.545 1.00 16.70 ?  116 ASN   B CA   1 
ATOM   2205 C C    . ASN   B 1 116 ? 25.308  20.500  -12.499 1.00 18.59 ?  116 ASN   B C    1 
ATOM   2206 O O    . ASN   B 1 116 ? 24.549  19.522  -12.366 1.00 20.70 ?  116 ASN   B O    1 
ATOM   2207 C CB   . ASN   B 1 116 ? 27.268  19.402  -11.354 1.00 18.92 ?  116 ASN   B CB   1 
ATOM   2208 C CG   . ASN   B 1 116 ? 27.871  18.891  -12.644 1.00 23.44 ?  116 ASN   B CG   1 
ATOM   2209 O OD1  . ASN   B 1 116 ? 27.518  19.349  -13.736 1.00 23.71 ?  116 ASN   B OD1  1 
ATOM   2210 N ND2  . ASN   B 1 116 ? 28.768  17.915  -12.531 1.00 21.66 ?  116 ASN   B ND2  1 
ATOM   2211 N N    . PRO   B 1 117 ? 25.102  21.408  -13.458 1.00 18.23 ?  117 PRO   B N    1 
ATOM   2212 C CA   . PRO   B 1 117 ? 23.914  21.324  -14.314 1.00 21.67 ?  117 PRO   B CA   1 
ATOM   2213 C C    . PRO   B 1 117 ? 24.031  20.296  -15.424 1.00 23.53 ?  117 PRO   B C    1 
ATOM   2214 O O    . PRO   B 1 117 ? 23.140  20.216  -16.270 1.00 27.80 ?  117 PRO   B O    1 
ATOM   2215 C CB   . PRO   B 1 117 ? 23.804  22.749  -14.889 1.00 18.24 ?  117 PRO   B CB   1 
ATOM   2216 C CG   . PRO   B 1 117 ? 25.242  23.216  -14.958 1.00 23.03 ?  117 PRO   B CG   1 
ATOM   2217 C CD   . PRO   B 1 117 ? 25.911  22.612  -13.736 1.00 19.37 ?  117 PRO   B CD   1 
ATOM   2218 N N    . ASP   B 1 118 ? 25.108  19.521  -15.461 1.00 27.09 ?  118 ASP   B N    1 
ATOM   2219 C CA   . ASP   B 1 118 ? 25.132  18.388  -16.373 1.00 31.58 ?  118 ASP   B CA   1 
ATOM   2220 C C    . ASP   B 1 118 ? 24.431  17.171  -15.776 1.00 43.72 ?  118 ASP   B C    1 
ATOM   2221 O O    . ASP   B 1 118 ? 23.830  16.386  -16.516 1.00 49.64 ?  118 ASP   B O    1 
ATOM   2222 C CB   . ASP   B 1 118 ? 26.569  18.049  -16.728 1.00 29.88 ?  118 ASP   B CB   1 
ATOM   2223 C CG   . ASP   B 1 118 ? 26.782  17.953  -18.217 1.00 51.95 ?  118 ASP   B CG   1 
ATOM   2224 O OD1  . ASP   B 1 118 ? 25.774  17.961  -18.962 1.00 55.12 -1 118 ASP   B OD1  1 
ATOM   2225 O OD2  . ASP   B 1 118 ? 27.957  17.903  -18.640 1.00 54.79 ?  118 ASP   B OD2  1 
ATOM   2226 N N    . ASP   B 1 119 ? 24.482  17.010  -14.438 1.00 43.12 ?  119 ASP   B N    1 
ATOM   2227 C CA   . ASP   B 1 119 ? 23.884  15.882  -13.722 1.00 34.83 ?  119 ASP   B CA   1 
ATOM   2228 C C    . ASP   B 1 119 ? 22.462  15.583  -14.190 1.00 51.00 ?  119 ASP   B C    1 
ATOM   2229 O O    . ASP   B 1 119 ? 22.201  14.482  -14.695 1.00 58.09 ?  119 ASP   B O    1 
ATOM   2230 C CB   . ASP   B 1 119 ? 23.874  16.130  -12.207 1.00 41.90 ?  119 ASP   B CB   1 
ATOM   2231 C CG   . ASP   B 1 119 ? 25.205  15.814  -11.548 1.00 50.57 ?  119 ASP   B CG   1 
ATOM   2232 O OD1  . ASP   B 1 119 ? 26.213  15.691  -12.274 1.00 53.42 ?  119 ASP   B OD1  1 
ATOM   2233 O OD2  . ASP   B 1 119 ? 25.237  15.680  -10.299 1.00 51.65 -1 119 ASP   B OD2  1 
ATOM   2234 N N    . PRO   B 1 120 ? 21.506  16.521  -14.028 1.00 48.65 ?  120 PRO   B N    1 
ATOM   2235 C CA   . PRO   B 1 120 ? 20.112  16.232  -14.378 1.00 45.45 ?  120 PRO   B CA   1 
ATOM   2236 C C    . PRO   B 1 120 ? 19.824  16.437  -15.867 1.00 42.15 ?  120 PRO   B C    1 
ATOM   2237 O O    . PRO   B 1 120 ? 18.768  15.995  -16.319 1.00 55.75 ?  120 PRO   B O    1 
ATOM   2238 C CB   . PRO   B 1 120 ? 19.338  17.233  -13.524 1.00 39.35 ?  120 PRO   B CB   1 
ATOM   2239 C CG   . PRO   B 1 120 ? 20.251  18.433  -13.493 1.00 42.68 ?  120 PRO   B CG   1 
ATOM   2240 C CD   . PRO   B 1 120 ? 21.669  17.902  -13.532 1.00 35.73 ?  120 PRO   B CD   1 
ATOM   2241 N N    . ALA   B 1 122 ? 17.837  17.562  -17.957 1.00 38.86 ?  122 ALA   B N    1 
ATOM   2242 C CA   . ALA   B 1 122 ? 17.298  18.677  -18.730 1.00 32.60 ?  122 ALA   B CA   1 
ATOM   2243 C C    . ALA   B 1 122 ? 16.116  19.325  -18.013 1.00 29.78 ?  122 ALA   B C    1 
ATOM   2244 O O    . ALA   B 1 122 ? 15.094  18.685  -17.788 1.00 33.64 ?  122 ALA   B O    1 
ATOM   2245 C CB   . ALA   B 1 122 ? 16.884  18.208  -20.120 1.00 36.95 ?  122 ALA   B CB   1 
ATOM   2246 N N    . ASN   B 1 123 ? 16.277  20.595  -17.651 1.00 27.30 ?  123 ASN   B N    1 
ATOM   2247 C CA   . ASN   B 1 123 ? 15.238  21.382  -16.999 1.00 23.65 ?  123 ASN   B CA   1 
ATOM   2248 C C    . ASN   B 1 123 ? 15.657  22.845  -17.074 1.00 23.41 ?  123 ASN   B C    1 
ATOM   2249 O O    . ASN   B 1 123 ? 16.804  23.165  -17.402 1.00 22.94 ?  123 ASN   B O    1 
ATOM   2250 C CB   . ASN   B 1 123 ? 14.998  20.920  -15.548 1.00 24.72 ?  123 ASN   B CB   1 
ATOM   2251 C CG   . ASN   B 1 123 ? 16.205  21.155  -14.637 1.00 19.70 ?  123 ASN   B CG   1 
ATOM   2252 O OD1  . ASN   B 1 123 ? 16.562  22.292  -14.368 1.00 22.25 ?  123 ASN   B OD1  1 
ATOM   2253 N ND2  . ASN   B 1 123 ? 16.834  20.073  -14.176 1.00 20.90 ?  123 ASN   B ND2  1 
ATOM   2254 N N    . ASP   B 1 124 ? 14.692  23.727  -16.781 1.00 24.82 ?  124 ASP   B N    1 
ATOM   2255 C CA   . ASP   B 1 124 ? 14.871  25.167  -16.937 1.00 22.29 ?  124 ASP   B CA   1 
ATOM   2256 C C    . ASP   B 1 124 ? 16.062  25.678  -16.133 1.00 24.96 ?  124 ASP   B C    1 
ATOM   2257 O O    . ASP   B 1 124 ? 16.791  26.567  -16.589 1.00 22.06 ?  124 ASP   B O    1 
ATOM   2258 C CB   . ASP   B 1 124 ? 13.590  25.875  -16.480 1.00 24.79 ?  124 ASP   B CB   1 
ATOM   2259 C CG   . ASP   B 1 124 ? 12.513  25.936  -17.569 1.00 41.52 ?  124 ASP   B CG   1 
ATOM   2260 O OD1  . ASP   B 1 124 ? 12.646  25.235  -18.604 1.00 32.75 ?  124 ASP   B OD1  1 
ATOM   2261 O OD2  . ASP   B 1 124 ? 11.485  26.621  -17.340 1.00 38.69 -1 124 ASP   B OD2  1 
ATOM   2262 N N    . VAL   B 1 125 ? 16.245  25.165  -14.906 1.00 20.96 ?  125 VAL   B N    1 
ATOM   2263 C CA   . VAL   B 1 125 ? 17.318  25.666  -14.051 1.00 18.96 ?  125 VAL   B CA   1 
ATOM   2264 C C    . VAL   B 1 125 ? 18.677  25.220  -14.579 1.00 16.74 ?  125 VAL   B C    1 
ATOM   2265 O O    . VAL   B 1 125 ? 19.620  26.008  -14.640 1.00 19.65 ?  125 VAL   B O    1 
ATOM   2266 C CB   . VAL   B 1 125 ? 17.109  25.221  -12.590 1.00 21.20 ?  125 VAL   B CB   1 
ATOM   2267 C CG1  . VAL   B 1 125 ? 18.281  25.667  -11.734 1.00 18.41 ?  125 VAL   B CG1  1 
ATOM   2268 C CG2  . VAL   B 1 125 ? 15.808  25.777  -12.051 1.00 20.71 ?  125 VAL   B CG2  1 
ATOM   2269 N N    . ALA   B 1 126 ? 18.808  23.946  -14.940 1.00 20.40 ?  126 ALA   B N    1 
ATOM   2270 C CA   . ALA   B 1 126 ? 20.064  23.482  -15.522 1.00 17.32 ?  126 ALA   B CA   1 
ATOM   2271 C C    . ALA   B 1 126 ? 20.389  24.229  -16.817 1.00 21.11 ?  126 ALA   B C    1 
ATOM   2272 O O    . ALA   B 1 126 ? 21.547  24.592  -17.061 1.00 19.04 ?  126 ALA   B O    1 
ATOM   2273 C CB   . ALA   B 1 126 ? 19.988  21.973  -15.761 1.00 21.95 ?  126 ALA   B CB   1 
ATOM   2274 N N    . GLU   B 1 127 ? 19.378  24.481  -17.659 1.00 25.54 ?  127 GLU   B N    1 
ATOM   2275 C CA   . GLU   B 1 127 ? 19.634  25.233  -18.892 1.00 23.55 ?  127 GLU   B CA   1 
ATOM   2276 C C    . GLU   B 1 127 ? 20.077  26.655  -18.578 1.00 23.15 ?  127 GLU   B C    1 
ATOM   2277 O O    . GLU   B 1 127 ? 21.021  27.168  -19.186 1.00 22.11 ?  127 GLU   B O    1 
ATOM   2278 C CB   . GLU   B 1 127 ? 18.392  25.222  -19.804 1.00 23.92 ?  127 GLU   B CB   1 
ATOM   2279 C CG   . GLU   B 1 127 ? 18.679  25.424  -21.320 1.00 33.84 ?  127 GLU   B CG   1 
ATOM   2280 C CD   . GLU   B 1 127 ? 17.416  25.721  -22.125 1.00 33.16 ?  127 GLU   B CD   1 
ATOM   2281 O OE1  . GLU   B 1 127 ? 17.374  26.726  -22.879 1.00 31.61 ?  127 GLU   B OE1  1 
ATOM   2282 O OE2  . GLU   B 1 127 ? 16.464  24.922  -22.005 1.00 27.96 -1 127 GLU   B OE2  1 
ATOM   2283 N N    . GLN   B 1 128 ? 19.433  27.300  -17.604 1.00 20.83 ?  128 GLN   B N    1 
ATOM   2284 C CA   . GLN   B 1 128 ? 19.873  28.635  -17.227 1.00 18.77 ?  128 GLN   B CA   1 
ATOM   2285 C C    . GLN   B 1 128 ? 21.286  28.609  -16.659 1.00 22.95 ?  128 GLN   B C    1 
ATOM   2286 O O    . GLN   B 1 128 ? 22.069  29.539  -16.872 1.00 21.85 ?  128 GLN   B O    1 
ATOM   2287 C CB   . GLN   B 1 128 ? 18.891  29.237  -16.215 1.00 22.89 ?  128 GLN   B CB   1 
ATOM   2288 C CG   . GLN   B 1 128 ? 19.324  30.565  -15.669 1.00 23.28 ?  128 GLN   B CG   1 
ATOM   2289 C CD   . GLN   B 1 128 ? 19.083  31.702  -16.638 1.00 36.44 ?  128 GLN   B CD   1 
ATOM   2290 O OE1  . GLN   B 1 128 ? 18.800  31.481  -17.821 1.00 32.54 ?  128 GLN   B OE1  1 
ATOM   2291 N NE2  . GLN   B 1 128 ? 19.184  32.934  -16.139 1.00 35.12 ?  128 GLN   B NE2  1 
ATOM   2292 N N    . TRP   B 1 129 ? 21.624  27.556  -15.915 1.00 19.51 ?  129 TRP   B N    1 
ATOM   2293 C CA   . TRP   B 1 129 ? 22.954  27.462  -15.324 1.00 17.89 ?  129 TRP   B CA   1 
ATOM   2294 C C    . TRP   B 1 129 ? 24.027  27.259  -16.387 1.00 17.16 ?  129 TRP   B C    1 
ATOM   2295 O O    . TRP   B 1 129 ? 25.157  27.736  -16.219 1.00 18.43 ?  129 TRP   B O    1 
ATOM   2296 C CB   . TRP   B 1 129 ? 22.989  26.314  -14.302 1.00 19.28 ?  129 TRP   B CB   1 
ATOM   2297 C CG   . TRP   B 1 129 ? 23.852  26.558  -13.085 1.00 16.58 ?  129 TRP   B CG   1 
ATOM   2298 C CD1  . TRP   B 1 129 ? 25.226  26.589  -13.038 1.00 20.20 ?  129 TRP   B CD1  1 
ATOM   2299 C CD2  . TRP   B 1 129 ? 23.403  26.805  -11.745 1.00 17.11 ?  129 TRP   B CD2  1 
ATOM   2300 N NE1  . TRP   B 1 129 ? 25.652  26.833  -11.746 1.00 23.44 ?  129 TRP   B NE1  1 
ATOM   2301 C CE2  . TRP   B 1 129 ? 24.553  26.960  -10.937 1.00 15.35 ?  129 TRP   B CE2  1 
ATOM   2302 C CE3  . TRP   B 1 129 ? 22.137  26.885  -11.141 1.00 16.86 ?  129 TRP   B CE3  1 
ATOM   2303 C CZ2  . TRP   B 1 129 ? 24.480  27.222  -9.562  1.00 17.14 ?  129 TRP   B CZ2  1 
ATOM   2304 C CZ3  . TRP   B 1 129 ? 22.069  27.145  -9.770  1.00 19.68 ?  129 TRP   B CZ3  1 
ATOM   2305 C CH2  . TRP   B 1 129 ? 23.231  27.306  -9.000  1.00 17.77 ?  129 TRP   B CH2  1 
ATOM   2306 N N    . LYS   B 1 130 ? 23.691  26.556  -17.475 1.00 19.54 ?  130 LYS   B N    1 
ATOM   2307 C CA   . LYS   B 1 130 ? 24.638  26.387  -18.582 1.00 18.33 ?  130 LYS   B CA   1 
ATOM   2308 C C    . LYS   B 1 130 ? 24.741  27.638  -19.460 1.00 22.43 ?  130 LYS   B C    1 
ATOM   2309 O O    . LYS   B 1 130 ? 25.843  28.007  -19.877 1.00 26.95 ?  130 LYS   B O    1 
ATOM   2310 C CB   . LYS   B 1 130 ? 24.249  25.194  -19.456 1.00 22.54 ?  130 LYS   B CB   1 
ATOM   2311 C CG   . LYS   B 1 130 ? 24.377  23.839  -18.797 1.00 23.98 ?  130 LYS   B CG   1 
ATOM   2312 C CD   . LYS   B 1 130 ? 23.552  22.824  -19.570 1.00 34.92 ?  130 LYS   B CD   1 
ATOM   2313 C CE   . LYS   B 1 130 ? 23.800  21.421  -19.074 1.00 35.84 ?  130 LYS   B CE   1 
ATOM   2314 N NZ   . LYS   B 1 130 ? 22.645  20.521  -19.364 1.00 37.01 ?  130 LYS   B NZ   1 
ATOM   2315 N N    . THR   B 1 131 ? 23.618  28.303  -19.755 1.00 21.21 ?  131 THR   B N    1 
ATOM   2316 C CA   . THR   B 1 131 ? 23.637  29.426  -20.694 1.00 22.59 ?  131 THR   B CA   1 
ATOM   2317 C C    . THR   B 1 131 ? 24.008  30.751  -20.048 1.00 26.31 ?  131 THR   B C    1 
ATOM   2318 O O    . THR   B 1 131 ? 24.612  31.607  -20.706 1.00 23.78 ?  131 THR   B O    1 
ATOM   2319 C CB   . THR   B 1 131 ? 22.278  29.595  -21.380 1.00 26.78 ?  131 THR   B CB   1 
ATOM   2320 O OG1  . THR   B 1 131 ? 21.428  30.381  -20.540 1.00 39.72 ?  131 THR   B OG1  1 
ATOM   2321 C CG2  . THR   B 1 131 ? 21.609  28.245  -21.661 1.00 23.03 ?  131 THR   B CG2  1 
ATOM   2322 N N    . ASN   B 1 132 ? 23.636  30.957  -18.778 1.00 23.48 ?  132 ASN   B N    1 
ATOM   2323 C CA   . ASN   B 1 132 ? 23.837  32.223  -18.076 1.00 23.99 ?  132 ASN   B CA   1 
ATOM   2324 C C    . ASN   B 1 132 ? 24.220  31.873  -16.631 1.00 20.30 ?  132 ASN   B C    1 
ATOM   2325 O O    . ASN   B 1 132 ? 23.439  32.076  -15.695 1.00 23.33 ?  132 ASN   B O    1 
ATOM   2326 C CB   . ASN   B 1 132 ? 22.578  33.104  -18.112 1.00 24.27 ?  132 ASN   B CB   1 
ATOM   2327 C CG   . ASN   B 1 132 ? 22.170  33.527  -19.526 1.00 34.13 ?  132 ASN   B CG   1 
ATOM   2328 O OD1  . ASN   B 1 132 ? 21.027  33.304  -19.949 1.00 43.71 ?  132 ASN   B OD1  1 
ATOM   2329 N ND2  . ASN   B 1 132 ? 23.084  34.174  -20.242 1.00 38.95 ?  132 ASN   B ND2  1 
ATOM   2330 N N    . GLU   B 1 133 ? 25.428  31.326  -16.457 1.00 22.21 ?  133 GLU   B N    1 
ATOM   2331 C CA   . GLU   B 1 133 ? 25.839  30.810  -15.152 1.00 25.23 ?  133 GLU   B CA   1 
ATOM   2332 C C    . GLU   B 1 133 ? 25.832  31.902  -14.076 1.00 25.81 ?  133 GLU   B C    1 
ATOM   2333 O O    . GLU   B 1 133 ? 25.407  31.662  -12.933 1.00 20.86 ?  133 GLU   B O    1 
ATOM   2334 C CB   . GLU   B 1 133 ? 27.225  30.160  -15.268 1.00 22.55 ?  133 GLU   B CB   1 
ATOM   2335 C CG   . GLU   B 1 133 ? 27.836  29.767  -13.938 1.00 22.59 ?  133 GLU   B CG   1 
ATOM   2336 C CD   . GLU   B 1 133 ? 29.243  29.198  -14.053 1.00 29.85 ?  133 GLU   B CD   1 
ATOM   2337 O OE1  . GLU   B 1 133 ? 29.804  29.188  -15.169 1.00 32.18 ?  133 GLU   B OE1  1 
ATOM   2338 O OE2  . GLU   B 1 133 ? 29.786  28.755  -13.018 1.00 34.38 -1 133 GLU   B OE2  1 
ATOM   2339 N N    . ALA   B 1 134 ? 26.309  33.108  -14.408 1.00 24.06 ?  134 ALA   B N    1 
ATOM   2340 C CA   . ALA   B 1 134 ? 26.355  34.168  -13.403 1.00 19.91 ?  134 ALA   B CA   1 
ATOM   2341 C C    . ALA   B 1 134 ? 24.955  34.524  -12.907 1.00 22.70 ?  134 ALA   B C    1 
ATOM   2342 O O    . ALA   B 1 134 ? 24.743  34.729  -11.702 1.00 23.99 ?  134 ALA   B O    1 
ATOM   2343 C CB   . ALA   B 1 134 ? 27.053  35.405  -13.968 1.00 31.37 ?  134 ALA   B CB   1 
ATOM   2344 N N    . GLN   B 1 135 ? 23.980  34.590  -13.818 1.00 22.16 ?  135 GLN   B N    1 
ATOM   2345 C CA   . GLN   B 1 135 ? 22.610  34.873  -13.396 1.00 22.30 ?  135 GLN   B CA   1 
ATOM   2346 C C    . GLN   B 1 135 ? 22.032  33.732  -12.565 1.00 23.97 ?  135 GLN   B C    1 
ATOM   2347 O O    . GLN   B 1 135 ? 21.305  33.976  -11.595 1.00 21.96 ?  135 GLN   B O    1 
ATOM   2348 C CB   . GLN   B 1 135 ? 21.714  35.145  -14.603 1.00 26.19 ?  135 GLN   B CB   1 
ATOM   2349 C CG   . GLN   B 1 135 ? 20.258  35.453  -14.228 1.00 33.32 ?  135 GLN   B CG   1 
ATOM   2350 C CD   . GLN   B 1 135 ? 20.115  36.636  -13.269 1.00 38.90 ?  135 GLN   B CD   1 
ATOM   2351 O OE1  . GLN   B 1 135 ? 19.769  36.472  -12.086 1.00 32.66 ?  135 GLN   B OE1  1 
ATOM   2352 N NE2  . GLN   B 1 135 ? 20.374  37.836  -13.779 1.00 27.23 ?  135 GLN   B NE2  1 
ATOM   2353 N N    . ALA   B 1 136 ? 22.305  32.481  -12.954 1.00 19.53 ?  136 ALA   B N    1 
ATOM   2354 C CA   . ALA   B 1 136 ? 21.799  31.344  -12.191 1.00 16.50 ?  136 ALA   B CA   1 
ATOM   2355 C C    . ALA   B 1 136 ? 22.334  31.364  -10.764 1.00 17.55 ?  136 ALA   B C    1 
ATOM   2356 O O    . ALA   B 1 136 ? 21.581  31.150  -9.801  1.00 19.09 ?  136 ALA   B O    1 
ATOM   2357 C CB   . ALA   B 1 136 ? 22.172  30.035  -12.896 1.00 18.67 ?  136 ALA   B CB   1 
ATOM   2358 N N    . ILE   B 1 137 ? 23.637  31.612  -10.609 1.00 17.45 ?  137 ILE   B N    1 
ATOM   2359 C CA   . ILE   B 1 137 ? 24.223  31.734  -9.275  1.00 14.65 ?  137 ILE   B CA   1 
ATOM   2360 C C    . ILE   B 1 137 ? 23.570  32.882  -8.507  1.00 20.44 ?  137 ILE   B C    1 
ATOM   2361 O O    . ILE   B 1 137 ? 23.276  32.757  -7.307  1.00 18.63 ?  137 ILE   B O    1 
ATOM   2362 C CB   . ILE   B 1 137 ? 25.750  31.914  -9.366  1.00 16.73 ?  137 ILE   B CB   1 
ATOM   2363 C CG1  . ILE   B 1 137 ? 26.403  30.628  -9.882  1.00 18.03 ?  137 ILE   B CG1  1 
ATOM   2364 C CG2  . ILE   B 1 137 ? 26.310  32.270  -8.013  1.00 17.16 ?  137 ILE   B CG2  1 
ATOM   2365 C CD1  . ILE   B 1 137 ? 27.850  30.824  -10.308 1.00 20.91 ?  137 ILE   B CD1  1 
ATOM   2366 N N    . GLU   B 1 138 ? 23.337  34.026  -9.175  1.00 18.43 ?  138 GLU   B N    1 
ATOM   2367 C CA   . GLU   B 1 138 ? 22.700  35.148  -8.479  1.00 18.54 ?  138 GLU   B CA   1 
ATOM   2368 C C    . GLU   B 1 138 ? 21.313  34.756  -7.976  1.00 17.39 ?  138 GLU   B C    1 
ATOM   2369 O O    . GLU   B 1 138 ? 20.931  35.080  -6.840  1.00 18.94 ?  138 GLU   B O    1 
ATOM   2370 C CB   . GLU   B 1 138 ? 22.590  36.378  -9.391  1.00 22.48 ?  138 GLU   B CB   1 
ATOM   2371 C CG   . GLU   B 1 138 ? 21.742  37.499  -8.750  1.00 28.53 ?  138 GLU   B CG   1 
ATOM   2372 C CD   . GLU   B 1 138 ? 21.506  38.712  -9.643  1.00 37.69 ?  138 GLU   B CD   1 
ATOM   2373 O OE1  . GLU   B 1 138 ? 22.452  39.495  -9.864  1.00 31.43 ?  138 GLU   B OE1  1 
ATOM   2374 O OE2  . GLU   B 1 138 ? 20.352  38.883  -10.106 1.00 32.99 -1 138 GLU   B OE2  1 
ATOM   2375 N N    . THR   B 1 139 ? 20.539  34.080  -8.820  1.00 15.82 ?  139 THR   B N    1 
ATOM   2376 C CA   . THR   B 1 139 ? 19.207  33.650  -8.413  1.00 19.46 ?  139 THR   B CA   1 
ATOM   2377 C C    . THR   B 1 139 ? 19.283  32.663  -7.254  1.00 17.49 ?  139 THR   B C    1 
ATOM   2378 O O    . THR   B 1 139 ? 18.452  32.706  -6.332  1.00 14.96 ?  139 THR   B O    1 
ATOM   2379 C CB   . THR   B 1 139 ? 18.461  33.036  -9.603  1.00 22.38 ?  139 THR   B CB   1 
ATOM   2380 O OG1  . THR   B 1 139 ? 18.355  34.014  -10.656 1.00 21.93 ?  139 THR   B OG1  1 
ATOM   2381 C CG2  . THR   B 1 139 ? 17.060  32.571  -9.186  1.00 17.96 ?  139 THR   B CG2  1 
ATOM   2382 N N    . ALA   B 1 140 ? 20.248  31.738  -7.299  1.00 15.39 ?  140 ALA   B N    1 
ATOM   2383 C CA   . ALA   B 1 140 ? 20.357  30.774  -6.205  1.00 15.45 ?  140 ALA   B CA   1 
ATOM   2384 C C    . ALA   B 1 140 ? 20.661  31.484  -4.890  1.00 13.17 ?  140 ALA   B C    1 
ATOM   2385 O O    . ALA   B 1 140 ? 20.091  31.140  -3.846  1.00 16.09 ?  140 ALA   B O    1 
ATOM   2386 C CB   . ALA   B 1 140 ? 21.429  29.724  -6.518  1.00 14.43 ?  140 ALA   B CB   1 
ATOM   2387 N N    . ARG   B 1 141 ? 21.546  32.499  -4.922  1.00 13.94 ?  141 ARG   B N    1 
ATOM   2388 C CA   . ARG   B 1 141 ? 21.812  33.275  -3.710  1.00 13.53 ?  141 ARG   B CA   1 
ATOM   2389 C C    . ARG   B 1 141 ? 20.568  34.038  -3.261  1.00 15.41 ?  141 ARG   B C    1 
ATOM   2390 O O    . ARG   B 1 141 ? 20.296  34.157  -2.059  1.00 15.24 ?  141 ARG   B O    1 
ATOM   2391 C CB   . ARG   B 1 141 ? 22.950  34.269  -3.948  1.00 16.31 ?  141 ARG   B CB   1 
ATOM   2392 C CG   . ARG   B 1 141 ? 24.327  33.638  -4.131  1.00 15.70 ?  141 ARG   B CG   1 
ATOM   2393 C CD   . ARG   B 1 141 ? 25.371  34.731  -4.437  1.00 18.30 ?  141 ARG   B CD   1 
ATOM   2394 N NE   . ARG   B 1 141 ? 26.632  34.133  -4.854  1.00 24.67 ?  141 ARG   B NE   1 
ATOM   2395 C CZ   . ARG   B 1 141 ? 27.434  33.457  -4.042  1.00 32.17 ?  141 ARG   B CZ   1 
ATOM   2396 N NH1  . ARG   B 1 141 ? 27.164  33.328  -2.748  1.00 28.58 ?  141 ARG   B NH1  1 
ATOM   2397 N NH2  . ARG   B 1 141 ? 28.538  32.902  -4.535  1.00 39.04 ?  141 ARG   B NH2  1 
ATOM   2398 N N    . ALA   B 1 142 ? 19.843  34.616  -4.222  1.00 14.51 ?  142 ALA   B N    1 
ATOM   2399 C CA   . ALA   B 1 142 ? 18.658  35.403  -3.898  1.00 14.44 ?  142 ALA   B CA   1 
ATOM   2400 C C    . ALA   B 1 142 ? 17.593  34.547  -3.233  1.00 15.30 ?  142 ALA   B C    1 
ATOM   2401 O O    . ALA   B 1 142 ? 16.978  34.975  -2.251  1.00 17.01 ?  142 ALA   B O    1 
ATOM   2402 C CB   . ALA   B 1 142 ? 18.108  36.064  -5.169  1.00 18.73 ?  142 ALA   B CB   1 
ATOM   2403 N N    . TRP   B 1 143 ? 17.362  33.332  -3.749  1.00 14.64 ?  143 TRP   B N    1 
ATOM   2404 C CA   . TRP   B 1 143 ? 16.402  32.423  -3.122  1.00 13.66 ?  143 TRP   B CA   1 
ATOM   2405 C C    . TRP   B 1 143 ? 16.907  31.910  -1.780  1.00 15.34 ?  143 TRP   B C    1 
ATOM   2406 O O    . TRP   B 1 143 ? 16.098  31.642  -0.886  1.00 14.35 ?  143 TRP   B O    1 
ATOM   2407 C CB   . TRP   B 1 143 ? 16.085  31.234  -4.029  1.00 13.00 ?  143 TRP   B CB   1 
ATOM   2408 C CG   . TRP   B 1 143 ? 15.165  31.542  -5.180  1.00 17.06 ?  143 TRP   B CG   1 
ATOM   2409 C CD1  . TRP   B 1 143 ? 15.065  32.720  -5.866  1.00 16.43 ?  143 TRP   B CD1  1 
ATOM   2410 C CD2  . TRP   B 1 143 ? 14.262  30.631  -5.802  1.00 15.58 ?  143 TRP   B CD2  1 
ATOM   2411 N NE1  . TRP   B 1 143 ? 14.124  32.601  -6.875  1.00 20.24 ?  143 TRP   B NE1  1 
ATOM   2412 C CE2  . TRP   B 1 143 ? 13.628  31.322  -6.863  1.00 19.53 ?  143 TRP   B CE2  1 
ATOM   2413 C CE3  . TRP   B 1 143 ? 13.928  29.298  -5.572  1.00 13.02 ?  143 TRP   B CE3  1 
ATOM   2414 C CZ2  . TRP   B 1 143 ? 12.661  30.715  -7.680  1.00 22.52 ?  143 TRP   B CZ2  1 
ATOM   2415 C CZ3  . TRP   B 1 143 ? 12.993  28.691  -6.392  1.00 23.73 ?  143 TRP   B CZ3  1 
ATOM   2416 C CH2  . TRP   B 1 143 ? 12.362  29.404  -7.431  1.00 22.57 ?  143 TRP   B CH2  1 
ATOM   2417 N N    . THR   B 1 144 ? 18.231  31.766  -1.610  1.00 12.99 ?  144 THR   B N    1 
ATOM   2418 C CA   . THR   B 1 144 ? 18.754  31.486  -0.275  1.00 11.52 ?  144 THR   B CA   1 
ATOM   2419 C C    . THR   B 1 144 ? 18.344  32.588  0.702   1.00 14.24 ?  144 THR   B C    1 
ATOM   2420 O O    . THR   B 1 144 ? 17.809  32.317  1.781   1.00 15.50 ?  144 THR   B O    1 
ATOM   2421 C CB   . THR   B 1 144 ? 20.277  31.328  -0.333  1.00 14.24 ?  144 THR   B CB   1 
ATOM   2422 O OG1  . THR   B 1 144 ? 20.595  30.213  -1.185  1.00 11.86 ?  144 THR   B OG1  1 
ATOM   2423 C CG2  . THR   B 1 144 ? 20.873  31.089  1.054   1.00 15.36 ?  144 THR   B CG2  1 
ATOM   2424 N N    . ARG   B 1 145 ? 18.551  33.845  0.320   1.00 14.24 ?  145 ARG   B N    1 
ATOM   2425 C CA   . ARG   B 1 145 ? 18.130  34.946  1.187   1.00 14.51 ?  145 ARG   B CA   1 
ATOM   2426 C C    . ARG   B 1 145 ? 16.616  34.946  1.423   1.00 16.12 ?  145 ARG   B C    1 
ATOM   2427 O O    . ARG   B 1 145 ? 16.164  35.151  2.558   1.00 16.45 ?  145 ARG   B O    1 
ATOM   2428 C CB   . ARG   B 1 145 ? 18.587  36.276  0.589   1.00 14.92 ?  145 ARG   B CB   1 
ATOM   2429 C CG   . ARG   B 1 145 ? 20.109  36.500  0.682   1.00 14.34 ?  145 ARG   B CG   1 
ATOM   2430 C CD   . ARG   B 1 145 ? 20.509  37.926  0.302   1.00 17.22 ?  145 ARG   B CD   1 
ATOM   2431 N NE   . ARG   B 1 145 ? 19.987  38.334  -0.996  1.00 14.28 ?  145 ARG   B NE   1 
ATOM   2432 C CZ   . ARG   B 1 145 ? 20.558  38.086  -2.169  1.00 18.81 ?  145 ARG   B CZ   1 
ATOM   2433 N NH1  . ARG   B 1 145 ? 21.678  37.379  -2.262  1.00 14.31 ?  145 ARG   B NH1  1 
ATOM   2434 N NH2  . ARG   B 1 145 ? 19.990  38.555  -3.281  1.00 15.38 ?  145 ARG   B NH2  1 
ATOM   2435 N N    . LEU   B 1 146 ? 15.819  34.709  0.371   1.00 14.16 ?  146 LEU   B N    1 
ATOM   2436 C CA   . LEU   B 1 146 ? 14.362  34.860  0.479   1.00 14.86 ?  146 LEU   B CA   1 
ATOM   2437 C C    . LEU   B 1 146 ? 13.747  33.758  1.320   1.00 15.84 ?  146 LEU   B C    1 
ATOM   2438 O O    . LEU   B 1 146 ? 12.826  34.005  2.106   1.00 18.36 ?  146 LEU   B O    1 
ATOM   2439 C CB   . LEU   B 1 146 ? 13.707  34.830  -0.902  1.00 16.69 ?  146 LEU   B CB   1 
ATOM   2440 C CG   . LEU   B 1 146 ? 13.706  36.094  -1.763  1.00 22.96 ?  146 LEU   B CG   1 
ATOM   2441 C CD1  . LEU   B 1 146 ? 13.312  35.741  -3.188  1.00 27.04 ?  146 LEU   B CD1  1 
ATOM   2442 C CD2  . LEU   B 1 146 ? 12.751  37.149  -1.156  1.00 23.25 ?  146 LEU   B CD2  1 
ATOM   2443 N N    . TYR   B 1 147 ? 14.222  32.529  1.153   1.00 14.20 ?  147 TYR   B N    1 
ATOM   2444 C CA   . TYR   B 1 147 ? 13.523  31.381  1.705   1.00 15.96 ?  147 TYR   B CA   1 
ATOM   2445 C C    . TYR   B 1 147 ? 14.301  30.628  2.761   1.00 14.25 ?  147 TYR   B C    1 
ATOM   2446 O O    . TYR   B 1 147 ? 13.684  29.902  3.551   1.00 16.70 ?  147 TYR   B O    1 
ATOM   2447 C CB   . TYR   B 1 147 ? 13.142  30.406  0.575   1.00 13.56 ?  147 TYR   B CB   1 
ATOM   2448 C CG   . TYR   B 1 147 ? 12.320  31.060  -0.516  1.00 19.04 ?  147 TYR   B CG   1 
ATOM   2449 C CD1  . TYR   B 1 147 ? 11.046  31.575  -0.258  1.00 20.72 ?  147 TYR   B CD1  1 
ATOM   2450 C CD2  . TYR   B 1 147 ? 12.821  31.194  -1.791  1.00 17.06 ?  147 TYR   B CD2  1 
ATOM   2451 C CE1  . TYR   B 1 147 ? 10.298  32.182  -1.271  1.00 26.48 ?  147 TYR   B CE1  1 
ATOM   2452 C CE2  . TYR   B 1 147 ? 12.092  31.800  -2.800  1.00 22.70 ?  147 TYR   B CE2  1 
ATOM   2453 C CZ   . TYR   B 1 147 ? 10.834  32.294  -2.538  1.00 32.02 ?  147 TYR   B CZ   1 
ATOM   2454 O OH   . TYR   B 1 147 ? 10.133  32.893  -3.564  1.00 32.36 ?  147 TYR   B OH   1 
ATOM   2455 N N    . ALA   B 1 148 ? 15.628  30.775  2.811   1.00 13.06 ?  148 ALA   B N    1 
ATOM   2456 C CA   . ALA   B 1 148 ? 16.435  29.946  3.703   1.00 16.35 ?  148 ALA   B CA   1 
ATOM   2457 C C    . ALA   B 1 148 ? 17.133  30.712  4.816   1.00 18.19 ?  148 ALA   B C    1 
ATOM   2458 O O    . ALA   B 1 148 ? 17.995  30.131  5.498   1.00 14.20 ?  148 ALA   B O    1 
ATOM   2459 C CB   . ALA   B 1 148 ? 17.486  29.169  2.897   1.00 13.12 ?  148 ALA   B CB   1 
ATOM   2460 N N    . MET   B 1 149 ? 16.804  31.982  5.046   1.00 21.24 ?  149 MET   B N    1 
ATOM   2461 C CA   . MET   B 1 149 ? 17.473  32.664  6.153   1.00 25.12 ?  149 MET   B CA   1 
ATOM   2462 C C    . MET   B 1 149 ? 16.504  33.375  7.058   1.00 32.94 ?  149 MET   B C    1 
ATOM   2463 O O    . MET   B 1 149 ? 16.745  34.520  7.460   1.00 31.15 ?  149 MET   B O    1 
ATOM   2464 C CB   . MET   B 1 149 ? 18.483  33.686  5.678   1.00 27.48 ?  149 MET   B CB   1 
ATOM   2465 C CG   . MET   B 1 149 ? 19.295  33.246  4.576   1.00 21.06 ?  149 MET   B CG   1 
ATOM   2466 S SD   . MET   B 1 149 ? 20.179  34.739  4.200   1.00 34.74 ?  149 MET   B SD   1 
ATOM   2467 C CE   . MET   B 1 149 ? 21.401  33.994  3.299   1.00 11.19 ?  149 MET   B CE   1 
ATOM   2468 N N    . ASN   B 1 150 ? 15.407  32.729  7.400   1.00 26.00 ?  150 ASN   B N    1 
ATOM   2469 C CA   . ASN   B 1 150 ? 14.493  33.319  8.365   1.00 35.43 ?  150 ASN   B CA   1 
ATOM   2470 C C    . ASN   B 1 150 ? 14.979  33.066  9.788   1.00 41.90 ?  150 ASN   B C    1 
ATOM   2471 O O    . ASN   B 1 150 ? 15.069  33.998  10.592  1.00 49.56 ?  150 ASN   B O    1 
ATOM   2472 C CB   . ASN   B 1 150 ? 13.088  32.774  8.174   1.00 30.11 ?  150 ASN   B CB   1 
ATOM   2473 C CG   . ASN   B 1 150 ? 12.535  33.085  6.804   1.00 32.89 ?  150 ASN   B CG   1 
ATOM   2474 O OD1  . ASN   B 1 150 ? 12.658  34.214  6.316   1.00 31.78 ?  150 ASN   B OD1  1 
ATOM   2475 N ND2  . ASN   B 1 150 ? 11.928  32.084  6.164   1.00 30.59 ?  150 ASN   B ND2  1 
ATOM   2476 N N    . VAL   C 2 7   ? -2.318  -32.321 -13.543 1.00 50.94 ?  7   VAL   C N    1 
ATOM   2477 C CA   . VAL   C 2 7   ? -3.258  -31.239 -13.272 1.00 41.48 ?  7   VAL   C CA   1 
ATOM   2478 C C    . VAL   C 2 7   ? -2.617  -30.216 -12.349 1.00 42.63 ?  7   VAL   C C    1 
ATOM   2479 O O    . VAL   C 2 7   ? -1.818  -30.562 -11.476 1.00 43.29 ?  7   VAL   C O    1 
ATOM   2480 C CB   . VAL   C 2 7   ? -4.574  -31.755 -12.650 1.00 35.14 ?  7   VAL   C CB   1 
ATOM   2481 C CG1  . VAL   C 2 7   ? -5.427  -32.471 -13.696 1.00 35.50 ?  7   VAL   C CG1  1 
ATOM   2482 C CG2  . VAL   C 2 7   ? -4.281  -32.642 -11.439 1.00 38.37 ?  7   VAL   C CG2  1 
ATOM   2483 N N    . LYS   C 2 8   ? -3.008  -28.959 -12.532 1.00 32.76 ?  8   LYS   C N    1 
ATOM   2484 C CA   . LYS   C 2 8   ? -2.415  -27.858 -11.784 1.00 30.60 ?  8   LYS   C CA   1 
ATOM   2485 C C    . LYS   C 2 8   ? -2.889  -27.881 -10.332 1.00 38.33 ?  8   LYS   C C    1 
ATOM   2486 O O    . LYS   C 2 8   ? -4.081  -28.064 -10.051 1.00 26.28 ?  8   LYS   C O    1 
ATOM   2487 C CB   . LYS   C 2 8   ? -2.760  -26.531 -12.472 1.00 34.83 ?  8   LYS   C CB   1 
ATOM   2488 C CG   . LYS   C 2 8   ? -2.290  -25.268 -11.772 1.00 38.61 ?  8   LYS   C CG   1 
ATOM   2489 C CD   . LYS   C 2 8   ? -2.736  -23.995 -12.515 1.00 47.26 ?  8   LYS   C CD   1 
ATOM   2490 C CE   . LYS   C 2 8   ? -2.328  -24.022 -14.001 1.00 49.71 ?  8   LYS   C CE   1 
ATOM   2491 N NZ   . LYS   C 2 8   ? -2.885  -22.880 -14.814 1.00 43.06 ?  8   LYS   C NZ   1 
ATOM   2492 N N    . VAL   C 2 9   ? -1.944  -27.728 -9.412  1.00 28.07 ?  9   VAL   C N    1 
ATOM   2493 C CA   . VAL   C 2 9   ? -2.262  -27.704 -7.980  1.00 25.98 ?  9   VAL   C CA   1 
ATOM   2494 C C    . VAL   C 2 9   ? -2.899  -26.358 -7.649  1.00 28.19 ?  9   VAL   C C    1 
ATOM   2495 O O    . VAL   C 2 9   ? -2.372  -25.316 -8.077  1.00 29.67 ?  9   VAL   C O    1 
ATOM   2496 C CB   . VAL   C 2 9   ? -0.986  -27.939 -7.144  1.00 29.58 ?  9   VAL   C CB   1 
ATOM   2497 C CG1  . VAL   C 2 9   ? -1.201  -27.534 -5.686  1.00 30.17 ?  9   VAL   C CG1  1 
ATOM   2498 C CG2  . VAL   C 2 9   ? -0.530  -29.388 -7.236  1.00 30.53 ?  9   VAL   C CG2  1 
ATOM   2499 N N    . PRO   C 2 10  ? -4.045  -26.315 -6.908  1.00 23.35 ?  10  PRO   C N    1 
ATOM   2500 C CA   . PRO   C 2 10  ? -4.624  -25.016 -6.533  1.00 23.47 ?  10  PRO   C CA   1 
ATOM   2501 C C    . PRO   C 2 10  ? -3.797  -24.323 -5.459  1.00 20.14 ?  10  PRO   C C    1 
ATOM   2502 O O    . PRO   C 2 10  ? -3.773  -24.733 -4.293  1.00 17.61 ?  10  PRO   C O    1 
ATOM   2503 C CB   . PRO   C 2 10  ? -6.035  -25.379 -6.042  1.00 26.10 ?  10  PRO   C CB   1 
ATOM   2504 C CG   . PRO   C 2 10  ? -5.866  -26.775 -5.479  1.00 23.08 ?  10  PRO   C CG   1 
ATOM   2505 C CD   . PRO   C 2 10  ? -4.809  -27.446 -6.346  1.00 26.29 ?  10  PRO   C CD   1 
ATOM   2506 N N    . ARG   C 2 11  ? -3.142  -23.236 -5.868  1.00 20.39 ?  11  ARG   C N    1 
ATOM   2507 C CA   . ARG   C 2 11  ? -2.135  -22.575 -5.043  1.00 20.34 ?  11  ARG   C CA   1 
ATOM   2508 C C    . ARG   C 2 11  ? -2.654  -22.214 -3.653  1.00 21.99 ?  11  ARG   C C    1 
ATOM   2509 O O    . ARG   C 2 11  ? -1.992  -22.486 -2.642  1.00 15.82 ?  11  ARG   C O    1 
ATOM   2510 C CB   . ARG   C 2 11  ? -1.641  -21.325 -5.781  1.00 23.09 ?  11  ARG   C CB   1 
ATOM   2511 C CG   . ARG   C 2 11  ? -0.784  -20.385 -4.946  1.00 18.90 ?  11  ARG   C CG   1 
ATOM   2512 C CD   . ARG   C 2 11  ? -0.480  -19.115 -5.731  1.00 23.07 ?  11  ARG   C CD   1 
ATOM   2513 N NE   . ARG   C 2 11  ? 0.437   -18.214 -5.042  1.00 20.72 ?  11  ARG   C NE   1 
ATOM   2514 C CZ   . ARG   C 2 11  ? 0.102   -17.384 -4.068  1.00 23.24 ?  11  ARG   C CZ   1 
ATOM   2515 N NH1  . ARG   C 2 11  ? -1.143  -17.318 -3.605  1.00 26.12 ?  11  ARG   C NH1  1 
ATOM   2516 N NH2  . ARG   C 2 11  ? 1.032   -16.581 -3.556  1.00 20.96 ?  11  ARG   C NH2  1 
ATOM   2517 N N    . ASN   C 2 12  ? -3.837  -21.584 -3.568  1.00 17.95 ?  12  ASN   C N    1 
ATOM   2518 C CA   . ASN   C 2 12  ? -4.226  -20.996 -2.289  1.00 19.73 ?  12  ASN   C CA   1 
ATOM   2519 C C    . ASN   C 2 12  ? -4.630  -22.063 -1.274  1.00 16.60 ?  12  ASN   C C    1 
ATOM   2520 O O    . ASN   C 2 12  ? -4.323  -21.927 -0.079  1.00 18.85 ?  12  ASN   C O    1 
ATOM   2521 C CB   . ASN   C 2 12  ? -5.355  -19.972 -2.471  1.00 20.11 ?  12  ASN   C CB   1 
ATOM   2522 C CG   . ASN   C 2 12  ? -4.911  -18.719 -3.220  1.00 24.03 ?  12  ASN   C CG   1 
ATOM   2523 O OD1  . ASN   C 2 12  ? -3.755  -18.295 -3.116  1.00 21.98 ?  12  ASN   C OD1  1 
ATOM   2524 N ND2  . ASN   C 2 12  ? -5.837  -18.098 -3.952  1.00 21.86 ?  12  ASN   C ND2  1 
ATOM   2525 N N    . PHE   C 2 13  ? -5.255  -23.154 -1.733  1.00 15.99 ?  13  PHE   C N    1 
ATOM   2526 C CA   . PHE   C 2 13  ? -5.596  -24.252 -0.832  1.00 11.50 ?  13  PHE   C CA   1 
ATOM   2527 C C    . PHE   C 2 13  ? -4.345  -24.980 -0.351  1.00 14.14 ?  13  PHE   C C    1 
ATOM   2528 O O    . PHE   C 2 13  ? -4.251  -25.364 0.828   1.00 15.15 ?  13  PHE   C O    1 
ATOM   2529 C CB   . PHE   C 2 13  ? -6.556  -25.230 -1.523  1.00 16.31 ?  13  PHE   C CB   1 
ATOM   2530 C CG   . PHE   C 2 13  ? -7.941  -24.686 -1.676  1.00 15.84 ?  13  PHE   C CG   1 
ATOM   2531 C CD1  . PHE   C 2 13  ? -8.682  -24.379 -0.551  1.00 14.65 ?  13  PHE   C CD1  1 
ATOM   2532 C CD2  . PHE   C 2 13  ? -8.486  -24.433 -2.936  1.00 16.51 ?  13  PHE   C CD2  1 
ATOM   2533 C CE1  . PHE   C 2 13  ? -10.002 -23.855 -0.665  1.00 15.47 ?  13  PHE   C CE1  1 
ATOM   2534 C CE2  . PHE   C 2 13  ? -9.776  -23.910 -3.064  1.00 15.36 ?  13  PHE   C CE2  1 
ATOM   2535 C CZ   . PHE   C 2 13  ? -10.529 -23.624 -1.925  1.00 12.69 ?  13  PHE   C CZ   1 
ATOM   2536 N N    A ARG   C 2 14  ? -3.374  -25.174 -1.247  0.43 16.14 ?  14  ARG   C N    1 
ATOM   2537 N N    B ARG   C 2 14  ? -3.364  -25.140 -1.238  0.57 16.12 ?  14  ARG   C N    1 
ATOM   2538 C CA   A ARG   C 2 14  ? -2.093  -25.742 -0.835  0.43 15.24 ?  14  ARG   C CA   1 
ATOM   2539 C CA   B ARG   C 2 14  ? -2.107  -25.758 -0.830  0.57 15.22 ?  14  ARG   C CA   1 
ATOM   2540 C C    A ARG   C 2 14  ? -1.425  -24.876 0.219   0.43 16.59 ?  14  ARG   C C    1 
ATOM   2541 C C    B ARG   C 2 14  ? -1.391  -24.889 0.195   0.57 16.60 ?  14  ARG   C C    1 
ATOM   2542 O O    A ARG   C 2 14  ? -0.918  -25.381 1.227   0.43 15.41 ?  14  ARG   C O    1 
ATOM   2543 O O    B ARG   C 2 14  ? -0.862  -25.399 1.191   0.57 15.39 ?  14  ARG   C O    1 
ATOM   2544 C CB   A ARG   C 2 14  ? -1.160  -25.905 -2.036  0.43 17.03 ?  14  ARG   C CB   1 
ATOM   2545 C CB   B ARG   C 2 14  ? -1.230  -26.004 -2.062  0.57 16.96 ?  14  ARG   C CB   1 
ATOM   2546 C CG   A ARG   C 2 14  ? 0.290   -26.143 -1.584  0.43 19.34 ?  14  ARG   C CG   1 
ATOM   2547 C CG   B ARG   C 2 14  ? 0.222   -26.395 -1.755  0.57 20.00 ?  14  ARG   C CG   1 
ATOM   2548 C CD   A ARG   C 2 14  ? 0.433   -27.491 -0.900  0.43 18.52 ?  14  ARG   C CD   1 
ATOM   2549 C CD   B ARG   C 2 14  ? 0.343   -27.820 -1.215  0.57 18.51 ?  14  ARG   C CD   1 
ATOM   2550 N NE   A ARG   C 2 14  ? 0.947   -28.495 -1.821  0.43 23.85 ?  14  ARG   C NE   1 
ATOM   2551 N NE   B ARG   C 2 14  ? -0.240  -28.824 -2.102  0.57 21.50 ?  14  ARG   C NE   1 
ATOM   2552 C CZ   A ARG   C 2 14  ? 2.193   -28.520 -2.279  0.43 19.12 ?  14  ARG   C CZ   1 
ATOM   2553 C CZ   B ARG   C 2 14  ? 0.448   -29.521 -3.000  0.57 24.35 ?  14  ARG   C CZ   1 
ATOM   2554 N NH1  A ARG   C 2 14  ? 3.112   -27.663 -1.844  0.43 13.49 ?  14  ARG   C NH1  1 
ATOM   2555 N NH1  B ARG   C 2 14  ? 1.720   -29.256 -3.255  0.57 19.57 ?  14  ARG   C NH1  1 
ATOM   2556 N NH2  A ARG   C 2 14  ? 2.532   -29.434 -3.185  0.43 22.85 ?  14  ARG   C NH2  1 
ATOM   2557 N NH2  B ARG   C 2 14  ? -0.162  -30.489 -3.681  0.57 21.58 ?  14  ARG   C NH2  1 
ATOM   2558 N N    . LEU   C 2 15  ? -1.375  -23.568 -0.019  1.00 16.23 ?  15  LEU   C N    1 
ATOM   2559 C CA   . LEU   C 2 15  ? -0.697  -22.693 0.929   1.00 19.37 ?  15  LEU   C CA   1 
ATOM   2560 C C    . LEU   C 2 15  ? -1.411  -22.665 2.273   1.00 19.52 ?  15  LEU   C C    1 
ATOM   2561 O O    . LEU   C 2 15  ? -0.761  -22.533 3.307   1.00 16.35 ?  15  LEU   C O    1 
ATOM   2562 C CB   . LEU   C 2 15  ? -0.551  -21.295 0.337   1.00 15.39 ?  15  LEU   C CB   1 
ATOM   2563 C CG   . LEU   C 2 15  ? 0.524   -21.183 -0.749  1.00 19.26 ?  15  LEU   C CG   1 
ATOM   2564 C CD1  . LEU   C 2 15  ? 0.513   -19.821 -1.356  1.00 23.04 ?  15  LEU   C CD1  1 
ATOM   2565 C CD2  . LEU   C 2 15  ? 1.910   -21.504 -0.177  1.00 20.11 ?  15  LEU   C CD2  1 
ATOM   2566 N N    . LEU   C 2 16  ? -2.751  -22.785 2.292   1.00 17.07 ?  16  LEU   C N    1 
ATOM   2567 C CA   . LEU   C 2 16  ? -3.432  -22.892 3.578   1.00 14.78 ?  16  LEU   C CA   1 
ATOM   2568 C C    . LEU   C 2 16  ? -3.036  -24.167 4.314   1.00 13.08 ?  16  LEU   C C    1 
ATOM   2569 O O    . LEU   C 2 16  ? -2.884  -24.163 5.549   1.00 17.85 ?  16  LEU   C O    1 
ATOM   2570 C CB   . LEU   C 2 16  ? -4.955  -22.838 3.381   1.00 15.78 ?  16  LEU   C CB   1 
ATOM   2571 C CG   . LEU   C 2 16  ? -5.402  -21.425 3.033   1.00 17.79 ?  16  LEU   C CG   1 
ATOM   2572 C CD1  . LEU   C 2 16  ? -6.913  -21.431 2.743   1.00 19.03 ?  16  LEU   C CD1  1 
ATOM   2573 C CD2  . LEU   C 2 16  ? -5.069  -20.461 4.158   1.00 25.22 ?  16  LEU   C CD2  1 
ATOM   2574 N N    . GLU   C 2 17  ? -2.885  -25.274 3.582   1.00 11.89 ?  17  GLU   C N    1 
ATOM   2575 C CA   . GLU   C 2 17  ? -2.373  -26.503 4.197   1.00 17.05 ?  17  GLU   C CA   1 
ATOM   2576 C C    . GLU   C 2 17  ? -0.968  -26.310 4.769   1.00 16.97 ?  17  GLU   C C    1 
ATOM   2577 O O    . GLU   C 2 17  ? -0.654  -26.792 5.870   1.00 19.77 ?  17  GLU   C O    1 
ATOM   2578 C CB   . GLU   C 2 17  ? -2.361  -27.626 3.174   1.00 16.18 ?  17  GLU   C CB   1 
ATOM   2579 C CG   . GLU   C 2 17  ? -3.762  -28.106 2.838   1.00 18.40 ?  17  GLU   C CG   1 
ATOM   2580 C CD   . GLU   C 2 17  ? -3.819  -28.882 1.536   1.00 32.75 ?  17  GLU   C CD   1 
ATOM   2581 O OE1  . GLU   C 2 17  ? -2.760  -29.061 0.895   1.00 34.99 ?  17  GLU   C OE1  1 
ATOM   2582 O OE2  . GLU   C 2 17  ? -4.936  -29.309 1.157   1.00 39.00 -1 17  GLU   C OE2  1 
ATOM   2583 N N    . GLU   C 2 18  ? -0.091  -25.659 4.005   1.00 16.33 ?  18  GLU   C N    1 
ATOM   2584 C CA   . GLU   C 2 18  ? 1.272   -25.439 4.509   1.00 13.91 ?  18  GLU   C CA   1 
ATOM   2585 C C    . GLU   C 2 18  ? 1.271   -24.496 5.708   1.00 18.53 ?  18  GLU   C C    1 
ATOM   2586 O O    . GLU   C 2 18  ? 2.091   -24.646 6.627   1.00 17.76 ?  18  GLU   C O    1 
ATOM   2587 C CB   . GLU   C 2 18  ? 2.190   -24.908 3.393   1.00 12.10 ?  18  GLU   C CB   1 
ATOM   2588 C CG   . GLU   C 2 18  ? 2.285   -25.844 2.206   1.00 16.09 ?  18  GLU   C CG   1 
ATOM   2589 C CD   . GLU   C 2 18  ? 3.474   -25.541 1.301   1.00 15.71 ?  18  GLU   C CD   1 
ATOM   2590 O OE1  . GLU   C 2 18  ? 4.600   -25.339 1.829   1.00 14.18 ?  18  GLU   C OE1  1 
ATOM   2591 O OE2  . GLU   C 2 18  ? 3.284   -25.503 0.059   1.00 18.46 -1 18  GLU   C OE2  1 
ATOM   2592 N N    . LEU   C 2 19  ? 0.356   -23.528 5.725   1.00 15.93 ?  19  LEU   C N    1 
ATOM   2593 C CA   . LEU   C 2 19  ? 0.227   -22.649 6.874   1.00 19.68 ?  19  LEU   C CA   1 
ATOM   2594 C C    . LEU   C 2 19  ? -0.154  -23.439 8.125   1.00 19.21 ?  19  LEU   C C    1 
