data_9NB7
# 
_entry.id   9NB7 
# 
_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   9NB7         pdb_00009nb7 10.2210/pdb9nb7/pdb 
WWPDB D_1000292969 ?            ?                   
# 
_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       2025-03-26 
_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                        9NB7 
_pdbx_database_status.recvd_initial_deposition_date   2025-02-13 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_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 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB 'MicroED structure of the same protein in apo-form'                       9NAG unspecified 
PDB 'SSX structure of the same protein complexed with a different ligand'     9NB4 unspecified 
PDB 'MicroED structure of the same protein complexed with a different ligand' 9NAE unspecified 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.email              jrodriguez@mbi.ucla.edu 
_pdbx_contact_author.name_first         Jose 
_pdbx_contact_author.name_last          Rodriguez 
_pdbx_contact_author.name_mi            A 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-0248-4964 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Vlahakis, N.W.'  1 0000-0002-5092-0265 
'Summers, J.A.'   2 ?                   
'Wakatsuki, S.'   3 ?                   
'Rodriguez, J.A.' 4 0000-0002-0248-4964 
# 
_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                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Biorxiv 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2692-8205 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
'Combining MicroED and native mass spectrometry for structural discovery of enzyme-biosynthetic inhibitor complexes.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1101/2025.02.20.638743 
_citation.pdbx_database_id_PubMed   40060639 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Vlahakis, N.W.'  1  0000-0002-5092-0265 
primary 'Flowers, C.W.'   2  ?                   
primary 'Liu, M.'         3  ?                   
primary 'Agdanowski, M.'  4  ?                   
primary 'Johnson, S.'     5  ?                   
primary 'Summers, J.A.'   6  ?                   
primary 'Keyser, C.'      7  ?                   
primary 'Russell, P.'     8  ?                   
primary 'Rose, S.'        9  ?                   
primary 'Orlans, J.'      10 ?                   
primary 'Adhami, N.'      11 ?                   
primary 'Chen, Y.'        12 ?                   
primary 'Sawaya, M.R.'    13 ?                   
primary 'Basu, S.'        14 ?                   
primary 'de Sanctis, D.'  15 ?                   
primary 'Wakatsuki, S.'   16 ?                   
primary 'Nelson, H.M.'    17 ?                   
primary 'Loo, J.A.'       18 ?                   
primary 'Tang, Y.'        19 ?                   
primary 'Rodriguez, J.A.' 20 0000-0002-0248-4964 
# 
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     nat Papain                                                                                                     
23452.301 1  3.4.22.2 ? ? ? 
2 non-polymer syn '(3R)-4-({(2S)-1-[(5-acetamidopentyl)amino]-1-oxo-3-phenylpropan-2-yl}amino)-3-hydroxy-4-oxobutanoic acid' 
407.461   1  ?        ? ? ? 
3 water       nat water                                                                                                      
18.015    79 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Papaya proteinase I,PPI' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;IPEYVDWRQKGAVTPVKNQGSCGSCWAFSAVVTIEGIIKIRTGNLNEYSEQELLDCDRRSYGCNGGYPWSALQLVAQYGI
HYRNTYPYEGVQRYCRSREKGPYAAKTDGVRQVQPYNEGALLYSIANQPVSVVLEAAGKDFQLYRGGIFVGPCGNKVDHA
VAAVGYGPNYILIKNSWGTGWGENGYIRIKRGTGNSYGVCGLYTSSFYPVKN
;
_entity_poly.pdbx_seq_one_letter_code_can   
;IPEYVDWRQKGAVTPVKNQGSCGSCWAFSAVVTIEGIIKIRTGNLNEYSEQELLDCDRRSYGCNGGYPWSALQLVAQYGI
HYRNTYPYEGVQRYCRSREKGPYAAKTDGVRQVQPYNEGALLYSIANQPVSVVLEAAGKDFQLYRGGIFVGPCGNKVDHA
VAAVGYGPNYILIKNSWGTGWGENGYIRIKRGTGNSYGVCGLYTSSFYPVKN
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '(3R)-4-({(2S)-1-[(5-acetamidopentyl)amino]-1-oxo-3-phenylpropan-2-yl}amino)-3-hydroxy-4-oxobutanoic acid' A1BWT 
3 water                                                                                                      HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ILE n 
1 2   PRO n 
1 3   GLU n 
1 4   TYR n 
1 5   VAL n 
1 6   ASP n 
1 7   TRP n 
1 8   ARG n 
1 9   GLN n 
1 10  LYS n 
1 11  GLY n 
1 12  ALA n 
1 13  VAL n 
1 14  THR n 
1 15  PRO n 
1 16  VAL n 
1 17  LYS n 
1 18  ASN n 
1 19  GLN n 
1 20  GLY n 
1 21  SER n 
1 22  CYS n 
1 23  GLY n 
1 24  SER n 
1 25  CYS n 
1 26  TRP n 
1 27  ALA n 
1 28  PHE n 
1 29  SER n 
1 30  ALA n 
1 31  VAL n 
1 32  VAL n 
1 33  THR n 
1 34  ILE n 
1 35  GLU n 
1 36  GLY n 
1 37  ILE n 
1 38  ILE n 
1 39  LYS n 
1 40  ILE n 
1 41  ARG n 
1 42  THR n 
1 43  GLY n 
1 44  ASN n 
1 45  LEU n 
1 46  ASN n 
1 47  GLU n 
1 48  TYR n 
1 49  SER n 
1 50  GLU n 
1 51  GLN n 
1 52  GLU n 
1 53  LEU n 
1 54  LEU n 
1 55  ASP n 
1 56  CYS n 
1 57  ASP n 
1 58  ARG n 
1 59  ARG n 
1 60  SER n 
1 61  TYR n 
1 62  GLY n 
1 63  CYS n 
1 64  ASN n 
1 65  GLY n 
1 66  GLY n 
1 67  TYR n 
1 68  PRO n 
1 69  TRP n 
1 70  SER n 
1 71  ALA n 
1 72  LEU n 
1 73  GLN n 
1 74  LEU n 
1 75  VAL n 
1 76  ALA n 
1 77  GLN n 
1 78  TYR n 
1 79  GLY n 
1 80  ILE n 
1 81  HIS n 
1 82  TYR n 
1 83  ARG n 
1 84  ASN n 
1 85  THR n 
1 86  TYR n 
1 87  PRO n 
1 88  TYR n 
1 89  GLU n 
1 90  GLY n 
1 91  VAL n 
1 92  GLN n 
1 93  ARG n 
1 94  TYR n 
1 95  CYS n 
1 96  ARG n 
1 97  SER n 
1 98  ARG n 
1 99  GLU n 
1 100 LYS n 
1 101 GLY n 
1 102 PRO n 
1 103 TYR n 
1 104 ALA n 
1 105 ALA n 
1 106 LYS n 
1 107 THR n 
1 108 ASP n 
1 109 GLY n 
1 110 VAL n 
1 111 ARG n 
1 112 GLN n 
1 113 VAL n 
1 114 GLN n 
1 115 PRO n 
1 116 TYR n 
1 117 ASN n 
1 118 GLU n 
1 119 GLY n 
1 120 ALA n 
1 121 LEU n 
1 122 LEU n 
1 123 TYR n 
1 124 SER n 
1 125 ILE n 
1 126 ALA n 
1 127 ASN n 
1 128 GLN n 
1 129 PRO n 
1 130 VAL n 
1 131 SER n 
1 132 VAL n 
1 133 VAL n 
1 134 LEU n 
1 135 GLU n 
1 136 ALA n 
1 137 ALA n 
1 138 GLY n 
1 139 LYS n 
1 140 ASP n 
1 141 PHE n 
1 142 GLN n 
1 143 LEU n 
1 144 TYR n 
1 145 ARG n 
1 146 GLY n 
1 147 GLY n 
1 148 ILE n 
1 149 PHE n 
1 150 VAL n 
1 151 GLY n 
1 152 PRO n 
1 153 CYS n 
1 154 GLY n 
1 155 ASN n 
1 156 LYS n 
1 157 VAL n 
1 158 ASP n 
1 159 HIS n 
1 160 ALA n 
1 161 VAL n 
1 162 ALA n 
1 163 ALA n 
1 164 VAL n 
1 165 GLY n 
1 166 TYR n 
1 167 GLY n 
1 168 PRO n 
1 169 ASN n 
1 170 TYR n 
1 171 ILE n 
1 172 LEU n 
1 173 ILE n 
1 174 LYS n 
1 175 ASN n 
1 176 SER n 
1 177 TRP n 
1 178 GLY n 
1 179 THR n 
1 180 GLY n 
1 181 TRP n 
1 182 GLY n 
1 183 GLU n 
1 184 ASN n 
1 185 GLY n 
1 186 TYR n 
1 187 ILE n 
1 188 ARG n 
1 189 ILE n 
1 190 LYS n 
1 191 ARG n 
1 192 GLY n 
1 193 THR n 
1 194 GLY n 
1 195 ASN n 
1 196 SER n 
1 197 TYR n 
1 198 GLY n 
1 199 VAL n 
1 200 CYS n 
1 201 GLY n 
1 202 LEU n 
1 203 TYR n 
1 204 THR n 
1 205 SER n 
1 206 SER n 
1 207 PHE n 
1 208 TYR n 
1 209 PRO n 
1 210 VAL n 
1 211 LYS n 
1 212 ASN n 
# 
_entity_src_nat.entity_id                  1 
_entity_src_nat.pdbx_src_id                1 
_entity_src_nat.pdbx_alt_source_flag       sample 
_entity_src_nat.pdbx_beg_seq_num           1 
_entity_src_nat.pdbx_end_seq_num           212 
_entity_src_nat.common_name                papaya 
_entity_src_nat.pdbx_organism_scientific   'Carica papaya' 
_entity_src_nat.pdbx_ncbi_taxonomy_id      3649 
_entity_src_nat.genus                      ? 
_entity_src_nat.species                    ? 
_entity_src_nat.strain                     ? 
_entity_src_nat.tissue                     ? 
_entity_src_nat.tissue_fraction            ? 
_entity_src_nat.pdbx_secretion             ? 
_entity_src_nat.pdbx_fragment              ? 
_entity_src_nat.pdbx_variant               ? 
_entity_src_nat.pdbx_cell_line             ? 
_entity_src_nat.pdbx_atcc                  ? 
_entity_src_nat.pdbx_cellular_location     ? 
_entity_src_nat.pdbx_organ                 ? 
_entity_src_nat.pdbx_organelle             ? 
_entity_src_nat.pdbx_cell                  ? 
_entity_src_nat.pdbx_plasmid_name          ? 
_entity_src_nat.pdbx_plasmid_details       ? 
_entity_src_nat.details                    ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1BWT non-polymer         . 
'(3R)-4-({(2S)-1-[(5-acetamidopentyl)amino]-1-oxo-3-phenylpropan-2-yl}amino)-3-hydroxy-4-oxobutanoic acid' ? 'C20 H29 N3 O6'  
407.461 
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 
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   ILE 1   1   1   ILE ILE A . n 
A 1 2   PRO 2   2   2   PRO PRO A . n 
A 1 3   GLU 3   3   3   GLU GLU A . n 
A 1 4   TYR 4   4   4   TYR TYR A . n 
A 1 5   VAL 5   5   5   VAL VAL A . n 
A 1 6   ASP 6   6   6   ASP ASP A . n 
A 1 7   TRP 7   7   7   TRP TRP A . n 
A 1 8   ARG 8   8   8   ARG ARG A . n 
A 1 9   GLN 9   9   9   GLN GLN A . n 
A 1 10  LYS 10  10  10  LYS LYS A . n 
A 1 11  GLY 11  11  11  GLY GLY A . n 
A 1 12  ALA 12  12  12  ALA ALA A . n 
A 1 13  VAL 13  13  13  VAL VAL A . n 
A 1 14  THR 14  14  14  THR THR A . n 
A 1 15  PRO 15  15  15  PRO PRO A . n 
A 1 16  VAL 16  16  16  VAL VAL A . n 
A 1 17  LYS 17  17  17  LYS LYS A . n 
A 1 18  ASN 18  18  18  ASN ASN A . n 
A 1 19  GLN 19  19  19  GLN GLN A . n 
A 1 20  GLY 20  20  20  GLY GLY A . n 
A 1 21  SER 21  21  21  SER SER A . n 
A 1 22  CYS 22  22  22  CYS CYS A . n 
A 1 23  GLY 23  23  23  GLY GLY A . n 
A 1 24  SER 24  24  24  SER SER A . n 
A 1 25  CYS 25  25  25  CYS CYS A . n 
A 1 26  TRP 26  26  26  TRP TRP A . n 
A 1 27  ALA 27  27  27  ALA ALA A . n 
A 1 28  PHE 28  28  28  PHE PHE A . n 
A 1 29  SER 29  29  29  SER SER A . n 
A 1 30  ALA 30  30  30  ALA ALA A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  VAL 32  32  32  VAL VAL A . n 
A 1 33  THR 33  33  33  THR THR A . n 
A 1 34  ILE 34  34  34  ILE ILE A . n 
A 1 35  GLU 35  35  35  GLU GLU A . n 
A 1 36  GLY 36  36  36  GLY GLY A . n 
A 1 37  ILE 37  37  37  ILE ILE A . n 
A 1 38  ILE 38  38  38  ILE ILE A . n 
A 1 39  LYS 39  39  39  LYS LYS A . n 
A 1 40  ILE 40  40  40  ILE ILE A . n 
A 1 41  ARG 41  41  41  ARG ARG A . n 
A 1 42  THR 42  42  42  THR THR A . n 
A 1 43  GLY 43  43  43  GLY GLY A . n 
A 1 44  ASN 44  44  44  ASN ASN A . n 
A 1 45  LEU 45  45  45  LEU LEU A . n 
A 1 46  ASN 46  46  46  ASN ASN A . n 
A 1 47  GLU 47  47  47  GLU GLU A . n 
A 1 48  TYR 48  48  48  TYR TYR A . n 
A 1 49  SER 49  49  49  SER SER A . n 
A 1 50  GLU 50  50  50  GLU GLU A . n 
A 1 51  GLN 51  51  51  GLN GLN A . n 
A 1 52  GLU 52  52  52  GLU GLU A . n 
A 1 53  LEU 53  53  53  LEU LEU A . n 
A 1 54  LEU 54  54  54  LEU LEU A . n 
A 1 55  ASP 55  55  55  ASP ASP A . n 
A 1 56  CYS 56  56  56  CYS CYS A . n 
A 1 57  ASP 57  57  57  ASP ASP A . n 
A 1 58  ARG 58  58  58  ARG ARG A . n 
A 1 59  ARG 59  59  59  ARG ARG A . n 
A 1 60  SER 60  60  60  SER SER A . n 
A 1 61  TYR 61  61  61  TYR TYR A . n 
A 1 62  GLY 62  62  62  GLY GLY A . n 
A 1 63  CYS 63  63  63  CYS CYS A . n 
A 1 64  ASN 64  64  64  ASN ASN A . n 
A 1 65  GLY 65  65  65  GLY GLY A . n 
A 1 66  GLY 66  66  66  GLY GLY A . n 
A 1 67  TYR 67  67  67  TYR TYR A . n 
A 1 68  PRO 68  68  68  PRO PRO A . n 
A 1 69  TRP 69  69  69  TRP TRP A . n 
A 1 70  SER 70  70  70  SER SER A . n 
A 1 71  ALA 71  71  71  ALA ALA A . n 
A 1 72  LEU 72  72  72  LEU LEU A . n 
A 1 73  GLN 73  73  73  GLN GLN A . n 
A 1 74  LEU 74  74  74  LEU LEU A . n 
A 1 75  VAL 75  75  75  VAL VAL A . n 
A 1 76  ALA 76  76  76  ALA ALA A . n 
A 1 77  GLN 77  77  77  GLN GLN A . n 
A 1 78  TYR 78  78  78  TYR TYR A . n 
A 1 79  GLY 79  79  79  GLY GLY A . n 
A 1 80  ILE 80  80  80  ILE ILE A . n 
A 1 81  HIS 81  81  81  HIS HIS A . n 
A 1 82  TYR 82  82  82  TYR TYR A . n 
A 1 83  ARG 83  83  83  ARG ARG A . n 
A 1 84  ASN 84  84  84  ASN ASN A . n 
A 1 85  THR 85  85  85  THR THR A . n 
A 1 86  TYR 86  86  86  TYR TYR A . n 
A 1 87  PRO 87  87  87  PRO PRO A . n 
A 1 88  TYR 88  88  88  TYR TYR A . n 
A 1 89  GLU 89  89  89  GLU GLU A . n 
A 1 90  GLY 90  90  90  GLY GLY A . n 
A 1 91  VAL 91  91  91  VAL VAL A . n 
A 1 92  GLN 92  92  92  GLN GLN A . n 
A 1 93  ARG 93  93  93  ARG ARG A . n 
A 1 94  TYR 94  94  94  TYR TYR A . n 
A 1 95  CYS 95  95  95  CYS CYS A . n 
A 1 96  ARG 96  96  96  ARG ARG A . n 
A 1 97  SER 97  97  97  SER SER A . n 
A 1 98  ARG 98  98  98  ARG ARG A . n 
A 1 99  GLU 99  99  99  GLU GLU A . n 
A 1 100 LYS 100 100 100 LYS LYS A . n 
A 1 101 GLY 101 101 101 GLY GLY A . n 
A 1 102 PRO 102 102 102 PRO PRO A . n 
A 1 103 TYR 103 103 103 TYR TYR A . n 
A 1 104 ALA 104 104 104 ALA ALA A . n 
A 1 105 ALA 105 105 105 ALA ALA A . n 
A 1 106 LYS 106 106 106 LYS LYS A . n 
A 1 107 THR 107 107 107 THR THR A . n 
A 1 108 ASP 108 108 108 ASP ASP A . n 
A 1 109 GLY 109 109 109 GLY GLY A . n 
A 1 110 VAL 110 110 110 VAL VAL A . n 
A 1 111 ARG 111 111 111 ARG ARG A . n 
A 1 112 GLN 112 112 112 GLN GLN A . n 
A 1 113 VAL 113 113 113 VAL VAL A . n 
A 1 114 GLN 114 114 114 GLN GLN A . n 
A 1 115 PRO 115 115 115 PRO PRO A . n 
A 1 116 TYR 116 116 116 TYR TYR A . n 
A 1 117 ASN 117 117 117 ASN ASN A . n 
A 1 118 GLU 118 118 118 GLU GLU A . n 
A 1 119 GLY 119 119 119 GLY GLY A . n 
A 1 120 ALA 120 120 120 ALA ALA A . n 
A 1 121 LEU 121 121 121 LEU LEU A . n 
A 1 122 LEU 122 122 122 LEU LEU A . n 
A 1 123 TYR 123 123 123 TYR TYR A . n 
A 1 124 SER 124 124 124 SER SER A . n 
A 1 125 ILE 125 125 125 ILE ILE A . n 
A 1 126 ALA 126 126 126 ALA ALA A . n 
A 1 127 ASN 127 127 127 ASN ASN A . n 
A 1 128 GLN 128 128 128 GLN GLN A . n 
A 1 129 PRO 129 129 129 PRO PRO A . n 
A 1 130 VAL 130 130 130 VAL VAL A . n 
A 1 131 SER 131 131 131 SER SER A . n 
A 1 132 VAL 132 132 132 VAL VAL A . n 
A 1 133 VAL 133 133 133 VAL VAL A . n 
A 1 134 LEU 134 134 134 LEU LEU A . n 
A 1 135 GLU 135 135 135 GLU GLU A . n 
A 1 136 ALA 136 136 136 ALA ALA A . n 
A 1 137 ALA 137 137 137 ALA ALA A . n 
A 1 138 GLY 138 138 138 GLY GLY A . n 
A 1 139 LYS 139 139 139 LYS LYS A . n 
A 1 140 ASP 140 140 140 ASP ASP A . n 
A 1 141 PHE 141 141 141 PHE PHE A . n 
A 1 142 GLN 142 142 142 GLN GLN A . n 
A 1 143 LEU 143 143 143 LEU LEU A . n 
A 1 144 TYR 144 144 144 TYR TYR A . n 
A 1 145 ARG 145 145 145 ARG ARG A . n 
A 1 146 GLY 146 146 146 GLY GLY A . n 
A 1 147 GLY 147 147 147 GLY GLY A . n 
A 1 148 ILE 148 148 148 ILE ILE A . n 
A 1 149 PHE 149 149 149 PHE PHE A . n 
A 1 150 VAL 150 150 150 VAL VAL A . n 
A 1 151 GLY 151 151 151 GLY GLY A . n 
A 1 152 PRO 152 152 152 PRO PRO A . n 
A 1 153 CYS 153 153 153 CYS CYS A . n 
A 1 154 GLY 154 154 154 GLY GLY A . n 
A 1 155 ASN 155 155 155 ASN ASN A . n 
A 1 156 LYS 156 156 156 LYS LYS A . n 
A 1 157 VAL 157 157 157 VAL VAL A . n 
A 1 158 ASP 158 158 158 ASP ASP A . n 
A 1 159 HIS 159 159 159 HIS HIS A . n 
A 1 160 ALA 160 160 160 ALA ALA A . n 
A 1 161 VAL 161 161 161 VAL VAL A . n 
A 1 162 ALA 162 162 162 ALA ALA A . n 
A 1 163 ALA 163 163 163 ALA ALA A . n 
A 1 164 VAL 164 164 164 VAL VAL A . n 
A 1 165 GLY 165 165 165 GLY GLY A . n 
A 1 166 TYR 166 166 166 TYR TYR A . n 
A 1 167 GLY 167 167 167 GLY GLY A . n 
A 1 168 PRO 168 168 168 PRO PRO A . n 
A 1 169 ASN 169 169 169 ASN ASN A . n 
A 1 170 TYR 170 170 170 TYR TYR A . n 
A 1 171 ILE 171 171 171 ILE ILE A . n 
A 1 172 LEU 172 172 172 LEU LEU A . n 
A 1 173 ILE 173 173 173 ILE ILE A . n 
A 1 174 LYS 174 174 174 LYS LYS A . n 
A 1 175 ASN 175 175 175 ASN ASN A . n 
A 1 176 SER 176 176 176 SER SER A . n 
A 1 177 TRP 177 177 177 TRP TRP A . n 
A 1 178 GLY 178 178 178 GLY GLY A . n 
A 1 179 THR 179 179 179 THR THR A . n 
A 1 180 GLY 180 180 180 GLY GLY A . n 
A 1 181 TRP 181 181 181 TRP TRP A . n 
A 1 182 GLY 182 182 182 GLY GLY A . n 
A 1 183 GLU 183 183 183 GLU GLU A . n 
A 1 184 ASN 184 184 184 ASN ASN A . n 
A 1 185 GLY 185 185 185 GLY GLY A . n 
A 1 186 TYR 186 186 186 TYR TYR A . n 
A 1 187 ILE 187 187 187 ILE ILE A . n 
A 1 188 ARG 188 188 188 ARG ARG A . n 
A 1 189 ILE 189 189 189 ILE ILE A . n 
A 1 190 LYS 190 190 190 LYS LYS A . n 
A 1 191 ARG 191 191 191 ARG ARG A . n 
A 1 192 GLY 192 192 192 GLY GLY A . n 
A 1 193 THR 193 193 193 THR THR A . n 
A 1 194 GLY 194 194 194 GLY GLY A . n 
A 1 195 ASN 195 195 195 ASN ASN A . n 
A 1 196 SER 196 196 196 SER SER A . n 
A 1 197 TYR 197 197 197 TYR TYR A . n 
A 1 198 GLY 198 198 198 GLY GLY A . n 
A 1 199 VAL 199 199 199 VAL VAL A . n 
A 1 200 CYS 200 200 200 CYS CYS A . n 
A 1 201 GLY 201 201 201 GLY GLY A . n 
A 1 202 LEU 202 202 202 LEU LEU A . n 
A 1 203 TYR 203 203 203 TYR TYR A . n 
A 1 204 THR 204 204 204 THR THR A . n 
A 1 205 SER 205 205 205 SER SER A . n 
A 1 206 SER 206 206 206 SER SER A . n 
A 1 207 PHE 207 207 207 PHE PHE A . n 
A 1 208 TYR 208 208 208 TYR TYR A . n 
A 1 209 PRO 209 209 209 PRO PRO A . n 
A 1 210 VAL 210 210 210 VAL VAL A . n 
A 1 211 LYS 211 211 211 LYS LYS A . n 
A 1 212 ASN 212 212 212 ASN ASN A . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 A1BWT 1  301 301 A1BWT LIG A . 
C 3 HOH   1  401 74  HOH   HOH A . 
C 3 HOH   2  402 42  HOH   HOH A . 
C 3 HOH   3  403 59  HOH   HOH A . 
C 3 HOH   4  404 64  HOH   HOH A . 
C 3 HOH   5  405 43  HOH   HOH A . 
C 3 HOH   6  406 78  HOH   HOH A . 
C 3 HOH   7  407 30  HOH   HOH A . 
C 3 HOH   8  408 73  HOH   HOH A . 
C 3 HOH   9  409 86  HOH   HOH A . 
C 3 HOH   10 410 10  HOH   HOH A . 
C 3 HOH   11 411 27  HOH   HOH A . 
C 3 HOH   12 412 56  HOH   HOH A . 
C 3 HOH   13 413 83  HOH   HOH A . 
C 3 HOH   14 414 77  HOH   HOH A . 
C 3 HOH   15 415 23  HOH   HOH A . 
C 3 HOH   16 416 68  HOH   HOH A . 
C 3 HOH   17 417 5   HOH   HOH A . 
C 3 HOH   18 418 60  HOH   HOH A . 
C 3 HOH   19 419 16  HOH   HOH A . 
C 3 HOH   20 420 4   HOH   HOH A . 
C 3 HOH   21 421 6   HOH   HOH A . 
C 3 HOH   22 422 55  HOH   HOH A . 
C 3 HOH   23 423 29  HOH   HOH A . 
C 3 HOH   24 424 28  HOH   HOH A . 
C 3 HOH   25 425 22  HOH   HOH A . 
C 3 HOH   26 426 39  HOH   HOH A . 
C 3 HOH   27 427 67  HOH   HOH A . 
C 3 HOH   28 428 50  HOH   HOH A . 
C 3 HOH   29 429 21  HOH   HOH A . 
C 3 HOH   30 430 71  HOH   HOH A . 
C 3 HOH   31 431 11  HOH   HOH A . 
C 3 HOH   32 432 53  HOH   HOH A . 
C 3 HOH   33 433 70  HOH   HOH A . 
C 3 HOH   34 434 32  HOH   HOH A . 
C 3 HOH   35 435 48  HOH   HOH A . 
C 3 HOH   36 436 79  HOH   HOH A . 
C 3 HOH   37 437 51  HOH   HOH A . 
C 3 HOH   38 438 80  HOH   HOH A . 
C 3 HOH   39 439 13  HOH   HOH A . 