ATOM   2595 O O    . LEU   C 2 19  ? 0.443   -23.269 9.196   1.00 20.33 ?  19  LEU   C O    1 
ATOM   2596 C CB   . LEU   C 2 19  ? -0.813  -21.569 6.572   1.00 17.20 ?  19  LEU   C CB   1 
ATOM   2597 C CG   . LEU   C 2 19  ? -1.091  -20.576 7.694   1.00 21.31 ?  19  LEU   C CG   1 
ATOM   2598 C CD1  . LEU   C 2 19  ? 0.168   -19.796 8.058   1.00 24.17 ?  19  LEU   C CD1  1 
ATOM   2599 C CD2  . LEU   C 2 19  ? -2.215  -19.629 7.276   1.00 24.06 ?  19  LEU   C CD2  1 
ATOM   2600 N N    . GLU   C 2 20  ? -1.164  -24.304 8.010   1.00 18.66 ?  20  GLU   C N    1 
ATOM   2601 C CA   . GLU   C 2 20  ? -1.581  -25.068 9.179   1.00 21.08 ?  20  GLU   C CA   1 
ATOM   2602 C C    . GLU   C 2 20  ? -0.471  -26.012 9.654   1.00 27.48 ?  20  GLU   C C    1 
ATOM   2603 O O    . GLU   C 2 20  ? -0.238  -26.145 10.871  1.00 22.55 ?  20  GLU   C O    1 
ATOM   2604 C CB   . GLU   C 2 20  ? -2.886  -25.810 8.870   1.00 29.16 ?  20  GLU   C CB   1 
ATOM   2605 C CG   . GLU   C 2 20  ? -3.480  -26.559 10.045  1.00 43.34 ?  20  GLU   C CG   1 
ATOM   2606 C CD   . GLU   C 2 20  ? -4.620  -27.472 9.623   1.00 55.04 ?  20  GLU   C CD   1 
ATOM   2607 O OE1  . GLU   C 2 20  ? -5.433  -27.055 8.763   1.00 51.87 ?  20  GLU   C OE1  1 
ATOM   2608 O OE2  . GLU   C 2 20  ? -4.704  -28.602 10.149  1.00 64.26 -1 20  GLU   C OE2  1 
ATOM   2609 N N    . GLU   C 2 21  ? 0.243   -26.656 8.710   1.00 21.00 ?  21  GLU   C N    1 
ATOM   2610 C CA   . GLU   C 2 21  ? 1.342   -27.550 9.087   1.00 25.08 ?  21  GLU   C CA   1 
ATOM   2611 C C    . GLU   C 2 21  ? 2.457   -26.794 9.786   1.00 26.14 ?  21  GLU   C C    1 
ATOM   2612 O O    . GLU   C 2 21  ? 3.025   -27.283 10.771  1.00 20.17 ?  21  GLU   C O    1 
ATOM   2613 C CB   . GLU   C 2 21  ? 1.920   -28.277 7.873   1.00 22.11 ?  21  GLU   C CB   1 
ATOM   2614 C CG   . GLU   C 2 21  ? 2.867   -29.419 8.283   1.00 26.01 ?  21  GLU   C CG   1 
ATOM   2615 C CD   . GLU   C 2 21  ? 3.458   -30.180 7.113   1.00 35.96 ?  21  GLU   C CD   1 
ATOM   2616 O OE1  . GLU   C 2 21  ? 3.045   -29.936 5.964   1.00 36.36 ?  21  GLU   C OE1  1 
ATOM   2617 O OE2  . GLU   C 2 21  ? 4.358   -31.015 7.343   1.00 36.44 -1 21  GLU   C OE2  1 
ATOM   2618 N N    . GLY   C 2 22  ? 2.815   -25.619 9.263   1.00 19.43 ?  22  GLY   C N    1 
ATOM   2619 C CA   . GLY   C 2 22  ? 3.855   -24.829 9.894   1.00 16.39 ?  22  GLY   C CA   1 
ATOM   2620 C C    . GLY   C 2 22  ? 3.467   -24.374 11.285  1.00 22.70 ?  22  GLY   C C    1 
ATOM   2621 O O    . GLY   C 2 22  ? 4.316   -24.280 12.178  1.00 20.77 ?  22  GLY   C O    1 
ATOM   2622 N N    . GLN   C 2 23  ? 2.179   -24.086 11.490  1.00 20.07 ?  23  GLN   C N    1 
ATOM   2623 C CA   . GLN   C 2 23  ? 1.732   -23.674 12.820  1.00 24.21 ?  23  GLN   C CA   1 
ATOM   2624 C C    . GLN   C 2 23  ? 1.759   -24.848 13.797  1.00 21.75 ?  23  GLN   C C    1 
ATOM   2625 O O    . GLN   C 2 23  ? 2.056   -24.666 14.986  1.00 30.51 ?  23  GLN   C O    1 
ATOM   2626 C CB   . GLN   C 2 23  ? 0.331   -23.061 12.737  1.00 22.67 ?  23  GLN   C CB   1 
ATOM   2627 C CG   . GLN   C 2 23  ? 0.320   -21.594 12.307  1.00 24.49 ?  23  GLN   C CG   1 
ATOM   2628 C CD   . GLN   C 2 23  ? -1.068  -21.149 11.872  1.00 32.89 ?  23  GLN   C CD   1 
ATOM   2629 O OE1  . GLN   C 2 23  ? -1.945  -21.980 11.628  1.00 32.48 ?  23  GLN   C OE1  1 
ATOM   2630 N NE2  . GLN   C 2 23  ? -1.274  -19.841 11.777  1.00 36.62 ?  23  GLN   C NE2  1 
ATOM   2631 N N    . LYS   C 2 24  ? 1.457   -26.057 13.316  1.00 24.26 ?  24  LYS   C N    1 
ATOM   2632 C CA   . LYS   C 2 24  ? 1.532   -27.234 14.179  1.00 27.58 ?  24  LYS   C CA   1 
ATOM   2633 C C    . LYS   C 2 24  ? 2.963   -27.450 14.659  1.00 31.88 ?  24  LYS   C C    1 
ATOM   2634 O O    . LYS   C 2 24  ? 3.208   -27.676 15.850  1.00 40.79 ?  24  LYS   C O    1 
ATOM   2635 C CB   . LYS   C 2 24  ? 1.050   -28.483 13.434  1.00 31.04 ?  24  LYS   C CB   1 
ATOM   2636 C CG   . LYS   C 2 24  ? -0.443  -28.673 13.288  1.00 41.64 ?  24  LYS   C CG   1 
ATOM   2637 C CD   . LYS   C 2 24  ? -0.670  -29.772 12.248  1.00 48.50 ?  24  LYS   C CD   1 
ATOM   2638 C CE   . LYS   C 2 24  ? -0.519  -29.233 10.818  1.00 39.12 ?  24  LYS   C CE   1 
ATOM   2639 N NZ   . LYS   C 2 24  ? -1.385  -29.876 9.786   1.00 35.18 ?  24  LYS   C NZ   1 
ATOM   2640 N N    . GLY   C 2 25  ? 3.927   -27.387 13.736  1.00 33.41 ?  25  GLY   C N    1 
ATOM   2641 C CA   . GLY   C 2 25  ? 5.324   -27.603 14.063  1.00 34.43 ?  25  GLY   C CA   1 
ATOM   2642 C C    . GLY   C 2 25  ? 5.535   -28.903 14.806  1.00 47.49 ?  25  GLY   C C    1 
ATOM   2643 O O    . GLY   C 2 25  ? 6.069   -28.918 15.921  1.00 43.14 ?  25  GLY   C O    1 
ATOM   2644 N N    . VAL   C 2 26  ? 5.123   -30.008 14.182  1.00 42.74 ?  26  VAL   C N    1 
ATOM   2645 C CA   . VAL   C 2 26  ? 5.144   -31.307 14.849  1.00 51.96 ?  26  VAL   C CA   1 
ATOM   2646 C C    . VAL   C 2 26  ? 6.553   -31.883 14.996  1.00 49.67 ?  26  VAL   C C    1 
ATOM   2647 O O    . VAL   C 2 26  ? 6.760   -32.790 15.814  1.00 57.74 ?  26  VAL   C O    1 
ATOM   2648 C CB   . VAL   C 2 26  ? 4.225   -32.282 14.087  1.00 40.77 ?  26  VAL   C CB   1 
ATOM   2649 C CG1  . VAL   C 2 26  ? 4.683   -33.725 14.264  1.00 49.54 ?  26  VAL   C CG1  1 
ATOM   2650 C CG2  . VAL   C 2 26  ? 2.780   -32.110 14.536  1.00 45.79 ?  26  VAL   C CG2  1 
ATOM   2651 N N    . GLY   C 2 27  ? 7.534   -31.379 14.252  1.00 52.89 ?  27  GLY   C N    1 
ATOM   2652 C CA   . GLY   C 2 27  ? 8.857   -31.967 14.236  1.00 52.37 ?  27  GLY   C CA   1 
ATOM   2653 C C    . GLY   C 2 27  ? 9.684   -31.666 15.478  1.00 50.10 ?  27  GLY   C C    1 
ATOM   2654 O O    . GLY   C 2 27  ? 9.203   -31.159 16.494  1.00 47.90 ?  27  GLY   C O    1 
ATOM   2655 N N    . ASP   C 2 28  ? 10.976  -31.994 15.375  1.00 43.46 ?  28  ASP   C N    1 
ATOM   2656 C CA   . ASP   C 2 28  ? 11.929  -31.725 16.446  1.00 36.55 ?  28  ASP   C CA   1 
ATOM   2657 C C    . ASP   C 2 28  ? 12.360  -30.268 16.484  1.00 40.03 ?  28  ASP   C C    1 
ATOM   2658 O O    . ASP   C 2 28  ? 13.243  -29.913 17.276  1.00 32.97 ?  28  ASP   C O    1 
ATOM   2659 C CB   . ASP   C 2 28  ? 13.154  -32.637 16.311  1.00 36.48 ?  28  ASP   C CB   1 
ATOM   2660 C CG   . ASP   C 2 28  ? 14.058  -32.250 15.153  1.00 39.59 ?  28  ASP   C CG   1 
ATOM   2661 O OD1  . ASP   C 2 28  ? 13.670  -31.385 14.338  1.00 31.10 ?  28  ASP   C OD1  1 
ATOM   2662 O OD2  . ASP   C 2 28  ? 15.168  -32.824 15.060  1.00 40.28 -1 28  ASP   C OD2  1 
ATOM   2663 N N    . GLY   C 2 29  ? 11.753  -29.428 15.643  1.00 37.77 ?  29  GLY   C N    1 
ATOM   2664 C CA   . GLY   C 2 29  ? 12.012  -28.007 15.618  1.00 29.48 ?  29  GLY   C CA   1 
ATOM   2665 C C    . GLY   C 2 29  ? 13.178  -27.568 14.760  1.00 21.65 ?  29  GLY   C C    1 
ATOM   2666 O O    . GLY   C 2 29  ? 13.486  -26.370 14.741  1.00 28.24 ?  29  GLY   C O    1 
ATOM   2667 N N    . THR   C 2 30  ? 13.838  -28.485 14.045  1.00 21.03 ?  30  THR   C N    1 
ATOM   2668 C CA   . THR   C 2 30  ? 15.046  -28.079 13.327  1.00 18.49 ?  30  THR   C CA   1 
ATOM   2669 C C    . THR   C 2 30  ? 14.760  -27.415 11.987  1.00 20.17 ?  30  THR   C C    1 
ATOM   2670 O O    . THR   C 2 30  ? 15.673  -26.803 11.427  1.00 15.24 ?  30  THR   C O    1 
ATOM   2671 C CB   . THR   C 2 30  ? 15.988  -29.261 13.087  1.00 19.48 ?  30  THR   C CB   1 
ATOM   2672 O OG1  . THR   C 2 30  ? 15.322  -30.239 12.293  1.00 22.62 ?  30  THR   C OG1  1 
ATOM   2673 C CG2  . THR   C 2 30  ? 16.443  -29.872 14.416  1.00 24.22 ?  30  THR   C CG2  1 
ATOM   2674 N N    . VAL   C 2 31  ? 13.542  -27.522 11.449  1.00 15.90 ?  31  VAL   C N    1 
ATOM   2675 C CA   . VAL   C 2 31  ? 13.096  -26.613 10.402  1.00 12.53 ?  31  VAL   C CA   1 
ATOM   2676 C C    . VAL   C 2 31  ? 11.711  -26.114 10.765  1.00 15.82 ?  31  VAL   C C    1 
ATOM   2677 O O    . VAL   C 2 31  ? 10.900  -26.852 11.335  1.00 17.17 ?  31  VAL   C O    1 
ATOM   2678 C CB   . VAL   C 2 31  ? 13.082  -27.227 8.987   1.00 20.81 ?  31  VAL   C CB   1 
ATOM   2679 C CG1  . VAL   C 2 31  ? 14.458  -27.752 8.624   1.00 16.34 ?  31  VAL   C CG1  1 
ATOM   2680 C CG2  . VAL   C 2 31  ? 12.027  -28.294 8.855   1.00 27.87 ?  31  VAL   C CG2  1 
ATOM   2681 N N    A SER   C 2 32  ? 11.450  -24.848 10.449  0.47 14.52 ?  32  SER   C N    1 
ATOM   2682 N N    B SER   C 2 32  ? 11.450  -24.852 10.438  0.53 14.50 ?  32  SER   C N    1 
ATOM   2683 C CA   A SER   C 2 32  ? 10.142  -24.255 10.713  0.47 15.52 ?  32  SER   C CA   1 
ATOM   2684 C CA   B SER   C 2 32  ? 10.154  -24.243 10.724  0.53 15.50 ?  32  SER   C CA   1 
ATOM   2685 C C    A SER   C 2 32  ? 9.851   -23.198 9.653   0.47 17.24 ?  32  SER   C C    1 
ATOM   2686 C C    B SER   C 2 32  ? 9.855   -23.181 9.669   0.53 17.24 ?  32  SER   C C    1 
ATOM   2687 O O    A SER   C 2 32  ? 10.760  -22.690 8.992   0.47 16.04 ?  32  SER   C O    1 
ATOM   2688 O O    B SER   C 2 32  ? 10.760  -22.665 9.009   0.53 16.04 ?  32  SER   C O    1 
ATOM   2689 C CB   A SER   C 2 32  ? 10.082  -23.657 12.125  0.47 19.09 ?  32  SER   C CB   1 
ATOM   2690 C CB   B SER   C 2 32  ? 10.129  -23.668 12.149  0.53 19.07 ?  32  SER   C CB   1 
ATOM   2691 O OG   A SER   C 2 32  ? 8.794   -23.131 12.404  0.47 20.00 ?  32  SER   C OG   1 
ATOM   2692 O OG   B SER   C 2 32  ? 11.023  -22.576 12.290  0.53 21.02 ?  32  SER   C OG   1 
ATOM   2693 N N    . TRP   C 2 33  ? 8.569   -22.868 9.494   1.00 17.05 ?  33  TRP   C N    1 
ATOM   2694 C CA   . TRP   C 2 33  ? 8.157   -21.907 8.465   1.00 14.97 ?  33  TRP   C CA   1 
ATOM   2695 C C    . TRP   C 2 33  ? 6.822   -21.279 8.849   1.00 12.96 ?  33  TRP   C C    1 
ATOM   2696 O O    . TRP   C 2 33  ? 6.054   -21.848 9.628   1.00 17.14 ?  33  TRP   C O    1 
ATOM   2697 C CB   . TRP   C 2 33  ? 8.043   -22.548 7.066   1.00 14.70 ?  33  TRP   C CB   1 
ATOM   2698 C CG   . TRP   C 2 33  ? 6.987   -23.600 6.970   1.00 15.82 ?  33  TRP   C CG   1 
ATOM   2699 C CD1  . TRP   C 2 33  ? 5.718   -23.458 6.458   1.00 14.82 ?  33  TRP   C CD1  1 
ATOM   2700 C CD2  . TRP   C 2 33  ? 7.092   -24.959 7.403   1.00 13.71 ?  33  TRP   C CD2  1 
ATOM   2701 N NE1  . TRP   C 2 33  ? 5.033   -24.644 6.557   1.00 15.09 ?  33  TRP   C NE1  1 
ATOM   2702 C CE2  . TRP   C 2 33  ? 5.854   -25.580 7.140   1.00 13.48 ?  33  TRP   C CE2  1 
ATOM   2703 C CE3  . TRP   C 2 33  ? 8.109   -25.711 8.002   1.00 15.98 ?  33  TRP   C CE3  1 
ATOM   2704 C CZ2  . TRP   C 2 33  ? 5.611   -26.922 7.434   1.00 12.69 ?  33  TRP   C CZ2  1 
ATOM   2705 C CZ3  . TRP   C 2 33  ? 7.866   -27.044 8.299   1.00 17.08 ?  33  TRP   C CZ3  1 
ATOM   2706 C CH2  . TRP   C 2 33  ? 6.614   -27.635 8.029   1.00 17.76 ?  33  TRP   C CH2  1 
ATOM   2707 N N    . GLY   C 2 34  ? 6.570   -20.091 8.302   1.00 15.55 ?  34  GLY   C N    1 
ATOM   2708 C CA   . GLY   C 2 34  ? 5.289   -19.427 8.556   1.00 19.53 ?  34  GLY   C CA   1 
ATOM   2709 C C    . GLY   C 2 34  ? 5.123   -18.205 7.683   1.00 22.65 ?  34  GLY   C C    1 
ATOM   2710 O O    . GLY   C 2 34  ? 6.040   -17.793 6.974   1.00 18.06 ?  34  GLY   C O    1 
ATOM   2711 N N    . LEU   C 2 35  ? 3.926   -17.621 7.721   1.00 16.41 ?  35  LEU   C N    1 
ATOM   2712 C CA   . LEU   C 2 35  ? 3.719   -16.384 6.979   1.00 20.64 ?  35  LEU   C CA   1 
ATOM   2713 C C    . LEU   C 2 35  ? 4.552   -15.252 7.577   1.00 20.97 ?  35  LEU   C C    1 
ATOM   2714 O O    . LEU   C 2 35  ? 4.728   -15.163 8.795   1.00 26.58 ?  35  LEU   C O    1 
ATOM   2715 C CB   . LEU   C 2 35  ? 2.232   -16.004 6.967   1.00 19.06 ?  35  LEU   C CB   1 
ATOM   2716 C CG   . LEU   C 2 35  ? 1.431   -16.834 5.967   1.00 23.55 ?  35  LEU   C CG   1 
ATOM   2717 C CD1  . LEU   C 2 35  ? -0.078  -16.718 6.245   1.00 25.29 ?  35  LEU   C CD1  1 
ATOM   2718 C CD2  . LEU   C 2 35  ? 1.751   -16.402 4.544   1.00 24.86 ?  35  LEU   C CD2  1 
ATOM   2719 N N    . GLU   C 2 36  ? 5.083   -14.384 6.711   1.00 21.08 ?  36  GLU   C N    1 
ATOM   2720 C CA   . GLU   C 2 36  ? 5.914   -13.290 7.207   1.00 23.37 ?  36  GLU   C CA   1 
ATOM   2721 C C    . GLU   C 2 36  ? 5.068   -12.200 7.842   1.00 40.00 ?  36  GLU   C C    1 
ATOM   2722 O O    . GLU   C 2 36  ? 5.485   -11.586 8.829   1.00 38.70 ?  36  GLU   C O    1 
ATOM   2723 C CB   . GLU   C 2 36  ? 6.763   -12.699 6.079   1.00 27.33 ?  36  GLU   C CB   1 
ATOM   2724 C CG   . GLU   C 2 36  ? 7.577   -11.475 6.489   1.00 31.98 ?  36  GLU   C CG   1 
ATOM   2725 C CD   . GLU   C 2 36  ? 8.735   -11.184 5.553   1.00 38.98 ?  36  GLU   C CD   1 
ATOM   2726 O OE1  . GLU   C 2 36  ? 9.870   -11.051 6.047   1.00 55.57 ?  36  GLU   C OE1  1 
ATOM   2727 O OE2  . GLU   C 2 36  ? 8.519   -11.096 4.327   1.00 40.78 -1 36  GLU   C OE2  1 
ATOM   2728 N N    . ASP   C 2 37  ? 3.877   -11.974 7.303   1.00 31.59 ?  37  ASP   C N    1 
ATOM   2729 C CA   . ASP   C 2 37  ? 2.990   -10.902 7.718   1.00 48.80 ?  37  ASP   C CA   1 
ATOM   2730 C C    . ASP   C 2 37  ? 1.620   -11.456 8.051   1.00 42.74 ?  37  ASP   C C    1 
ATOM   2731 O O    . ASP   C 2 37  ? 1.317   -12.632 7.830   1.00 41.47 ?  37  ASP   C O    1 
ATOM   2732 C CB   . ASP   C 2 37  ? 2.803   -9.852  6.615   1.00 46.10 ?  37  ASP   C CB   1 
ATOM   2733 C CG   . ASP   C 2 37  ? 3.822   -8.756  6.672   1.00 52.84 ?  37  ASP   C CG   1 
ATOM   2734 O OD1  . ASP   C 2 37  ? 3.853   -7.937  5.729   1.00 57.33 ?  37  ASP   C OD1  1 
ATOM   2735 O OD2  . ASP   C 2 37  ? 4.576   -8.700  7.663   1.00 56.50 -1 37  ASP   C OD2  1 
ATOM   2736 N N    A ASP   C 2 38  ? 0.788   -10.572 8.590   0.48 50.15 ?  38  ASP   C N    1 
ATOM   2737 N N    B ASP   C 2 38  ? 0.783   -10.577 8.593   0.52 50.15 ?  38  ASP   C N    1 
ATOM   2738 C CA   A ASP   C 2 38  ? -0.644  -10.789 8.696   0.48 52.32 ?  38  ASP   C CA   1 
ATOM   2739 C CA   B ASP   C 2 38  ? -0.649  -10.805 8.678   0.52 52.33 ?  38  ASP   C CA   1 
ATOM   2740 C C    A ASP   C 2 38  ? -1.409  -9.982  7.656   0.48 50.28 ?  38  ASP   C C    1 
ATOM   2741 C C    B ASP   C 2 38  ? -1.413  -9.975  7.657   0.52 50.28 ?  38  ASP   C C    1 
ATOM   2742 O O    A ASP   C 2 38  ? -2.634  -10.118 7.555   0.48 49.32 ?  38  ASP   C O    1 
ATOM   2743 O O    B ASP   C 2 38  ? -2.641  -10.091 7.568   0.52 49.31 ?  38  ASP   C O    1 
ATOM   2744 C CB   A ASP   C 2 38  ? -1.124  -10.426 10.107  0.48 52.37 ?  38  ASP   C CB   1 
ATOM   2745 C CB   B ASP   C 2 38  ? -1.152  -10.497 10.095  0.52 52.38 ?  38  ASP   C CB   1 
ATOM   2746 C CG   A ASP   C 2 38  ? -0.808  -11.505 11.131  0.48 50.35 ?  38  ASP   C CG   1 
ATOM   2747 C CG   B ASP   C 2 38  ? -1.202  -9.008  10.390  0.52 51.79 ?  38  ASP   C CG   1 
ATOM   2748 O OD1  A ASP   C 2 38  ? -0.201  -12.529 10.755  0.48 51.66 -1 38  ASP   C OD1  1 
ATOM   2749 O OD1  B ASP   C 2 38  ? -0.292  -8.277  9.940   0.52 54.20 -1 38  ASP   C OD1  1 
ATOM   2750 O OD2  A ASP   C 2 38  ? -1.156  -11.323 12.318  0.48 54.57 ?  38  ASP   C OD2  1 
ATOM   2751 O OD2  B ASP   C 2 38  ? -2.151  -8.570  11.075  0.52 50.42 ?  38  ASP   C OD2  1 
ATOM   2752 N N    . GLU   C 2 39  ? -0.706  -9.158  6.872   1.00 54.60 ?  39  GLU   C N    1 
ATOM   2753 C CA   . GLU   C 2 39  ? -1.316  -8.210  5.948   1.00 56.20 ?  39  GLU   C CA   1 
ATOM   2754 C C    . GLU   C 2 39  ? -1.083  -8.552  4.482   1.00 54.71 ?  39  GLU   C C    1 
ATOM   2755 O O    . GLU   C 2 39  ? -1.506  -7.786  3.608   1.00 44.05 ?  39  GLU   C O    1 
ATOM   2756 C CB   . GLU   C 2 39  ? -0.782  -6.799  6.228   1.00 56.96 ?  39  GLU   C CB   1 
ATOM   2757 C CG   . GLU   C 2 39  ? -0.952  -6.344  7.675   1.00 59.87 ?  39  GLU   C CG   1 
ATOM   2758 C CD   . GLU   C 2 39  ? -0.667  -4.868  7.861   1.00 69.55 ?  39  GLU   C CD   1 
ATOM   2759 O OE1  . GLU   C 2 39  ? 0.368   -4.391  7.345   1.00 68.56 ?  39  GLU   C OE1  1 
ATOM   2760 O OE2  . GLU   C 2 39  ? -1.471  -4.188  8.535   1.00 75.70 -1 39  GLU   C OE2  1 
ATOM   2761 N N    . ASP   C 2 40  ? -0.415  -9.665  4.183   1.00 51.76 ?  40  ASP   C N    1 
ATOM   2762 C CA   . ASP   C 2 40  ? -0.225  -10.090 2.797   1.00 46.57 ?  40  ASP   C CA   1 
ATOM   2763 C C    . ASP   C 2 40  ? -1.340  -11.074 2.459   1.00 38.92 ?  40  ASP   C C    1 
ATOM   2764 O O    . ASP   C 2 40  ? -1.245  -12.269 2.757   1.00 42.96 ?  40  ASP   C O    1 
ATOM   2765 C CB   . ASP   C 2 40  ? 1.162   -10.694 2.593   1.00 40.28 ?  40  ASP   C CB   1 
ATOM   2766 C CG   . ASP   C 2 40  ? 1.361   -11.242 1.185   1.00 42.52 ?  40  ASP   C CG   1 
ATOM   2767 O OD1  . ASP   C 2 40  ? 0.577   -10.865 0.284   1.00 40.57 ?  40  ASP   C OD1  1 
ATOM   2768 O OD2  . ASP   C 2 40  ? 2.306   -12.036 0.970   1.00 31.68 -1 40  ASP   C OD2  1 
ATOM   2769 N N    . MET   C 2 41  ? -2.415  -10.564 1.845   1.00 42.55 ?  41  MET   C N    1 
ATOM   2770 C CA   . MET   C 2 41  ? -3.529  -11.425 1.456   1.00 35.46 ?  41  MET   C CA   1 
ATOM   2771 C C    . MET   C 2 41  ? -3.145  -12.429 0.374   1.00 40.26 ?  41  MET   C C    1 
ATOM   2772 O O    . MET   C 2 41  ? -3.853  -13.429 0.196   1.00 36.69 ?  41  MET   C O    1 
ATOM   2773 C CB   . MET   C 2 41  ? -4.723  -10.586 0.973   1.00 48.97 ?  41  MET   C CB   1 
ATOM   2774 C CG   . MET   C 2 41  ? -5.171  -9.444  1.894   1.00 42.13 ?  41  MET   C CG   1 
ATOM   2775 S SD   . MET   C 2 41  ? -6.964  -9.175  1.801   1.00 54.41 ?  41  MET   C SD   1 
ATOM   2776 C CE   . MET   C 2 41  ? -7.203  -9.155  0.025   1.00 42.39 ?  41  MET   C CE   1 
ATOM   2777 N N    . THR   C 2 42  ? -2.052  -12.197 -0.356  1.00 29.23 ?  42  THR   C N    1 
ATOM   2778 C CA   . THR   C 2 42  ? -1.722  -13.115 -1.435  1.00 33.83 ?  42  THR   C CA   1 
ATOM   2779 C C    . THR   C 2 42  ? -0.958  -14.343 -0.954  1.00 26.01 ?  42  THR   C C    1 
ATOM   2780 O O    . THR   C 2 42  ? -0.654  -15.204 -1.782  1.00 26.98 ?  42  THR   C O    1 
ATOM   2781 C CB   . THR   C 2 42  ? -0.921  -12.407 -2.536  1.00 35.81 ?  42  THR   C CB   1 
ATOM   2782 O OG1  . THR   C 2 42  ? 0.368   -12.014 -2.040  1.00 34.72 ?  42  THR   C OG1  1 
ATOM   2783 C CG2  . THR   C 2 42  ? -1.667  -11.176 -3.030  1.00 42.08 ?  42  THR   C CG2  1 
ATOM   2784 N N    . LEU   C 2 43  ? -0.678  -14.451 0.350   1.00 25.66 ?  43  LEU   C N    1 
ATOM   2785 C CA   . LEU   C 2 43  ? 0.040   -15.592 0.929   1.00 25.82 ?  43  LEU   C CA   1 
ATOM   2786 C C    . LEU   C 2 43  ? 1.386   -15.813 0.255   1.00 21.24 ?  43  LEU   C C    1 
ATOM   2787 O O    . LEU   C 2 43  ? 1.837   -16.954 0.112   1.00 18.65 ?  43  LEU   C O    1 
ATOM   2788 C CB   . LEU   C 2 43  ? -0.790  -16.873 0.859   1.00 27.53 ?  43  LEU   C CB   1 
ATOM   2789 C CG   . LEU   C 2 43  ? -2.232  -16.678 1.354   1.00 33.24 ?  43  LEU   C CG   1 
ATOM   2790 C CD1  . LEU   C 2 43  ? -3.066  -17.913 1.095   1.00 31.86 ?  43  LEU   C CD1  1 
ATOM   2791 C CD2  . LEU   C 2 43  ? -2.195  -16.336 2.830   1.00 32.90 ?  43  LEU   C CD2  1 
ATOM   2792 N N    . THR   C 2 44  ? 2.027   -14.726 -0.164  1.00 23.85 ?  44  THR   C N    1 
ATOM   2793 C CA   . THR   C 2 44  ? 3.250   -14.831 -0.950  1.00 19.46 ?  44  THR   C CA   1 
ATOM   2794 C C    . THR   C 2 44  ? 4.516   -14.895 -0.098  1.00 19.61 ?  44  THR   C C    1 
ATOM   2795 O O    . THR   C 2 44  ? 5.421   -15.678 -0.406  1.00 17.15 ?  44  THR   C O    1 
ATOM   2796 C CB   . THR   C 2 44  ? 3.345   -13.648 -1.910  1.00 20.70 ?  44  THR   C CB   1 
ATOM   2797 O OG1  . THR   C 2 44  ? 2.255   -13.718 -2.841  1.00 22.60 ?  44  THR   C OG1  1 
ATOM   2798 C CG2  . THR   C 2 44  ? 4.658   -13.693 -2.668  1.00 21.38 ?  44  THR   C CG2  1 
ATOM   2799 N N    . ARG   C 2 45  ? 4.599   -14.092 0.961   1.00 20.08 ?  45  ARG   C N    1 
ATOM   2800 C CA   . ARG   C 2 45  ? 5.837   -13.917 1.715   1.00 22.34 ?  45  ARG   C CA   1 
ATOM   2801 C C    . ARG   C 2 45  ? 5.837   -14.751 2.987   1.00 21.30 ?  45  ARG   C C    1 
ATOM   2802 O O    . ARG   C 2 45  ? 5.009   -14.549 3.885   1.00 21.11 ?  45  ARG   C O    1 
ATOM   2803 C CB   . ARG   C 2 45  ? 6.090   -12.443 2.027   1.00 26.73 ?  45  ARG   C CB   1 
ATOM   2804 C CG   . ARG   C 2 45  ? 6.189   -11.604 0.766   1.00 26.56 ?  45  ARG   C CG   1 
ATOM   2805 C CD   . ARG   C 2 45  ? 6.597   -10.158 1.063   1.00 36.77 ?  45  ARG   C CD   1 
ATOM   2806 N NE   . ARG   C 2 45  ? 5.488   -9.356  1.569   1.00 52.82 ?  45  ARG   C NE   1 
ATOM   2807 C CZ   . ARG   C 2 45  ? 4.337   -9.165  0.933   1.00 57.39 ?  45  ARG   C CZ   1 
ATOM   2808 N NH1  . ARG   C 2 45  ? 4.109   -9.686  -0.264  1.00 57.20 ?  45  ARG   C NH1  1 
ATOM   2809 N NH2  . ARG   C 2 45  ? 3.391   -8.429  1.512   1.00 56.67 ?  45  ARG   C NH2  1 
ATOM   2810 N N    . TRP   C 2 46  ? 6.797   -15.662 3.068   1.00 15.58 ?  46  TRP   C N    1 
ATOM   2811 C CA   . TRP   C 2 46  ? 6.970   -16.600 4.153   1.00 14.45 ?  46  TRP   C CA   1 
ATOM   2812 C C    . TRP   C 2 46  ? 8.352   -16.405 4.759   1.00 16.24 ?  46  TRP   C C    1 
ATOM   2813 O O    . TRP   C 2 46  ? 9.279   -15.901 4.111   1.00 18.65 ?  46  TRP   C O    1 
ATOM   2814 C CB   . TRP   C 2 46  ? 6.813   -18.052 3.646   1.00 16.27 ?  46  TRP   C CB   1 
ATOM   2815 C CG   . TRP   C 2 46  ? 5.425   -18.374 3.151   1.00 14.79 ?  46  TRP   C CG   1 
ATOM   2816 C CD1  . TRP   C 2 46  ? 4.837   -17.923 2.012   1.00 17.43 ?  46  TRP   C CD1  1 
ATOM   2817 C CD2  . TRP   C 2 46  ? 4.464   -19.206 3.805   1.00 17.01 ?  46  TRP   C CD2  1 
ATOM   2818 N NE1  . TRP   C 2 46  ? 3.547   -18.422 1.917   1.00 19.26 ?  46  TRP   C NE1  1 
ATOM   2819 C CE2  . TRP   C 2 46  ? 3.300   -19.215 3.005   1.00 19.05 ?  46  TRP   C CE2  1 
ATOM   2820 C CE3  . TRP   C 2 46  ? 4.476   -19.945 4.990   1.00 16.94 ?  46  TRP   C CE3  1 
ATOM   2821 C CZ2  . TRP   C 2 46  ? 2.153   -19.930 3.356   1.00 17.13 ?  46  TRP   C CZ2  1 
ATOM   2822 C CZ3  . TRP   C 2 46  ? 3.323   -20.679 5.345   1.00 18.63 ?  46  TRP   C CZ3  1 
ATOM   2823 C CH2  . TRP   C 2 46  ? 2.186   -20.664 4.525   1.00 18.37 ?  46  TRP   C CH2  1 
ATOM   2824 N N    . THR   C 2 47  ? 8.479   -16.816 6.011   1.00 15.92 ?  47  THR   C N    1 
ATOM   2825 C CA   . THR   C 2 47  ? 9.765   -16.957 6.664   1.00 16.66 ?  47  THR   C CA   1 
ATOM   2826 C C    . THR   C 2 47  ? 10.069  -18.430 6.843   1.00 15.71 ?  47  THR   C C    1 
ATOM   2827 O O    . THR   C 2 47  ? 9.167   -19.271 6.931   1.00 18.62 ?  47  THR   C O    1 
ATOM   2828 C CB   . THR   C 2 47  ? 9.801   -16.285 8.039   1.00 22.76 ?  47  THR   C CB   1 
ATOM   2829 O OG1  . THR   C 2 47  ? 8.809   -16.895 8.876   1.00 24.69 ?  47  THR   C OG1  1 
ATOM   2830 C CG2  . THR   C 2 47  ? 9.548   -14.795 7.917   1.00 23.08 ?  47  THR   C CG2  1 
ATOM   2831 N N    . GLY   C 2 48  ? 11.370  -18.719 6.934   1.00 17.16 ?  48  GLY   C N    1 
ATOM   2832 C CA   . GLY   C 2 48  ? 11.814  -20.048 7.303   1.00 16.53 ?  48  GLY   C CA   1 
ATOM   2833 C C    . GLY   C 2 48  ? 12.970  -19.978 8.282   1.00 13.01 ?  48  GLY   C C    1 
ATOM   2834 O O    . GLY   C 2 48  ? 13.675  -18.974 8.376   1.00 14.60 ?  48  GLY   C O    1 
ATOM   2835 N N    . MET   C 2 49  ? 13.122  -21.061 9.042   1.00 14.63 ?  49  MET   C N    1 
ATOM   2836 C CA   . MET   C 2 49  ? 14.201  -21.231 10.008  1.00 16.09 ?  49  MET   C CA   1 
ATOM   2837 C C    . MET   C 2 49  ? 14.800  -22.622 9.840   1.00 16.60 ?  49  MET   C C    1 
ATOM   2838 O O    . MET   C 2 49  ? 14.062  -23.611 9.802   1.00 15.19 ?  49  MET   C O    1 
ATOM   2839 C CB   . MET   C 2 49  ? 13.704  -21.114 11.451  1.00 19.54 ?  49  MET   C CB   1 
ATOM   2840 C CG   . MET   C 2 49  ? 14.791  -21.525 12.446  1.00 23.02 ?  49  MET   C CG   1 
ATOM   2841 S SD   . MET   C 2 49  ? 14.106  -21.921 14.048  1.00 52.46 ?  49  MET   C SD   1 
ATOM   2842 C CE   . MET   C 2 49  ? 13.393  -23.535 13.646  1.00 22.58 ?  49  MET   C CE   1 
ATOM   2843 N N    . ILE   C 2 50  ? 16.137  -22.702 9.786   1.00 14.12 ?  50  ILE   C N    1 
ATOM   2844 C CA   . ILE   C 2 50  ? 16.860  -23.969 9.747   1.00 14.57 ?  50  ILE   C CA   1 
ATOM   2845 C C    . ILE   C 2 50  ? 17.861  -23.966 10.892  1.00 14.57 ?  50  ILE   C C    1 
ATOM   2846 O O    . ILE   C 2 50  ? 18.619  -23.000 11.050  1.00 14.77 ?  50  ILE   C O    1 
ATOM   2847 C CB   . ILE   C 2 50  ? 17.602  -24.162 8.405   1.00 14.43 ?  50  ILE   C CB   1 
ATOM   2848 C CG1  . ILE   C 2 50  ? 16.624  -24.271 7.233   1.00 12.80 ?  50  ILE   C CG1  1 
ATOM   2849 C CG2  . ILE   C 2 50  ? 18.561  -25.385 8.463   1.00 15.39 ?  50  ILE   C CG2  1 
ATOM   2850 C CD1  . ILE   C 2 50  ? 17.294  -24.105 5.861   1.00 14.07 ?  50  ILE   C CD1  1 
ATOM   2851 N N    . ILE   C 2 51  ? 17.899  -25.048 11.669  1.00 12.40 ?  51  ILE   C N    1 
ATOM   2852 C CA   . ILE   C 2 51  ? 18.979  -25.211 12.644  1.00 14.71 ?  51  ILE   C CA   1 
ATOM   2853 C C    . ILE   C 2 51  ? 20.097  -26.023 12.004  1.00 15.88 ?  51  ILE   C C    1 
ATOM   2854 O O    . ILE   C 2 51  ? 19.867  -27.121 11.486  1.00 16.89 ?  51  ILE   C O    1 
ATOM   2855 C CB   . ILE   C 2 51  ? 18.490  -25.884 13.938  1.00 16.65 ?  51  ILE   C CB   1 
ATOM   2856 C CG1  . ILE   C 2 51  ? 17.222  -25.223 14.471  1.00 22.49 ?  51  ILE   C CG1  1 
ATOM   2857 C CG2  . ILE   C 2 51  ? 19.643  -25.914 14.980  1.00 19.69 ?  51  ILE   C CG2  1 
ATOM   2858 C CD1  . ILE   C 2 51  ? 17.385  -23.751 14.781  1.00 25.99 ?  51  ILE   C CD1  1 
ATOM   2859 N N    . GLY   C 2 52  ? 21.317  -25.484 12.025  1.00 17.88 ?  52  GLY   C N    1 
ATOM   2860 C CA   . GLY   C 2 52  ? 22.426  -26.176 11.401  1.00 17.08 ?  52  GLY   C CA   1 
ATOM   2861 C C    . GLY   C 2 52  ? 22.595  -27.583 11.955  1.00 18.29 ?  52  GLY   C C    1 
ATOM   2862 O O    . GLY   C 2 52  ? 22.507  -27.799 13.165  1.00 17.16 ?  52  GLY   C O    1 
ATOM   2863 N N    . PRO   C 2 53  ? 22.857  -28.561 11.090  1.00 16.35 ?  53  PRO   C N    1 
ATOM   2864 C CA   . PRO   C 2 53  ? 22.872  -29.973 11.534  1.00 16.19 ?  53  PRO   C CA   1 
ATOM   2865 C C    . PRO   C 2 53  ? 24.152  -30.345 12.267  1.00 20.66 ?  53  PRO   C C    1 
ATOM   2866 O O    . PRO   C 2 53  ? 25.225  -29.758 12.047  1.00 20.88 ?  53  PRO   C O    1 
ATOM   2867 C CB   . PRO   C 2 53  ? 22.737  -30.754 10.219  1.00 17.02 ?  53  PRO   C CB   1 
ATOM   2868 C CG   . PRO   C 2 53  ? 23.306  -29.824 9.175   1.00 18.30 ?  53  PRO   C CG   1 
ATOM   2869 C CD   . PRO   C 2 53  ? 22.851  -28.453 9.619   1.00 16.76 ?  53  PRO   C CD   1 
ATOM   2870 N N    . PRO   C 2 54  ? 24.081  -31.357 13.129  1.00 20.39 ?  54  PRO   C N    1 
ATOM   2871 C CA   . PRO   C 2 54  ? 25.249  -31.735 13.942  1.00 22.36 ?  54  PRO   C CA   1 
ATOM   2872 C C    . PRO   C 2 54  ? 26.409  -32.276 13.109  1.00 22.88 ?  54  PRO   C C    1 
ATOM   2873 O O    . PRO   C 2 54  ? 26.247  -32.790 12.003  1.00 22.51 ?  54  PRO   C O    1 
ATOM   2874 C CB   . PRO   C 2 54  ? 24.697  -32.826 14.873  1.00 22.60 ?  54  PRO   C CB   1 
ATOM   2875 C CG   . PRO   C 2 54  ? 23.454  -33.349 14.175  1.00 26.32 ?  54  PRO   C CG   1 
ATOM   2876 C CD   . PRO   C 2 54  ? 22.886  -32.165 13.431  1.00 22.60 ?  54  PRO   C CD   1 
ATOM   2877 N N    . ARG   C 2 55  ? 27.605  -32.189 13.691  1.00 22.79 ?  55  ARG   C N    1 
ATOM   2878 C CA   . ARG   C 2 55  ? 28.826  -32.709 13.064  1.00 25.67 ?  55  ARG   C CA   1 
ATOM   2879 C C    . ARG   C 2 55  ? 29.093  -32.059 11.701  1.00 19.54 ?  55  ARG   C C    1 
ATOM   2880 O O    . ARG   C 2 55  ? 29.555  -32.707 10.758  1.00 24.87 ?  55  ARG   C O    1 
ATOM   2881 C CB   . ARG   C 2 55  ? 28.775  -34.236 12.957  1.00 30.42 ?  55  ARG   C CB   1 
ATOM   2882 C CG   . ARG   C 2 55  ? 28.521  -34.911 14.314  1.00 33.40 ?  55  ARG   C CG   1 
ATOM   2883 C CD   . ARG   C 2 55  ? 28.206  -36.391 14.167  1.00 37.76 ?  55  ARG   C CD   1 
ATOM   2884 N NE   . ARG   C 2 55  ? 26.999  -36.613 13.379  1.00 46.39 ?  55  ARG   C NE   1 
ATOM   2885 C CZ   . ARG   C 2 55  ? 25.802  -36.864 13.894  1.00 47.26 ?  55  ARG   C CZ   1 
ATOM   2886 N NH1  . ARG   C 2 55  ? 25.609  -36.906 15.202  1.00 47.56 ?  55  ARG   C NH1  1 
ATOM   2887 N NH2  . ARG   C 2 55  ? 24.770  -37.062 13.075  1.00 38.44 ?  55  ARG   C NH2  1 
ATOM   2888 N N    . THR   C 2 56  ? 28.803  -30.760 11.611  1.00 21.30 ?  56  THR   C N    1 
ATOM   2889 C CA   . THR   C 2 56  ? 29.139  -29.920 10.466  1.00 19.13 ?  56  THR   C CA   1 
ATOM   2890 C C    . THR   C 2 56  ? 29.533  -28.560 11.017  1.00 16.18 ?  56  THR   C C    1 
ATOM   2891 O O    . THR   C 2 56  ? 29.270  -28.254 12.183  1.00 20.40 ?  56  THR   C O    1 
ATOM   2892 C CB   . THR   C 2 56  ? 27.965  -29.745 9.485   1.00 17.03 ?  56  THR   C CB   1 
ATOM   2893 O OG1  . THR   C 2 56  ? 26.995  -28.859 10.065  1.00 17.07 ?  56  THR   C OG1  1 
ATOM   2894 C CG2  . THR   C 2 56  ? 27.306  -31.074 9.180   1.00 23.44 ?  56  THR   C CG2  1 
ATOM   2895 N N    . ASN   C 2 57  ? 30.146  -27.721 10.166  1.00 16.10 ?  57  ASN   C N    1 
ATOM   2896 C CA   . ASN   C 2 57  ? 30.492  -26.376 10.619  1.00 17.81 ?  57  ASN   C CA   1 
ATOM   2897 C C    . ASN   C 2 57  ? 29.263  -25.500 10.807  1.00 19.28 ?  57  ASN   C C    1 
ATOM   2898 O O    . ASN   C 2 57  ? 29.396  -24.382 11.312  1.00 22.25 ?  57  ASN   C O    1 
ATOM   2899 C CB   . ASN   C 2 57  ? 31.447  -25.678 9.646   1.00 17.86 ?  57  ASN   C CB   1 
ATOM   2900 C CG   . ASN   C 2 57  ? 32.859  -26.249 9.678   1.00 24.92 ?  57  ASN   C CG   1 
ATOM   2901 O OD1  . ASN   C 2 57  ? 33.176  -27.151 10.452  1.00 22.23 ?  57  ASN   C OD1  1 
ATOM   2902 N ND2  . ASN   C 2 57  ? 33.701  -25.729 8.807   1.00 21.26 ?  57  ASN   C ND2  1 
ATOM   2903 N N    . TYR   C 2 58  ? 28.078  -25.982 10.419  1.00 15.71 ?  58  TYR   C N    1 
ATOM   2904 C CA   . TYR   C 2 58  ? 26.848  -25.238 10.621  1.00 14.27 ?  58  TYR   C CA   1 
ATOM   2905 C C    . TYR   C 2 58  ? 26.174  -25.545 11.955  1.00 20.37 ?  58  TYR   C C    1 
ATOM   2906 O O    . TYR   C 2 58  ? 25.165  -24.910 12.281  1.00 20.61 ?  58  TYR   C O    1 
ATOM   2907 C CB   . TYR   C 2 58  ? 25.855  -25.551 9.492   1.00 13.89 ?  58  TYR   C CB   1 
ATOM   2908 C CG   . TYR   C 2 58  ? 26.413  -25.427 8.090   1.00 13.98 ?  58  TYR   C CG   1 
ATOM   2909 C CD1  . TYR   C 2 58  ? 26.568  -24.179 7.489   1.00 12.97 ?  58  TYR   C CD1  1 
ATOM   2910 C CD2  . TYR   C 2 58  ? 26.753  -26.553 7.352   1.00 12.43 ?  58  TYR   C CD2  1 
ATOM   2911 C CE1  . TYR   C 2 58  ? 27.055  -24.058 6.187   1.00 13.41 ?  58  TYR   C CE1  1 
ATOM   2912 C CE2  . TYR   C 2 58  ? 27.227  -26.449 6.077   1.00 15.39 ?  58  TYR   C CE2  1 
ATOM   2913 C CZ   . TYR   C 2 58  ? 27.381  -25.200 5.488   1.00 13.00 ?  58  TYR   C CZ   1 
ATOM   2914 O OH   . TYR   C 2 58  ? 27.847  -25.118 4.186   1.00 14.66 ?  58  TYR   C OH   1 
ATOM   2915 N N    . GLU   C 2 59  ? 26.710  -26.479 12.736  1.00 19.96 ?  59  GLU   C N    1 
ATOM   2916 C CA   . GLU   C 2 59  ? 25.922  -27.124 13.789  1.00 18.31 ?  59  GLU   C CA   1 
ATOM   2917 C C    . GLU   C 2 59  ? 25.436  -26.129 14.847  1.00 19.36 ?  59  GLU   C C    1 
ATOM   2918 O O    . GLU   C 2 59  ? 26.190  -25.281 15.335  1.00 22.24 ?  59  GLU   C O    1 
ATOM   2919 C CB   . GLU   C 2 59  ? 26.750  -28.261 14.399  1.00 26.36 ?  59  GLU   C CB   1 
ATOM   2920 C CG   . GLU   C 2 59  ? 27.330  -28.061 15.761  1.00 44.63 ?  59  GLU   C CG   1 
ATOM   2921 C CD   . GLU   C 2 59  ? 28.269  -29.205 16.121  1.00 42.39 ?  59  GLU   C CD   1 
ATOM   2922 O OE1  . GLU   C 2 59  ? 27.860  -30.387 16.019  1.00 34.75 ?  59  GLU   C OE1  1 
ATOM   2923 O OE2  . GLU   C 2 59  ? 29.432  -28.916 16.480  1.00 51.57 -1 59  GLU   C OE2  1 
ATOM   2924 N N    . ASN   C 2 60  ? 24.134  -26.182 15.127  1.00 19.08 ?  60  ASN   C N    1 
ATOM   2925 C CA   . ASN   C 2 60  ? 23.434  -25.407 16.149  1.00 19.69 ?  60  ASN   C CA   1 
ATOM   2926 C C    . ASN   C 2 60  ? 23.286  -23.925 15.816  1.00 21.51 ?  60  ASN   C C    1 
ATOM   2927 O O    . ASN   C 2 60  ? 22.728  -23.181 16.629  1.00 22.70 ?  60  ASN   C O    1 
ATOM   2928 C CB   . ASN   C 2 60  ? 24.100  -25.556 17.519  1.00 22.48 ?  60  ASN   C CB   1 
ATOM   2929 C CG   . ASN   C 2 60  ? 23.849  -26.923 18.136  1.00 31.26 ?  60  ASN   C CG   1 
ATOM   2930 O OD1  . ASN   C 2 60  ? 22.894  -27.618 17.779  1.00 34.21 ?  60  ASN   C OD1  1 
ATOM   2931 N ND2  . ASN   C 2 60  ? 24.717  -27.322 19.056  1.00 39.72 ?  60  ASN   C ND2  1 
ATOM   2932 N N    . ARG   C 2 61  ? 23.747  -23.465 14.658  1.00 19.59 ?  61  ARG   C N    1 
ATOM   2933 C CA   . ARG   C 2 61  ? 23.449  -22.099 14.260  1.00 18.88 ?  61  ARG   C CA   1 
ATOM   2934 C C    . ARG   C 2 61  ? 21.996  -21.989 13.799  1.00 15.88 ?  61  ARG   C C    1 
ATOM   2935 O O    . ARG   C 2 61  ? 21.465  -22.912 13.176  1.00 20.29 ?  61  ARG   C O    1 
ATOM   2936 C CB   . ARG   C 2 61  ? 24.409  -21.665 13.162  1.00 23.93 ?  61  ARG   C CB   1 
ATOM   2937 C CG   . ARG   C 2 61  ? 25.802  -21.487 13.725  1.00 24.93 ?  61  ARG   C CG   1 
ATOM   2938 C CD   . ARG   C 2 61  ? 26.769  -21.091 12.669  1.00 26.77 ?  61  ARG   C CD   1 
ATOM   2939 N NE   . ARG   C 2 61  ? 28.059  -20.697 13.223  1.00 28.96 ?  61  ARG   C NE   1 
ATOM   2940 C CZ   . ARG   C 2 61  ? 28.777  -19.688 12.751  1.00 23.53 ?  61  ARG   C CZ   1 
ATOM   2941 N NH1  . ARG   C 2 61  ? 28.312  -18.902 11.792  1.00 23.85 ?  61  ARG   C NH1  1 
ATOM   2942 N NH2  . ARG   C 2 61  ? 29.998  -19.478 13.232  1.00 30.51 ?  61  ARG   C NH2  1 
ATOM   2943 N N    . ILE   C 2 62  ? 21.348  -20.872 14.135  1.00 18.49 ?  62  ILE   C N    1 
ATOM   2944 C CA   . ILE   C 2 62  ? 19.983  -20.576 13.682  1.00 16.49 ?  62  ILE   C CA   1 
ATOM   2945 C C    . ILE   C 2 62  ? 20.028  -19.732 12.417  1.00 13.70 ?  62  ILE   C C    1 
ATOM   2946 O O    . ILE   C 2 62  ? 20.431  -18.560 12.452  1.00 18.59 ?  62  ILE   C O    1 
ATOM   2947 C CB   . ILE   C 2 62  ? 19.142  -19.863 14.754  1.00 24.06 ?  62  ILE   C CB   1 
ATOM   2948 C CG1  . ILE   C 2 62  ? 19.484  -20.333 16.167  1.00 27.34 ?  62  ILE   C CG1  1 
ATOM   2949 C CG2  . ILE   C 2 62  ? 17.662  -19.915 14.388  1.00 21.75 ?  62  ILE   C CG2  1 
ATOM   2950 C CD1  . ILE   C 2 62  ? 18.597  -19.719 17.234  1.00 37.26 ?  62  ILE   C CD1  1 
ATOM   2951 N N    . TYR   C 2 63  ? 19.561  -20.305 11.302  1.00 14.03 ?  63  TYR   C N    1 
ATOM   2952 C CA   . TYR   C 2 63  ? 19.479  -19.603 10.029  1.00 15.85 ?  63  TYR   C CA   1 
ATOM   2953 C C    . TYR   C 2 63  ? 18.051  -19.124 9.825   1.00 14.20 ?  63  TYR   C C    1 
ATOM   2954 O O    . TYR   C 2 63  ? 17.117  -19.934 9.841   1.00 15.52 ?  63  TYR   C O    1 
ATOM   2955 C CB   . TYR   C 2 63  ? 19.915  -20.512 8.869   1.00 11.50 ?  63  TYR   C CB   1 
ATOM   2956 C CG   . TYR   C 2 63  ? 21.362  -20.881 9.021   1.00 13.85 ?  63  TYR   C CG   1 
ATOM   2957 C CD1  . TYR   C 2 63  ? 22.345  -19.988 8.651   1.00 14.22 ?  63  TYR   C CD1  1 
ATOM   2958 C CD2  . TYR   C 2 63  ? 21.733  -22.084 9.611   1.00 15.16 ?  63  TYR   C CD2  1 
ATOM   2959 C CE1  . TYR   C 2 63  ? 23.679  -20.293 8.818   1.00 14.49 ?  63  TYR   C CE1  1 
ATOM   2960 C CE2  . TYR   C 2 63  ? 23.062  -22.391 9.813   1.00 17.49 ?  63  TYR   C CE2  1 
ATOM   2961 C CZ   . TYR   C 2 63  ? 24.023  -21.499 9.411   1.00 17.20 ?  63  TYR   C CZ   1 
ATOM   2962 O OH   . TYR   C 2 63  ? 25.347  -21.810 9.606   1.00 18.50 ?  63  TYR   C OH   1 
ATOM   2963 N N    . SER   C 2 64  ? 17.893  -17.817 9.614   1.00 14.59 ?  64  SER   C N    1 
ATOM   2964 C CA   . SER   C 2 64  ? 16.633  -17.235 9.155   1.00 16.31 ?  64  SER   C CA   1 
ATOM   2965 C C    . SER   C 2 64  ? 16.646  -17.035 7.641   1.00 15.88 ?  64  SER   C C    1 
ATOM   2966 O O    . SER   C 2 64  ? 17.650  -16.603 7.064   1.00 17.43 ?  64  SER   C O    1 
ATOM   2967 C CB   . SER   C 2 64  ? 16.363  -15.890 9.829   1.00 20.53 ?  64  SER   C CB   1 
ATOM   2968 O OG   . SER   C 2 64  ? 16.264  -16.045 11.230  1.00 27.96 ?  64  SER   C OG   1 
ATOM   2969 N N    . LEU   C 2 65  ? 15.523  -17.351 7.004   1.00 12.30 ?  65  LEU   C N    1 
ATOM   2970 C CA   . LEU   C 2 65  ? 15.348  -17.241 5.567   1.00 13.73 ?  65  LEU   C CA   1 
ATOM   2971 C C    . LEU   C 2 65  ? 14.036  -16.544 5.236   1.00 16.42 ?  65  LEU   C C    1 
ATOM   2972 O O    . LEU   C 2 65  ? 13.104  -16.509 6.048   1.00 16.92 ?  65  LEU   C O    1 
ATOM   2973 C CB   . LEU   C 2 65  ? 15.345  -18.629 4.894   1.00 14.23 ?  65  LEU   C CB   1 
ATOM   2974 C CG   . LEU   C 2 65  ? 16.557  -19.546 5.127   1.00 11.28 ?  65  LEU   C CG   1 
ATOM   2975 C CD1  . LEU   C 2 65  ? 16.357  -20.373 6.405   1.00 12.50 ?  65  LEU   C CD1  1 
ATOM   2976 C CD2  . LEU   C 2 65  ? 16.710  -20.461 3.912   1.00 11.77 ?  65  LEU   C CD2  1 
ATOM   2977 N N    . LYS   C 2 66  ? 13.973  -16.015 4.012   1.00 15.23 ?  66  LYS   C N    1 
ATOM   2978 C CA   . LYS   C 2 66  ? 12.730  -15.556 3.395   1.00 16.64 ?  66  LYS   C CA   1 
ATOM   2979 C C    . LYS   C 2 66  ? 12.403  -16.416 2.179   1.00 16.20 ?  66  LYS   C C    1 
ATOM   2980 O O    . LYS   C 2 66  ? 13.272  -16.697 1.343   1.00 16.88 ?  66  LYS   C O    1 
ATOM   2981 C CB   . LYS   C 2 66  ? 12.816  -14.081 2.997   1.00 19.70 ?  66  LYS   C CB   1 
ATOM   2982 C CG   . LYS   C 2 66  ? 13.295  -13.223 4.150   1.00 27.55 ?  66  LYS   C CG   1 
ATOM   2983 C CD   . LYS   C 2 66  ? 12.119  -12.743 4.990   1.00 35.57 ?  66  LYS   C CD   1 
ATOM   2984 C CE   . LYS   C 2 66  ? 12.566  -11.851 6.153   1.00 37.10 ?  66  LYS   C CE   1 
ATOM   2985 N NZ   . LYS   C 2 66  ? 13.424  -10.721 5.711   1.00 52.51 ?  66  LYS   C NZ   1 
ATOM   2986 N N    . VAL   C 2 67  ? 11.142  -16.827 2.080   1.00 14.23 ?  67  VAL   C N    1 
ATOM   2987 C CA   . VAL   C 2 67  ? 10.678  -17.701 1.008   1.00 11.41 ?  67  VAL   C CA   1 
ATOM   2988 C C    . VAL   C 2 67  ? 9.488   -17.023 0.337   1.00 15.01 ?  67  VAL   C C    1 
ATOM   2989 O O    . VAL   C 2 67  ? 8.546   -16.604 1.016   1.00 18.56 ?  67  VAL   C O    1 
ATOM   2990 C CB   . VAL   C 2 67  ? 10.274  -19.084 1.561   1.00 13.34 ?  67  VAL   C CB   1 
ATOM   2991 C CG1  . VAL   C 2 67  ? 9.754   -20.000 0.445   1.00 17.09 ?  67  VAL   C CG1  1 
ATOM   2992 C CG2  . VAL   C 2 67  ? 11.457  -19.728 2.315   1.00 17.27 ?  67  VAL   C CG2  1 
ATOM   2993 N N    . GLU   C 2 68  ? 9.528   -16.922 -0.983  1.00 16.27 ?  68  GLU   C N    1 
ATOM   2994 C CA   . GLU   C 2 68  ? 8.493   -16.247 -1.758  1.00 17.53 ?  68  GLU   C CA   1 
ATOM   2995 C C    . GLU   C 2 68  ? 7.772   -17.284 -2.603  1.00 15.69 ?  68  GLU   C C    1 
ATOM   2996 O O    . GLU   C 2 68  ? 8.389   -17.942 -3.452  1.00 15.78 ?  68  GLU   C O    1 
ATOM   2997 C CB   . GLU   C 2 68  ? 9.116   -15.152 -2.628  1.00 25.41 ?  68  GLU   C CB   1 
ATOM   2998 C CG   . GLU   C 2 68  ? 8.167   -14.345 -3.472  1.00 30.54 ?  68  GLU   C CG   1 
ATOM   2999 C CD   . GLU   C 2 68  ? 8.435   -12.849 -3.364  1.00 37.19 ?  68  GLU   C CD   1 
ATOM   3000 O OE1  . GLU   C 2 68  ? 8.844   -12.384 -2.275  1.00 33.44 ?  68  GLU   C OE1  1 
ATOM   3001 O OE2  . GLU   C 2 68  ? 8.266   -12.149 -4.380  1.00 50.32 -1 68  GLU   C OE2  1 
ATOM   3002 N N    . CYS   C 2 69  ? 6.457   -17.428 -2.370  1.00 15.84 ?  69  CYS   C N    1 
ATOM   3003 C CA   . CYS   C 2 69  ? 5.610   -18.326 -3.140  1.00 15.06 ?  69  CYS   C CA   1 
ATOM   3004 C C    . CYS   C 2 69  ? 4.829   -17.465 -4.123  1.00 20.79 ?  69  CYS   C C    1 
ATOM   3005 O O    . CYS   C 2 69  ? 3.829   -16.837 -3.755  1.00 20.20 ?  69  CYS   C O    1 
ATOM   3006 C CB   . CYS   C 2 69  ? 4.690   -19.131 -2.225  1.00 18.59 ?  69  CYS   C CB   1 
ATOM   3007 S SG   . CYS   C 2 69  ? 5.632   -20.266 -1.140  1.00 17.54 ?  69  CYS   C SG   1 
ATOM   3008 N N    . GLY   C 2 70  ? 5.311   -17.421 -5.378  1.00 16.77 ?  70  GLY   C N    1 
ATOM   3009 C CA   . GLY   C 2 70  ? 4.739   -16.551 -6.392  1.00 20.08 ?  70  GLY   C CA   1 
ATOM   3010 C C    . GLY   C 2 70  ? 3.444   -17.087 -6.962  1.00 21.09 ?  70  GLY   C C    1 
ATOM   3011 O O    . GLY   C 2 70  ? 2.927   -18.126 -6.556  1.00 20.60 ?  70  GLY   C O    1 
ATOM   3012 N N    . PRO   C 2 71  ? 2.905   -16.361 -7.949  1.00 24.29 ?  71  PRO   C N    1 
ATOM   3013 C CA   . PRO   C 2 71  ? 1.581   -16.724 -8.499  1.00 25.37 ?  71  PRO   C CA   1 
ATOM   3014 C C    . PRO   C 2 71  ? 1.508   -18.121 -9.096  1.00 23.82 ?  71  PRO   C C    1 
ATOM   3015 O O    . PRO   C 2 71  ? 0.406   -18.671 -9.212  1.00 26.92 ?  71  PRO   C O    1 
ATOM   3016 C CB   . PRO   C 2 71  ? 1.327   -15.656 -9.580  1.00 30.86 ?  71  PRO   C CB   1 
ATOM   3017 C CG   . PRO   C 2 71  ? 2.420   -14.668 -9.497  1.00 35.17 ?  71  PRO   C CG   1 
ATOM   3018 C CD   . PRO   C 2 71  ? 3.379   -15.041 -8.398  1.00 24.41 ?  71  PRO   C CD   1 
ATOM   3019 N N    . LYS   C 2 72  ? 2.633   -18.714 -9.498  1.00 24.10 ?  72  LYS   C N    1 
ATOM   3020 C CA   . LYS   C 2 72  ? 2.620   -20.017 -10.145 1.00 25.80 ?  72  LYS   C CA   1 
ATOM   3021 C C    . LYS   C 2 72  ? 2.998   -21.141 -9.194  1.00 23.76 ?  72  LYS   C C    1 
ATOM   3022 O O    . LYS   C 2 72  ? 3.040   -22.304 -9.606  1.00 25.09 ?  72  LYS   C O    1 
ATOM   3023 C CB   . LYS   C 2 72  ? 3.562   -20.005 -11.353 1.00 24.79 ?  72  LYS   C CB   1 
ATOM   3024 C CG   . LYS   C 2 72  ? 3.021   -19.176 -12.518 1.00 33.09 ?  72  LYS   C CG   1 
ATOM   3025 C CD   . LYS   C 2 72  ? 3.695   -19.507 -13.828 1.00 39.11 ?  72  LYS   C CD   1 
ATOM   3026 C CE   . LYS   C 2 72  ? 3.314   -18.499 -14.911 1.00 42.07 ?  72  LYS   C CE   1 
ATOM   3027 N NZ   . LYS   C 2 72  ? 4.091   -18.690 -16.173 1.00 49.08 ?  72  LYS   C NZ   1 
ATOM   3028 N N    . TYR   C 2 73  ? 3.251   -20.819 -7.934  1.00 23.83 ?  73  TYR   C N    1 
ATOM   3029 C CA   . TYR   C 2 73  ? 3.519   -21.845 -6.941  1.00 25.37 ?  73  TYR   C CA   1 
ATOM   3030 C C    . TYR   C 2 73  ? 2.266   -22.685 -6.700  1.00 24.62 ?  73  TYR   C C    1 
ATOM   3031 O O    . TYR   C 2 73  ? 1.145   -22.152 -6.676  1.00 21.78 ?  73  TYR   C O    1 
ATOM   3032 C CB   . TYR   C 2 73  ? 3.994   -21.189 -5.641  1.00 19.46 ?  73  TYR   C CB   1 
ATOM   3033 C CG   . TYR   C 2 73  ? 4.339   -22.148 -4.504  1.00 19.97 ?  73  TYR   C CG   1 
ATOM   3034 C CD1  . TYR   C 2 73  ? 3.365   -22.611 -3.641  1.00 18.26 ?  73  TYR   C CD1  1 
ATOM   3035 C CD2  . TYR   C 2 73  ? 5.648   -22.581 -4.310  1.00 17.12 ?  73  TYR   C CD2  1 
ATOM   3036 C CE1  . TYR   C 2 73  ? 3.666   -23.472 -2.606  1.00 14.79 ?  73  TYR   C CE1  1 
ATOM   3037 C CE2  . TYR   C 2 73  ? 5.962   -23.459 -3.284  1.00 17.09 ?  73  TYR   C CE2  1 
ATOM   3038 C CZ   . TYR   C 2 73  ? 4.975   -23.905 -2.433  1.00 17.95 ?  73  TYR   C CZ   1 
ATOM   3039 O OH   . TYR   C 2 73  ? 5.278   -24.769 -1.391  1.00 15.40 ?  73  TYR   C OH   1 
ATOM   3040 N N    . PRO   C 2 74  ? 2.412   -24.004 -6.517  1.00 19.00 ?  74  PRO   C N    1 
ATOM   3041 C CA   . PRO   C 2 74  ? 3.653   -24.792 -6.561  1.00 19.82 ?  74  PRO   C CA   1 
ATOM   3042 C C    . PRO   C 2 74  ? 3.923   -25.426 -7.915  1.00 22.05 ?  74  PRO   C C    1 
ATOM   3043 O O    . PRO   C 2 74  ? 4.671   -26.401 -7.974  1.00 20.15 ?  74  PRO   C O    1 
ATOM   3044 C CB   . PRO   C 2 74  ? 3.398   -25.866 -5.497  1.00 17.11 ?  74  PRO   C CB   1 
ATOM   3045 C CG   . PRO   C 2 74  ? 1.908   -26.146 -5.646  1.00 26.72 ?  74  PRO   C CG   1 
ATOM   3046 C CD   . PRO   C 2 74  ? 1.287   -24.802 -5.995  1.00 19.20 ?  74  PRO   C CD   1 
ATOM   3047 N N    . GLU   C 2 75  ? 3.324   -24.955 -9.015  1.00 20.90 ?  75  GLU   C N    1 
ATOM   3048 C CA   . GLU   C 2 75  ? 3.767   -25.434 -10.320 1.00 23.24 ?  75  GLU   C CA   1 
ATOM   3049 C C    . GLU   C 2 75  ? 5.207   -25.014 -10.581 1.00 22.60 ?  75  GLU   C C    1 
ATOM   3050 O O    . GLU   C 2 75  ? 5.980   -25.757 -11.192 1.00 22.64 ?  75  GLU   C O    1 
ATOM   3051 C CB   . GLU   C 2 75  ? 2.854   -24.910 -11.433 1.00 29.77 ?  75  GLU   C CB   1 
ATOM   3052 C CG   . GLU   C 2 75  ? 1.446   -25.508 -11.473 1.00 32.85 ?  75  GLU   C CG   1 
ATOM   3053 C CD   . GLU   C 2 75  ? 1.424   -27.007 -11.279 1.00 31.94 ?  75  GLU   C CD   1 
ATOM   3054 O OE1  . GLU   C 2 75  ? 2.061   -27.716 -12.086 1.00 40.93 ?  75  GLU   C OE1  1 
ATOM   3055 O OE2  . GLU   C 2 75  ? 0.760   -27.480 -10.330 1.00 35.31 -1 75  GLU   C OE2  1 
ATOM   3056 N N    . ALA   C 2 76  ? 5.575   -23.814 -10.143 1.00 22.99 ?  76  ALA   C N    1 
ATOM   3057 C CA   . ALA   C 2 76  ? 6.930   -23.293 -10.163 1.00 23.15 ?  76  ALA   C CA   1 
ATOM   3058 C C    . ALA   C 2 76  ? 7.490   -23.272 -8.746  1.00 22.66 ?  76  ALA   C C    1 
ATOM   3059 O O    . ALA   C 2 76  ? 6.731   -23.175 -7.773  1.00 21.44 ?  76  ALA   C O    1 
ATOM   3060 C CB   . ALA   C 2 76  ? 6.981   -21.874 -10.734 1.00 26.72 ?  76  ALA   C CB   1 
ATOM   3061 N N    . PRO   C 2 77  ? 8.806   -23.352 -8.594  1.00 18.96 ?  77  PRO   C N    1 
ATOM   3062 C CA   . PRO   C 2 77  ? 9.399   -23.354 -7.262  1.00 17.41 ?  77  PRO   C CA   1 
ATOM   3063 C C    . PRO   C 2 77  ? 9.325   -21.986 -6.612  1.00 14.52 ?  77  PRO   C C    1 
ATOM   3064 O O    . PRO   C 2 77  ? 9.162   -20.957 -7.292  1.00 17.80 ?  77  PRO   C O    1 
ATOM   3065 C CB   . PRO   C 2 77  ? 10.858  -23.759 -7.531  1.00 18.28 ?  77  PRO   C CB   1 
ATOM   3066 C CG   . PRO   C 2 77  ? 11.126  -23.307 -8.906  1.00 17.12 ?  77  PRO   C CG   1 
ATOM   3067 C CD   . PRO   C 2 77  ? 9.820   -23.477 -9.655  1.00 21.74 ?  77  PRO   C CD   1 
ATOM   3068 N N    . PRO   C 2 78  ? 9.432   -21.944 -5.285  1.00 16.31 ?  78  PRO   C N    1 
ATOM   3069 C CA   . PRO   C 2 78  ? 9.532   -20.671 -4.575  1.00 14.69 ?  78  PRO   C CA   1 
ATOM   3070 C C    . PRO   C 2 78  ? 10.925  -20.084 -4.726  1.00 17.50 ?  78  PRO   C C    1 
ATOM   3071 O O    . PRO   C 2 78  ? 11.886  -20.777 -5.062  1.00 18.33 ?  78  PRO   C O    1 
ATOM   3072 C CB   . PRO   C 2 78  ? 9.249   -21.064 -3.121  1.00 17.13 ?  78  PRO   C CB   1 
ATOM   3073 C CG   . PRO   C 2 78  ? 9.850   -22.452 -3.031  1.00 14.95 ?  78  PRO   C CG   1 
ATOM   3074 C CD   . PRO   C 2 78  ? 9.559   -23.103 -4.382  1.00 12.95 ?  78  PRO   C CD   1 
ATOM   3075 N N    . SER   C 2 79  ? 11.021  -18.780 -4.496  1.00 15.85 ?  79  SER   C N    1 
ATOM   3076 C CA   . SER   C 2 79  ? 12.341  -18.158 -4.403  1.00 17.02 ?  79  SER   C CA   1 
ATOM   3077 C C    . SER   C 2 79  ? 12.784  -18.169 -2.949  1.00 18.05 ?  79  SER   C C    1 
ATOM   3078 O O    . SER   C 2 79  ? 11.966  -18.013 -2.046  1.00 19.18 ?  79  SER   C O    1 
ATOM   3079 C CB   . SER   C 2 79  ? 12.328  -16.723 -4.927  1.00 23.63 ?  79  SER   C CB   1 
ATOM   3080 O OG   . SER   C 2 79  ? 11.630  -15.897 -4.018  1.00 31.98 ?  79  SER   C OG   1 
ATOM   3081 N N    . VAL   C 2 80  ? 14.084  -18.367 -2.713  1.00 13.98 ?  80  VAL   C N    1 
ATOM   3082 C CA   . VAL   C 2 80  ? 14.584  -18.519 -1.350  1.00 11.97 ?  80  VAL   C CA   1 
ATOM   3083 C C    . VAL   C 2 80  ? 15.797  -17.631 -1.134  1.00 15.31 ?  80  VAL   C C    1 
ATOM   3084 O O    . VAL   C 2 80  ? 16.688  -17.565 -1.985  1.00 16.28 ?  80  VAL   C O    1 
ATOM   3085 C CB   . VAL   C 2 80  ? 14.950  -19.990 -1.042  1.00 14.70 ?  80  VAL   C CB   1 
ATOM   3086 C CG1  . VAL   C 2 80  ? 15.371  -20.153 0.409   1.00 14.90 ?  80  VAL   C CG1  1 
ATOM   3087 C CG2  . VAL   C 2 80  ? 13.787  -20.900 -1.357  1.00 17.80 ?  80  VAL   C CG2  1 
ATOM   3088 N N    . ARG   C 2 81  ? 15.854  -16.968 0.017   1.00 12.79 ?  81  ARG   C N    1 
ATOM   3089 C CA   . ARG   C 2 81  ? 17.021  -16.149 0.336   1.00 16.75 ?  81  ARG   C CA   1 
ATOM   3090 C C    . ARG   C 2 81  ? 17.377  -16.315 1.809   1.00 14.01 ?  81  ARG   C C    1 
ATOM   3091 O O    . ARG   C 2 81  ? 16.495  -16.277 2.671   1.00 14.84 ?  81  ARG   C O    1 
ATOM   3092 C CB   . ARG   C 2 81  ? 16.736  -14.675 0.003   1.00 21.11 ?  81  ARG   C CB   1 
ATOM   3093 C CG   . ARG   C 2 81  ? 17.554  -13.674 0.786   1.00 25.25 ?  81  ARG   C CG   1 
ATOM   3094 C CD   . ARG   C 2 81  ? 17.280  -12.267 0.264   1.00 29.50 ?  81  ARG   C CD   1 
ATOM   3095 N NE   . ARG   C 2 81  ? 15.987  -11.747 0.695   1.00 33.40 ?  81  ARG   C NE   1 
ATOM   3096 C CZ   . ARG   C 2 81  ? 15.795  -11.004 1.778   1.00 33.40 ?  81  ARG   C CZ   1 
ATOM   3097 N NH1  . ARG   C 2 81  ? 16.790  -10.708 2.601   1.00 32.99 ?  81  ARG   C NH1  1 
ATOM   3098 N NH2  . ARG   C 2 81  ? 14.572  -10.551 2.045   1.00 34.80 ?  81  ARG   C NH2  1 
ATOM   3099 N N    . PHE   C 2 82  ? 18.663  -16.538 2.107   1.00 14.30 ?  82  PHE   C N    1 
ATOM   3100 C CA   . PHE   C 2 82  ? 19.131  -16.529 3.489   1.00 12.22 ?  82  PHE   C CA   1 
ATOM   3101 C C    . PHE   C 2 82  ? 19.282  -15.092 3.974   1.00 12.82 ?  82  PHE   C C    1 
ATOM   3102 O O    . PHE   C 2 82  ? 19.849  -14.252 3.268   1.00 16.17 ?  82  PHE   C O    1 
ATOM   3103 C CB   . PHE   C 2 82  ? 20.487  -17.235 3.620   1.00 12.02 ?  82  PHE   C CB   1 
ATOM   3104 C CG   . PHE   C 2 82  ? 20.401  -18.729 3.752   1.00 12.40 ?  82  PHE   C CG   1 
ATOM   3105 C CD1  . PHE   C 2 82  ? 20.311  -19.525 2.616   1.00 13.62 ?  82  PHE   C CD1  1 
ATOM   3106 C CD2  . PHE   C 2 82  ? 20.456  -19.347 5.008   1.00 12.55 ?  82  PHE   C CD2  1 
ATOM   3107 C CE1  . PHE   C 2 82  ? 20.273  -20.910 2.719   1.00 13.43 ?  82  PHE   C CE1  1 
ATOM   3108 C CE2  . PHE   C 2 82  ? 20.410  -20.728 5.112   1.00 14.63 ?  82  PHE   C CE2  1 
ATOM   3109 C CZ   . PHE   C 2 82  ? 20.320  -21.511 3.951   1.00 14.29 ?  82  PHE   C CZ   1 
ATOM   3110 N N    . VAL   C 2 83  ? 18.745  -14.808 5.164   1.00 13.12 ?  83  VAL   C N    1 
ATOM   3111 C CA   . VAL   C 2 83  ? 19.028  -13.551 5.859   1.00 16.28 ?  83  VAL   C CA   1 
ATOM   3112 C C    . VAL   C 2 83  ? 20.317  -13.666 6.662   1.00 16.70 ?  83  VAL   C C    1 
ATOM   3113 O O    . VAL   C 2 83  ? 21.217  -12.825 6.556   1.00 18.62 ?  83  VAL   C O    1 
ATOM   3114 C CB   . VAL   C 2 83  ? 17.830  -13.179 6.761   1.00 16.14 ?  83  VAL   C CB   1 
ATOM   3115 C CG1  . VAL   C 2 83  ? 18.132  -11.925 7.574   1.00 22.38 ?  83  VAL   C CG1  1 
ATOM   3116 C CG2  . VAL   C 2 83  ? 16.554  -13.021 5.939   1.00 17.08 ?  83  VAL   C CG2  1 
ATOM   3117 N N    . THR   C 2 84  ? 20.418  -14.751 7.424   1.00 17.98 ?  84  THR   C N    1 
ATOM   3118 C CA   . THR   C 2 84  ? 21.622  -15.124 8.155   1.00 16.06 ?  84  THR   C CA   1 
ATOM   3119 C C    . THR   C 2 84  ? 22.737  -15.530 7.191   1.00 13.53 ?  84  THR   C C    1 
ATOM   3120 O O    . THR   C 2 84  ? 22.518  -16.348 6.291   1.00 15.42 ?  84  THR   C O    1 
ATOM   3121 C CB   . THR   C 2 84  ? 21.297  -16.293 9.082   1.00 18.46 ?  84  THR   C CB   1 
ATOM   3122 O OG1  . THR   C 2 84  ? 20.109  -16.002 9.842   1.00 15.48 ?  84  THR   C OG1  1 
ATOM   3123 C CG2  . THR   C 2 84  ? 22.436  -16.593 10.016  1.00 17.07 ?  84  THR   C CG2  1 
ATOM   3124 N N    . LYS   C 2 85  ? 23.944  -15.017 7.412   1.00 15.39 ?  85  LYS   C N    1 
ATOM   3125 C CA   . LYS   C 2 85  ? 25.032  -15.305 6.478   1.00 14.51 ?  85  LYS   C CA   1 
ATOM   3126 C C    . LYS   C 2 85  ? 25.433  -16.773 6.555   1.00 16.01 ?  85  LYS   C C    1 
ATOM   3127 O O    . LYS   C 2 85  ? 25.544  -17.352 7.639   1.00 18.45 ?  85  LYS   C O    1 
ATOM   3128 C CB   . LYS   C 2 85  ? 26.249  -14.431 6.788   1.00 18.20 ?  85  LYS   C CB   1 
ATOM   3129 C CG   . LYS   C 2 85  ? 26.183  -13.084 6.164   1.00 19.55 ?  85  LYS   C CG   1 
ATOM   3130 C CD   . LYS   C 2 85  ? 27.597  -12.623 5.756   1.00 25.18 ?  85  LYS   C CD   1 
ATOM   3131 C CE   . LYS   C 2 85  ? 27.681  -11.106 5.769   1.00 30.93 ?  85  LYS   C CE   1 
ATOM   3132 N NZ   . LYS   C 2 85  ? 29.013  -10.632 5.296   1.00 30.78 ?  85  LYS   C NZ   1 
ATOM   3133 N N    . ILE   C 2 86  ? 25.674  -17.378 5.397   1.00 17.61 ?  86  ILE   C N    1 
ATOM   3134 C CA   . ILE   C 2 86  ? 26.066  -18.782 5.359   1.00 16.08 ?  86  ILE   C CA   1 
ATOM   3135 C C    . ILE   C 2 86  ? 26.984  -18.969 4.157   1.00 13.52 ?  86  ILE   C C    1 
ATOM   3136 O O    . ILE   C 2 86  ? 26.728  -18.432 3.076   1.00 16.28 ?  86  ILE   C O    1 
ATOM   3137 C CB   . ILE   C 2 86  ? 24.827  -19.715 5.304   1.00 15.54 ?  86  ILE   C CB   1 
ATOM   3138 C CG1  . ILE   C 2 86  ? 25.224  -21.180 5.531   1.00 14.43 ?  86  ILE   C CG1  1 
ATOM   3139 C CG2  . ILE   C 2 86  ? 24.064  -19.523 3.995   1.00 15.82 ?  86  ILE   C CG2  1 
ATOM   3140 C CD1  . ILE   C 2 86  ? 23.992  -22.117 5.723   1.00 17.74 ?  86  ILE   C CD1  1 
ATOM   3141 N N    . ASN   C 2 87  ? 28.064  -19.712 4.352   1.00 16.38 ?  87  ASN   C N    1 
ATOM   3142 C CA   . ASN   C 2 87  ? 28.933  -20.124 3.255   1.00 14.43 ?  87  ASN   C CA   1 
ATOM   3143 C C    . ASN   C 2 87  ? 28.515  -21.527 2.841   1.00 12.20 ?  87  ASN   C C    1 
ATOM   3144 O O    . ASN   C 2 87  ? 28.696  -22.486 3.608   1.00 13.40 ?  87  ASN   C O    1 
ATOM   3145 C CB   . ASN   C 2 87  ? 30.394  -20.067 3.698   1.00 12.81 ?  87  ASN   C CB   1 
ATOM   3146 C CG   . ASN   C 2 87  ? 30.846  -18.641 3.952   1.00 15.22 ?  87  ASN   C CG   1 
ATOM   3147 O OD1  . ASN   C 2 87  ? 30.439  -17.732 3.219   1.00 23.12 ?  87  ASN   C OD1  1 
ATOM   3148 N ND2  . ASN   C 2 87  ? 31.668  -18.430 4.977   1.00 16.92 ?  87  ASN   C ND2  1 
ATOM   3149 N N    . MET   C 2 88  ? 27.930  -21.650 1.652   1.00 13.84 ?  88  MET   C N    1 
ATOM   3150 C CA   . MET   C 2 88  ? 27.389  -22.949 1.247   1.00 13.36 ?  88  MET   C CA   1 
ATOM   3151 C C    . MET   C 2 88  ? 27.142  -22.893 -0.249  1.00 13.75 ?  88  MET   C C    1 
ATOM   3152 O O    . MET   C 2 88  ? 26.795  -21.836 -0.770  1.00 13.87 ?  88  MET   C O    1 
ATOM   3153 C CB   . MET   C 2 88  ? 26.129  -23.287 2.088   1.00 18.74 ?  88  MET   C CB   1 
ATOM   3154 C CG   . MET   C 2 88  ? 25.210  -24.394 1.602   1.00 12.93 ?  88  MET   C CG   1 
ATOM   3155 S SD   . MET   C 2 88  ? 23.541  -24.367 2.364   1.00 14.98 ?  88  MET   C SD   1 
ATOM   3156 C CE   . MET   C 2 88  ? 22.946  -25.909 1.617   1.00 13.35 ?  88  MET   C CE   1 
ATOM   3157 N N    A ASN   C 2 89  ? 27.414  -23.995 -0.946  0.56 16.31 ?  89  ASN   C N    1 
ATOM   3158 N N    B ASN   C 2 89  ? 27.380  -24.007 -0.951  0.44 16.31 ?  89  ASN   C N    1 
ATOM   3159 C CA   A ASN   C 2 89  ? 27.233  -24.006 -2.392  0.56 15.33 ?  89  ASN   C CA   1 
ATOM   3160 C CA   B ASN   C 2 89  ? 27.225  -23.991 -2.406  0.44 15.36 ?  89  ASN   C CA   1 
ATOM   3161 C C    A ASN   C 2 89  ? 25.815  -23.585 -2.795  0.56 16.80 ?  89  ASN   C C    1 
ATOM   3162 C C    B ASN   C 2 89  ? 25.812  -23.562 -2.790  0.44 16.81 ?  89  ASN   C C    1 
ATOM   3163 O O    A ASN   C 2 89  ? 24.824  -24.100 -2.265  0.56 15.16 ?  89  ASN   C O    1 
ATOM   3164 O O    B ASN   C 2 89  ? 24.823  -24.066 -2.248  0.44 15.16 ?  89  ASN   C O    1 
ATOM   3165 C CB   A ASN   C 2 89  ? 27.575  -25.397 -2.937  0.56 17.30 ?  89  ASN   C CB   1 
ATOM   3166 C CB   B ASN   C 2 89  ? 27.531  -25.370 -3.006  0.44 17.31 ?  89  ASN   C CB   1 
ATOM   3167 C CG   A ASN   C 2 89  ? 29.084  -25.656 -2.984  0.56 16.03 ?  89  ASN   C CG   1 
ATOM   3168 C CG   B ASN   C 2 89  ? 27.247  -25.443 -4.509  0.44 18.89 ?  89  ASN   C CG   1 
ATOM   3169 O OD1  A ASN   C 2 89  ? 29.695  -25.472 -4.031  0.56 29.82 ?  89  ASN   C OD1  1 
ATOM   3170 O OD1  B ASN   C 2 89  ? 27.913  -24.785 -5.312  0.44 21.78 ?  89  ASN   C OD1  1 
ATOM   3171 N ND2  A ASN   C 2 89  ? 29.693  -26.065 -1.857  0.56 21.27 ?  89  ASN   C ND2  1 
ATOM   3172 N ND2  B ASN   C 2 89  ? 26.263  -26.256 -4.893  0.44 21.00 ?  89  ASN   C ND2  1 
ATOM   3173 N N    . GLY   C 2 90  ? 25.722  -22.624 -3.728  1.00 15.54 ?  90  GLY   C N    1 
ATOM   3174 C CA   . GLY   C 2 90  ? 24.447  -22.159 -4.248  1.00 17.34 ?  90  GLY   C CA   1 
ATOM   3175 C C    . GLY   C 2 90  ? 23.915  -20.907 -3.577  1.00 17.98 ?  90  GLY   C C    1 
ATOM   3176 O O    . GLY   C 2 90  ? 22.894  -20.374 -4.029  1.00 17.00 ?  90  GLY   C O    1 
ATOM   3177 N N    . ILE   C 2 91  ? 24.568  -20.434 -2.514  1.00 12.34 ?  91  ILE   C N    1 
ATOM   3178 C CA   . ILE   C 2 91  ? 24.119  -19.253 -1.769  1.00 15.92 ?  91  ILE   C CA   1 
ATOM   3179 C C    . ILE   C 2 91  ? 25.070  -18.098 -2.076  1.00 16.08 ?  91  ILE   C C    1 
ATOM   3180 O O    . ILE   C 2 91  ? 26.278  -18.175 -1.798  1.00 15.93 ?  91  ILE   C O    1 
ATOM   3181 C CB   . ILE   C 2 91  ? 24.034  -19.519 -0.256  1.00 14.57 ?  91  ILE   C CB   1 
ATOM   3182 C CG1  . ILE   C 2 91  ? 22.830  -20.422 0.110   1.00 15.51 ?  91  ILE   C CG1  1 
ATOM   3183 C CG2  . ILE   C 2 91  ? 23.880  -18.190 0.500   1.00 14.46 ?  91  ILE   C CG2  1 
ATOM   3184 C CD1  . ILE   C 2 91  ? 22.826  -21.807 -0.543  1.00 10.74 ?  91  ILE   C CD1  1 
ATOM   3185 N N    . ASN   C 2 92  ? 24.527  -17.030 -2.669  1.00 16.28 ?  92  ASN   C N    1 
ATOM   3186 C CA   . ASN   C 2 92  ? 25.335  -15.860 -3.017  1.00 16.70 ?  92  ASN   C CA   1 
ATOM   3187 C C    . ASN   C 2 92  ? 25.906  -15.212 -1.759  1.00 16.87 ?  92  ASN   C C    1 
ATOM   3188 O O    . ASN   C 2 92  ? 25.170  -14.932 -0.809  1.00 15.40 ?  92  ASN   C O    1 
ATOM   3189 C CB   . ASN   C 2 92  ? 24.473  -14.870 -3.802  1.00 17.11 ?  92  ASN   C CB   1 
ATOM   3190 C CG   . ASN   C 2 92  ? 25.263  -13.681 -4.308  1.00 23.79 ?  92  ASN   C CG   1 
ATOM   3191 O OD1  . ASN   C 2 92  ? 25.640  -12.799 -3.537  1.00 20.59 ?  92  ASN   C OD1  1 
ATOM   3192 N ND2  . ASN   C 2 92  ? 25.533  -13.663 -5.608  1.00 31.50 ?  92  ASN   C ND2  1 
ATOM   3193 N N    . ASN   C 2 93  ? 27.231  -14.971 -1.740  1.00 15.44 ?  93  ASN   C N    1 
ATOM   3194 C CA   . ASN   C 2 93  ? 27.860  -14.543 -0.495  1.00 16.67 ?  93  ASN   C CA   1 
ATOM   3195 C C    . ASN   C 2 93  ? 27.742  -13.035 -0.245  1.00 18.87 ?  93  ASN   C C    1 
ATOM   3196 O O    . ASN   C 2 93  ? 28.288  -12.559 0.758   1.00 20.10 ?  93  ASN   C O    1 
ATOM   3197 C CB   . ASN   C 2 93  ? 29.336  -15.002 -0.423  1.00 15.73 ?  93  ASN   C CB   1 
ATOM   3198 C CG   . ASN   C 2 93  ? 30.233  -14.331 -1.454  1.00 21.39 ?  93  ASN   C CG   1 
ATOM   3199 O OD1  . ASN   C 2 93  ? 29.874  -13.318 -2.056  1.00 18.32 ?  93  ASN   C OD1  1 
ATOM   3200 N ND2  . ASN   C 2 93  ? 31.431  -14.900 -1.648  1.00 17.46 ?  93  ASN   C ND2  1 
ATOM   3201 N N    . SER   C 2 94  ? 27.003  -12.289 -1.078  1.00 18.75 ?  94  SER   C N    1 
ATOM   3202 C CA   . SER   C 2 94  ? 26.668  -10.908 -0.740  1.00 21.10 ?  94  SER   C CA   1 
ATOM   3203 C C    . SER   C 2 94  ? 25.172  -10.650 -0.615  1.00 22.56 ?  94  SER   C C    1 
ATOM   3204 O O    . SER   C 2 94  ? 24.777  -9.768  0.153   1.00 23.93 ?  94  SER   C O    1 
ATOM   3205 C CB   . SER   C 2 94  ? 27.295  -9.932  -1.759  1.00 25.48 ?  94  SER   C CB   1 
ATOM   3206 O OG   . SER   C 2 94  ? 26.900  -10.201 -3.085  1.00 36.03 ?  94  SER   C OG   1 
ATOM   3207 N N    . SER   C 2 95  ? 24.325  -11.429 -1.292  1.00 17.45 ?  95  SER   C N    1 
ATOM   3208 C CA   . SER   C 2 95  ? 22.877  -11.228 -1.234  1.00 15.29 ?  95  SER   C CA   1 
ATOM   3209 C C    . SER   C 2 95  ? 22.129  -12.268 -0.420  1.00 16.81 ?  95  SER   C C    1 
ATOM   3210 O O    . SER   C 2 95  ? 20.979  -12.011 -0.036  1.00 18.24 ?  95  SER   C O    1 
ATOM   3211 C CB   . SER   C 2 95  ? 22.278  -11.228 -2.644  1.00 21.13 ?  95  SER   C CB   1 
ATOM   3212 O OG   . SER   C 2 95  ? 22.346  -12.526 -3.224  1.00 20.04 ?  95  SER   C OG   1 
ATOM   3213 N N    . GLY   C 2 96  ? 22.723  -13.433 -0.193  1.00 16.56 ?  96  GLY   C N    1 
ATOM   3214 C CA   . GLY   C 2 96  ? 22.032  -14.559 0.401   1.00 15.85 ?  96  GLY   C CA   1 
ATOM   3215 C C    . GLY   C 2 96  ? 21.075  -15.288 -0.524  1.00 15.72 ?  96  GLY   C C    1 
ATOM   3216 O O    . GLY   C 2 96  ? 20.440  -16.263 -0.091  1.00 15.31 ?  96  GLY   C O    1 
ATOM   3217 N N    A MET   C 2 97  ? 20.951  -14.868 -1.780  0.61 16.10 ?  97  MET   C N    1 
ATOM   3218 N N    B MET   C 2 97  ? 20.955  -14.871 -1.781  0.39 16.13 ?  97  MET   C N    1 
ATOM   3219 C CA   A MET   C 2 97  ? 19.991  -15.519 -2.661  0.61 15.30 ?  97  MET   C CA   1 
ATOM   3220 C CA   B MET   C 2 97  ? 19.989  -15.507 -2.668  0.39 15.37 ?  97  MET   C CA   1 
ATOM   3221 C C    A MET   C 2 97  ? 20.427  -16.933 -3.000  0.61 15.50 ?  97  MET   C C    1 
ATOM   3222 C C    B MET   C 2 97  ? 20.423  -16.927 -3.005  0.39 15.54 ?  97  MET   C C    1 
ATOM   3223 O O    A MET   C 2 97  ? 21.612  -17.206 -3.229  0.61 15.95 ?  97  MET   C O    1 
ATOM   3224 O O    B MET   C 2 97  ? 21.605  -17.197 -3.242  0.39 15.96 ?  97  MET   C O    1 
ATOM   3225 C CB   A MET   C 2 97  ? 19.775  -14.710 -3.933  0.61 21.54 ?  97  MET   C CB   1 
ATOM   3226 C CB   B MET   C 2 97  ? 19.811  -14.691 -3.945  0.39 21.49 ?  97  MET   C CB   1 
ATOM   3227 C CG   A MET   C 2 97  ? 19.175  -13.374 -3.622  0.61 24.61 ?  97  MET   C CG   1 
ATOM   3228 C CG   B MET   C 2 97  ? 18.972  -13.444 -3.744  0.39 24.48 ?  97  MET   C CG   1 
ATOM   3229 S SD   A MET   C 2 97  ? 17.400  -13.589 -3.385  0.61 23.78 ?  97  MET   C SD   1 
ATOM   3230 S SD   B MET   C 2 97  ? 19.183  -12.261 -5.077  0.39 26.08 ?  97  MET   C SD   1 
ATOM   3231 C CE   A MET   C 2 97  ? 17.039  -15.124 -4.254  0.61 21.18 ?  97  MET   C CE   1 
ATOM   3232 C CE   B MET   C 2 97  ? 18.140  -12.982 -6.339  0.39 24.97 ?  97  MET   C CE   1 
ATOM   3233 N N    . VAL   C 2 98  ? 19.454  -17.838 -3.009  1.00 15.11 ?  98  VAL   C N    1 
ATOM   3234 C CA   . VAL   C 2 98  ? 19.695  -19.234 -3.340  1.00 15.22 ?  98  VAL   C CA   1 
ATOM   3235 C C    . VAL   C 2 98  ? 19.543  -19.391 -4.847  1.00 16.17 ?  98  VAL   C C    1 
ATOM   3236 O O    . VAL   C 2 98  ? 18.513  -19.033 -5.420  1.00 16.94 ?  98  VAL   C O    1 
ATOM   3237 C CB   . VAL   C 2 98  ? 18.731  -20.160 -2.574  1.00 14.42 ?  98  VAL   C CB   1 
ATOM   3238 C CG1  . VAL   C 2 98  ? 18.913  -21.617 -3.026  1.00 14.48 ?  98  VAL   C CG1  1 
ATOM   3239 C CG2  . VAL   C 2 98  ? 18.993  -20.036 -1.070  1.00 16.08 ?  98  VAL   C CG2  1 
ATOM   3240 N N    . ASP   C 2 99  ? 20.590  -19.889 -5.494  1.00 15.06 ?  99  ASP   C N    1 
ATOM   3241 C CA   . ASP   C 2 99  ? 20.557  -20.170 -6.925  1.00 13.20 ?  99  ASP   C CA   1 
ATOM   3242 C C    . ASP   C 2 99  ? 19.847  -21.500 -7.145  1.00 14.48 ?  99  ASP   C C    1 
ATOM   3243 O O    . ASP   C 2 99  ? 20.375  -22.554 -6.782  1.00 17.63 ?  99  ASP   C O    1 
ATOM   3244 C CB   . ASP   C 2 99  ? 21.992  -20.215 -7.450  1.00 19.20 ?  99  ASP   C CB   1 
ATOM   3245 C CG   . ASP   C 2 99  ? 22.074  -20.538 -8.918  1.00 22.19 ?  99  ASP   C CG   1 
ATOM   3246 O OD1  . ASP   C 2 99  ? 21.033  -20.665 -9.594  1.00 21.34 ?  99  ASP   C OD1  1 
ATOM   3247 O OD2  . ASP   C 2 99  ? 23.209  -20.685 -9.405  1.00 34.56 -1 99  ASP   C OD2  1 
ATOM   3248 N N    . ALA   C 2 100 ? 18.635  -21.446 -7.703  1.00 14.82 ?  100 ALA   C N    1 
ATOM   3249 C CA   . ALA   C 2 100 ? 17.843  -22.652 -7.926  1.00 14.95 ?  100 ALA   C CA   1 
ATOM   3250 C C    . ALA   C 2 100 ? 18.590  -23.696 -8.743  1.00 15.57 ?  100 ALA   C C    1 
ATOM   3251 O O    . ALA   C 2 100 ? 18.415  -24.895 -8.504  1.00 16.26 ?  100 ALA   C O    1 
ATOM   3252 C CB   . ALA   C 2 100 ? 16.526  -22.285 -8.611  1.00 17.55 ?  100 ALA   C CB   1 
ATOM   3253 N N    . ARG   C 2 101 ? 19.432  -23.274 -9.701  1.00 18.29 ?  101 ARG   C N    1 
ATOM   3254 C CA   . ARG   C 2 101 ? 20.198  -24.241 -10.484 1.00 20.88 ?  101 ARG   C CA   1 
ATOM   3255 C C    . ARG   C 2 101 ? 21.100  -25.121 -9.626  1.00 18.73 ?  101 ARG   C C    1 
ATOM   3256 O O    . ARG   C 2 101 ? 21.449  -26.232 -10.048 1.00 20.76 ?  101 ARG   C O    1 
ATOM   3257 C CB   . ARG   C 2 101 ? 21.053  -23.527 -11.537 1.00 23.68 ?  101 ARG   C CB   1 
ATOM   3258 C CG   . ARG   C 2 101 ? 20.243  -22.747 -12.563 1.00 27.40 ?  101 ARG   C CG   1 
ATOM   3259 C CD   . ARG   C 2 101 ? 21.154  -21.857 -13.419 1.00 35.16 ?  101 ARG   C CD   1 
ATOM   3260 N NE   . ARG   C 2 101 ? 22.017  -21.009 -12.607 1.00 39.31 ?  101 ARG   C NE   1 
ATOM   3261 C CZ   . ARG   C 2 101 ? 22.611  -19.902 -13.036 1.00 48.10 ?  101 ARG   C CZ   1 
ATOM   3262 N NH1  . ARG   C 2 101 ? 22.463  -19.472 -14.282 1.00 45.57 ?  101 ARG   C NH1  1 
ATOM   3263 N NH2  . ARG   C 2 101 ? 23.381  -19.214 -12.198 1.00 40.30 ?  101 ARG   C NH2  1 
ATOM   3264 N N    . SER   C 2 102 ? 21.506  -24.647 -8.450  1.00 18.29 ?  102 SER   C N    1 
ATOM   3265 C CA   . SER   C 2 102 ? 22.473  -25.334 -7.611  1.00 19.52 ?  102 SER   C CA   1 
ATOM   3266 C C    . SER   C 2 102 ? 21.840  -26.258 -6.584  1.00 14.66 ?  102 SER   C C    1 
ATOM   3267 O O    . SER   C 2 102 ? 22.564  -27.057 -5.985  1.00 16.89 ?  102 SER   C O    1 
ATOM   3268 C CB   . SER   C 2 102 ? 23.356  -24.313 -6.874  1.00 22.06 ?  102 SER   C CB   1 
ATOM   3269 O OG   . SER   C 2 102 ? 24.088  -23.524 -7.805  1.00 24.48 ?  102 SER   C OG   1 
ATOM   3270 N N    . ILE   C 2 103 ? 20.530  -26.157 -6.349  1.00 11.44 ?  103 ILE   C N    1 
ATOM   3271 C CA   . ILE   C 2 103 ? 19.843  -26.949 -5.329  1.00 14.79 ?  103 ILE   C CA   1 
ATOM   3272 C C    . ILE   C 2 103 ? 18.902  -27.923 -6.042  1.00 16.36 ?  103 ILE   C C    1 
ATOM   3273 O O    . ILE   C 2 103 ? 17.914  -27.486 -6.644  1.00 15.16 ?  103 ILE   C O    1 
ATOM   3274 C CB   . ILE   C 2 103 ? 19.063  -26.050 -4.358  1.00 14.48 ?  103 ILE   C CB   1 
ATOM   3275 C CG1  . ILE   C 2 103 ? 19.915  -24.904 -3.789  1.00 13.70 ?  103 ILE   C CG1  1 
ATOM   3276 C CG2  . ILE   C 2 103 ? 18.391  -26.896 -3.259  1.00 15.17 ?  103 ILE   C CG2  1 
ATOM   3277 C CD1  . ILE   C 2 103 ? 21.150  -25.369 -3.013  1.00 15.28 ?  103 ILE   C CD1  1 
ATOM   3278 N N    . PRO   C 2 104 ? 19.159  -29.236 -6.017  1.00 15.59 ?  104 PRO   C N    1 
ATOM   3279 C CA   . PRO   C 2 104 ? 18.362  -30.148 -6.864  1.00 20.51 ?  104 PRO   C CA   1 
ATOM   3280 C C    . PRO   C 2 104 ? 16.844  -30.053 -6.684  1.00 18.63 ?  104 PRO   C C    1 
ATOM   3281 O O    . PRO   C 2 104 ? 16.115  -30.106 -7.682  1.00 19.66 ?  104 PRO   C O    1 
ATOM   3282 C CB   . PRO   C 2 104 ? 18.912  -31.524 -6.463  1.00 18.79 ?  104 PRO   C CB   1 
ATOM   3283 C CG   . PRO   C 2 104 ? 20.362  -31.241 -6.186  1.00 21.14 ?  104 PRO   C CG   1 
ATOM   3284 C CD   . PRO   C 2 104 ? 20.334  -29.913 -5.433  1.00 18.06 ?  104 PRO   C CD   1 
ATOM   3285 N N    . VAL   C 2 105 ? 16.340  -29.920 -5.451  1.00 13.84 ?  105 VAL   C N    1 
ATOM   3286 C CA   . VAL   C 2 105 ? 14.893  -29.815 -5.245  1.00 18.57 ?  105 VAL   C CA   1 
ATOM   3287 C C    . VAL   C 2 105 ? 14.324  -28.623 -6.004  1.00 18.31 ?  105 VAL   C C    1 
ATOM   3288 O O    . VAL   C 2 105 ? 13.182  -28.666 -6.492  1.00 19.12 ?  105 VAL   C O    1 
ATOM   3289 C CB   . VAL   C 2 105 ? 14.570  -29.733 -3.738  1.00 18.54 ?  105 VAL   C CB   1 
ATOM   3290 C CG1  . VAL   C 2 105 ? 13.254  -28.980 -3.500  1.00 21.04 ?  105 VAL   C CG1  1 
ATOM   3291 C CG2  . VAL   C 2 105 ? 14.524  -31.125 -3.133  1.00 21.22 ?  105 VAL   C CG2  1 
ATOM   3292 N N    . LEU   C 2 106 ? 15.090  -27.528 -6.099  1.00 15.51 ?  106 LEU   C N    1 
ATOM   3293 C CA   . LEU   C 2 106 ? 14.590  -26.365 -6.829  1.00 14.66 ?  106 LEU   C CA   1 
ATOM   3294 C C    . LEU   C 2 106 ? 14.828  -26.506 -8.332  1.00 16.89 ?  106 LEU   C C    1 
ATOM   3295 O O    . LEU   C 2 106 ? 13.963  -26.133 -9.135  1.00 19.81 ?  106 LEU   C O    1 
ATOM   3296 C CB   . LEU   C 2 106 ? 15.246  -25.080 -6.324  1.00 15.18 ?  106 LEU   C CB   1 
ATOM   3297 C CG   . LEU   C 2 106 ? 14.976  -24.725 -4.854  1.00 12.27 ?  106 LEU   C CG   1 
ATOM   3298 C CD1  . LEU   C 2 106 ? 15.906  -23.569 -4.451  1.00 15.73 ?  106 LEU   C CD1  1 
ATOM   3299 C CD2  . LEU   C 2 106 ? 13.516  -24.328 -4.649  1.00 14.16 ?  106 LEU   C CD2  1 
ATOM   3300 N N    . ALA   C 2 107 ? 16.007  -27.015 -8.712  1.00 15.56 ?  107 ALA   C N    1 
ATOM   3301 C CA   . ALA   C 2 107 ? 16.355  -27.187 -10.120 1.00 15.50 ?  107 ALA   C CA   1 
ATOM   3302 C C    . ALA   C 2 107 ? 15.435  -28.193 -10.795 1.00 18.20 ?  107 ALA   C C    1 
ATOM   3303 O O    . ALA   C 2 107 ? 15.066  -28.022 -11.965 1.00 23.53 ?  107 ALA   C O    1 
ATOM   3304 C CB   . ALA   C 2 107 ? 17.814  -27.644 -10.251 1.00 14.70 ?  107 ALA   C CB   1 
ATOM   3305 N N    A LYS   C 2 108 ? 15.080  -29.259 -10.080 0.50 18.54 ?  108 LYS   C N    1 
ATOM   3306 N N    B LYS   C 2 108 ? 15.072  -29.256 -10.081 0.50 18.54 ?  108 LYS   C N    1 
ATOM   3307 C CA   A LYS   C 2 108 ? 14.170  -30.285 -10.571 0.50 21.13 ?  108 LYS   C CA   1 
ATOM   3308 C CA   B LYS   C 2 108 ? 14.165  -30.269 -10.597 0.50 21.12 ?  108 LYS   C CA   1 
ATOM   3309 C C    A LYS   C 2 108 ? 12.860  -30.227 -9.797  0.50 19.91 ?  108 LYS   C C    1 
ATOM   3310 C C    B LYS   C 2 108 ? 12.862  -30.226 -9.809  0.50 19.91 ?  108 LYS   C C    1 
ATOM   3311 O O    A LYS   C 2 108 ? 12.371  -31.254 -9.319  0.50 23.55 ?  108 LYS   C O    1 
ATOM   3312 O O    B LYS   C 2 108 ? 12.384  -31.259 -9.332  0.50 23.55 ?  108 LYS   C O    1 
ATOM   3313 C CB   A LYS   C 2 108 ? 14.793  -31.677 -10.438 0.50 24.48 ?  108 LYS   C CB   1 
ATOM   3314 C CB   B LYS   C 2 108 ? 14.794  -31.662 -10.512 0.50 24.48 ?  108 LYS   C CB   1 
ATOM   3315 C CG   A LYS   C 2 108 ? 16.180  -31.814 -11.017 0.50 27.74 ?  108 LYS   C CG   1 
ATOM   3316 C CG   B LYS   C 2 108 ? 16.201  -31.755 -11.070 0.50 27.73 ?  108 LYS   C CG   1 
ATOM   3317 C CD   A LYS   C 2 108 ? 16.199  -31.463 -12.489 0.50 31.00 ?  108 LYS   C CD   1 
ATOM   3318 C CD   B LYS   C 2 108 ? 16.270  -31.350 -12.531 0.50 31.11 ?  108 LYS   C CD   1 
ATOM   3319 C CE   A LYS   C 2 108 ? 17.536  -31.840 -13.116 0.50 35.56 ?  108 LYS   C CE   1 
ATOM   3320 C CE   B LYS   C 2 108 ? 17.599  -31.789 -13.150 0.50 35.54 ?  108 LYS   C CE   1 
ATOM   3321 N NZ   A LYS   C 2 108 ? 17.432  -31.885 -14.597 0.50 30.80 ?  108 LYS   C NZ   1 
ATOM   3322 N NZ   B LYS   C 2 108 ? 18.592  -30.681 -13.232 0.50 32.21 ?  108 LYS   C NZ   1 
ATOM   3323 N N    . TRP   C 2 109 ? 12.296  -29.031 -9.662  1.00 21.14 ?  109 TRP   C N    1 
ATOM   3324 C CA   . TRP   C 2 109 ? 11.096  -28.854 -8.850  1.00 18.90 ?  109 TRP   C CA   1 
ATOM   3325 C C    . TRP   C 2 109 ? 9.935   -29.729 -9.334  1.00 21.45 ?  109 TRP   C C    1 
ATOM   3326 O O    . TRP   C 2 109 ? 9.703   -29.875 -10.538 1.00 24.09 ?  109 TRP   C O    1 
ATOM   3327 C CB   . TRP   C 2 109 ? 10.686  -27.374 -8.868  1.00 18.47 ?  109 TRP   C CB   1 
ATOM   3328 C CG   . TRP   C 2 109 ? 9.472   -27.060 -8.036  1.00 18.70 ?  109 TRP   C CG   1 
ATOM   3329 C CD1  . TRP   C 2 109 ? 8.195   -26.869 -8.491  1.00 22.26 ?  109 TRP   C CD1  1 
ATOM   3330 C CD2  . TRP   C 2 109 ? 9.425   -26.894 -6.615  1.00 19.51 ?  109 TRP   C CD2  1 
ATOM   3331 N NE1  . TRP   C 2 109 ? 7.350   -26.611 -7.432  1.00 20.84 ?  109 TRP   C NE1  1 
ATOM   3332 C CE2  . TRP   C 2 109 ? 8.086   -26.602 -6.272  1.00 21.70 ?  109 TRP   C CE2  1 
ATOM   3333 C CE3  . TRP   C 2 109 ? 10.390  -26.947 -5.599  1.00 17.11 ?  109 TRP   C CE3  1 
ATOM   3334 C CZ2  . TRP   C 2 109 ? 7.679   -26.386 -4.953  1.00 19.61 ?  109 TRP   C CZ2  1 
ATOM   3335 C CZ3  . TRP   C 2 109 ? 9.988   -26.731 -4.282  1.00 15.46 ?  109 TRP   C CZ3  1 
ATOM   3336 C CH2  . TRP   C 2 109 ? 8.634   -26.453 -3.972  1.00 16.08 ?  109 TRP   C CH2  1 
ATOM   3337 N N    A GLN   C 2 110 ? 9.213   -30.327 -8.384  0.50 20.85 ?  110 GLN   C N    1 
ATOM   3338 N N    B GLN   C 2 110 ? 9.205   -30.309 -8.377  0.50 20.84 ?  110 GLN   C N    1 
ATOM   3339 C CA   A GLN   C 2 110 ? 7.955   -31.015 -8.656  0.50 22.25 ?  110 GLN   C CA   1 
ATOM   3340 C CA   B GLN   C 2 110 ? 7.958   -31.019 -8.640  0.50 22.27 ?  110 GLN   C CA   1 
ATOM   3341 C C    A GLN   C 2 110 ? 6.852   -30.346 -7.849  0.50 24.08 ?  110 GLN   C C    1 
ATOM   3342 C C    B GLN   C 2 110 ? 6.845   -30.373 -7.825  0.50 24.09 ?  110 GLN   C C    1 
ATOM   3343 O O    A GLN   C 2 110 ? 7.102   -29.810 -6.767  0.50 21.35 ?  110 GLN   C O    1 
ATOM   3344 O O    B GLN   C 2 110 ? 7.079   -29.888 -6.715  0.50 21.37 ?  110 GLN   C O    1 
ATOM   3345 C CB   A GLN   C 2 110 ? 8.021   -32.507 -8.289  0.50 26.15 ?  110 GLN   C CB   1 
ATOM   3346 C CB   B GLN   C 2 110 ? 8.059   -32.505 -8.266  0.50 26.17 ?  110 GLN   C CB   1 
ATOM   3347 C CG   A GLN   C 2 110 ? 9.366   -33.173 -8.547  0.50 26.30 ?  110 GLN   C CG   1 
ATOM   3348 C CG   B GLN   C 2 110 ? 9.347   -33.181 -8.702  0.50 26.32 ?  110 GLN   C CG   1 
ATOM   3349 C CD   A GLN   C 2 110 ? 9.491   -33.723 -9.955  0.50 28.59 ?  110 GLN   C CD   1 
ATOM   3350 C CD   B GLN   C 2 110 ? 9.255   -34.690 -8.616  0.50 25.15 ?  110 GLN   C CD   1 
ATOM   3351 O OE1  A GLN   C 2 110 ? 10.405  -33.364 -10.698 0.50 32.32 ?  110 GLN   C OE1  1 
ATOM   3352 O OE1  B GLN   C 2 110 ? 8.494   -35.231 -7.811  0.50 32.31 ?  110 GLN   C OE1  1 
ATOM   3353 N NE2  A GLN   C 2 110 ? 8.563   -34.597 -10.331 0.50 32.22 ?  110 GLN   C NE2  1 
ATOM   3354 N NE2  B GLN   C 2 110 ? 10.033  -35.380 -9.442  0.50 32.22 ?  110 GLN   C NE2  1 
ATOM   3355 N N    . ASN   C 2 111 ? 5.619   -30.390 -8.366  1.00 25.57 ?  111 ASN   C N    1 
ATOM   3356 C CA   . ASN   C 2 111 ? 4.536   -29.678 -7.688  1.00 25.26 ?  111 ASN   C CA   1 
ATOM   3357 C C    . ASN   C 2 111 ? 4.060   -30.382 -6.425  1.00 21.55 ?  111 ASN   C C    1 
ATOM   3358 O O    . ASN   C 2 111 ? 3.194   -29.837 -5.732  1.00 23.52 ?  111 ASN   C O    1 
ATOM   3359 C CB   . ASN   C 2 111 ? 3.350   -29.384 -8.639  1.00 23.57 ?  111 ASN   C CB   1 
ATOM   3360 C CG   . ASN   C 2 111 ? 2.575   -30.621 -9.069  1.00 25.79 ?  111 ASN   C CG   1 
ATOM   3361 O OD1  . ASN   C 2 111 ? 2.708   -31.704 -8.509  1.00 27.07 ?  111 ASN   C OD1  1 
ATOM   3362 N ND2  . ASN   C 2 111 ? 1.719   -30.437 -10.070 1.00 28.85 ?  111 ASN   C ND2  1 
ATOM   3363 N N    . SER   C 2 112 ? 4.629   -31.536 -6.087  1.00 18.55 ?  112 SER   C N    1 
ATOM   3364 C CA   . SER   C 2 112 ? 4.434   -32.173 -4.796  1.00 20.73 ?  112 SER   C CA   1 
ATOM   3365 C C    . SER   C 2 112 ? 5.391   -31.665 -3.722  1.00 25.17 ?  112 SER   C C    1 
ATOM   3366 O O    . SER   C 2 112 ? 5.212   -32.011 -2.550  1.00 21.86 ?  112 SER   C O    1 
ATOM   3367 C CB   . SER   C 2 112 ? 4.590   -33.690 -4.923  1.00 27.75 ?  112 SER   C CB   1 
ATOM   3368 O OG   . SER   C 2 112 ? 5.889   -34.045 -5.377  1.00 29.48 ?  112 SER   C OG   1 
ATOM   3369 N N    . TYR   C 2 113 ? 6.413   -30.892 -4.088  1.00 17.47 ?  113 TYR   C N    1 
ATOM   3370 C CA   . TYR   C 2 113 ? 7.298   -30.326 -3.072  1.00 16.36 ?  113 TYR   C CA   1 
ATOM   3371 C C    . TYR   C 2 113 ? 6.606   -29.162 -2.343  1.00 19.49 ?  113 TYR   C C    1 
ATOM   3372 O O    . TYR   C 2 113 ? 5.498   -28.738 -2.688  1.00 19.53 ?  113 TYR   C O    1 
ATOM   3373 C CB   . TYR   C 2 113 ? 8.613   -29.861 -3.716  1.00 14.77 ?  113 TYR   C CB   1 
ATOM   3374 C CG   . TYR   C 2 113 ? 9.451   -30.985 -4.306  1.00 18.88 ?  113 TYR   C CG   1 