C 3 HOH   40 440 52  HOH   HOH A . 
C 3 HOH   41 441 63  HOH   HOH A . 
C 3 HOH   42 442 19  HOH   HOH A . 
C 3 HOH   43 443 8   HOH   HOH A . 
C 3 HOH   44 444 37  HOH   HOH A . 
C 3 HOH   45 445 33  HOH   HOH A . 
C 3 HOH   46 446 2   HOH   HOH A . 
C 3 HOH   47 447 54  HOH   HOH A . 
C 3 HOH   48 448 7   HOH   HOH A . 
C 3 HOH   49 449 72  HOH   HOH A . 
C 3 HOH   50 450 62  HOH   HOH A . 
C 3 HOH   51 451 57  HOH   HOH A . 
C 3 HOH   52 452 47  HOH   HOH A . 
C 3 HOH   53 453 84  HOH   HOH A . 
C 3 HOH   54 454 38  HOH   HOH A . 
C 3 HOH   55 455 66  HOH   HOH A . 
C 3 HOH   56 456 25  HOH   HOH A . 
C 3 HOH   57 457 20  HOH   HOH A . 
C 3 HOH   58 458 34  HOH   HOH A . 
C 3 HOH   59 459 75  HOH   HOH A . 
C 3 HOH   60 460 15  HOH   HOH A . 
C 3 HOH   61 461 26  HOH   HOH A . 
C 3 HOH   62 462 41  HOH   HOH A . 
C 3 HOH   63 463 81  HOH   HOH A . 
C 3 HOH   64 464 31  HOH   HOH A . 
C 3 HOH   65 465 61  HOH   HOH A . 
C 3 HOH   66 466 40  HOH   HOH A . 
C 3 HOH   67 467 58  HOH   HOH A . 
C 3 HOH   68 468 3   HOH   HOH A . 
C 3 HOH   69 469 18  HOH   HOH A . 
C 3 HOH   70 470 24  HOH   HOH A . 
C 3 HOH   71 471 69  HOH   HOH A . 
C 3 HOH   72 472 45  HOH   HOH A . 
C 3 HOH   73 473 76  HOH   HOH A . 
C 3 HOH   74 474 85  HOH   HOH A . 
C 3 HOH   75 475 17  HOH   HOH A . 
C 3 HOH   76 476 44  HOH   HOH A . 
C 3 HOH   77 477 36  HOH   HOH A . 
C 3 HOH   78 478 49  HOH   HOH A . 
C 3 HOH   79 479 35  HOH   HOH A . 
# 
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'   ? ? ? ? ? ? ? ? ? ? ? CrystFEL ? ? ? .           2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? CrystFEL ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .           4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9NB7 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     42.500 
_cell.length_a_esd                 ? 
_cell.length_b                     48.900 
_cell.length_b_esd                 ? 
_cell.length_c                     101.500 
_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                         9NB7 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_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                   9NB7 
_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          45.30 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '889 mM NaCl, 58% methanol in reservoir. 66% methanol in sitting drop' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            298 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     298 
_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   Y 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'PSI JUNGFRAU 4M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-11-05 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.072 
_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                        'ESRF BEAMLINE ID29' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.072 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ID29 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9NB7 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.8 
_reflns.d_resolution_low                               44.05 
_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                                     37928 
_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 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                297.15 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          4.6 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.935 
_reflns.pdbx_CC_star                                   0.983 
_reflns.pdbx_R_split                                   0.206 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.80 
_reflns_shell.d_res_low                                     1.83 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.2 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1877 
_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                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.397 
_reflns_shell.pdbx_CC_star                                  0.754 
_reflns_shell.pdbx_R_split                                  0.921 
_reflns_shell.percent_possible_all                          100 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_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                                 9NB7 
_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                            1.80 
_refine.ls_d_res_low                             44.05 
_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                     20274 
_refine.ls_number_reflns_R_free                  1014 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.93 
_refine.ls_percent_reflns_R_free                 5.00 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1759 
_refine.ls_R_factor_R_free                       0.2150 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1739 
_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.correlation_coeff_I_to_Fcsqd_work        ? 
_refine.correlation_coeff_I_to_Fcsqd_free        ? 
_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                          1.35 
_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                 21.57 
_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                            0.19 
_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                       1.80 
_refine_hist.d_res_low                        44.05 
_refine_hist.number_atoms_solvent             79 
_refine_hist.number_atoms_total               1763 
_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        1655 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         29 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.007 ? 1787 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.041 ? 2434 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 6.310 ? 270  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.076 ? 240  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.013 ? 323  ? 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.correlation_coeff_Fo_to_Fc 
_refine_ls_shell.correlation_coeff_Fo_to_Fc_free 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_work 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_free 
_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' 1.80 1.89  . . 142 2692 100.00 . . . . 0.2647 . . . . . . . . . . . . . . . 0.3105 
'X-RAY DIFFRACTION' 1.90 2.01  . . 142 2716 100.00 . . . . 0.2385 . . . . . . . . . . . . . . . 0.2724 
'X-RAY DIFFRACTION' 2.01 2.17  . . 142 2696 100.00 . . . . 0.1877 . . . . . . . . . . . . . . . 0.2361 
'X-RAY DIFFRACTION' 2.17 2.39  . . 144 2734 100.00 . . . . 0.1808 . . . . . . . . . . . . . . . 0.2519 
'X-RAY DIFFRACTION' 2.39 2.73  . . 145 2742 100.00 . . . . 0.1901 . . . . . . . . . . . . . . . 0.2455 
'X-RAY DIFFRACTION' 2.73 3.44  . . 146 2773 100.00 . . . . 0.1736 . . . . . . . . . . . . . . . 0.2002 
'X-RAY DIFFRACTION' 3.44 44.05 . . 153 2907 100.00 . . . . 0.1470 . . . . . . . . . . . . . . . 0.1834 
# 
_struct.entry_id                     9NB7 
_struct.title                        
'Serial synchrotron X-ray diffraction structure of papain microcrystals soaked with natural product E405' 
_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        9NB7 
_struct_keywords.text            'Inhibitor, Complex, Enzyme, Serial, HYDROLASE' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    PAPA1_CARPA 
_struct_ref.pdbx_db_accession          P00784 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;IPEYVDWRQKGAVTPVKNQGSCGSCWAFSAVVTIEGIIKIRTGNLNEYSEQELLDCDRRSYGCNGGYPWSALQLVAQYGI
HYRNTYPYEGVQRYCRSREKGPYAAKTDGVRQVQPYNEGALLYSIANQPVSVVLEAAGKDFQLYRGGIFVGPCGNKVDHA
VAAVGYGPNYILIKNSWGTGWGENGYIRIKRGTGNSYGVCGLYTSSFYPVKN
;
_struct_ref.pdbx_align_begin           134 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9NB7 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 212 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P00784 
_struct_ref_seq.db_align_beg                  134 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  345 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       212 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C 
# 
_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                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 SER A 24  ? GLY A 43  ? SER A 24  GLY A 43  1 ? 20 
HELX_P HELX_P2 AA2 SER A 49  ? ASP A 57  ? SER A 49  ASP A 57  1 ? 9  
HELX_P HELX_P3 AA3 TYR A 61  ? GLY A 65  ? TYR A 61  GLY A 65  5 ? 5  
HELX_P HELX_P4 AA4 TYR A 67  ? TYR A 78  ? TYR A 67  TYR A 78  1 ? 12 
HELX_P HELX_P5 AA5 SER A 97  ? GLY A 101 ? SER A 97  GLY A 101 5 ? 5  
HELX_P HELX_P6 AA6 ASN A 117 ? GLN A 128 ? ASN A 117 GLN A 128 1 ? 12 
HELX_P HELX_P7 AA7 GLY A 138 ? LEU A 143 ? GLY A 138 LEU A 143 1 ? 6  
HELX_P HELX_P8 AA8 GLY A 198 ? LEU A 202 ? GLY A 198 LEU A 202 5 ? 5  
# 
_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 
disulf1 disulf ?    ? A CYS 22  SG ? ? ? 1_555 A CYS   63  SG ? ? A CYS 22  A CYS   63  1_555 ? ? ? ? ? ? ? 2.019 ? ? 
disulf2 disulf ?    ? A CYS 56  SG ? ? ? 1_555 A CYS   95  SG ? ? A CYS 56  A CYS   95  1_555 ? ? ? ? ? ? ? 2.040 ? ? 
disulf3 disulf ?    ? A CYS 153 SG ? ? ? 1_555 A CYS   200 SG ? ? A CYS 153 A CYS   200 1_555 ? ? ? ? ? ? ? 2.039 ? ? 
covale1 covale none ? A CYS 25  SG ? ? ? 1_555 B A1BWT .   C2 ? ? A CYS 25  A A1BWT 301 1_555 ? ? ? ? ? ? ? 1.773 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
# 
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 A1BWT B .   ? CYS A 25  ? A1BWT A 301 ? 1_555 CYS A 25  ? 1_555 C2 SG CYS 1 A1BWT None 'Covalent chemical modification' 
2 CYS   A 22  ? CYS A 63  ? CYS   A 22  ? 1_555 CYS A 63  ? 1_555 SG SG .   . .     None 'Disulfide bridge'               
3 CYS   A 56  ? CYS A 95  ? CYS   A 56  ? 1_555 CYS A 95  ? 1_555 SG SG .   . .     None 'Disulfide bridge'               
4 CYS   A 153 ? CYS A 200 ? CYS   A 153 ? 1_555 CYS A 200 ? 1_555 SG SG .   . .     None 'Disulfide bridge'               
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          GLY 
_struct_mon_prot_cis.label_seq_id           151 
_struct_mon_prot_cis.label_asym_id          A 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           GLY 
_struct_mon_prot_cis.auth_seq_id            151 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    152 
_struct_mon_prot_cis.pdbx_label_asym_id_2   A 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     152 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       2.43 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 5 ? 
AA3 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? parallel      
AA3 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 VAL A 5   ? ASP A 6   ? VAL A 5   ASP A 6   
AA1 2 HIS A 159 ? GLY A 167 ? HIS A 159 GLY A 167 
AA1 3 VAL A 130 ? LEU A 134 ? VAL A 130 LEU A 134 
AA2 1 VAL A 5   ? ASP A 6   ? VAL A 5   ASP A 6   
AA2 2 HIS A 159 ? GLY A 167 ? HIS A 159 GLY A 167 
AA2 3 TYR A 170 ? LYS A 174 ? TYR A 170 LYS A 174 
AA2 4 TYR A 186 ? LYS A 190 ? TYR A 186 LYS A 190 
AA2 5 ILE A 148 ? PHE A 149 ? ILE A 148 PHE A 149 
AA3 1 GLY A 109 ? GLN A 112 ? GLY A 109 GLN A 112 
AA3 2 PHE A 207 ? VAL A 210 ? PHE A 207 VAL A 210 
# 
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 VAL A 5   ? N VAL A 5   O TYR A 166 ? O TYR A 166 
AA1 2 3 O ALA A 163 ? O ALA A 163 N VAL A 130 ? N VAL A 130 
AA2 1 2 N VAL A 5   ? N VAL A 5   O TYR A 166 ? O TYR A 166 
AA2 2 3 N ALA A 162 ? N ALA A 162 O LYS A 174 ? O LYS A 174 
AA2 3 4 N ILE A 173 ? N ILE A 173 O ILE A 187 ? O ILE A 187 
AA2 4 5 O ARG A 188 ? O ARG A 188 N PHE A 149 ? N PHE A 149 
AA3 1 2 N GLY A 109 ? N GLY A 109 O VAL A 210 ? O VAL A 210 
# 
_pdbx_entry_details.entry_id                   9NB7 
_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_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 TYR A 78 ? ? -121.73 -70.31  
2 1 ARG A 93 ? ? -123.20 -159.98 
3 1 ARG A 93 ? ? -123.20 -157.94 
# 
_pdbx_validate_planes.id              1 
_pdbx_validate_planes.PDB_model_num   1 
_pdbx_validate_planes.auth_comp_id    ARG 
_pdbx_validate_planes.auth_asym_id    A 
_pdbx_validate_planes.auth_seq_id     111 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.101 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
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 
A1BWT N1   N N N 1   
A1BWT N3   N N N 2   
A1BWT C4   C N N 3   
A1BWT C5   C N S 4   
A1BWT C7   C N N 5   
A1BWT C8   C N N 6   
A1BWT C10  C N N 7   
A1BWT C13  C N N 8   
A1BWT C15  C Y N 9   
A1BWT C17  C Y N 10  
A1BWT C20  C N N 11  
A1BWT C21  C N N 12  
A1BWT C1   C N N 13  
A1BWT C11  C N N 14  
A1BWT C12  C N N 15  
A1BWT C14  C Y N 16  
A1BWT C16  C Y N 17  
A1BWT C18  C Y N 18  
A1BWT C19  C Y N 19  
A1BWT C2   C N N 20  
A1BWT C3   C N R 21  
A1BWT C9   C N N 22  
A1BWT N2   N N N 23  
A1BWT O1   O N N 24  
A1BWT O2   O N N 25  
A1BWT O3   O N N 26  
A1BWT O4   O N N 27  
A1BWT O5   O N N 28  
A1BWT O6   O N N 29  
A1BWT H1   H N N 30  
A1BWT H2   H N N 31  
A1BWT H3   H N N 32  
A1BWT H4   H N N 33  
A1BWT H5   H N N 34  
A1BWT H6   H N N 35  
A1BWT H7   H N N 36  
A1BWT H8   H N N 37  
A1BWT H9   H N N 38  
A1BWT H10  H N N 39  
A1BWT H11  H N N 40  
A1BWT H12  H N N 41  
A1BWT H13  H N N 42  
A1BWT H14  H N N 43  
A1BWT H15  H N N 44  
A1BWT H16  H N N 45  
A1BWT H17  H N N 46  
A1BWT H18  H N N 47  
A1BWT H19  H N N 48  
A1BWT H20  H N N 49  
A1BWT H21  H N N 50  
A1BWT H22  H N N 51  
A1BWT H23  H N N 52  
A1BWT H24  H N N 53  
A1BWT H25  H N N 54  
A1BWT H26  H N N 55  
A1BWT H27  H N N 56  
A1BWT H28  H N N 57  
A1BWT H29  H N N 58  
ALA   N    N N N 59  
ALA   CA   C N S 60  
ALA   C    C N N 61  
ALA   O    O N N 62  
ALA   CB   C N N 63  
ALA   OXT  O N N 64  
ALA   H    H N N 65  
ALA   H2   H N N 66  
ALA   HA   H N N 67  
ALA   HB1  H N N 68  
ALA   HB2  H N N 69  
ALA   HB3  H N N 70  
ALA   HXT  H N N 71  
ARG   N    N N N 72  
ARG   CA   C N S 73  
ARG   C    C N N 74  
ARG   O    O N N 75  
ARG   CB   C N N 76  
ARG   CG   C N N 77  
ARG   CD   C N N 78  
ARG   NE   N N N 79  
ARG   CZ   C N N 80  
ARG   NH1  N N N 81  
ARG   NH2  N N N 82  
ARG   OXT  O N N 83  
ARG   H    H N N 84  
ARG   H2   H N N 85  
ARG   HA   H N N 86  
ARG   HB2  H N N 87  
ARG   HB3  H N N 88  
ARG   HG2  H N N 89  
ARG   HG3  H N N 90  
ARG   HD2  H N N 91  
ARG   HD3  H N N 92  
ARG   HE   H N N 93  
ARG   HH11 H N N 94  
ARG   HH12 H N N 95  
ARG   HH21 H N N 96  
ARG   HH22 H N N 97  
ARG   HXT  H N N 98  
ASN   N    N N N 99  
ASN   CA   C N S 100 
ASN   C    C N N 101 
ASN   O    O N N 102 
ASN   CB   C N N 103 
ASN   CG   C N N 104 
ASN   OD1  O N N 105 
ASN   ND2  N N N 106 
ASN   OXT  O N N 107 
ASN   H    H N N 108 
ASN   H2   H N N 109 
ASN   HA   H N N 110 
ASN   HB2  H N N 111 
ASN   HB3  H N N 112 
ASN   HD21 H N N 113 
ASN   HD22 H N N 114 
ASN   HXT  H N N 115 
ASP   N    N N N 116 
ASP   CA   C N S 117 
ASP   C    C N N 118 
ASP   O    O N N 119 
ASP   CB   C N N 120 
ASP   CG   C N N 121 
ASP   OD1  O N N 122 
ASP   OD2  O N N 123 
ASP   OXT  O N N 124 
ASP   H    H N N 125 
ASP   H2   H N N 126 
ASP   HA   H N N 127 
ASP   HB2  H N N 128 
ASP   HB3  H N N 129 
ASP   HD2  H N N 130 
ASP   HXT  H N N 131 
CYS   N    N N N 132 
CYS   CA   C N R 133 
CYS   C    C N N 134 
CYS   O    O N N 135 
CYS   CB   C N N 136 
CYS   SG   S N N 137 
CYS   OXT  O N N 138 
CYS   H    H N N 139 
CYS   H2   H N N 140 
CYS   HA   H N N 141 
CYS   HB2  H N N 142 
CYS   HB3  H N N 143 
CYS   HG   H N N 144 
CYS   HXT  H N N 145 
GLN   N    N N N 146 
GLN   CA   C N S 147 
GLN   C    C N N 148 
GLN   O    O N N 149 
GLN   CB   C N N 150 
GLN   CG   C N N 151 
GLN   CD   C N N 152 
GLN   OE1  O N N 153 
GLN   NE2  N N N 154 
GLN   OXT  O N N 155 
GLN   H    H N N 156 
GLN   H2   H N N 157 
GLN   HA   H N N 158 
GLN   HB2  H N N 159 
GLN   HB3  H N N 160 
GLN   HG2  H N N 161 
GLN   HG3  H N N 162 
GLN   HE21 H N N 163 
GLN   HE22 H N N 164 
GLN   HXT  H N N 165 
GLU   N    N N N 166 
GLU   CA   C N S 167 
GLU   C    C N N 168 
GLU   O    O N N 169 
GLU   CB   C N N 170 
GLU   CG   C N N 171 
GLU   CD   C N N 172 
GLU   OE1  O N N 173 
GLU   OE2  O N N 174 
GLU   OXT  O N N 175 
GLU   H    H N N 176 
GLU   H2   H N N 177 
GLU   HA   H N N 178 
GLU   HB2  H N N 179 
GLU   HB3  H N N 180 
GLU   HG2  H N N 181 
GLU   HG3  H N N 182 
GLU   HE2  H N N 183 
GLU   HXT  H N N 184 
GLY   N    N N N 185 
GLY   CA   C N N 186 
GLY   C    C N N 187 
GLY   O    O N N 188 
GLY   OXT  O N N 189 
GLY   H    H N N 190 
GLY   H2   H N N 191 
GLY   HA2  H N N 192 
GLY   HA3  H N N 193 
GLY   HXT  H N N 194 
HIS   N    N N N 195 
HIS   CA   C N S 196 
HIS   C    C N N 197 
HIS   O    O N N 198 
HIS   CB   C N N 199 
HIS   CG   C Y N 200 
HIS   ND1  N Y N 201 
HIS   CD2  C Y N 202 
HIS   CE1  C Y N 203 
HIS   NE2  N Y N 204 
HIS   OXT  O N N 205 
HIS   H    H N N 206 
HIS   H2   H N N 207 
HIS   HA   H N N 208 
HIS   HB2  H N N 209 
HIS   HB3  H N N 210 
HIS   HD1  H N N 211 
HIS   HD2  H N N 212 
HIS   HE1  H N N 213 
HIS   HE2  H N N 214 
HIS   HXT  H N N 215 
HOH   O    O N N 216 
HOH   H1   H N N 217 
HOH   H2   H N N 218 
ILE   N    N N N 219 
ILE   CA   C N S 220 
ILE   C    C N N 221 
ILE   O    O N N 222 
ILE   CB   C N S 223 
ILE   CG1  C N N 224 
ILE   CG2  C N N 225 
ILE   CD1  C N N 226 
ILE   OXT  O N N 227 
ILE   H    H N N 228 
ILE   H2   H N N 229 
ILE   HA   H N N 230 
ILE   HB   H N N 231 
ILE   HG12 H N N 232 
ILE   HG13 H N N 233 
ILE   HG21 H N N 234 
ILE   HG22 H N N 235 
ILE   HG23 H N N 236 
ILE   HD11 H N N 237 
ILE   HD12 H N N 238 
ILE   HD13 H N N 239 
ILE   HXT  H N N 240 
LEU   N    N N N 241 
LEU   CA   C N S 242 
LEU   C    C N N 243 
LEU   O    O N N 244 
LEU   CB   C N N 245 
LEU   CG   C N N 246 
LEU   CD1  C N N 247 
LEU   CD2  C N N 248 
LEU   OXT  O N N 249 
LEU   H    H N N 250 
LEU   H2   H N N 251 
LEU   HA   H N N 252 
LEU   HB2  H N N 253 
LEU   HB3  H N N 254 
LEU   HG   H N N 255 
LEU   HD11 H N N 256 
LEU   HD12 H N N 257 
LEU   HD13 H N N 258 
LEU   HD21 H N N 259 
LEU   HD22 H N N 260 
LEU   HD23 H N N 261 
LEU   HXT  H N N 262 
LYS   N    N N N 263 
LYS   CA   C N S 264 
LYS   C    C N N 265 
LYS   O    O N N 266 