ATOM   3375 C CD1  . TYR   C 2 113 ? 9.253   -32.304 -3.929  1.00 16.97 ?  113 TYR   C CD1  1 
ATOM   3376 C CD2  . TYR   C 2 113 ? 10.457  -30.712 -5.227  1.00 15.73 ?  113 TYR   C CD2  1 
ATOM   3377 C CE1  . TYR   C 2 113 ? 10.048  -33.336 -4.471  1.00 17.76 ?  113 TYR   C CE1  1 
ATOM   3378 C CE2  . TYR   C 2 113 ? 11.251  -31.732 -5.760  1.00 17.15 ?  113 TYR   C CE2  1 
ATOM   3379 C CZ   . TYR   C 2 113 ? 11.042  -33.035 -5.382  1.00 17.68 ?  113 TYR   C CZ   1 
ATOM   3380 O OH   . TYR   C 2 113 ? 11.844  -34.042 -5.923  1.00 21.85 ?  113 TYR   C OH   1 
ATOM   3381 N N    . SER   C 2 114 ? 7.280   -28.627 -1.326  1.00 13.04 ?  114 SER   C N    1 
ATOM   3382 C CA   . SER   C 2 114 ? 6.679   -27.673 -0.389  1.00 12.83 ?  114 SER   C CA   1 
ATOM   3383 C C    . SER   C 2 114 ? 7.778   -26.820 0.241   1.00 12.31 ?  114 SER   C C    1 
ATOM   3384 O O    . SER   C 2 114 ? 8.966   -27.107 0.085   1.00 14.48 ?  114 SER   C O    1 
ATOM   3385 C CB   . SER   C 2 114 ? 5.920   -28.397 0.724   1.00 15.13 ?  114 SER   C CB   1 
ATOM   3386 O OG   . SER   C 2 114 ? 6.815   -29.222 1.490   1.00 15.91 ?  114 SER   C OG   1 
ATOM   3387 N N    . ILE   C 2 115 ? 7.372   -25.802 1.011   1.00 12.05 ?  115 ILE   C N    1 
ATOM   3388 C CA   . ILE   C 2 115 ? 8.362   -25.004 1.746   1.00 11.58 ?  115 ILE   C CA   1 
ATOM   3389 C C    . ILE   C 2 115 ? 9.145   -25.899 2.696   1.00 13.36 ?  115 ILE   C C    1 
ATOM   3390 O O    . ILE   C 2 115 ? 10.381  -25.802 2.794   1.00 11.68 ?  115 ILE   C O    1 
ATOM   3391 C CB   . ILE   C 2 115 ? 7.689   -23.854 2.522   1.00 15.26 ?  115 ILE   C CB   1 
ATOM   3392 C CG1  . ILE   C 2 115 ? 6.958   -22.899 1.591   1.00 16.24 ?  115 ILE   C CG1  1 
ATOM   3393 C CG2  . ILE   C 2 115 ? 8.716   -23.130 3.390   1.00 15.66 ?  115 ILE   C CG2  1 
ATOM   3394 C CD1  . ILE   C 2 115 ? 5.962   -21.996 2.340   1.00 14.81 ?  115 ILE   C CD1  1 
ATOM   3395 N N    . LYS   C 2 116 ? 8.442   -26.781 3.415   1.00 12.40 ?  116 LYS   C N    1 
ATOM   3396 C CA   . LYS   C 2 116 ? 9.134   -27.679 4.337   1.00 14.52 ?  116 LYS   C CA   1 
ATOM   3397 C C    . LYS   C 2 116 ? 10.189  -28.493 3.600   1.00 15.42 ?  116 LYS   C C    1 
ATOM   3398 O O    . LYS   C 2 116 ? 11.306  -28.676 4.103   1.00 15.64 ?  116 LYS   C O    1 
ATOM   3399 C CB   . LYS   C 2 116 ? 8.141   -28.617 5.034   1.00 19.33 ?  116 LYS   C CB   1 
ATOM   3400 C CG   . LYS   C 2 116 ? 8.817   -29.821 5.719   1.00 21.06 ?  116 LYS   C CG   1 
ATOM   3401 C CD   . LYS   C 2 116 ? 7.818   -30.703 6.465   1.00 20.93 ?  116 LYS   C CD   1 
ATOM   3402 C CE   . LYS   C 2 116 ? 7.182   -31.680 5.499   1.00 31.80 ?  116 LYS   C CE   1 
ATOM   3403 N NZ   . LYS   C 2 116 ? 6.223   -32.615 6.176   1.00 40.94 ?  116 LYS   C NZ   1 
ATOM   3404 N N    . VAL   C 2 117 ? 9.843   -29.006 2.415   1.00 14.30 ?  117 VAL   C N    1 
ATOM   3405 C CA   . VAL   C 2 117 ? 10.777  -29.840 1.664   1.00 11.53 ?  117 VAL   C CA   1 
ATOM   3406 C C    . VAL   C 2 117 ? 11.991  -29.026 1.232   1.00 13.04 ?  117 VAL   C C    1 
ATOM   3407 O O    . VAL   C 2 117 ? 13.122  -29.520 1.282   1.00 14.52 ?  117 VAL   C O    1 
ATOM   3408 C CB   . VAL   C 2 117 ? 10.065  -30.494 0.467   1.00 16.03 ?  117 VAL   C CB   1 
ATOM   3409 C CG1  . VAL   C 2 117 ? 11.053  -31.033 -0.568  1.00 15.37 ?  117 VAL   C CG1  1 
ATOM   3410 C CG2  . VAL   C 2 117 ? 9.132   -31.617 0.990   1.00 17.76 ?  117 VAL   C CG2  1 
ATOM   3411 N N    . VAL   C 2 118 ? 11.781  -27.767 0.825   1.00 12.34 ?  118 VAL   C N    1 
ATOM   3412 C CA   . VAL   C 2 118 ? 12.907  -26.894 0.465   1.00 11.82 ?  118 VAL   C CA   1 
ATOM   3413 C C    . VAL   C 2 118 ? 13.836  -26.699 1.665   1.00 12.44 ?  118 VAL   C C    1 
ATOM   3414 O O    . VAL   C 2 118 ? 15.076  -26.759 1.543   1.00 10.92 ?  118 VAL   C O    1 
ATOM   3415 C CB   . VAL   C 2 118 ? 12.388  -25.541 -0.061  1.00 12.37 ?  118 VAL   C CB   1 
ATOM   3416 C CG1  . VAL   C 2 118 ? 13.541  -24.581 -0.274  1.00 16.60 ?  118 VAL   C CG1  1 
ATOM   3417 C CG2  . VAL   C 2 118 ? 11.620  -25.736 -1.367  1.00 16.43 ?  118 VAL   C CG2  1 
ATOM   3418 N N    . LEU   C 2 119 ? 13.254  -26.417 2.831   1.00 11.97 ?  119 LEU   C N    1 
ATOM   3419 C CA   . LEU   C 2 119 ? 14.084  -26.157 4.013   1.00 10.35 ?  119 LEU   C CA   1 
ATOM   3420 C C    . LEU   C 2 119 ? 14.823  -27.421 4.458   1.00 11.89 ?  119 LEU   C C    1 
ATOM   3421 O O    . LEU   C 2 119 ? 15.998  -27.357 4.845   1.00 12.34 ?  119 LEU   C O    1 
ATOM   3422 C CB   . LEU   C 2 119 ? 13.241  -25.582 5.166   1.00 14.13 ?  119 LEU   C CB   1 
ATOM   3423 C CG   . LEU   C 2 119 ? 12.579  -24.207 4.905   1.00 14.63 ?  119 LEU   C CG   1 
ATOM   3424 C CD1  . LEU   C 2 119 ? 11.726  -23.770 6.123   1.00 13.52 ?  119 LEU   C CD1  1 
ATOM   3425 C CD2  . LEU   C 2 119 ? 13.602  -23.151 4.586   1.00 13.84 ?  119 LEU   C CD2  1 
ATOM   3426 N N    . GLN   C 2 120 ? 14.169  -28.582 4.386   1.00 13.04 ?  120 GLN   C N    1 
ATOM   3427 C CA   . GLN   C 2 120 ? 14.862  -29.816 4.753   1.00 14.14 ?  120 GLN   C CA   1 
ATOM   3428 C C    . GLN   C 2 120 ? 15.949  -30.152 3.734   1.00 11.85 ?  120 GLN   C C    1 
ATOM   3429 O O    . GLN   C 2 120 ? 17.011  -30.668 4.103   1.00 14.60 ?  120 GLN   C O    1 
ATOM   3430 C CB   . GLN   C 2 120 ? 13.846  -30.951 4.903   1.00 15.71 ?  120 GLN   C CB   1 
ATOM   3431 C CG   . GLN   C 2 120 ? 13.067  -30.824 6.196   1.00 16.72 ?  120 GLN   C CG   1 
ATOM   3432 C CD   . GLN   C 2 120 ? 11.900  -31.794 6.323   1.00 19.94 ?  120 GLN   C CD   1 
ATOM   3433 O OE1  . GLN   C 2 120 ? 11.418  -32.334 5.339   1.00 24.11 ?  120 GLN   C OE1  1 
ATOM   3434 N NE2  . GLN   C 2 120 ? 11.460  -32.020 7.551   1.00 28.31 ?  120 GLN   C NE2  1 
ATOM   3435 N N    . GLU   C 2 121 ? 15.705  -29.862 2.451   1.00 12.37 ?  121 GLU   C N    1 
ATOM   3436 C CA   . GLU   C 2 121 ? 16.732  -30.062 1.431   1.00 11.07 ?  121 GLU   C CA   1 
ATOM   3437 C C    . GLU   C 2 121 ? 17.966  -29.237 1.763   1.00 13.47 ?  121 GLU   C C    1 
ATOM   3438 O O    . GLU   C 2 121 ? 19.108  -29.727 1.691   1.00 12.80 ?  121 GLU   C O    1 
ATOM   3439 C CB   . GLU   C 2 121 ? 16.183  -29.699 0.038   1.00 13.56 ?  121 GLU   C CB   1 
ATOM   3440 C CG   . GLU   C 2 121 ? 17.277  -29.540 -1.068  1.00 13.64 ?  121 GLU   C CG   1 
ATOM   3441 C CD   . GLU   C 2 121 ? 17.657  -30.852 -1.760  1.00 16.60 ?  121 GLU   C CD   1 
ATOM   3442 O OE1  . GLU   C 2 121 ? 17.532  -31.921 -1.116  1.00 17.05 ?  121 GLU   C OE1  1 
ATOM   3443 O OE2  . GLU   C 2 121 ? 18.092  -30.795 -2.930  1.00 13.00 -1 121 GLU   C OE2  1 
ATOM   3444 N N    . LEU   C 2 122 ? 17.758  -27.962 2.112   1.00 10.63 ?  122 LEU   C N    1 
ATOM   3445 C CA   . LEU   C 2 122 ? 18.916  -27.132 2.451   1.00 13.51 ?  122 LEU   C CA   1 
ATOM   3446 C C    . LEU   C 2 122 ? 19.638  -27.657 3.698   1.00 14.31 ?  122 LEU   C C    1 
ATOM   3447 O O    . LEU   C 2 122 ? 20.884  -27.739 3.720   1.00 12.48 ?  122 LEU   C O    1 
ATOM   3448 C CB   . LEU   C 2 122 ? 18.485  -25.667 2.617   1.00 10.10 ?  122 LEU   C CB   1 
ATOM   3449 C CG   . LEU   C 2 122 ? 18.079  -25.002 1.292   1.00 10.01 ?  122 LEU   C CG   1 
ATOM   3450 C CD1  . LEU   C 2 122 ? 17.417  -23.682 1.638   1.00 13.47 ?  122 LEU   C CD1  1 
ATOM   3451 C CD2  . LEU   C 2 122 ? 19.287  -24.749 0.394   1.00 14.40 ?  122 LEU   C CD2  1 
ATOM   3452 N N    . ARG   C 2 123 ? 18.885  -28.021 4.748   1.00 13.87 ?  123 ARG   C N    1 
ATOM   3453 C CA   . ARG   C 2 123 ? 19.534  -28.553 5.944   1.00 13.45 ?  123 ARG   C CA   1 
ATOM   3454 C C    . ARG   C 2 123 ? 20.326  -29.822 5.640   1.00 12.17 ?  123 ARG   C C    1 
ATOM   3455 O O    . ARG   C 2 123 ? 21.409  -30.035 6.202   1.00 13.52 ?  123 ARG   C O    1 
ATOM   3456 C CB   . ARG   C 2 123 ? 18.497  -28.823 7.042   1.00 13.31 ?  123 ARG   C CB   1 
ATOM   3457 C CG   . ARG   C 2 123 ? 19.128  -29.218 8.388   1.00 12.51 ?  123 ARG   C CG   1 
ATOM   3458 C CD   . ARG   C 2 123 ? 18.042  -29.307 9.477   1.00 14.65 ?  123 ARG   C CD   1 
ATOM   3459 N NE   . ARG   C 2 123 ? 18.639  -29.650 10.762  1.00 15.73 ?  123 ARG   C NE   1 
ATOM   3460 C CZ   . ARG   C 2 123 ? 18.791  -30.890 11.199  1.00 19.18 ?  123 ARG   C CZ   1 
ATOM   3461 N NH1  . ARG   C 2 123 ? 18.398  -31.926 10.476  1.00 18.76 ?  123 ARG   C NH1  1 
ATOM   3462 N NH2  . ARG   C 2 123 ? 19.372  -31.095 12.382  1.00 22.05 ?  123 ARG   C NH2  1 
ATOM   3463 N N    . ARG   C 2 124 ? 19.808  -30.680 4.761   1.00 11.91 ?  124 ARG   C N    1 
ATOM   3464 C CA   . ARG   C 2 124 ? 20.505  -31.925 4.450   1.00 11.21 ?  124 ARG   C CA   1 
ATOM   3465 C C    . ARG   C 2 124 ? 21.672  -31.705 3.493   1.00 13.44 ?  124 ARG   C C    1 
ATOM   3466 O O    . ARG   C 2 124 ? 22.654  -32.455 3.540   1.00 14.67 ?  124 ARG   C O    1 
ATOM   3467 C CB   . ARG   C 2 124 ? 19.513  -32.941 3.877   1.00 14.36 ?  124 ARG   C CB   1 
ATOM   3468 C CG   . ARG   C 2 124 ? 18.513  -33.402 4.983   1.00 11.30 ?  124 ARG   C CG   1 
ATOM   3469 C CD   . ARG   C 2 124 ? 17.176  -33.981 4.468   1.00 15.51 ?  124 ARG   C CD   1 
ATOM   3470 N NE   . ARG   C 2 124 ? 16.225  -34.009 5.577   1.00 19.08 ?  124 ARG   C NE   1 
ATOM   3471 C CZ   . ARG   C 2 124 ? 15.024  -34.570 5.543   1.00 15.49 ?  124 ARG   C CZ   1 
ATOM   3472 N NH1  . ARG   C 2 124 ? 14.589  -35.196 4.469   1.00 19.31 ?  124 ARG   C NH1  1 
ATOM   3473 N NH2  . ARG   C 2 124 ? 14.251  -34.520 6.633   1.00 17.20 ?  124 ARG   C NH2  1 
ATOM   3474 N N    . LEU   C 2 125 ? 21.604  -30.679 2.652   1.00 13.60 ?  125 LEU   C N    1 
ATOM   3475 C CA   . LEU   C 2 125 ? 22.784  -30.316 1.859   1.00 12.78 ?  125 LEU   C CA   1 
ATOM   3476 C C    . LEU   C 2 125 ? 23.880  -29.723 2.734   1.00 15.01 ?  125 LEU   C C    1 
ATOM   3477 O O    . LEU   C 2 125 ? 25.055  -29.787 2.356   1.00 15.54 ?  125 LEU   C O    1 
ATOM   3478 C CB   . LEU   C 2 125 ? 22.379  -29.336 0.738   1.00 10.20 ?  125 LEU   C CB   1 
ATOM   3479 C CG   . LEU   C 2 125 ? 21.643  -29.948 -0.445  1.00 14.59 ?  125 LEU   C CG   1 
ATOM   3480 C CD1  . LEU   C 2 125 ? 21.038  -28.860 -1.332  1.00 15.44 ?  125 LEU   C CD1  1 
ATOM   3481 C CD2  . LEU   C 2 125 ? 22.647  -30.795 -1.245  1.00 15.32 ?  125 LEU   C CD2  1 
ATOM   3482 N N    . MET   C 2 126 ? 23.527  -29.151 3.888   1.00 14.45 ?  126 MET   C N    1 
ATOM   3483 C CA   . MET   C 2 126 ? 24.550  -28.711 4.836   1.00 12.89 ?  126 MET   C CA   1 
ATOM   3484 C C    . MET   C 2 126 ? 25.390  -29.887 5.340   1.00 15.46 ?  126 MET   C C    1 
ATOM   3485 O O    . MET   C 2 126 ? 26.523  -29.685 5.790   1.00 17.62 ?  126 MET   C O    1 
ATOM   3486 C CB   . MET   C 2 126 ? 23.888  -28.003 6.008   1.00 15.22 ?  126 MET   C CB   1 
ATOM   3487 C CG   . MET   C 2 126 ? 23.414  -26.599 5.656   1.00 14.37 ?  126 MET   C CG   1 
ATOM   3488 S SD   . MET   C 2 126 ? 22.494  -25.896 7.026   1.00 15.76 ?  126 MET   C SD   1 
ATOM   3489 C CE   . MET   C 2 126 ? 21.504  -24.689 6.105   1.00 12.65 ?  126 MET   C CE   1 
ATOM   3490 N N    . MET   C 2 127 ? 24.848  -31.105 5.281   1.00 15.85 ?  127 MET   C N    1 
ATOM   3491 C CA   . MET   C 2 127 ? 25.571  -32.305 5.681   1.00 19.43 ?  127 MET   C CA   1 
ATOM   3492 C C    . MET   C 2 127 ? 26.466  -32.877 4.583   1.00 19.13 ?  127 MET   C C    1 
ATOM   3493 O O    . MET   C 2 127 ? 27.220  -33.816 4.864   1.00 20.09 ?  127 MET   C O    1 
ATOM   3494 C CB   . MET   C 2 127 ? 24.577  -33.389 6.143   1.00 15.89 ?  127 MET   C CB   1 
ATOM   3495 C CG   . MET   C 2 127 ? 23.422  -32.885 6.958   1.00 17.46 ?  127 MET   C CG   1 
ATOM   3496 S SD   . MET   C 2 127 ? 22.172  -34.192 7.233   1.00 21.53 ?  127 MET   C SD   1 
ATOM   3497 C CE   . MET   C 2 127 ? 21.116  -33.387 8.428   1.00 25.11 ?  127 MET   C CE   1 
ATOM   3498 N N    . SER   C 2 128 ? 26.429  -32.353 3.357   1.00 15.49 ?  128 SER   C N    1 
ATOM   3499 C CA   . SER   C 2 128 ? 27.170  -32.966 2.258   1.00 19.98 ?  128 SER   C CA   1 
ATOM   3500 C C    . SER   C 2 128 ? 28.677  -32.734 2.408   1.00 21.83 ?  128 SER   C C    1 
ATOM   3501 O O    . SER   C 2 128 ? 29.123  -31.788 3.055   1.00 19.96 ?  128 SER   C O    1 
ATOM   3502 C CB   . SER   C 2 128 ? 26.715  -32.412 0.912   1.00 22.36 ?  128 SER   C CB   1 
ATOM   3503 O OG   . SER   C 2 128 ? 27.311  -31.141 0.680   1.00 21.13 ?  128 SER   C OG   1 
ATOM   3504 N N    . LYS   C 2 129 ? 29.465  -33.603 1.767   1.00 21.47 ?  129 LYS   C N    1 
ATOM   3505 C CA   . LYS   C 2 129 ? 30.917  -33.479 1.913   1.00 21.34 ?  129 LYS   C CA   1 
ATOM   3506 C C    . LYS   C 2 129 ? 31.445  -32.186 1.302   1.00 21.58 ?  129 LYS   C C    1 
ATOM   3507 O O    . LYS   C 2 129 ? 32.458  -31.651 1.777   1.00 27.24 ?  129 LYS   C O    1 
ATOM   3508 C CB   . LYS   C 2 129 ? 31.641  -34.690 1.309   1.00 28.33 ?  129 LYS   C CB   1 
ATOM   3509 C CG   . LYS   C 2 129 ? 30.921  -35.373 0.166   1.00 38.22 ?  129 LYS   C CG   1 
ATOM   3510 C CD   . LYS   C 2 129 ? 31.633  -36.673 -0.226  1.00 46.41 ?  129 LYS   C CD   1 
ATOM   3511 C CE   . LYS   C 2 129 ? 31.470  -37.731 0.871   1.00 44.80 ?  129 LYS   C CE   1 
ATOM   3512 N NZ   . LYS   C 2 129 ? 32.366  -38.921 0.711   1.00 35.54 ?  129 LYS   C NZ   1 
ATOM   3513 N N    . GLU   C 2 130 ? 30.797  -31.661 0.255   1.00 18.58 ?  130 GLU   C N    1 
ATOM   3514 C CA   . GLU   C 2 130 ? 31.242  -30.389 -0.298  1.00 20.68 ?  130 GLU   C CA   1 
ATOM   3515 C C    . GLU   C 2 130 ? 30.957  -29.198 0.623   1.00 24.31 ?  130 GLU   C C    1 
ATOM   3516 O O    . GLU   C 2 130 ? 31.680  -28.195 0.549   1.00 18.52 ?  130 GLU   C O    1 
ATOM   3517 C CB   . GLU   C 2 130 ? 30.628  -30.162 -1.692  1.00 23.51 ?  130 GLU   C CB   1 
ATOM   3518 C CG   . GLU   C 2 130 ? 29.144  -29.899 -1.674  1.00 31.14 ?  130 GLU   C CG   1 
ATOM   3519 C CD   . GLU   C 2 130 ? 28.324  -31.169 -1.905  1.00 45.36 ?  130 GLU   C CD   1 
ATOM   3520 O OE1  . GLU   C 2 130 ? 28.855  -32.289 -1.666  1.00 30.56 ?  130 GLU   C OE1  1 
ATOM   3521 O OE2  . GLU   C 2 130 ? 27.105  -31.033 -2.213  1.00 33.08 -1 130 GLU   C OE2  1 
ATOM   3522 N N    . ASN   C 2 131 ? 29.942  -29.271 1.496   1.00 14.20 ?  131 ASN   C N    1 
ATOM   3523 C CA   . ASN   C 2 131 ? 29.561  -28.106 2.297   1.00 15.87 ?  131 ASN   C CA   1 
ATOM   3524 C C    . ASN   C 2 131 ? 30.016  -28.161 3.748   1.00 14.68 ?  131 ASN   C C    1 
ATOM   3525 O O    . ASN   C 2 131 ? 30.310  -27.113 4.339   1.00 16.25 ?  131 ASN   C O    1 
ATOM   3526 C CB   . ASN   C 2 131 ? 28.032  -27.940 2.304   1.00 13.31 ?  131 ASN   C CB   1 
ATOM   3527 C CG   . ASN   C 2 131 ? 27.485  -27.398 0.983   1.00 13.85 ?  131 ASN   C CG   1 
ATOM   3528 O OD1  . ASN   C 2 131 ? 28.090  -26.532 0.326   1.00 16.18 ?  131 ASN   C OD1  1 
ATOM   3529 N ND2  . ASN   C 2 131 ? 26.302  -27.899 0.591   1.00 14.53 ?  131 ASN   C ND2  1 
ATOM   3530 N N    . MET   C 2 132 ? 30.058  -29.346 4.349   1.00 15.62 ?  132 MET   C N    1 
ATOM   3531 C CA   . MET   C 2 132 ? 30.099  -29.445 5.806   1.00 16.83 ?  132 MET   C CA   1 
ATOM   3532 C C    . MET   C 2 132 ? 31.378  -28.889 6.419   1.00 18.61 ?  132 MET   C C    1 
ATOM   3533 O O    . MET   C 2 132 ? 31.364  -28.507 7.590   1.00 18.49 ?  132 MET   C O    1 
ATOM   3534 C CB   . MET   C 2 132 ? 29.863  -30.909 6.206   1.00 23.53 ?  132 MET   C CB   1 
ATOM   3535 C CG   . MET   C 2 132 ? 30.717  -31.907 5.396   1.00 27.94 ?  132 MET   C CG   1 
ATOM   3536 S SD   . MET   C 2 132 ? 30.796  -33.586 6.069   1.00 28.52 ?  132 MET   C SD   1 
ATOM   3537 C CE   . MET   C 2 132 ? 30.719  -33.285 7.813   1.00 25.08 ?  132 MET   C CE   1 
ATOM   3538 N N    . LYS   C 2 133 ? 32.462  -28.794 5.654   1.00 16.58 ?  133 LYS   C N    1 
ATOM   3539 C CA   . LYS   C 2 133 ? 33.718  -28.262 6.160   1.00 18.51 ?  133 LYS   C CA   1 
ATOM   3540 C C    . LYS   C 2 133 ? 34.012  -26.839 5.679   1.00 18.03 ?  133 LYS   C C    1 
ATOM   3541 O O    . LYS   C 2 133 ? 35.105  -26.325 5.942   1.00 19.88 ?  133 LYS   C O    1 
ATOM   3542 C CB   . LYS   C 2 133 ? 34.858  -29.216 5.776   1.00 15.86 ?  133 LYS   C CB   1 
ATOM   3543 C CG   . LYS   C 2 133 ? 34.832  -30.525 6.577   1.00 23.82 ?  133 LYS   C CG   1 
ATOM   3544 C CD   . LYS   C 2 133 ? 34.916  -30.316 8.079   1.00 30.25 ?  133 LYS   C CD   1 
ATOM   3545 C CE   . LYS   C 2 133 ? 35.815  -29.135 8.452   1.00 32.52 ?  133 LYS   C CE   1 
ATOM   3546 N NZ   . LYS   C 2 133 ? 35.786  -28.808 9.912   1.00 34.40 ?  133 LYS   C NZ   1 
ATOM   3547 N N    . LEU   C 2 134 ? 33.074  -26.175 5.012   1.00 15.57 ?  134 LEU   C N    1 
ATOM   3548 C CA   . LEU   C 2 134 ? 33.311  -24.786 4.616   1.00 12.62 ?  134 LEU   C CA   1 
ATOM   3549 C C    . LEU   C 2 134 ? 33.436  -23.903 5.858   1.00 17.40 ?  134 LEU   C C    1 
ATOM   3550 O O    . LEU   C 2 134 ? 32.620  -24.014 6.783   1.00 18.42 ?  134 LEU   C O    1 
ATOM   3551 C CB   . LEU   C 2 134 ? 32.173  -24.268 3.715   1.00 14.40 ?  134 LEU   C CB   1 
ATOM   3552 C CG   . LEU   C 2 134 ? 32.079  -24.895 2.315   1.00 15.23 ?  134 LEU   C CG   1 
ATOM   3553 C CD1  . LEU   C 2 134 ? 30.846  -24.442 1.584   1.00 14.80 ?  134 LEU   C CD1  1 
ATOM   3554 C CD2  . LEU   C 2 134 ? 33.307  -24.542 1.488   1.00 18.22 ?  134 LEU   C CD2  1 
ATOM   3555 N N    . PRO   C 2 135 ? 34.440  -23.026 5.929   1.00 14.81 ?  135 PRO   C N    1 
ATOM   3556 C CA   . PRO   C 2 135 ? 34.498  -22.056 7.035   1.00 15.98 ?  135 PRO   C CA   1 
ATOM   3557 C C    . PRO   C 2 135 ? 33.284  -21.139 7.026   1.00 15.42 ?  135 PRO   C C    1 
ATOM   3558 O O    . PRO   C 2 135 ? 32.797  -20.751 5.959   1.00 14.86 ?  135 PRO   C O    1 
ATOM   3559 C CB   . PRO   C 2 135 ? 35.782  -21.263 6.744   1.00 17.49 ?  135 PRO   C CB   1 
ATOM   3560 C CG   . PRO   C 2 135 ? 36.463  -21.967 5.620   1.00 24.09 ?  135 PRO   C CG   1 
ATOM   3561 C CD   . PRO   C 2 135 ? 35.430  -22.727 4.880   1.00 16.86 ?  135 PRO   C CD   1 
ATOM   3562 N N    . GLN   C 2 136 ? 32.813  -20.766 8.226   1.00 16.37 ?  136 GLN   C N    1 
ATOM   3563 C CA   . GLN   C 2 136 ? 31.589  -19.989 8.387   1.00 14.80 ?  136 GLN   C CA   1 
ATOM   3564 C C    . GLN   C 2 136 ? 31.847  -18.609 8.981   1.00 15.31 ?  136 GLN   C C    1 
ATOM   3565 O O    . GLN   C 2 136 ? 32.869  -18.387 9.647   1.00 16.33 ?  136 GLN   C O    1 
ATOM   3566 C CB   . GLN   C 2 136 ? 30.581  -20.746 9.272   1.00 15.69 ?  136 GLN   C CB   1 
ATOM   3567 C CG   . GLN   C 2 136 ? 30.150  -22.061 8.652   1.00 18.17 ?  136 GLN   C CG   1 
ATOM   3568 C CD   . GLN   C 2 136 ? 29.549  -21.860 7.266   1.00 16.91 ?  136 GLN   C CD   1 
ATOM   3569 O OE1  . GLN   C 2 136 ? 28.714  -20.977 7.063   1.00 15.05 ?  136 GLN   C OE1  1 
ATOM   3570 N NE2  . GLN   C 2 136 ? 29.993  -22.672 6.303   1.00 13.77 ?  136 GLN   C NE2  1 
ATOM   3571 N N    . PRO   C 2 137 ? 30.955  -17.652 8.741   1.00 16.09 ?  137 PRO   C N    1 
ATOM   3572 C CA   . PRO   C 2 137 ? 31.120  -16.302 9.317   1.00 15.75 ?  137 PRO   C CA   1 
ATOM   3573 C C    . PRO   C 2 137 ? 30.981  -16.336 10.826  1.00 17.35 ?  137 PRO   C C    1 
ATOM   3574 O O    . PRO   C 2 137 ? 30.556  -17.350 11.393  1.00 18.84 ?  137 PRO   C O    1 
ATOM   3575 C CB   . PRO   C 2 137 ? 29.968  -15.501 8.686   1.00 20.40 ?  137 PRO   C CB   1 
ATOM   3576 C CG   . PRO   C 2 137 ? 29.503  -16.292 7.537   1.00 20.17 ?  137 PRO   C CG   1 
ATOM   3577 C CD   . PRO   C 2 137 ? 29.732  -17.741 7.920   1.00 17.28 ?  137 PRO   C CD   1 
ATOM   3578 N N    . PRO   C 2 138 ? 31.333  -15.254 11.516  1.00 18.38 ?  138 PRO   C N    1 
ATOM   3579 C CA   . PRO   C 2 138 ? 30.983  -15.151 12.941  1.00 20.67 ?  138 PRO   C CA   1 
ATOM   3580 C C    . PRO   C 2 138 ? 29.496  -15.399 13.155  1.00 19.00 ?  138 PRO   C C    1 
ATOM   3581 O O    . PRO   C 2 138 ? 28.662  -14.976 12.354  1.00 19.76 ?  138 PRO   C O    1 
ATOM   3582 C CB   . PRO   C 2 138 ? 31.367  -13.714 13.301  1.00 23.68 ?  138 PRO   C CB   1 
ATOM   3583 C CG   . PRO   C 2 138 ? 32.444  -13.350 12.297  1.00 22.75 ?  138 PRO   C CG   1 
ATOM   3584 C CD   . PRO   C 2 138 ? 32.072  -14.075 11.026  1.00 19.37 ?  138 PRO   C CD   1 
ATOM   3585 N N    . GLU   C 2 139 ? 29.168  -16.090 14.247  1.00 19.76 ?  139 GLU   C N    1 
ATOM   3586 C CA   . GLU   C 2 139 ? 27.774  -16.465 14.488  1.00 16.17 ?  139 GLU   C CA   1 
ATOM   3587 C C    . GLU   C 2 139 ? 26.853  -15.245 14.482  1.00 20.96 ?  139 GLU   C C    1 
ATOM   3588 O O    . GLU   C 2 139 ? 27.135  -14.226 15.121  1.00 20.84 ?  139 GLU   C O    1 
ATOM   3589 C CB   . GLU   C 2 139 ? 27.634  -17.218 15.808  1.00 18.55 ?  139 GLU   C CB   1 
ATOM   3590 C CG   . GLU   C 2 139 ? 26.189  -17.638 16.075  1.00 23.32 ?  139 GLU   C CG   1 
ATOM   3591 C CD   . GLU   C 2 139 ? 26.054  -18.716 17.132  1.00 33.44 ?  139 GLU   C CD   1 
ATOM   3592 O OE1  . GLU   C 2 139 ? 27.047  -18.990 17.848  1.00 25.96 ?  139 GLU   C OE1  1 
ATOM   3593 O OE2  . GLU   C 2 139 ? 24.945  -19.296 17.231  1.00 27.21 -1 139 GLU   C OE2  1 
ATOM   3594 N N    . GLY   C 2 140 ? 25.743  -15.355 13.743  1.00 19.46 ?  140 GLY   C N    1 
ATOM   3595 C CA   . GLY   C 2 140 ? 24.731  -14.322 13.717  1.00 25.09 ?  140 GLY   C CA   1 
ATOM   3596 C C    . GLY   C 2 140 ? 24.893  -13.238 12.666  1.00 22.09 ?  140 GLY   C C    1 
ATOM   3597 O O    . GLY   C 2 140 ? 23.979  -12.421 12.502  1.00 23.56 ?  140 GLY   C O    1 
ATOM   3598 N N    . GLN   C 2 141 ? 26.010  -13.187 11.944  1.00 17.41 ?  141 GLN   C N    1 
ATOM   3599 C CA   . GLN   C 2 141 ? 26.121  -12.193 10.884  1.00 18.44 ?  141 GLN   C CA   1 
ATOM   3600 C C    . GLN   C 2 141 ? 24.988  -12.358 9.881   1.00 19.43 ?  141 GLN   C C    1 
ATOM   3601 O O    . GLN   C 2 141 ? 24.577  -13.477 9.578   1.00 19.90 ?  141 GLN   C O    1 
ATOM   3602 C CB   . GLN   C 2 141 ? 27.453  -12.330 10.156  1.00 17.44 ?  141 GLN   C CB   1 
ATOM   3603 C CG   . GLN   C 2 141 ? 28.650  -11.955 10.984  1.00 26.63 ?  141 GLN   C CG   1 
ATOM   3604 C CD   . GLN   C 2 141 ? 29.832  -11.549 10.121  1.00 29.01 ?  141 GLN   C CD   1 
ATOM   3605 O OE1  . GLN   C 2 141 ? 29.857  -11.797 8.907   1.00 30.03 ?  141 GLN   C OE1  1 
ATOM   3606 N NE2  . GLN   C 2 141 ? 30.829  -10.943 10.747  1.00 36.10 ?  141 GLN   C NE2  1 
ATOM   3607 N N    . THR   C 2 142 ? 24.506  -11.234 9.350   1.00 22.30 ?  142 THR   C N    1 
ATOM   3608 C CA   . THR   C 2 142 ? 23.472  -11.193 8.326   1.00 19.12 ?  142 THR   C CA   1 
ATOM   3609 C C    . THR   C 2 142 ? 23.970  -10.389 7.126   1.00 24.07 ?  142 THR   C C    1 
ATOM   3610 O O    . THR   C 2 142 ? 24.911  -9.601  7.232   1.00 25.32 ?  142 THR   C O    1 
ATOM   3611 C CB   . THR   C 2 142 ? 22.179  -10.566 8.874   1.00 24.80 ?  142 THR   C CB   1 
ATOM   3612 O OG1  . THR   C 2 142 ? 22.458  -9.235  9.330   1.00 28.98 ?  142 THR   C OG1  1 
ATOM   3613 C CG2  . THR   C 2 142 ? 21.638  -11.379 10.037  1.00 22.86 ?  142 THR   C CG2  1 
ATOM   3614 N N    . TYR   C 2 143 ? 23.327  -10.589 5.977   1.00 18.00 ?  143 TYR   C N    1 
ATOM   3615 C CA   . TYR   C 2 143 ? 23.653  -9.824  4.783   1.00 20.70 ?  143 TYR   C CA   1 
ATOM   3616 C C    . TYR   C 2 143 ? 23.055  -8.425  4.866   1.00 30.47 ?  143 TYR   C C    1 
ATOM   3617 O O    . TYR   C 2 143 ? 22.025  -8.208  5.506   1.00 29.29 ?  143 TYR   C O    1 
ATOM   3618 C CB   . TYR   C 2 143 ? 23.131  -10.514 3.517   1.00 22.51 ?  143 TYR   C CB   1 
ATOM   3619 C CG   . TYR   C 2 143 ? 23.679  -11.907 3.330   1.00 17.75 ?  143 TYR   C CG   1 
ATOM   3620 C CD1  . TYR   C 2 143 ? 24.922  -12.107 2.736   1.00 18.89 ?  143 TYR   C CD1  1 
ATOM   3621 C CD2  . TYR   C 2 143 ? 22.959  -13.018 3.757   1.00 18.92 ?  143 TYR   C CD2  1 
ATOM   3622 C CE1  . TYR   C 2 143 ? 25.424  -13.389 2.573   1.00 20.06 ?  143 TYR   C CE1  1 
ATOM   3623 C CE2  . TYR   C 2 143 ? 23.446  -14.295 3.611   1.00 18.90 ?  143 TYR   C CE2  1 
ATOM   3624 C CZ   . TYR   C 2 143 ? 24.685  -14.480 3.018   1.00 18.86 ?  143 TYR   C CZ   1 
ATOM   3625 O OH   . TYR   C 2 143 ? 25.172  -15.763 2.874   1.00 19.37 ?  143 TYR   C OH   1 
ATOM   3626 N N    . ASN   C 2 144 ? 23.697  -7.479  4.185   1.00 35.47 ?  144 ASN   C N    1 
ATOM   3627 C CA   . ASN   C 2 144 ? 23.138  -6.128  4.070   1.00 41.60 ?  144 ASN   C CA   1 
ATOM   3628 C C    . ASN   C 2 144 ? 22.995  -5.442  5.422   1.00 42.79 ?  144 ASN   C C    1 
ATOM   3629 O O    . ASN   C 2 144 ? 21.934  -4.875  5.716   1.00 40.57 ?  144 ASN   C O    1 
ATOM   3630 C CB   . ASN   C 2 144 ? 21.763  -6.157  3.382   1.00 35.05 ?  144 ASN   C CB   1 
ATOM   3631 C CG   . ASN   C 2 144 ? 21.792  -6.836  2.011   1.00 48.79 ?  144 ASN   C CG   1 
ATOM   3632 O OD1  . ASN   C 2 144 ? 22.751  -6.682  1.245   1.00 45.40 ?  144 ASN   C OD1  1 
ATOM   3633 N ND2  . ASN   C 2 144 ? 20.720  -7.561  1.685   1.00 42.06 ?  144 ASN   C ND2  1 
ATOM   3634 N N    . VAL   D 2 7   ? -29.923 -23.998 -42.726 1.00 55.13 ?  7   VAL   D N    1 
ATOM   3635 C CA   . VAL   D 2 7   ? -30.897 -22.948 -42.450 1.00 48.67 ?  7   VAL   D CA   1 
ATOM   3636 C C    . VAL   D 2 7   ? -30.208 -21.613 -42.176 1.00 38.28 ?  7   VAL   D C    1 
ATOM   3637 O O    . VAL   D 2 7   ? -29.520 -21.460 -41.164 1.00 37.25 ?  7   VAL   D O    1 
ATOM   3638 C CB   . VAL   D 2 7   ? -31.811 -23.340 -41.264 1.00 43.21 ?  7   VAL   D CB   1 
ATOM   3639 C CG1  . VAL   D 2 7   ? -32.616 -22.142 -40.792 1.00 31.08 ?  7   VAL   D CG1  1 
ATOM   3640 C CG2  . VAL   D 2 7   ? -32.738 -24.473 -41.657 1.00 42.77 ?  7   VAL   D CG2  1 
ATOM   3641 N N    . LYS   D 2 8   ? -30.403 -20.646 -43.076 1.00 34.65 ?  8   LYS   D N    1 
ATOM   3642 C CA   . LYS   D 2 8   ? -29.885 -19.299 -42.858 1.00 36.30 ?  8   LYS   D CA   1 
ATOM   3643 C C    . LYS   D 2 8   ? -30.678 -18.583 -41.772 1.00 34.11 ?  8   LYS   D C    1 
ATOM   3644 O O    . LYS   D 2 8   ? -31.900 -18.432 -41.884 1.00 30.74 ?  8   LYS   D O    1 
ATOM   3645 C CB   . LYS   D 2 8   ? -29.963 -18.461 -44.129 1.00 39.55 ?  8   LYS   D CB   1 
ATOM   3646 C CG   . LYS   D 2 8   ? -28.695 -18.315 -44.919 1.00 41.37 ?  8   LYS   D CG   1 
ATOM   3647 C CD   . LYS   D 2 8   ? -28.869 -17.099 -45.817 1.00 51.21 ?  8   LYS   D CD   1 
ATOM   3648 C CE   . LYS   D 2 8   ? -29.301 -17.472 -47.224 1.00 49.08 ?  8   LYS   D CE   1 
ATOM   3649 N NZ   . LYS   D 2 8   ? -29.860 -16.272 -47.925 1.00 45.33 ?  8   LYS   D NZ   1 
ATOM   3650 N N    . VAL   D 2 9   ? -29.976 -18.105 -40.751 1.00 31.67 ?  9   VAL   D N    1 
ATOM   3651 C CA   . VAL   D 2 9   ? -30.550 -17.247 -39.716 1.00 24.45 ?  9   VAL   D CA   1 
ATOM   3652 C C    . VAL   D 2 9   ? -30.162 -15.805 -40.033 1.00 28.97 ?  9   VAL   D C    1 
ATOM   3653 O O    . VAL   D 2 9   ? -28.964 -15.495 -40.064 1.00 25.80 ?  9   VAL   D O    1 
ATOM   3654 C CB   . VAL   D 2 9   ? -30.060 -17.648 -38.317 1.00 24.70 ?  9   VAL   D CB   1 
ATOM   3655 C CG1  . VAL   D 2 9   ? -30.688 -16.760 -37.268 1.00 24.91 ?  9   VAL   D CG1  1 
ATOM   3656 C CG2  . VAL   D 2 9   ? -30.372 -19.110 -38.040 1.00 25.49 ?  9   VAL   D CG2  1 
ATOM   3657 N N    . PRO   D 2 10  ? -31.115 -14.904 -40.249 1.00 20.46 ?  10  PRO   D N    1 
ATOM   3658 C CA   . PRO   D 2 10  ? -30.757 -13.507 -40.540 1.00 24.94 ?  10  PRO   D CA   1 
ATOM   3659 C C    . PRO   D 2 10  ? -30.039 -12.856 -39.368 1.00 22.00 ?  10  PRO   D C    1 
ATOM   3660 O O    . PRO   D 2 10  ? -30.210 -13.234 -38.208 1.00 17.93 ?  10  PRO   D O    1 
ATOM   3661 C CB   . PRO   D 2 10  ? -32.108 -12.821 -40.800 1.00 21.66 ?  10  PRO   D CB   1 
ATOM   3662 C CG   . PRO   D 2 10  ? -33.132 -13.873 -40.762 1.00 26.27 ?  10  PRO   D CG   1 
ATOM   3663 C CD   . PRO   D 2 10  ? -32.564 -15.119 -40.154 1.00 21.74 ?  10  PRO   D CD   1 
ATOM   3664 N N    . ARG   D 2 11  ? -29.244 -11.832 -39.700 1.00 18.19 ?  11  ARG   D N    1 
ATOM   3665 C CA   . ARG   D 2 11  ? -28.410 -11.131 -38.720 1.00 17.20 ?  11  ARG   D CA   1 
ATOM   3666 C C    . ARG   D 2 11  ? -29.131 -10.846 -37.405 1.00 18.89 ?  11  ARG   D C    1 
ATOM   3667 O O    . ARG   D 2 11  ? -28.621 -11.151 -36.317 1.00 18.62 ?  11  ARG   D O    1 
ATOM   3668 C CB   . ARG   D 2 11  ? -27.917 -9.813  -39.330 1.00 18.99 ?  11  ARG   D CB   1 
ATOM   3669 C CG   . ARG   D 2 11  ? -27.126 -8.911  -38.377 1.00 20.67 ?  11  ARG   D CG   1 
ATOM   3670 C CD   . ARG   D 2 11  ? -26.754 -7.589  -39.047 1.00 20.52 ?  11  ARG   D CD   1 
ATOM   3671 N NE   . ARG   D 2 11  ? -25.823 -6.802  -38.248 1.00 20.89 ?  11  ARG   D NE   1 
ATOM   3672 C CZ   . ARG   D 2 11  ? -26.146 -6.143  -37.142 1.00 22.92 ?  11  ARG   D CZ   1 
ATOM   3673 N NH1  . ARG   D 2 11  ? -27.386 -6.146  -36.669 1.00 22.13 ?  11  ARG   D NH1  1 
ATOM   3674 N NH2  . ARG   D 2 11  ? -25.197 -5.474  -36.485 1.00 22.40 ?  11  ARG   D NH2  1 
ATOM   3675 N N    . ASN   D 2 12  ? -30.306 -10.215 -37.491 1.00 20.33 ?  12  ASN   D N    1 
ATOM   3676 C CA   . ASN   D 2 12  ? -30.957 -9.701  -36.292 1.00 24.30 ?  12  ASN   D CA   1 
ATOM   3677 C C    . ASN   D 2 12  ? -31.370 -10.821 -35.345 1.00 28.73 ?  12  ASN   D C    1 
ATOM   3678 O O    . ASN   D 2 12  ? -31.420 -10.608 -34.129 1.00 37.43 ?  12  ASN   D O    1 
ATOM   3679 C CB   . ASN   D 2 12  ? -32.152 -8.827  -36.677 1.00 22.11 ?  12  ASN   D CB   1 
ATOM   3680 C CG   . ASN   D 2 12  ? -31.728 -7.514  -37.315 1.00 24.83 ?  12  ASN   D CG   1 
ATOM   3681 O OD1  . ASN   D 2 12  ? -30.619 -7.017  -37.063 1.00 29.92 ?  12  ASN   D OD1  1 
ATOM   3682 N ND2  . ASN   D 2 12  ? -32.589 -6.961  -38.162 1.00 27.76 ?  12  ASN   D ND2  1 
ATOM   3683 N N    . PHE   D 2 13  ? -31.627 -12.019 -35.864 1.00 15.79 ?  13  PHE   D N    1 
ATOM   3684 C CA   . PHE   D 2 13  ? -31.906 -13.153 -35.004 1.00 14.21 ?  13  PHE   D CA   1 
ATOM   3685 C C    . PHE   D 2 13  ? -30.645 -13.925 -34.631 1.00 15.88 ?  13  PHE   D C    1 
ATOM   3686 O O    . PHE   D 2 13  ? -30.556 -14.445 -33.507 1.00 18.86 ?  13  PHE   D O    1 
ATOM   3687 C CB   . PHE   D 2 13  ? -32.918 -14.086 -35.674 1.00 17.65 ?  13  PHE   D CB   1 
ATOM   3688 C CG   . PHE   D 2 13  ? -34.288 -13.481 -35.780 1.00 20.71 ?  13  PHE   D CG   1 
ATOM   3689 C CD1  . PHE   D 2 13  ? -35.130 -13.481 -34.686 1.00 19.10 ?  13  PHE   D CD1  1 
ATOM   3690 C CD2  . PHE   D 2 13  ? -34.721 -12.902 -36.967 1.00 20.46 ?  13  PHE   D CD2  1 
ATOM   3691 C CE1  . PHE   D 2 13  ? -36.400 -12.923 -34.762 1.00 19.36 ?  13  PHE   D CE1  1 
ATOM   3692 C CE2  . PHE   D 2 13  ? -36.000 -12.326 -37.053 1.00 19.10 ?  13  PHE   D CE2  1 
ATOM   3693 C CZ   . PHE   D 2 13  ? -36.836 -12.345 -35.950 1.00 17.15 ?  13  PHE   D CZ   1 
ATOM   3694 N N    . ARG   D 2 14  ? -29.672 -13.992 -35.540 1.00 16.61 ?  14  ARG   D N    1 
ATOM   3695 C CA   . ARG   D 2 14  ? -28.417 -14.661 -35.207 1.00 19.11 ?  14  ARG   D CA   1 
ATOM   3696 C C    . ARG   D 2 14  ? -27.745 -13.993 -34.017 1.00 16.37 ?  14  ARG   D C    1 
ATOM   3697 O O    . ARG   D 2 14  ? -27.261 -14.673 -33.103 1.00 18.58 ?  14  ARG   D O    1 
ATOM   3698 C CB   . ARG   D 2 14  ? -27.482 -14.670 -36.416 1.00 17.93 ?  14  ARG   D CB   1 
ATOM   3699 C CG   . ARG   D 2 14  ? -26.013 -14.948 -36.037 1.00 19.90 ?  14  ARG   D CG   1 
ATOM   3700 C CD   . ARG   D 2 14  ? -25.817 -16.400 -35.619 1.00 23.21 ?  14  ARG   D CD   1 
ATOM   3701 N NE   . ARG   D 2 14  ? -25.219 -17.172 -36.698 1.00 24.77 ?  14  ARG   D NE   1 
ATOM   3702 C CZ   . ARG   D 2 14  ? -23.953 -17.071 -37.090 1.00 25.68 ?  14  ARG   D CZ   1 
ATOM   3703 N NH1  . ARG   D 2 14  ? -23.090 -16.283 -36.463 1.00 18.18 ?  14  ARG   D NH1  1 
ATOM   3704 N NH2  . ARG   D 2 14  ? -23.544 -17.769 -38.147 1.00 22.07 ?  14  ARG   D NH2  1 
ATOM   3705 N N    . LEU   D 2 15  ? -27.712 -12.659 -34.004 1.00 16.00 ?  15  LEU   D N    1 
ATOM   3706 C CA   . LEU   D 2 15  ? -26.990 -11.973 -32.939 1.00 15.03 ?  15  LEU   D CA   1 
ATOM   3707 C C    . LEU   D 2 15  ? -27.738 -12.070 -31.616 1.00 17.39 ?  15  LEU   D C    1 
ATOM   3708 O O    . LEU   D 2 15  ? -27.112 -12.061 -30.555 1.00 17.61 ?  15  LEU   D O    1 
ATOM   3709 C CB   . LEU   D 2 15  ? -26.727 -10.516 -33.331 1.00 15.01 ?  15  LEU   D CB   1 
ATOM   3710 C CG   . LEU   D 2 15  ? -25.647 -10.376 -34.415 1.00 15.51 ?  15  LEU   D CG   1 
ATOM   3711 C CD1  . LEU   D 2 15  ? -25.551 -8.943  -34.927 1.00 21.19 ?  15  LEU   D CD1  1 
ATOM   3712 C CD2  . LEU   D 2 15  ? -24.300 -10.838 -33.849 1.00 19.13 ?  15  LEU   D CD2  1 
ATOM   3713 N N    . LEU   D 2 16  ? -29.074 -12.207 -31.643 1.00 17.81 ?  16  LEU   D N    1 
ATOM   3714 C CA   . LEU   D 2 16  ? -29.767 -12.504 -30.390 1.00 22.42 ?  16  LEU   D CA   1 
ATOM   3715 C C    . LEU   D 2 16  ? -29.439 -13.911 -29.894 1.00 18.93 ?  16  LEU   D C    1 
ATOM   3716 O O    . LEU   D 2 16  ? -29.338 -14.142 -28.679 1.00 20.75 ?  16  LEU   D O    1 
ATOM   3717 C CB   . LEU   D 2 16  ? -31.279 -12.318 -30.563 1.00 17.97 ?  16  LEU   D CB   1 
ATOM   3718 C CG   . LEU   D 2 16  ? -31.670 -10.842 -30.719 1.00 21.17 ?  16  LEU   D CG   1 
ATOM   3719 C CD1  . LEU   D 2 16  ? -33.187 -10.714 -30.941 1.00 26.35 ?  16  LEU   D CD1  1 
ATOM   3720 C CD2  . LEU   D 2 16  ? -31.243 -10.034 -29.524 1.00 22.04 ?  16  LEU   D CD2  1 
ATOM   3721 N N    . GLU   D 2 17  ? -29.247 -14.864 -30.815 1.00 16.30 ?  17  GLU   D N    1 
ATOM   3722 C CA   . GLU   D 2 17  ? -28.765 -16.180 -30.386 1.00 17.09 ?  17  GLU   D CA   1 
ATOM   3723 C C    . GLU   D 2 17  ? -27.390 -16.072 -29.740 1.00 17.21 ?  17  GLU   D C    1 
ATOM   3724 O O    . GLU   D 2 17  ? -27.124 -16.717 -28.716 1.00 20.43 ?  17  GLU   D O    1 
ATOM   3725 C CB   . GLU   D 2 17  ? -28.676 -17.172 -31.550 1.00 20.57 ?  17  GLU   D CB   1 
ATOM   3726 C CG   . GLU   D 2 17  ? -29.952 -17.488 -32.343 1.00 30.09 ?  17  GLU   D CG   1 
ATOM   3727 C CD   . GLU   D 2 17  ? -29.691 -18.427 -33.551 1.00 43.54 ?  17  GLU   D CD   1 
ATOM   3728 O OE1  . GLU   D 2 17  ? -28.629 -18.322 -34.232 1.00 36.11 ?  17  GLU   D OE1  1 
ATOM   3729 O OE2  . GLU   D 2 17  ? -30.571 -19.272 -33.838 1.00 47.72 -1 17  GLU   D OE2  1 
ATOM   3730 N N    . GLU   D 2 18  ? -26.489 -15.300 -30.357 1.00 18.73 ?  18  GLU   D N    1 
ATOM   3731 C CA   . GLU   D 2 18  ? -25.133 -15.189 -29.814 1.00 15.83 ?  18  GLU   D CA   1 
ATOM   3732 C C    . GLU   D 2 18  ? -25.140 -14.453 -28.475 1.00 19.28 ?  18  GLU   D C    1 
ATOM   3733 O O    . GLU   D 2 18  ? -24.328 -14.754 -27.586 1.00 19.18 ?  18  GLU   D O    1 
ATOM   3734 C CB   . GLU   D 2 18  ? -24.208 -14.501 -30.834 1.00 12.60 ?  18  GLU   D CB   1 
ATOM   3735 C CG   . GLU   D 2 18  ? -24.040 -15.276 -32.135 1.00 14.65 ?  18  GLU   D CG   1 
ATOM   3736 C CD   . GLU   D 2 18  ? -22.835 -14.812 -32.945 1.00 17.20 ?  18  GLU   D CD   1 
ATOM   3737 O OE1  . GLU   D 2 18  ? -21.719 -14.760 -32.372 1.00 15.32 ?  18  GLU   D OE1  1 
ATOM   3738 O OE2  . GLU   D 2 18  ? -23.004 -14.503 -34.149 1.00 16.56 -1 18  GLU   D OE2  1 
ATOM   3739 N N    . LEU   D 2 19  ? -26.078 -13.527 -28.290 1.00 20.52 ?  19  LEU   D N    1 
ATOM   3740 C CA   . LEU   D 2 19  ? -26.243 -12.879 -26.995 1.00 20.51 ?  19  LEU   D CA   1 
ATOM   3741 C C    . LEU   D 2 19  ? -26.636 -13.890 -25.921 1.00 20.46 ?  19  LEU   D C    1 
ATOM   3742 O O    . LEU   D 2 19  ? -26.047 -13.916 -24.831 1.00 20.39 ?  19  LEU   D O    1 
ATOM   3743 C CB   . LEU   D 2 19  ? -27.282 -11.760 -27.107 1.00 21.99 ?  19  LEU   D CB   1 
ATOM   3744 C CG   . LEU   D 2 19  ? -27.712 -11.140 -25.777 1.00 24.10 ?  19  LEU   D CG   1 
ATOM   3745 C CD1  . LEU   D 2 19  ? -26.495 -10.627 -25.056 1.00 27.80 ?  19  LEU   D CD1  1 
ATOM   3746 C CD2  . LEU   D 2 19  ? -28.721 -10.017 -26.010 1.00 27.55 ?  19  LEU   D CD2  1 
ATOM   3747 N N    . GLU   D 2 20  ? -27.639 -14.730 -26.205 1.00 22.07 ?  20  GLU   D N    1 
ATOM   3748 C CA   . GLU   D 2 20  ? -28.010 -15.742 -25.216 1.00 26.83 ?  20  GLU   D CA   1 
ATOM   3749 C C    . GLU   D 2 20  ? -26.889 -16.751 -24.967 1.00 26.48 ?  20  GLU   D C    1 
ATOM   3750 O O    . GLU   D 2 20  ? -26.665 -17.151 -23.816 1.00 25.73 ?  20  GLU   D O    1 
ATOM   3751 C CB   . GLU   D 2 20  ? -29.311 -16.454 -25.593 1.00 26.14 ?  20  GLU   D CB   1 
ATOM   3752 C CG   . GLU   D 2 20  ? -30.568 -15.609 -25.367 1.00 44.03 ?  20  GLU   D CG   1 
ATOM   3753 C CD   . GLU   D 2 20  ? -31.056 -14.858 -26.587 1.00 50.15 ?  20  GLU   D CD   1 
ATOM   3754 O OE1  . GLU   D 2 20  ? -31.514 -15.526 -27.542 1.00 56.98 ?  20  GLU   D OE1  1 
ATOM   3755 O OE2  . GLU   D 2 20  ? -31.006 -13.604 -26.586 1.00 50.93 -1 20  GLU   D OE2  1 
ATOM   3756 N N    . GLU   D 2 21  ? -26.174 -17.176 -26.018 1.00 21.25 ?  21  GLU   D N    1 
ATOM   3757 C CA   . GLU   D 2 21  ? -25.056 -18.096 -25.802 1.00 29.11 ?  21  GLU   D CA   1 
ATOM   3758 C C    . GLU   D 2 21  ? -23.964 -17.462 -24.946 1.00 21.75 ?  21  GLU   D C    1 
ATOM   3759 O O    . GLU   D 2 21  ? -23.362 -18.135 -24.102 1.00 23.88 ?  21  GLU   D O    1 
ATOM   3760 C CB   . GLU   D 2 21  ? -24.461 -18.571 -27.129 1.00 28.54 ?  21  GLU   D CB   1 
ATOM   3761 C CG   . GLU   D 2 21  ? -23.462 -19.712 -26.913 1.00 39.10 ?  21  GLU   D CG   1 
ATOM   3762 C CD   . GLU   D 2 21  ? -22.941 -20.344 -28.193 1.00 42.46 ?  21  GLU   D CD   1 
ATOM   3763 O OE1  . GLU   D 2 21  ? -22.201 -21.351 -28.092 1.00 39.33 ?  21  GLU   D OE1  1 
ATOM   3764 O OE2  . GLU   D 2 21  ? -23.250 -19.833 -29.293 1.00 53.77 -1 21  GLU   D OE2  1 
ATOM   3765 N N    . GLY   D 2 22  ? -23.670 -16.179 -25.167 1.00 18.01 ?  22  GLY   D N    1 
ATOM   3766 C CA   . GLY   D 2 22  ? -22.654 -15.514 -24.368 1.00 20.30 ?  22  GLY   D CA   1 
ATOM   3767 C C    . GLY   D 2 22  ? -23.064 -15.384 -22.916 1.00 27.64 ?  22  GLY   D C    1 
ATOM   3768 O O    . GLY   D 2 22  ? -22.233 -15.526 -22.008 1.00 28.22 ?  22  GLY   D O    1 
ATOM   3769 N N    . GLN   D 2 23  ? -24.349 -15.110 -22.671 1.00 27.71 ?  23  GLN   D N    1 
ATOM   3770 C CA   . GLN   D 2 23  ? -24.831 -15.104 -21.292 1.00 30.28 ?  23  GLN   D CA   1 
ATOM   3771 C C    . GLN   D 2 23  ? -24.682 -16.479 -20.655 1.00 25.86 ?  23  GLN   D C    1 
ATOM   3772 O O    . GLN   D 2 23  ? -24.285 -16.592 -19.489 1.00 38.63 ?  23  GLN   D O    1 
ATOM   3773 C CB   . GLN   D 2 23  ? -26.288 -14.645 -21.240 1.00 31.22 ?  23  GLN   D CB   1 
ATOM   3774 C CG   . GLN   D 2 23  ? -26.472 -13.182 -21.603 1.00 29.76 ?  23  GLN   D CG   1 
ATOM   3775 C CD   . GLN   D 2 23  ? -27.932 -12.818 -21.814 1.00 32.03 ?  23  GLN   D CD   1 
ATOM   3776 O OE1  . GLN   D 2 23  ? -28.770 -13.686 -22.079 1.00 37.27 ?  23  GLN   D OE1  1 
ATOM   3777 N NE2  . GLN   D 2 23  ? -28.244 -11.527 -21.702 1.00 38.28 ?  23  GLN   D NE2  1 
ATOM   3778 N N    . LYS   D 2 24  ? -25.010 -17.539 -21.394 1.00 38.06 ?  24  LYS   D N    1 
ATOM   3779 C CA   . LYS   D 2 24  ? -24.804 -18.886 -20.871 1.00 32.09 ?  24  LYS   D CA   1 
ATOM   3780 C C    . LYS   D 2 24  ? -23.320 -19.179 -20.667 1.00 40.42 ?  24  LYS   D C    1 
ATOM   3781 O O    . LYS   D 2 24  ? -22.940 -19.835 -19.689 1.00 35.69 ?  24  LYS   D O    1 
ATOM   3782 C CB   . LYS   D 2 24  ? -25.437 -19.913 -21.811 1.00 41.10 ?  24  LYS   D CB   1 
ATOM   3783 C CG   . LYS   D 2 24  ? -26.964 -19.882 -21.819 1.00 55.77 ?  24  LYS   D CG   1 
ATOM   3784 C CD   . LYS   D 2 24  ? -27.562 -20.689 -22.972 1.00 57.14 ?  24  LYS   D CD   1 
ATOM   3785 C CE   . LYS   D 2 24  ? -26.839 -22.017 -23.193 1.00 62.58 ?  24  LYS   D CE   1 
ATOM   3786 N NZ   . LYS   D 2 24  ? -26.876 -22.415 -24.634 1.00 65.72 ?  24  LYS   D NZ   1 
ATOM   3787 N N    . GLY   D 2 25  ? -22.471 -18.695 -21.574 1.00 33.40 ?  25  GLY   D N    1 
ATOM   3788 C CA   . GLY   D 2 25  ? -21.030 -18.871 -21.492 1.00 30.09 ?  25  GLY   D CA   1 
ATOM   3789 C C    . GLY   D 2 25  ? -20.533 -20.247 -21.884 1.00 38.44 ?  25  GLY   D C    1 
ATOM   3790 O O    . GLY   D 2 25  ? -21.322 -21.192 -21.959 1.00 40.12 ?  25  GLY   D O    1 
ATOM   3791 N N    . VAL   D 2 26  ? -19.228 -20.375 -22.145 1.00 34.78 ?  26  VAL   D N    1 
ATOM   3792 C CA   . VAL   D 2 26  ? -18.627 -21.693 -22.291 1.00 32.58 ?  26  VAL   D CA   1 
ATOM   3793 C C    . VAL   D 2 26  ? -18.291 -22.244 -20.905 1.00 33.03 ?  26  VAL   D C    1 
ATOM   3794 O O    . VAL   D 2 26  ? -18.238 -21.517 -19.902 1.00 37.48 ?  26  VAL   D O    1 
ATOM   3795 C CB   . VAL   D 2 26  ? -17.385 -21.670 -23.215 1.00 41.14 ?  26  VAL   D CB   1 
ATOM   3796 C CG1  . VAL   D 2 26  ? -17.735 -21.080 -24.579 1.00 41.22 ?  26  VAL   D CG1  1 
ATOM   3797 C CG2  . VAL   D 2 26  ? -16.189 -20.926 -22.583 1.00 31.88 ?  26  VAL   D CG2  1 
ATOM   3798 N N    . GLY   D 2 27  ? -18.067 -23.553 -20.849 1.00 31.70 ?  27  GLY   D N    1 
ATOM   3799 C CA   . GLY   D 2 27  ? -17.987 -24.231 -19.561 1.00 25.39 ?  27  GLY   D CA   1 
ATOM   3800 C C    . GLY   D 2 27  ? -16.953 -23.646 -18.617 1.00 28.17 ?  27  GLY   D C    1 
ATOM   3801 O O    . GLY   D 2 27  ? -17.244 -23.381 -17.445 1.00 24.63 ?  27  GLY   D O    1 
ATOM   3802 N N    . ASP   D 2 28  ? -15.734 -23.435 -19.113 1.00 22.04 ?  28  ASP   D N    1 
ATOM   3803 C CA   . ASP   D 2 28  ? -14.572 -23.184 -18.271 1.00 21.03 ?  28  ASP   D CA   1 
ATOM   3804 C C    . ASP   D 2 28  ? -14.140 -21.725 -18.271 1.00 21.22 ?  28  ASP   D C    1 
ATOM   3805 O O    . ASP   D 2 28  ? -13.078 -21.399 -17.716 1.00 22.12 ?  28  ASP   D O    1 
ATOM   3806 C CB   . ASP   D 2 28  ? -13.407 -24.078 -18.703 1.00 23.58 ?  28  ASP   D CB   1 
ATOM   3807 C CG   . ASP   D 2 28  ? -12.953 -23.821 -20.134 1.00 26.69 ?  28  ASP   D CG   1 
ATOM   3808 O OD1  . ASP   D 2 28  ? -13.323 -22.780 -20.732 1.00 21.00 ?  28  ASP   D OD1  1 
ATOM   3809 O OD2  . ASP   D 2 28  ? -12.206 -24.672 -20.646 1.00 23.58 -1 28  ASP   D OD2  1 
ATOM   3810 N N    . GLY   D 2 29  ? -14.930 -20.846 -18.880 1.00 19.00 ?  29  GLY   D N    1 
ATOM   3811 C CA   . GLY   D 2 29  ? -14.677 -19.426 -18.829 1.00 26.42 ?  29  GLY   D CA   1 
ATOM   3812 C C    . GLY   D 2 29  ? -13.453 -18.968 -19.582 1.00 23.94 ?  29  GLY   D C    1 
ATOM   3813 O O    . GLY   D 2 29  ? -13.042 -17.818 -19.405 1.00 26.12 ?  29  GLY   D O    1 
ATOM   3814 N N    . THR   D 2 30  ? -12.857 -19.831 -20.412 1.00 20.98 ?  30  THR   D N    1 
ATOM   3815 C CA   . THR   D 2 30  ? -11.616 -19.459 -21.097 1.00 16.92 ?  30  THR   D CA   1 
ATOM   3816 C C    . THR   D 2 30  ? -11.848 -18.419 -22.198 1.00 21.71 ?  30  THR   D C    1 
ATOM   3817 O O    . THR   D 2 30  ? -10.921 -17.676 -22.539 1.00 19.08 ?  30  THR   D O    1 
ATOM   3818 C CB   . THR   D 2 30  ? -10.925 -20.696 -21.677 1.00 17.79 ?  30  THR   D CB   1 
ATOM   3819 O OG1  . THR   D 2 30  ? -11.860 -21.475 -22.421 1.00 21.53 ?  30  THR   D OG1  1 
ATOM   3820 C CG2  . THR   D 2 30  ? -10.365 -21.568 -20.561 1.00 20.57 ?  30  THR   D CG2  1 
ATOM   3821 N N    . VAL   D 2 31  ? -13.038 -18.365 -22.787 1.00 19.60 ?  31  VAL   D N    1 
ATOM   3822 C CA   . VAL   D 2 31  ? -13.432 -17.222 -23.607 1.00 18.02 ?  31  VAL   D CA   1 
ATOM   3823 C C    . VAL   D 2 31  ? -14.823 -16.775 -23.182 1.00 20.93 ?  31  VAL   D C    1 
ATOM   3824 O O    . VAL   D 2 31  ? -15.634 -17.564 -22.682 1.00 20.65 ?  31  VAL   D O    1 
ATOM   3825 C CB   . VAL   D 2 31  ? -13.411 -17.496 -25.144 1.00 17.18 ?  31  VAL   D CB   1 
ATOM   3826 C CG1  . VAL   D 2 31  ? -12.042 -18.030 -25.610 1.00 18.00 ?  31  VAL   D CG1  1 
ATOM   3827 C CG2  . VAL   D 2 31  ? -14.529 -18.416 -25.569 1.00 23.02 ?  31  VAL   D CG2  1 
ATOM   3828 N N    . SER   D 2 32  ? -15.100 -15.493 -23.398 1.00 15.80 ?  32  SER   D N    1 
ATOM   3829 C CA   . SER   D 2 32  ? -16.403 -14.927 -23.071 1.00 17.19 ?  32  SER   D CA   1 
ATOM   3830 C C    . SER   D 2 32  ? -16.722 -13.798 -24.046 1.00 20.46 ?  32  SER   D C    1 
ATOM   3831 O O    . SER   D 2 32  ? -15.817 -13.157 -24.579 1.00 18.57 ?  32  SER   D O    1 
ATOM   3832 C CB   . SER   D 2 32  ? -16.429 -14.401 -21.628 1.00 22.49 ?  32  SER   D CB   1 
ATOM   3833 O OG   . SER   D 2 32  ? -17.753 -14.027 -21.282 1.00 32.17 ?  32  SER   D OG   1 
ATOM   3834 N N    . TRP   D 2 33  ? -18.011 -13.547 -24.277 1.00 17.88 ?  33  TRP   D N    1 
ATOM   3835 C CA   . TRP   D 2 33  ? -18.390 -12.399 -25.095 1.00 19.68 ?  33  TRP   D CA   1 
ATOM   3836 C C    . TRP   D 2 33  ? -19.732 -11.860 -24.616 1.00 18.04 ?  33  TRP   D C    1 
ATOM   3837 O O    . TRP   D 2 33  ? -20.494 -12.560 -23.948 1.00 20.14 ?  33  TRP   D O    1 
ATOM   3838 C CB   . TRP   D 2 33  ? -18.466 -12.749 -26.594 1.00 19.58 ?  33  TRP   D CB   1 
ATOM   3839 C CG   . TRP   D 2 33  ? -19.472 -13.804 -26.893 1.00 19.64 ?  33  TRP   D CG   1 
ATOM   3840 C CD1  . TRP   D 2 33  ? -20.733 -13.625 -27.398 1.00 18.04 ?  33  TRP   D CD1  1 
ATOM   3841 C CD2  . TRP   D 2 33  ? -19.327 -15.206 -26.661 1.00 17.53 ?  33  TRP   D CD2  1 
ATOM   3842 N NE1  . TRP   D 2 33  ? -21.371 -14.831 -27.512 1.00 17.68 ?  33  TRP   D NE1  1 
ATOM   3843 C CE2  . TRP   D 2 33  ? -20.536 -15.819 -27.053 1.00 17.73 ?  33  TRP   D CE2  1 
ATOM   3844 C CE3  . TRP   D 2 33  ? -18.287 -16.006 -26.160 1.00 16.45 ?  33  TRP   D CE3  1 
ATOM   3845 C CZ2  . TRP   D 2 33  ? -20.739 -17.190 -26.966 1.00 19.89 ?  33  TRP   D CZ2  1 
ATOM   3846 C CZ3  . TRP   D 2 33  ? -18.483 -17.358 -26.071 1.00 20.26 ?  33  TRP   D CZ3  1 
ATOM   3847 C CH2  . TRP   D 2 33  ? -19.710 -17.949 -26.475 1.00 20.76 ?  33  TRP   D CH2  1 
ATOM   3848 N N    . GLY   D 2 34  ? -20.001 -10.602 -24.977 1.00 20.94 ?  34  GLY   D N    1 
ATOM   3849 C CA   . GLY   D 2 34  ? -21.263 -9.957  -24.623 1.00 20.14 ?  34  GLY   D CA   1 
ATOM   3850 C C    . GLY   D 2 34  ? -21.374 -8.609  -25.304 1.00 23.53 ?  34  GLY   D C    1 
ATOM   3851 O O    . GLY   D 2 34  ? -20.453 -8.163  -25.984 1.00 22.94 ?  34  GLY   D O    1 
ATOM   3852 N N    . LEU   D 2 35  ? -22.526 -7.961  -25.140 1.00 21.30 ?  35  LEU   D N    1 
ATOM   3853 C CA   . LEU   D 2 35  ? -22.711 -6.658  -25.769 1.00 25.89 ?  35  LEU   D CA   1 
ATOM   3854 C C    . LEU   D 2 35  ? -21.941 -5.582  -25.016 1.00 28.17 ?  35  LEU   D C    1 
ATOM   3855 O O    . LEU   D 2 35  ? -21.847 -5.609  -23.787 1.00 31.24 ?  35  LEU   D O    1 
ATOM   3856 C CB   . LEU   D 2 35  ? -24.190 -6.288  -25.806 1.00 25.77 ?  35  LEU   D CB   1 
ATOM   3857 C CG   . LEU   D 2 35  ? -25.014 -6.847  -26.955 1.00 26.82 ?  35  LEU   D CG   1 
ATOM   3858 C CD1  . LEU   D 2 35  ? -26.476 -6.518  -26.673 1.00 26.20 ?  35  LEU   D CD1  1 
ATOM   3859 C CD2  . LEU   D 2 35  ? -24.589 -6.258  -28.291 1.00 25.03 ?  35  LEU   D CD2  1 
ATOM   3860 N N    . GLU   D 2 36  ? -21.376 -4.628  -25.756 1.00 27.44 ?  36  GLU   D N    1 
ATOM   3861 C CA   . GLU   D 2 36  ? -20.729 -3.508  -25.084 1.00 30.61 ?  36  GLU   D CA   1 
ATOM   3862 C C    . GLU   D 2 36  ? -21.758 -2.658  -24.352 1.00 36.97 ?  36  GLU   D C    1 
ATOM   3863 O O    . GLU   D 2 36  ? -21.513 -2.200  -23.229 1.00 32.29 ?  36  GLU   D O    1 
ATOM   3864 C CB   . GLU   D 2 36  ? -19.957 -2.655  -26.079 1.00 31.19 ?  36  GLU   D CB   1 
ATOM   3865 C CG   . GLU   D 2 36  ? -19.114 -1.614  -25.394 1.00 36.58 ?  36  GLU   D CG   1 
ATOM   3866 C CD   . GLU   D 2 36  ? -18.158 -0.964  -26.336 1.00 41.20 ?  36  GLU   D CD   1 
ATOM   3867 O OE1  . GLU   D 2 36  ? -17.108 -1.576  -26.625 1.00 43.02 ?  36  GLU   D OE1  1 
ATOM   3868 O OE2  . GLU   D 2 36  ? -18.456 0.161   -26.786 1.00 50.28 -1 36  GLU   D OE2  1 
ATOM   3869 N N    . ASP   D 2 37  ? -22.910 -2.438  -24.982 1.00 32.65 ?  37  ASP   D N    1 
ATOM   3870 C CA   . ASP   D 2 37  ? -24.037 -1.728  -24.388 1.00 37.76 ?  37  ASP   D CA   1 
ATOM   3871 C C    . ASP   D 2 37  ? -25.247 -2.634  -24.540 1.00 31.55 ?  37  ASP   D C    1 
ATOM   3872 O O    . ASP   D 2 37  ? -25.751 -2.809  -25.654 1.00 34.38 ?  37  ASP   D O    1 
ATOM   3873 C CB   . ASP   D 2 37  ? -24.260 -0.380  -25.073 1.00 30.22 ?  37  ASP   D CB   1 
ATOM   3874 C CG   . ASP   D 2 37  ? -25.539 0.310   -24.622 1.00 29.45 ?  37  ASP   D CG   1 
ATOM   3875 O OD1  . ASP   D 2 37  ? -26.220 -0.200  -23.706 1.00 34.02 ?  37  ASP   D OD1  1 
ATOM   3876 O OD2  . ASP   D 2 37  ? -25.861 1.369   -25.194 1.00 40.65 -1 37  ASP   D OD2  1 
ATOM   3877 N N    . ASP   D 2 38  ? -25.707 -3.220  -23.428 1.00 38.62 ?  38  ASP   D N    1 
ATOM   3878 C CA   . ASP   D 2 38  ? -26.804 -4.195  -23.504 1.00 45.82 ?  38  ASP   D CA   1 
ATOM   3879 C C    . ASP   D 2 38  ? -28.131 -3.574  -23.895 1.00 40.03 ?  38  ASP   D C    1 
ATOM   3880 O O    . ASP   D 2 38  ? -29.130 -4.314  -23.863 1.00 38.36 ?  38  ASP   D O    1 
ATOM   3881 C CB   . ASP   D 2 38  ? -26.960 -4.946  -22.178 1.00 45.92 ?  38  ASP   D CB   1 
ATOM   3882 C CG   . ASP   D 2 38  ? -27.076 -4.019  -20.981 1.00 52.14 ?  38  ASP   D CG   1 
ATOM   3883 O OD1  . ASP   D 2 38  ? -27.399 -2.824  -21.167 1.00 53.06 ?  38  ASP   D OD1  1 
ATOM   3884 O OD2  . ASP   D 2 38  ? -26.836 -4.489  -19.848 1.00 62.00 -1 38  ASP   D OD2  1 
ATOM   3885 N N    . GLU   D 2 39  ? -28.167 -2.282  -24.229 1.00 36.12 ?  39  GLU   D N    1 
ATOM   3886 C CA   . GLU   D 2 39  ? -29.328 -1.660  -24.856 1.00 39.39 ?  39  GLU   D CA   1 
ATOM   3887 C C    . GLU   D 2 39  ? -29.056 -1.247  -26.299 1.00 36.01 ?  39  GLU   D C    1 
ATOM   3888 O O    . GLU   D 2 39  ? -29.846 -0.495  -26.878 1.00 38.34 ?  39  GLU   D O    1 
ATOM   3889 C CB   . GLU   D 2 39  ? -29.796 -0.450  -24.035 1.00 46.06 ?  39  GLU   D CB   1 
ATOM   3890 C CG   . GLU   D 2 39  ? -30.020 -0.764  -22.563 1.00 32.45 ?  39  GLU   D CG   1 
ATOM   3891 C CD   . GLU   D 2 39  ? -30.444 0.444   -21.727 1.00 47.65 ?  39  GLU   D CD   1 
ATOM   3892 O OE1  . GLU   D 2 39  ? -30.631 1.553   -22.279 1.00 48.43 ?  39  GLU   D OE1  1 
ATOM   3893 O OE2  . GLU   D 2 39  ? -30.607 0.271   -20.500 1.00 42.81 -1 39  GLU   D OE2  1 
ATOM   3894 N N    . ASP   D 2 40  ? -27.951 -1.709  -26.888 1.00 35.98 ?  40  ASP   D N    1 
ATOM   3895 C CA   . ASP   D 2 40  ? -27.604 -1.407  -28.277 1.00 32.90 ?  40  ASP   D CA   1 
ATOM   3896 C C    . ASP   D 2 40  ? -28.496 -2.218  -29.212 1.00 33.87 ?  40  ASP   D C    1 
ATOM   3897 O O    . ASP   D 2 40  ? -28.194 -3.368  -29.545 1.00 30.80 ?  40  ASP   D O    1 
ATOM   3898 C CB   . ASP   D 2 40  ? -26.124 -1.699  -28.533 1.00 30.47 ?  40  ASP   D CB   1 
ATOM   3899 C CG   . ASP   D 2 40  ? -25.744 -1.591  -30.005 1.00 31.61 ?  40  ASP   D CG   1 
ATOM   3900 O OD1  . ASP   D 2 40  ? -26.537 -1.031  -30.797 1.00 36.64 ?  40  ASP   D OD1  1 
ATOM   3901 O OD2  . ASP   D 2 40  ? -24.647 -2.077  -30.383 1.00 33.42 -1 40  ASP   D OD2  1 
ATOM   3902 N N    . MET   D 2 41  ? -29.590 -1.596  -29.662 1.00 31.49 ?  41  MET   D N    1 
ATOM   3903 C CA   . MET   D 2 41  ? -30.508 -2.224  -30.606 1.00 34.21 ?  41  MET   D CA   1 
ATOM   3904 C C    . MET   D 2 41  ? -29.822 -2.783  -31.843 1.00 25.03 ?  41  MET   D C    1 
ATOM   3905 O O    . MET   D 2 41  ? -30.305 -3.768  -32.415 1.00 24.34 ?  41  MET   D O    1 
ATOM   3906 C CB   . MET   D 2 41  ? -31.564 -1.220  -31.067 1.00 31.96 ?  41  MET   D CB   1 
ATOM   3907 C CG   . MET   D 2 41  ? -32.687 -1.885  -31.838 1.00 27.18 ?  41  MET   D CG   1 
ATOM   3908 S SD   . MET   D 2 41  ? -33.716 -2.991  -30.901 1.00 24.74 ?  41  MET   D SD   1 
ATOM   3909 C CE   . MET   D 2 41  ? -34.793 -3.585  -32.223 1.00 27.87 ?  41  MET   D CE   1 
ATOM   3910 N N    . THR   D 2 42  ? -28.748 -2.142  -32.319 1.00 25.13 ?  42  THR   D N    1 
ATOM   3911 C CA   . THR   D 2 42  ? -28.118 -2.596  -33.556 1.00 25.26 ?  42  THR   D CA   1 
ATOM   3912 C C    . THR   D 2 42  ? -27.275 -3.850  -33.361 1.00 24.19 ?  42  THR   D C    1 
ATOM   3913 O O    . THR   D 2 42  ? -26.821 -4.431  -34.355 1.00 25.79 ?  42  THR   D O    1 
ATOM   3914 C CB   . THR   D 2 42  ? -27.232 -1.500  -34.155 1.00 30.72 ?  42  THR   D CB   1 
ATOM   3915 O OG1  . THR   D 2 42  ? -26.060 -1.332  -33.339 1.00 30.52 ?  42  THR   D OG1  1 
ATOM   3916 C CG2  . THR   D 2 42  ? -27.995 -0.175  -34.234 1.00 28.60 ?  42  THR   D CG2  1 
ATOM   3917 N N    . LEU   D 2 43  ? -27.056 -4.264  -32.115 1.00 23.40 ?  43  LEU   D N    1 
ATOM   3918 C CA   . LEU   D 2 43  ? -26.261 -5.454  -31.798 1.00 19.91 ?  43  LEU   D CA   1 
ATOM   3919 C C    . LEU   D 2 43  ? -24.904 -5.435  -32.494 1.00 23.25 ?  43  LEU   D C    1 
ATOM   3920 O O    . LEU   D 2 43  ? -24.367 -6.478  -32.880 1.00 20.09 ?  43  LEU   D O    1 
ATOM   3921 C CB   . LEU   D 2 43  ? -27.035 -6.723  -32.149 1.00 19.08 ?  43  LEU   D CB   1 
ATOM   3922 C CG   . LEU   D 2 43  ? -28.402 -6.769  -31.469 1.00 25.80 ?  43  LEU   D CG   1 
ATOM   3923 C CD1  . LEU   D 2 43  ? -29.198 -7.966  -31.958 1.00 25.87 ?  43  LEU   D CD1  1 
ATOM   3924 C CD2  . LEU   D 2 43  ? -28.176 -6.831  -29.958 1.00 25.74 ?  43  LEU   D CD2  1 
ATOM   3925 N N    . THR   D 2 44  ? -24.324 -4.241  -32.627 1.00 23.18 ?  44  THR   D N    1 
ATOM   3926 C CA   . THR   D 2 44  ? -23.116 -4.115  -33.436 1.00 26.56 ?  44  THR   D CA   1 
ATOM   3927 C C    . THR   D 2 44  ? -21.830 -4.267  -32.631 1.00 24.54 ?  44  THR   D C    1 
ATOM   3928 O O    . THR   D 2 44  ? -20.905 -4.949  -33.086 1.00 22.15 ?  44  THR   D O    1 
ATOM   3929 C CB   . THR   D 2 44  ? -23.106 -2.770  -34.169 1.00 29.15 ?  44  THR   D CB   1 
ATOM   3930 O OG1  . THR   D 2 44  ? -24.198 -2.736  -35.088 1.00 23.51 ?  44  THR   D OG1  1 
ATOM   3931 C CG2  . THR   D 2 44  ? -21.812 -2.597  -34.957 1.00 24.57 ?  44  THR   D CG2  1 
ATOM   3932 N N    . ARG   D 2 45  ? -21.728 -3.644  -31.456 1.00 21.47 ?  45  ARG   D N    1 
ATOM   3933 C CA   . ARG   D 2 45  ? -20.471 -3.603  -30.715 1.00 24.27 ?  45  ARG   D CA   1 
ATOM   3934 C C    . ARG   D 2 45  ? -20.509 -4.579  -29.540 1.00 24.98 ?  45  ARG   D C    1 
ATOM   3935 O O    . ARG   D 2 45  ? -21.387 -4.495  -28.673 1.00 25.53 ?  45  ARG   D O    1 
ATOM   3936 C CB   . ARG   D 2 45  ? -20.151 -2.177  -30.249 1.00 28.83 ?  45  ARG   D CB   1 
ATOM   3937 C CG   . ARG   D 2 45  ? -20.292 -1.132  -31.354 1.00 35.38 ?  45  ARG   D CG   1 
ATOM   3938 C CD   . ARG   D 2 45  ? -20.233 0.306   -30.831 1.00 42.59 ?  45  ARG   D CD   1 
ATOM   3939 N NE   . ARG   D 2 45  ? -21.566 0.873   -30.640 1.00 54.24 ?  45  ARG   D NE   1 
ATOM   3940 C CZ   . ARG   D 2 45  ? -22.480 1.016   -31.593 1.00 53.02 ?  45  ARG   D CZ   1 
ATOM   3941 N NH1  . ARG   D 2 45  ? -22.238 0.665   -32.848 1.00 53.53 ?  45  ARG   D NH1  1 
ATOM   3942 N NH2  . ARG   D 2 45  ? -23.667 1.529   -31.279 1.00 55.53 ?  45  ARG   D NH2  1 
ATOM   3943 N N    . TRP   D 2 46  ? -19.534 -5.485  -29.509 1.00 24.12 ?  46  TRP   D N    1 
ATOM   3944 C CA   . TRP   D 2 46  ? -19.398 -6.531  -28.514 1.00 23.08 ?  46  TRP   D CA   1 
ATOM   3945 C C    . TRP   D 2 46  ? -18.045 -6.409  -27.829 1.00 19.96 ?  46  TRP   D C    1 
ATOM   3946 O O    . TRP   D 2 46  ? -17.080 -5.864  -28.381 1.00 21.80 ?  46  TRP   D O    1 
ATOM   3947 C CB   . TRP   D 2 46  ? -19.527 -7.932  -29.159 1.00 18.84 ?  46  TRP   D CB   1 
ATOM   3948 C CG   . TRP   D 2 46  ? -20.866 -8.198  -29.781 1.00 21.92 ?  46  TRP   D CG   1 
ATOM   3949 C CD1  . TRP   D 2 46  ? -21.356 -7.637  -30.928 1.00 20.15 ?  46  TRP   D CD1  1 
ATOM   3950 C CD2  . TRP   D 2 46  ? -21.885 -9.096  -29.303 1.00 18.11 ?  46  TRP   D CD2  1 
ATOM   3951 N NE1  . TRP   D 2 46  ? -22.621 -8.116  -31.182 1.00 18.03 ?  46  TRP   D NE1  1 
ATOM   3952 C CE2  . TRP   D 2 46  ? -22.966 -9.020  -30.210 1.00 17.79 ?  46  TRP   D CE2  1 
ATOM   3953 C CE3  . TRP   D 2 46  ? -21.985 -9.963  -28.205 1.00 17.32 ?  46  TRP   D CE3  1 
ATOM   3954 C CZ2  . TRP   D 2 46  ? -24.146 -9.764  -30.041 1.00 22.16 ?  46  TRP   D CZ2  1 
ATOM   3955 C CZ3  . TRP   D 2 46  ? -23.168 -10.707 -28.035 1.00 21.37 ?  46  TRP   D CZ3  1 
ATOM   3956 C CH2  . TRP   D 2 46  ? -24.228 -10.596 -28.952 1.00 19.23 ?  46  TRP   D CH2  1 
ATOM   3957 N N    . THR   D 2 47  ? -17.988 -6.944  -26.620 1.00 20.80 ?  47  THR   D N    1 
ATOM   3958 C CA   . THR   D 2 47  ? -16.753 -7.140  -25.888 1.00 23.29 ?  47  THR   D CA   1 
ATOM   3959 C C    . THR   D 2 47  ? -16.426 -8.625  -25.879 1.00 24.12 ?  47  THR   D C    1 
ATOM   3960 O O    . THR   D 2 47  ? -17.331 -9.474  -25.848 1.00 26.64 ?  47  THR   D O    1 
ATOM   3961 C CB   . THR   D 2 47  ? -16.865 -6.627  -24.451 1.00 29.07 ?  47  THR   D CB   1 
ATOM   3962 O OG1  . THR   D 2 47  ? -17.893 -7.357  -23.777 1.00 32.32 ?  47  THR   D OG1  1 
ATOM   3963 C CG2  . THR   D 2 47  ? -17.240 -5.150  -24.441 1.00 27.80 ?  47  THR   D CG2  1 
ATOM   3964 N N    . GLY   D 2 48  ? -15.129 -8.924  -25.912 1.00 23.28 ?  48  GLY   D N    1 
ATOM   3965 C CA   . GLY   D 2 48  ? -14.663 -10.284 -25.773 1.00 20.72 ?  48  GLY   D CA   1 
ATOM   3966 C C    . GLY   D 2 48  ? -13.586 -10.375 -24.709 1.00 20.81 ?  48  GLY   D C    1 
ATOM   3967 O O    . GLY   D 2 48  ? -12.905 -9.404  -24.391 1.00 21.08 ?  48  GLY   D O    1 
ATOM   3968 N N    . MET   D 2 49  ? -13.434 -11.585 -24.186 1.00 19.33 ?  49  MET   D N    1 
ATOM   3969 C CA   . MET   D 2 49  ? -12.471 -11.923 -23.147 1.00 19.08 ?  49  MET   D CA   1 
ATOM   3970 C C    . MET   D 2 49  ? -11.828 -13.260 -23.476 1.00 18.81 ?  49  MET   D C    1 
ATOM   3971 O O    . MET   D 2 49  ? -12.527 -14.231 -23.796 1.00 18.06 ?  49  MET   D O    1 
ATOM   3972 C CB   . MET   D 2 49  ? -13.178 -11.909 -21.770 1.00 25.61 ?  49  MET   D CB   1 
ATOM   3973 C CG   . MET   D 2 49  ? -12.311 -12.005 -20.509 1.00 28.10 ?  49  MET   D CG   1 
ATOM   3974 S SD   . MET   D 2 49  ? -11.467 -13.591 -20.290 1.00 28.71 ?  49  MET   D SD   1 
ATOM   3975 C CE   . MET   D 2 49  ? -12.906 -14.677 -20.106 1.00 24.36 ?  49  MET   D CE   1 
ATOM   3976 N N    . ILE   D 2 50  ? -10.492 -13.286 -23.456 1.00 16.56 ?  50  ILE   D N    1 
ATOM   3977 C CA   . ILE   D 2 50  ? -9.717  -14.509 -23.624 1.00 17.65 ?  50  ILE   D CA   1 
ATOM   3978 C C    . ILE   D 2 50  ? -8.767  -14.654 -22.445 1.00 18.12 ?  50  ILE   D C    1 
ATOM   3979 O O    . ILE   D 2 50  ? -8.013  -13.726 -22.135 1.00 18.82 ?  50  ILE   D O    1 
ATOM   3980 C CB   . ILE   D 2 50  ? -8.895  -14.516 -24.923 1.00 15.96 ?  50  ILE   D CB   1 
ATOM   3981 C CG1  . ILE   D 2 50  ? -9.818  -14.459 -26.138 1.00 14.34 ?  50  ILE   D CG1  1 
ATOM   3982 C CG2  . ILE   D 2 50  ? -7.994  -15.771 -24.953 1.00 14.84 ?  50  ILE   D CG2  1 
ATOM   3983 C CD1  . ILE   D 2 50  ? -9.028  -14.278 -27.451 1.00 15.06 ?  50  ILE   D CD1  1 
ATOM   3984 N N    . ILE   D 2 51  ? -8.762  -15.818 -21.828 1.00 17.03 ?  51  ILE   D N    1 
ATOM   3985 C CA   . ILE   D 2 51  ? -7.739  -16.127 -20.833 1.00 19.57 ?  51  ILE   D CA   1 
ATOM   3986 C C    . ILE   D 2 51  ? -6.530  -16.724 -21.548 1.00 20.03 ?  51  ILE   D C    1 
ATOM   3987 O O    . ILE   D 2 51  ? -6.650  -17.716 -22.274 1.00 20.33 ?  51  ILE   D O    1 
ATOM   3988 C CB   . ILE   D 2 51  ? -8.280  -17.093 -19.766 1.00 19.95 ?  51  ILE   D CB   1 
ATOM   3989 C CG1  . ILE   D 2 51  ? -9.411  -16.429 -18.998 1.00 25.50 ?  51  ILE   D CG1  1 
ATOM   3990 C CG2  . ILE   D 2 51  ? -7.124  -17.435 -18.791 1.00 22.82 ?  51  ILE   D CG2  1 
ATOM   3991 C CD1  . ILE   D 2 51  ? -9.996  -17.284 -17.873 1.00 31.12 ?  51  ILE   D CD1  1 
ATOM   3992 N N    . GLY   D 2 52  ? -5.351  -16.131 -21.343 1.00 22.58 ?  52  GLY   D N    1 
ATOM   3993 C CA   . GLY   D 2 52  ? -4.152  -16.667 -21.951 1.00 21.46 ?  52  GLY   D CA   1 
ATOM   3994 C C    . GLY   D 2 52  ? -3.927  -18.139 -21.631 1.00 18.93 ?  52  GLY   D C    1 
ATOM   3995 O O    . GLY   D 2 52  ? -4.032  -18.565 -20.478 1.00 22.81 ?  52  GLY   D O    1 
ATOM   3996 N N    . PRO   D 2 53  ? -3.588  -18.942 -22.638 1.00 19.82 ?  53  PRO   D N    1 
ATOM   3997 C CA   . PRO   D 2 53  ? -3.514  -20.406 -22.437 1.00 20.68 ?  53  PRO   D CA   1 
ATOM   3998 C C    . PRO   D 2 53  ? -2.290  -20.811 -21.632 1.00 24.83 ?  53  PRO   D C    1 
ATOM   3999 O O    . PRO   D 2 53  ? -1.283  -20.082 -21.574 1.00 22.42 ?  53  PRO   D O    1 
ATOM   4000 C CB   . PRO   D 2 53  ? -3.465  -20.970 -23.868 1.00 23.07 ?  53  PRO   D CB   1 
ATOM   4001 C CG   . PRO   D 2 53  ? -3.164  -19.795 -24.756 1.00 26.48 ?  53  PRO   D CG   1 
ATOM   4002 C CD   . PRO   D 2 53  ? -3.642  -18.570 -24.060 1.00 18.38 ?  53  PRO   D CD   1 
ATOM   4003 N N    . PRO   D 2 54  ? -2.338  -21.982 -21.003 1.00 28.29 ?  54  PRO   D N    1 
ATOM   4004 C CA   . PRO   D 2 54  ? -1.222  -22.412 -20.155 1.00 28.06 ?  54  PRO   D CA   1 
ATOM   4005 C C    . PRO   D 2 54  ? -0.017  -22.844 -20.972 1.00 25.24 ?  54  PRO   D C    1 
ATOM   4006 O O    . PRO   D 2 54  ? -0.119  -23.260 -22.130 1.00 30.35 ?  54  PRO   D O    1 
ATOM   4007 C CB   . PRO   D 2 54  ? -1.812  -23.594 -19.376 1.00 31.03 ?  54  PRO   D CB   1 
ATOM   4008 C CG   . PRO   D 2 54  ? -2.847  -24.151 -20.283 1.00 31.77 ?  54  PRO   D CG   1 
ATOM   4009 C CD   . PRO   D 2 54  ? -3.444  -22.961 -21.000 1.00 30.11 ?  54  PRO   D CD   1 
ATOM   4010 N N    . ARG   D 2 55  ? 1.150   -22.753 -20.333 1.00 32.97 ?  55  ARG   D N    1 
ATOM   4011 C CA   . ARG   D 2 55  ? 2.409   -23.159 -20.954 1.00 26.07 ?  55  ARG   D CA   1 
ATOM   4012 C C    . ARG   D 2 55  ? 2.741   -22.294 -22.169 1.00 25.03 ?  55  ARG   D C    1 
ATOM   4013 O O    . ARG   D 2 55  ? 3.303   -22.769 -23.159 1.00 34.24 ?  55  ARG   D O    1 
ATOM   4014 C CB   . ARG   D 2 55  ? 2.387   -24.646 -21.316 1.00 31.57 ?  55  ARG   D CB   1 
ATOM   4015 C CG   . ARG   D 2 55  ? 2.338   -25.551 -20.077 1.00 34.95 ?  55  ARG   D CG   1 
ATOM   4016 C CD   . ARG   D 2 55  ? 2.046   -26.992 -20.441 1.00 36.19 ?  55  ARG   D CD   1 
ATOM   4017 N NE   . ARG   D 2 55  ? 0.840   -27.119 -21.250 1.00 44.26 ?  55  ARG   D NE   1 
ATOM   4018 C CZ   . ARG   D 2 55  ? -0.384  -27.190 -20.743 1.00 39.09 ?  55  ARG   D CZ   1 
ATOM   4019 N NH1  . ARG   D 2 55  ? -0.594  -27.115 -19.438 1.00 35.87 ?  55  ARG   D NH1  1 
ATOM   4020 N NH2  . ARG   D 2 55  ? -1.421  -27.323 -21.564 1.00 45.34 ?  55  ARG   D NH2  1 
ATOM   4021 N N    . THR   D 2 56  ? 2.376   -21.021 -22.091 1.00 27.81 ?  56  THR   D N    1 
ATOM   4022 C CA   . THR   D 2 56  ? 2.715   -20.024 -23.091 1.00 23.51 ?  56  THR   D CA   1 
ATOM   4023 C C    . THR   D 2 56  ? 3.061   -18.751 -22.343 1.00 21.63 ?  56  THR   D C    1 
ATOM   4024 O O    . THR   D 2 56  ? 2.754   -18.603 -21.159 1.00 26.64 ?  56  THR   D O    1 
ATOM   4025 C CB   . THR   D 2 56  ? 1.564   -19.737 -24.074 1.00 24.24 ?  56  THR   D CB   1 
ATOM   4026 O OG1  . THR   D 2 56  ? 0.602   -18.906 -23.414 1.00 24.74 ?  56  THR   D OG1  1 
ATOM   4027 C CG2  . THR   D 2 56  ? 0.909   -21.019 -24.543 1.00 28.93 ?  56  THR   D CG2  1 
ATOM   4028 N N    . ASN   D 2 57  ? 3.694   -17.811 -23.046 1.00 26.13 ?  57  ASN   D N    1 
ATOM   4029 C CA   . ASN   D 2 57  ? 3.964   -16.509 -22.452 1.00 26.00 ?  57  ASN   D CA   1 
ATOM   4030 C C    . ASN   D 2 57  ? 2.701   -15.686 -22.208 1.00 23.93 ?  57  ASN   D C    1 
ATOM   4031 O O    . ASN   D 2 57  ? 2.781   -14.626 -21.576 1.00 24.79 ?  57  ASN   D O    1 
ATOM   4032 C CB   . ASN   D 2 57  ? 4.942   -15.722 -23.338 1.00 24.28 ?  57  ASN   D CB   1 
ATOM   4033 C CG   . ASN   D 2 57  ? 6.355   -16.303 -23.324 1.00 33.62 ?  57  ASN   D CG   1 
ATOM   4034 O OD1  . ASN   D 2 57  ? 6.609   -17.356 -22.739 1.00 32.14 ?  57  ASN   D OD1  1 
ATOM   4035 N ND2  . ASN   D 2 57  ? 7.276   -15.620 -23.997 1.00 29.31 ?  57  ASN   D ND2  1 
ATOM   4036 N N    . TYR   D 2 58  ? 1.532   -16.137 -22.679 1.00 26.67 ?  58  TYR   D N    1 
ATOM   4037 C CA   . TYR   D 2 58  ? 0.276   -15.467 -22.366 1.00 22.31 ?  58  TYR   D CA   1 
ATOM   4038 C C    . TYR   D 2 58  ? -0.375  -16.009 -21.100 1.00 26.97 ?  58  TYR   D C    1 
ATOM   4039 O O    . TYR   D 2 58  ? -1.351  -15.417 -20.618 1.00 25.33 ?  58  TYR   D O    1 
ATOM   4040 C CB   . TYR   D 2 58  ? -0.728  -15.616 -23.532 1.00 18.84 ?  58  TYR   D CB   1 
ATOM   4041 C CG   . TYR   D 2 58  ? -0.152  -15.289 -24.901 1.00 19.08 ?  58  TYR   D CG   1 
ATOM   4042 C CD1  . TYR   D 2 58  ? 0.041   -13.973 -25.296 1.00 22.21 ?  58  TYR   D CD1  1 
ATOM   4043 C CD2  . TYR   D 2 58  ? 0.203   -16.303 -25.790 1.00 21.26 ?  58  TYR   D CD2  1 
ATOM   4044 C CE1  . TYR   D 2 58  ? 0.563   -13.665 -26.555 1.00 19.59 ?  58  TYR   D CE1  1 
ATOM   4045 C CE2  . TYR   D 2 58  ? 0.724   -16.008 -27.056 1.00 20.40 ?  58  TYR   D CE2  1 
ATOM   4046 C CZ   . TYR   D 2 58  ? 0.909   -14.684 -27.426 1.00 19.56 ?  58  TYR   D CZ   1 
ATOM   4047 O OH   . TYR   D 2 58  ? 1.426   -14.388 -28.673 1.00 21.83 ?  58  TYR   D OH   1 
ATOM   4048 N N    . GLU   D 2 59  ? 0.161   -17.106 -20.563 1.00 25.99 ?  59  GLU   D N    1 
ATOM   4049 C CA   . GLU   D 2 59  ? -0.497  -17.893 -19.528 1.00 27.27 ?  59  GLU   D CA   1 
ATOM   4050 C C    . GLU   D 2 59  ? -1.107  -17.018 -18.443 1.00 30.18 ?  59  GLU   D C    1 
ATOM   4051 O O    . GLU   D 2 59  ? -0.433  -16.164 -17.857 1.00 26.22 ?  59  GLU   D O    1 
ATOM   4052 C CB   . GLU   D 2 59  ? 0.513   -18.877 -18.937 1.00 32.81 ?  59  GLU   D CB   1 
ATOM   4053 C CG   . GLU   D 2 59  ? -0.100  -19.988 -18.121 1.00 40.33 ?  59  GLU   D CG   1 
ATOM   4054 C CD   . GLU   D 2 59  ? 0.912   -20.634 -17.194 1.00 44.98 ?  59  GLU   D CD   1 
ATOM   4055 O OE1  . GLU   D 2 59  ? 2.115   -20.655 -17.549 1.00 46.44 ?  59  GLU   D OE1  1 
ATOM   4056 O OE2  . GLU   D 2 59  ? 0.502   -21.114 -16.115 1.00 51.82 -1 59  GLU   D OE2  1 
ATOM   4057 N N    . ASN   D 2 60  ? -2.410  -17.214 -18.218 1.00 28.63 ?  60  ASN   D N    1 
ATOM   4058 C CA   . ASN   D 2 60  ? -3.128  -16.658 -17.075 1.00 34.47 ?  60  ASN   D CA   1 
ATOM   4059 C C    . ASN   D 2 60  ? -3.556  -15.207 -17.270 1.00 33.84 ?  60  ASN   D C    1 
ATOM   4060 O O    . ASN   D 2 60  ? -4.453  -14.731 -16.570 1.00 31.58 ?  60  ASN   D O    1 
ATOM   4061 C CB   . ASN   D 2 60  ? -2.279  -16.760 -15.797 1.00 42.80 ?  60  ASN   D CB   1 
ATOM   4062 C CG   . ASN   D 2 60  ? -2.046  -18.200 -15.349 1.00 48.41 ?  60  ASN   D CG   1 
ATOM   4063 O OD1  . ASN   D 2 60  ? -2.948  -19.038 -15.408 1.00 50.68 ?  60  ASN   D OD1  1 
ATOM   4064 N ND2  . ASN   D 2 60  ? -0.833  -18.483 -14.869 1.00 48.46 ?  60  ASN   D ND2  1 
ATOM   4065 N N    . ARG   D 2 61  ? -2.925  -14.483 -18.189 1.00 26.64 ?  61  ARG   D N    1 
ATOM   4066 C CA   . ARG   D 2 61  ? -3.306  -13.092 -18.410 1.00 25.57 ?  61  ARG   D CA   1 
ATOM   4067 C C    . ARG   D 2 61  ? -4.714  -12.998 -18.988 1.00 25.32 ?  61  ARG   D C    1 
ATOM   4068 O O    . ARG   D 2 61  ? -5.129  -13.833 -19.797 1.00 27.43 ?  61  ARG   D O    1 
ATOM   4069 C CB   . ARG   D 2 61  ? -2.315  -12.402 -19.350 1.00 25.28 ?  61  ARG   D CB   1 
ATOM   4070 C CG   . ARG   D 2 61  ? -0.854  -12.549 -18.962 1.00 33.88 ?  61  ARG   D CG   1 
ATOM   4071 C CD   . ARG   D 2 61  ? -0.043  -11.461 -19.645 1.00 29.23 ?  61  ARG   D CD   1 
ATOM   4072 N NE   . ARG   D 2 61  ? 1.346   -11.415 -19.195 1.00 39.70 ?  61  ARG   D NE   1 
ATOM   4073 C CZ   . ARG   D 2 61  ? 2.193   -10.444 -19.510 1.00 39.86 ?  61  ARG   D CZ   1 
ATOM   4074 N NH1  . ARG   D 2 61  ? 1.829   -9.436  -20.290 1.00 35.99 ?  61  ARG   D NH1  1 
ATOM   4075 N NH2  . ARG   D 2 61  ? 3.433   -10.483 -19.029 1.00 35.52 ?  61  ARG   D NH2  1 
ATOM   4076 N N    . ILE   D 2 62  ? -5.437  -11.962 -18.580 1.00 25.01 ?  62  ILE   D N    1 
ATOM   4077 C CA   . ILE   D 2 62  ? -6.793  -11.701 -19.049 1.00 26.33 ?  62  ILE   D CA   1 
ATOM   4078 C C    . ILE   D 2 62  ? -6.717  -10.695 -20.185 1.00 22.84 ?  62  ILE   D C    1 
ATOM   4079 O O    . ILE   D 2 62  ? -6.261  -9.562  -19.983 1.00 24.36 ?  62  ILE   D O    1 
ATOM   4080 C CB   . ILE   D 2 62  ? -7.692  -11.171 -17.919 1.00 27.26 ?  62  ILE   D CB   1 
ATOM   4081 C CG1  . ILE   D 2 62  ? -7.572  -12.042 -16.654 1.00 25.13 ?  62  ILE   D CG1  1 
ATOM   4082 C CG2  . ILE   D 2 62  ? -9.133  -11.064 -18.397 1.00 27.99 ?  62  ILE   D CG2  1 
ATOM   4083 C CD1  . ILE   D 2 62  ? -8.225  -13.404 -16.782 1.00 29.72 ?  62  ILE   D CD1  1 
ATOM   4084 N N    . TYR   D 2 63  ? -7.189  -11.082 -21.379 1.00 20.28 ?  63  TYR   D N    1 
ATOM   4085 C CA   . TYR   D 2 63  ? -7.198  -10.194 -22.536 1.00 23.45 ?  63  TYR   D CA   1 
ATOM   4086 C C    . TYR   D 2 63  ? -8.620  -9.730  -22.818 1.00 22.49 ?  63  TYR   D C    1 
ATOM   4087 O O    . TYR   D 2 63  ? -9.527  -10.557 -22.980 1.00 19.89 ?  63  TYR   D O    1 
ATOM   4088 C CB   . TYR   D 2 63  ? -6.599  -10.884 -23.766 1.00 18.73 ?  63  TYR   D CB   1 
ATOM   4089 C CG   . TYR   D 2 63  ? -5.150  -11.213 -23.551 1.00 19.77 ?  63  TYR   D CG   1 
ATOM   4090 C CD1  . TYR   D 2 63  ? -4.163  -10.258 -23.771 1.00 20.74 ?  63  TYR   D CD1  1 
ATOM   4091 C CD2  . TYR   D 2 63  ? -4.766  -12.453 -23.057 1.00 19.90 ?  63  TYR   D CD2  1 
ATOM   4092 C CE1  . TYR   D 2 63  ? -2.819  -10.552 -23.530 1.00 21.01 ?  63  TYR   D CE1  1 
ATOM   4093 C CE2  . TYR   D 2 63  ? -3.425  -12.756 -22.814 1.00 23.09 ?  63  TYR   D CE2  1 
ATOM   4094 C CZ   . TYR   D 2 63  ? -2.462  -11.799 -23.056 1.00 28.69 ?  63  TYR   D CZ   1 
ATOM   4095 O OH   . TYR   D 2 63  ? -1.138  -12.104 -22.817 1.00 22.93 ?  63  TYR   D OH   1 
ATOM   4096 N N    . SER   D 2 64  ? -8.801  -8.412  -22.880 1.00 21.57 ?  64  SER   D N    1 
ATOM   4097 C CA   . SER   D 2 64  ? -10.051 -7.786  -23.280 1.00 22.64 ?  64  SER   D CA   1 
ATOM   4098 C C    . SER   D 2 64  ? -9.980  -7.368  -24.744 1.00 20.65 ?  64  SER   D C    1 
ATOM   4099 O O    . SER   D 2 64  ? -8.949  -6.876  -25.208 1.00 24.73 ?  64  SER   D O    1 
ATOM   4100 C CB   . SER   D 2 64  ? -10.347 -6.556  -22.420 1.00 30.72 ?  64  SER   D CB   1 
ATOM   4101 O OG   . SER   D 2 64  ? -10.725 -6.936  -21.108 1.00 34.81 ?  64  SER   D OG   1 
ATOM   4102 N N    . LEU   D 2 65  ? -11.094 -7.540  -25.454 1.00 21.81 ?  65  LEU   D N    1 
ATOM   4103 C CA   . LEU   D 2 65  ? -11.174 -7.292  -26.889 1.00 23.02 ?  65  LEU   D CA   1 
ATOM   4104 C C    . LEU   D 2 65  ? -12.470 -6.570  -27.202 1.00 21.60 ?  65  LEU   D C    1 
ATOM   4105 O O    . LEU   D 2 65  ? -13.438 -6.636  -26.442 1.00 21.99 ?  65  LEU   D O    1 
ATOM   4106 C CB   . LEU   D 2 65  ? -11.150 -8.593  -27.717 1.00 23.97 ?  65  LEU   D CB   1 
ATOM   4107 C CG   . LEU   D 2 65  ? -9.965  -9.544  -27.590 1.00 19.91 ?  65  LEU   D CG   1 
ATOM   4108 C CD1  . LEU   D 2 65  ? -10.174 -10.526 -26.439 1.00 16.51 ?  65  LEU   D CD1  1 
ATOM   4109 C CD2  . LEU   D 2 65  ? -9.771  -10.293 -28.888 1.00 18.56 ?  65  LEU   D CD2  1 
ATOM   4110 N N    . LYS   D 2 66  ? -12.491 -5.924  -28.368 1.00 21.48 ?  66  LYS   D N    1 
ATOM   4111 C CA   . LYS   D 2 66  ? -13.678 -5.303  -28.938 1.00 23.71 ?  66  LYS   D CA   1 
ATOM   4112 C C    . LYS   D 2 66  ? -13.960 -5.962  -30.285 1.00 22.75 ?  66  LYS   D C    1 
ATOM   4113 O O    . LYS   D 2 66  ? -13.044 -6.118  -31.099 1.00 21.08 ?  66  LYS   D O    1 
ATOM   4114 C CB   . LYS   D 2 66  ? -13.447 -3.800  -29.116 1.00 29.94 ?  66  LYS   D CB   1 
ATOM   4115 C CG   . LYS   D 2 66  ? -13.470 -3.004  -27.818 1.00 31.90 ?  66  LYS   D CG   1 
ATOM   4116 C CD   . LYS   D 2 66  ? -14.298 -1.727  -27.956 1.00 44.31 ?  66  LYS   D CD   1 
ATOM   4117 C CE   . LYS   D 2 66  ? -14.359 -0.964  -26.636 1.00 46.49 ?  66  LYS   D CE   1 
ATOM   4118 N NZ   . LYS   D 2 66  ? -14.431 -1.886  -25.462 1.00 48.28 ?  66  LYS   D NZ   1 
ATOM   4119 N N    . VAL   D 2 67  ? -15.208 -6.377  -30.506 1.00 24.55 ?  67  VAL   D N    1 
ATOM   4120 C CA   . VAL   D 2 67  ? -15.621 -7.069  -31.729 1.00 17.40 ?  67  VAL   D CA   1 
ATOM   4121 C C    . VAL   D 2 67  ? -16.802 -6.315  -32.321 1.00 18.19 ?  67  VAL   D C    1 
ATOM   4122 O O    . VAL   D 2 67  ? -17.763 -6.002  -31.612 1.00 21.72 ?  67  VAL   D O    1 
ATOM   4123 C CB   . VAL   D 2 67  ? -16.013 -8.537  -31.448 1.00 18.18 ?  67  VAL   D CB   1 
ATOM   4124 C CG1  . VAL   D 2 67  ? -16.516 -9.231  -32.722 1.00 20.58 ?  67  VAL   D CG1  1 
ATOM   4125 C CG2  . VAL   D 2 67  ? -14.859 -9.294  -30.830 1.00 15.69 ?  67  VAL   D CG2  1 
ATOM   4126 N N    . GLU   D 2 68  ? -16.747 -6.037  -33.617 1.00 18.57 ?  68  GLU   D N    1 
ATOM   4127 C CA   . GLU   D 2 68  ? -17.795 -5.288  -34.299 1.00 19.35 ?  68  GLU   D CA   1 
ATOM   4128 C C    . GLU   D 2 68  ? -18.440 -6.169  -35.361 1.00 19.31 ?  68  GLU   D C    1 
ATOM   4129 O O    . GLU   D 2 68  ? -17.754 -6.677  -36.256 1.00 20.54 ?  68  GLU   D O    1 
ATOM   4130 C CB   . GLU   D 2 68  ? -17.241 -4.007  -34.932 1.00 27.55 ?  68  GLU   D CB   1 
ATOM   4131 C CG   . GLU   D 2 68  ? -16.835 -2.942  -33.925 1.00 33.09 ?  68  GLU   D CG   1 
ATOM   4132 C CD   . GLU   D 2 68  ? -17.416 -1.579  -34.251 1.00 36.82 ?  68  GLU   D CD   1 
ATOM   4133 O OE1  . GLU   D 2 68  ? -17.793 -1.358  -35.424 1.00 42.42 ?  68  GLU   D OE1  1 
ATOM   4134 O OE2  . GLU   D 2 68  ? -17.491 -0.732  -33.335 1.00 45.15 -1 68  GLU   D OE2  1 
ATOM   4135 N N    . CYS   D 2 69  ? -19.749 -6.342  -35.251 1.00 17.66 ?  69  CYS   D N    1 
ATOM   4136 C CA   . CYS   D 2 69  ? -20.548 -7.120  -36.202 1.00 17.26 ?  69  CYS   D CA   1 
ATOM   4137 C C    . CYS   D 2 69  ? -21.330 -6.112  -37.037 1.00 18.31 ?  69  CYS   D C    1 
ATOM   4138 O O    . CYS   D 2 69  ? -22.362 -5.596  -36.594 1.00 22.15 ?  69  CYS   D O    1 
ATOM   4139 C CB   . CYS   D 2 69  ? -21.463 -8.111  -35.483 1.00 15.75 ?  69  CYS   D CB   1 
ATOM   4140 S SG   . CYS   D 2 69  ? -20.539 -9.379  -34.508 1.00 18.69 ?  69  CYS   D SG   1 
ATOM   4141 N N    . GLY   D 2 70  ? -20.843 -5.859  -38.260 1.00 22.95 ?  70  GLY   D N    1 
ATOM   4142 C CA   . GLY   D 2 70  ? -21.423 -4.857  -39.115 1.00 26.64 ?  70  GLY   D CA   1 
ATOM   4143 C C    . GLY   D 2 70  ? -22.746 -5.286  -39.743 1.00 20.88 ?  70  GLY   D C    1 
ATOM   4144 O O    . GLY   D 2 70  ? -23.293 -6.371  -39.463 1.00 21.29 ?  70  GLY   D O    1 
ATOM   4145 N N    . PRO   D 2 71  ? -23.277 -4.419  -40.614 1.00 24.91 ?  71  PRO   D N    1 
ATOM   4146 C CA   . PRO   D 2 71  ? -24.624 -4.649  -41.175 1.00 28.48 ?  71  PRO   D CA   1 
ATOM   4147 C C    . PRO   D 2 71  ? -24.736 -5.895  -42.024 1.00 22.08 ?  71  PRO   D C    1 
ATOM   4148 O O    . PRO   D 2 71  ? -25.854 -6.381  -42.255 1.00 23.29 ?  71  PRO   D O    1 
ATOM   4149 C CB   . PRO   D 2 71  ? -24.874 -3.397  -42.034 1.00 33.00 ?  71  PRO   D CB   1 
ATOM   4150 C CG   . PRO   D 2 71  ? -23.825 -2.434  -41.665 1.00 32.44 ?  71  PRO   D CG   1 
ATOM   4151 C CD   . PRO   D 2 71  ? -22.665 -3.175  -41.103 1.00 27.27 ?  71  PRO   D CD   1 
ATOM   4152 N N    . LYS   D 2 72  ? -23.628 -6.404  -42.550 1.00 22.95 ?  72  LYS   D N    1 
ATOM   4153 C CA   . LYS   D 2 72  ? -23.683 -7.581  -43.394 1.00 18.57 ?  72  LYS   D CA   1 
ATOM   4154 C C    . LYS   D 2 72  ? -23.212 -8.837  -42.678 1.00 19.26 ?  72  LYS   D C    1 