LYS   CB   C N N 267 
LYS   CG   C N N 268 
LYS   CD   C N N 269 
LYS   CE   C N N 270 
LYS   NZ   N N N 271 
LYS   OXT  O N N 272 
LYS   H    H N N 273 
LYS   H2   H N N 274 
LYS   HA   H N N 275 
LYS   HB2  H N N 276 
LYS   HB3  H N N 277 
LYS   HG2  H N N 278 
LYS   HG3  H N N 279 
LYS   HD2  H N N 280 
LYS   HD3  H N N 281 
LYS   HE2  H N N 282 
LYS   HE3  H N N 283 
LYS   HZ1  H N N 284 
LYS   HZ2  H N N 285 
LYS   HZ3  H N N 286 
LYS   HXT  H N N 287 
PHE   N    N N N 288 
PHE   CA   C N S 289 
PHE   C    C N N 290 
PHE   O    O N N 291 
PHE   CB   C N N 292 
PHE   CG   C Y N 293 
PHE   CD1  C Y N 294 
PHE   CD2  C Y N 295 
PHE   CE1  C Y N 296 
PHE   CE2  C Y N 297 
PHE   CZ   C Y N 298 
PHE   OXT  O N N 299 
PHE   H    H N N 300 
PHE   H2   H N N 301 
PHE   HA   H N N 302 
PHE   HB2  H N N 303 
PHE   HB3  H N N 304 
PHE   HD1  H N N 305 
PHE   HD2  H N N 306 
PHE   HE1  H N N 307 
PHE   HE2  H N N 308 
PHE   HZ   H N N 309 
PHE   HXT  H N N 310 
PRO   N    N N N 311 
PRO   CA   C N S 312 
PRO   C    C N N 313 
PRO   O    O N N 314 
PRO   CB   C N N 315 
PRO   CG   C N N 316 
PRO   CD   C N N 317 
PRO   OXT  O N N 318 
PRO   H    H N N 319 
PRO   HA   H N N 320 
PRO   HB2  H N N 321 
PRO   HB3  H N N 322 
PRO   HG2  H N N 323 
PRO   HG3  H N N 324 
PRO   HD2  H N N 325 
PRO   HD3  H N N 326 
PRO   HXT  H N N 327 
SER   N    N N N 328 
SER   CA   C N S 329 
SER   C    C N N 330 
SER   O    O N N 331 
SER   CB   C N N 332 
SER   OG   O N N 333 
SER   OXT  O N N 334 
SER   H    H N N 335 
SER   H2   H N N 336 
SER   HA   H N N 337 
SER   HB2  H N N 338 
SER   HB3  H N N 339 
SER   HG   H N N 340 
SER   HXT  H N N 341 
THR   N    N N N 342 
THR   CA   C N S 343 
THR   C    C N N 344 
THR   O    O N N 345 
THR   CB   C N R 346 
THR   OG1  O N N 347 
THR   CG2  C N N 348 
THR   OXT  O N N 349 
THR   H    H N N 350 
THR   H2   H N N 351 
THR   HA   H N N 352 
THR   HB   H N N 353 
THR   HG1  H N N 354 
THR   HG21 H N N 355 
THR   HG22 H N N 356 
THR   HG23 H N N 357 
THR   HXT  H N N 358 
TRP   N    N N N 359 
TRP   CA   C N S 360 
TRP   C    C N N 361 
TRP   O    O N N 362 
TRP   CB   C N N 363 
TRP   CG   C Y N 364 
TRP   CD1  C Y N 365 
TRP   CD2  C Y N 366 
TRP   NE1  N Y N 367 
TRP   CE2  C Y N 368 
TRP   CE3  C Y N 369 
TRP   CZ2  C Y N 370 
TRP   CZ3  C Y N 371 
TRP   CH2  C Y N 372 
TRP   OXT  O N N 373 
TRP   H    H N N 374 
TRP   H2   H N N 375 
TRP   HA   H N N 376 
TRP   HB2  H N N 377 
TRP   HB3  H N N 378 
TRP   HD1  H N N 379 
TRP   HE1  H N N 380 
TRP   HE3  H N N 381 
TRP   HZ2  H N N 382 
TRP   HZ3  H N N 383 
TRP   HH2  H N N 384 
TRP   HXT  H N N 385 
TYR   N    N N N 386 
TYR   CA   C N S 387 
TYR   C    C N N 388 
TYR   O    O N N 389 
TYR   CB   C N N 390 
TYR   CG   C Y N 391 
TYR   CD1  C Y N 392 
TYR   CD2  C Y N 393 
TYR   CE1  C Y N 394 
TYR   CE2  C Y N 395 
TYR   CZ   C Y N 396 
TYR   OH   O N N 397 
TYR   OXT  O N N 398 
TYR   H    H N N 399 
TYR   H2   H N N 400 
TYR   HA   H N N 401 
TYR   HB2  H N N 402 
TYR   HB3  H N N 403 
TYR   HD1  H N N 404 
TYR   HD2  H N N 405 
TYR   HE1  H N N 406 
TYR   HE2  H N N 407 
TYR   HH   H N N 408 
TYR   HXT  H N N 409 
VAL   N    N N N 410 
VAL   CA   C N S 411 
VAL   C    C N N 412 
VAL   O    O N N 413 
VAL   CB   C N N 414 
VAL   CG1  C N N 415 
VAL   CG2  C N N 416 
VAL   OXT  O N N 417 
VAL   H    H N N 418 
VAL   H2   H N N 419 
VAL   HA   H N N 420 
VAL   HB   H N N 421 
VAL   HG11 H N N 422 
VAL   HG12 H N N 423 
VAL   HG13 H N N 424 
VAL   HG21 H N N 425 
VAL   HG22 H N N 426 
VAL   HG23 H N N 427 
VAL   HXT  H N N 428 
# 
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 
A1BWT O2  C1   doub N N 1   
A1BWT C1  O1   sing N N 2   
A1BWT C1  C2   sing N N 3   
A1BWT C2  C3   sing N N 4   
A1BWT O3  C3   sing N N 5   
A1BWT O4  C4   doub N N 6   
A1BWT C3  C4   sing N N 7   
A1BWT C4  N1   sing N N 8   
A1BWT N1  C5   sing N N 9   
A1BWT C5  C13  sing N N 10  
A1BWT C5  C7   sing N N 11  
A1BWT C21 C20  sing N N 12  
A1BWT C13 C14  sing N N 13  
A1BWT C10 C11  sing N N 14  
A1BWT C10 C9   sing N N 15  
A1BWT N3  C20  sing N N 16  
A1BWT N3  C12  sing N N 17  
A1BWT C11 C12  sing N N 18  
A1BWT C15 C14  doub Y N 19  
A1BWT C15 C16  sing Y N 20  
A1BWT C8  C9   sing N N 21  
A1BWT C8  N2   sing N N 22  
A1BWT C20 O6   doub N N 23  
A1BWT C14 C19  sing Y N 24  
A1BWT C7  N2   sing N N 25  
A1BWT C7  O5   doub N N 26  
A1BWT C16 C17  doub Y N 27  
A1BWT C19 C18  doub Y N 28  
A1BWT C17 C18  sing Y N 29  
A1BWT N1  H1   sing N N 30  
A1BWT N3  H2   sing N N 31  
A1BWT C5  H3   sing N N 32  
A1BWT C8  H4   sing N N 33  
A1BWT C8  H5   sing N N 34  
A1BWT C10 H6   sing N N 35  
A1BWT C10 H7   sing N N 36  
A1BWT C13 H8   sing N N 37  
A1BWT C13 H9   sing N N 38  
A1BWT C15 H10  sing N N 39  
A1BWT C17 H11  sing N N 40  
A1BWT C21 H12  sing N N 41  
A1BWT C21 H13  sing N N 42  
A1BWT C21 H14  sing N N 43  
A1BWT C11 H15  sing N N 44  
A1BWT C11 H16  sing N N 45  
A1BWT C12 H17  sing N N 46  
A1BWT C12 H18  sing N N 47  
A1BWT C16 H19  sing N N 48  
A1BWT C18 H20  sing N N 49  
A1BWT C19 H21  sing N N 50  
A1BWT C2  H22  sing N N 51  
A1BWT C2  H23  sing N N 52  
A1BWT C3  H24  sing N N 53  
A1BWT C9  H25  sing N N 54  
A1BWT C9  H26  sing N N 55  
A1BWT N2  H27  sing N N 56  
A1BWT O1  H28  sing N N 57  
A1BWT O3  H29  sing N N 58  
ALA   N   CA   sing N N 59  
ALA   N   H    sing N N 60  
ALA   N   H2   sing N N 61  
ALA   CA  C    sing N N 62  
ALA   CA  CB   sing N N 63  
ALA   CA  HA   sing N N 64  
ALA   C   O    doub N N 65  
ALA   C   OXT  sing N N 66  
ALA   CB  HB1  sing N N 67  
ALA   CB  HB2  sing N N 68  
ALA   CB  HB3  sing N N 69  
ALA   OXT HXT  sing N N 70  
ARG   N   CA   sing N N 71  
ARG   N   H    sing N N 72  
ARG   N   H2   sing N N 73  
ARG   CA  C    sing N N 74  
ARG   CA  CB   sing N N 75  
ARG   CA  HA   sing N N 76  
ARG   C   O    doub N N 77  
ARG   C   OXT  sing N N 78  
ARG   CB  CG   sing N N 79  
ARG   CB  HB2  sing N N 80  
ARG   CB  HB3  sing N N 81  
ARG   CG  CD   sing N N 82  
ARG   CG  HG2  sing N N 83  
ARG   CG  HG3  sing N N 84  
ARG   CD  NE   sing N N 85  
ARG   CD  HD2  sing N N 86  
ARG   CD  HD3  sing N N 87  
ARG   NE  CZ   sing N N 88  
ARG   NE  HE   sing N N 89  
ARG   CZ  NH1  sing N N 90  
ARG   CZ  NH2  doub N N 91  
ARG   NH1 HH11 sing N N 92  
ARG   NH1 HH12 sing N N 93  
ARG   NH2 HH21 sing N N 94  
ARG   NH2 HH22 sing N N 95  
ARG   OXT HXT  sing N N 96  
ASN   N   CA   sing N N 97  
ASN   N   H    sing N N 98  
ASN   N   H2   sing N N 99  
ASN   CA  C    sing N N 100 
ASN   CA  CB   sing N N 101 
ASN   CA  HA   sing N N 102 
ASN   C   O    doub N N 103 
ASN   C   OXT  sing N N 104 
ASN   CB  CG   sing N N 105 
ASN   CB  HB2  sing N N 106 
ASN   CB  HB3  sing N N 107 
ASN   CG  OD1  doub N N 108 
ASN   CG  ND2  sing N N 109 
ASN   ND2 HD21 sing N N 110 
ASN   ND2 HD22 sing N N 111 
ASN   OXT HXT  sing N N 112 
ASP   N   CA   sing N N 113 
ASP   N   H    sing N N 114 
ASP   N   H2   sing N N 115 
ASP   CA  C    sing N N 116 
ASP   CA  CB   sing N N 117 
ASP   CA  HA   sing N N 118 
ASP   C   O    doub N N 119 
ASP   C   OXT  sing N N 120 
ASP   CB  CG   sing N N 121 
ASP   CB  HB2  sing N N 122 
ASP   CB  HB3  sing N N 123 
ASP   CG  OD1  doub N N 124 
ASP   CG  OD2  sing N N 125 
ASP   OD2 HD2  sing N N 126 
ASP   OXT HXT  sing N N 127 
CYS   N   CA   sing N N 128 
CYS   N   H    sing N N 129 
CYS   N   H2   sing N N 130 
CYS   CA  C    sing N N 131 
CYS   CA  CB   sing N N 132 
CYS   CA  HA   sing N N 133 
CYS   C   O    doub N N 134 
CYS   C   OXT  sing N N 135 
CYS   CB  SG   sing N N 136 
CYS   CB  HB2  sing N N 137 
CYS   CB  HB3  sing N N 138 
CYS   SG  HG   sing N N 139 
CYS   OXT HXT  sing N N 140 
GLN   N   CA   sing N N 141 
GLN   N   H    sing N N 142 
GLN   N   H2   sing N N 143 
GLN   CA  C    sing N N 144 
GLN   CA  CB   sing N N 145 
GLN   CA  HA   sing N N 146 
GLN   C   O    doub N N 147 
GLN   C   OXT  sing N N 148 
GLN   CB  CG   sing N N 149 
GLN   CB  HB2  sing N N 150 
GLN   CB  HB3  sing N N 151 
GLN   CG  CD   sing N N 152 
GLN   CG  HG2  sing N N 153 
GLN   CG  HG3  sing N N 154 
GLN   CD  OE1  doub N N 155 
GLN   CD  NE2  sing N N 156 
GLN   NE2 HE21 sing N N 157 
GLN   NE2 HE22 sing N N 158 
GLN   OXT HXT  sing N N 159 
GLU   N   CA   sing N N 160 
GLU   N   H    sing N N 161 
GLU   N   H2   sing N N 162 
GLU   CA  C    sing N N 163 
GLU   CA  CB   sing N N 164 
GLU   CA  HA   sing N N 165 
GLU   C   O    doub N N 166 
GLU   C   OXT  sing N N 167 
GLU   CB  CG   sing N N 168 
GLU   CB  HB2  sing N N 169 
GLU   CB  HB3  sing N N 170 
GLU   CG  CD   sing N N 171 
GLU   CG  HG2  sing N N 172 
GLU   CG  HG3  sing N N 173 
GLU   CD  OE1  doub N N 174 
GLU   CD  OE2  sing N N 175 
GLU   OE2 HE2  sing N N 176 
GLU   OXT HXT  sing N N 177 
GLY   N   CA   sing N N 178 
GLY   N   H    sing N N 179 
GLY   N   H2   sing N N 180 
GLY   CA  C    sing N N 181 
GLY   CA  HA2  sing N N 182 
GLY   CA  HA3  sing N N 183 
GLY   C   O    doub N N 184 
GLY   C   OXT  sing N N 185 
GLY   OXT HXT  sing N N 186 
HIS   N   CA   sing N N 187 
HIS   N   H    sing N N 188 
HIS   N   H2   sing N N 189 
HIS   CA  C    sing N N 190 
HIS   CA  CB   sing N N 191 
HIS   CA  HA   sing N N 192 
HIS   C   O    doub N N 193 
HIS   C   OXT  sing N N 194 
HIS   CB  CG   sing N N 195 
HIS   CB  HB2  sing N N 196 
HIS   CB  HB3  sing N N 197 
HIS   CG  ND1  sing Y N 198 
HIS   CG  CD2  doub Y N 199 
HIS   ND1 CE1  doub Y N 200 
HIS   ND1 HD1  sing N N 201 
HIS   CD2 NE2  sing Y N 202 
HIS   CD2 HD2  sing N N 203 
HIS   CE1 NE2  sing Y N 204 
HIS   CE1 HE1  sing N N 205 
HIS   NE2 HE2  sing N N 206 
HIS   OXT HXT  sing N N 207 
HOH   O   H1   sing N N 208 
HOH   O   H2   sing N N 209 
ILE   N   CA   sing N N 210 
ILE   N   H    sing N N 211 
ILE   N   H2   sing N N 212 
ILE   CA  C    sing N N 213 
ILE   CA  CB   sing N N 214 
ILE   CA  HA   sing N N 215 
ILE   C   O    doub N N 216 
ILE   C   OXT  sing N N 217 
ILE   CB  CG1  sing N N 218 
ILE   CB  CG2  sing N N 219 
ILE   CB  HB   sing N N 220 
ILE   CG1 CD1  sing N N 221 
ILE   CG1 HG12 sing N N 222 
ILE   CG1 HG13 sing N N 223 
ILE   CG2 HG21 sing N N 224 
ILE   CG2 HG22 sing N N 225 
ILE   CG2 HG23 sing N N 226 
ILE   CD1 HD11 sing N N 227 
ILE   CD1 HD12 sing N N 228 
ILE   CD1 HD13 sing N N 229 
ILE   OXT HXT  sing N N 230 
LEU   N   CA   sing N N 231 
LEU   N   H    sing N N 232 
LEU   N   H2   sing N N 233 
LEU   CA  C    sing N N 234 
LEU   CA  CB   sing N N 235 
LEU   CA  HA   sing N N 236 
LEU   C   O    doub N N 237 
LEU   C   OXT  sing N N 238 
LEU   CB  CG   sing N N 239 
LEU   CB  HB2  sing N N 240 
LEU   CB  HB3  sing N N 241 
LEU   CG  CD1  sing N N 242 
LEU   CG  CD2  sing N N 243 
LEU   CG  HG   sing N N 244 
LEU   CD1 HD11 sing N N 245 
LEU   CD1 HD12 sing N N 246 
LEU   CD1 HD13 sing N N 247 
LEU   CD2 HD21 sing N N 248 
LEU   CD2 HD22 sing N N 249 
LEU   CD2 HD23 sing N N 250 
LEU   OXT HXT  sing N N 251 
LYS   N   CA   sing N N 252 
LYS   N   H    sing N N 253 
LYS   N   H2   sing N N 254 
LYS   CA  C    sing N N 255 
LYS   CA  CB   sing N N 256 
LYS   CA  HA   sing N N 257 
LYS   C   O    doub N N 258 
LYS   C   OXT  sing N N 259 
LYS   CB  CG   sing N N 260 
LYS   CB  HB2  sing N N 261 
LYS   CB  HB3  sing N N 262 
LYS   CG  CD   sing N N 263 
LYS   CG  HG2  sing N N 264 
LYS   CG  HG3  sing N N 265 
LYS   CD  CE   sing N N 266 
LYS   CD  HD2  sing N N 267 
LYS   CD  HD3  sing N N 268 
LYS   CE  NZ   sing N N 269 
LYS   CE  HE2  sing N N 270 
LYS   CE  HE3  sing N N 271 
LYS   NZ  HZ1  sing N N 272 
LYS   NZ  HZ2  sing N N 273 
LYS   NZ  HZ3  sing N N 274 
LYS   OXT HXT  sing N N 275 
PHE   N   CA   sing N N 276 
PHE   N   H    sing N N 277 
PHE   N   H2   sing N N 278 
PHE   CA  C    sing N N 279 
PHE   CA  CB   sing N N 280 
PHE   CA  HA   sing N N 281 
PHE   C   O    doub N N 282 
PHE   C   OXT  sing N N 283 
PHE   CB  CG   sing N N 284 
PHE   CB  HB2  sing N N 285 
PHE   CB  HB3  sing N N 286 
PHE   CG  CD1  doub Y N 287 
PHE   CG  CD2  sing Y N 288 
PHE   CD1 CE1  sing Y N 289 
PHE   CD1 HD1  sing N N 290 
PHE   CD2 CE2  doub Y N 291 
PHE   CD2 HD2  sing N N 292 
PHE   CE1 CZ   doub Y N 293 
PHE   CE1 HE1  sing N N 294 
PHE   CE2 CZ   sing Y N 295 
PHE   CE2 HE2  sing N N 296 
PHE   CZ  HZ   sing N N 297 
PHE   OXT HXT  sing N N 298 
PRO   N   CA   sing N N 299 
PRO   N   CD   sing N N 300 
PRO   N   H    sing N N 301 
PRO   CA  C    sing N N 302 
PRO   CA  CB   sing N N 303 
PRO   CA  HA   sing N N 304 
PRO   C   O    doub N N 305 
PRO   C   OXT  sing N N 306 
PRO   CB  CG   sing N N 307 
PRO   CB  HB2  sing N N 308 
PRO   CB  HB3  sing N N 309 
PRO   CG  CD   sing N N 310 
PRO   CG  HG2  sing N N 311 
PRO   CG  HG3  sing N N 312 
PRO   CD  HD2  sing N N 313 
PRO   CD  HD3  sing N N 314 
PRO   OXT HXT  sing N N 315 
SER   N   CA   sing N N 316 
SER   N   H    sing N N 317 
SER   N   H2   sing N N 318 
SER   CA  C    sing N N 319 
SER   CA  CB   sing N N 320 
SER   CA  HA   sing N N 321 
SER   C   O    doub N N 322 
SER   C   OXT  sing N N 323 
SER   CB  OG   sing N N 324 
SER   CB  HB2  sing N N 325 
SER   CB  HB3  sing N N 326 
SER   OG  HG   sing N N 327 
SER   OXT HXT  sing N N 328 
THR   N   CA   sing N N 329 
THR   N   H    sing N N 330 
THR   N   H2   sing N N 331 
THR   CA  C    sing N N 332 
THR   CA  CB   sing N N 333 
THR   CA  HA   sing N N 334 
THR   C   O    doub N N 335 
THR   C   OXT  sing N N 336 
THR   CB  OG1  sing N N 337 
THR   CB  CG2  sing N N 338 
THR   CB  HB   sing N N 339 
THR   OG1 HG1  sing N N 340 
THR   CG2 HG21 sing N N 341 
THR   CG2 HG22 sing N N 342 
THR   CG2 HG23 sing N N 343 
THR   OXT HXT  sing N N 344 
TRP   N   CA   sing N N 345 
TRP   N   H    sing N N 346 
TRP   N   H2   sing N N 347 
TRP   CA  C    sing N N 348 
TRP   CA  CB   sing N N 349 
TRP   CA  HA   sing N N 350 
TRP   C   O    doub N N 351 
TRP   C   OXT  sing N N 352 
TRP   CB  CG   sing N N 353 
TRP   CB  HB2  sing N N 354 
TRP   CB  HB3  sing N N 355 
TRP   CG  CD1  doub Y N 356 
TRP   CG  CD2  sing Y N 357 
TRP   CD1 NE1  sing Y N 358 
TRP   CD1 HD1  sing N N 359 
TRP   CD2 CE2  doub Y N 360 
TRP   CD2 CE3  sing Y N 361 
TRP   NE1 CE2  sing Y N 362 
TRP   NE1 HE1  sing N N 363 
TRP   CE2 CZ2  sing Y N 364 
TRP   CE3 CZ3  doub Y N 365 
TRP   CE3 HE3  sing N N 366 
TRP   CZ2 CH2  doub Y N 367 
TRP   CZ2 HZ2  sing N N 368 
TRP   CZ3 CH2  sing Y N 369 
TRP   CZ3 HZ3  sing N N 370 
TRP   CH2 HH2  sing N N 371 
TRP   OXT HXT  sing N N 372 
TYR   N   CA   sing N N 373 
TYR   N   H    sing N N 374 
TYR   N   H2   sing N N 375 
TYR   CA  C    sing N N 376 
TYR   CA  CB   sing N N 377 
TYR   CA  HA   sing N N 378 
TYR   C   O    doub N N 379 
TYR   C   OXT  sing N N 380 
TYR   CB  CG   sing N N 381 
TYR   CB  HB2  sing N N 382 
TYR   CB  HB3  sing N N 383 
TYR   CG  CD1  doub Y N 384 
TYR   CG  CD2  sing Y N 385 
TYR   CD1 CE1  sing Y N 386 
TYR   CD1 HD1  sing N N 387 
TYR   CD2 CE2  doub Y N 388 
TYR   CD2 HD2  sing N N 389 
TYR   CE1 CZ   doub Y N 390 
TYR   CE1 HE1  sing N N 391 
TYR   CE2 CZ   sing Y N 392 
TYR   CE2 HE2  sing N N 393 
TYR   CZ  OH   sing N N 394 
TYR   OH  HH   sing N N 395 
TYR   OXT HXT  sing N N 396 
VAL   N   CA   sing N N 397 
VAL   N   H    sing N N 398 
VAL   N   H2   sing N N 399 
VAL   CA  C    sing N N 400 
VAL   CA  CB   sing N N 401 
VAL   CA  HA   sing N N 402 
VAL   C   O    doub N N 403 
VAL   C   OXT  sing N N 404 
VAL   CB  CG1  sing N N 405 
VAL   CB  CG2  sing N N 406 
VAL   CB  HB   sing N N 407 
VAL   CG1 HG11 sing N N 408 
VAL   CG1 HG12 sing N N 409 
VAL   CG1 HG13 sing N N 410 
VAL   CG2 HG21 sing N N 411 
VAL   CG2 HG22 sing N N 412 
VAL   CG2 HG23 sing N N 413 
VAL   OXT HXT  sing N N 414 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Howard Hughes Medical Institute (HHMI)'           'United States' HHMI-EPI          1 
'National Science Foundation (NSF, United States)' 'United States' DMR-1548924       2 
'Department of Energy (DOE, United States)'        'United States' DE-FC02-02ER63421 3 
# 
_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   9PAP 
_pdbx_initial_refinement_model.details          ? 
# 
_pdbx_serial_crystallography_data_reduction.diffrn_id             1 
_pdbx_serial_crystallography_data_reduction.frames_total          ? 
_pdbx_serial_crystallography_data_reduction.xfel_pulse_events     ? 
_pdbx_serial_crystallography_data_reduction.frame_hits            ? 
_pdbx_serial_crystallography_data_reduction.crystal_hits          27585 
_pdbx_serial_crystallography_data_reduction.droplet_hits          ? 
_pdbx_serial_crystallography_data_reduction.frames_failed_index   ? 
_pdbx_serial_crystallography_data_reduction.frames_indexed        21818 
_pdbx_serial_crystallography_data_reduction.lattices_indexed      23401 
_pdbx_serial_crystallography_data_reduction.xfel_run_numbers      ? 
_pdbx_serial_crystallography_data_reduction.lattices_merged       ? 
# 
_pdbx_serial_crystallography_sample_delivery.diffrn_id     1 
_pdbx_serial_crystallography_sample_delivery.description   ? 
_pdbx_serial_crystallography_sample_delivery.method        'fixed target' 
# 
_pdbx_serial_crystallography_sample_delivery_fixed_target.diffrn_id                       1 
_pdbx_serial_crystallography_sample_delivery_fixed_target.description                     'mylar foils' 
_pdbx_serial_crystallography_sample_delivery_fixed_target.sample_holding                  ? 
_pdbx_serial_crystallography_sample_delivery_fixed_target.support_base                    ? 
_pdbx_serial_crystallography_sample_delivery_fixed_target.sample_unit_size                ? 
_pdbx_serial_crystallography_sample_delivery_fixed_target.crystals_per_unit               ? 
_pdbx_serial_crystallography_sample_delivery_fixed_target.sample_solvent                  ? 
_pdbx_serial_crystallography_sample_delivery_fixed_target.sample_dehydration_prevention   ? 
_pdbx_serial_crystallography_sample_delivery_fixed_target.motion_control                  ? 
_pdbx_serial_crystallography_sample_delivery_fixed_target.velocity_horizontal             ? 
_pdbx_serial_crystallography_sample_delivery_fixed_target.velocity_vertical               ? 
_pdbx_serial_crystallography_sample_delivery_fixed_target.details                         ? 
# 
_atom_sites.entry_id                    9NB7 
_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]   0.023529 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.020450 
_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]   0.009852 
_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 
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   . ILE   A 1 1   ? 22.838  -9.997  21.066 1.00 32.73 ?  1   ILE   A N   1 
ATOM   2    C CA  . ILE   A 1 1   ? 22.631  -9.052  19.965 1.00 28.86 ?  1   ILE   A CA  1 
ATOM   3    C C   . ILE   A 1 1   ? 23.892  -8.222  19.732 1.00 25.67 ?  1   ILE   A C   1 
ATOM   4    O O   . ILE   A 1 1   ? 24.705  -8.051  20.643 1.00 28.19 ?  1   ILE   A O   1 
ATOM   5    C CB  . ILE   A 1 1   ? 21.405  -8.155  20.237 1.00 23.99 ?  1   ILE   A CB  1 
ATOM   6    C CG1 . ILE   A 1 1   ? 21.644  -7.261  21.461 1.00 25.52 ?  1   ILE   A CG1 1 
ATOM   7    C CG2 . ILE   A 1 1   ? 20.179  -9.021  20.438 1.00 30.42 ?  1   ILE   A CG2 1 
ATOM   8    C CD1 . ILE   A 1 1   ? 20.438  -6.435  21.853 1.00 27.04 ?  1   ILE   A CD1 1 
ATOM   9    N N   . PRO   A 1 2   ? 24.044  -7.692  18.522 1.00 27.64 ?  2   PRO   A N   1 
ATOM   10   C CA  . PRO   A 1 2   ? 25.319  -7.078  18.133 1.00 35.20 ?  2   PRO   A CA  1 
ATOM   11   C C   . PRO   A 1 2   ? 25.511  -5.706  18.758 1.00 29.94 ?  2   PRO   A C   1 
ATOM   12   O O   . PRO   A 1 2   ? 24.601  -5.107  19.331 1.00 27.54 ?  2   PRO   A O   1 
ATOM   13   C CB  . PRO   A 1 2   ? 25.224  -6.954  16.610 1.00 29.14 ?  2   PRO   A CB  1 
ATOM   14   C CG  . PRO   A 1 2   ? 23.940  -7.556  16.209 1.00 37.51 ?  2   PRO   A CG  1 
ATOM   15   C CD  . PRO   A 1 2   ? 23.076  -7.701  17.413 1.00 32.17 ?  2   PRO   A CD  1 
ATOM   16   N N   . GLU   A 1 3   ? 26.740  -5.209  18.599 1.00 28.75 ?  3   GLU   A N   1 
ATOM   17   C CA  . GLU   A 1 3   ? 27.117  -3.892  19.095 1.00 29.25 ?  3   GLU   A CA  1 
ATOM   18   C C   . GLU   A 1 3   ? 26.420  -2.794  18.298 1.00 31.50 ?  3   GLU   A C   1 
ATOM   19   O O   . GLU   A 1 3   ? 26.034  -1.757  18.851 1.00 26.80 ?  3   GLU   A O   1 
ATOM   20   C CB  . GLU   A 1 3   ? 28.630  -3.728  18.982 1.00 35.86 ?  3   GLU   A CB  1 
ATOM   21   C CG  . GLU   A 1 3   ? 29.464  -4.761  19.737 1.00 52.59 ?  3   GLU   A CG  1 
ATOM   22   C CD  . GLU   A 1 3   ? 30.390  -4.125  20.752 1.00 56.46 ?  3   GLU   A CD  1 
ATOM   23   O OE1 . GLU   A 1 3   ? 30.038  -4.079  21.948 1.00 65.57 ?  3   GLU   A OE1 1 
ATOM   24   O OE2 . GLU   A 1 3   ? 31.470  -3.653  20.342 1.00 63.53 ?  3   GLU   A OE2 1 
ATOM   25   N N   . TYR   A 1 4   ? 26.279  -2.995  16.990 1.00 26.15 ?  4   TYR   A N   1 
ATOM   26   C CA  . TYR   A 1 4   ? 25.650  -2.025  16.107 1.00 28.08 ?  4   TYR   A CA  1 
ATOM   27   C C   . TYR   A 1 4   ? 24.547  -2.716  15.331 1.00 28.80 ?  4   TYR   A C   1 
ATOM   28   O O   . TYR   A 1 4   ? 24.727  -3.831  14.825 1.00 29.32 ?  4   TYR   A O   1 
ATOM   29   C CB  . TYR   A 1 4   ? 26.647  -1.422  15.113 1.00 27.63 ?  4   TYR   A CB  1 
ATOM   30   C CG  . TYR   A 1 4   ? 27.636  -0.475  15.736 1.00 33.30 ?  4   TYR   A CG  1 
ATOM   31   C CD1 . TYR   A 1 4   ? 28.810  -0.946  16.312 1.00 35.42 ?  4   TYR   A CD1 1 
ATOM   32   C CD2 . TYR   A 1 4   ? 27.402  0.889   15.744 1.00 31.22 ?  4   TYR   A CD2 1 
ATOM   33   C CE1 . TYR   A 1 4   ? 29.726  -0.073  16.876 1.00 34.21 ?  4   TYR   A CE1 1 
ATOM   34   C CE2 . TYR   A 1 4   ? 28.305  1.763   16.296 1.00 36.62 ?  4   TYR   A CE2 1 
ATOM   35   C CZ  . TYR   A 1 4   ? 29.469  1.279   16.861 1.00 35.70 ?  4   TYR   A CZ  1 
ATOM   36   O OH  . TYR   A 1 4   ? 30.362  2.165   17.418 1.00 45.41 ?  4   TYR   A OH  1 
ATOM   37   N N   . VAL   A 1 5   ? 23.410  -2.049  15.241 1.00 24.82 ?  5   VAL   A N   1 
ATOM   38   C CA  . VAL   A 1 5   ? 22.334  -2.460  14.353 1.00 26.19 ?  5   VAL   A CA  1 
ATOM   39   C C   . VAL   A 1 5   ? 21.936  -1.240  13.551 1.00 26.79 ?  5   VAL   A C   1 
ATOM   40   O O   . VAL   A 1 5   ? 21.821  -0.148  14.106 1.00 23.66 ?  5   VAL   A O   1 
ATOM   41   C CB  . VAL   A 1 5   ? 21.140  -3.017  15.145 1.00 25.89 ?  5   VAL   A CB  1 
ATOM   42   C CG1 . VAL   A 1 5   ? 19.907  -3.117  14.249 1.00 27.55 ?  5   VAL   A CG1 1 
ATOM   43   C CG2 . VAL   A 1 5   ? 21.524  -4.366  15.781 1.00 28.56 ?  5   VAL   A CG2 1 
ATOM   44   N N   . ASP   A 1 6   ? 21.745  -1.412  12.242 1.00 22.17 ?  6   ASP   A N   1 
ATOM   45   C CA  . ASP   A 1 6   ? 21.295  -0.301  11.402 1.00 24.17 ?  6   ASP   A CA  1 
ATOM   46   C C   . ASP   A 1 6   ? 20.455  -0.919  10.297 1.00 28.07 ?  6   ASP   A C   1 
ATOM   47   O O   . ASP   A 1 6   ? 21.007  -1.439  9.326  1.00 28.19 ?  6   ASP   A O   1 
ATOM   48   C CB  . ASP   A 1 6   ? 22.456  0.489   10.822 1.00 26.01 ?  6   ASP   A CB  1 
ATOM   49   C CG  . ASP   A 1 6   ? 22.012  1.807   10.180 1.00 29.12 ?  6   ASP   A CG  1 
ATOM   50   O OD1 . ASP   A 1 6   ? 20.846  1.922   9.746  1.00 28.28 ?  6   ASP   A OD1 1 
ATOM   51   O OD2 . ASP   A 1 6   ? 22.851  2.712   10.062 1.00 36.87 ?  6   ASP   A OD2 1 
ATOM   52   N N   . TRP   A 1 7   ? 19.134  -0.855  10.453 1.00 26.12 ?  7   TRP   A N   1 
ATOM   53   C CA  . TRP   A 1 7   ? 18.242  -1.462  9.474  1.00 26.60 ?  7   TRP   A CA  1 
ATOM   54   C C   . TRP   A 1 7   ? 18.299  -0.781  8.119  1.00 29.29 ?  7   TRP   A C   1 
ATOM   55   O O   . TRP   A 1 7   ? 17.869  -1.380  7.125  1.00 26.33 ?  7   TRP   A O   1 
ATOM   56   C CB  . TRP   A 1 7   ? 16.814  -1.466  10.017 1.00 24.74 ?  7   TRP   A CB  1 
ATOM   57   C CG  . TRP   A 1 7   ? 16.675  -2.553  10.995 1.00 28.39 ?  7   TRP   A CG  1 
ATOM   58   C CD1 . TRP   A 1 7   ? 16.513  -2.445  12.347 1.00 26.20 ?  7   TRP   A CD1 1 
ATOM   59   C CD2 . TRP   A 1 7   ? 16.752  -3.947  10.706 1.00 28.37 ?  7   TRP   A CD2 1 
ATOM   60   N NE1 . TRP   A 1 7   ? 16.464  -3.697  12.912 1.00 29.47 ?  7   TRP   A NE1 1 
ATOM   61   C CE2 . TRP   A 1 7   ? 16.612  -4.634  11.924 1.00 29.63 ?  7   TRP   A CE2 1 
ATOM   62   C CE3 . TRP   A 1 7   ? 16.909  -4.686  9.524  1.00 31.29 ?  7   TRP   A CE3 1 
ATOM   63   C CZ2 . TRP   A 1 7   ? 16.619  -6.030  11.996 1.00 33.32 ?  7   TRP   A CZ2 1 
ATOM   64   C CZ3 . TRP   A 1 7   ? 16.924  -6.060  9.602  1.00 37.28 ?  7   TRP   A CZ3 1 
ATOM   65   C CH2 . TRP   A 1 7   ? 16.780  -6.719  10.828 1.00 33.55 ?  7   TRP   A CH2 1 
ATOM   66   N N   . ARG   A 1 8   ? 18.818  0.448   8.044  1.00 23.92 ?  8   ARG   A N   1 
ATOM   67   C CA  . ARG   A 1 8   ? 18.988  1.068   6.733  1.00 28.46 ?  8   ARG   A CA  1 
ATOM   68   C C   . ARG   A 1 8   ? 20.031  0.337   5.902  1.00 34.85 ?  8   ARG   A C   1 
ATOM   69   O O   . ARG   A 1 8   ? 19.924  0.295   4.672  1.00 31.20 ?  8   ARG   A O   1 
ATOM   70   C CB  . ARG   A 1 8   ? 19.385  2.534   6.883  1.00 27.31 ?  8   ARG   A CB  1 
ATOM   71   C CG  . ARG   A 1 8   ? 18.485  3.329   7.789  1.00 30.62 ?  8   ARG   A CG  1 
ATOM   72   C CD  . ARG   A 1 8   ? 19.082  4.693   7.885  1.00 37.93 ?  8   ARG   A CD  1 
ATOM   73   N NE  . ARG   A 1 8   ? 20.343  4.610   8.604  1.00 26.41 ?  8   ARG   A NE  1 
ATOM   74   C CZ  . ARG   A 1 8   ? 21.029  5.652   9.036  1.00 35.87 ?  8   ARG   A CZ  1 
ATOM   75   N NH1 . ARG   A 1 8   ? 20.641  6.889   8.769  1.00 37.36 ?  8   ARG   A NH1 1 
ATOM   76   N NH2 . ARG   A 1 8   ? 22.158  5.447   9.710  1.00 30.71 ?  8   ARG   A NH2 1 
ATOM   77   N N   . GLN   A 1 9   ? 21.047  -0.235  6.553  1.00 33.91 ?  9   GLN   A N   1 
ATOM   78   C CA  . GLN   A 1 9   ? 22.074  -0.976  5.830  1.00 38.72 ?  9   GLN   A CA  1 
ATOM   79   C C   . GLN   A 1 9   ? 21.582  -2.338  5.351  1.00 34.20 ?  9   GLN   A C   1 
ATOM   80   O O   . GLN   A 1 9   ? 22.169  -2.903  4.425  1.00 35.94 ?  9   GLN   A O   1 
ATOM   81   C CB  . GLN   A 1 9   ? 23.323  -1.127  6.706  1.00 36.39 ?  9   GLN   A CB  1 
ATOM   82   C CG  . GLN   A 1 9   ? 24.116  0.172   6.799  1.00 44.49 ?  9   GLN   A CG  1 
ATOM   83   C CD  . GLN   A 1 9   ? 25.089  0.217   7.966  1.00 64.81 ?  9   GLN   A CD  1 
ATOM   84   O OE1 . GLN   A 1 9   ? 25.715  1.249   8.223  1.00 70.99 ?  9   GLN   A OE1 1 
ATOM   85   N NE2 . GLN   A 1 9   ? 25.238  -0.905  8.667  1.00 61.28 ?  9   GLN   A NE2 1 
ATOM   86   N N   . LYS   A 1 10  ? 20.527  -2.878  5.954  1.00 29.04 ?  10  LYS   A N   1 
ATOM   87   C CA  . LYS   A 1 10  ? 19.900  -4.099  5.476  1.00 31.39 ?  10  LYS   A CA  1 
ATOM   88   C C   . LYS   A 1 10  ? 18.780  -3.821  4.488  1.00 38.34 ?  10  LYS   A C   1 
ATOM   89   O O   . LYS   A 1 10  ? 18.004  -4.730  4.173  1.00 38.11 ?  10  LYS   A O   1 
ATOM   90   C CB  . LYS   A 1 10  ? 19.378  -4.916  6.662  1.00 35.04 ?  10  LYS   A CB  1 
ATOM   91   C CG  . LYS   A 1 10  ? 20.461  -5.284  7.676  1.00 46.50 ?  10  LYS   A CG  1 
ATOM   92   C CD  . LYS   A 1 10  ? 21.241  -6.512  7.201  1.00 51.75 ?  10  LYS   A CD  1 
ATOM   93   C CE  . LYS   A 1 10  ? 22.717  -6.443  7.595  1.00 61.23 ?  10  LYS   A CE  1 
ATOM   94   N NZ  . LYS   A 1 10  ? 23.052  -7.314  8.762  1.00 63.39 ?  10  LYS   A NZ  1 
ATOM   95   N N   . GLY   A 1 11  ? 18.688  -2.590  3.993  1.00 32.35 ?  11  GLY   A N   1 
ATOM   96   C CA  . GLY   A 1 11  ? 17.667  -2.232  3.025  1.00 30.77 ?  11  GLY   A CA  1 
ATOM   97   C C   . GLY   A 1 11  ? 16.250  -2.385  3.526  1.00 33.29 ?  11  GLY   A C   1 
ATOM   98   O O   . GLY   A 1 11  ? 15.351  -2.663  2.728  1.00 30.93 ?  11  GLY   A O   1 
ATOM   99   N N   . ALA   A 1 12  ? 16.019  -2.182  4.830  1.00 28.74 ?  12  ALA   A N   1 
ATOM   100  C CA  . ALA   A 1 12  ? 14.700  -2.350  5.430  1.00 29.28 ?  12  ALA   A CA  1 
ATOM   101  C C   . ALA   A 1 12  ? 14.044  -1.027  5.796  1.00 29.83 ?  12  ALA   A C   1 
ATOM   102  O O   . ALA   A 1 12  ? 13.038  -1.013  6.520  1.00 27.66 ?  12  ALA   A O   1 
ATOM   103  C CB  . ALA   A 1 12  ? 14.789  -3.229  6.670  1.00 28.16 ?  12  ALA   A CB  1 
ATOM   104  N N   . VAL   A 1 13  ? 14.597  0.085   5.339  1.00 26.46 ?  13  VAL   A N   1 
ATOM   105  C CA  . VAL   A 1 13  ? 14.092  1.402   5.689  1.00 27.08 ?  13  VAL   A CA  1 
ATOM   106  C C   . VAL   A 1 13  ? 13.895  2.189   4.408  1.00 23.81 ?  13  VAL   A C   1 
ATOM   107  O O   . VAL   A 1 13  ? 14.804  2.276   3.570  1.00 26.88 ?  13  VAL   A O   1 
ATOM   108  C CB  . VAL   A 1 13  ? 15.042  2.153   6.638  1.00 25.64 ?  13  VAL   A CB  1 
ATOM   109  C CG1 . VAL   A 1 13  ? 14.421  3.483   7.070  1.00 23.93 ?  13  VAL   A CG1 1 
ATOM   110  C CG2 . VAL   A 1 13  ? 15.346  1.293   7.856  1.00 25.49 ?  13  VAL   A CG2 1 
ATOM   111  N N   . THR   A 1 14  ? 12.724  2.767   4.264  1.00 23.04 ?  14  THR   A N   1 
ATOM   112  C CA  . THR   A 1 14  ? 12.402  3.580   3.105  1.00 25.85 ?  14  THR   A CA  1 
ATOM   113  C C   . THR   A 1 14  ? 12.853  5.007   3.352  1.00 22.04 ?  14  THR   A C   1 
ATOM   114  O O   . THR   A 1 14  ? 13.274  5.363   4.464  1.00 21.25 ?  14  THR   A O   1 
ATOM   115  C CB  . THR   A 1 14  ? 10.903  3.494   2.827  1.00 20.50 ?  14  THR   A CB  1 
ATOM   116  O OG1 . THR   A 1 14  ? 10.203  4.175   3.875  1.00 24.88 ?  14  THR   A OG1 1 
ATOM   117  C CG2 . THR   A 1 14  ? 10.470  2.031   2.708  1.00 20.99 ?  14  THR   A CG2 1 
ATOM   118  N N   . PRO   A 1 15  ? 12.799  5.859   2.333  1.00 22.64 ?  15  PRO   A N   1 
ATOM   119  C CA  . PRO   A 1 15  ? 13.271  7.232   2.514  1.00 22.21 ?  15  PRO   A CA  1 
ATOM   120  C C   . PRO   A 1 15  ? 12.504  7.935   3.622  1.00 24.53 ?  15  PRO   A C   1 
ATOM   121  O O   . PRO   A 1 15  ? 11.352  7.606   3.928  1.00 25.08 ?  15  PRO   A O   1 
ATOM   122  C CB  . PRO   A 1 15  ? 12.991  7.864   1.153  1.00 24.58 ?  15  PRO   A CB  1 
ATOM   123  C CG  . PRO   A 1 15  ? 13.257  6.699   0.217  1.00 23.60 ?  15  PRO   A CG  1 
ATOM   124  C CD  . PRO   A 1 15  ? 12.487  5.604   0.908  1.00 23.92 ?  15  PRO   A CD  1 
ATOM   125  N N   . VAL   A 1 16  ? 13.171  8.920   4.212  1.00 20.70 ?  16  VAL   A N   1 
ATOM   126  C CA  . VAL   A 1 16  ? 12.591  9.720   5.277  1.00 22.90 ?  16  VAL   A CA  1 
ATOM   127  C C   . VAL   A 1 16  ? 11.426  10.531  4.731  1.00 24.82 ?  16  VAL   A C   1 
ATOM   128  O O   . VAL   A 1 16  ? 11.484  11.102  3.631  1.00 22.70 ?  16  VAL   A O   1 
ATOM   129  C CB  . VAL   A 1 16  ? 13.673  10.624  5.889  1.00 25.70 ?  16  VAL   A CB  1 
ATOM   130  C CG1 . VAL   A 1 16  ? 13.063  11.733  6.750  1.00 19.19 ?  16  VAL   A CG1 1 
ATOM   131  C CG2 . VAL   A 1 16  ? 14.623  9.771   6.680  1.00 23.46 ?  16  VAL   A CG2 1 
ATOM   132  N N   . LYS   A 1 17  ? 10.349  10.570  5.491  1.00 21.78 ?  17  LYS   A N   1 
ATOM   133  C CA  . LYS   A 1 17  ? 9.173   11.306  5.073  1.00 21.75 ?  17  LYS   A CA  1 
ATOM   134  C C   . LYS   A 1 17  ? 9.031   12.564  5.910  1.00 27.50 ?  17  LYS   A C   1 
ATOM   135  O O   . LYS   A 1 17  ? 9.725   12.768  6.908  1.00 23.98 ?  17  LYS   A O   1 
ATOM   136  C CB  . LYS   A 1 17  ? 7.919   10.436  5.189  1.00 25.72 ?  17  LYS   A CB  1 
ATOM   137  C CG  . LYS   A 1 17  ? 8.068   9.016   4.625  1.00 25.68 ?  17  LYS   A CG  1 
ATOM   138  C CD  . LYS   A 1 17  ? 8.546   9.052   3.176  1.00 28.10 ?  17  LYS   A CD  1 
ATOM   139  C CE  . LYS   A 1 17  ? 8.164   7.773   2.473  1.00 27.50 ?  17  LYS   A CE  1 
ATOM   140  N NZ  . LYS   A 1 17  ? 8.917   6.595   2.953  1.00 22.71 ?  17  LYS   A NZ  1 
ATOM   141  N N   . ASN   A 1 18  ? 8.125   13.427  5.465  1.00 23.07 ?  18  ASN   A N   1 
ATOM   142  C CA  . ASN   A 1 18  ? 7.776   14.634  6.197  1.00 26.31 ?  18  ASN   A CA  1 
ATOM   143  C C   . ASN   A 1 18  ? 6.283   14.571  6.475  1.00 24.41 ?  18  ASN   A C   1 
ATOM   144  O O   . ASN   A 1 18  ? 5.462   14.618  5.546  1.00 26.62 ?  18  ASN   A O   1 
ATOM   145  C CB  . ASN   A 1 18  ? 8.157   15.879  5.412  1.00 24.11 ?  18  ASN   A CB  1 
ATOM   146  C CG  . ASN   A 1 18  ? 8.033   17.131  6.230  1.00 26.31 ?  18  ASN   A CG  1 
ATOM   147  O OD1 . ASN   A 1 18  ? 7.369   17.141  7.273  1.00 28.32 ?  18  ASN   A OD1 1 
ATOM   148  N ND2 . ASN   A 1 18  ? 8.714   18.188  5.800  1.00 42.08 ?  18  ASN   A ND2 1 
ATOM   149  N N   . GLN   A 1 19  ? 5.929   14.434  7.751  1.00 21.62 ?  19  GLN   A N   1 
ATOM   150  C CA  . GLN   A 1 19  ? 4.515   14.388  8.079  1.00 24.66 ?  19  GLN   A CA  1 
ATOM   151  C C   . GLN   A 1 19  ? 3.832   15.731  7.849  1.00 23.93 ?  19  GLN   A C   1 
ATOM   152  O O   . GLN   A 1 19  ? 2.594   15.787  7.828  1.00 23.81 ?  19  GLN   A O   1 
ATOM   153  C CB  . GLN   A 1 19  ? 4.322   13.974  9.526  1.00 19.03 ?  19  GLN   A CB  1 
ATOM   154  C CG  . GLN   A 1 19  ? 4.846   14.996  10.529 1.00 23.36 ?  19  GLN   A CG  1 
ATOM   155  C CD  . GLN   A 1 19  ? 4.730   14.478  11.930 1.00 25.37 ?  19  GLN   A CD  1 
ATOM   156  O OE1 . GLN   A 1 19  ? 5.554   13.686  12.390 1.00 26.33 ?  19  GLN   A OE1 1 
ATOM   157  N NE2 . GLN   A 1 19  ? 3.653   14.867  12.605 1.00 26.51 ?  19  GLN   A NE2 1 
ATOM   158  N N   . GLY   A 1 20  ? 4.593   16.815  7.721  1.00 22.48 ?  20  GLY   A N   1 
ATOM   159  C CA  . GLY   A 1 20  ? 3.889   18.082  7.517  1.00 26.66 ?  20  GLY   A CA  1 
ATOM   160  C C   . GLY   A 1 20  ? 3.249   18.559  8.816  1.00 27.88 ?  20  GLY   A C   1 
ATOM   161  O O   . GLY   A 1 20  ? 3.644   18.172  9.913  1.00 28.24 ?  20  GLY   A O   1 
ATOM   162  N N   . SER   A 1 21  ? 2.233   19.418  8.690  1.00 27.46 ?  21  SER   A N   1 
ATOM   163  C CA  . SER   A 1 21  ? 1.675   20.009  9.909  1.00 33.57 ?  21  SER   A CA  1 
ATOM   164  C C   . SER   A 1 21  ? 0.772   19.042  10.661 1.00 40.84 ?  21  SER   A C   1 
ATOM   165  O O   . SER   A 1 21  ? 0.488   19.255  11.846 1.00 41.62 ?  21  SER   A O   1 
ATOM   166  C CB  . SER   A 1 21  ? 0.892   21.285  9.590  1.00 36.50 ?  21  SER   A CB  1 
ATOM   167  O OG  . SER   A 1 21  ? 0.175   21.145  8.378  1.00 46.05 ?  21  SER   A OG  1 
ATOM   168  N N   . CYS   A 1 22  ? 0.336   17.987  9.997  1.00 31.61 ?  22  CYS   A N   1 
ATOM   169  C CA  . CYS   A 1 22  ? -0.573  17.011  10.566 1.00 27.01 ?  22  CYS   A CA  1 
ATOM   170  C C   . CYS   A 1 22  ? 0.099   16.219  11.684 1.00 25.97 ?  22  CYS   A C   1 
ATOM   171  O O   . CYS   A 1 22  ? 1.251   15.801  11.554 1.00 27.16 ?  22  CYS   A O   1 
ATOM   172  C CB  . CYS   A 1 22  ? -1.030  16.090  9.442  1.00 24.74 ?  22  CYS   A CB  1 
ATOM   173  S SG  . CYS   A 1 22  ? -2.033  14.724  9.901  1.00 28.09 ?  22  CYS   A SG  1 
ATOM   174  N N   . GLY   A 1 23  ? -0.632  16.008  12.781 1.00 27.69 ?  23  GLY   A N   1 
ATOM   175  C CA  . GLY   A 1 23  ? -0.138  15.237  13.910 1.00 27.27 ?  23  GLY   A CA  1 
ATOM   176  C C   . GLY   A 1 23  ? -0.266  13.750  13.681 1.00 27.38 ?  23  GLY   A C   1 
ATOM   177  O O   . GLY   A 1 23  ? -0.918  13.024  14.443 1.00 27.80 ?  23  GLY   A O   1 
ATOM   178  N N   . SER   A 1 24  ? 0.382   13.287  12.617 1.00 24.52 ?  24  SER   A N   1 
ATOM   179  C CA  . SER   A 1 24  ? 0.280   11.919  12.127 1.00 24.44 ?  24  SER   A CA  1 
ATOM   180  C C   . SER   A 1 24  ? 1.530   11.101  12.421 1.00 20.79 ?  24  SER   A C   1 
ATOM   181  O O   . SER   A 1 24  ? 1.715   10.028  11.841 1.00 23.23 ?  24  SER   A O   1 
ATOM   182  C CB  . SER   A 1 24  ? -0.010  11.944  10.630 1.00 25.28 ?  24  SER   A CB  1 
ATOM   183  O OG  . SER   A 1 24  ? 0.960   12.744  9.985  1.00 26.70 ?  24  SER   A OG  1 
ATOM   184  N N   . CYS   A 1 25  ? 2.386   11.587  13.321 1.00 22.51 ?  25  CYS   A N   1 
ATOM   185  C CA  . CYS   A 1 25  ? 3.615   10.872  13.640 1.00 22.51 ?  25  CYS   A CA  1 
ATOM   186  C C   . CYS   A 1 25  ? 3.345   9.420   13.992 1.00 24.36 ?  25  CYS   A C   1 