ATOM   4155 O O    . LYS   D 2 72  ? -23.207 -9.911  -43.282 1.00 23.22 ?  72  LYS   D O    1 
ATOM   4156 C CB   . LYS   D 2 72  ? -22.860 -7.367  -44.672 1.00 22.78 ?  72  LYS   D CB   1 
ATOM   4157 C CG   . LYS   D 2 72  ? -23.405 -6.242  -45.552 1.00 27.59 ?  72  LYS   D CG   1 
ATOM   4158 C CD   . LYS   D 2 72  ? -24.849 -6.487  -45.899 1.00 28.79 ?  72  LYS   D CD   1 
ATOM   4159 C CE   . LYS   D 2 72  ? -25.454 -5.287  -46.617 1.00 35.26 ?  72  LYS   D CE   1 
ATOM   4160 N NZ   . LYS   D 2 72  ? -26.797 -5.603  -47.153 1.00 32.13 ?  72  LYS   D NZ   1 
ATOM   4161 N N    . TYR   D 2 73  ? -22.816 -8.727  -41.418 1.00 19.29 ?  73  TYR   D N    1 
ATOM   4162 C CA   . TYR   D 2 73  ? -22.576 -9.921  -40.624 1.00 19.72 ?  73  TYR   D CA   1 
ATOM   4163 C C    . TYR   D 2 73  ? -23.848 -10.768 -40.571 1.00 18.92 ?  73  TYR   D C    1 
ATOM   4164 O O    . TYR   D 2 73  ? -24.955 -10.226 -40.517 1.00 23.81 ?  73  TYR   D O    1 
ATOM   4165 C CB   . TYR   D 2 73  ? -22.145 -9.506  -39.221 1.00 17.91 ?  73  TYR   D CB   1 
ATOM   4166 C CG   . TYR   D 2 73  ? -21.835 -10.635 -38.270 1.00 18.18 ?  73  TYR   D CG   1 
ATOM   4167 C CD1  . TYR   D 2 73  ? -22.837 -11.215 -37.494 1.00 16.81 ?  73  TYR   D CD1  1 
ATOM   4168 C CD2  . TYR   D 2 73  ? -20.525 -11.079 -38.096 1.00 15.34 ?  73  TYR   D CD2  1 
ATOM   4169 C CE1  . TYR   D 2 73  ? -22.554 -12.227 -36.593 1.00 17.07 ?  73  TYR   D CE1  1 
ATOM   4170 C CE2  . TYR   D 2 73  ? -20.230 -12.091 -37.193 1.00 16.08 ?  73  TYR   D CE2  1 
ATOM   4171 C CZ   . TYR   D 2 73  ? -21.241 -12.656 -36.443 1.00 17.97 ?  73  TYR   D CZ   1 
ATOM   4172 O OH   . TYR   D 2 73  ? -20.921 -13.651 -35.546 1.00 16.03 ?  73  TYR   D OH   1 
ATOM   4173 N N    . PRO   D 2 74  ? -23.737 -12.110 -40.555 1.00 17.99 ?  74  PRO   D N    1 
ATOM   4174 C CA   . PRO   D 2 74  ? -22.531 -12.949 -40.594 1.00 19.06 ?  74  PRO   D CA   1 
ATOM   4175 C C    . PRO   D 2 74  ? -22.063 -13.254 -42.011 1.00 20.53 ?  74  PRO   D C    1 
ATOM   4176 O O    . PRO   D 2 74  ? -21.180 -14.095 -42.201 1.00 18.93 ?  74  PRO   D O    1 
ATOM   4177 C CB   . PRO   D 2 74  ? -22.989 -14.222 -39.868 1.00 16.50 ?  74  PRO   D CB   1 
ATOM   4178 C CG   . PRO   D 2 74  ? -24.460 -14.346 -40.255 1.00 20.03 ?  74  PRO   D CG   1 
ATOM   4179 C CD   . PRO   D 2 74  ? -24.962 -12.923 -40.376 1.00 21.13 ?  74  PRO   D CD   1 
ATOM   4180 N N    . GLU   D 2 75  ? -22.626 -12.620 -43.050 1.00 17.37 ?  75  GLU   D N    1 
ATOM   4181 C CA   . GLU   D 2 75  ? -22.068 -12.819 -44.387 1.00 24.37 ?  75  GLU   D CA   1 
ATOM   4182 C C    . GLU   D 2 75  ? -20.636 -12.304 -44.468 1.00 20.57 ?  75  GLU   D C    1 
ATOM   4183 O O    . GLU   D 2 75  ? -19.764 -12.942 -45.077 1.00 25.92 ?  75  GLU   D O    1 
ATOM   4184 C CB   . GLU   D 2 75  ? -22.944 -12.125 -45.431 1.00 24.22 ?  75  GLU   D CB   1 
ATOM   4185 C CG   . GLU   D 2 75  ? -24.268 -12.804 -45.653 1.00 27.33 ?  75  GLU   D CG   1 
ATOM   4186 C CD   . GLU   D 2 75  ? -24.132 -14.296 -45.747 1.00 30.94 ?  75  GLU   D CD   1 
ATOM   4187 O OE1  . GLU   D 2 75  ? -23.302 -14.764 -46.561 1.00 34.03 ?  75  GLU   D OE1  1 
ATOM   4188 O OE2  . GLU   D 2 75  ? -24.863 -14.999 -45.015 1.00 40.01 -1 75  GLU   D OE2  1 
ATOM   4189 N N    . ALA   D 2 76  ? -20.379 -11.147 -43.879 1.00 21.83 ?  76  ALA   D N    1 
ATOM   4190 C CA   . ALA   D 2 76  ? -19.079 -10.516 -43.761 1.00 24.24 ?  76  ALA   D CA   1 
ATOM   4191 C C    . ALA   D 2 76  ? -18.515 -10.790 -42.378 1.00 18.98 ?  76  ALA   D C    1 
ATOM   4192 O O    . ALA   D 2 76  ? -19.272 -10.851 -41.400 1.00 17.46 ?  76  ALA   D O    1 
ATOM   4193 C CB   . ALA   D 2 76  ? -19.177 -9.007  -43.972 1.00 23.30 ?  76  ALA   D CB   1 
ATOM   4194 N N    . PRO   D 2 77  ? -17.206 -10.979 -42.280 1.00 16.82 ?  77  PRO   D N    1 
ATOM   4195 C CA   . PRO   D 2 77  ? -16.593 -11.252 -40.981 1.00 17.29 ?  77  PRO   D CA   1 
ATOM   4196 C C    . PRO   D 2 77  ? -16.669 -10.037 -40.075 1.00 22.34 ?  77  PRO   D C    1 
ATOM   4197 O O    . PRO   D 2 77  ? -16.760 -8.887  -40.544 1.00 20.95 ?  77  PRO   D O    1 
ATOM   4198 C CB   . PRO   D 2 77  ? -15.132 -11.571 -41.334 1.00 18.02 ?  77  PRO   D CB   1 
ATOM   4199 C CG   . PRO   D 2 77  ? -14.893 -10.851 -42.612 1.00 18.74 ?  77  PRO   D CG   1 
ATOM   4200 C CD   . PRO   D 2 77  ? -16.209 -10.886 -43.364 1.00 22.18 ?  77  PRO   D CD   1 
ATOM   4201 N N    . PRO   D 2 78  ? -16.587 -10.246 -38.771 1.00 16.53 ?  78  PRO   D N    1 
ATOM   4202 C CA   . PRO   D 2 78  ? -16.536 -9.114  -37.844 1.00 16.03 ?  78  PRO   D CA   1 
ATOM   4203 C C    . PRO   D 2 78  ? -15.131 -8.540  -37.776 1.00 17.86 ?  78  PRO   D C    1 
ATOM   4204 O O    . PRO   D 2 78  ? -14.155 -9.183  -38.164 1.00 19.43 ?  78  PRO   D O    1 
ATOM   4205 C CB   . PRO   D 2 78  ? -16.951 -9.740  -36.507 1.00 16.02 ?  78  PRO   D CB   1 
ATOM   4206 C CG   . PRO   D 2 78  ? -16.456 -11.165 -36.604 1.00 18.26 ?  78  PRO   D CG   1 
ATOM   4207 C CD   . PRO   D 2 78  ? -16.537 -11.546 -38.079 1.00 16.75 ?  78  PRO   D CD   1 
ATOM   4208 N N    . SER   D 2 79  ? -15.060 -7.295  -37.300 1.00 17.48 ?  79  SER   D N    1 
ATOM   4209 C CA   . SER   D 2 79  ? -13.801 -6.628  -36.976 1.00 22.29 ?  79  SER   D CA   1 
ATOM   4210 C C    . SER   D 2 79  ? -13.409 -6.954  -35.542 1.00 20.26 ?  79  SER   D C    1 
ATOM   4211 O O    . SER   D 2 79  ? -14.278 -7.057  -34.680 1.00 22.58 ?  79  SER   D O    1 
ATOM   4212 C CB   . SER   D 2 79  ? -13.968 -5.116  -37.111 1.00 23.71 ?  79  SER   D CB   1 
ATOM   4213 O OG   . SER   D 2 79  ? -14.175 -4.761  -38.460 1.00 43.97 ?  79  SER   D OG   1 
ATOM   4214 N N    . VAL   D 2 80  ? -12.107 -7.111  -35.283 1.00 16.10 ?  80  VAL   D N    1 
ATOM   4215 C CA   . VAL   D 2 80  ? -11.624 -7.489  -33.952 1.00 13.81 ?  80  VAL   D CA   1 
ATOM   4216 C C    . VAL   D 2 80  ? -10.425 -6.632  -33.558 1.00 20.50 ?  80  VAL   D C    1 
ATOM   4217 O O    . VAL   D 2 80  ? -9.490  -6.447  -34.343 1.00 20.38 ?  80  VAL   D O    1 
ATOM   4218 C CB   . VAL   D 2 80  ? -11.243 -8.985  -33.886 1.00 20.69 ?  80  VAL   D CB   1 
ATOM   4219 C CG1  . VAL   D 2 80  ? -10.816 -9.365  -32.461 1.00 20.32 ?  80  VAL   D CG1  1 
ATOM   4220 C CG2  . VAL   D 2 80  ? -12.407 -9.848  -34.376 1.00 20.00 ?  80  VAL   D CG2  1 
ATOM   4221 N N    . ARG   D 2 81  ? -10.423 -6.164  -32.313 1.00 18.50 ?  81  ARG   D N    1 
ATOM   4222 C CA   . ARG   D 2 81  ? -9.327  -5.352  -31.793 1.00 24.21 ?  81  ARG   D CA   1 
ATOM   4223 C C    . ARG   D 2 81  ? -9.015  -5.772  -30.365 1.00 19.95 ?  81  ARG   D C    1 
ATOM   4224 O O    . ARG   D 2 81  ? -9.932  -5.916  -29.552 1.00 22.04 ?  81  ARG   D O    1 
ATOM   4225 C CB   . ARG   D 2 81  ? -9.707  -3.868  -31.844 1.00 22.94 ?  81  ARG   D CB   1 
ATOM   4226 C CG   . ARG   D 2 81  ? -8.677  -2.915  -31.306 1.00 32.78 ?  81  ARG   D CG   1 
ATOM   4227 C CD   . ARG   D 2 81  ? -9.058  -1.475  -31.663 1.00 34.60 ?  81  ARG   D CD   1 
ATOM   4228 N NE   . ARG   D 2 81  ? -10.397 -1.098  -31.211 1.00 38.07 ?  81  ARG   D NE   1 
ATOM   4229 C CZ   . ARG   D 2 81  ? -10.673 -0.547  -30.034 1.00 47.83 ?  81  ARG   D CZ   1 
ATOM   4230 N NH1  . ARG   D 2 81  ? -9.730  -0.340  -29.126 1.00 38.23 ?  81  ARG   D NH1  1 
ATOM   4231 N NH2  . ARG   D 2 81  ? -11.927 -0.193  -29.761 1.00 46.24 ?  81  ARG   D NH2  1 
ATOM   4232 N N    . PHE   D 2 82  ? -7.727  -5.976  -30.061 1.00 20.73 ?  82  PHE   D N    1 
ATOM   4233 C CA   . PHE   D 2 82  ? -7.298  -6.173  -28.675 1.00 22.40 ?  82  PHE   D CA   1 
ATOM   4234 C C    . PHE   D 2 82  ? -7.211  -4.827  -27.967 1.00 27.42 ?  82  PHE   D C    1 
ATOM   4235 O O    . PHE   D 2 82  ? -6.622  -3.885  -28.502 1.00 23.03 ?  82  PHE   D O    1 
ATOM   4236 C CB   . PHE   D 2 82  ? -5.936  -6.865  -28.611 1.00 19.64 ?  82  PHE   D CB   1 
ATOM   4237 C CG   . PHE   D 2 82  ? -6.001  -8.361  -28.686 1.00 20.57 ?  82  PHE   D CG   1 
ATOM   4238 C CD1  . PHE   D 2 82  ? -6.021  -9.000  -29.911 1.00 19.22 ?  82  PHE   D CD1  1 
ATOM   4239 C CD2  . PHE   D 2 82  ? -6.014  -9.130  -27.536 1.00 18.15 ?  82  PHE   D CD2  1 
ATOM   4240 C CE1  . PHE   D 2 82  ? -6.072  -10.372 -29.994 1.00 19.45 ?  82  PHE   D CE1  1 
ATOM   4241 C CE2  . PHE   D 2 82  ? -6.068  -10.511 -27.605 1.00 17.86 ?  82  PHE   D CE2  1 
ATOM   4242 C CZ   . PHE   D 2 82  ? -6.101  -11.137 -28.838 1.00 17.76 ?  82  PHE   D CZ   1 
ATOM   4243 N N    . VAL   D 2 83  ? -7.820  -4.730  -26.779 1.00 21.42 ?  83  VAL   D N    1 
ATOM   4244 C CA   . VAL   D 2 83  ? -7.578  -3.583  -25.905 1.00 28.54 ?  83  VAL   D CA   1 
ATOM   4245 C C    . VAL   D 2 83  ? -6.327  -3.820  -25.065 1.00 27.22 ?  83  VAL   D C    1 
ATOM   4246 O O    . VAL   D 2 83  ? -5.428  -2.970  -24.998 1.00 30.47 ?  83  VAL   D O    1 
ATOM   4247 C CB   . VAL   D 2 83  ? -8.815  -3.304  -25.027 1.00 26.98 ?  83  VAL   D CB   1 
ATOM   4248 C CG1  . VAL   D 2 83  ? -8.558  -2.117  -24.065 1.00 27.99 ?  83  VAL   D CG1  1 
ATOM   4249 C CG2  . VAL   D 2 83  ? -10.036 -3.052  -25.886 1.00 29.42 ?  83  VAL   D CG2  1 
ATOM   4250 N N    . THR   D 2 84  ? -6.231  -4.995  -24.444 1.00 26.01 ?  84  THR   D N    1 
ATOM   4251 C CA   . THR   D 2 84  ? -5.032  -5.401  -23.717 1.00 28.33 ?  84  THR   D CA   1 
ATOM   4252 C C    . THR   D 2 84  ? -3.848  -5.573  -24.671 1.00 34.32 ?  84  THR   D C    1 
ATOM   4253 O O    . THR   D 2 84  ? -3.964  -6.246  -25.700 1.00 24.96 ?  84  THR   D O    1 
ATOM   4254 C CB   . THR   D 2 84  ? -5.322  -6.710  -22.970 1.00 24.36 ?  84  THR   D CB   1 
ATOM   4255 O OG1  . THR   D 2 84  ? -6.562  -6.581  -22.262 1.00 25.54 ?  84  THR   D OG1  1 
ATOM   4256 C CG2  . THR   D 2 84  ? -4.180  -7.090  -22.015 1.00 21.62 ?  84  THR   D CG2  1 
ATOM   4257 N N    . LYS   D 2 85  ? -2.698  -4.972  -24.346 1.00 27.63 ?  85  LYS   D N    1 
ATOM   4258 C CA   . LYS   D 2 85  ? -1.559  -5.131  -25.240 1.00 27.80 ?  85  LYS   D CA   1 
ATOM   4259 C C    . LYS   D 2 85  ? -1.137  -6.590  -25.278 1.00 26.58 ?  85  LYS   D C    1 
ATOM   4260 O O    . LYS   D 2 85  ? -1.118  -7.289  -24.257 1.00 28.52 ?  85  LYS   D O    1 
ATOM   4261 C CB   . LYS   D 2 85  ? -0.373  -4.243  -24.836 1.00 30.40 ?  85  LYS   D CB   1 
ATOM   4262 C CG   . LYS   D 2 85  ? -0.711  -2.768  -24.803 1.00 34.80 ?  85  LYS   D CG   1 
ATOM   4263 C CD   . LYS   D 2 85  ? 0.459   -1.881  -24.364 1.00 38.68 ?  85  LYS   D CD   1 
ATOM   4264 C CE   . LYS   D 2 85  ? 1.241   -1.328  -25.563 1.00 34.39 ?  85  LYS   D CE   1 
ATOM   4265 N NZ   . LYS   D 2 85  ? 2.735   -1.541  -25.535 1.00 39.86 ?  85  LYS   D NZ   1 
ATOM   4266 N N    . ILE   D 2 86  ? -0.836  -7.060  -26.477 1.00 23.27 ?  86  ILE   D N    1 
ATOM   4267 C CA   . ILE   D 2 86  ? -0.435  -8.438  -26.682 1.00 19.67 ?  86  ILE   D CA   1 
ATOM   4268 C C    . ILE   D 2 86  ? 0.511   -8.467  -27.868 1.00 23.60 ?  86  ILE   D C    1 
ATOM   4269 O O    . ILE   D 2 86  ? 0.291   -7.787  -28.875 1.00 26.15 ?  86  ILE   D O    1 
ATOM   4270 C CB   . ILE   D 2 86  ? -1.651  -9.360  -26.921 1.00 25.10 ?  86  ILE   D CB   1 
ATOM   4271 C CG1  . ILE   D 2 86  ? -1.240  -10.832 -26.864 1.00 21.23 ?  86  ILE   D CG1  1 
ATOM   4272 C CG2  . ILE   D 2 86  ? -2.295  -9.045  -28.255 1.00 27.63 ?  86  ILE   D CG2  1 
ATOM   4273 C CD1  . ILE   D 2 86  ? -2.442  -11.801 -26.949 1.00 21.47 ?  86  ILE   D CD1  1 
ATOM   4274 N N    . ASN   D 2 87  ? 1.567   -9.232  -27.738 1.00 23.47 ?  87  ASN   D N    1 
ATOM   4275 C CA   . ASN   D 2 87  ? 2.481   -9.462  -28.846 1.00 22.86 ?  87  ASN   D CA   1 
ATOM   4276 C C    . ASN   D 2 87  ? 2.124   -10.810 -29.446 1.00 22.68 ?  87  ASN   D C    1 
ATOM   4277 O O    . ASN   D 2 87  ? 2.382   -11.858 -28.847 1.00 24.10 ?  87  ASN   D O    1 
ATOM   4278 C CB   . ASN   D 2 87  ? 3.938   -9.412  -28.392 1.00 23.02 ?  87  ASN   D CB   1 
ATOM   4279 C CG   . ASN   D 2 87  ? 4.375   -8.011  -28.035 1.00 21.70 ?  87  ASN   D CG   1 
ATOM   4280 O OD1  . ASN   D 2 87  ? 3.795   -7.037  -28.501 1.00 26.05 ?  87  ASN   D OD1  1 
ATOM   4281 N ND2  . ASN   D 2 87  ? 5.401   -7.903  -27.178 1.00 22.79 ?  87  ASN   D ND2  1 
ATOM   4282 N N    . MET   D 2 88  ? 1.526   -10.778 -30.629 1.00 23.07 ?  88  MET   D N    1 
ATOM   4283 C CA   . MET   D 2 88  ? 1.125   -12.017 -31.269 1.00 20.11 ?  88  MET   D CA   1 
ATOM   4284 C C    . MET   D 2 88  ? 0.995   -11.741 -32.762 1.00 15.52 ?  88  MET   D C    1 
ATOM   4285 O O    . MET   D 2 88  ? 0.585   -10.642 -33.153 1.00 19.08 ?  88  MET   D O    1 
ATOM   4286 C CB   . MET   D 2 88  ? -0.171  -12.541 -30.608 1.00 25.39 ?  88  MET   D CB   1 
ATOM   4287 C CG   . MET   D 2 88  ? -1.124  -13.324 -31.455 1.00 17.52 ?  88  MET   D CG   1 
ATOM   4288 S SD   . MET   D 2 88  ? -2.760  -13.538 -30.645 1.00 22.10 ?  88  MET   D SD   1 
ATOM   4289 C CE   . MET   D 2 88  ? -3.322  -14.986 -31.552 1.00 20.45 ?  88  MET   D CE   1 
ATOM   4290 N N    . ASN   D 2 89  ? 1.429   -12.706 -33.580 1.00 19.44 ?  89  ASN   D N    1 
ATOM   4291 C CA   . ASN   D 2 89  ? 1.319   -12.580 -35.028 1.00 20.63 ?  89  ASN   D CA   1 
ATOM   4292 C C    . ASN   D 2 89  ? -0.087  -12.164 -35.427 1.00 18.69 ?  89  ASN   D C    1 
ATOM   4293 O O    . ASN   D 2 89  ? -1.082  -12.736 -34.962 1.00 21.90 ?  89  ASN   D O    1 
ATOM   4294 C CB   . ASN   D 2 89  ? 1.711   -13.895 -35.711 1.00 22.79 ?  89  ASN   D CB   1 
ATOM   4295 C CG   . ASN   D 2 89  ? 3.207   -14.170 -35.654 1.00 39.68 ?  89  ASN   D CG   1 
ATOM   4296 O OD1  . ASN   D 2 89  ? 3.684   -14.977 -34.853 1.00 33.66 ?  89  ASN   D OD1  1 
ATOM   4297 N ND2  . ASN   D 2 89  ? 3.951   -13.545 -36.573 1.00 36.88 ?  89  ASN   D ND2  1 
ATOM   4298 N N    . GLY   D 2 90  ? -0.166  -11.137 -36.269 1.00 18.80 ?  90  GLY   D N    1 
ATOM   4299 C CA   . GLY   D 2 90  ? -1.430  -10.639 -36.770 1.00 20.18 ?  90  GLY   D CA   1 
ATOM   4300 C C    . GLY   D 2 90  ? -2.046  -9.521  -35.953 1.00 19.70 ?  90  GLY   D C    1 
ATOM   4301 O O    . GLY   D 2 90  ? -3.074  -8.978  -36.359 1.00 18.91 ?  90  GLY   D O    1 
ATOM   4302 N N    . ILE   D 2 91  ? -1.477  -9.170  -34.804 1.00 17.49 ?  91  ILE   D N    1 
ATOM   4303 C CA   . ILE   D 2 91  ? -2.033  -8.123  -33.954 1.00 17.67 ?  91  ILE   D CA   1 
ATOM   4304 C C    . ILE   D 2 91  ? -1.081  -6.932  -34.027 1.00 18.67 ?  91  ILE   D C    1 
ATOM   4305 O O    . ILE   D 2 91  ? 0.119   -7.068  -33.753 1.00 19.15 ?  91  ILE   D O    1 
ATOM   4306 C CB   . ILE   D 2 91  ? -2.238  -8.596  -32.503 1.00 21.37 ?  91  ILE   D CB   1 
ATOM   4307 C CG1  . ILE   D 2 91  ? -3.474  -9.512  -32.381 1.00 17.55 ?  91  ILE   D CG1  1 
ATOM   4308 C CG2  . ILE   D 2 91  ? -2.454  -7.402  -31.582 1.00 21.00 ?  91  ILE   D CG2  1 
ATOM   4309 C CD1  . ILE   D 2 91  ? -3.422  -10.813 -33.226 1.00 18.39 ?  91  ILE   D CD1  1 
ATOM   4310 N N    . ASN   D 2 92  ? -1.620  -5.777  -34.406 1.00 22.03 ?  92  ASN   D N    1 
ATOM   4311 C CA   . ASN   D 2 92  ? -0.787  -4.599  -34.618 1.00 23.81 ?  92  ASN   D CA   1 
ATOM   4312 C C    . ASN   D 2 92  ? -0.254  -4.120  -33.279 1.00 23.37 ?  92  ASN   D C    1 
ATOM   4313 O O    . ASN   D 2 92  ? -1.027  -3.944  -32.332 1.00 20.48 ?  92  ASN   D O    1 
ATOM   4314 C CB   . ASN   D 2 92  ? -1.602  -3.493  -35.288 1.00 21.32 ?  92  ASN   D CB   1 
ATOM   4315 C CG   . ASN   D 2 92  ? -0.779  -2.244  -35.538 1.00 26.90 ?  92  ASN   D CG   1 
ATOM   4316 O OD1  . ASN   D 2 92  ? -0.616  -1.408  -34.652 1.00 27.19 ?  92  ASN   D OD1  1 
ATOM   4317 N ND2  . ASN   D 2 92  ? -0.261  -2.113  -36.749 1.00 40.26 ?  92  ASN   D ND2  1 
ATOM   4318 N N    . ASN   D 2 93  ? 1.068   -3.901  -33.189 1.00 20.20 ?  93  ASN   D N    1 
ATOM   4319 C CA   . ASN   D 2 93  ? 1.637   -3.667  -31.871 1.00 23.87 ?  93  ASN   D CA   1 
ATOM   4320 C C    . ASN   D 2 93  ? 1.429   -2.243  -31.371 1.00 28.31 ?  93  ASN   D C    1 
ATOM   4321 O O    . ASN   D 2 93  ? 1.870   -1.926  -30.262 1.00 25.81 ?  93  ASN   D O    1 
ATOM   4322 C CB   . ASN   D 2 93  ? 3.127   -4.042  -31.840 1.00 20.51 ?  93  ASN   D CB   1 
ATOM   4323 C CG   . ASN   D 2 93  ? 3.984   -3.190  -32.737 1.00 28.64 ?  93  ASN   D CG   1 
ATOM   4324 O OD1  . ASN   D 2 93  ? 3.608   -2.085  -33.138 1.00 30.02 ?  93  ASN   D OD1  1 
ATOM   4325 N ND2  . ASN   D 2 93  ? 5.159   -3.716  -33.077 1.00 21.52 ?  93  ASN   D ND2  1 
ATOM   4326 N N    . SER   D 2 94  ? 0.751   -1.378  -32.125 1.00 23.43 ?  94  SER   D N    1 
ATOM   4327 C CA   . SER   D 2 94  ? 0.412   -0.073  -31.578 1.00 23.67 ?  94  SER   D CA   1 
ATOM   4328 C C    . SER   D 2 94  ? -1.083  0.200   -31.497 1.00 24.40 ?  94  SER   D C    1 
ATOM   4329 O O    . SER   D 2 94  ? -1.495  1.001   -30.650 1.00 23.37 ?  94  SER   D O    1 
ATOM   4330 C CB   . SER   D 2 94  ? 1.119   1.052   -32.365 1.00 27.34 ?  94  SER   D CB   1 
ATOM   4331 O OG   . SER   D 2 94  ? 0.533   1.310   -33.621 1.00 35.45 ?  94  SER   D OG   1 
ATOM   4332 N N    . SER   D 2 95  ? -1.913  -0.478  -32.294 1.00 25.37 ?  95  SER   D N    1 
ATOM   4333 C CA   . SER   D 2 95  ? -3.352  -0.253  -32.246 1.00 21.25 ?  95  SER   D CA   1 
ATOM   4334 C C    . SER   D 2 95  ? -4.139  -1.421  -31.674 1.00 24.84 ?  95  SER   D C    1 
ATOM   4335 O O    . SER   D 2 95  ? -5.319  -1.250  -31.340 1.00 20.66 ?  95  SER   D O    1 
ATOM   4336 C CB   . SER   D 2 95  ? -3.895  0.031   -33.652 1.00 23.61 ?  95  SER   D CB   1 
ATOM   4337 O OG   . SER   D 2 95  ? -3.958  -1.170  -34.406 1.00 24.10 ?  95  SER   D OG   1 
ATOM   4338 N N    . GLY   D 2 96  ? -3.527  -2.592  -31.578 1.00 23.16 ?  96  GLY   D N    1 
ATOM   4339 C CA   . GLY   D 2 96  ? -4.238  -3.787  -31.196 1.00 22.61 ?  96  GLY   D CA   1 
ATOM   4340 C C    . GLY   D 2 96  ? -5.171  -4.350  -32.246 1.00 22.99 ?  96  GLY   D C    1 
ATOM   4341 O O    . GLY   D 2 96  ? -5.805  -5.380  -31.980 1.00 20.18 ?  96  GLY   D O    1 
ATOM   4342 N N    . MET   D 2 97  ? -5.285  -3.730  -33.426 1.00 20.88 ?  97  MET   D N    1 
ATOM   4343 C CA   . MET   D 2 97  ? -6.195  -4.290  -34.425 1.00 23.68 ?  97  MET   D CA   1 
ATOM   4344 C C    . MET   D 2 97  ? -5.682  -5.597  -35.000 1.00 19.30 ?  97  MET   D C    1 
ATOM   4345 O O    . MET   D 2 97  ? -4.475  -5.794  -35.188 1.00 18.94 ?  97  MET   D O    1 
ATOM   4346 C CB   . MET   D 2 97  ? -6.506  -3.312  -35.560 1.00 24.07 ?  97  MET   D CB   1 
ATOM   4347 C CG   . MET   D 2 97  ? -6.860  -1.911  -35.120 1.00 30.17 ?  97  MET   D CG   1 
ATOM   4348 S SD   . MET   D 2 97  ? -6.942  -0.828  -36.553 1.00 38.35 ?  97  MET   D SD   1 
ATOM   4349 C CE   . MET   D 2 97  ? -8.705  -0.841  -36.882 1.00 47.05 ?  97  MET   D CE   1 
ATOM   4350 N N    . VAL   D 2 98  ? -6.627  -6.509  -35.243 1.00 19.49 ?  98  VAL   D N    1 
ATOM   4351 C CA   . VAL   D 2 98  ? -6.343  -7.840  -35.755 1.00 14.51 ?  98  VAL   D CA   1 
ATOM   4352 C C    . VAL   D 2 98  ? -6.419  -7.789  -37.275 1.00 18.02 ?  98  VAL   D C    1 
ATOM   4353 O O    . VAL   D 2 98  ? -7.450  -7.395  -37.835 1.00 20.19 ?  98  VAL   D O    1 
ATOM   4354 C CB   . VAL   D 2 98  ? -7.341  -8.870  -35.197 1.00 18.66 ?  98  VAL   D CB   1 
ATOM   4355 C CG1  . VAL   D 2 98  ? -7.176  -10.220 -35.893 1.00 18.98 ?  98  VAL   D CG1  1 
ATOM   4356 C CG2  . VAL   D 2 98  ? -7.184  -9.003  -33.681 1.00 20.77 ?  98  VAL   D CG2  1 
ATOM   4357 N N    . ASP   D 2 99  ? -5.337  -8.202  -37.928 1.00 18.23 ?  99  ASP   D N    1 
ATOM   4358 C CA   . ASP   D 2 99  ? -5.261  -8.275  -39.382 1.00 21.81 ?  99  ASP   D CA   1 
ATOM   4359 C C    . ASP   D 2 99  ? -5.960  -9.544  -39.847 1.00 17.15 ?  99  ASP   D C    1 
ATOM   4360 O O    . ASP   D 2 99  ? -5.456  -10.645 -39.627 1.00 18.58 ?  99  ASP   D O    1 
ATOM   4361 C CB   . ASP   D 2 99  ? -3.800  -8.257  -39.816 1.00 23.25 ?  99  ASP   D CB   1 
ATOM   4362 C CG   . ASP   D 2 99  ? -3.629  -8.455  -41.311 1.00 29.36 ?  99  ASP   D CG   1 
ATOM   4363 O OD1  . ASP   D 2 99  ? -4.623  -8.348  -42.060 1.00 25.54 -1 99  ASP   D OD1  1 
ATOM   4364 O OD2  . ASP   D 2 99  ? -2.489  -8.719  -41.737 1.00 33.23 ?  99  ASP   D OD2  1 
ATOM   4365 N N    . ALA   D 2 100 ? -7.113  -9.387  -40.517 1.00 18.50 ?  100 ALA   D N    1 
ATOM   4366 C CA   . ALA   D 2 100 ? -7.896  -10.550 -40.931 1.00 18.24 ?  100 ALA   D CA   1 
ATOM   4367 C C    . ALA   D 2 100 ? -7.084  -11.514 -41.785 1.00 19.41 ?  100 ALA   D C    1 
ATOM   4368 O O    . ALA   D 2 100 ? -7.252  -12.732 -41.673 1.00 18.84 ?  100 ALA   D O    1 
ATOM   4369 C CB   . ALA   D 2 100 ? -9.144  -10.100 -41.685 1.00 17.78 ?  100 ALA   D CB   1 
ATOM   4370 N N    . ARG   D 2 101 ? -6.198  -10.994 -42.652 1.00 19.95 ?  101 ARG   D N    1 
ATOM   4371 C CA   . ARG   D 2 101 ? -5.390  -11.873 -43.502 1.00 23.11 ?  101 ARG   D CA   1 
ATOM   4372 C C    . ARG   D 2 101 ? -4.556  -12.860 -42.693 1.00 21.45 ?  101 ARG   D C    1 
ATOM   4373 O O    . ARG   D 2 101 ? -4.243  -13.956 -43.175 1.00 20.94 ?  101 ARG   D O    1 
ATOM   4374 C CB   . ARG   D 2 101 ? -4.466  -11.040 -44.399 1.00 22.37 ?  101 ARG   D CB   1 
ATOM   4375 C CG   . ARG   D 2 101 ? -5.162  -10.000 -45.250 1.00 32.05 ?  101 ARG   D CG   1 
ATOM   4376 C CD   . ARG   D 2 101 ? -4.477  -9.902  -46.615 1.00 40.14 ?  101 ARG   D CD   1 
ATOM   4377 N NE   . ARG   D 2 101 ? -5.076  -8.887  -47.472 1.00 47.93 ?  101 ARG   D NE   1 
ATOM   4378 C CZ   . ARG   D 2 101 ? -5.950  -9.146  -48.434 1.00 48.60 ?  101 ARG   D CZ   1 
ATOM   4379 N NH1  . ARG   D 2 101 ? -6.407  -10.370 -48.637 1.00 40.45 ?  101 ARG   D NH1  1 
ATOM   4380 N NH2  . ARG   D 2 101 ? -6.377  -8.152  -49.212 1.00 48.46 ?  101 ARG   D NH2  1 
ATOM   4381 N N    . SER   D 2 102 ? -4.177  -12.487 -41.472 1.00 22.88 ?  102 SER   D N    1 
ATOM   4382 C CA   . SER   D 2 102 ? -3.288  -13.284 -40.642 1.00 19.56 ?  102 SER   D CA   1 
ATOM   4383 C C    . SER   D 2 102 ? -3.997  -14.337 -39.800 1.00 18.03 ?  102 SER   D C    1 
ATOM   4384 O O    . SER   D 2 102 ? -3.316  -15.203 -39.236 1.00 19.58 ?  102 SER   D O    1 
ATOM   4385 C CB   . SER   D 2 102 ? -2.478  -12.358 -39.726 1.00 22.73 ?  102 SER   D CB   1 
ATOM   4386 O OG   . SER   D 2 102 ? -1.564  -11.601 -40.500 1.00 29.92 ?  102 SER   D OG   1 
ATOM   4387 N N    . ILE   D 2 103 ? -5.333  -14.310 -39.725 1.00 18.37 ?  103 ILE   D N    1 
ATOM   4388 C CA   . ILE   D 2 103 ? -6.098  -15.217 -38.867 1.00 19.12 ?  103 ILE   D CA   1 
ATOM   4389 C C    . ILE   D 2 103 ? -6.993  -16.089 -39.741 1.00 15.14 ?  103 ILE   D C    1 
ATOM   4390 O O    . ILE   D 2 103 ? -7.949  -15.579 -40.341 1.00 18.31 ?  103 ILE   D O    1 
ATOM   4391 C CB   . ILE   D 2 103 ? -6.937  -14.443 -37.840 1.00 19.18 ?  103 ILE   D CB   1 
ATOM   4392 C CG1  . ILE   D 2 103 ? -6.096  -13.369 -37.127 1.00 21.33 ?  103 ILE   D CG1  1 
ATOM   4393 C CG2  . ILE   D 2 103 ? -7.624  -15.418 -36.867 1.00 18.99 ?  103 ILE   D CG2  1 
ATOM   4394 C CD1  . ILE   D 2 103 ? -4.955  -13.912 -36.278 1.00 19.67 ?  103 ILE   D CD1  1 
ATOM   4395 N N    . PRO   D 2 104 ? -6.722  -17.396 -39.850 1.00 21.06 ?  104 PRO   D N    1 
ATOM   4396 C CA   . PRO   D 2 104 ? -7.429  -18.211 -40.858 1.00 23.15 ?  104 PRO   D CA   1 
ATOM   4397 C C    . PRO   D 2 104 ? -8.949  -18.144 -40.773 1.00 18.56 ?  104 PRO   D C    1 
ATOM   4398 O O    . PRO   D 2 104 ? -9.624  -18.090 -41.806 1.00 17.87 ?  104 PRO   D O    1 
ATOM   4399 C CB   . PRO   D 2 104 ? -6.896  -19.621 -40.578 1.00 26.36 ?  104 PRO   D CB   1 
ATOM   4400 C CG   . PRO   D 2 104 ? -5.485  -19.375 -40.072 1.00 24.58 ?  104 PRO   D CG   1 
ATOM   4401 C CD   . PRO   D 2 104 ? -5.616  -18.140 -39.211 1.00 22.29 ?  104 PRO   D CD   1 
ATOM   4402 N N    . VAL   D 2 105 ? -9.518  -18.121 -39.569 1.00 17.95 ?  105 VAL   D N    1 
ATOM   4403 C CA   . VAL   D 2 105 ? -10.976 -18.068 -39.468 1.00 16.39 ?  105 VAL   D CA   1 
ATOM   4404 C C    . VAL   D 2 105 ? -11.533 -16.770 -40.051 1.00 16.84 ?  105 VAL   D C    1 
ATOM   4405 O O    . VAL   D 2 105 ? -12.671 -16.741 -40.534 1.00 18.04 ?  105 VAL   D O    1 
ATOM   4406 C CB   . VAL   D 2 105 ? -11.402 -18.286 -38.002 1.00 17.57 ?  105 VAL   D CB   1 
ATOM   4407 C CG1  . VAL   D 2 105 ? -11.050 -17.078 -37.160 1.00 23.23 ?  105 VAL   D CG1  1 
ATOM   4408 C CG2  . VAL   D 2 105 ? -12.886 -18.548 -37.922 1.00 25.70 ?  105 VAL   D CG2  1 
ATOM   4409 N N    . LEU   D 2 106 ? -10.762 -15.678 -40.009 1.00 19.44 ?  106 LEU   D N    1 
ATOM   4410 C CA   . LEU   D 2 106 ? -11.214 -14.417 -40.605 1.00 15.45 ?  106 LEU   D CA   1 
ATOM   4411 C C    . LEU   D 2 106 ? -10.856 -14.339 -42.083 1.00 15.00 ?  106 LEU   D C    1 
ATOM   4412 O O    . LEU   D 2 106 ? -11.687 -13.911 -42.893 1.00 17.26 ?  106 LEU   D O    1 
ATOM   4413 C CB   . LEU   D 2 106 ? -10.605 -13.220 -39.860 1.00 14.56 ?  106 LEU   D CB   1 
ATOM   4414 C CG   . LEU   D 2 106 ? -10.995 -13.032 -38.386 1.00 17.04 ?  106 LEU   D CG   1 
ATOM   4415 C CD1  . LEU   D 2 106 ? -10.169 -11.912 -37.720 1.00 17.27 ?  106 LEU   D CD1  1 
ATOM   4416 C CD2  . LEU   D 2 106 ? -12.475 -12.761 -38.232 1.00 17.69 ?  106 LEU   D CD2  1 
ATOM   4417 N N    . ALA   D 2 107 ? -9.641  -14.774 -42.439 1.00 15.76 ?  107 ALA   D N    1 
ATOM   4418 C CA   . ALA   D 2 107 ? -9.203  -14.761 -43.834 1.00 17.80 ?  107 ALA   D CA   1 
ATOM   4419 C C    . ALA   D 2 107 ? -10.099 -15.625 -44.712 1.00 22.67 ?  107 ALA   D C    1 
ATOM   4420 O O    . ALA   D 2 107 ? -10.360 -15.282 -45.870 1.00 23.50 ?  107 ALA   D O    1 
ATOM   4421 C CB   . ALA   D 2 107 ? -7.756  -15.244 -43.937 1.00 17.92 ?  107 ALA   D CB   1 
ATOM   4422 N N    . LYS   D 2 108 ? -10.542 -16.768 -44.192 1.00 16.86 ?  108 LYS   D N    1 
ATOM   4423 C CA   . LYS   D 2 108 ? -11.424 -17.686 -44.903 1.00 17.63 ?  108 LYS   D CA   1 
ATOM   4424 C C    . LYS   D 2 108 ? -12.786 -17.711 -44.214 1.00 18.63 ?  108 LYS   D C    1 
ATOM   4425 O O    . LYS   D 2 108 ? -13.343 -18.780 -43.968 1.00 18.26 ?  108 LYS   D O    1 
ATOM   4426 C CB   . LYS   D 2 108 ? -10.830 -19.091 -44.927 1.00 20.69 ?  108 LYS   D CB   1 
ATOM   4427 C CG   . LYS   D 2 108 ? -9.333  -19.130 -45.239 1.00 30.36 ?  108 LYS   D CG   1 
ATOM   4428 C CD   . LYS   D 2 108 ? -8.955  -20.247 -46.195 1.00 37.16 ?  108 LYS   D CD   1 
ATOM   4429 C CE   . LYS   D 2 108 ? -7.674  -19.908 -46.951 1.00 33.90 ?  108 LYS   D CE   1 
ATOM   4430 N NZ   . LYS   D 2 108 ? -7.959  -19.570 -48.368 1.00 41.28 ?  108 LYS   D NZ   1 
ATOM   4431 N N    . TRP   D 2 109 ? -13.323 -16.539 -43.897 1.00 18.92 ?  109 TRP   D N    1 
ATOM   4432 C CA   . TRP   D 2 109 ? -14.579 -16.475 -43.160 1.00 17.43 ?  109 TRP   D CA   1 
ATOM   4433 C C    . TRP   D 2 109 ? -15.715 -17.186 -43.901 1.00 18.68 ?  109 TRP   D C    1 
ATOM   4434 O O    . TRP   D 2 109 ? -15.838 -17.099 -45.129 1.00 23.38 ?  109 TRP   D O    1 
ATOM   4435 C CB   . TRP   D 2 109 ? -14.941 -15.005 -42.908 1.00 18.92 ?  109 TRP   D CB   1 
ATOM   4436 C CG   . TRP   D 2 109 ? -16.231 -14.807 -42.201 1.00 15.86 ?  109 TRP   D CG   1 
ATOM   4437 C CD1  . TRP   D 2 109 ? -17.457 -14.538 -42.775 1.00 16.31 ?  109 TRP   D CD1  1 
ATOM   4438 C CD2  . TRP   D 2 109 ? -16.453 -14.838 -40.782 1.00 15.69 ?  109 TRP   D CD2  1 
ATOM   4439 N NE1  . TRP   D 2 109 ? -18.413 -14.409 -41.797 1.00 19.05 ?  109 TRP   D NE1  1 
ATOM   4440 C CE2  . TRP   D 2 109 ? -17.825 -14.580 -40.566 1.00 18.60 ?  109 TRP   D CE2  1 
ATOM   4441 C CE3  . TRP   D 2 109 ? -15.623 -15.047 -39.671 1.00 16.44 ?  109 TRP   D CE3  1 
ATOM   4442 C CZ2  . TRP   D 2 109 ? -18.384 -14.550 -39.283 1.00 16.14 ?  109 TRP   D CZ2  1 
ATOM   4443 C CZ3  . TRP   D 2 109 ? -16.182 -15.005 -38.408 1.00 17.25 ?  109 TRP   D CZ3  1 
ATOM   4444 C CH2  . TRP   D 2 109 ? -17.547 -14.757 -38.223 1.00 17.97 ?  109 TRP   D CH2  1 
ATOM   4445 N N    . GLN   D 2 110 ? -16.549 -17.894 -43.140 1.00 16.99 ?  110 GLN   D N    1 
ATOM   4446 C CA   . GLN   D 2 110 ? -17.779 -18.500 -43.631 1.00 21.29 ?  110 GLN   D CA   1 
ATOM   4447 C C    . GLN   D 2 110 ? -18.941 -18.048 -42.757 1.00 19.71 ?  110 GLN   D C    1 
ATOM   4448 O O    . GLN   D 2 110 ? -18.769 -17.815 -41.564 1.00 17.92 ?  110 GLN   D O    1 
ATOM   4449 C CB   . GLN   D 2 110 ? -17.692 -20.018 -43.602 1.00 25.92 ?  110 GLN   D CB   1 
ATOM   4450 C CG   . GLN   D 2 110 ? -16.726 -20.598 -44.599 1.00 34.52 ?  110 GLN   D CG   1 
ATOM   4451 C CD   . GLN   D 2 110 ? -16.581 -22.088 -44.413 1.00 43.98 ?  110 GLN   D CD   1 
ATOM   4452 O OE1  . GLN   D 2 110 ? -15.597 -22.688 -44.841 1.00 39.49 ?  110 GLN   D OE1  1 
ATOM   4453 N NE2  . GLN   D 2 110 ? -17.571 -22.700 -43.766 1.00 44.66 ?  110 GLN   D NE2  1 
ATOM   4454 N N    . ASN   D 2 111 ? -20.147 -17.978 -43.331 1.00 22.71 ?  111 ASN   D N    1 
ATOM   4455 C CA   . ASN   D 2 111 ? -21.245 -17.376 -42.574 1.00 21.13 ?  111 ASN   D CA   1 
ATOM   4456 C C    . ASN   D 2 111 ? -21.754 -18.234 -41.405 1.00 21.93 ?  111 ASN   D C    1 
ATOM   4457 O O    . ASN   D 2 111 ? -22.572 -17.742 -40.616 1.00 21.67 ?  111 ASN   D O    1 
ATOM   4458 C CB   . ASN   D 2 111 ? -22.396 -17.016 -43.522 1.00 26.32 ?  111 ASN   D CB   1 
ATOM   4459 C CG   . ASN   D 2 111 ? -22.924 -18.206 -44.287 1.00 29.76 ?  111 ASN   D CG   1 
ATOM   4460 O OD1  . ASN   D 2 111 ? -22.967 -19.324 -43.775 1.00 30.14 ?  111 ASN   D OD1  1 
ATOM   4461 N ND2  . ASN   D 2 111 ? -23.347 -17.968 -45.532 1.00 35.40 ?  111 ASN   D ND2  1 
ATOM   4462 N N    . SER   D 2 112 ? -21.283 -19.472 -41.246 1.00 17.91 ?  112 SER   D N    1 
ATOM   4463 C CA   . SER   D 2 112 ? -21.594 -20.285 -40.077 1.00 16.83 ?  112 SER   D CA   1 
ATOM   4464 C C    . SER   D 2 112 ? -20.734 -19.942 -38.861 1.00 15.45 ?  112 SER   D C    1 
ATOM   4465 O O    . SER   D 2 112 ? -21.064 -20.369 -37.750 1.00 16.45 ?  112 SER   D O    1 
ATOM   4466 C CB   . SER   D 2 112 ? -21.409 -21.765 -40.412 1.00 20.11 ?  112 SER   D CB   1 
ATOM   4467 O OG   . SER   D 2 112 ? -20.139 -21.958 -41.017 1.00 31.07 ?  112 SER   D OG   1 
ATOM   4468 N N    . TYR   D 2 113 ? -19.654 -19.198 -39.050 1.00 15.27 ?  113 TYR   D N    1 
ATOM   4469 C CA   . TYR   D 2 113 ? -18.811 -18.803 -37.928 1.00 17.99 ?  113 TYR   D CA   1 
ATOM   4470 C C    . TYR   D 2 113 ? -19.516 -17.738 -37.071 1.00 17.56 ?  113 TYR   D C    1 
ATOM   4471 O O    . TYR   D 2 113 ? -20.557 -17.179 -37.438 1.00 18.07 ?  113 TYR   D O    1 
ATOM   4472 C CB   . TYR   D 2 113 ? -17.465 -18.272 -38.427 1.00 14.96 ?  113 TYR   D CB   1 
ATOM   4473 C CG   . TYR   D 2 113 ? -16.553 -19.274 -39.099 1.00 12.82 ?  113 TYR   D CG   1 
ATOM   4474 C CD1  . TYR   D 2 113 ? -16.643 -20.634 -38.827 1.00 14.68 ?  113 TYR   D CD1  1 
ATOM   4475 C CD2  . TYR   D 2 113 ? -15.566 -18.842 -39.981 1.00 17.40 ?  113 TYR   D CD2  1 
ATOM   4476 C CE1  . TYR   D 2 113 ? -15.786 -21.547 -39.451 1.00 18.45 ?  113 TYR   D CE1  1 
ATOM   4477 C CE2  . TYR   D 2 113 ? -14.707 -19.748 -40.606 1.00 19.75 ?  113 TYR   D CE2  1 
ATOM   4478 C CZ   . TYR   D 2 113 ? -14.827 -21.096 -40.328 1.00 22.36 ?  113 TYR   D CZ   1 
ATOM   4479 O OH   . TYR   D 2 113 ? -13.968 -21.972 -40.946 1.00 20.59 ?  113 TYR   D OH   1 
ATOM   4480 N N    . SER   D 2 114 ? -18.932 -17.464 -35.907 1.00 12.18 ?  114 SER   D N    1 
ATOM   4481 C CA   . SER   D 2 114 ? -19.572 -16.667 -34.865 1.00 14.31 ?  114 SER   D CA   1 
ATOM   4482 C C    . SER   D 2 114 ? -18.492 -15.993 -34.033 1.00 14.47 ?  114 SER   D C    1 
ATOM   4483 O O    . SER   D 2 114 ? -17.306 -16.258 -34.203 1.00 14.23 ?  114 SER   D O    1 
ATOM   4484 C CB   . SER   D 2 114 ? -20.433 -17.541 -33.958 1.00 16.33 ?  114 SER   D CB   1 
ATOM   4485 O OG   . SER   D 2 114 ? -19.579 -18.474 -33.294 1.00 16.56 ?  114 SER   D OG   1 
ATOM   4486 N N    . ILE   D 2 115 ? -18.913 -15.083 -33.152 1.00 14.85 ?  115 ILE   D N    1 
ATOM   4487 C CA   . ILE   D 2 115 ? -17.968 -14.441 -32.239 1.00 14.73 ?  115 ILE   D CA   1 
ATOM   4488 C C    . ILE   D 2 115 ? -17.194 -15.494 -31.447 1.00 12.97 ?  115 ILE   D C    1 
ATOM   4489 O O    . ILE   D 2 115 ? -15.964 -15.407 -31.308 1.00 13.08 ?  115 ILE   D O    1 
ATOM   4490 C CB   . ILE   D 2 115 ? -18.707 -13.465 -31.306 1.00 15.04 ?  115 ILE   D CB   1 
ATOM   4491 C CG1  . ILE   D 2 115 ? -19.383 -12.352 -32.125 1.00 14.79 ?  115 ILE   D CG1  1 
ATOM   4492 C CG2  . ILE   D 2 115 ? -17.717 -12.873 -30.269 1.00 15.44 ?  115 ILE   D CG2  1 
ATOM   4493 C CD1  . ILE   D 2 115 ? -20.466 -11.555 -31.341 1.00 15.74 ?  115 ILE   D CD1  1 
ATOM   4494 N N    . LYS   D 2 116 ? -17.920 -16.462 -30.865 1.00 14.41 ?  116 LYS   D N    1 
ATOM   4495 C CA   . LYS   D 2 116 ? -17.292 -17.556 -30.120 1.00 13.88 ?  116 LYS   D CA   1 
ATOM   4496 C C    . LYS   D 2 116 ? -16.176 -18.194 -30.923 1.00 12.47 ?  116 LYS   D C    1 
ATOM   4497 O O    . LYS   D 2 116 ? -15.066 -18.403 -30.419 1.00 15.10 ?  116 LYS   D O    1 
ATOM   4498 C CB   . LYS   D 2 116 ? -18.321 -18.636 -29.768 1.00 15.48 ?  116 LYS   D CB   1 
ATOM   4499 C CG   . LYS   D 2 116 ? -17.728 -19.762 -28.934 1.00 19.08 ?  116 LYS   D CG   1 
ATOM   4500 C CD   . LYS   D 2 116 ? -18.744 -20.865 -28.673 1.00 22.26 ?  116 LYS   D CD   1 
ATOM   4501 C CE   . LYS   D 2 116 ? -19.144 -21.545 -29.958 1.00 32.11 ?  116 LYS   D CE   1 
ATOM   4502 N NZ   . LYS   D 2 116 ? -20.481 -22.220 -29.836 1.00 43.48 ?  116 LYS   D NZ   1 
ATOM   4503 N N    . VAL   D 2 117 ? -16.469 -18.556 -32.173 1.00 13.85 ?  117 VAL   D N    1 
ATOM   4504 C CA   . VAL   D 2 117 ? -15.465 -19.221 -32.999 1.00 11.59 ?  117 VAL   D CA   1 
ATOM   4505 C C    . VAL   D 2 117 ? -14.228 -18.339 -33.176 1.00 13.15 ?  117 VAL   D C    1 
ATOM   4506 O O    . VAL   D 2 117 ? -13.093 -18.821 -33.087 1.00 14.47 ?  117 VAL   D O    1 
ATOM   4507 C CB   . VAL   D 2 117 ? -16.082 -19.616 -34.352 1.00 13.45 ?  117 VAL   D CB   1 
ATOM   4508 C CG1  . VAL   D 2 117 ? -14.986 -20.084 -35.323 1.00 15.21 ?  117 VAL   D CG1  1 
ATOM   4509 C CG2  . VAL   D 2 117 ? -17.100 -20.736 -34.152 1.00 16.93 ?  117 VAL   D CG2  1 
ATOM   4510 N N    . VAL   D 2 118 ? -14.424 -17.045 -33.451 1.00 11.46 ?  118 VAL   D N    1 
ATOM   4511 C CA   . VAL   D 2 118 ? -13.290 -16.130 -33.612 1.00 12.39 ?  118 VAL   D CA   1 
ATOM   4512 C C    . VAL   D 2 118 ? -12.437 -16.106 -32.349 1.00 12.40 ?  118 VAL   D C    1 
ATOM   4513 O O    . VAL   D 2 118 ? -11.200 -16.202 -32.402 1.00 13.79 ?  118 VAL   D O    1 
ATOM   4514 C CB   . VAL   D 2 118 ? -13.798 -14.722 -33.980 1.00 15.36 ?  118 VAL   D CB   1 
ATOM   4515 C CG1  . VAL   D 2 118 ? -12.675 -13.703 -33.895 1.00 16.88 ?  118 VAL   D CG1  1 
ATOM   4516 C CG2  . VAL   D 2 118 ? -14.423 -14.729 -35.374 1.00 12.87 ?  118 VAL   D CG2  1 
ATOM   4517 N N    . LEU   D 2 119 ? -13.088 -15.971 -31.185 1.00 11.89 ?  119 LEU   D N    1 
ATOM   4518 C CA   . LEU   D 2 119 ? -12.319 -15.872 -29.942 1.00 14.43 ?  119 LEU   D CA   1 
ATOM   4519 C C    . LEU   D 2 119 ? -11.585 -17.176 -29.644 1.00 15.20 ?  119 LEU   D C    1 
ATOM   4520 O O    . LEU   D 2 119 ? -10.423 -17.163 -29.196 1.00 15.97 ?  119 LEU   D O    1 
ATOM   4521 C CB   . LEU   D 2 119 ? -13.249 -15.503 -28.780 1.00 12.34 ?  119 LEU   D CB   1 
ATOM   4522 C CG   . LEU   D 2 119 ? -13.922 -14.125 -28.809 1.00 14.35 ?  119 LEU   D CG   1 
ATOM   4523 C CD1  . LEU   D 2 119 ? -14.849 -13.918 -27.568 1.00 17.00 ?  119 LEU   D CD1  1 
ATOM   4524 C CD2  . LEU   D 2 119 ? -12.879 -13.006 -28.905 1.00 19.25 ?  119 LEU   D CD2  1 
ATOM   4525 N N    . GLN   D 2 120 ? -12.236 -18.315 -29.900 1.00 13.08 ?  120 GLN   D N    1 
ATOM   4526 C CA   . GLN   D 2 120 ? -11.590 -19.608 -29.690 1.00 15.63 ?  120 GLN   D CA   1 
ATOM   4527 C C    . GLN   D 2 120 ? -10.412 -19.799 -30.635 1.00 17.21 ?  120 GLN   D C    1 
ATOM   4528 O O    . GLN   D 2 120 ? -9.383  -20.358 -30.243 1.00 16.56 ?  120 GLN   D O    1 
ATOM   4529 C CB   . GLN   D 2 120 ? -12.604 -20.728 -29.868 1.00 19.54 ?  120 GLN   D CB   1 
ATOM   4530 C CG   . GLN   D 2 120 ? -13.611 -20.748 -28.733 1.00 17.06 ?  120 GLN   D CG   1 
ATOM   4531 C CD   . GLN   D 2 120 ? -14.647 -21.856 -28.886 1.00 20.91 ?  120 GLN   D CD   1 
ATOM   4532 O OE1  . GLN   D 2 120 ? -15.084 -22.163 -29.990 1.00 25.56 ?  120 GLN   D OE1  1 
ATOM   4533 N NE2  . GLN   D 2 120 ? -15.027 -22.462 -27.776 1.00 35.93 ?  120 GLN   D NE2  1 
ATOM   4534 N N    . GLU   D 2 121 ? -10.542 -19.336 -31.879 1.00 14.41 ?  121 GLU   D N    1 
ATOM   4535 C CA   . GLU   D 2 121 ? -9.437  -19.426 -32.830 1.00 11.19 ?  121 GLU   D CA   1 
ATOM   4536 C C    . GLU   D 2 121 ? -8.248  -18.591 -32.375 1.00 16.07 ?  121 GLU   D C    1 
ATOM   4537 O O    . GLU   D 2 121 ? -7.101  -19.048 -32.445 1.00 17.31 ?  121 GLU   D O    1 
ATOM   4538 C CB   . GLU   D 2 121 ? -9.906  -18.963 -34.217 1.00 17.19 ?  121 GLU   D CB   1 
ATOM   4539 C CG   . GLU   D 2 121 ? -8.776  -18.732 -35.232 1.00 21.80 ?  121 GLU   D CG   1 
ATOM   4540 C CD   . GLU   D 2 121 ? -8.648  -19.864 -36.245 1.00 30.42 ?  121 GLU   D CD   1 
ATOM   4541 O OE1  . GLU   D 2 121 ? -9.046  -21.009 -35.917 1.00 28.62 ?  121 GLU   D OE1  1 
ATOM   4542 O OE2  . GLU   D 2 121 ? -8.123  -19.608 -37.359 1.00 23.49 -1 121 GLU   D OE2  1 
ATOM   4543 N N    . LEU   D 2 122 ? -8.498  -17.351 -31.928 1.00 13.33 ?  122 LEU   D N    1 
ATOM   4544 C CA   . LEU   D 2 122 ? -7.400  -16.520 -31.415 1.00 13.87 ?  122 LEU   D CA   1 
ATOM   4545 C C    . LEU   D 2 122 ? -6.726  -17.184 -30.218 1.00 16.60 ?  122 LEU   D C    1 
ATOM   4546 O O    . LEU   D 2 122 ? -5.488  -17.160 -30.091 1.00 15.93 ?  122 LEU   D O    1 
ATOM   4547 C CB   . LEU   D 2 122 ? -7.914  -15.127 -31.033 1.00 13.23 ?  122 LEU   D CB   1 
ATOM   4548 C CG   . LEU   D 2 122 ? -8.324  -14.211 -32.193 1.00 15.11 ?  122 LEU   D CG   1 
ATOM   4549 C CD1  . LEU   D 2 122 ? -9.048  -12.977 -31.671 1.00 14.98 ?  122 LEU   D CD1  1 
ATOM   4550 C CD2  . LEU   D 2 122 ? -7.071  -13.823 -33.001 1.00 15.29 ?  122 LEU   D CD2  1 
ATOM   4551 N N    . ARG   D 2 123 ? -7.521  -17.779 -29.323 1.00 16.64 ?  123 ARG   D N    1 
ATOM   4552 C CA   . ARG   D 2 123 ? -6.930  -18.491 -28.191 1.00 14.08 ?  123 ARG   D CA   1 
ATOM   4553 C C    . ARG   D 2 123 ? -6.090  -19.678 -28.657 1.00 16.90 ?  123 ARG   D C    1 
ATOM   4554 O O    . ARG   D 2 123 ? -5.007  -19.946 -28.111 1.00 19.25 ?  123 ARG   D O    1 
ATOM   4555 C CB   . ARG   D 2 123 ? -8.042  -18.960 -27.234 1.00 14.54 ?  123 ARG   D CB   1 
ATOM   4556 C CG   . ARG   D 2 123 ? -7.485  -19.380 -25.876 1.00 16.47 ?  123 ARG   D CG   1 
ATOM   4557 C CD   . ARG   D 2 123 ? -8.590  -19.659 -24.842 1.00 16.93 ?  123 ARG   D CD   1 
ATOM   4558 N NE   . ARG   D 2 123 ? -8.006  -19.702 -23.506 1.00 18.50 ?  123 ARG   D NE   1 
ATOM   4559 C CZ   . ARG   D 2 123 ? -7.613  -20.801 -22.878 1.00 17.10 ?  123 ARG   D CZ   1 
ATOM   4560 N NH1  . ARG   D 2 123 ? -7.842  -22.007 -23.379 1.00 19.88 ?  123 ARG   D NH1  1 
ATOM   4561 N NH2  . ARG   D 2 123 ? -6.974  -20.684 -21.708 1.00 17.75 ?  123 ARG   D NH2  1 
ATOM   4562 N N    . ARG   D 2 124 ? -6.564  -20.414 -29.660 1.00 14.87 ?  124 ARG   D N    1 
ATOM   4563 C CA   . ARG   D 2 124 ? -5.764  -21.525 -30.161 1.00 15.27 ?  124 ARG   D CA   1 
ATOM   4564 C C    . ARG   D 2 124 ? -4.475  -21.017 -30.782 1.00 18.31 ?  124 ARG   D C    1 
ATOM   4565 O O    . ARG   D 2 124 ? -3.433  -21.669 -30.685 1.00 18.43 ?  124 ARG   D O    1 
ATOM   4566 C CB   . ARG   D 2 124 ? -6.542  -22.350 -31.184 1.00 19.52 ?  124 ARG   D CB   1 
ATOM   4567 C CG   . ARG   D 2 124 ? -7.632  -23.203 -30.561 1.00 28.71 ?  124 ARG   D CG   1 
ATOM   4568 C CD   . ARG   D 2 124 ? -8.144  -24.226 -31.572 1.00 32.70 ?  124 ARG   D CD   1 
ATOM   4569 N NE   . ARG   D 2 124 ? -8.590  -23.594 -32.809 1.00 39.26 ?  124 ARG   D NE   1 
ATOM   4570 C CZ   . ARG   D 2 124 ? -9.808  -23.110 -33.034 1.00 39.61 ?  124 ARG   D CZ   1 
ATOM   4571 N NH1  . ARG   D 2 124 ? -10.770 -23.184 -32.117 1.00 33.17 ?  124 ARG   D NH1  1 
ATOM   4572 N NH2  . ARG   D 2 124 ? -10.071 -22.546 -34.212 1.00 27.81 ?  124 ARG   D NH2  1 
ATOM   4573 N N    . LEU   D 2 125 ? -4.534  -19.863 -31.440 1.00 17.28 ?  125 LEU   D N    1 
ATOM   4574 C CA   . LEU   D 2 125 ? -3.329  -19.330 -32.065 1.00 17.69 ?  125 LEU   D CA   1 
ATOM   4575 C C    . LEU   D 2 125 ? -2.306  -18.887 -31.023 1.00 18.46 ?  125 LEU   D C    1 
ATOM   4576 O O    . LEU   D 2 125 ? -1.096  -18.973 -31.284 1.00 20.84 ?  125 LEU   D O    1 
ATOM   4577 C CB   . LEU   D 2 125 ? -3.683  -18.181 -33.013 1.00 18.18 ?  125 LEU   D CB   1 
ATOM   4578 C CG   . LEU   D 2 125 ? -4.373  -18.609 -34.317 1.00 19.35 ?  125 LEU   D CG   1 
ATOM   4579 C CD1  . LEU   D 2 125 ? -5.006  -17.385 -34.990 1.00 20.16 ?  125 LEU   D CD1  1 
ATOM   4580 C CD2  . LEU   D 2 125 ? -3.413  -19.301 -35.286 1.00 25.99 ?  125 LEU   D CD2  1 
ATOM   4581 N N    . MET   D 2 126 ? -2.747  -18.391 -29.854 1.00 19.62 ?  126 MET   D N    1 
ATOM   4582 C CA   . MET   D 2 126 ? -1.716  -18.103 -28.836 1.00 19.01 ?  126 MET   D CA   1 
ATOM   4583 C C    . MET   D 2 126 ? -0.975  -19.336 -28.329 1.00 25.26 ?  126 MET   D C    1 
ATOM   4584 O O    . MET   D 2 126 ? 0.061   -19.205 -27.658 1.00 24.23 ?  126 MET   D O    1 
ATOM   4585 C CB   . MET   D 2 126 ? -2.219  -17.281 -27.640 1.00 22.17 ?  126 MET   D CB   1 
ATOM   4586 C CG   . MET   D 2 126 ? -3.299  -16.247 -27.830 1.00 16.75 ?  126 MET   D CG   1 
ATOM   4587 S SD   . MET   D 2 126 ? -4.262  -15.817 -26.356 1.00 21.26 ?  126 MET   D SD   1 
ATOM   4588 C CE   . MET   D 2 126 ? -5.059  -14.346 -26.981 1.00 17.82 ?  126 MET   D CE   1 
ATOM   4589 N N    . MET   D 2 127 ? -1.434  -20.501 -28.722 1.00 20.89 ?  127 MET   D N    1 
ATOM   4590 C CA   . MET   D 2 127 ? -0.977  -21.806 -28.322 1.00 22.91 ?  127 MET   D CA   1 
ATOM   4591 C C    . MET   D 2 127 ? 0.101   -22.288 -29.294 1.00 28.20 ?  127 MET   D C    1 
ATOM   4592 O O    . MET   D 2 127 ? 0.809   -23.259 -29.013 1.00 32.14 ?  127 MET   D O    1 
ATOM   4593 C CB   . MET   D 2 127 ? -2.270  -22.618 -28.345 1.00 31.76 ?  127 MET   D CB   1 
ATOM   4594 C CG   . MET   D 2 127 ? -2.978  -22.774 -27.034 1.00 30.30 ?  127 MET   D CG   1 
ATOM   4595 S SD   . MET   D 2 127 ? -4.143  -24.129 -27.107 1.00 30.70 ?  127 MET   D SD   1 
ATOM   4596 C CE   . MET   D 2 127 ? -5.371  -23.505 -25.987 1.00 28.96 ?  127 MET   D CE   1 
ATOM   4597 N N    . SER   D 2 128 ? 0.265   -21.578 -30.411 1.00 21.25 ?  128 SER   D N    1 
ATOM   4598 C CA   . SER   D 2 128 ? 1.089   -22.016 -31.530 1.00 22.43 ?  128 SER   D CA   1 
ATOM   4599 C C    . SER   D 2 128 ? 2.574   -21.762 -31.262 1.00 23.43 ?  128 SER   D C    1 
ATOM   4600 O O    . SER   D 2 128 ? 2.940   -20.849 -30.523 1.00 25.44 ?  128 SER   D O    1 
ATOM   4601 C CB   . SER   D 2 128 ? 0.657   -21.297 -32.808 1.00 27.71 ?  128 SER   D CB   1 
ATOM   4602 O OG   . SER   D 2 128 ? 1.416   -20.119 -33.024 1.00 30.58 ?  128 SER   D OG   1 
ATOM   4603 N N    . LYS   D 2 129 ? 3.424   -22.575 -31.905 1.00 32.94 ?  129 LYS   D N    1 
ATOM   4604 C CA   . LYS   D 2 129 ? 4.876   -22.445 -31.737 1.00 33.83 ?  129 LYS   D CA   1 
ATOM   4605 C C    . LYS   D 2 129 ? 5.356   -21.034 -32.050 1.00 36.82 ?  129 LYS   D C    1 
ATOM   4606 O O    . LYS   D 2 129 ? 6.312   -20.538 -31.439 1.00 34.80 ?  129 LYS   D O    1 
ATOM   4607 C CB   . LYS   D 2 129 ? 5.606   -23.445 -32.637 1.00 34.35 ?  129 LYS   D CB   1 
ATOM   4608 C CG   . LYS   D 2 129 ? 5.134   -24.886 -32.506 1.00 41.77 ?  129 LYS   D CG   1 
ATOM   4609 C CD   . LYS   D 2 129 ? 4.986   -25.561 -33.869 1.00 56.44 ?  129 LYS   D CD   1 
ATOM   4610 C CE   . LYS   D 2 129 ? 4.246   -26.899 -33.757 1.00 54.58 ?  129 LYS   D CE   1 
ATOM   4611 N NZ   . LYS   D 2 129 ? 5.158   -28.084 -33.699 1.00 46.08 ?  129 LYS   D NZ   1 
ATOM   4612 N N    . GLU   D 2 130 ? 4.716   -20.382 -33.017 1.00 31.81 ?  130 GLU   D N    1 
ATOM   4613 C CA   . GLU   D 2 130 ? 5.158   -19.060 -33.443 1.00 29.11 ?  130 GLU   D CA   1 
ATOM   4614 C C    . GLU   D 2 130 ? 4.828   -17.989 -32.413 1.00 30.71 ?  130 GLU   D C    1 
ATOM   4615 O O    . GLU   D 2 130 ? 5.558   -16.998 -32.292 1.00 26.91 ?  130 GLU   D O    1 
ATOM   4616 C CB   . GLU   D 2 130 ? 4.527   -18.726 -34.794 1.00 30.97 ?  130 GLU   D CB   1 
ATOM   4617 C CG   . GLU   D 2 130 ? 5.146   -19.511 -35.930 1.00 40.95 ?  130 GLU   D CG   1 
ATOM   4618 C CD   . GLU   D 2 130 ? 6.632   -19.222 -36.057 1.00 42.88 ?  130 GLU   D CD   1 
ATOM   4619 O OE1  . GLU   D 2 130 ? 7.421   -19.845 -35.314 1.00 49.02 ?  130 GLU   D OE1  1 
ATOM   4620 O OE2  . GLU   D 2 130 ? 7.008   -18.357 -36.876 1.00 46.48 -1 130 GLU   D OE2  1 
ATOM   4621 N N    . ASN   D 2 131 ? 3.738   -18.158 -31.662 1.00 22.60 ?  131 ASN   D N    1 
ATOM   4622 C CA   . ASN   D 2 131 ? 3.317   -17.137 -30.724 1.00 18.74 ?  131 ASN   D CA   1 
ATOM   4623 C C    . ASN   D 2 131 ? 3.708   -17.427 -29.282 1.00 24.37 ?  131 ASN   D C    1 
ATOM   4624 O O    . ASN   D 2 131 ? 3.929   -16.489 -28.516 1.00 22.17 ?  131 ASN   D O    1 
ATOM   4625 C CB   . ASN   D 2 131 ? 1.789   -16.965 -30.803 1.00 21.82 ?  131 ASN   D CB   1 
ATOM   4626 C CG   . ASN   D 2 131 ? 1.332   -16.268 -32.082 1.00 27.32 ?  131 ASN   D CG   1 
ATOM   4627 O OD1  . ASN   D 2 131 ? 1.929   -15.288 -32.518 1.00 22.68 ?  131 ASN   D OD1  1 
ATOM   4628 N ND2  . ASN   D 2 131 ? 0.248   -16.775 -32.683 1.00 20.99 ?  131 ASN   D ND2  1 
ATOM   4629 N N    . MET   D 2 132 ? 3.805   -18.696 -28.890 1.00 22.66 ?  132 MET   D N    1 
ATOM   4630 C CA   . MET   D 2 132 ? 3.799   -19.041 -27.469 1.00 25.01 ?  132 MET   D CA   1 
ATOM   4631 C C    . MET   D 2 132 ? 5.028   -18.533 -26.721 1.00 29.88 ?  132 MET   D C    1 
ATOM   4632 O O    . MET   D 2 132 ? 4.966   -18.364 -25.498 1.00 29.69 ?  132 MET   D O    1 
ATOM   4633 C CB   . MET   D 2 132 ? 3.641   -20.558 -27.327 1.00 30.50 ?  132 MET   D CB   1 
ATOM   4634 C CG   . MET   D 2 132 ? 4.833   -21.372 -27.841 1.00 34.96 ?  132 MET   D CG   1 
ATOM   4635 S SD   . MET   D 2 132 ? 4.518   -23.149 -27.848 1.00 41.54 ?  132 MET   D SD   1 
ATOM   4636 C CE   . MET   D 2 132 ? 4.752   -23.492 -26.101 1.00 42.40 ?  132 MET   D CE   1 
ATOM   4637 N N    . LYS   D 2 133 ? 6.128   -18.263 -27.422 1.00 31.79 ?  133 LYS   D N    1 
ATOM   4638 C CA   . LYS   D 2 133 ? 7.347   -17.775 -26.791 1.00 33.40 ?  133 LYS   D CA   1 
ATOM   4639 C C    . LYS   D 2 133 ? 7.645   -16.312 -27.107 1.00 36.32 ?  133 LYS   D C    1 
ATOM   4640 O O    . LYS   D 2 133 ? 8.699   -15.805 -26.702 1.00 37.89 ?  133 LYS   D O    1 
ATOM   4641 C CB   . LYS   D 2 133 ? 8.522   -18.663 -27.211 1.00 33.17 ?  133 LYS   D CB   1 
ATOM   4642 C CG   . LYS   D 2 133 ? 8.702   -19.875 -26.309 1.00 36.30 ?  133 LYS   D CG   1 
ATOM   4643 C CD   . LYS   D 2 133 ? 8.954   -21.120 -27.138 1.00 47.06 ?  133 LYS   D CD   1 
ATOM   4644 C CE   . LYS   D 2 133 ? 8.911   -22.386 -26.297 1.00 50.64 ?  133 LYS   D CE   1 
ATOM   4645 N NZ   . LYS   D 2 133 ? 10.225  -23.088 -26.381 1.00 43.20 ?  133 LYS   D NZ   1 
ATOM   4646 N N    . LEU   D 2 134 ? 6.754   -15.623 -27.813 1.00 30.27 ?  134 LEU   D N    1 
ATOM   4647 C CA   . LEU   D 2 134 ? 6.948   -14.204 -28.095 1.00 26.93 ?  134 LEU   D CA   1 
ATOM   4648 C C    . LEU   D 2 134 ? 7.084   -13.423 -26.790 1.00 36.95 ?  134 LEU   D C    1 
ATOM   4649 O O    . LEU   D 2 134 ? 6.231   -13.560 -25.899 1.00 29.57 ?  134 LEU   D O    1 
ATOM   4650 C CB   . LEU   D 2 134 ? 5.770   -13.642 -28.897 1.00 25.20 ?  134 LEU   D CB   1 
ATOM   4651 C CG   . LEU   D 2 134 ? 5.681   -13.923 -30.398 1.00 25.73 ?  134 LEU   D CG   1 
ATOM   4652 C CD1  . LEU   D 2 134 ? 4.437   -13.271 -30.982 1.00 24.17 ?  134 LEU   D CD1  1 
ATOM   4653 C CD2  . LEU   D 2 134 ? 6.951   -13.455 -31.119 1.00 29.17 ?  134 LEU   D CD2  1 
ATOM   4654 N N    . PRO   D 2 135 ? 8.107   -12.578 -26.647 1.00 27.54 ?  135 PRO   D N    1 
ATOM   4655 C CA   . PRO   D 2 135 ? 8.188   -11.727 -25.456 1.00 28.73 ?  135 PRO   D CA   1 
ATOM   4656 C C    . PRO   D 2 135 ? 6.926   -10.902 -25.326 1.00 28.19 ?  135 PRO   D C    1 
ATOM   4657 O O    . PRO   D 2 135 ? 6.385   -10.402 -26.316 1.00 27.81 ?  135 PRO   D O    1 
ATOM   4658 C CB   . PRO   D 2 135 ? 9.409   -10.829 -25.723 1.00 29.39 ?  135 PRO   D CB   1 
ATOM   4659 C CG   . PRO   D 2 135 ? 10.069  -11.375 -26.912 1.00 30.11 ?  135 PRO   D CG   1 
ATOM   4660 C CD   . PRO   D 2 135 ? 9.078   -12.180 -27.679 1.00 23.71 ?  135 PRO   D CD   1 
ATOM   4661 N N    . GLN   D 2 136 ? 6.449   -10.763 -24.080 1.00 26.42 ?  136 GLN   D N    1 
ATOM   4662 C CA   . GLN   D 2 136 ? 5.228   -10.005 -23.888 1.00 23.89 ?  136 GLN   D CA   1 
ATOM   4663 C C    . GLN   D 2 136 ? 5.495   -8.707  -23.150 1.00 25.96 ?  136 GLN   D C    1 
ATOM   4664 O O    . GLN   D 2 136 ? 6.459   -8.597  -22.382 1.00 29.90 ?  136 GLN   D O    1 
ATOM   4665 C CB   . GLN   D 2 136 ? 4.183   -10.815 -23.102 1.00 25.30 ?  136 GLN   D CB   1 
ATOM   4666 C CG   . GLN   D 2 136 ? 3.669   -12.034 -23.859 1.00 24.36 ?  136 GLN   D CG   1 
ATOM   4667 C CD   . GLN   D 2 136 ? 3.126   -11.662 -25.221 1.00 17.13 ?  136 GLN   D CD   1 
ATOM   4668 O OE1  . GLN   D 2 136 ? 2.252   -10.807 -25.329 1.00 22.84 ?  136 GLN   D OE1  1 
ATOM   4669 N NE2  . GLN   D 2 136 ? 3.642   -12.305 -26.263 1.00 23.54 ?  136 GLN   D NE2  1 
ATOM   4670 N N    . PRO   D 2 137 ? 4.654   -7.706  -23.353 1.00 22.86 ?  137 PRO   D N    1 
ATOM   4671 C CA   . PRO   D 2 137 ? 4.783   -6.462  -22.589 1.00 29.43 ?  137 PRO   D CA   1 
ATOM   4672 C C    . PRO   D 2 137 ? 4.526   -6.691  -21.111 1.00 38.45 ?  137 PRO   D C    1 
ATOM   4673 O O    . PRO   D 2 137 ? 4.013   -7.749  -20.715 1.00 31.87 ?  137 PRO   D O    1 
ATOM   4674 C CB   . PRO   D 2 137 ? 3.714   -5.549  -23.208 1.00 28.36 ?  137 PRO   D CB   1 
ATOM   4675 C CG   . PRO   D 2 137 ? 2.878   -6.407  -24.084 1.00 25.71 ?  137 PRO   D CG   1 
ATOM   4676 C CD   . PRO   D 2 137 ? 3.634   -7.628  -24.416 1.00 28.51 ?  137 PRO   D CD   1 
ATOM   4677 N N    . PRO   D 2 138 ? 4.886   -5.734  -20.260 1.00 36.68 ?  138 PRO   D N    1 
ATOM   4678 C CA   . PRO   D 2 138 ? 4.502   -5.819  -18.851 1.00 35.32 ?  138 PRO   D CA   1 
ATOM   4679 C C    . PRO   D 2 138 ? 2.996   -6.039  -18.722 1.00 31.13 ?  138 PRO   D C    1 
ATOM   4680 O O    . PRO   D 2 138 ? 2.191   -5.410  -19.414 1.00 39.18 ?  138 PRO   D O    1 
ATOM   4681 C CB   . PRO   D 2 138 ? 4.933   -4.458  -18.305 1.00 38.21 ?  138 PRO   D CB   1 
ATOM   4682 C CG   . PRO   D 2 138 ? 6.183   -4.126  -19.071 1.00 34.15 ?  138 PRO   D CG   1 
ATOM   4683 C CD   . PRO   D 2 138 ? 6.018   -4.809  -20.454 1.00 35.13 ?  138 PRO   D CD   1 
ATOM   4684 N N    . GLU   D 2 139 ? 2.620   -6.949  -17.826 1.00 36.74 ?  139 GLU   D N    1 
ATOM   4685 C CA   . GLU   D 2 139 ? 1.212   -7.278  -17.632 1.00 30.85 ?  139 GLU   D CA   1 
ATOM   4686 C C    . GLU   D 2 139 ? 0.383   -6.024  -17.371 1.00 37.61 ?  139 GLU   D C    1 
ATOM   4687 O O    . GLU   D 2 139 ? 0.841   -5.067  -16.739 1.00 45.14 ?  139 GLU   D O    1 
ATOM   4688 C CB   . GLU   D 2 139 ? 1.053   -8.258  -16.464 1.00 39.02 ?  139 GLU   D CB   1 
ATOM   4689 C CG   . GLU   D 2 139 ? -0.377  -8.748  -16.226 1.00 43.27 ?  139 GLU   D CG   1 
ATOM   4690 C CD   . GLU   D 2 139 ? -0.425  -10.020 -15.391 1.00 45.34 ?  139 GLU   D CD   1 
ATOM   4691 O OE1  . GLU   D 2 139 ? 0.617   -10.398 -14.811 1.00 45.80 ?  139 GLU   D OE1  1 
ATOM   4692 O OE2  . GLU   D 2 139 ? -1.504  -10.646 -15.319 1.00 47.34 -1 139 GLU   D OE2  1 
ATOM   4693 N N    . GLY   D 2 140 ? -0.855  -6.031  -17.873 1.00 33.17 ?  140 GLY   D N    1 
ATOM   4694 C CA   . GLY   D 2 140 ? -1.796  -4.957  -17.650 1.00 38.62 ?  140 GLY   D CA   1 
ATOM   4695 C C    . GLY   D 2 140 ? -1.778  -3.838  -18.675 1.00 32.99 ?  140 GLY   D C    1 
ATOM   4696 O O    . GLY   D 2 140 ? -2.752  -3.086  -18.761 1.00 35.39 ?  140 GLY   D O    1 
ATOM   4697 N N    . GLN   D 2 141 ? -0.706  -3.696  -19.452 1.00 42.83 ?  141 GLN   D N    1 
ATOM   4698 C CA   . GLN   D 2 141 ? -0.628  -2.587  -20.394 1.00 35.60 ?  141 GLN   D CA   1 
ATOM   4699 C C    . GLN   D 2 141 ? -1.755  -2.681  -21.424 1.00 43.98 ?  141 GLN   D C    1 
ATOM   4700 O O    . GLN   D 2 141 ? -2.281  -3.759  -21.722 1.00 36.65 ?  141 GLN   D O    1 
ATOM   4701 C CB   . GLN   D 2 141 ? 0.736   -2.564  -21.099 1.00 38.17 ?  141 GLN   D CB   1 
ATOM   4702 C CG   . GLN   D 2 141 ? 1.873   -1.986  -20.254 1.00 33.07 ?  141 GLN   D CG   1 
ATOM   4703 C CD   . GLN   D 2 141 ? 3.182   -1.844  -21.025 1.00 48.01 ?  141 GLN   D CD   1 
ATOM   4704 O OE1  . GLN   D 2 141 ? 3.351   -2.418  -22.100 1.00 41.21 ?  141 GLN   D OE1  1 
ATOM   4705 N NE2  . GLN   D 2 141 ? 4.118   -1.080  -20.469 1.00 53.86 ?  141 GLN   D NE2  1 
ATOM   4706 N N    . THR   D 2 142 ? -2.126  -1.524  -21.965 1.00 43.76 ?  142 THR   D N    1 
ATOM   4707 C CA   . THR   D 2 142 ? -3.126  -1.427  -23.018 1.00 42.41 ?  142 THR   D CA   1 
ATOM   4708 C C    . THR   D 2 142 ? -2.624  -0.462  -24.083 1.00 43.63 ?  142 THR   D C    1 
ATOM   4709 O O    . THR   D 2 142 ? -1.627  0.242   -23.893 1.00 40.57 ?  142 THR   D O    1 
ATOM   4710 C CB   . THR   D 2 142 ? -4.476  -0.954  -22.474 1.00 36.91 ?  142 THR   D CB   1 
ATOM   4711 O OG1  . THR   D 2 142 ? -4.341  0.387   -21.989 1.00 42.55 ?  142 THR   D OG1  1 
ATOM   4712 C CG2  . THR   D 2 142 ? -4.921  -1.853  -21.343 1.00 38.95 ?  142 THR   D CG2  1 
ATOM   4713 N N    . TYR   D 2 143 ? -3.326  -0.435  -25.215 1.00 39.49 ?  143 TYR   D N    1 
ATOM   4714 C CA   . TYR   D 2 143 ? -3.009  0.482   -26.302 1.00 44.27 ?  143 TYR   D CA   1 
ATOM   4715 C C    . TYR   D 2 143 ? -3.726  1.811   -26.096 1.00 48.05 ?  143 TYR   D C    1 
ATOM   4716 O O    . TYR   D 2 143 ? -4.784  1.877   -25.463 1.00 47.28 ?  143 TYR   D O    1 
ATOM   4717 C CB   . TYR   D 2 143 ? -3.397  -0.116  -27.663 1.00 34.37 ?  143 TYR   D CB   1 
ATOM   4718 C CG   . TYR   D 2 143 ? -2.791  -1.478  -27.935 1.00 33.20 ?  143 TYR   D CG   1 
ATOM   4719 C CD1  . TYR   D 2 143 ? -1.492  -1.592  -28.413 1.00 29.36 ?  143 TYR   D CD1  1 
ATOM   4720 C CD2  . TYR   D 2 143 ? -3.530  -2.652  -27.748 1.00 28.31 ?  143 TYR   D CD2  1 
ATOM   4721 C CE1  . TYR   D 2 143 ? -0.927  -2.817  -28.659 1.00 29.84 ?  143 TYR   D CE1  1 
ATOM   4722 C CE2  . TYR   D 2 143 ? -2.970  -3.884  -28.000 1.00 23.60 ?  143 TYR   D CE2  1 
ATOM   4723 C CZ   . TYR   D 2 143 ? -1.667  -3.966  -28.447 1.00 23.50 ?  143 TYR   D CZ   1 
ATOM   4724 O OH   . TYR   D 2 143 ? -1.080  -5.175  -28.713 1.00 28.44 ?  143 TYR   D OH   1 
ATOM   4725 N N    . ASN   D 2 144 ? -3.141  2.872   -26.647 1.00 48.63 ?  144 ASN   D N    1 
ATOM   4726 C CA   . ASN   D 2 144 ? -3.748  4.203   -26.576 1.00 60.73 ?  144 ASN   D CA   1 
ATOM   4727 C C    . ASN   D 2 144 ? -5.219  4.187   -26.996 1.00 55.61 ?  144 ASN   D C    1 
ATOM   4728 O O    . ASN   D 2 144 ? -5.672  5.035   -27.766 1.00 60.54 ?  144 ASN   D O    1 
ATOM   4729 C CB   . ASN   D 2 144 ? -2.965  5.192   -27.444 1.00 61.44 ?  144 ASN   D CB   1 
ATOM   4730 C CG   . ASN   D 2 144 ? -1.501  5.282   -27.047 1.00 60.55 ?  144 ASN   D CG   1 
ATOM   4731 O OD1  . ASN   D 2 144 ? -1.149  5.056   -25.889 1.00 70.20 ?  144 ASN   D OD1  1 
ATOM   4732 N ND2  . ASN   D 2 144 ? -0.642  5.615   -28.004 1.00 57.84 ?  144 ASN   D ND2  1 
HETATM 4733 O O    . HOH   E 3 .   ? 11.810  -9.469  -19.042 1.00 43.13 ?  201 HOH   A O    1 
HETATM 4734 O O    . HOH   E 3 .   ? 9.588   3.918   -36.820 1.00 27.69 ?  202 HOH   A O    1 
HETATM 4735 O O    . HOH   E 3 .   ? 3.463   -3.077  -28.050 1.00 32.08 ?  203 HOH   A O    1 
HETATM 4736 O O    . HOH   E 3 .   ? 17.750  -27.394 -29.950 1.00 40.04 ?  204 HOH   A O    1 
HETATM 4737 O O    . HOH   E 3 .   ? 7.478   -6.679  -25.539 1.00 34.00 ?  205 HOH   A O    1 
HETATM 4738 O O    . HOH   E 3 .   ? 11.803  7.842   -30.703 1.00 26.17 ?  206 HOH   A O    1 
HETATM 4739 O O    . HOH   E 3 .   ? 6.698   1.017   -25.844 1.00 36.66 ?  207 HOH   A O    1 
HETATM 4740 O O    . HOH   E 3 .   ? 8.870   -2.354  -36.697 1.00 21.74 ?  208 HOH   A O    1 
HETATM 4741 O O    . HOH   E 3 .   ? 23.372  -25.996 -40.339 1.00 32.22 ?  209 HOH   A O    1 
HETATM 4742 O O    . HOH   E 3 .   ? 7.212   -1.362  -21.754 1.00 33.20 ?  210 HOH   A O    1 
HETATM 4743 O O    . HOH   E 3 .   ? 5.688   -7.370  -37.747 1.00 23.09 ?  211 HOH   A O    1 
HETATM 4744 O O    . HOH   E 3 .   ? 26.992  -9.481  -56.095 1.00 37.28 ?  212 HOH   A O    1 
HETATM 4745 O O    . HOH   E 3 .   ? 20.615  -18.566 -47.434 1.00 28.53 ?  213 HOH   A O    1 
HETATM 4746 O O    . HOH   E 3 .   ? 21.354  8.662   -37.036 1.00 36.56 ?  214 HOH   A O    1 
HETATM 4747 O O    . HOH   E 3 .   ? 11.382  13.330  -25.900 1.00 32.86 ?  215 HOH   A O    1 
HETATM 4748 O O    . HOH   E 3 .   ? 22.018  -17.428 -30.113 1.00 19.73 ?  216 HOH   A O    1 
HETATM 4749 O O    . HOH   E 3 .   ? 12.801  -8.799  -21.155 1.00 43.10 ?  217 HOH   A O    1 
HETATM 4750 O O    . HOH   E 3 .   ? 26.983  0.907   -35.372 1.00 38.30 ?  218 HOH   A O    1 
HETATM 4751 O O    . HOH   E 3 .   ? 23.481  1.885   -37.656 1.00 26.20 ?  219 HOH   A O    1 
HETATM 4752 O O    . HOH   E 3 .   ? 4.523   -0.510  -30.809 1.00 32.53 ?  220 HOH   A O    1 
HETATM 4753 O O    . HOH   E 3 .   ? 22.583  3.794   -42.222 1.00 51.33 ?  221 HOH   A O    1 
HETATM 4754 O O    . HOH   E 3 .   ? 26.290  -9.161  -21.646 1.00 44.17 ?  222 HOH   A O    1 
HETATM 4755 O O    . HOH   E 3 .   ? 21.477  -1.030  -24.668 1.00 17.52 ?  223 HOH   A O    1 
HETATM 4756 O O    . HOH   E 3 .   ? 31.135  1.129   -29.024 1.00 43.82 ?  224 HOH   A O    1 
HETATM 4757 O O    . HOH   E 3 .   ? 19.315  4.172   -31.017 1.00 16.31 ?  225 HOH   A O    1 
HETATM 4758 O O    . HOH   E 3 .   ? 11.969  -18.291 -40.981 1.00 22.22 ?  226 HOH   A O    1 
HETATM 4759 O O    . HOH   E 3 .   ? 21.183  11.763  -36.583 1.00 36.29 ?  227 HOH   A O    1 
HETATM 4760 O O    . HOH   E 3 .   ? 8.925   0.657   -15.778 1.00 43.09 ?  228 HOH   A O    1 
HETATM 4761 O O    . HOH   E 3 .   ? 8.250   1.271   -21.160 1.00 33.84 ?  229 HOH   A O    1 
HETATM 4762 O O    . HOH   E 3 .   ? 24.069  -5.605  -41.508 1.00 32.44 ?  230 HOH   A O    1 
HETATM 4763 O O    . HOH   E 3 .   ? 30.223  -12.011 -45.974 1.00 37.17 ?  231 HOH   A O    1 
HETATM 4764 O O    . HOH   E 3 .   ? 24.967  -16.134 -52.730 1.00 47.05 ?  232 HOH   A O    1 
HETATM 4765 O O    . HOH   E 3 .   ? 24.450  4.133   -36.245 1.00 26.91 ?  233 HOH   A O    1 
HETATM 4766 O O    . HOH   E 3 .   ? 23.936  -21.126 -31.384 1.00 29.03 ?  234 HOH   A O    1 
HETATM 4767 O O    . HOH   E 3 .   ? 6.646   -8.593  -33.669 1.00 26.70 ?  235 HOH   A O    1 
HETATM 4768 O O    . HOH   E 3 .   ? 27.697  -19.286 -48.535 1.00 32.42 ?  236 HOH   A O    1 
HETATM 4769 O O    . HOH   E 3 .   ? 11.250  -9.732  -43.055 1.00 28.47 ?  237 HOH   A O    1 
HETATM 4770 O O    . HOH   E 3 .   ? 28.753  -20.255 -44.637 1.00 37.13 ?  238 HOH   A O    1 
HETATM 4771 O O    . HOH   E 3 .   ? 24.969  -3.367  -16.298 1.00 28.62 ?  239 HOH   A O    1 
HETATM 4772 O O    . HOH   E 3 .   ? 9.044   -6.028  -44.792 1.00 30.04 ?  240 HOH   A O    1 
HETATM 4773 O O    . HOH   E 3 .   ? 23.606  -15.971 -50.202 1.00 35.01 ?  241 HOH   A O    1 
HETATM 4774 O O    . HOH   E 3 .   ? 23.331  -30.990 -44.260 1.00 41.83 ?  242 HOH   A O    1 
HETATM 4775 O O    . HOH   E 3 .   ? 12.912  -8.529  -46.186 1.00 31.26 ?  243 HOH   A O    1 
HETATM 4776 O O    . HOH   E 3 .   ? 24.082  -10.159 -55.017 1.00 39.71 ?  244 HOH   A O    1 
HETATM 4777 O O    . HOH   E 3 .   ? 12.553  -10.729 -45.179 1.00 36.69 ?  245 HOH   A O    1 
HETATM 4778 O O    . HOH   E 3 .   ? 11.498  3.922   -39.006 1.00 28.54 ?  246 HOH   A O    1 
HETATM 4779 O O    . HOH   E 3 .   ? 22.385  3.029   -17.521 1.00 42.06 ?  247 HOH   A O    1 
HETATM 4780 O O    . HOH   E 3 .   ? 25.532  -8.939  -49.189 1.00 39.97 ?  248 HOH   A O    1 
HETATM 4781 O O    . HOH   E 3 .   ? 17.360  -29.392 -43.719 1.00 34.13 ?  249 HOH   A O    1 
HETATM 4782 O O    . HOH   E 3 .   ? 15.209  -11.728 -48.600 1.00 34.70 ?  250 HOH   A O    1 
HETATM 4783 O O    . HOH   E 3 .   ? 20.497  -14.657 -25.183 1.00 34.44 ?  251 HOH   A O    1 
HETATM 4784 O O    . HOH   E 3 .   ? 11.059  -17.903 -43.301 1.00 33.28 ?  252 HOH   A O    1 
HETATM 4785 O O    . HOH   E 3 .   ? 9.881   3.749   -13.000 1.00 34.83 ?  253 HOH   A O    1 
HETATM 4786 O O    . HOH   E 3 .   ? 21.716  -4.686  -41.572 1.00 26.06 ?  254 HOH   A O    1 
HETATM 4787 O O    . HOH   E 3 .   ? 31.058  -12.517 -22.930 1.00 43.22 ?  255 HOH   A O    1 
HETATM 4788 O O    . HOH   E 3 .   ? 9.114   8.050   -28.864 1.00 34.95 ?  256 HOH   A O    1 
HETATM 4789 O O    . HOH   E 3 .   ? 18.963  -5.577  -44.975 1.00 33.62 ?  257 HOH   A O    1 
HETATM 4790 O O    . HOH   E 3 .   ? 7.621   -3.327  -44.024 1.00 45.10 ?  258 HOH   A O    1 
HETATM 4791 O O    . HOH   E 3 .   ? 16.027  -14.228 -48.938 1.00 35.49 ?  259 HOH   A O    1 
HETATM 4792 O O    . HOH   E 3 .   ? 20.607  -7.660  -21.448 1.00 27.08 ?  260 HOH   A O    1 
HETATM 4793 O O    . HOH   E 3 .   ? 10.231  10.333  -20.899 1.00 33.77 ?  261 HOH   A O    1 
HETATM 4794 O O    . HOH   E 3 .   ? 15.348  6.229   -39.655 1.00 33.07 ?  262 HOH   A O    1 
HETATM 4795 O O    . HOH   E 3 .   ? 17.913  3.821   -28.483 1.00 15.66 ?  263 HOH   A O    1 
HETATM 4796 O O    . HOH   E 3 .   ? 22.303  -8.499  -23.483 1.00 22.94 ?  264 HOH   A O    1 
HETATM 4797 O O    . HOH   E 3 .   ? 13.608  -13.576 -22.648 1.00 24.75 ?  265 HOH   A O    1 
HETATM 4798 O O    . HOH   E 3 .   ? 29.310  -22.197 -36.963 1.00 35.43 ?  266 HOH   A O    1 
HETATM 4799 O O    . HOH   E 3 .   ? 31.403  -14.240 -44.633 1.00 34.63 ?  267 HOH   A O    1 
HETATM 4800 O O    . HOH   E 3 .   ? 22.539  -14.709 -30.314 1.00 22.92 ?  268 HOH   A O    1 
HETATM 4801 O O    . HOH   E 3 .   ? 26.100  3.544   -21.530 1.00 34.73 ?  269 HOH   A O    1 
HETATM 4802 O O    . HOH   E 3 .   ? 20.305  4.023   -39.172 1.00 32.68 ?  270 HOH   A O    1 
HETATM 4803 O O    . HOH   E 3 .   ? 21.698  -23.073 -29.031 1.00 34.94 ?  271 HOH   A O    1 
HETATM 4804 O O    . HOH   E 3 .   ? 24.262  -18.895 -29.487 1.00 35.50 ?  272 HOH   A O    1 
HETATM 4805 O O    . HOH   E 3 .   ? 6.943   1.180   -37.223 1.00 32.53 ?  273 HOH   A O    1 
HETATM 4806 O O    . HOH   E 3 .   ? 25.554  2.998   -34.198 1.00 21.93 ?  274 HOH   A O    1 
HETATM 4807 O O    . HOH   E 3 .   ? 22.280  -16.103 -26.691 1.00 37.33 ?  275 HOH   A O    1 
HETATM 4808 O O    . HOH   E 3 .   ? 28.203  -5.293  -22.266 1.00 31.21 ?  276 HOH   A O    1 
HETATM 4809 O O    . HOH   E 3 .   ? 26.731  -24.881 -33.941 1.00 40.39 ?  277 HOH   A O    1 
HETATM 4810 O O    . HOH   E 3 .   ? 22.827  -12.861 -28.813 1.00 38.02 ?  278 HOH   A O    1 
HETATM 4811 O O    . HOH   E 3 .   ? 23.972  -7.677  -51.777 1.00 55.47 ?  279 HOH   A O    1 
HETATM 4812 O O    . HOH   E 3 .   ? 22.958  -8.346  -48.664 1.00 38.21 ?  280 HOH   A O    1 
HETATM 4813 O O    . HOH   E 3 .   ? 12.686  -2.149  -42.133 1.00 29.27 ?  281 HOH   A O    1 
HETATM 4814 O O    . HOH   E 3 .   ? 26.394  -25.623 -45.303 1.00 38.28 ?  282 HOH   A O    1 
HETATM 4815 O O    . HOH   E 3 .   ? 11.252  -6.316  -46.461 1.00 35.59 ?  283 HOH   A O    1 
HETATM 4816 O O    . HOH   E 3 .   ? 23.862  12.741  -34.752 1.00 38.07 ?  284 HOH   A O    1 
HETATM 4817 O O    . HOH   E 3 .   ? 7.042   4.883   -24.722 1.00 42.49 ?  285 HOH   A O    1 
HETATM 4818 O O    . HOH   E 3 .   ? 25.086  -3.780  -43.735 1.00 46.08 ?  286 HOH   A O    1 
HETATM 4819 O O    . HOH   E 3 .   ? 4.681   -4.177  -36.951 1.00 24.74 ?  287 HOH   A O    1 
HETATM 4820 O O    . HOH   E 3 .   ? 22.967  -14.705 -52.051 1.00 42.88 ?  288 HOH   A O    1 
HETATM 4821 O O    . HOH   E 3 .   ? 15.804  -17.178 -51.893 1.00 37.78 ?  289 HOH   A O    1 
HETATM 4822 O O    . HOH   E 3 .   ? 8.347   -1.272  -18.156 1.00 41.84 ?  290 HOH   A O    1 
HETATM 4823 O O    . HOH   E 3 .   ? 10.569  -13.379 -23.206 1.00 42.88 ?  291 HOH   A O    1 
HETATM 4824 O O    . HOH   E 3 .   ? 27.471  5.018   -33.538 1.00 30.62 ?  292 HOH   A O    1 
HETATM 4825 O O    . HOH   E 3 .   ? 27.420  -14.155 -30.846 1.00 36.48 ?  293 HOH   A O    1 
HETATM 4826 O O    . HOH   E 3 .   ? 6.541   -6.200  -45.581 1.00 39.06 ?  294 HOH   A O    1 
HETATM 4827 O O    . HOH   E 3 .   ? 9.491   14.804  -24.858 1.00 35.00 ?  295 HOH   A O    1 
HETATM 4828 O O    . HOH   E 3 .   ? 21.192  -17.085 -49.474 1.00 31.88 ?  296 HOH   A O    1 
HETATM 4829 O O    . HOH   E 3 .   ? 10.755  -9.633  -22.382 1.00 39.45 ?  297 HOH   A O    1 
HETATM 4830 O O    . HOH   E 3 .   ? 10.033  -14.565 -54.166 1.00 37.59 ?  298 HOH   A O    1 
HETATM 4831 O O    . HOH   E 3 .   ? 24.775  -19.875 -27.451 1.00 44.87 ?  299 HOH   A O    1 
HETATM 4832 O O    . HOH   E 3 .   ? 7.183   -0.937  -38.568 1.00 28.32 ?  300 HOH   A O    1 
HETATM 4833 O O    . HOH   E 3 .   ? 17.093  -14.823 -51.049 1.00 38.13 ?  301 HOH   A O    1 
HETATM 4834 O O    . HOH   E 3 .   ? 8.296   2.235   -23.422 1.00 39.04 ?  302 HOH   A O    1 
HETATM 4835 O O    . HOH   E 3 .   ? 7.428   -3.260  -15.939 1.00 41.00 ?  303 HOH   A O    1 
HETATM 4836 O O    . HOH   E 3 .   ? 21.098  -3.867  -44.088 1.00 33.76 ?  304 HOH   A O    1 
HETATM 4837 O O    . HOH   E 3 .   ? 26.050  -22.633 -31.662 1.00 40.35 ?  305 HOH   A O    1 
HETATM 4838 O O    . HOH   E 3 .   ? 11.228  2.787   -41.196 1.00 41.26 ?  306 HOH   A O    1 
HETATM 4839 O O    . HOH   E 3 .   ? 13.904  -17.256 -53.798 1.00 36.88 ?  307 HOH   A O    1 
HETATM 4840 O O    . HOH   E 3 .   ? 29.962  4.148   -35.112 1.00 37.74 ?  308 HOH   A O    1 
HETATM 4841 O O    . HOH   E 3 .   ? 24.175  -24.161 -28.875 1.00 39.65 ?  309 HOH   A O    1 
HETATM 4842 O O    . HOH   E 3 .   ? 16.146  -29.988 -40.005 1.00 43.84 ?  310 HOH   A O    1 
HETATM 4843 O O    . HOH   E 3 .   ? 9.905   -6.940  -48.943 1.00 40.78 ?  311 HOH   A O    1 
HETATM 4844 O O    . HOH   E 3 .   ? 19.598  -17.074 -51.712 1.00 43.52 ?  312 HOH   A O    1 
HETATM 4845 O O    . HOH   E 3 .   ? 7.989   -5.946  -49.311 1.00 42.22 ?  313 HOH   A O    1 
HETATM 4846 O O    . HOH   F 3 .   ? 29.234  32.534  -0.542  1.00 38.16 ?  201 HOH   B O    1 
HETATM 4847 O O    . HOH   F 3 .   ? 15.778  28.891  -14.425 1.00 35.00 ?  202 HOH   B O    1 
HETATM 4848 O O    . HOH   F 3 .   ? 6.299   1.792   5.348   1.00 44.84 ?  203 HOH   B O    1 
HETATM 4849 O O    . HOH   F 3 .   ? 19.869  41.246  -10.598 1.00 31.43 ?  204 HOH   B O    1 
HETATM 4850 O O    . HOH   F 3 .   ? 16.390  15.341  -16.554 1.00 41.80 ?  205 HOH   B O    1 
HETATM 4851 O O    . HOH   F 3 .   ? 19.276  28.242  -23.389 1.00 31.79 ?  206 HOH   B O    1 
HETATM 4852 O O    . HOH   F 3 .   ? 19.423  15.623  17.316  1.00 43.94 ?  207 HOH   B O    1 
HETATM 4853 O O    . HOH   F 3 .   ? 23.606  7.563   -12.895 1.00 40.61 ?  208 HOH   B O    1 
HETATM 4854 O O    . HOH   F 3 .   ? 15.078  24.226  -23.976 1.00 27.81 ?  209 HOH   B O    1 
HETATM 4855 O O    . HOH   F 3 .   ? 31.541  24.456  -0.859  1.00 26.19 ?  210 HOH   B O    1 
HETATM 4856 O O    . HOH   F 3 .   ? 7.002   32.189  -2.764  1.00 44.14 ?  211 HOH   B O    1 
HETATM 4857 O O    . HOH   F 3 .   ? 22.243  26.224  8.811   1.00 34.60 ?  212 HOH   B O    1 
HETATM 4858 O O    . HOH   F 3 .   ? 14.213  23.822  -20.027 1.00 36.47 ?  213 HOH   B O    1 
HETATM 4859 O O    . HOH   F 3 .   ? 18.595  -2.631  -4.446  1.00 31.42 ?  214 HOH   B O    1 
HETATM 4860 O O    . HOH   F 3 .   ? 6.076   14.251  17.552  1.00 32.95 ?  215 HOH   B O    1 
HETATM 4861 O O    . HOH   F 3 .   ? 27.980  4.245   1.089   1.00 29.67 ?  216 HOH   B O    1 
HETATM 4862 O O    . HOH   F 3 .   ? 30.685  19.049  6.936   1.00 37.28 ?  217 HOH   B O    1 
HETATM 4863 O O    . HOH   F 3 .   ? 30.395  26.247  -5.230  1.00 37.45 ?  218 HOH   B O    1 
HETATM 4864 O O    . HOH   F 3 .   ? 15.659  26.867  -24.819 1.00 38.96 ?  219 HOH   B O    1 
HETATM 4865 O O    . HOH   F 3 .   ? 25.732  10.135  -7.930  1.00 29.73 ?  220 HOH   B O    1 
HETATM 4866 O O    . HOH   F 3 .   ? 25.850  28.469  5.657   1.00 24.24 ?  221 HOH   B O    1 
HETATM 4867 O O    . HOH   F 3 .   ? 21.586  4.304   -14.854 1.00 45.48 ?  222 HOH   B O    1 
HETATM 4868 O O    . HOH   F 3 .   ? 12.654  -1.778  5.806   1.00 25.62 ?  223 HOH   B O    1 
HETATM 4869 O O    . HOH   F 3 .   ? 16.707  28.860  -0.985  1.00 13.58 ?  224 HOH   B O    1 
HETATM 4870 O O    . HOH   F 3 .   ? 17.238  18.822  18.493  1.00 37.71 ?  225 HOH   B O    1 
HETATM 4871 O O    . HOH   F 3 .   ? 11.381  28.658  3.969   1.00 21.18 ?  226 HOH   B O    1 
HETATM 4872 O O    . HOH   F 3 .   ? 26.855  22.049  5.150   1.00 18.31 ?  227 HOH   B O    1 
HETATM 4873 O O    . HOH   F 3 .   ? 28.820  7.039   3.969   1.00 27.04 ?  228 HOH   B O    1 
HETATM 4874 O O    . HOH   F 3 .   ? 14.990  24.266  -7.831  1.00 15.92 ?  229 HOH   B O    1 
HETATM 4875 O O    . HOH   F 3 .   ? 26.697  35.640  -10.114 1.00 28.47 ?  230 HOH   B O    1 
HETATM 4876 O O    . HOH   F 3 .   ? 12.256  26.299  5.374   1.00 24.42 ?  231 HOH   B O    1 
HETATM 4877 O O    . HOH   F 3 .   ? 28.375  2.297   2.226   1.00 28.87 ?  232 HOH   B O    1 
HETATM 4878 O O    . HOH   F 3 .   ? 23.903  5.728   7.556   1.00 18.68 ?  233 HOH   B O    1 
HETATM 4879 O O    . HOH   F 3 .   ? 14.089  7.607   -3.553  1.00 15.82 ?  234 HOH   B O    1 
HETATM 4880 O O    . HOH   F 3 .   ? 30.466  16.945  5.638   1.00 26.56 ?  235 HOH   B O    1 
HETATM 4881 O O    . HOH   F 3 .   ? 11.975  5.954   -4.135  1.00 35.63 ?  236 HOH   B O    1 
HETATM 4882 O O    . HOH   F 3 .   ? 27.011  30.234  -18.894 1.00 30.24 ?  237 HOH   B O    1 
HETATM 4883 O O    . HOH   F 3 .   ? 28.907  25.054  -9.412  1.00 26.52 ?  238 HOH   B O    1 
HETATM 4884 O O    . HOH   F 3 .   ? 25.459  1.924   -6.987  1.00 33.77 ?  239 HOH   B O    1 
HETATM 4885 O O    . HOH   F 3 .   ? 32.292  28.160  -15.444 1.00 41.81 ?  240 HOH   B O    1 
HETATM 4886 O O    . HOH   F 3 .   ? 27.599  26.600  -16.487 1.00 26.19 ?  241 HOH   B O    1 
HETATM 4887 O O    . HOH   F 3 .   ? 5.249   22.917  -6.638  1.00 35.96 ?  242 HOH   B O    1 
HETATM 4888 O O    . HOH   F 3 .   ? 20.362  30.399  8.073   1.00 21.53 ?  243 HOH   B O    1 
HETATM 4889 O O    . HOH   F 3 .   ? 32.905  23.005  -3.410  1.00 34.58 ?  244 HOH   B O    1 
HETATM 4890 O O    . HOH   F 3 .   ? 22.188  -0.642  -8.211  1.00 37.54 ?  245 HOH   B O    1 
HETATM 4891 O O    . HOH   F 3 .   ? 21.182  1.484   -13.300 1.00 31.07 ?  246 HOH   B O    1 
HETATM 4892 O O    . HOH   F 3 .   ? 9.316   -2.636  10.203  1.00 47.15 ?  247 HOH   B O    1 
HETATM 4893 O O    . HOH   F 3 .   ? 23.834  32.630  -0.320  1.00 20.41 ?  248 HOH   B O    1 
HETATM 4894 O O    . HOH   F 3 .   ? 20.913  6.150   -14.003 1.00 44.68 ?  249 HOH   B O    1 
HETATM 4895 O O    . HOH   F 3 .   ? 24.958  32.355  -23.319 1.00 33.81 ?  250 HOH   B O    1 
HETATM 4896 O O    . HOH   F 3 .   ? 17.116  36.786  8.956   1.00 33.31 ?  251 HOH   B O    1 
HETATM 4897 O O    . HOH   F 3 .   ? 9.011   28.432  -12.978 1.00 38.24 ?  252 HOH   B O    1 
HETATM 4898 O O    . HOH   F 3 .   ? 3.927   8.359   19.002  1.00 37.41 ?  253 HOH   B O    1 
HETATM 4899 O O    . HOH   F 3 .   ? 16.198  17.677  12.485  1.00 28.99 ?  254 HOH   B O    1 
HETATM 4900 O O    . HOH   F 3 .   ? 7.971   22.336  0.508   1.00 31.38 ?  255 HOH   B O    1 
HETATM 4901 O O    . HOH   F 3 .   ? 12.430  4.009   -2.732  1.00 20.18 ?  256 HOH   B O    1 
HETATM 4902 O O    . HOH   F 3 .   ? 9.351   -0.384  -0.122  1.00 32.66 ?  257 HOH   B O    1 
HETATM 4903 O O    . HOH   F 3 .   ? 14.582  33.514  4.382   1.00 26.72 ?  258 HOH   B O    1 
HETATM 4904 O O    . HOH   F 3 .   ? 16.161  35.711  -10.855 1.00 40.93 ?  259 HOH   B O    1 
HETATM 4905 O O    . HOH   F 3 .   ? 29.152  16.302  1.430   1.00 20.75 ?  260 HOH   B O    1 
HETATM 4906 O O    . HOH   F 3 .   ? 13.663  12.761  -4.399  1.00 23.70 ?  261 HOH   B O    1 
HETATM 4907 O O    . HOH   F 3 .   ? 15.142  27.721  6.799   1.00 33.91 ?  262 HOH   B O    1 
HETATM 4908 O O    . HOH   F 3 .   ? 16.053  28.028  -18.854 1.00 32.47 ?  263 HOH   B O    1 
HETATM 4909 O O    . HOH   F 3 .   ? 9.464   20.016  10.451  1.00 44.73 ?  264 HOH   B O    1 
HETATM 4910 O O    . HOH   F 3 .   ? 15.246  5.152   13.514  1.00 20.41 ?  265 HOH   B O    1 
HETATM 4911 O O    . HOH   F 3 .   ? 24.460  19.352  -8.797  1.00 18.16 ?  266 HOH   B O    1 
HETATM 4912 O O    . HOH   F 3 .   ? 28.698  18.782  -6.470  1.00 22.96 ?  267 HOH   B O    1 
HETATM 4913 O O    . HOH   F 3 .   ? 21.749  37.310  -5.358  1.00 18.03 ?  268 HOH   B O    1 
HETATM 4914 O O    . HOH   F 3 .   ? 8.954   25.667  2.626   1.00 33.93 ?  269 HOH   B O    1 
HETATM 4915 O O    . HOH   F 3 .   ? 28.549  26.955  -11.242 1.00 37.71 ?  270 HOH   B O    1 
HETATM 4916 O O    . HOH   F 3 .   ? 23.782  6.691   19.212  1.00 36.45 ?  271 HOH   B O    1 
HETATM 4917 O O    . HOH   F 3 .   ? 10.704  35.879  2.034   1.00 32.06 ?  272 HOH   B O    1 
HETATM 4918 O O    . HOH   F 3 .   ? 6.818   28.331  -10.894 1.00 48.15 ?  273 HOH   B O    1 
HETATM 4919 O O    . HOH   F 3 .   ? 13.155  14.273  14.662  1.00 35.64 ?  274 HOH   B O    1 
HETATM 4920 O O    . HOH   F 3 .   ? 27.885  26.211  -20.715 1.00 28.91 ?  275 HOH   B O    1 
HETATM 4921 O O    . HOH   F 3 .   ? 29.364  5.257   5.788   1.00 34.62 ?  276 HOH   B O    1 
HETATM 4922 O O    . HOH   F 3 .   ? 24.214  14.042  10.780  1.00 25.99 ?  277 HOH   B O    1 
HETATM 4923 O O    . HOH   F 3 .   ? 30.844  24.477  4.554   1.00 24.07 ?  278 HOH   B O    1 
HETATM 4924 O O    . HOH   F 3 .   ? 5.735   14.528  5.699   1.00 22.20 ?  279 HOH   B O    1 
HETATM 4925 O O    . HOH   F 3 .   ? 17.666  29.901  -19.916 1.00 32.31 ?  280 HOH   B O    1 
HETATM 4926 O O    . HOH   F 3 .   ? 18.337  32.387  -13.212 1.00 33.93 ?  281 HOH   B O    1 
HETATM 4927 O O    . HOH   F 3 .   ? 17.482  35.248  11.500  1.00 34.19 ?  282 HOH   B O    1 
HETATM 4928 O O    . HOH   F 3 .   ? 18.000  -5.790  9.398   1.00 34.27 ?  283 HOH   B O    1 
HETATM 4929 O O    . HOH   F 3 .   ? 11.803  7.225   16.889  1.00 29.53 ?  284 HOH   B O    1 
HETATM 4930 O O    . HOH   F 3 .   ? 28.510  20.329  -16.250 1.00 37.07 ?  285 HOH   B O    1 
HETATM 4931 O O    . HOH   F 3 .   ? 10.375  13.452  17.019  1.00 19.63 ?  286 HOH   B O    1 
HETATM 4932 O O    . HOH   F 3 .   ? 6.886   11.553  -6.753  1.00 29.64 ?  287 HOH   B O    1 
HETATM 4933 O O    . HOH   F 3 .   ? 16.164  37.697  -2.758  1.00 22.06 ?  288 HOH   B O    1 
HETATM 4934 O O    . HOH   F 3 .   ? 29.382  29.719  -17.977 1.00 37.57 ?  289 HOH   B O    1 