ATOM   187  O O   . CYS   A 1 25  ? 4.117   8.530   13.620 1.00 24.14 ?  25  CYS   A O   1 
ATOM   188  C CB  . CYS   A 1 25  ? 4.334   11.561  14.795 1.00 23.80 ?  25  CYS   A CB  1 
ATOM   189  S SG  . CYS   A 1 25  ? 3.328   11.601  16.294 1.00 31.85 ?  25  CYS   A SG  1 
ATOM   190  N N   . TRP   A 1 26  ? 2.259   9.168   14.731 1.00 23.62 ?  26  TRP   A N   1 
ATOM   191  C CA  . TRP   A 1 26  ? 1.907   7.805   15.111 1.00 25.69 ?  26  TRP   A CA  1 
ATOM   192  C C   . TRP   A 1 26  ? 1.733   6.911   13.888 1.00 26.46 ?  26  TRP   A C   1 
ATOM   193  O O   . TRP   A 1 26  ? 2.108   5.736   13.918 1.00 22.33 ?  26  TRP   A O   1 
ATOM   194  C CB  . TRP   A 1 26  ? 0.630   7.818   15.951 1.00 25.99 ?  26  TRP   A CB  1 
ATOM   195  C CG  . TRP   A 1 26  ? -0.513  8.506   15.246 1.00 23.77 ?  26  TRP   A CG  1 
ATOM   196  C CD1 . TRP   A 1 26  ? -0.761  9.858   15.184 1.00 29.26 ?  26  TRP   A CD1 1 
ATOM   197  C CD2 . TRP   A 1 26  ? -1.550  7.874   14.494 1.00 25.81 ?  26  TRP   A CD2 1 
ATOM   198  N NE1 . TRP   A 1 26  ? -1.897  10.093  14.427 1.00 25.23 ?  26  TRP   A NE1 1 
ATOM   199  C CE2 . TRP   A 1 26  ? -2.396  8.891   13.999 1.00 25.10 ?  26  TRP   A CE2 1 
ATOM   200  C CE3 . TRP   A 1 26  ? -1.845  6.546   14.184 1.00 22.77 ?  26  TRP   A CE3 1 
ATOM   201  C CZ2 . TRP   A 1 26  ? -3.525  8.614   13.223 1.00 25.51 ?  26  TRP   A CZ2 1 
ATOM   202  C CZ3 . TRP   A 1 26  ? -2.973  6.281   13.394 1.00 26.19 ?  26  TRP   A CZ3 1 
ATOM   203  C CH2 . TRP   A 1 26  ? -3.794  7.306   12.943 1.00 25.29 ?  26  TRP   A CH2 1 
ATOM   204  N N   . ALA   A 1 27  ? 1.182   7.452   12.790 1.00 23.03 ?  27  ALA   A N   1 
ATOM   205  C CA  . ALA   A 1 27  ? 1.013   6.639   11.590 1.00 24.14 ?  27  ALA   A CA  1 
ATOM   206  C C   . ALA   A 1 27  ? 2.334   6.448   10.866 1.00 22.36 ?  27  ALA   A C   1 
ATOM   207  O O   . ALA   A 1 27  ? 2.627   5.356   10.370 1.00 22.08 ?  27  ALA   A O   1 
ATOM   208  C CB  . ALA   A 1 27  ? -0.011  7.283   10.653 1.00 23.68 ?  27  ALA   A CB  1 
ATOM   209  N N   . PHE   A 1 28  ? 3.137   7.509   10.774 1.00 21.80 ?  28  PHE   A N   1 
ATOM   210  C CA  . PHE   A 1 28  ? 4.447   7.378   10.148 1.00 22.30 ?  28  PHE   A CA  1 
ATOM   211  C C   . PHE   A 1 28  ? 5.288   6.369   10.897 1.00 20.09 ?  28  PHE   A C   1 
ATOM   212  O O   . PHE   A 1 28  ? 5.912   5.496   10.291 1.00 24.18 ?  28  PHE   A O   1 
ATOM   213  C CB  . PHE   A 1 28  ? 5.122   8.738   10.109 1.00 19.20 ?  28  PHE   A CB  1 
ATOM   214  C CG  . PHE   A 1 28  ? 4.660   9.561   8.950  1.00 22.45 ?  28  PHE   A CG  1 
ATOM   215  C CD1 . PHE   A 1 28  ? 3.497   10.307  9.055  1.00 26.73 ?  28  PHE   A CD1 1 
ATOM   216  C CD2 . PHE   A 1 28  ? 5.366   9.572   7.761  1.00 22.83 ?  28  PHE   A CD2 1 
ATOM   217  C CE1 . PHE   A 1 28  ? 3.026   11.065  7.979  1.00 28.56 ?  28  PHE   A CE1 1 
ATOM   218  C CE2 . PHE   A 1 28  ? 4.905   10.322  6.671  1.00 23.39 ?  28  PHE   A CE2 1 
ATOM   219  C CZ  . PHE   A 1 28  ? 3.725   11.078  6.793  1.00 23.80 ?  28  PHE   A CZ  1 
ATOM   220  N N   . SER   A 1 29  ? 5.294   6.479   12.226 1.00 20.80 ?  29  SER   A N   1 
ATOM   221  C CA  . SER   A 1 29  ? 6.002   5.539   13.084 1.00 23.64 ?  29  SER   A CA  1 
ATOM   222  C C   . SER   A 1 29  ? 5.580   4.101   12.795 1.00 22.29 ?  29  SER   A C   1 
ATOM   223  O O   . SER   A 1 29  ? 6.418   3.226   12.539 1.00 23.11 ?  29  SER   A O   1 
ATOM   224  C CB  . SER   A 1 29  ? 5.729   5.921   14.537 1.00 24.33 ?  29  SER   A CB  1 
ATOM   225  O OG  . SER   A 1 29  ? 6.208   4.946   15.434 1.00 30.31 ?  29  SER   A OG  1 
ATOM   226  N N   . ALA   A 1 30  ? 4.272   3.844   12.829 1.00 21.61 ?  30  ALA   A N   1 
ATOM   227  C CA  . ALA   A 1 30  ? 3.770   2.498   12.578 1.00 25.83 ?  30  ALA   A CA  1 
ATOM   228  C C   . ALA   A 1 30  ? 4.197   2.007   11.212 1.00 25.79 ?  30  ALA   A C   1 
ATOM   229  O O   . ALA   A 1 30  ? 4.611   0.854   11.052 1.00 24.63 ?  30  ALA   A O   1 
ATOM   230  C CB  . ALA   A 1 30  ? 2.242   2.477   12.693 1.00 24.25 ?  30  ALA   A CB  1 
ATOM   231  N N   . VAL   A 1 31  ? 4.123   2.878   10.216 1.00 25.98 ?  31  VAL   A N   1 
ATOM   232  C CA  . VAL   A 1 31  ? 4.448   2.451   8.866  1.00 21.61 ?  31  VAL   A CA  1 
ATOM   233  C C   . VAL   A 1 31  ? 5.910   2.044   8.753  1.00 22.31 ?  31  VAL   A C   1 
ATOM   234  O O   . VAL   A 1 31  ? 6.227   1.069   8.060  1.00 25.94 ?  31  VAL   A O   1 
ATOM   235  C CB  . VAL   A 1 31  ? 4.053   3.540   7.856  1.00 21.27 ?  31  VAL   A CB  1 
ATOM   236  C CG1 . VAL   A 1 31  ? 4.884   3.414   6.556  1.00 24.64 ?  31  VAL   A CG1 1 
ATOM   237  C CG2 . VAL   A 1 31  ? 2.567   3.391   7.546  1.00 22.22 ?  31  VAL   A CG2 1 
ATOM   238  N N   . VAL   A 1 32  ? 6.835   2.752   9.420  1.00 22.02 ?  32  VAL   A N   1 
ATOM   239  C CA  . VAL   A 1 32  ? 8.201   2.313   9.149  1.00 23.11 ?  32  VAL   A CA  1 
ATOM   240  C C   . VAL   A 1 32  ? 8.419   0.939   9.775  1.00 21.79 ?  32  VAL   A C   1 
ATOM   241  O O   . VAL   A 1 32  ? 9.160   0.120   9.225  1.00 26.25 ?  32  VAL   A O   1 
ATOM   242  C CB  . VAL   A 1 32  ? 9.314   3.332   9.534  1.00 35.78 ?  32  VAL   A CB  1 
ATOM   243  C CG1 . VAL   A 1 32  ? 8.828   4.720   9.965  1.00 26.66 ?  32  VAL   A CG1 1 
ATOM   244  C CG2 . VAL   A 1 32  ? 10.461  2.722   10.378 1.00 24.42 ?  32  VAL   A CG2 1 
ATOM   245  N N   . THR   A 1 33  ? 7.695   0.605   10.855 1.00 23.00 ?  33  THR   A N   1 
ATOM   246  C CA  . THR   A 1 33  ? 7.847   -0.751  11.382 1.00 24.74 ?  33  THR   A CA  1 
ATOM   247  C C   . THR   A 1 33  ? 7.235   -1.779  10.433 1.00 24.69 ?  33  THR   A C   1 
ATOM   248  O O   . THR   A 1 33  ? 7.765   -2.886  10.286 1.00 25.38 ?  33  THR   A O   1 
ATOM   249  C CB  . THR   A 1 33  ? 7.234   -0.883  12.778 1.00 24.01 ?  33  THR   A CB  1 
ATOM   250  O OG1 . THR   A 1 33  ? 5.797   -0.853  12.705 1.00 25.49 ?  33  THR   A OG1 1 
ATOM   251  C CG2 . THR   A 1 33  ? 7.722   0.202   13.706 1.00 23.00 ?  33  THR   A CG2 1 
ATOM   252  N N   . ILE   A 1 34  ? 6.148   -1.423  9.753  1.00 25.18 ?  34  ILE   A N   1 
ATOM   253  C CA  . ILE   A 1 34  ? 5.565   -2.335  8.778  1.00 26.02 ?  34  ILE   A CA  1 
ATOM   254  C C   . ILE   A 1 34  ? 6.484   -2.477  7.571  1.00 26.61 ?  34  ILE   A C   1 
ATOM   255  O O   . ILE   A 1 34  ? 6.779   -3.589  7.121  1.00 26.47 ?  34  ILE   A O   1 
ATOM   256  C CB  . ILE   A 1 34  ? 4.160   -1.851  8.391  1.00 25.84 ?  34  ILE   A CB  1 
ATOM   257  C CG1 . ILE   A 1 34  ? 3.259   -1.895  9.613  1.00 25.89 ?  34  ILE   A CG1 1 
ATOM   258  C CG2 . ILE   A 1 34  ? 3.574   -2.703  7.267  1.00 28.12 ?  34  ILE   A CG2 1 
ATOM   259  C CD1 . ILE   A 1 34  ? 2.071   -0.998  9.467  1.00 36.78 ?  34  ILE   A CD1 1 
ATOM   260  N N   . GLU   A 1 35  ? 6.981   -1.355  7.040  1.00 27.23 ?  35  GLU   A N   1 
ATOM   261  C CA  . GLU   A 1 35  ? 7.954   -1.443  5.955  1.00 23.02 ?  35  GLU   A CA  1 
ATOM   262  C C   . GLU   A 1 35  ? 9.136   -2.321  6.343  1.00 26.99 ?  35  GLU   A C   1 
ATOM   263  O O   . GLU   A 1 35  ? 9.616   -3.123  5.532  1.00 27.03 ?  35  GLU   A O   1 
ATOM   264  C CB  . GLU   A 1 35  ? 8.433   -0.048  5.571  1.00 22.14 ?  35  GLU   A CB  1 
ATOM   265  C CG  . GLU   A 1 35  ? 7.282   0.757   5.015  1.00 22.28 ?  35  GLU   A CG  1 
ATOM   266  C CD  . GLU   A 1 35  ? 7.596   2.193   4.789  1.00 28.70 ?  35  GLU   A CD  1 
ATOM   267  O OE1 . GLU   A 1 35  ? 8.568   2.703   5.386  1.00 24.99 ?  35  GLU   A OE1 1 
ATOM   268  O OE2 . GLU   A 1 35  ? 6.817   2.814   4.043  1.00 24.53 ?  35  GLU   A OE2 1 
ATOM   269  N N   . GLY   A 1 36  ? 9.605   -2.189  7.586  1.00 24.58 ?  36  GLY   A N   1 
ATOM   270  C CA  . GLY   A 1 36  ? 10.755  -2.964  8.014  1.00 25.73 ?  36  GLY   A CA  1 
ATOM   271  C C   . GLY   A 1 36  ? 10.455  -4.449  8.092  1.00 27.40 ?  36  GLY   A C   1 
ATOM   272  O O   . GLY   A 1 36  ? 11.201  -5.274  7.561  1.00 31.38 ?  36  GLY   A O   1 
ATOM   273  N N   . ILE   A 1 37  ? 9.357   -4.811  8.755  1.00 27.06 ?  37  ILE   A N   1 
ATOM   274  C CA  . ILE   A 1 37  ? 9.060   -6.226  8.953  1.00 28.31 ?  37  ILE   A CA  1 
ATOM   275  C C   . ILE   A 1 37  ? 8.693   -6.912  7.635  1.00 30.39 ?  37  ILE   A C   1 
ATOM   276  O O   . ILE   A 1 37  ? 9.035   -8.086  7.429  1.00 28.82 ?  37  ILE   A O   1 
ATOM   277  C CB  . ILE   A 1 37  ? 7.975   -6.405  10.032 1.00 30.75 ?  37  ILE   A CB  1 
ATOM   278  C CG1 . ILE   A 1 37  ? 7.996   -7.855  10.542 1.00 32.37 ?  37  ILE   A CG1 1 
ATOM   279  C CG2 . ILE   A 1 37  ? 6.603   -5.984  9.529  1.00 29.15 ?  37  ILE   A CG2 1 
ATOM   280  C CD1 . ILE   A 1 37  ? 9.355   -8.249  11.124 1.00 35.64 ?  37  ILE   A CD1 1 
ATOM   281  N N   . ILE   A 1 38  ? 8.025   -6.206  6.707  1.00 30.62 ?  38  ILE   A N   1 
ATOM   282  C CA  . ILE   A 1 38  ? 7.750   -6.827  5.406  1.00 27.15 ?  38  ILE   A CA  1 
ATOM   283  C C   . ILE   A 1 38  ? 9.050   -7.103  4.665  1.00 31.01 ?  38  ILE   A C   1 
ATOM   284  O O   . ILE   A 1 38  ? 9.224   -8.171  4.068  1.00 36.48 ?  38  ILE   A O   1 
ATOM   285  C CB  . ILE   A 1 38  ? 6.789   -5.974  4.556  1.00 30.75 ?  38  ILE   A CB  1 
ATOM   286  C CG1 . ILE   A 1 38  ? 5.423   -5.889  5.222  1.00 30.83 ?  38  ILE   A CG1 1 
ATOM   287  C CG2 . ILE   A 1 38  ? 6.640   -6.584  3.156  1.00 27.46 ?  38  ILE   A CG2 1 
ATOM   288  C CD1 . ILE   A 1 38  ? 4.813   -7.243  5.501  1.00 36.70 ?  38  ILE   A CD1 1 
ATOM   289  N N   . LYS   A 1 39  ? 9.994   -6.162  4.704  1.00 28.40 ?  39  LYS   A N   1 
ATOM   290  C CA  . LYS   A 1 39  ? 11.274  -6.416  4.050  1.00 32.46 ?  39  LYS   A CA  1 
ATOM   291  C C   . LYS   A 1 39  ? 12.007  -7.570  4.717  1.00 32.25 ?  39  LYS   A C   1 
ATOM   292  O O   . LYS   A 1 39  ? 12.573  -8.433  4.034  1.00 32.89 ?  39  LYS   A O   1 
ATOM   293  C CB  . LYS   A 1 39  ? 12.148  -5.164  4.054  1.00 29.84 ?  39  LYS   A CB  1 
ATOM   294  C CG  . LYS   A 1 39  ? 13.619  -5.473  3.783  1.00 32.87 ?  39  LYS   A CG  1 
ATOM   295  C CD  . LYS   A 1 39  ? 13.858  -5.704  2.307  1.00 36.34 ?  39  LYS   A CD  1 
ATOM   296  C CE  . LYS   A 1 39  ? 15.319  -6.039  2.043  1.00 41.90 ?  39  LYS   A CE  1 
ATOM   297  N NZ  . LYS   A 1 39  ? 15.581  -6.201  0.588  1.00 49.83 ?  39  LYS   A NZ  1 
ATOM   298  N N   . ILE   A 1 40  ? 11.990  -7.608  6.052  1.00 30.38 ?  40  ILE   A N   1 
ATOM   299  C CA  . ILE   A 1 40  ? 12.695  -8.657  6.784  1.00 31.59 ?  40  ILE   A CA  1 
ATOM   300  C C   . ILE   A 1 40  ? 12.129  -10.032 6.434  1.00 39.75 ?  40  ILE   A C   1 
ATOM   301  O O   . ILE   A 1 40  ? 12.883  -10.986 6.207  1.00 36.63 ?  40  ILE   A O   1 
ATOM   302  C CB  . ILE   A 1 40  ? 12.644  -8.360  8.294  1.00 33.81 ?  40  ILE   A CB  1 
ATOM   303  C CG1 . ILE   A 1 40  ? 13.557  -7.162  8.585  1.00 26.81 ?  40  ILE   A CG1 1 
ATOM   304  C CG2 . ILE   A 1 40  ? 13.054  -9.591  9.124  1.00 34.41 ?  40  ILE   A CG2 1 
ATOM   305  C CD1 . ILE   A 1 40  ? 13.330  -6.499  9.939  1.00 31.35 ?  40  ILE   A CD1 1 
ATOM   306  N N   . ARG   A 1 41  ? 10.800  -10.147 6.332  1.00 37.97 ?  41  ARG   A N   1 
ATOM   307  C CA  . ARG   A 1 41  ? 10.196  -11.449 6.048  1.00 38.21 ?  41  ARG   A CA  1 
ATOM   308  C C   . ARG   A 1 41  ? 10.138  -11.791 4.568  1.00 39.50 ?  41  ARG   A C   1 
ATOM   309  O O   . ARG   A 1 41  ? 10.230  -12.970 4.214  1.00 44.33 ?  41  ARG   A O   1 
ATOM   310  C CB  . ARG   A 1 41  ? 8.786   -11.539 6.621  1.00 35.17 ?  41  ARG   A CB  1 
ATOM   311  C CG  . ARG   A 1 41  ? 8.748   -11.257 8.087  1.00 48.42 ?  41  ARG   A CG  1 
ATOM   312  C CD  . ARG   A 1 41  ? 9.232   -12.469 8.865  1.00 44.40 ?  41  ARG   A CD  1 
ATOM   313  N NE  . ARG   A 1 41  ? 9.183   -12.186 10.291 1.00 48.34 ?  41  ARG   A NE  1 
ATOM   314  C CZ  . ARG   A 1 41  ? 10.132  -12.525 11.150 1.00 58.15 ?  41  ARG   A CZ  1 
ATOM   315  N NH1 . ARG   A 1 41  ? 11.213  -13.182 10.758 1.00 65.14 ?  41  ARG   A NH1 1 
ATOM   316  N NH2 . ARG   A 1 41  ? 10.006  -12.175 12.427 1.00 62.82 ?  41  ARG   A NH2 1 
ATOM   317  N N   . THR   A 1 42  ? 9.946   -10.814 3.689  1.00 39.65 ?  42  THR   A N   1 
ATOM   318  C CA  . THR   A 1 42  ? 9.705   -11.131 2.292  1.00 40.34 ?  42  THR   A CA  1 
ATOM   319  C C   . THR   A 1 42  ? 10.850  -10.743 1.375  1.00 42.79 ?  42  THR   A C   1 
ATOM   320  O O   . THR   A 1 42  ? 10.856  -11.166 0.211  1.00 42.55 ?  42  THR   A O   1 
ATOM   321  C CB  . THR   A 1 42  ? 8.415   -10.457 1.808  1.00 36.14 ?  42  THR   A CB  1 
ATOM   322  O OG1 . THR   A 1 42  ? 8.642   -9.049  1.640  1.00 40.50 ?  42  THR   A OG1 1 
ATOM   323  C CG2 . THR   A 1 42  ? 7.294   -10.676 2.815  1.00 38.60 ?  42  THR   A CG2 1 
ATOM   324  N N   . GLY   A 1 43  ? 11.821  -9.962  1.859  1.00 36.71 ?  43  GLY   A N   1 
ATOM   325  C CA  . GLY   A 1 43  ? 12.895  -9.482  1.016  1.00 34.98 ?  43  GLY   A CA  1 
ATOM   326  C C   . GLY   A 1 43  ? 12.555  -8.275  0.176  1.00 34.96 ?  43  GLY   A C   1 
ATOM   327  O O   . GLY   A 1 43  ? 13.454  -7.712  -0.464 1.00 37.91 ?  43  GLY   A O   1 
ATOM   328  N N   . ASN   A 1 44  ? 11.290  -7.859  0.153  1.00 33.84 ?  44  ASN   A N   1 
ATOM   329  C CA  . ASN   A 1 44  ? 10.831  -6.715  -0.621 1.00 34.17 ?  44  ASN   A CA  1 
ATOM   330  C C   . ASN   A 1 44  ? 10.693  -5.513  0.299  1.00 30.79 ?  44  ASN   A C   1 
ATOM   331  O O   . ASN   A 1 44  ? 10.008  -5.592  1.320  1.00 31.23 ?  44  ASN   A O   1 
ATOM   332  C CB  . ASN   A 1 44  ? 9.474   -7.009  -1.255 1.00 39.62 ?  44  ASN   A CB  1 
ATOM   333  C CG  . ASN   A 1 44  ? 9.518   -8.204  -2.154 1.00 39.37 ?  44  ASN   A CG  1 
ATOM   334  O OD1 . ASN   A 1 44  ? 10.470  -8.381  -2.912 1.00 46.81 ?  44  ASN   A OD1 1 
ATOM   335  N ND2 . ASN   A 1 44  ? 8.506   -9.057  -2.049 1.00 43.40 ?  44  ASN   A ND2 1 
ATOM   336  N N   . LEU   A 1 45  ? 11.328  -4.411  -0.067 1.00 34.18 ?  45  LEU   A N   1 
ATOM   337  C CA  . LEU   A 1 45  ? 11.078  -3.143  0.596  1.00 35.67 ?  45  LEU   A CA  1 
ATOM   338  C C   . LEU   A 1 45  ? 10.025  -2.386  -0.202 1.00 31.11 ?  45  LEU   A C   1 
ATOM   339  O O   . LEU   A 1 45  ? 10.231  -2.068  -1.379 1.00 30.80 ?  45  LEU   A O   1 
ATOM   340  C CB  . LEU   A 1 45  ? 12.359  -2.330  0.719  1.00 32.52 ?  45  LEU   A CB  1 
ATOM   341  C CG  . LEU   A 1 45  ? 12.245  -1.035  1.532  1.00 29.70 ?  45  LEU   A CG  1 
ATOM   342  C CD1 . LEU   A 1 45  ? 11.941  -1.347  2.995  1.00 27.23 ?  45  LEU   A CD1 1 
ATOM   343  C CD2 . LEU   A 1 45  ? 13.521  -0.248  1.392  1.00 33.74 ?  45  LEU   A CD2 1 
ATOM   344  N N   . ASN   A 1 46  ? 8.897   -2.125  0.426  1.00 24.80 ?  46  ASN   A N   1 
ATOM   345  C CA  . ASN   A 1 46  ? 7.843   -1.313  -0.156 1.00 27.83 ?  46  ASN   A CA  1 
ATOM   346  C C   . ASN   A 1 46  ? 7.531   -0.164  0.781  1.00 30.13 ?  46  ASN   A C   1 
ATOM   347  O O   . ASN   A 1 46  ? 7.845   -0.218  1.969  1.00 32.62 ?  46  ASN   A O   1 
ATOM   348  C CB  . ASN   A 1 46  ? 6.573   -2.119  -0.378 1.00 32.68 ?  46  ASN   A CB  1 
ATOM   349  C CG  . ASN   A 1 46  ? 6.829   -3.371  -1.174 1.00 40.23 ?  46  ASN   A CG  1 
ATOM   350  O OD1 . ASN   A 1 46  ? 6.672   -4.480  -0.669 1.00 47.88 ?  46  ASN   A OD1 1 
ATOM   351  N ND2 . ASN   A 1 46  ? 7.236   -3.200  -2.421 1.00 36.11 ?  46  ASN   A ND2 1 
ATOM   352  N N   . GLU   A 1 47  ? 6.893   0.865   0.244  1.00 25.28 ?  47  GLU   A N   1 
ATOM   353  C CA  . GLU   A 1 47  ? 6.347   1.925   1.080  1.00 26.09 ?  47  GLU   A CA  1 
ATOM   354  C C   . GLU   A 1 47  ? 4.859   1.726   1.266  1.00 27.18 ?  47  GLU   A C   1 
ATOM   355  O O   . GLU   A 1 47  ? 4.133   1.463   0.306  1.00 27.72 ?  47  GLU   A O   1 
ATOM   356  C CB  . GLU   A 1 47  ? 6.595   3.296   0.470  1.00 24.79 ?  47  GLU   A CB  1 
ATOM   357  C CG  . GLU   A 1 47  ? 8.044   3.610   0.405  1.00 27.83 ?  47  GLU   A CG  1 
ATOM   358  C CD  . GLU   A 1 47  ? 8.281   4.953   -0.193 1.00 32.09 ?  47  GLU   A CD  1 
ATOM   359  O OE1 . GLU   A 1 47  ? 7.605   5.293   -1.181 1.00 34.59 ?  47  GLU   A OE1 1 
ATOM   360  O OE2 . GLU   A 1 47  ? 9.111   5.682   0.354  1.00 27.22 ?  47  GLU   A OE2 1 
ATOM   361  N N   . TYR   A 1 48  ? 4.400   1.935   2.485  1.00 24.14 ?  48  TYR   A N   1 
ATOM   362  C CA  . TYR   A 1 48  ? 3.008   1.721   2.815  1.00 23.98 ?  48  TYR   A CA  1 
ATOM   363  C C   . TYR   A 1 48  ? 2.389   3.029   3.265  1.00 22.18 ?  48  TYR   A C   1 
ATOM   364  O O   . TYR   A 1 48  ? 3.072   4.022   3.514  1.00 21.12 ?  48  TYR   A O   1 
ATOM   365  C CB  . TYR   A 1 48  ? 2.875   0.635   3.886  1.00 22.86 ?  48  TYR   A CB  1 
ATOM   366  C CG  . TYR   A 1 48  ? 3.347   -0.689  3.349  1.00 25.85 ?  48  TYR   A CG  1 
ATOM   367  C CD1 . TYR   A 1 48  ? 2.624   -1.337  2.350  1.00 28.27 ?  48  TYR   A CD1 1 
ATOM   368  C CD2 . TYR   A 1 48  ? 4.542   -1.265  3.791  1.00 24.20 ?  48  TYR   A CD2 1 
ATOM   369  C CE1 . TYR   A 1 48  ? 3.034   -2.529  1.838  1.00 29.66 ?  48  TYR   A CE1 1 
ATOM   370  C CE2 . TYR   A 1 48  ? 4.972   -2.477  3.275  1.00 26.02 ?  48  TYR   A CE2 1 
ATOM   371  C CZ  . TYR   A 1 48  ? 4.205   -3.096  2.285  1.00 33.32 ?  48  TYR   A CZ  1 
ATOM   372  O OH  . TYR   A 1 48  ? 4.593   -4.293  1.731  1.00 33.72 ?  48  TYR   A OH  1 
ATOM   373  N N   . SER   A 1 49  ? 1.073   3.009   3.382  1.00 24.23 ?  49  SER   A N   1 
ATOM   374  C CA  . SER   A 1 49  ? 0.299   4.238   3.442  1.00 22.81 ?  49  SER   A CA  1 
ATOM   375  C C   . SER   A 1 49  ? 0.154   4.706   4.881  1.00 23.69 ?  49  SER   A C   1 