HETATM 4935 O O    . HOH   F 3 .   ? 14.558  -4.995  5.526   1.00 45.01 ?  290 HOH   B O    1 
HETATM 4936 O O    . HOH   F 3 .   ? 25.364  34.715  -0.937  1.00 37.11 ?  291 HOH   B O    1 
HETATM 4937 O O    . HOH   F 3 .   ? 8.232   4.266   15.141  1.00 33.62 ?  292 HOH   B O    1 
HETATM 4938 O O    . HOH   F 3 .   ? 26.085  17.703  12.828  1.00 27.34 ?  293 HOH   B O    1 
HETATM 4939 O O    . HOH   F 3 .   ? 14.496  16.696  -9.388  1.00 30.05 ?  294 HOH   B O    1 
HETATM 4940 O O    . HOH   F 3 .   ? 26.626  20.522  12.299  1.00 38.63 ?  295 HOH   B O    1 
HETATM 4941 O O    . HOH   F 3 .   ? 8.753   3.972   -4.804  1.00 40.46 ?  296 HOH   B O    1 
HETATM 4942 O O    . HOH   F 3 .   ? 23.457  35.844  -0.507  1.00 27.24 ?  297 HOH   B O    1 
HETATM 4943 O O    . HOH   F 3 .   ? 23.779  13.652  17.302  1.00 34.54 ?  298 HOH   B O    1 
HETATM 4944 O O    . HOH   F 3 .   ? 22.847  11.684  -10.156 1.00 32.65 ?  299 HOH   B O    1 
HETATM 4945 O O    . HOH   F 3 .   ? 28.385  25.880  6.234   1.00 32.39 ?  300 HOH   B O    1 
HETATM 4946 O O    . HOH   F 3 .   ? 6.886   1.951   2.484   1.00 27.20 ?  301 HOH   B O    1 
HETATM 4947 O O    . HOH   F 3 .   ? 7.783   0.363   10.578  1.00 37.96 ?  302 HOH   B O    1 
HETATM 4948 O O    . HOH   F 3 .   ? 8.102   2.595   11.700  1.00 39.24 ?  303 HOH   B O    1 
HETATM 4949 O O    . HOH   F 3 .   ? 12.794  16.866  15.081  1.00 41.58 ?  304 HOH   B O    1 
HETATM 4950 O O    . HOH   F 3 .   ? 22.341  14.727  13.552  1.00 29.51 ?  305 HOH   B O    1 
HETATM 4951 O O    . HOH   F 3 .   ? 16.161  -7.442  11.476  1.00 41.61 ?  306 HOH   B O    1 
HETATM 4952 O O    . HOH   F 3 .   ? 14.340  30.089  6.483   1.00 25.96 ?  307 HOH   B O    1 
HETATM 4953 O O    . HOH   F 3 .   ? 18.244  28.794  -3.421  1.00 14.42 ?  308 HOH   B O    1 
HETATM 4954 O O    . HOH   F 3 .   ? 29.751  16.596  -15.047 1.00 35.37 ?  309 HOH   B O    1 
HETATM 4955 O O    . HOH   F 3 .   ? 6.843   20.829  2.584   1.00 24.70 ?  310 HOH   B O    1 
HETATM 4956 O O    . HOH   F 3 .   ? 11.854  22.763  -16.517 1.00 29.54 ?  311 HOH   B O    1 
HETATM 4957 O O    . HOH   F 3 .   ? 10.210  28.978  -10.784 1.00 26.22 ?  312 HOH   B O    1 
HETATM 4958 O O    . HOH   F 3 .   ? 18.054  37.246  -9.032  1.00 30.24 ?  313 HOH   B O    1 
HETATM 4959 O O    . HOH   F 3 .   ? 24.162  28.448  7.453   1.00 30.05 ?  314 HOH   B O    1 
HETATM 4960 O O    . HOH   F 3 .   ? 16.668  21.961  -21.377 1.00 37.92 ?  315 HOH   B O    1 
HETATM 4961 O O    . HOH   F 3 .   ? 13.222  18.908  8.787   1.00 25.42 ?  316 HOH   B O    1 
HETATM 4962 O O    . HOH   F 3 .   ? 9.326   21.707  -13.842 1.00 38.50 ?  317 HOH   B O    1 
HETATM 4963 O O    . HOH   F 3 .   ? 13.559  10.257  -3.221  1.00 20.62 ?  318 HOH   B O    1 
HETATM 4964 O O    . HOH   F 3 .   ? 7.306   5.131   16.826  1.00 39.81 ?  319 HOH   B O    1 
HETATM 4965 O O    . HOH   F 3 .   ? 15.752  2.301   -5.199  1.00 25.26 ?  320 HOH   B O    1 
HETATM 4966 O O    . HOH   F 3 .   ? 27.551  33.907  -17.093 1.00 34.54 ?  321 HOH   B O    1 
HETATM 4967 O O    . HOH   F 3 .   ? 26.186  3.176   17.648  1.00 38.75 ?  322 HOH   B O    1 
HETATM 4968 O O    . HOH   F 3 .   ? 10.309  27.522  1.649   1.00 20.10 ?  323 HOH   B O    1 
HETATM 4969 O O    . HOH   F 3 .   ? 25.146  34.854  2.954   1.00 27.68 ?  324 HOH   B O    1 
HETATM 4970 O O    . HOH   F 3 .   ? 16.222  17.164  -15.005 1.00 38.94 ?  325 HOH   B O    1 
HETATM 4971 O O    . HOH   F 3 .   ? 24.964  5.419   9.922   1.00 26.07 ?  326 HOH   B O    1 
HETATM 4972 O O    . HOH   F 3 .   ? 11.832  23.365  11.507  1.00 44.75 ?  327 HOH   B O    1 
HETATM 4973 O O    . HOH   F 3 .   ? 6.070   3.326   8.303   1.00 27.59 ?  328 HOH   B O    1 
HETATM 4974 O O    . HOH   F 3 .   ? 18.238  3.379   16.884  1.00 38.69 ?  329 HOH   B O    1 
HETATM 4975 O O    . HOH   F 3 .   ? 8.691   20.095  -11.104 1.00 31.39 ?  330 HOH   B O    1 
HETATM 4976 O O    . HOH   F 3 .   ? 22.817  12.928  12.537  1.00 30.03 ?  331 HOH   B O    1 
HETATM 4977 O O    . HOH   F 3 .   ? 11.451  19.254  12.221  1.00 35.47 ?  332 HOH   B O    1 
HETATM 4978 O O    . HOH   F 3 .   ? 16.147  17.819  -11.355 1.00 28.10 ?  333 HOH   B O    1 
HETATM 4979 O O    . HOH   F 3 .   ? 4.670   24.782  -12.422 1.00 45.93 ?  334 HOH   B O    1 
HETATM 4980 O O    . HOH   F 3 .   ? 22.008  -0.334  -11.271 1.00 28.58 ?  335 HOH   B O    1 
HETATM 4981 O O    . HOH   F 3 .   ? 17.626  30.635  8.627   1.00 32.31 ?  336 HOH   B O    1 
HETATM 4982 O O    . HOH   F 3 .   ? 27.305  12.243  19.459  1.00 41.30 ?  337 HOH   B O    1 
HETATM 4983 O O    . HOH   F 3 .   ? 22.766  21.749  10.371  1.00 28.67 ?  338 HOH   B O    1 
HETATM 4984 O O    . HOH   F 3 .   ? 23.502  41.936  -7.942  1.00 33.11 ?  339 HOH   B O    1 
HETATM 4985 O O    . HOH   F 3 .   ? 24.627  3.385   -16.750 1.00 51.31 ?  340 HOH   B O    1 
HETATM 4986 O O    . HOH   F 3 .   ? 23.978  16.979  14.290  1.00 30.22 ?  341 HOH   B O    1 
HETATM 4987 O O    . HOH   F 3 .   ? 17.236  33.519  13.036  1.00 29.58 ?  342 HOH   B O    1 
HETATM 4988 O O    . HOH   F 3 .   ? 17.396  30.025  -22.447 1.00 50.76 ?  343 HOH   B O    1 
HETATM 4989 O O    . HOH   F 3 .   ? 24.985  -3.900  -2.755  1.00 31.21 ?  344 HOH   B O    1 
HETATM 4990 O O    . HOH   F 3 .   ? 27.572  32.808  -19.571 1.00 34.24 ?  345 HOH   B O    1 
HETATM 4991 O O    . HOH   F 3 .   ? 19.532  -4.125  17.472  1.00 45.58 ?  346 HOH   B O    1 
HETATM 4992 O O    . HOH   F 3 .   ? 19.308  21.320  -19.138 1.00 35.56 ?  347 HOH   B O    1 
HETATM 4993 O O    . HOH   F 3 .   ? 26.012  36.312  -7.486  1.00 36.06 ?  348 HOH   B O    1 
HETATM 4994 O O    . HOH   F 3 .   ? 5.647   1.186   8.978   1.00 36.49 ?  349 HOH   B O    1 
HETATM 4995 O O    . HOH   F 3 .   ? 25.524  0.291   10.775  1.00 41.36 ?  350 HOH   B O    1 
HETATM 4996 O O    . HOH   F 3 .   ? 25.839  12.123  -10.005 1.00 41.34 ?  351 HOH   B O    1 
HETATM 4997 O O    . HOH   F 3 .   ? 9.255   29.695  5.245   1.00 37.36 ?  352 HOH   B O    1 
HETATM 4998 O O    . HOH   F 3 .   ? 5.941   12.542  10.774  1.00 47.83 ?  353 HOH   B O    1 
HETATM 4999 O O    . HOH   F 3 .   ? 24.707  22.337  11.192  1.00 43.94 ?  354 HOH   B O    1 
HETATM 5000 O O    . HOH   F 3 .   ? 3.548   4.911   7.443   1.00 33.63 ?  355 HOH   B O    1 
HETATM 5001 O O    . HOH   F 3 .   ? 19.937  34.322  9.548   1.00 37.28 ?  356 HOH   B O    1 
HETATM 5002 O O    . HOH   F 3 .   ? 26.088  11.850  21.059  1.00 50.83 ?  357 HOH   B O    1 
HETATM 5003 O O    . HOH   F 3 .   ? 25.855  2.355   10.294  1.00 38.04 ?  358 HOH   B O    1 
HETATM 5004 O O    . HOH   F 3 .   ? 15.526  3.383   15.466  1.00 35.97 ?  359 HOH   B O    1 
HETATM 5005 O O    . HOH   F 3 .   ? 21.505  14.217  16.132  1.00 37.56 ?  360 HOH   B O    1 
HETATM 5006 O O    . HOH   F 3 .   ? 13.367  3.099   -5.350  1.00 36.88 ?  361 HOH   B O    1 
HETATM 5007 O O    . HOH   F 3 .   ? 24.007  27.279  9.887   1.00 43.48 ?  362 HOH   B O    1 
HETATM 5008 O O    . HOH   F 3 .   ? 10.322  2.300   -2.446  1.00 30.50 ?  363 HOH   B O    1 
HETATM 5009 O O    . HOH   F 3 .   ? 18.849  5.431   18.146  1.00 35.81 ?  364 HOH   B O    1 
HETATM 5010 O O    . HOH   F 3 .   ? 22.147  30.696  10.658  1.00 34.30 ?  365 HOH   B O    1 
HETATM 5011 O O    . HOH   F 3 .   ? 22.777  23.961  10.531  1.00 42.73 ?  366 HOH   B O    1 
HETATM 5012 O O    . HOH   F 3 .   ? 7.786   4.165   1.418   1.00 33.48 ?  367 HOH   B O    1 
HETATM 5013 O O    . HOH   F 3 .   ? 28.666  22.395  -16.394 1.00 37.49 ?  368 HOH   B O    1 
HETATM 5014 O O    . HOH   F 3 .   ? 17.547  24.386  12.241  1.00 43.85 ?  369 HOH   B O    1 
HETATM 5015 O O    . HOH   F 3 .   ? 13.230  26.705  7.779   1.00 39.67 ?  370 HOH   B O    1 
HETATM 5016 O O    . HOH   F 3 .   ? 28.169  17.833  14.165  1.00 41.29 ?  371 HOH   B O    1 
HETATM 5017 O O    . HOH   F 3 .   ? 13.922  19.780  11.214  1.00 27.61 ?  372 HOH   B O    1 
HETATM 5018 O O    . HOH   F 3 .   ? 21.117  22.466  12.211  1.00 46.35 ?  373 HOH   B O    1 
HETATM 5019 O O    . HOH   F 3 .   ? 27.279  24.168  9.820   1.00 40.48 ?  374 HOH   B O    1 
HETATM 5020 O O    . HOH   F 3 .   ? 28.377  23.368  7.144   1.00 25.93 ?  375 HOH   B O    1 
HETATM 5021 O O    . HOH   F 3 .   ? 7.949   11.001  -5.217  1.00 36.04 ?  376 HOH   B O    1 
HETATM 5022 O O    . HOH   F 3 .   ? 24.199  38.391  -5.875  1.00 34.12 ?  377 HOH   B O    1 
HETATM 5023 O O    . HOH   F 3 .   ? 28.450  24.725  -14.562 1.00 31.51 ?  378 HOH   B O    1 
HETATM 5024 O O    . HOH   F 3 .   ? 21.158  5.851   19.658  1.00 38.96 ?  379 HOH   B O    1 
HETATM 5025 O O    . HOH   F 3 .   ? 6.728   22.514  4.224   1.00 42.74 ?  380 HOH   B O    1 
HETATM 5026 O O    . HOH   F 3 .   ? 13.911  33.563  -11.659 1.00 46.65 ?  381 HOH   B O    1 
HETATM 5027 O O    . HOH   F 3 .   ? 14.130  22.725  11.569  1.00 37.06 ?  382 HOH   B O    1 
HETATM 5028 O O    . HOH   F 3 .   ? 14.340  6.009   16.270  1.00 37.03 ?  383 HOH   B O    1 
HETATM 5029 O O    . HOH   F 3 .   ? 22.558  21.587  14.164  1.00 49.42 ?  384 HOH   B O    1 
HETATM 5030 O O    . HOH   F 3 .   ? 28.611  27.531  -7.801  1.00 33.83 ?  385 HOH   B O    1 
HETATM 5031 O O    . HOH   F 3 .   ? 18.727  31.962  -24.402 1.00 52.26 ?  386 HOH   B O    1 
HETATM 5032 O O    . HOH   F 3 .   ? 5.739   20.410  -10.836 1.00 42.01 ?  387 HOH   B O    1 
HETATM 5033 O O    . HOH   F 3 .   ? 15.387  24.603  9.988   1.00 44.61 ?  388 HOH   B O    1 
HETATM 5034 O O    . HOH   F 3 .   ? 8.515   29.618  1.291   1.00 30.66 ?  389 HOH   B O    1 
HETATM 5035 O O    . HOH   F 3 .   ? 8.377   35.943  0.193   1.00 45.57 ?  390 HOH   B O    1 
HETATM 5036 O O    . HOH   F 3 .   ? 12.192  0.706   -5.675  1.00 37.91 ?  391 HOH   B O    1 
HETATM 5037 O O    . HOH   F 3 .   ? 26.787  26.864  9.408   1.00 50.53 ?  392 HOH   B O    1 
HETATM 5038 O O    . HOH   F 3 .   ? 16.715  6.689   17.932  1.00 42.33 ?  393 HOH   B O    1 
HETATM 5039 O O    . HOH   G 3 .   ? 11.662  -33.342 3.259   1.00 28.58 ?  201 HOH   C O    1 
HETATM 5040 O O    . HOH   G 3 .   ? 7.014   -24.533 11.716  1.00 19.82 ?  202 HOH   C O    1 
HETATM 5041 O O    . HOH   G 3 .   ? 4.109   -29.040 4.013   1.00 36.26 ?  203 HOH   C O    1 
HETATM 5042 O O    . HOH   G 3 .   ? 26.938  -23.604 -7.176  1.00 32.65 ?  204 HOH   C O    1 
HETATM 5043 O O    . HOH   G 3 .   ? 6.953   -16.322 10.308  1.00 34.80 ?  205 HOH   C O    1 
HETATM 5044 O O    . HOH   G 3 .   ? -2.423  -6.279  10.314  1.00 51.54 ?  206 HOH   C O    1 
HETATM 5045 O O    . HOH   G 3 .   ? 1.486   -29.038 4.324   1.00 33.33 ?  207 HOH   C O    1 
HETATM 5046 O O    . HOH   G 3 .   ? 30.709  -33.348 -2.856  1.00 40.47 ?  208 HOH   C O    1 
HETATM 5047 O O    . HOH   G 3 .   ? 4.278   -9.603  3.991   1.00 40.03 ?  209 HOH   C O    1 
HETATM 5048 O O    . HOH   G 3 .   ? 29.747  -23.184 -4.952  1.00 33.63 ?  210 HOH   C O    1 
HETATM 5049 O O    . HOH   G 3 .   ? -4.630  -9.057  10.831  1.00 49.16 ?  211 HOH   C O    1 
HETATM 5050 O O    . HOH   G 3 .   ? 22.266  -12.070 -5.723  1.00 33.97 ?  212 HOH   C O    1 
HETATM 5051 O O    . HOH   G 3 .   ? 24.506  -33.858 10.441  1.00 31.58 ?  213 HOH   C O    1 
HETATM 5052 O O    . HOH   G 3 .   ? -3.848  -10.992 5.456   1.00 34.75 ?  214 HOH   C O    1 
HETATM 5053 O O    . HOH   G 3 .   ? 22.877  -18.924 15.712  1.00 22.14 ?  215 HOH   C O    1 
HETATM 5054 O O    . HOH   G 3 .   ? 5.783   -31.383 2.550   1.00 32.32 ?  216 HOH   C O    1 
HETATM 5055 O O    . HOH   G 3 .   ? -5.358  -23.140 -15.665 1.00 29.05 ?  217 HOH   C O    1 
HETATM 5056 O O    . HOH   G 3 .   ? 35.277  -30.794 11.560  1.00 45.45 ?  218 HOH   C O    1 
HETATM 5057 O O    . HOH   G 3 .   ? 19.870  -14.201 11.759  1.00 32.06 ?  219 HOH   C O    1 
HETATM 5058 O O    . HOH   G 3 .   ? 30.301  -18.376 0.658   1.00 28.02 ?  220 HOH   C O    1 
HETATM 5059 O O    . HOH   G 3 .   ? 5.515   -26.571 3.990   1.00 16.10 ?  221 HOH   C O    1 
HETATM 5060 O O    . HOH   G 3 .   ? 26.600  -28.648 -3.270  1.00 37.71 ?  222 HOH   C O    1 
HETATM 5061 O O    . HOH   G 3 .   ? 27.093  -19.890 8.899   1.00 16.29 ?  223 HOH   C O    1 
HETATM 5062 O O    . HOH   G 3 .   ? -1.912  -28.961 6.824   1.00 33.56 ?  224 HOH   C O    1 
HETATM 5063 O O    . HOH   G 3 .   ? 30.000  -15.093 3.444   1.00 31.22 ?  225 HOH   C O    1 
HETATM 5064 O O    . HOH   G 3 .   ? 15.827  -33.260 0.470   1.00 21.42 ?  226 HOH   C O    1 
HETATM 5065 O O    . HOH   G 3 .   ? 20.231  -10.207 5.578   1.00 33.28 ?  227 HOH   C O    1 
HETATM 5066 O O    . HOH   G 3 .   ? 3.243   -12.627 4.552   1.00 33.13 ?  228 HOH   C O    1 
HETATM 5067 O O    . HOH   G 3 .   ? 3.418   -29.714 11.865  1.00 38.89 ?  229 HOH   C O    1 
HETATM 5068 O O    . HOH   G 3 .   ? 19.560  -11.672 2.536   1.00 24.04 ?  230 HOH   C O    1 
HETATM 5069 O O    . HOH   G 3 .   ? 14.105  -31.042 10.019  1.00 33.00 ?  231 HOH   C O    1 
HETATM 5070 O O    . HOH   G 3 .   ? 29.040  -11.939 -4.225  1.00 31.42 ?  232 HOH   C O    1 
HETATM 5071 O O    . HOH   G 3 .   ? 13.399  -33.539 -8.077  1.00 30.01 ?  233 HOH   C O    1 
HETATM 5072 O O    . HOH   G 3 .   ? 27.626  -18.950 0.416   1.00 21.08 ?  234 HOH   C O    1 
HETATM 5073 O O    . HOH   G 3 .   ? 26.658  -22.994 16.711  1.00 42.02 ?  235 HOH   C O    1 
HETATM 5074 O O    . HOH   G 3 .   ? 15.864  -33.923 12.664  1.00 36.30 ?  236 HOH   C O    1 
HETATM 5075 O O    . HOH   G 3 .   ? 20.888  -27.149 -12.555 1.00 34.83 ?  237 HOH   C O    1 
HETATM 5076 O O    . HOH   G 3 .   ? 30.781  -25.660 -6.528  1.00 35.93 ?  238 HOH   C O    1 
HETATM 5077 O O    . HOH   G 3 .   ? 21.456  -12.766 13.496  1.00 28.31 ?  239 HOH   C O    1 
HETATM 5078 O O    . HOH   G 3 .   ? 32.204  -17.205 -0.396  1.00 24.03 ?  240 HOH   C O    1 
HETATM 5079 O O    . HOH   G 3 .   ? 27.668  -34.522 -2.710  1.00 37.35 ?  241 HOH   C O    1 
HETATM 5080 O O    . HOH   G 3 .   ? 25.475  -20.495 -7.876  1.00 32.59 ?  242 HOH   C O    1 
HETATM 5081 O O    . HOH   G 3 .   ? 14.279  -20.892 -6.393  1.00 18.95 ?  243 HOH   C O    1 
HETATM 5082 O O    . HOH   G 3 .   ? 14.111  -24.323 -11.189 1.00 26.26 ?  244 HOH   C O    1 
HETATM 5083 O O    . HOH   G 3 .   ? 18.896  -19.648 -10.979 1.00 34.85 ?  245 HOH   C O    1 
HETATM 5084 O O    . HOH   G 3 .   ? 32.749  -26.778 -1.544  1.00 28.08 ?  246 HOH   C O    1 
HETATM 5085 O O    . HOH   G 3 .   ? 29.762  -18.719 18.175  1.00 40.85 ?  247 HOH   C O    1 
HETATM 5086 O O    . HOH   G 3 .   ? 25.927  -15.961 9.982   1.00 19.62 ?  248 HOH   C O    1 
HETATM 5087 O O    . HOH   G 3 .   ? 7.404   -18.862 -6.931  1.00 27.56 ?  249 HOH   C O    1 
HETATM 5088 O O    . HOH   G 3 .   ? 24.394  -28.043 -3.928  1.00 28.38 ?  250 HOH   C O    1 
HETATM 5089 O O    . HOH   G 3 .   ? 25.171  -5.360  1.044   1.00 40.05 ?  251 HOH   C O    1 
HETATM 5090 O O    . HOH   G 3 .   ? 31.811  -23.479 12.329  1.00 31.87 ?  252 HOH   C O    1 
HETATM 5091 O O    . HOH   G 3 .   ? 13.247  -15.155 8.467   1.00 26.27 ?  253 HOH   C O    1 
HETATM 5092 O O    . HOH   G 3 .   ? 0.034   -12.653 5.368   1.00 50.72 ?  254 HOH   C O    1 
HETATM 5093 O O    . HOH   G 3 .   ? 8.304   -27.103 12.297  1.00 25.52 ?  255 HOH   C O    1 
HETATM 5094 O O    . HOH   G 3 .   ? 15.746  -18.924 -5.075  1.00 19.07 ?  256 HOH   C O    1 
HETATM 5095 O O    . HOH   G 3 .   ? 20.175  -29.166 14.242  1.00 25.05 ?  257 HOH   C O    1 
HETATM 5096 O O    . HOH   G 3 .   ? 5.392   -18.321 -9.210  1.00 25.49 ?  258 HOH   C O    1 
HETATM 5097 O O    . HOH   G 3 .   ? 27.971  -15.795 2.997   1.00 27.56 ?  259 HOH   C O    1 
HETATM 5098 O O    . HOH   G 3 .   ? 32.502  -29.665 11.498  1.00 30.00 ?  260 HOH   C O    1 
HETATM 5099 O O    . HOH   G 3 .   ? 33.737  -22.020 10.565  1.00 31.87 ?  261 HOH   C O    1 
HETATM 5100 O O    . HOH   G 3 .   ? 9.741   -19.769 -9.774  1.00 33.17 ?  262 HOH   C O    1 
HETATM 5101 O O    . HOH   G 3 .   ? 15.844  -30.462 18.196  1.00 40.86 ?  263 HOH   C O    1 
HETATM 5102 O O    . HOH   G 3 .   ? 19.869  -9.434  -0.275  1.00 35.02 ?  264 HOH   C O    1 
HETATM 5103 O O    . HOH   G 3 .   ? 18.694  -16.311 12.642  1.00 26.42 ?  265 HOH   C O    1 
HETATM 5104 O O    . HOH   G 3 .   ? 27.448  -37.119 10.631  1.00 41.72 ?  266 HOH   C O    1 
HETATM 5105 O O    . HOH   G 3 .   ? 23.824  -34.544 2.030   1.00 17.87 ?  267 HOH   C O    1 
HETATM 5106 O O    . HOH   G 3 .   ? 22.925  -17.570 13.354  1.00 29.92 ?  268 HOH   C O    1 
HETATM 5107 O O    . HOH   G 3 .   ? -5.643  -29.264 -1.593  1.00 37.38 ?  269 HOH   C O    1 
HETATM 5108 O O    . HOH   G 3 .   ? -6.743  -25.953 2.057   1.00 23.36 ?  270 HOH   C O    1 
HETATM 5109 O O    . HOH   G 3 .   ? 2.103   -14.296 -5.623  1.00 27.99 ?  271 HOH   C O    1 
HETATM 5110 O O    . HOH   G 3 .   ? -1.746  -17.010 -8.367  1.00 38.33 ?  272 HOH   C O    1 
HETATM 5111 O O    . HOH   G 3 .   ? 24.550  -26.831 -1.509  1.00 14.98 ?  273 HOH   C O    1 
HETATM 5112 O O    . HOH   G 3 .   ? 33.317  -29.135 2.955   1.00 19.91 ?  274 HOH   C O    1 
HETATM 5113 O O    . HOH   G 3 .   ? 5.522   -30.884 9.947   1.00 29.58 ?  275 HOH   C O    1 
HETATM 5114 O O    . HOH   G 3 .   ? 22.908  -17.493 -5.771  1.00 25.75 ?  276 HOH   C O    1 
HETATM 5115 O O    . HOH   G 3 .   ? -4.139  -15.586 -2.255  1.00 36.33 ?  277 HOH   C O    1 
HETATM 5116 O O    . HOH   G 3 .   ? 27.736  -20.801 -4.655  1.00 32.16 ?  278 HOH   C O    1 
HETATM 5117 O O    . HOH   G 3 .   ? 25.989  -8.580  2.470   1.00 38.93 ?  279 HOH   C O    1 
HETATM 5118 O O    . HOH   G 3 .   ? 3.976   -21.111 11.479  1.00 28.16 ?  280 HOH   C O    1 
HETATM 5119 O O    . HOH   G 3 .   ? -4.351  -22.219 10.036  1.00 38.00 ?  281 HOH   C O    1 
HETATM 5120 O O    . HOH   G 3 .   ? 13.536  -32.365 1.668   1.00 20.10 ?  282 HOH   C O    1 
HETATM 5121 O O    . HOH   G 3 .   ? 31.117  -16.960 16.219  1.00 30.55 ?  283 HOH   C O    1 
HETATM 5122 O O    . HOH   G 3 .   ? 9.879   -14.074 -5.843  1.00 42.85 ?  284 HOH   C O    1 
HETATM 5123 O O    . HOH   G 3 .   ? 10.968  -36.813 -5.876  1.00 33.47 ?  285 HOH   C O    1 
HETATM 5124 O O    . HOH   G 3 .   ? 27.450  -34.965 7.527   1.00 32.11 ?  286 HOH   C O    1 
HETATM 5125 O O    . HOH   G 3 .   ? 5.330   -31.271 -11.131 1.00 32.21 ?  287 HOH   C O    1 
HETATM 5126 O O    . HOH   G 3 .   ? -0.034  -21.678 -9.301  1.00 35.12 ?  288 HOH   C O    1 
HETATM 5127 O O    . HOH   G 3 .   ? 28.740  -16.232 -3.900  1.00 22.08 ?  289 HOH   C O    1 
HETATM 5128 O O    . HOH   G 3 .   ? 9.288   -13.364 2.633   1.00 23.42 ?  290 HOH   C O    1 
HETATM 5129 O O    . HOH   G 3 .   ? 21.229  -28.907 -8.837  1.00 24.05 ?  291 HOH   C O    1 
HETATM 5130 O O    . HOH   G 3 .   ? 25.564  -17.709 11.973  1.00 23.26 ?  292 HOH   C O    1 
HETATM 5131 O O    . HOH   G 3 .   ? -5.213  -15.802 -5.698  1.00 28.65 ?  293 HOH   C O    1 
HETATM 5132 O O    . HOH   G 3 .   ? 4.722   -33.878 -8.402  1.00 39.08 ?  294 HOH   C O    1 
HETATM 5133 O O    . HOH   G 3 .   ? 29.511  -13.698 16.816  1.00 33.04 ?  295 HOH   C O    1 
HETATM 5134 O O    . HOH   G 3 .   ? 14.648  -34.048 -4.933  1.00 29.42 ?  296 HOH   C O    1 
HETATM 5135 O O    . HOH   G 3 .   ? 27.969  -35.679 0.245   1.00 36.74 ?  297 HOH   C O    1 
HETATM 5136 O O    . HOH   G 3 .   ? 0.884   -32.172 -5.925  1.00 31.43 ?  298 HOH   C O    1 
HETATM 5137 O O    . HOH   G 3 .   ? 2.470   -18.483 10.194  1.00 27.98 ?  299 HOH   C O    1 
HETATM 5138 O O    . HOH   G 3 .   ? 30.498  -23.182 -2.051  1.00 28.80 ?  300 HOH   C O    1 
HETATM 5139 O O    . HOH   G 3 .   ? 25.295  -33.357 -2.785  1.00 35.48 ?  301 HOH   C O    1 
HETATM 5140 O O    . HOH   G 3 .   ? -3.129  -22.195 -8.685  1.00 33.10 ?  302 HOH   C O    1 
HETATM 5141 O O    . HOH   G 3 .   ? 35.594  -18.308 8.380   1.00 23.15 ?  303 HOH   C O    1 
HETATM 5142 O O    . HOH   G 3 .   ? 28.757  -24.074 14.315  1.00 31.14 ?  304 HOH   C O    1 
HETATM 5143 O O    . HOH   G 3 .   ? 32.961  -13.709 -3.959  1.00 18.35 ?  305 HOH   C O    1 
HETATM 5144 O O    . HOH   G 3 .   ? 10.269  -19.237 10.114  1.00 25.55 ?  306 HOH   C O    1 
HETATM 5145 O O    . HOH   G 3 .   ? 25.574  -16.322 -7.059  1.00 40.70 ?  307 HOH   C O    1 
HETATM 5146 O O    . HOH   G 3 .   ? 17.976  -32.909 16.194  1.00 42.98 ?  308 HOH   C O    1 
HETATM 5147 O O    . HOH   G 3 .   ? 10.827  -25.036 15.335  1.00 32.28 ?  309 HOH   C O    1 
HETATM 5148 O O    . HOH   G 3 .   ? 25.205  -24.844 -10.301 1.00 40.27 ?  310 HOH   C O    1 
HETATM 5149 O O    . HOH   G 3 .   ? 17.393  -18.911 -8.827  1.00 22.75 ?  311 HOH   C O    1 
HETATM 5150 O O    . HOH   G 3 .   ? 13.175  -35.206 9.427   1.00 37.03 ?  312 HOH   C O    1 
HETATM 5151 O O    . HOH   G 3 .   ? 25.948  -8.808  10.624  1.00 36.20 ?  313 HOH   C O    1 
HETATM 5152 O O    . HOH   G 3 .   ? 0.366   -32.772 -11.671 1.00 49.51 ?  314 HOH   C O    1 
HETATM 5153 O O    . HOH   G 3 .   ? 12.862  -15.030 -1.255  1.00 26.16 ?  315 HOH   C O    1 
HETATM 5154 O O    . HOH   G 3 .   ? 3.495   -30.747 -0.190  1.00 37.68 ?  316 HOH   C O    1 
HETATM 5155 O O    . HOH   G 3 .   ? 16.054  -31.896 7.965   1.00 13.13 ?  317 HOH   C O    1 
HETATM 5156 O O    . HOH   G 3 .   ? 11.556  -30.114 12.305  1.00 36.23 ?  318 HOH   C O    1 
HETATM 5157 O O    . HOH   G 3 .   ? 9.162   -19.981 11.954  1.00 41.92 ?  319 HOH   C O    1 
HETATM 5158 O O    . HOH   G 3 .   ? 18.336  -16.571 -7.490  1.00 40.46 ?  320 HOH   C O    1 
HETATM 5159 O O    . HOH   G 3 .   ? 13.156  -12.602 -0.636  1.00 37.96 ?  321 HOH   C O    1 
HETATM 5160 O O    . HOH   G 3 .   ? 22.329  -17.397 17.579  1.00 40.83 ?  322 HOH   C O    1 
HETATM 5161 O O    . HOH   G 3 .   ? 25.707  -27.559 -7.858  1.00 42.45 ?  323 HOH   C O    1 
HETATM 5162 O O    . HOH   G 3 .   ? 24.626  -23.049 -11.239 1.00 38.99 ?  324 HOH   C O    1 
HETATM 5163 O O    . HOH   G 3 .   ? 10.561  -12.315 0.600   1.00 32.34 ?  325 HOH   C O    1 
HETATM 5164 O O    . HOH   G 3 .   ? 16.072  -33.427 -7.200  1.00 38.26 ?  326 HOH   C O    1 
HETATM 5165 O O    . HOH   G 3 .   ? 12.197  -17.363 10.979  1.00 34.45 ?  327 HOH   C O    1 
HETATM 5166 O O    . HOH   G 3 .   ? 0.340   -30.253 1.726   1.00 39.85 ?  328 HOH   C O    1 
HETATM 5167 O O    . HOH   G 3 .   ? 28.766  -20.182 -3.161  1.00 33.36 ?  329 HOH   C O    1 
HETATM 5168 O O    . HOH   G 3 .   ? 27.748  -36.516 2.581   1.00 39.27 ?  330 HOH   C O    1 
HETATM 5169 O O    . HOH   G 3 .   ? 19.694  -33.136 15.192  1.00 34.73 ?  331 HOH   C O    1 
HETATM 5170 O O    . HOH   G 3 .   ? 13.349  -33.357 11.479  1.00 28.75 ?  332 HOH   C O    1 
HETATM 5171 O O    . HOH   G 3 .   ? -5.928  -25.087 -10.107 1.00 36.57 ?  333 HOH   C O    1 
HETATM 5172 O O    . HOH   G 3 .   ? 16.879  -23.873 -12.130 1.00 31.58 ?  334 HOH   C O    1 
HETATM 5173 O O    . HOH   G 3 .   ? 25.515  -18.817 -5.902  1.00 26.91 ?  335 HOH   C O    1 
HETATM 5174 O O    . HOH   G 3 .   ? -5.092  -20.931 -7.797  1.00 38.92 ?  336 HOH   C O    1 
HETATM 5175 O O    . HOH   G 3 .   ? 8.944   -16.409 -6.644  1.00 34.66 ?  337 HOH   C O    1 
HETATM 5176 O O    . HOH   G 3 .   ? -4.945  -24.026 11.463  1.00 53.99 ?  338 HOH   C O    1 
HETATM 5177 O O    . HOH   G 3 .   ? -3.827  -30.264 -3.737  1.00 38.14 ?  339 HOH   C O    1 
HETATM 5178 O O    . HOH   G 3 .   ? 30.785  -20.864 -0.532  1.00 35.43 ?  340 HOH   C O    1 
HETATM 5179 O O    . HOH   G 3 .   ? -2.314  -13.893 8.026   1.00 46.48 ?  341 HOH   C O    1 
HETATM 5180 O O    . HOH   G 3 .   ? 25.785  -35.285 9.233   1.00 32.82 ?  342 HOH   C O    1 
HETATM 5181 O O    . HOH   G 3 .   ? 22.132  -14.015 -7.274  1.00 36.38 ?  343 HOH   C O    1 
HETATM 5182 O O    . HOH   G 3 .   ? -0.694  -14.379 -6.165  1.00 36.46 ?  344 HOH   C O    1 
HETATM 5183 O O    . HOH   G 3 .   ? 13.929  -18.460 13.171  1.00 42.47 ?  345 HOH   C O    1 
HETATM 5184 O O    . HOH   G 3 .   ? 19.809  -34.831 13.601  1.00 32.82 ?  346 HOH   C O    1 
HETATM 5185 O O    . HOH   G 3 .   ? 2.337   -29.596 1.721   1.00 34.83 ?  347 HOH   C O    1 
HETATM 5186 O O    . HOH   G 3 .   ? 6.368   -18.677 12.009  1.00 41.22 ?  348 HOH   C O    1 
HETATM 5187 O O    . HOH   G 3 .   ? 17.657  -12.293 11.118  1.00 35.17 ?  349 HOH   C O    1 
HETATM 5188 O O    . HOH   G 3 .   ? 31.015  -15.295 -5.622  1.00 31.51 ?  350 HOH   C O    1 
HETATM 5189 O O    . HOH   G 3 .   ? 10.527  -15.941 12.441  1.00 41.25 ?  351 HOH   C O    1 
HETATM 5190 O O    . HOH   G 3 .   ? 21.441  -35.475 11.269  1.00 40.75 ?  352 HOH   C O    1 
HETATM 5191 O O    . HOH   G 3 .   ? 21.235  -16.347 -7.498  1.00 38.45 ?  353 HOH   C O    1 
HETATM 5192 O O    . HOH   G 3 .   ? 16.989  -21.337 -12.457 1.00 43.22 ?  354 HOH   C O    1 
HETATM 5193 O O    . HOH   G 3 .   ? 15.216  -16.654 -6.772  1.00 41.14 ?  355 HOH   C O    1 
HETATM 5194 O O    . HOH   G 3 .   ? 14.775  -6.596  3.697   1.00 43.76 ?  356 HOH   C O    1 
HETATM 5195 O O    . HOH   G 3 .   ? 13.769  -19.973 -8.909  1.00 36.37 ?  357 HOH   C O    1 
HETATM 5196 O O    . HOH   G 3 .   ? 28.043  -24.344 -9.682  1.00 45.34 ?  358 HOH   C O    1 
HETATM 5197 O O    . HOH   G 3 .   ? 30.398  -21.119 -6.355  1.00 33.92 ?  359 HOH   C O    1 
HETATM 5198 O O    . HOH   G 3 .   ? 18.354  -25.416 -13.726 1.00 34.48 ?  360 HOH   C O    1 
HETATM 5199 O O    . HOH   G 3 .   ? 18.235  -9.611  11.147  1.00 36.12 ?  361 HOH   C O    1 
HETATM 5200 O O    . HOH   G 3 .   ? 11.119  -21.089 -12.034 1.00 39.26 ?  362 HOH   C O    1 
HETATM 5201 O O    . HOH   G 3 .   ? 13.793  -21.620 -11.104 1.00 35.36 ?  363 HOH   C O    1 
HETATM 5202 O O    . HOH   H 3 .   ? -22.271 -18.646 -30.714 1.00 35.23 ?  201 HOH   D O    1 
HETATM 5203 O O    . HOH   H 3 .   ? 10.376  -15.079 -25.181 1.00 39.68 ?  202 HOH   D O    1 
HETATM 5204 O O    . HOH   H 3 .   ? 7.019   -18.568 -30.297 1.00 29.27 ?  203 HOH   D O    1 
HETATM 5205 O O    . HOH   H 3 .   ? 6.683   -16.213 -35.869 1.00 35.87 ?  204 HOH   D O    1 
HETATM 5206 O O    . HOH   H 3 .   ? -32.207 -0.061  -26.982 1.00 31.30 ?  205 HOH   D O    1 
HETATM 5207 O O    . HOH   H 3 .   ? 4.675   -0.537  -34.785 1.00 30.38 ?  206 HOH   D O    1 
HETATM 5208 O O    . HOH   H 3 .   ? -27.665 -7.876  -43.146 1.00 35.90 ?  207 HOH   D O    1 
HETATM 5209 O O    . HOH   H 3 .   ? -11.157 -24.617 -22.962 1.00 34.57 ?  208 HOH   D O    1 
HETATM 5210 O O    . HOH   H 3 .   ? -19.628 -6.406  -22.178 1.00 36.29 ?  209 HOH   D O    1 
HETATM 5211 O O    . HOH   H 3 .   ? -21.047 -20.428 -32.503 1.00 38.43 ?  210 HOH   D O    1 
HETATM 5212 O O    . HOH   H 3 .   ? 6.480   -15.351 -34.092 1.00 32.44 ?  211 HOH   D O    1 
HETATM 5213 O O    . HOH   H 3 .   ? -1.495  -8.925  -44.140 1.00 36.84 ?  212 HOH   D O    1 
HETATM 5214 O O    . HOH   H 3 .   ? -19.691 -15.710 -22.596 1.00 27.31 ?  213 HOH   D O    1 
HETATM 5215 O O    . HOH   H 3 .   ? -20.878 -16.257 -30.398 1.00 15.68 ?  214 HOH   D O    1 
HETATM 5216 O O    . HOH   H 3 .   ? -23.071 -2.546  -28.085 1.00 29.83 ?  215 HOH   D O    1 
HETATM 5217 O O    . HOH   H 3 .   ? 6.179   -19.923 -22.264 1.00 39.00 ?  216 HOH   D O    1 
HETATM 5218 O O    . HOH   H 3 .   ? 1.268   -7.943  -31.330 1.00 26.08 ?  217 HOH   D O    1 
HETATM 5219 O O    . HOH   H 3 .   ? -12.556 -21.767 -33.668 1.00 29.82 ?  218 HOH   D O    1 
HETATM 5220 O O    . HOH   H 3 .   ? 2.618   -5.004  -14.753 1.00 39.57 ?  219 HOH   D O    1 
HETATM 5221 O O    . HOH   H 3 .   ? -12.388 -21.751 -25.020 1.00 35.01 ?  220 HOH   D O    1 
HETATM 5222 O O    . HOH   H 3 .   ? -15.785 -24.827 -46.432 1.00 41.90 ?  221 HOH   D O    1 
HETATM 5223 O O    . HOH   H 3 .   ? -13.170 -21.402 -43.437 1.00 24.37 ?  222 HOH   D O    1 
HETATM 5224 O O    . HOH   H 3 .   ? -3.945  -20.273 -18.416 1.00 34.61 ?  223 HOH   D O    1 
HETATM 5225 O O    . HOH   H 3 .   ? -7.122  -1.323  -29.350 1.00 35.61 ?  224 HOH   D O    1 
HETATM 5226 O O    . HOH   H 3 .   ? -6.625  -5.085  -20.012 1.00 31.05 ?  225 HOH   D O    1 
HETATM 5227 O O    . HOH   H 3 .   ? -18.089 -17.930 -21.599 1.00 32.63 ?  226 HOH   D O    1 
HETATM 5228 O O    . HOH   H 3 .   ? -22.435 0.128   -28.170 1.00 41.60 ?  227 HOH   D O    1 
HETATM 5229 O O    . HOH   H 3 .   ? -1.623  -16.254 -37.381 1.00 26.78 ?  228 HOH   D O    1 
HETATM 5230 O O    . HOH   H 3 .   ? -14.403 -22.855 -32.538 1.00 30.84 ?  229 HOH   D O    1 
HETATM 5231 O O    . HOH   H 3 .   ? -27.055 -16.805 -41.506 1.00 42.66 ?  230 HOH   D O    1 
HETATM 5232 O O    . HOH   H 3 .   ? -33.676 -13.847 -27.778 1.00 35.33 ?  231 HOH   D O    1 
HETATM 5233 O O    . HOH   H 3 .   ? -19.825 -15.447 -46.235 1.00 38.33 ?  232 HOH   D O    1 
HETATM 5234 O O    . HOH   H 3 .   ? -27.058 1.069   -21.380 1.00 41.14 ?  233 HOH   D O    1 
HETATM 5235 O O    . HOH   H 3 .   ? -0.669  -6.622  -21.596 1.00 28.32 ?  234 HOH   D O    1 
HETATM 5236 O O    . HOH   H 3 .   ? -20.884 -5.957  -42.378 1.00 30.32 ?  235 HOH   D O    1 
HETATM 5237 O O    . HOH   H 3 .   ? -0.098  2.065   -28.482 1.00 35.14 ?  236 HOH   D O    1 
HETATM 5238 O O    . HOH   H 3 .   ? -12.194 -27.282 -19.650 1.00 26.81 ?  237 HOH   D O    1 
HETATM 5239 O O    . HOH   H 3 .   ? -3.183  -5.712  -37.670 1.00 27.19 ?  238 HOH   D O    1 
HETATM 5240 O O    . HOH   H 3 .   ? -1.390  -15.514 -34.793 1.00 19.88 ?  239 HOH   D O    1 
HETATM 5241 O O    . HOH   H 3 .   ? -26.436 -10.189 -42.896 1.00 30.12 ?  240 HOH   D O    1 
HETATM 5242 O O    . HOH   H 3 .   ? -32.901 -15.303 -32.229 1.00 25.20 ?  241 HOH   D O    1 
HETATM 5243 O O    . HOH   H 3 .   ? 0.635   -9.815  -23.262 1.00 26.67 ?  242 HOH   D O    1 
HETATM 5244 O O    . HOH   H 3 .   ? 7.080   -12.259 -21.789 1.00 38.59 ?  243 HOH   D O    1 
HETATM 5245 O O    . HOH   H 3 .   ? -24.016 -2.570  -37.888 1.00 25.53 ?  244 HOH   D O    1 
HETATM 5246 O O    . HOH   H 3 .   ? -4.308  -16.581 -42.156 1.00 27.39 ?  245 HOH   D O    1 
HETATM 5247 O O    . HOH   H 3 .   ? -4.669  -14.518 -45.902 1.00 31.57 ?  246 HOH   D O    1 
HETATM 5248 O O    . HOH   H 3 .   ? -11.633 -8.984  -39.404 1.00 22.37 ?  247 HOH   D O    1 
HETATM 5249 O O    . HOH   H 3 .   ? -18.779 -6.887  -39.880 1.00 31.64 ?  248 HOH   D O    1 
HETATM 5250 O O    . HOH   H 3 .   ? -25.811 -20.134 -30.437 1.00 49.77 ?  249 HOH   D O    1 
HETATM 5251 O O    . HOH   H 3 .   ? -31.613 -4.956  -22.684 1.00 41.29 ?  250 HOH   D O    1 
HETATM 5252 O O    . HOH   H 3 .   ? -22.666 -12.123 -22.193 1.00 33.13 ?  251 HOH   D O    1 
HETATM 5253 O O    . HOH   H 3 .   ? -27.080 -19.163 -37.458 1.00 36.59 ?  252 HOH   D O    1 
HETATM 5254 O O    . HOH   H 3 .   ? -10.268 -7.328  -37.571 1.00 19.67 ?  253 HOH   D O    1 
HETATM 5255 O O    . HOH   H 3 .   ? 9.101   -8.330  -23.391 1.00 40.86 ?  254 HOH   D O    1 
HETATM 5256 O O    . HOH   H 3 .   ? -16.149 -7.169  -42.729 1.00 34.34 ?  255 HOH   D O    1 
HETATM 5257 O O    . HOH   H 3 .   ? -3.786  -8.635  -18.907 1.00 40.37 ?  256 HOH   D O    1 
HETATM 5258 O O    . HOH   H 3 .   ? -13.524 -5.570  -23.796 1.00 36.17 ?  257 HOH   D O    1 
HETATM 5259 O O    . HOH   H 3 .   ? -9.418  -22.416 -28.259 1.00 34.32 ?  258 HOH   D O    1 
HETATM 5260 O O    . HOH   H 3 .   ? -9.077  -23.037 -25.743 1.00 37.22 ?  259 HOH   D O    1 
HETATM 5261 O O    . HOH   H 3 .   ? -29.923 -5.960  -34.492 1.00 30.00 ?  260 HOH   D O    1 
HETATM 5262 O O    . HOH   H 3 .   ? -24.265 -9.167  -23.196 1.00 32.07 ?  261 HOH   D O    1 
HETATM 5263 O O    . HOH   H 3 .   ? -28.718 -11.469 -42.502 1.00 29.25 ?  262 HOH   D O    1 
HETATM 5264 O O    . HOH   H 3 .   ? -20.597 -20.692 -34.928 1.00 38.40 ?  263 HOH   D O    1 
HETATM 5265 O O    . HOH   H 3 .   ? 5.208   -13.483 -20.530 1.00 36.52 ?  264 HOH   D O    1 
HETATM 5266 O O    . HOH   H 3 .   ? -17.977 -11.159 -21.515 1.00 35.79 ?  265 HOH   D O    1 
HETATM 5267 O O    . HOH   H 3 .   ? -1.716  -8.117  -19.674 1.00 42.50 ?  266 HOH   D O    1 
HETATM 5268 O O    . HOH   H 3 .   ? -4.146  -10.237 -16.635 1.00 31.18 ?  267 HOH   D O    1 
HETATM 5269 O O    . HOH   H 3 .   ? -17.342 -12.458 -46.606 1.00 29.86 ?  268 HOH   D O    1 
HETATM 5270 O O    . HOH   H 3 .   ? -7.889  -4.866  -39.205 1.00 38.20 ?  269 HOH   D O    1 
HETATM 5271 O O    . HOH   H 3 .   ? -15.568 -1.725  -31.390 1.00 43.81 ?  270 HOH   D O    1 
HETATM 5272 O O    . HOH   H 3 .   ? -31.866 -4.221  -38.841 1.00 41.01 ?  271 HOH   D O    1 
HETATM 5273 O O    . HOH   H 3 .   ? -2.113  -23.734 -32.266 1.00 32.86 ?  272 HOH   D O    1 
HETATM 5274 O O    . HOH   H 3 .   ? -27.453 -19.431 -40.110 1.00 37.93 ?  273 HOH   D O    1 
HETATM 5275 O O    . HOH   H 3 .   ? 2.227   -9.479  -36.593 1.00 32.66 ?  274 HOH   D O    1 
HETATM 5276 O O    . HOH   H 3 .   ? -8.211  -6.736  -41.153 1.00 24.25 ?  275 HOH   D O    1 
HETATM 5277 O O    . HOH   H 3 .   ? 6.472   -2.491  -35.426 1.00 22.59 ?  276 HOH   D O    1 
HETATM 5278 O O    . HOH   H 3 .   ? -20.259 -18.675 -46.214 1.00 32.01 ?  277 HOH   D O    1 
HETATM 5279 O O    . HOH   H 3 .   ? 5.921   -6.492  -32.328 1.00 27.35 ?  278 HOH   D O    1 
HETATM 5280 O O    . HOH   H 3 .   ? -9.471  -4.457  -36.560 1.00 35.43 ?  279 HOH   D O    1 
HETATM 5281 O O    . HOH   H 3 .   ? -15.315 -14.686 -46.823 1.00 34.68 ?  280 HOH   D O    1 
HETATM 5282 O O    . HOH   H 3 .   ? -8.323  -7.489  -19.318 1.00 34.00 ?  281 HOH   D O    1 
HETATM 5283 O O    . HOH   H 3 .   ? -30.208 -4.073  -36.666 1.00 38.70 ?  282 HOH   D O    1 
HETATM 5284 O O    . HOH   H 3 .   ? -17.184 -3.111  -29.592 1.00 28.20 ?  283 HOH   D O    1 
HETATM 5285 O O    . HOH   H 3 .   ? 2.656   -7.735  -35.246 1.00 38.42 ?  284 HOH   D O    1 
HETATM 5286 O O    . HOH   H 3 .   ? -31.456 -9.486  -40.185 1.00 27.05 ?  285 HOH   D O    1 
HETATM 5287 O O    . HOH   H 3 .   ? -25.020 -20.172 -39.290 1.00 32.57 ?  286 HOH   D O    1 
HETATM 5288 O O    . HOH   H 3 .   ? -25.301 -17.757 -41.967 1.00 37.18 ?  287 HOH   D O    1 
HETATM 5289 O O    . HOH   H 3 .   ? 1.079   -19.144 -35.944 1.00 40.45 ?  288 HOH   D O    1 
HETATM 5290 O O    . HOH   H 3 .   ? -17.155 -4.912  -39.300 1.00 42.28 ?  289 HOH   D O    1 
HETATM 5291 O O    . HOH   H 3 .   ? 4.253   -7.842  -31.460 1.00 27.93 ?  290 HOH   D O    1 
HETATM 5292 O O    . HOH   H 3 .   ? 2.962   -5.295  -35.275 1.00 26.48 ?  291 HOH   D O    1 
HETATM 5293 O O    . HOH   H 3 .   ? 3.158   -21.571 -35.488 1.00 38.87 ?  292 HOH   D O    1 
HETATM 5294 O O    . HOH   H 3 .   ? -25.806 -19.255 -33.119 1.00 38.94 ?  293 HOH   D O    1 
HETATM 5295 O O    . HOH   H 3 .   ? -13.214 -4.129  -33.577 1.00 31.43 ?  294 HOH   D O    1 
HETATM 5296 O O    . HOH   H 3 .   ? 5.049   -16.318 -38.393 1.00 40.99 ?  295 HOH   D O    1 
HETATM 5297 O O    . HOH   H 3 .   ? -16.320 -9.941  -22.681 1.00 34.89 ?  296 HOH   D O    1 
HETATM 5298 O O    . HOH   H 3 .   ? -24.737 -19.608 -17.029 1.00 35.76 ?  297 HOH   D O    1 
HETATM 5299 O O    . HOH   H 3 .   ? 2.526   -0.440  -35.719 1.00 38.11 ?  298 HOH   D O    1 
HETATM 5300 O O    . HOH   H 3 .   ? -14.589 -6.285  -41.359 1.00 45.59 ?  299 HOH   D O    1 
HETATM 5301 O O    . HOH   H 3 .   ? -2.338  -6.934  -44.620 1.00 41.15 ?  300 HOH   D O    1 
HETATM 5302 O O    . HOH   H 3 .   ? 1.255   -4.743  -38.414 1.00 42.29 ?  301 HOH   D O    1 
HETATM 5303 O O    . HOH   H 3 .   ? -13.709 -1.589  -32.417 1.00 39.50 ?  302 HOH   D O    1 
HETATM 5304 O O    . HOH   H 3 .   ? -23.730 -18.871 -34.036 1.00 35.60 ?  303 HOH   D O    1 
HETATM 5305 O O    . HOH   H 3 .   ? -26.629 -8.450  -49.383 1.00 40.36 ?  304 HOH   D O    1 
HETATM 5306 O O    . HOH   H 3 .   ? -0.863  -6.543  -37.881 1.00 34.30 ?  305 HOH   D O    1 
HETATM 5307 O O    . HOH   H 3 .   ? -1.816  -18.462 -38.617 1.00 36.45 ?  306 HOH   D O    1 
HETATM 5308 O O    . HOH   H 3 .   ? -25.979 -9.927  -45.672 1.00 31.62 ?  307 HOH   D O    1 
HETATM 5309 O O    . HOH   H 3 .   ? -2.156  -17.801 -41.620 1.00 36.05 ?  308 HOH   D O    1 
HETATM 5310 O O    . HOH   H 3 .   ? -8.691  -11.251 -45.398 1.00 25.55 ?  309 HOH   D O    1 
HETATM 5311 O O    . HOH   H 3 .   ? -12.682 -7.802  -41.454 1.00 39.27 ?  310 HOH   D O    1 
HETATM 5312 O O    . HOH   H 3 .   ? -26.721 -2.655  -38.656 1.00 40.03 ?  311 HOH   D O    1 
HETATM 5313 O O    . HOH   H 3 .   ? -30.024 -7.038  -41.072 1.00 34.94 ?  312 HOH   D O    1 
HETATM 5314 O O    . HOH   H 3 .   ? 9.069   -20.442 -22.572 1.00 40.84 ?  313 HOH   D O    1 
HETATM 5315 O O    . HOH   H 3 .   ? -27.171 -18.307 -17.348 1.00 32.98 ?  314 HOH   D O    1 
HETATM 5316 O O    . HOH   H 3 .   ? -20.257 -3.658  -43.192 1.00 47.75 ?  315 HOH   D O    1 
HETATM 5317 O O    . HOH   H 3 .   ? -28.589 -13.815 -43.736 1.00 41.21 ?  316 HOH   D O    1 
HETATM 5318 O O    . HOH   H 3 .   ? 0.993   -6.153  -12.789 1.00 51.52 ?  317 HOH   D O    1 
HETATM 5319 O O    . HOH   H 3 .   ? 2.217   -10.871 -41.943 1.00 42.61 ?  318 HOH   D O    1 
HETATM 5320 O O    . HOH   H 3 .   ? -5.192  -16.906 -46.470 1.00 35.69 ?  319 HOH   D O    1 
HETATM 5321 O O    . HOH   H 3 .   ? -8.050  -25.457 -25.928 1.00 44.48 ?  320 HOH   D O    1 
HETATM 5322 O O    . HOH   H 3 .   ? -5.701  -18.111 -44.015 1.00 26.45 ?  321 HOH   D O    1 
HETATM 5323 O O    . HOH   H 3 .   ? 2.905   -7.021  -37.366 1.00 33.42 ?  322 HOH   D O    1 
HETATM 5324 O O    . HOH   H 3 .   ? -2.860  -21.273 -38.088 1.00 36.35 ?  323 HOH   D O    1 
# 