ATOM   376  O O   . SER   A 1 49  ? -0.619  4.136   5.655  1.00 24.15 ?  49  SER   A O   1 
ATOM   377  C CB  . SER   A 1 49  ? -1.068  4.038   2.793  1.00 21.27 ?  49  SER   A CB  1 
ATOM   378  O OG  . SER   A 1 49  ? -1.800  5.225   2.900  1.00 23.71 ?  49  SER   A OG  1 
ATOM   379  N N   . GLU   A 1 50  ? 0.854   5.788   5.223  1.00 22.18 ?  50  GLU   A N   1 
ATOM   380  C CA  . GLU   A 1 50  ? 0.507   6.513   6.441  1.00 25.47 ?  50  GLU   A CA  1 
ATOM   381  C C   . GLU   A 1 50  ? -0.905  7.062   6.358  1.00 23.98 ?  50  GLU   A C   1 
ATOM   382  O O   . GLU   A 1 50  ? -1.631  7.108   7.362  1.00 23.52 ?  50  GLU   A O   1 
ATOM   383  C CB  . GLU   A 1 50  ? 1.494   7.657   6.679  1.00 24.36 ?  50  GLU   A CB  1 
ATOM   384  C CG  . GLU   A 1 50  ? 2.918   7.171   6.817  1.00 20.27 ?  50  GLU   A CG  1 
ATOM   385  C CD  . GLU   A 1 50  ? 3.610   7.091   5.487  1.00 24.13 ?  50  GLU   A CD  1 
ATOM   386  O OE1 . GLU   A 1 50  ? 2.955   7.364   4.461  1.00 23.44 ?  50  GLU   A OE1 1 
ATOM   387  O OE2 . GLU   A 1 50  ? 4.809   6.762   5.469  1.00 29.09 ?  50  GLU   A OE2 1 
ATOM   388  N N   . GLN   A 1 51  ? -1.293  7.524   5.173  1.00 21.98 ?  51  GLN   A N   1 
ATOM   389  C CA  . GLN   A 1 51  ? -2.602  8.147   5.022  1.00 21.68 ?  51  GLN   A CA  1 
ATOM   390  C C   . GLN   A 1 51  ? -3.703  7.173   5.396  1.00 19.97 ?  51  GLN   A C   1 
ATOM   391  O O   . GLN   A 1 51  ? -4.707  7.555   6.009  1.00 24.68 ?  51  GLN   A O   1 
ATOM   392  C CB  . GLN   A 1 51  ? -2.793  8.628   3.579  1.00 22.25 ?  51  GLN   A CB  1 
ATOM   393  C CG  . GLN   A 1 51  ? -4.130  9.316   3.354  1.00 23.82 ?  51  GLN   A CG  1 
ATOM   394  C CD  . GLN   A 1 51  ? -4.118  10.682  3.966  1.00 26.18 ?  51  GLN   A CD  1 
ATOM   395  O OE1 . GLN   A 1 51  ? -3.081  11.338  3.978  1.00 23.16 ?  51  GLN   A OE1 1 
ATOM   396  N NE2 . GLN   A 1 51  ? -5.255  11.117  4.510  1.00 26.96 ?  51  GLN   A NE2 1 
ATOM   397  N N   . GLU   A 1 52  ? -3.535  5.912   5.018  1.00 23.37 ?  52  GLU   A N   1 
ATOM   398  C CA  . GLU   A 1 52  ? -4.571  4.928   5.292  1.00 26.41 ?  52  GLU   A CA  1 
ATOM   399  C C   . GLU   A 1 52  ? -4.790  4.781   6.790  1.00 24.73 ?  52  GLU   A C   1 
ATOM   400  O O   . GLU   A 1 52  ? -5.936  4.732   7.256  1.00 24.86 ?  52  GLU   A O   1 
ATOM   401  C CB  . GLU   A 1 52  ? -4.187  3.603   4.659  1.00 25.30 ?  52  GLU   A CB  1 
ATOM   402  C CG  . GLU   A 1 52  ? -5.258  2.542   4.760  1.00 29.64 ?  52  GLU   A CG  1 
ATOM   403  C CD  . GLU   A 1 52  ? -4.989  1.443   3.784  1.00 28.20 ?  52  GLU   A CD  1 
ATOM   404  O OE1 . GLU   A 1 52  ? -3.797  1.209   3.493  1.00 30.78 ?  52  GLU   A OE1 1 
ATOM   405  O OE2 . GLU   A 1 52  ? -5.952  0.825   3.288  1.00 33.91 ?  52  GLU   A OE2 1 
ATOM   406  N N   . LEU   A 1 53  ? -3.704  4.752   7.563  1.00 26.35 ?  53  LEU   A N   1 
ATOM   407  C CA  . LEU   A 1 53  ? -3.843  4.682   9.012  1.00 25.02 ?  53  LEU   A CA  1 
ATOM   408  C C   . LEU   A 1 53  ? -4.462  5.944   9.552  1.00 22.90 ?  53  LEU   A C   1 
ATOM   409  O O   . LEU   A 1 53  ? -5.342  5.886   10.417 1.00 26.66 ?  53  LEU   A O   1 
ATOM   410  C CB  . LEU   A 1 53  ? -2.489  4.450   9.665  1.00 24.42 ?  53  LEU   A CB  1 
ATOM   411  C CG  . LEU   A 1 53  ? -1.804  3.179   9.177  1.00 30.37 ?  53  LEU   A CG  1 
ATOM   412  C CD1 . LEU   A 1 53  ? -0.384  3.129   9.707  1.00 26.04 ?  53  LEU   A CD1 1 
ATOM   413  C CD2 . LEU   A 1 53  ? -2.631  1.968   9.597  1.00 29.69 ?  53  LEU   A CD2 1 
ATOM   414  N N   . LEU   A 1 54  ? -3.994  7.096   9.066  1.00 23.90 ?  54  LEU   A N   1 
ATOM   415  C CA  . LEU   A 1 54  ? -4.597  8.376   9.413  1.00 26.44 ?  54  LEU   A CA  1 
ATOM   416  C C   . LEU   A 1 54  ? -6.103  8.329   9.252  1.00 29.91 ?  54  LEU   A C   1 
ATOM   417  O O   . LEU   A 1 54  ? -6.857  8.724   10.151 1.00 28.21 ?  54  LEU   A O   1 
ATOM   418  C CB  . LEU   A 1 54  ? -4.051  9.481   8.512  1.00 22.98 ?  54  LEU   A CB  1 
ATOM   419  C CG  . LEU   A 1 54  ? -3.991  10.944  8.956  1.00 33.92 ?  54  LEU   A CG  1 
ATOM   420  C CD1 . LEU   A 1 54  ? -3.681  11.091  10.431 1.00 33.86 ?  54  LEU   A CD1 1 
ATOM   421  C CD2 . LEU   A 1 54  ? -3.007  11.719  8.087  1.00 33.89 ?  54  LEU   A CD2 1 
ATOM   422  N N   . ASP   A 1 55  ? -6.548  7.868   8.085  1.00 26.98 ?  55  ASP   A N   1 
ATOM   423  C CA  . ASP   A 1 55  ? -7.957  7.897   7.724  1.00 26.14 ?  55  ASP   A CA  1 
ATOM   424  C C   . ASP   A 1 55  ? -8.746  6.827   8.449  1.00 29.94 ?  55  ASP   A C   1 
ATOM   425  O O   . ASP   A 1 55  ? -9.920  7.036   8.768  1.00 32.07 ?  55  ASP   A O   1 
ATOM   426  C CB  . ASP   A 1 55  ? -8.124  7.654   6.231  1.00 26.03 ?  55  ASP   A CB  1 
ATOM   427  C CG  . ASP   A 1 55  ? -7.640  8.813   5.382  1.00 27.99 ?  55  ASP   A CG  1 
ATOM   428  O OD1 . ASP   A 1 55  ? -7.409  9.908   5.924  1.00 26.64 ?  55  ASP   A OD1 1 
ATOM   429  O OD2 . ASP   A 1 55  ? -7.471  8.588   4.179  1.00 28.01 ?  55  ASP   A OD2 1 
ATOM   430  N N   . CYS   A 1 56  ? -8.127  5.676   8.698  1.00 23.59 ?  56  CYS   A N   1 
ATOM   431  C CA  . CYS   A 1 56  ? -8.871  4.472   9.026  1.00 32.03 ?  56  CYS   A CA  1 
ATOM   432  C C   . CYS   A 1 56  ? -8.749  4.017   10.465 1.00 33.60 ?  56  CYS   A C   1 
ATOM   433  O O   . CYS   A 1 56  ? -9.534  3.160   10.881 1.00 31.13 ?  56  CYS   A O   1 
ATOM   434  C CB  . CYS   A 1 56  ? -8.433  3.319   8.121  1.00 23.57 ?  56  CYS   A CB  1 
ATOM   435  S SG  . CYS   A 1 56  ? -8.598  3.728   6.379  1.00 27.87 ?  56  CYS   A SG  1 
ATOM   436  N N   . ASP   A 1 57  ? -7.773  4.517   11.217 1.00 26.96 ?  57  ASP   A N   1 
ATOM   437  C CA  . ASP   A 1 57  ? -7.641  4.112   12.618 1.00 28.51 ?  57  ASP   A CA  1 
ATOM   438  C C   . ASP   A 1 57  ? -8.619  4.926   13.448 1.00 28.66 ?  57  ASP   A C   1 
ATOM   439  O O   . ASP   A 1 57  ? -8.330  6.058   13.839 1.00 30.72 ?  57  ASP   A O   1 
ATOM   440  C CB  . ASP   A 1 57  ? -6.213  4.290   13.106 1.00 25.36 ?  57  ASP   A CB  1 
ATOM   441  C CG  . ASP   A 1 57  ? -6.044  3.871   14.548 1.00 38.38 ?  57  ASP   A CG  1 
ATOM   442  O OD1 . ASP   A 1 57  ? -7.008  3.323   15.133 1.00 31.83 ?  57  ASP   A OD1 1 
ATOM   443  O OD2 . ASP   A 1 57  ? -4.941  4.080   15.087 1.00 32.07 ?  57  ASP   A OD2 1 
ATOM   444  N N   . ARG   A 1 58  ? -9.774  4.319   13.758 1.00 31.40 ?  58  ARG   A N   1 
ATOM   445  C CA  . ARG   A 1 58  ? -10.827 5.003   14.499 1.00 36.28 ?  58  ARG   A CA  1 
ATOM   446  C C   . ARG   A 1 58  ? -10.484 5.210   15.972 1.00 36.31 ?  58  ARG   A C   1 
ATOM   447  O O   . ARG   A 1 58  ? -11.134 6.029   16.632 1.00 36.43 ?  58  ARG   A O   1 
ATOM   448  C CB  . ARG   A 1 58  ? -12.132 4.211   14.373 1.00 36.99 ?  58  ARG   A CB  1 
ATOM   449  C CG  . ARG   A 1 58  ? -12.640 4.088   12.934 1.00 38.45 ?  58  ARG   A CG  1 
ATOM   450  C CD  . ARG   A 1 58  ? -13.956 3.345   12.895 1.00 45.74 ?  58  ARG   A CD  1 
ATOM   451  N NE  . ARG   A 1 58  ? -13.712 1.909   12.787 1.00 46.08 ?  58  ARG   A NE  1 
ATOM   452  C CZ  . ARG   A 1 58  ? -14.593 1.016   12.348 1.00 55.85 ?  58  ARG   A CZ  1 
ATOM   453  N NH1 . ARG   A 1 58  ? -15.817 1.368   11.981 1.00 49.11 ?  58  ARG   A NH1 1 
ATOM   454  N NH2 . ARG   A 1 58  ? -14.238 -0.266  12.284 1.00 53.70 ?  58  ARG   A NH2 1 
ATOM   455  N N   . ARG   A 1 59  ? -9.490  4.494   16.510 1.00 30.78 ?  59  ARG   A N   1 
ATOM   456  C CA  . ARG   A 1 59  ? -9.099  4.744   17.896 1.00 31.00 ?  59  ARG   A CA  1 
ATOM   457  C C   . ARG   A 1 59  ? -8.103  5.891   18.006 1.00 35.19 ?  59  ARG   A C   1 
ATOM   458  O O   . ARG   A 1 59  ? -7.896  6.412   19.103 1.00 36.89 ?  59  ARG   A O   1 
ATOM   459  C CB  . ARG   A 1 59  ? -8.523  3.472   18.532 1.00 37.53 ?  59  ARG   A CB  1 
ATOM   460  C CG  . ARG   A 1 59  ? -8.927  2.193   17.797 1.00 49.30 ?  59  ARG   A CG  1 
ATOM   461  C CD  . ARG   A 1 59  ? -8.445  0.909   18.480 1.00 50.67 ?  59  ARG   A CD  1 
ATOM   462  N NE  . ARG   A 1 59  ? -9.056  0.687   19.780 1.00 59.27 ?  59  ARG   A NE  1 
ATOM   463  C CZ  . ARG   A 1 59  ? -9.775  -0.387  20.074 1.00 59.82 ?  59  ARG   A CZ  1 
ATOM   464  N NH1 . ARG   A 1 59  ? -9.963  -1.355  19.188 1.00 61.62 ?  59  ARG   A NH1 1 
ATOM   465  N NH2 . ARG   A 1 59  ? -10.321 -0.492  21.282 1.00 59.29 ?  59  ARG   A NH2 1 
ATOM   466  N N   . SER   A 1 60  ? -7.488  6.299   16.896 1.00 32.53 ?  60  SER   A N   1 
ATOM   467  C CA  . SER   A 1 60  ? -6.623  7.464   16.884 1.00 28.99 ?  60  SER   A CA  1 
ATOM   468  C C   . SER   A 1 60  ? -7.423  8.686   16.460 1.00 34.89 ?  60  SER   A C   1 
ATOM   469  O O   . SER   A 1 60  ? -8.600  8.593   16.097 1.00 32.54 ?  60  SER   A O   1 
ATOM   470  C CB  . SER   A 1 60  ? -5.429  7.244   15.958 1.00 24.99 ?  60  SER   A CB  1 
ATOM   471  O OG  . SER   A 1 60  ? -4.537  6.304   16.525 1.00 28.55 ?  60  SER   A OG  1 
ATOM   472  N N   . TYR   A 1 61  ? -6.768  9.850   16.478 1.00 32.31 ?  61  TYR   A N   1 
ATOM   473  C CA  . TYR   A 1 61  ? -7.450  11.129  16.314 1.00 32.90 ?  61  TYR   A CA  1 
ATOM   474  C C   . TYR   A 1 61  ? -6.956  11.882  15.082 1.00 32.86 ?  61  TYR   A C   1 
ATOM   475  O O   . TYR   A 1 61  ? -6.912  13.116  15.075 1.00 32.34 ?  61  TYR   A O   1 
ATOM   476  C CB  . TYR   A 1 61  ? -7.290  11.978  17.572 1.00 36.17 ?  61  TYR   A CB  1 
ATOM   477  C CG  . TYR   A 1 61  ? -7.626  11.201  18.821 1.00 40.54 ?  61  TYR   A CG  1 
ATOM   478  C CD1 . TYR   A 1 61  ? -8.946  10.979  19.197 1.00 45.49 ?  61  TYR   A CD1 1 
ATOM   479  C CD2 . TYR   A 1 61  ? -6.619  10.650  19.605 1.00 48.39 ?  61  TYR   A CD2 1 
ATOM   480  C CE1 . TYR   A 1 61  ? -9.250  10.242  20.334 1.00 43.31 ?  61  TYR   A CE1 1 
ATOM   481  C CE2 . TYR   A 1 61  ? -6.915  9.918   20.740 1.00 50.85 ?  61  TYR   A CE2 1 
ATOM   482  C CZ  . TYR   A 1 61  ? -8.229  9.717   21.101 1.00 52.62 ?  61  TYR   A CZ  1 
ATOM   483  O OH  . TYR   A 1 61  ? -8.511  8.986   22.240 1.00 61.89 ?  61  TYR   A OH  1 
ATOM   484  N N   . GLY   A 1 62  ? -6.583  11.145  14.044 1.00 30.83 ?  62  GLY   A N   1 
ATOM   485  C CA  . GLY   A 1 62  ? -6.194  11.761  12.787 1.00 27.47 ?  62  GLY   A CA  1 
ATOM   486  C C   . GLY   A 1 62  ? -4.988  12.654  12.971 1.00 27.00 ?  62  GLY   A C   1 
ATOM   487  O O   . GLY   A 1 62  ? -3.974  12.260  13.550 1.00 30.12 ?  62  GLY   A O   1 
ATOM   488  N N   . CYS   A 1 63  ? -5.098  13.885  12.485 1.00 27.11 ?  63  CYS   A N   1 
ATOM   489  C CA  . CYS   A 1 63  ? -4.002  14.828  12.592 1.00 23.35 ?  63  CYS   A CA  1 
ATOM   490  C C   . CYS   A 1 63  ? -3.863  15.397  13.991 1.00 28.24 ?  63  CYS   A C   1 
ATOM   491  O O   . CYS   A 1 63  ? -2.957  16.202  14.222 1.00 28.44 ?  63  CYS   A O   1 
ATOM   492  C CB  . CYS   A 1 63  ? -4.185  15.981  11.607 1.00 25.32 ?  63  CYS   A CB  1 
ATOM   493  S SG  . CYS   A 1 63  ? -3.900  15.492  9.901  1.00 28.18 ?  63  CYS   A SG  1 
ATOM   494  N N   . ASN   A 1 64  ? -4.748  15.035  14.909 1.00 31.46 ?  64  ASN   A N   1 
ATOM   495  C CA  . ASN   A 1 64  ? -4.645  15.502  16.281 1.00 36.51 ?  64  ASN   A CA  1 
ATOM   496  C C   . ASN   A 1 64  ? -3.875  14.531  17.145 1.00 36.32 ?  64  ASN   A C   1 
ATOM   497  O O   . ASN   A 1 64  ? -3.758  14.748  18.351 1.00 38.10 ?  64  ASN   A O   1 
ATOM   498  C CB  . ASN   A 1 64  ? -6.038  15.740  16.877 1.00 36.69 ?  64  ASN   A CB  1 
ATOM   499  C CG  . ASN   A 1 64  ? -6.773  16.872  16.188 1.00 43.75 ?  64  ASN   A CG  1 
ATOM   500  O OD1 . ASN   A 1 64  ? -6.192  17.924  15.921 1.00 43.63 ?  64  ASN   A OD1 1 
ATOM   501  N ND2 . ASN   A 1 64  ? -8.057  16.665  15.904 1.00 45.43 ?  64  ASN   A ND2 1 
ATOM   502  N N   . GLY   A 1 65  ? -3.346  13.473  16.554 1.00 32.30 ?  65  GLY   A N   1 
ATOM   503  C CA  . GLY   A 1 65  ? -2.572  12.500  17.286 1.00 30.47 ?  65  GLY   A CA  1 
ATOM   504  C C   . GLY   A 1 65  ? -3.221  11.133  17.256 1.00 31.49 ?  65  GLY   A C   1 
ATOM   505  O O   . GLY   A 1 65  ? -4.323  10.935  16.743 1.00 30.83 ?  65  GLY   A O   1 
ATOM   506  N N   . GLY   A 1 66  ? -2.488  10.178  17.805 1.00 29.59 ?  66  GLY   A N   1 
ATOM   507  C CA  . GLY   A 1 66  ? -2.973  8.824   17.783 1.00 29.56 ?  66  GLY   A CA  1 
ATOM   508  C C   . GLY   A 1 66  ? -1.969  7.885   18.392 1.00 32.26 ?  66  GLY   A C   1 
ATOM   509  O O   . GLY   A 1 66  ? -0.993  8.298   19.021 1.00 34.15 ?  66  GLY   A O   1 
ATOM   510  N N   . TYR   A 1 67  ? -2.224  6.605   18.179 1.00 28.60 ?  67  TYR   A N   1 
ATOM   511  C CA  . TYR   A 1 67  ? -1.519  5.552   18.889 1.00 32.80 ?  67  TYR   A CA  1 
ATOM   512  C C   . TYR   A 1 67  ? -0.847  4.631   17.896 1.00 27.96 ?  67  TYR   A C   1 
ATOM   513  O O   . TYR   A 1 67  ? -1.537  4.005   17.069 1.00 30.44 ?  67  TYR   A O   1 
ATOM   514  C CB  . TYR   A 1 67  ? -2.464  4.762   19.791 1.00 32.73 ?  67  TYR   A CB  1 
ATOM   515  C CG  . TYR   A 1 67  ? -3.260  5.660   20.679 1.00 35.37 ?  67  TYR   A CG  1 
ATOM   516  C CD1 . TYR   A 1 67  ? -2.688  6.181   21.843 1.00 34.67 ?  67  TYR   A CD1 1 
ATOM   517  C CD2 . TYR   A 1 67  ? -4.584  5.979   20.383 1.00 37.73 ?  67  TYR   A CD2 1 
ATOM   518  C CE1 . TYR   A 1 67  ? -3.403  7.015   22.679 1.00 35.85 ?  67  TYR   A CE1 1 
ATOM   519  C CE2 . TYR   A 1 67  ? -5.318  6.813   21.219 1.00 37.85 ?  67  TYR   A CE2 1 
ATOM   520  C CZ  . TYR   A 1 67  ? -4.719  7.319   22.372 1.00 46.84 ?  67  TYR   A CZ  1 
ATOM   521  O OH  . TYR   A 1 67  ? -5.427  8.143   23.211 1.00 45.29 ?  67  TYR   A OH  1 
ATOM   522  N N   . PRO   A 1 68  ? 0.475   4.532   17.931 1.00 25.74 ?  68  PRO   A N   1 
ATOM   523  C CA  . PRO   A 1 68  ? 1.154   3.511   17.125 1.00 30.52 ?  68  PRO   A CA  1 
ATOM   524  C C   . PRO   A 1 68  ? 0.561   2.124   17.303 1.00 29.67 ?  68  PRO   A C   1 
ATOM   525  O O   . PRO   A 1 68  ? 0.410   1.388   16.317 1.00 28.86 ?  68  PRO   A O   1 
ATOM   526  C CB  . PRO   A 1 68  ? 2.596   3.571   17.650 1.00 26.17 ?  68  PRO   A CB  1 
ATOM   527  C CG  . PRO   A 1 68  ? 2.748   4.974   18.148 1.00 33.51 ?  68  PRO   A CG  1 
ATOM   528  C CD  . PRO   A 1 68  ? 1.412   5.294   18.776 1.00 29.53 ?  68  PRO   A CD  1 
ATOM   529  N N   A TRP   A 1 69  ? 0.217   1.748   18.539 0.76 29.17 ?  69  TRP   A N   1 
ATOM   530  N N   B TRP   A 1 69  ? 0.248   1.733   18.545 0.24 29.24 ?  69  TRP   A N   1 
ATOM   531  C CA  A TRP   A 1 69  ? -0.285  0.400   18.769 0.76 30.28 ?  69  TRP   A CA  1 
ATOM   532  C CA  B TRP   A 1 69  ? -0.299  0.400   18.778 0.24 30.30 ?  69  TRP   A CA  1 
ATOM   533  C C   A TRP   A 1 69  ? -1.641  0.194   18.105 0.76 27.77 ?  69  TRP   A C   1 
ATOM   534  C C   B TRP   A 1 69  ? -1.613  0.219   18.036 0.24 27.97 ?  69  TRP   A C   1 
ATOM   535  O O   A TRP   A 1 69  ? -1.919  -0.890  17.587 0.76 30.51 ?  69  TRP   A O   1 
ATOM   536  O O   B TRP   A 1 69  ? -1.849  -0.828  17.423 0.24 30.55 ?  69  TRP   A O   1 
ATOM   537  C CB  A TRP   A 1 69  ? -0.327  0.111   20.275 0.76 30.21 ?  69  TRP   A CB  1 
ATOM   538  C CB  B TRP   A 1 69  ? -0.504  0.153   20.276 0.24 30.43 ?  69  TRP   A CB  1 
ATOM   539  C CG  A TRP   A 1 69  ? -1.100  1.101   21.083 0.76 31.05 ?  69  TRP   A CG  1 
ATOM   540  C CG  B TRP   A 1 69  ? -1.882  -0.363  20.599 0.24 33.31 ?  69  TRP   A CG  1 
ATOM   541  C CD1 A TRP   A 1 69  ? -0.595  2.156   21.796 0.76 32.73 ?  69  TRP   A CD1 1 
ATOM   542  C CD1 B TRP   A 1 69  ? -2.349  -1.638  20.424 0.24 34.42 ?  69  TRP   A CD1 1 
ATOM   543  C CD2 A TRP   A 1 69  ? -2.513  1.126   21.277 0.76 36.57 ?  69  TRP   A CD2 1 
ATOM   544  C CD2 B TRP   A 1 69  ? -2.980  0.395   21.119 0.24 36.60 ?  69  TRP   A CD2 1 
ATOM   545  N NE1 A TRP   A 1 69  ? -1.614  2.838   22.415 0.76 35.18 ?  69  TRP   A NE1 1 
ATOM   546  N NE1 B TRP   A 1 69  ? -3.664  -1.718  20.811 0.24 36.16 ?  69  TRP   A NE1 1 
ATOM   547  C CE2 A TRP   A 1 69  ? -2.802  2.225   22.113 0.76 37.41 ?  69  TRP   A CE2 1 
ATOM   548  C CE2 B TRP   A 1 69  ? -4.075  -0.485  21.244 0.24 36.67 ?  69  TRP   A CE2 1 
ATOM   549  C CE3 A TRP   A 1 69  ? -3.570  0.323   20.823 0.76 37.85 ?  69  TRP   A CE3 1 
ATOM   550  C CE3 B TRP   A 1 69  ? -3.142  1.733   21.498 0.24 36.32 ?  69  TRP   A CE3 1 
ATOM   551  C CZ2 A TRP   A 1 69  ? -4.103  2.550   22.496 0.76 40.02 ?  69  TRP   A CZ2 1 
ATOM   552  C CZ2 B TRP   A 1 69  ? -5.314  -0.070  21.735 0.24 40.24 ?  69  TRP   A CZ2 1 
ATOM   553  C CZ3 A TRP   A 1 69  ? -4.863  0.650   21.203 0.76 39.75 ?  69  TRP   A CZ3 1 
ATOM   554  C CZ3 B TRP   A 1 69  ? -4.371  2.142   21.982 0.24 38.14 ?  69  TRP   A CZ3 1 
ATOM   555  C CH2 A TRP   A 1 69  ? -5.116  1.752   22.036 0.76 41.17 ?  69  TRP   A CH2 1 
ATOM   556  C CH2 B TRP   A 1 69  ? -5.440  1.244   22.098 0.24 40.79 ?  69  TRP   A CH2 1 
ATOM   557  N N   . SER   A 1 70  ? -2.483  1.228   18.091 1.00 29.71 ?  70  SER   A N   1 
ATOM   558  C CA  . SER   A 1 70  ? -3.758  1.154   17.384 1.00 28.99 ?  70  SER   A CA  1 
ATOM   559  C C   . SER   A 1 70  ? -3.553  0.980   15.893 1.00 28.98 ?  70  SER   A C   1 
ATOM   560  O O   . SER   A 1 70  ? -4.194  0.137   15.253 1.00 30.79 ?  70  SER   A O   1 
ATOM   561  C CB  . SER   A 1 70  ? -4.563  2.424   17.637 1.00 30.35 ?  70  SER   A CB  1 
ATOM   562  O OG  . SER   A 1 70  ? -5.921  2.156   17.428 1.00 48.83 ?  70  SER   A OG  1 
ATOM   563  N N   . ALA   A 1 71  ? -2.704  1.819   15.312 1.00 30.20 ?  71  ALA   A N   1 
ATOM   564  C CA  . ALA   A 1 71  ? -2.403  1.703   13.892 1.00 28.28 ?  71  ALA   A CA  1 
ATOM   565  C C   . ALA   A 1 71  ? -1.853  0.321   13.571 1.00 23.53 ?  71  ALA   A C   1 
ATOM   566  O O   . ALA   A 1 71  ? -2.208  -0.284  12.549 1.00 27.11 ?  71  ALA   A O   1 
ATOM   567  C CB  . ALA   A 1 71  ? -1.404  2.792   13.499 1.00 27.28 ?  71  ALA   A CB  1 
ATOM   568  N N   . LEU   A 1 72  ? -0.980  -0.198  14.435 1.00 26.15 ?  72  LEU   A N   1 
ATOM   569  C CA  . LEU   A 1 72  ? -0.386  -1.502  14.167 1.00 30.19 ?  72  LEU   A CA  1 
ATOM   570  C C   . LEU   A 1 72  ? -1.432  -2.599  14.284 1.00 31.79 ?  72  LEU   A C   1 
ATOM   571  O O   . LEU   A 1 72  ? -1.377  -3.594  13.551 1.00 29.86 ?  72  LEU   A O   1 
ATOM   572  C CB  . LEU   A 1 72  ? 0.766   -1.749  15.133 1.00 26.69 ?  72  LEU   A CB  1 
ATOM   573  C CG  . LEU   A 1 72  ? 2.017   -0.922  14.761 1.00 29.16 ?  72  LEU   A CG  1 
ATOM   574  C CD1 . LEU   A 1 72  ? 3.152   -1.159  15.768 1.00 32.24 ?  72  LEU   A CD1 1 
ATOM   575  C CD2 . LEU   A 1 72  ? 2.460   -1.189  13.326 1.00 26.99 ?  72  LEU   A CD2 1 
ATOM   576  N N   A GLN   A 1 73  ? -2.381  -2.443  15.212 0.48 29.87 ?  73  GLN   A N   1 
ATOM   577  N N   B GLN   A 1 73  ? -2.381  -2.438  15.208 0.52 29.85 ?  73  GLN   A N   1 
ATOM   578  C CA  A GLN   A 1 73  ? -3.452  -3.428  15.342 0.48 33.42 ?  73  GLN   A CA  1 
ATOM   579  C CA  B GLN   A 1 73  ? -3.459  -3.412  15.349 0.52 33.43 ?  73  GLN   A CA  1 
ATOM   580  C C   A GLN   A 1 73  ? -4.318  -3.445  14.089 0.48 33.65 ?  73  GLN   A C   1 
ATOM   581  C C   B GLN   A 1 73  ? -4.343  -3.434  14.110 0.52 33.65 ?  73  GLN   A C   1 
ATOM   582  O O   A GLN   A 1 73  ? -4.764  -4.510  13.645 0.48 35.04 ?  73  GLN   A O   1 
ATOM   583  O O   B GLN   A 1 73  ? -4.828  -4.495  13.701 0.52 35.06 ?  73  GLN   A O   1 
ATOM   584  C CB  A GLN   A 1 73  ? -4.300  -3.130  16.584 0.48 32.96 ?  73  GLN   A CB  1 
ATOM   585  C CB  B GLN   A 1 73  ? -4.275  -3.090  16.601 0.52 32.94 ?  73  GLN   A CB  1 
ATOM   586  C CG  A GLN   A 1 73  ? -3.687  -3.573  17.919 0.48 32.31 ?  73  GLN   A CG  1 
ATOM   587  C CG  B GLN   A 1 73  ? -5.471  -3.992  16.831 0.52 32.75 ?  73  GLN   A CG  1 
ATOM   588  C CD  A GLN   A 1 73  ? -4.450  -3.045  19.135 0.48 36.07 ?  73  GLN   A CD  1 
ATOM   589  C CD  B GLN   A 1 73  ? -5.113  -5.450  16.789 0.52 41.75 ?  73  GLN   A CD  1 
ATOM   590  O OE1 A GLN   A 1 73  ? -5.436  -2.316  19.003 0.48 41.88 ?  73  GLN   A OE1 1 
ATOM   591  O OE1 B GLN   A 1 73  ? -5.683  -6.214  16.007 0.52 46.60 ?  73  GLN   A OE1 1 
ATOM   592  N NE2 A GLN   A 1 73  ? -3.985  -3.406  20.327 0.48 42.17 ?  73  GLN   A NE2 1 
ATOM   593  N NE2 B GLN   A 1 73  ? -4.148  -5.850  17.610 0.52 42.32 ?  73  GLN   A NE2 1 
ATOM   594  N N   . LEU   A 1 74  ? -4.543  -2.272  13.490 1.00 31.78 ?  74  LEU   A N   1 
ATOM   595  C CA  . LEU   A 1 74  ? -5.398  -2.192  12.314 1.00 31.01 ?  74  LEU   A CA  1 
ATOM   596  C C   . LEU   A 1 74  ? -4.755  -2.879  11.116 1.00 29.68 ?  74  LEU   A C   1 
ATOM   597  O O   . LEU   A 1 74  ? -5.448  -3.503  10.306 1.00 35.35 ?  74  LEU   A O   1 
ATOM   598  C CB  . LEU   A 1 74  ? -5.710  -0.723  12.017 1.00 34.61 ?  74  LEU   A CB  1 
ATOM   599  C CG  . LEU   A 1 74  ? -6.691  -0.414  10.889 1.00 43.43 ?  74  LEU   A CG  1 
ATOM   600  C CD1 . LEU   A 1 74  ? -8.115  -0.603  11.386 1.00 45.34 ?  74  LEU   A CD1 1 
ATOM   601  C CD2 . LEU   A 1 74  ? -6.492  1.011   10.430 1.00 38.98 ?  74  LEU   A CD2 1 
ATOM   602  N N   . VAL   A 1 75  ? -3.430  -2.806  10.997 1.00 29.27 ?  75  VAL   A N   1 
ATOM   603  C CA  . VAL   A 1 75  ? -2.765  -3.505  9.903  1.00 27.98 ?  75  VAL   A CA  1 
ATOM   604  C C   . VAL   A 1 75  ? -2.741  -5.012  10.161 1.00 34.16 ?  75  VAL   A C   1 
ATOM   605  O O   . VAL   A 1 75  ? -2.752  -5.819  9.218  1.00 33.13 ?  75  VAL   A O   1 
ATOM   606  C CB  . VAL   A 1 75  ? -1.350  -2.924  9.713  1.00 30.24 ?  75  VAL   A CB  1 
ATOM   607  C CG1 . VAL   A 1 75  ? -0.600  -3.661  8.614  1.00 29.61 ?  75  VAL   A CG1 1 
ATOM   608  C CG2 . VAL   A 1 75  ? -1.440  -1.439  9.423  1.00 28.40 ?  75  VAL   A CG2 1 
ATOM   609  N N   . ALA   A 1 76  ? -2.697  -5.416  11.436 1.00 33.64 ?  76  ALA   A N   1 
ATOM   610  C CA  . ALA   A 1 76  ? -2.798  -6.832  11.767 1.00 34.71 ?  76  ALA   A CA  1 
ATOM   611  C C   . ALA   A 1 76  ? -4.199  -7.356  11.508 1.00 34.91 ?  76  ALA   A C   1 
ATOM   612  O O   . ALA   A 1 76  ? -4.367  -8.511  11.118 1.00 37.45 ?  76  ALA   A O   1 
ATOM   613  C CB  . ALA   A 1 76  ? -2.433  -7.058  13.232 1.00 32.03 ?  76  ALA   A CB  1 
ATOM   614  N N   . GLN   A 1 77  ? -5.206  -6.533  11.748 1.00 35.80 ?  77  GLN   A N   1 
ATOM   615  C CA  . GLN   A 1 77  ? -6.589  -6.970  11.653 1.00 38.49 ?  77  GLN   A CA  1 
ATOM   616  C C   . GLN   A 1 77  ? -7.113  -6.880  10.229 1.00 43.07 ?  77  GLN   A C   1 
ATOM   617  O O   . GLN   A 1 77  ? -7.930  -7.711  9.812  1.00 38.84 ?  77  GLN   A O   1 
ATOM   618  C CB  . GLN   A 1 77  ? -7.427  -6.130  12.618 1.00 40.89 ?  77  GLN   A CB  1 
ATOM   619  C CG  . GLN   A 1 77  ? -8.870  -6.527  12.782 1.00 60.59 ?  77  GLN   A CG  1 
ATOM   620  C CD  . GLN   A 1 77  ? -9.502  -5.808  13.966 1.00 69.22 ?  77  GLN   A CD  1 
ATOM   621  O OE1 . GLN   A 1 77  ? -8.796  -5.323  14.861 1.00 64.50 ?  77  GLN   A OE1 1 
ATOM   622  N NE2 . GLN   A 1 77  ? -10.829 -5.731  13.977 1.00 74.93 ?  77  GLN   A NE2 1 
ATOM   623  N N   . TYR   A 1 78  ? -6.631  -5.910  9.457  1.00 35.08 ?  78  TYR   A N   1 
ATOM   624  C CA  . TYR   A 1 78  ? -7.092  -5.727  8.084  1.00 37.35 ?  78  TYR   A CA  1 
ATOM   625  C C   . TYR   A 1 78  ? -5.917  -5.824  7.124  1.00 36.87 ?  78  TYR   A C   1 
ATOM   626  O O   . TYR   A 1 78  ? -5.787  -6.825  6.413  1.00 47.05 ?  78  TYR   A O   1 
ATOM   627  C CB  . TYR   A 1 78  ? -7.824  -4.390  7.964  1.00 36.04 ?  78  TYR   A CB  1 
ATOM   628  C CG  . TYR   A 1 78  ? -9.086  -4.357  8.793  1.00 47.74 ?  78  TYR   A CG  1 
ATOM   629  C CD1 . TYR   A 1 78  ? -10.234 -5.032  8.382  1.00 51.27 ?  78  TYR   A CD1 1 
ATOM   630  C CD2 . TYR   A 1 78  ? -9.122  -3.688  10.008 1.00 46.50 ?  78  TYR   A CD2 1 
ATOM   631  C CE1 . TYR   A 1 78  ? -11.388 -5.016  9.147  1.00 48.15 ?  78  TYR   A CE1 1 
ATOM   632  C CE2 . TYR   A 1 78  ? -10.270 -3.671  10.782 1.00 55.68 ?  78  TYR   A CE2 1 
ATOM   633  C CZ  . TYR   A 1 78  ? -11.400 -4.336  10.345 1.00 55.70 ?  78  TYR   A CZ  1 
ATOM   634  O OH  . TYR   A 1 78  ? -12.541 -4.315  11.115 1.00 65.03 ?  78  TYR   A OH  1 
ATOM   635  N N   . GLY   A 1 79  ? -5.036  -4.851  7.122  1.00 34.81 ?  79  GLY   A N   1 
ATOM   636  C CA  . GLY   A 1 79  ? -3.944  -4.804  6.182  1.00 26.40 ?  79  GLY   A CA  1 
ATOM   637  C C   . GLY   A 1 79  ? -3.646  -3.352  5.887  1.00 30.84 ?  79  GLY   A C   1 
ATOM   638  O O   . GLY   A 1 79  ? -4.187  -2.454  6.513  1.00 31.69 ?  79  GLY   A O   1 
ATOM   639  N N   . ILE   A 1 80  ? -2.799  -3.140  4.895  1.00 27.37 ?  80  ILE   A N   1 
ATOM   640  C CA  . ILE   A 1 80  ? -2.384  -1.792  4.531  1.00 27.83 ?  80  ILE   A CA  1 
ATOM   641  C C   . ILE   A 1 80  ? -2.102  -1.782  3.043  1.00 27.71 ?  80  ILE   A C   1 
ATOM   642  O O   . ILE   A 1 80  ? -1.732  -2.804  2.455  1.00 27.15 ?  80  ILE   A O   1 
ATOM   643  C CB  . ILE   A 1 80  ? -1.147  -1.333  5.342  1.00 24.51 ?  80  ILE   A CB  1 
ATOM   644  C CG1 . ILE   A 1 80  ? -0.934  0.184   5.191  1.00 27.22 ?  80  ILE   A CG1 1 
ATOM   645  C CG2 . ILE   A 1 80  ? 0.089   -2.118  4.917  1.00 26.25 ?  80  ILE   A CG2 1 
ATOM   646  C CD1 . ILE   A 1 80  ? -0.099  0.773   6.317  1.00 33.61 ?  80  ILE   A CD1 1 
ATOM   647  N N   . HIS   A 1 81  ? -2.283  -0.618  2.433  1.00 27.45 ?  81  HIS   A N   1 
ATOM   648  C CA  . HIS   A 1 81  ? -2.051  -0.462  1.007  1.00 27.84 ?  81  HIS   A CA  1 
ATOM   649  C C   . HIS   A 1 81  ? -0.680  0.156   0.783  1.00 31.10 ?  81  HIS   A C   1 
ATOM   650  O O   . HIS   A 1 81  ? -0.095  0.758   1.692  1.00 26.94 ?  81  HIS   A O   1 
ATOM   651  C CB  . HIS   A 1 81  ? -3.143  0.415   0.410  1.00 26.44 ?  81  HIS   A CB  1 
ATOM   652  C CG  . HIS   A 1 81  ? -4.417  -0.325  0.183  1.00 32.31 ?  81  HIS   A CG  1 
ATOM   653  N ND1 . HIS   A 1 81  ? -5.483  -0.236  1.055  1.00 31.36 ?  81  HIS   A ND1 1 
ATOM   654  C CD2 . HIS   A 1 81  ? -4.814  -1.140  -0.821 1.00 30.66 ?  81  HIS   A CD2 1 
ATOM   655  C CE1 . HIS   A 1 81  ? -6.473  -0.990  0.609  1.00 35.40 ?  81  HIS   A CE1 1 
ATOM   656  N NE2 . HIS   A 1 81  ? -6.092  -1.547  -0.527 1.00 37.15 ?  81  HIS   A NE2 1 
ATOM   657  N N   . TYR   A 1 82  ? -0.169  -0.021  -0.436 1.00 27.82 ?  82  TYR   A N   1 
ATOM   658  C CA  . TYR   A 1 82  ? 1.031   0.682   -0.859 1.00 28.51 ?  82  TYR   A CA  1 
ATOM   659  C C   . TYR   A 1 82  ? 0.823   2.179   -0.738 1.00 26.70 ?  82  TYR   A C   1 
ATOM   660  O O   . TYR   A 1 82  ? -0.286  2.688   -0.943 1.00 25.58 ?  82  TYR   A O   1 
ATOM   661  C CB  . TYR   A 1 82  ? 1.376   0.336   -2.307 1.00 26.71 ?  82  TYR   A CB  1 
ATOM   662  C CG  . TYR   A 1 82  ? 1.872   -1.068  -2.485 1.00 33.24 ?  82  TYR   A CG  1 
ATOM   663  C CD1 . TYR   A 1 82  ? 2.942   -1.531  -1.751 1.00 33.47 ?  82  TYR   A CD1 1 
ATOM   664  C CD2 . TYR   A 1 82  ? 1.283   -1.925  -3.413 1.00 35.89 ?  82  TYR   A CD2 1 
ATOM   665  C CE1 . TYR   A 1 82  ? 3.416   -2.811  -1.918 1.00 38.01 ?  82  TYR   A CE1 1 
ATOM   666  C CE2 . TYR   A 1 82  ? 1.747   -3.220  -3.581 1.00 38.12 ?  82  TYR   A CE2 1 
ATOM   667  C CZ  . TYR   A 1 82  ? 2.814   -3.651  -2.826 1.00 39.76 ?  82  TYR   A CZ  1 
ATOM   668  O OH  . TYR   A 1 82  ? 3.296   -4.921  -2.966 1.00 43.63 ?  82  TYR   A OH  1 
ATOM   669  N N   . ARG   A 1 83  ? 1.897   2.877   -0.374 1.00 22.98 ?  83  ARG   A N   1 
ATOM   670  C CA  . ARG   A 1 83  ? 1.847   4.329   -0.304 1.00 22.15 ?  83  ARG   A CA  1 
ATOM   671  C C   . ARG   A 1 83  ? 1.434   4.927   -1.643 1.00 24.70 ?  83  ARG   A C   1 
ATOM   672  O O   . ARG   A 1 83  ? 0.679   5.901   -1.691 1.00 27.04 ?  83  ARG   A O   1 
ATOM   673  C CB  . ARG   A 1 83  ? 3.207   4.866   0.117  1.00 24.14 ?  83  ARG   A CB  1 
ATOM   674  C CG  . ARG   A 1 83  ? 3.167   6.308   0.587  1.00 22.73 ?  83  ARG   A CG  1 
ATOM   675  C CD  . ARG   A 1 83  ? 4.487   6.657   1.223  1.00 26.01 ?  83  ARG   A CD  1 
ATOM   676  N NE  . ARG   A 1 83  ? 4.345   7.744   2.186  1.00 25.52 ?  83  ARG   A NE  1 
ATOM   677  C CZ  . ARG   A 1 83  ? 4.737   8.998   2.015  1.00 26.82 ?  83  ARG   A CZ  1 
ATOM   678  N NH1 . ARG   A 1 83  ? 5.371   9.386   0.921  1.00 28.28 ?  83  ARG   A NH1 1 
ATOM   679  N NH2 . ARG   A 1 83  ? 4.516   9.879   2.989  1.00 27.61 ?  83  ARG   A NH2 1 
ATOM   680  N N   . ASN   A 1 84  ? 1.924   4.356   -2.740 1.00 28.72 ?  84  ASN   A N   1 
ATOM   681  C CA  . ASN   A 1 84  ? 1.596   4.869   -4.067 1.00 33.84 ?  84  ASN   A CA  1 
ATOM   682  C C   . ASN   A 1 84  ? 0.098   4.788   -4.346 1.00 30.50 ?  84  ASN   A C   1 
ATOM   683  O O   . ASN   A 1 84  ? -0.454  5.653   -5.036 1.00 33.31 ?  84  ASN   A O   1 
ATOM   684  C CB  . ASN   A 1 84  ? 2.400   4.092   -5.113 1.00 37.05 ?  84  ASN   A CB  1 
ATOM   685  C CG  . ASN   A 1 84  ? 2.132   4.557   -6.529 1.00 57.49 ?  84  ASN   A CG  1 
ATOM   686  O OD1 . ASN   A 1 84  ? 2.177   5.755   -6.828 1.00 62.40 ?  84  ASN   A OD1 1 
ATOM   687  N ND2 . ASN   A 1 84  ? 1.862   3.601   -7.419 1.00 59.06 ?  84  ASN   A ND2 1 
ATOM   688  N N   . THR   A 1 85  ? -0.576  3.777   -3.796 1.00 26.68 ?  85  THR   A N   1 
ATOM   689  C CA  . THR   A 1 85  ? -2.009  3.593   -4.002 1.00 26.23 ?  85  THR   A CA  1 
ATOM   690  C C   . THR   A 1 85  ? -2.821  4.552   -3.147 1.00 24.87 ?  85  THR   A C   1 
ATOM   691  O O   . THR   A 1 85  ? -3.938  4.946   -3.510 1.00 27.75 ?  85  THR   A O   1 
ATOM   692  C CB  . THR   A 1 85  ? -2.396  2.153   -3.636 1.00 31.91 ?  85  THR   A CB  1 
ATOM   693  O OG1 . THR   A 1 85  ? -1.653  1.236   -4.442 1.00 37.97 ?  85  THR   A OG1 1 
ATOM   694  C CG2 . THR   A 1 85  ? -3.893  1.913   -3.854 1.00 35.59 ?  85  THR   A CG2 1 
ATOM   695  N N   . TYR   A 1 86  ? -2.270  4.925   -2.008 1.00 25.12 ?  86  TYR   A N   1 
ATOM   696  C CA  . TYR   A 1 86  ? -2.993  5.645   -0.975 1.00 25.85 ?  86  TYR   A CA  1 
ATOM   697  C C   . TYR   A 1 86  ? -2.035  6.701   -0.463 1.00 25.72 ?  86  TYR   A C   1 
ATOM   698  O O   . TYR   A 1 86  ? -1.561  6.644   0.679  1.00 26.05 ?  86  TYR   A O   1 
ATOM   699  C CB  . TYR   A 1 86  ? -3.458  4.659   0.101  1.00 25.72 ?  86  TYR   A CB  1 
ATOM   700  C CG  . TYR   A 1 86  ? -4.627  5.082   0.948  1.00 21.91 ?  86  TYR   A CG  1 
ATOM   701  C CD1 . TYR   A 1 86  ? -4.870  6.415   1.241  1.00 23.50 ?  86  TYR   A CD1 1 
ATOM   702  C CD2 . TYR   A 1 86  ? -5.505  4.125   1.448  1.00 25.69 ?  86  TYR   A CD2 1 
ATOM   703  C CE1 . TYR   A 1 86  ? -5.958  6.784   2.016  1.00 24.37 ?  86  TYR   A CE1 1 
ATOM   704  C CE2 . TYR   A 1 86  ? -6.581  4.475   2.211  1.00 23.91 ?  86  TYR   A CE2 1 
ATOM   705  C CZ  . TYR   A 1 86  ? -6.813  5.806   2.486  1.00 25.49 ?  86  TYR   A CZ  1 
ATOM   706  O OH  . TYR   A 1 86  ? -7.872  6.152   3.263  1.00 27.31 ?  86  TYR   A OH  1 
ATOM   707  N N   . PRO   A 1 87  ? -1.694  7.674   -1.304 1.00 22.88 ?  87  PRO   A N   1 
ATOM   708  C CA  . PRO   A 1 87  ? -0.600  8.579   -0.961 1.00 24.24 ?  87  PRO   A CA  1 
ATOM   709  C C   . PRO   A 1 87  ? -0.969  9.501   0.183  1.00 24.03 ?  87  PRO   A C   1 
ATOM   710  O O   . PRO   A 1 87  ? -2.132  9.675   0.548  1.00 24.03 ?  87  PRO   A O   1 
ATOM   711  C CB  . PRO   A 1 87  ? -0.353  9.355   -2.262 1.00 27.38 ?  87  PRO   A CB  1 
ATOM   712  C CG  . PRO   A 1 87  ? -1.636  9.303   -2.980 1.00 24.92 ?  87  PRO   A CG  1 
ATOM   713  C CD  . PRO   A 1 87  ? -2.294  8.004   -2.614 1.00 23.05 ?  87  PRO   A CD  1 
ATOM   714  N N   . TYR   A 1 88  ? 0.067   10.099  0.748  1.00 26.50 ?  88  TYR   A N   1 
ATOM   715  C CA  . TYR   A 1 88  ? -0.091  10.982  1.885  1.00 25.47 ?  88  TYR   A CA  1 
ATOM   716  C C   . TYR   A 1 88  ? -0.613  12.340  1.443  1.00 27.19 ?  88  TYR   A C   1 
ATOM   717  O O   . TYR   A 1 88  ? -0.073  12.951  0.516  1.00 27.18 ?  88  TYR   A O   1 
ATOM   718  C CB  . TYR   A 1 88  ? 1.249   11.153  2.572  1.00 24.22 ?  88  TYR   A CB  1 
ATOM   719  C CG  . TYR   A 1 88  ? 1.136   11.902  3.856  1.00 22.03 ?  88  TYR   A CG  1 
ATOM   720  C CD1 . TYR   A 1 88  ? 0.340   11.413  4.894  1.00 23.64 ?  88  TYR   A CD1 1 
ATOM   721  C CD2 . TYR   A 1 88  ? 1.819   13.090  4.045  1.00 26.23 ?  88  TYR   A CD2 1 
ATOM   722  C CE1 . TYR   A 1 88  ? 0.245   12.091  6.099  1.00 25.36 ?  88  TYR   A CE1 1 
ATOM   723  C CE2 . TYR   A 1 88  ? 1.729   13.778  5.246  1.00 25.16 ?  88  TYR   A CE2 1 
ATOM   724  C CZ  . TYR   A 1 88  ? 0.949   13.273  6.268  1.00 27.33 ?  88  TYR   A CZ  1 
ATOM   725  O OH  . TYR   A 1 88  ? 0.877   13.968  7.459  1.00 24.98 ?  88  TYR   A OH  1 
ATOM   726  N N   . GLU   A 1 89  ? -1.653  12.815  2.111  1.00 24.78 ?  89  GLU   A N   1 
ATOM   727  C CA  . GLU   A 1 89  ? -2.220  14.121  1.819  1.00 26.01 ?  89  GLU   A CA  1 
ATOM   728  C C   . GLU   A 1 89  ? -2.114  15.077  2.993  1.00 25.51 ?  89  GLU   A C   1 
ATOM   729  O O   . GLU   A 1 89  ? -2.384  16.268  2.815  1.00 27.14 ?  89  GLU   A O   1 
ATOM   730  C CB  . GLU   A 1 89  ? -3.699  13.997  1.406  1.00 26.72 ?  89  GLU   A CB  1 
ATOM   731  C CG  . GLU   A 1 89  ? -4.023  12.705  0.694  1.00 26.65 ?  89  GLU   A CG  1 
ATOM   732  C CD  . GLU   A 1 89  ? -5.432  12.650  0.150  1.00 25.02 ?  89  GLU   A CD  1 
ATOM   733  O OE1 . GLU   A 1 89  ? -6.043  13.690  -0.179 1.00 26.15 ?  89  GLU   A OE1 1 
ATOM   734  O OE2 . GLU   A 1 89  ? -5.990  11.550  0.196  1.00 27.82 ?  89  GLU   A OE2 1 
ATOM   735  N N   . GLY   A 1 90  ? -1.727  14.599  4.174  1.00 27.10 ?  90  GLY   A N   1 
ATOM   736  C CA  . GLY   A 1 90  ? -1.472  15.504  5.282  1.00 26.57 ?  90  GLY   A CA  1 
ATOM   737  C C   . GLY   A 1 90  ? -2.721  15.994  5.962  1.00 25.08 ?  90  GLY   A C   1 
ATOM   738  O O   . GLY   A 1 90  ? -2.660  16.936  6.755  1.00 32.74 ?  90  GLY   A O   1 
ATOM   739  N N   . VAL   A 1 91  ? -3.858  15.398  5.650  1.00 28.49 ?  91  VAL   A N   1 
ATOM   740  C CA  . VAL   A 1 91  ? -5.121  15.758  6.260  1.00 30.71 ?  91  VAL   A CA  1 
ATOM   741  C C   . VAL   A 1 91  ? -5.904  14.474  6.403  1.00 29.21 ?  91  VAL   A C   1 
ATOM   742  O O   . VAL   A 1 91  ? -5.814  13.580  5.555  1.00 27.61 ?  91  VAL   A O   1 
ATOM   743  C CB  . VAL   A 1 91  ? -5.889  16.803  5.416  1.00 30.79 ?  91  VAL   A CB  1 
ATOM   744  C CG1 . VAL   A 1 91  ? -6.205  16.251  4.038  1.00 31.43 ?  91  VAL   A CG1 1 
ATOM   745  C CG2 . VAL   A 1 91  ? -7.162  17.227  6.119  1.00 43.16 ?  91  VAL   A CG2 1 
ATOM   746  N N   . GLN   A 1 92  ? -6.639  14.361  7.497  1.00 26.17 ?  92  GLN   A N   1 
ATOM   747  C CA  . GLN   A 1 92  ? -7.496  13.204  7.651  1.00 26.57 ?  92  GLN   A CA  1 
ATOM   748  C C   . GLN   A 1 92  ? -8.677  13.329  6.710  1.00 28.95 ?  92  GLN   A C   1 
ATOM   749  O O   . GLN   A 1 92  ? -9.325  14.376  6.642  1.00 30.04 ?  92  GLN   A O   1 
ATOM   750  C CB  . GLN   A 1 92  ? -7.979  13.064  9.086  1.00 26.86 ?  92  GLN   A CB  1 
ATOM   751  C CG  . GLN   A 1 92  ? -8.688  11.756  9.284  1.00 26.15 ?  92  GLN   A CG  1 
ATOM   752  C CD  . GLN   A 1 92  ? -9.235  11.594  10.683 1.00 33.81 ?  92  GLN   A CD  1 
ATOM   753  O OE1 . GLN   A 1 92  ? -9.632  12.565  11.323 1.00 39.95 ?  92  GLN   A OE1 1 
ATOM   754  N NE2 . GLN   A 1 92  ? -9.257  10.354  11.166 1.00 36.75 ?  92  GLN   A NE2 1 
ATOM   755  N N   . ARG   A 1 93  ? -8.917  12.276  5.943  1.00 25.06 ?  93  ARG   A N   1 
ATOM   756  C CA  . ARG   A 1 93  ? -10.105 12.233  5.114  1.00 33.39 ?  93  ARG   A CA  1 
ATOM   757  C C   . ARG   A 1 93  ? -10.836 10.973  5.532  1.00 33.81 ?  93  ARG   A C   1 
ATOM   758  O O   . ARG   A 1 93  ? -10.607 10.460  6.630  1.00 40.77 ?  93  ARG   A O   1 
ATOM   759  C CB  . ARG   A 1 93  ? -9.716  12.263  3.634  1.00 25.47 ?  93  ARG   A CB  1 
ATOM   760  C CG  . ARG   A 1 93  ? -8.868  13.505  3.323  1.00 26.74 ?  93  ARG   A CG  1 
ATOM   761  C CD  . ARG   A 1 93  ? -8.593  13.668  1.847  1.00 30.24 ?  93  ARG   A CD  1 
ATOM   762  N NE  . ARG   A 1 93  ? -9.790  13.477  1.038  1.00 26.33 ?  93  ARG   A NE  1 
ATOM   763  C CZ  . ARG   A 1 93  ? -9.778  13.356  -0.283 1.00 27.92 ?  93  ARG   A CZ  1 
ATOM   764  N NH1 . ARG   A 1 93  ? -8.645  13.370  -0.965 1.00 21.66 ?  93  ARG   A NH1 1 
ATOM   765  N NH2 . ARG   A 1 93  ? -10.930 13.241  -0.933 1.00 33.12 ?  93  ARG   A NH2 1 
ATOM   766  N N   A TYR   A 1 94  ? -11.720 10.465  4.697  0.56 34.47 ?  94  TYR   A N   1 
ATOM   767  N N   B TYR   A 1 94  ? -11.690 10.454  4.663  0.44 34.44 ?  94  TYR   A N   1 
ATOM   768  C CA  A TYR   A 1 94  ? -12.412 9.247   5.073  0.56 33.94 ?  94  TYR   A CA  1 
ATOM   769  C CA  B TYR   A 1 94  ? -12.425 9.243   4.975  0.44 33.99 ?  94  TYR   A CA  1 
ATOM   770  C C   A TYR   A 1 94  ? -11.576 8.032   4.692  0.56 31.24 ?  94  TYR   A C   1 
ATOM   771  C C   B TYR   A 1 94  ? -11.547 8.028   4.694  0.44 31.24 ?  94  TYR   A C   1 
ATOM   772  O O   A TYR   A 1 94  ? -10.709 8.087   3.815  0.56 30.15 ?  94  TYR   A O   1 
ATOM   773  O O   B TYR   A 1 94  ? -10.620 8.080   3.879  0.44 30.17 ?  94  TYR   A O   1 
ATOM   774  C CB  A TYR   A 1 94  ? -13.794 9.190   4.420  0.56 35.90 ?  94  TYR   A CB  1 
ATOM   775  C CB  B TYR   A 1 94  ? -13.705 9.182   4.142  0.44 35.46 ?  94  TYR   A CB  1 
ATOM   776  C CG  A TYR   A 1 94  ? -13.781 9.092   2.914  0.56 34.47 ?  94  TYR   A CG  1 
ATOM   777  C CG  B TYR   A 1 94  ? -14.661 10.325  4.426  0.44 38.14 ?  94  TYR   A CG  1 
ATOM   778  C CD1 A TYR   A 1 94  ? -13.416 10.179  2.125  0.56 36.71 ?  94  TYR   A CD1 1 
ATOM   779  C CD1 B TYR   A 1 94  ? -14.735 10.905  5.687  0.44 37.04 ?  94  TYR   A CD1 1 
ATOM   780  C CD2 A TYR   A 1 94  ? -14.166 7.924   2.278  0.56 36.13 ?  94  TYR   A CD2 1 
ATOM   781  C CD2 B TYR   A 1 94  ? -15.481 10.836  3.423  0.44 40.30 ?  94  TYR   A CD2 1 
ATOM   782  C CE1 A TYR   A 1 94  ? -13.414 10.092  0.747  0.56 36.00 ?  94  TYR   A CE1 1 
ATOM   783  C CE1 B TYR   A 1 94  ? -15.604 11.954  5.946  0.44 37.16 ?  94  TYR   A CE1 1 
ATOM   784  C CE2 A TYR   A 1 94  ? -14.171 7.834   0.909  0.56 35.92 ?  94  TYR   A CE2 1 
ATOM   785  C CE2 B TYR   A 1 94  ? -16.352 11.884  3.673  0.44 37.60 ?  94  TYR   A CE2 1 
ATOM   786  C CZ  A TYR   A 1 94  ? -13.793 8.916   0.144  0.56 36.71 ?  94  TYR   A CZ  1 
ATOM   787  C CZ  B TYR   A 1 94  ? -16.408 12.436  4.932  0.44 39.15 ?  94  TYR   A CZ  1 
ATOM   788  O OH  A TYR   A 1 94  ? -13.796 8.814   -1.231 0.56 39.31 ?  94  TYR   A OH  1 
ATOM   789  O OH  B TYR   A 1 94  ? -17.274 13.476  5.174  0.44 44.95 ?  94  TYR   A OH  1 
ATOM   790  N N   . CYS   A 1 95  ? -11.840 6.929   5.383  1.00 29.38 ?  95  CYS   A N   1 
ATOM   791  C CA  . CYS   A 1 95  ? -11.125 5.687   5.133  1.00 24.06 ?  95  CYS   A CA  1 
ATOM   792  C C   . CYS   A 1 95  ? -11.479 5.164   3.752  1.00 34.40 ?  95  CYS   A C   1 
ATOM   793  O O   . CYS   A 1 95  ? -12.635 4.801   3.494  1.00 28.98 ?  95  CYS   A O   1 
ATOM   794  C CB  . CYS   A 1 95  ? -11.473 4.651   6.199  1.00 26.17 ?  95  CYS   A CB  1 
ATOM   795  S SG  . CYS   A 1 95  ? -10.529 3.185   6.007  1.00 31.16 ?  95  CYS   A SG  1 
ATOM   796  N N   . ARG   A 1 96  ? -10.482 5.097   2.872  1.00 26.61 ?  96  ARG   A N   1 
ATOM   797  C CA  . ARG   A 1 96  ? -10.702 4.720   1.481  1.00 27.58 ?  96  ARG   A CA  1 
ATOM   798  C C   . ARG   A 1 96  ? -10.104 3.365   1.147  1.00 26.86 ?  96  ARG   A C   1 
ATOM   799  O O   . ARG   A 1 96  ? -9.862  3.068   -0.029 1.00 33.52 ?  96  ARG   A O   1 
ATOM   800  C CB  . ARG   A 1 96  ? -10.140 5.799   0.567  1.00 28.56 ?  96  ARG   A CB  1 
ATOM   801  C CG  . ARG   A 1 96  ? -10.923 7.076   0.686  1.00 32.00 ?  96  ARG   A CG  1 
ATOM   802  C CD  . ARG   A 1 96  ? -10.129 8.210   0.162  1.00 36.00 ?  96  ARG   A CD  1 
ATOM   803  N NE  . ARG   A 1 96  ? -9.245  8.738   1.192  1.00 28.79 ?  96  ARG   A NE  1 
ATOM   804  C CZ  . ARG   A 1 96  ? -8.324  9.656   0.948  1.00 26.70 ?  96  ARG   A CZ  1 
ATOM   805  N NH1 . ARG   A 1 96  ? -8.165  10.154  -0.268 1.00 23.70 ?  96  ARG   A NH1 1 
ATOM   806  N NH2 . ARG   A 1 96  ? -7.525  10.055  1.937  1.00 23.17 ?  96  ARG   A NH2 1 
ATOM   807  N N   . SER   A 1 97  ? -9.872  2.532   2.165  1.00 31.34 ?  97  SER   A N   1 
ATOM   808  C CA  . SER   A 1 97  ? -9.256  1.228   1.948  1.00 32.51 ?  97  SER   A CA  1 
ATOM   809  C C   . SER   A 1 97  ? -10.020 0.409   0.913  1.00 37.11 ?  97  SER   A C   1 
ATOM   810  O O   . SER   A 1 97  ? -9.416  -0.204  0.027  1.00 33.88 ?  97  SER   A O   1 
ATOM   811  C CB  . SER   A 1 97  ? -9.204  0.471   3.272  1.00 31.15 ?  97  SER   A CB  1 
ATOM   812  O OG  . SER   A 1 97  ? -8.433  1.198   4.196  1.00 33.16 ?  97  SER   A OG  1 
ATOM   813  N N   . ARG   A 1 98  ? -11.353 0.407   1.003  1.00 37.86 ?  98  ARG   A N   1 
ATOM   814  C CA  . ARG   A 1 98  ? -12.155 -0.455  0.139  1.00 44.78 ?  98  ARG   A CA  1 
ATOM   815  C C   . ARG   A 1 98  ? -12.064 -0.010  -1.312 1.00 42.00 ?  98  ARG   A C   1 
ATOM   816  O O   . ARG   A 1 98  ? -12.057 -0.840  -2.229 1.00 52.33 ?  98  ARG   A O   1 
ATOM   817  C CB  . ARG   A 1 98  ? -13.610 -0.454  0.608  1.00 48.18 ?  98  ARG   A CB  1 
ATOM   818  C CG  . ARG   A 1 98  ? -14.279 -1.817  0.573  1.00 71.14 ?  98  ARG   A CG  1 
ATOM   819  C CD  . ARG   A 1 98  ? -15.778 -1.670  0.336  1.00 83.73 ?  98  ARG   A CD  1 
ATOM   820  N NE  . ARG   A 1 98  ? -16.360 -2.859  -0.279 1.00 89.49 ?  98  ARG   A NE  1 
ATOM   821  C CZ  . ARG   A 1 98  ? -17.588 -2.922  -0.779 1.00 96.56 ?  98  ARG   A CZ  1 
ATOM   822  N NH1 . ARG   A 1 98  ? -18.380 -1.860  -0.809 1.00 92.34 ?  98  ARG   A NH1 1 
ATOM   823  N NH2 . ARG   A 1 98  ? -18.031 -4.076  -1.272 1.00 99.86 ?  98  ARG   A NH2 1 
ATOM   824  N N   . GLU   A 1 99  ? -11.981 1.299   -1.531 1.00 42.28 ?  99  GLU   A N   1 
ATOM   825  C CA  . GLU   A 1 99  ? -11.887 1.855   -2.871 1.00 41.41 ?  99  GLU   A CA  1 
ATOM   826  C C   . GLU   A 1 99  ? -10.554 1.547   -3.522 1.00 42.91 ?  99  GLU   A C   1 
ATOM   827  O O   . GLU   A 1 99  ? -10.434 1.661   -4.746 1.00 46.79 ?  99  GLU   A O   1 
ATOM   828  C CB  . GLU   A 1 99  ? -12.064 3.365   -2.788 1.00 39.42 ?  99  GLU   A CB  1 
ATOM   829  C CG  . GLU   A 1 99  ? -13.305 3.747   -2.051 1.00 45.61 ?  99  GLU   A CG  1 
ATOM   830  C CD  . GLU   A 1 99  ? -13.473 5.239   -1.923 1.00 59.38 ?  99  GLU   A CD  1 
ATOM   831  O OE1 . GLU   A 1 99  ? -14.198 5.652   -0.993 1.00 62.28 ?  99  GLU   A OE1 1 
ATOM   832  O OE2 . GLU   A 1 99  ? -12.848 5.997   -2.701 1.00 54.20 ?  99  GLU   A OE2 1 
ATOM   833  N N   . LYS   A 1 100 ? -9.553  1.174   -2.732 1.00 37.13 ?  100 LYS   A N   1 
ATOM   834  C CA  . LYS   A 1 100 ? -8.186  1.022   -3.199 1.00 34.17 ?  100 LYS   A CA  1 
ATOM   835  C C   . LYS   A 1 100 ? -7.858  -0.415  -3.571 1.00 39.72 ?  100 LYS   A C   1 
ATOM   836  O O   . LYS   A 1 100 ? -6.680  -0.744  -3.743 1.00 38.35 ?  100 LYS   A O   1 
ATOM   837  C CB  . LYS   A 1 100 ? -7.199  1.466   -2.112 1.00 38.39 ?  100 LYS   A CB  1 
ATOM   838  C CG  . LYS   A 1 100 ? -7.226  2.916   -1.672 1.00 43.63 ?  100 LYS   A CG  1 
ATOM   839  C CD  . LYS   A 1 100 ? -7.012  3.885   -2.757 1.00 41.72 ?  100 LYS   A CD  1 
ATOM   840  C CE  . LYS   A 1 100 ? -7.241  5.292   -2.222 1.00 34.51 ?  100 LYS   A CE  1 
ATOM   841  N NZ  . LYS   A 1 100 ? -6.438  6.219   -3.043 1.00 27.83 ?  100 LYS   A NZ  1 
ATOM   842  N N   . GLY   A 1 101 ? -8.852  -1.291  -3.627 1.00 37.14 ?  101 GLY   A N   1 
ATOM   843  C CA  . GLY   A 1 101 ? -8.604  -2.666  -3.969 1.00 37.62 ?  101 GLY   A CA  1 
ATOM   844  C C   . GLY   A 1 101 ? -7.965  -3.454  -2.846 1.00 39.89 ?  101 GLY   A C   1 
ATOM   845  O O   . GLY   A 1 101 ? -7.948  -3.038  -1.683 1.00 36.48 ?  101 GLY   A O   1 
ATOM   846  N N   . PRO   A 1 102 ? -7.408  -4.615  -3.187 1.00 41.96 ?  102 PRO   A N   1 
ATOM   847  C CA  . PRO   A 1 102 ? -6.880  -5.512  -2.152 1.00 45.09 ?  102 PRO   A CA  1 
ATOM   848  C C   . PRO   A 1 102 ? -5.735  -4.869  -1.391 1.00 39.33 ?  102 PRO   A C   1 
ATOM   849  O O   . PRO   A 1 102 ? -4.936  -4.115  -1.951 1.00 34.83 ?  102 PRO   A O   1 
ATOM   850  C CB  . PRO   A 1 102 ? -6.394  -6.739  -2.937 1.00 47.88 ?  102 PRO   A CB  1 
ATOM   851  C CG  . PRO   A 1 102 ? -6.781  -6.537  -4.349 1.00 52.37 ?  102 PRO   A CG  1 
ATOM   852  C CD  . PRO   A 1 102 ? -7.315  -5.166  -4.549 1.00 41.75 ?  102 PRO   A CD  1 
ATOM   853  N N   . TYR   A 1 103 ? -5.654  -5.195  -0.107 1.00 40.34 ?  103 TYR   A N   1 
ATOM   854  C CA  . TYR   A 1 103 ? -4.535  -4.738  0.704  1.00 35.21 ?  103 TYR   A CA  1 
ATOM   855  C C   . TYR   A 1 103 ? -3.227  -5.252  0.117  1.00 36.15 ?  103 TYR   A C   1 
ATOM   856  O O   . TYR   A 1 103 ? -3.165  -6.339  -0.462 1.00 40.32 ?  103 TYR   A O   1 
ATOM   857  C CB  . TYR   A 1 103 ? -4.690  -5.231  2.140  1.00 34.27 ?  103 TYR   A CB  1 
ATOM   858  C CG  . TYR   A 1 103 ? -5.765  -4.526  2.923  1.00 36.23 ?  103 TYR   A CG  1 
ATOM   859  C CD1 . TYR   A 1 103 ? -5.653  -3.180  3.242  1.00 31.87 ?  103 TYR   A CD1 1 
ATOM   860  C CD2 . TYR   A 1 103 ? -6.906  -5.205  3.331  1.00 41.61 ?  103 TYR   A CD2 1 
ATOM   861  C CE1 . TYR   A 1 103 ? -6.637  -2.539  3.961  1.00 36.81 ?  103 TYR   A CE1 1 
ATOM   862  C CE2 . TYR   A 1 103 ? -7.897  -4.572  4.050  1.00 36.98 ?  103 TYR   A CE2 1 
ATOM   863  C CZ  . TYR   A 1 103 ? -7.762  -3.242  4.364  1.00 37.50 ?  103 TYR   A CZ  1 
ATOM   864  O OH  . TYR   A 1 103 ? -8.747  -2.596  5.081  1.00 39.58 ?  103 TYR   A OH  1 
ATOM   865  N N   . ALA   A 1 104 ? -2.170  -4.454  0.273  1.00 34.53 ?  104 ALA   A N   1 
ATOM   866  C CA  . ALA   A 1 104 ? -0.857  -4.855  -0.213 1.00 34.25 ?  104 ALA   A CA  1 
ATOM   867  C C   . ALA   A 1 104 ? -0.129  -5.759  0.772  1.00 32.01 ?  104 ALA   A C   1 
ATOM   868  O O   . ALA   A 1 104 ? 0.675   -6.600  0.353  1.00 38.55 ?  104 ALA   A O   1 
ATOM   869  C CB  . ALA   A 1 104 ? 0.000   -3.620  -0.506 1.00 36.96 ?  104 ALA   A CB  1 
ATOM   870  N N   . ALA   A 1 105 ? -0.371  -5.588  2.071  1.00 32.89 ?  105 ALA   A N   1 
ATOM   871  C CA  . ALA   A 1 105 ? 0.363   -6.337  3.079  1.00 34.79 ?  105 ALA   A CA  1 
ATOM   872  C C   . ALA   A 1 105 ? -0.471  -6.392  4.345  1.00 34.01 ?  105 ALA   A C   1 
ATOM   873  O O   . ALA   A 1 105 ? -1.397  -5.606  4.544  1.00 33.03 ?  105 ALA   A O   1 
ATOM   874  C CB  . ALA   A 1 105 ? 1.742   -5.728  3.356  1.00 34.68 ?  105 ALA   A CB  1 
ATOM   875  N N   . LYS   A 1 106 ? -0.108  -7.324  5.211  1.00 35.59 ?  106 LYS   A N   1 
ATOM   876  C CA  . LYS   A 1 106 ? -0.976  -7.719  6.303  1.00 32.86 ?  106 LYS   A CA  1 
ATOM   877  C C   . LYS   A 1 106 ? -0.042  -8.277  7.364  1.00 35.93 ?  106 LYS   A C   1 
ATOM   878  O O   . LYS   A 1 106 ? 0.861   -9.049  7.033  1.00 42.10 ?  106 LYS   A O   1 
ATOM   879  C CB  . LYS   A 1 106 ? -1.971  -8.755  5.757  1.00 40.13 ?  106 LYS   A CB  1 
ATOM   880  C CG  . LYS   A 1 106 ? -2.889  -9.559  6.649  1.00 52.11 ?  106 LYS   A CG  1 
ATOM   881  C CD  . LYS   A 1 106 ? -3.360  -8.905  7.903  1.00 52.21 ?  106 LYS   A CD  1 
ATOM   882  C CE  . LYS   A 1 106 ? -4.257  -9.911  8.631  1.00 50.88 ?  106 LYS   A CE  1 
ATOM   883  N NZ  . LYS   A 1 106 ? -3.474  -10.890 9.443  1.00 50.66 ?  106 LYS   A NZ  1 
ATOM   884  N N   . THR   A 1 107 ? -0.197  -7.844  8.604  1.00 33.88 ?  107 THR   A N   1 
ATOM   885  C CA  . THR   A 1 107 ? 0.634   -8.378  9.671  1.00 35.92 ?  107 THR   A CA  1 
ATOM   886  C C   . THR   A 1 107 ? -0.190  -9.328  10.533 1.00 36.20 ?  107 THR   A C   1 
ATOM   887  O O   . THR   A 1 107 ? -1.406  -9.455  10.382 1.00 38.07 ?  107 THR   A O   1 
ATOM   888  C CB  . THR   A 1 107 ? 1.233   -7.256  10.527 1.00 29.42 ?  107 THR   A CB  1 
ATOM   889  O OG1 . THR   A 1 107 ? 0.185   -6.416  11.016 1.00 32.46 ?  107 THR   A OG1 1 
ATOM   890  C CG2 . THR   A 1 107 ? 2.193   -6.409  9.698  1.00 35.18 ?  107 THR   A CG2 1 
ATOM   891  N N   . ASP   A 1 108 ? 0.487   -9.990  11.467 1.00 41.10 ?  108 ASP   A N   1 
ATOM   892  C CA  . ASP   A 1 108 ? -0.161  -11.012 12.275 1.00 40.54 ?  108 ASP   A CA  1 
ATOM   893  C C   . ASP   A 1 108 ? -0.441  -10.564 13.697 1.00 44.28 ?  108 ASP   A C   1 
ATOM   894  O O   . ASP   A 1 108 ? -1.187  -11.241 14.407 1.00 48.19 ?  108 ASP   A O   1 
ATOM   895  C CB  . ASP   A 1 108 ? 0.691   -12.284 12.270 1.00 36.95 ?  108 ASP   A CB  1 
ATOM   896  C CG  . ASP   A 1 108 ? 0.967   -12.773 10.866 1.00 39.53 ?  108 ASP   A CG  1 
ATOM   897  O OD1 . ASP   A 1 108 ? 0.002   -12.930 10.095 1.00 45.47 ?  108 ASP   A OD1 1 
ATOM   898  O OD2 . ASP   A 1 108 ? 2.143   -12.977 10.513 1.00 53.34 ?  108 ASP   A OD2 1 
ATOM   899  N N   . GLY   A 1 109 ? 0.109   -9.437  14.126 1.00 35.90 ?  109 GLY   A N   1 
ATOM   900  C CA  . GLY   A 1 109 ? -0.212  -8.930  15.440 1.00 34.33 ?  109 GLY   A CA  1 
ATOM   901  C C   . GLY   A 1 109 ? 0.720   -7.797  15.817 1.00 39.35 ?  109 GLY   A C   1 
ATOM   902  O O   . GLY   A 1 109 ? 1.505   -7.312  14.993 1.00 32.27 ?  109 GLY   A O   1 
ATOM   903  N N   . VAL   A 1 110 ? 0.582   -7.374  17.079 1.00 38.50 ?  110 VAL   A N   1 
ATOM   904  C CA  . VAL   A 1 110 ? 1.325   -6.271  17.677 1.00 37.03 ?  110 VAL   A CA  1 
ATOM   905  C C   . VAL   A 1 110 ? 1.842   -6.723  19.031 1.00 40.28 ?  110 VAL   A C   1 
ATOM   906  O O   . VAL   A 1 110 ? 1.076   -7.266  19.833 1.00 36.19 ?  110 VAL   A O   1 
ATOM   907  C CB  . VAL   A 1 110 ? 0.446   -5.029  17.876 1.00 34.01 ?  110 VAL   A CB  1 
ATOM   908  C CG1 . VAL   A 1 110 ? 1.325   -3.819  18.138 1.00 34.11 ?  110 VAL   A CG1 1 
ATOM   909  C CG2 . VAL   A 1 110 ? -0.448  -4.822  16.697 1.00 38.15 ?  110 VAL   A CG2 1 
ATOM   910  N N   . ARG   A 1 111 ? 3.115   -6.461  19.313 1.00 34.28 ?  111 ARG   A N   1 
ATOM   911  C CA  . ARG   A 1 111 ? 3.653   -6.711  20.644 1.00 40.46 ?  111 ARG   A CA  1 
ATOM   912  C C   . ARG   A 1 111 ? 4.133   -5.409  21.261 1.00 40.24 ?  111 ARG   A C   1 
ATOM   913  O O   . ARG   A 1 111 ? 4.608   -4.512  20.560 1.00 33.65 ?  111 ARG   A O   1 
ATOM   914  C CB  . ARG   A 1 111 ? 4.834   -7.682  20.636 1.00 40.33 ?  111 ARG   A CB  1 
ATOM   915  C CG  . ARG   A 1 111 ? 4.514   -9.052  20.121 1.00 55.32 ?  111 ARG   A CG  1 
ATOM   916  C CD  . ARG   A 1 111 ? 3.358   -9.755  20.830 1.00 57.00 ?  111 ARG   A CD  1 
ATOM   917  N NE  . ARG   A 1 111 ? 3.307   -11.153 20.421 1.00 71.03 ?  111 ARG   A NE  1 
ATOM   918  C CZ  . ARG   A 1 111 ? 4.362   -11.944 20.260 1.00 75.47 ?  111 ARG   A CZ  1 
ATOM   919  N NH1 . ARG   A 1 111 ? 5.519   -11.699 20.864 1.00 77.20 ?  111 ARG   A NH1 1 
ATOM   920  N NH2 . ARG   A 1 111 ? 4.243   -13.038 19.509 1.00 75.83 ?  111 ARG   A NH2 1 
ATOM   921  N N   . GLN   A 1 112 ? 4.035   -5.321  22.581 1.00 33.89 ?  112 GLN   A N   1 
ATOM   922  C CA  . GLN   A 1 112 ? 4.633   -4.216  23.309 1.00 29.14 ?  112 GLN   A CA  1 
ATOM   923  C C   . GLN   A 1 112 ? 6.000   -4.636  23.827 1.00 31.19 ?  112 GLN   A C   1 
ATOM   924  O O   . GLN   A 1 112 ? 6.204   -5.784  24.220 1.00 35.70 ?  112 GLN   A O   1 
ATOM   925  C CB  . GLN   A 1 112 ? 3.756   -3.759  24.470 1.00 34.74 ?  112 GLN   A CB  1 
ATOM   926  C CG  . GLN   A 1 112 ? 4.230   -2.427  25.039 1.00 33.90 ?  112 GLN   A CG  1 
ATOM   927  C CD  . GLN   A 1 112 ? 3.402   -1.947  26.210 1.00 45.27 ?  112 GLN   A CD  1 
ATOM   928  O OE1 . GLN   A 1 112 ? 2.462   -2.617  26.638 1.00 54.44 ?  112 GLN   A OE1 1 
ATOM   929  N NE2 . GLN   A 1 112 ? 3.742   -0.768  26.730 1.00 42.09 ?  112 GLN   A NE2 1 
ATOM   930  N N   . VAL   A 1 113 ? 6.940   -3.722  23.780 1.00 31.34 ?  113 VAL   A N   1 
ATOM   931  C CA  . VAL   A 1 113 ? 8.216   -3.924  24.452 1.00 32.63 ?  113 VAL   A CA  1 
ATOM   932  C C   . VAL   A 1 113 ? 7.987   -3.613  25.921 1.00 25.10 ?  113 VAL   A C   1 
ATOM   933  O O   . VAL   A 1 113 ? 7.260   -2.672  26.250 1.00 28.06 ?  113 VAL   A O   1 
ATOM   934  C CB  . VAL   A 1 113 ? 9.303   -3.014  23.844 1.00 28.72 ?  113 VAL   A CB  1 
ATOM   935  C CG1 . VAL   A 1 113 ? 10.665  -3.297  24.454 1.00 30.14 ?  113 VAL   A CG1 1 
ATOM   936  C CG2 . VAL   A 1 113 ? 9.343   -3.152  22.324 1.00 27.31 ?  113 VAL   A CG2 1 
ATOM   937  N N   . GLN   A 1 114 ? 8.564   -4.420  26.809 1.00 33.17 ?  114 GLN   A N   1 
ATOM   938  C CA  . GLN   A 1 114 ? 8.506   -4.111  28.224 1.00 34.03 ?  114 GLN   A CA  1 
ATOM   939  C C   . GLN   A 1 114 ? 8.969   -2.677  28.450 1.00 33.35 ?  114 GLN   A C   1 
ATOM   940  O O   . GLN   A 1 114 ? 10.101  -2.338  28.082 1.00 33.09 ?  114 GLN   A O   1 
ATOM   941  C CB  . GLN   A 1 114 ? 9.391   -5.055  29.024 1.00 40.12 ?  114 GLN   A CB  1 
ATOM   942  C CG  . GLN   A 1 114 ? 9.461   -4.659  30.491 1.00 44.65 ?  114 GLN   A CG  1 
ATOM   943  C CD  . GLN   A 1 114 ? 9.307   -5.841  31.406 1.00 57.08 ?  114 GLN   A CD  1 
ATOM   944  O OE1 . GLN   A 1 114 ? 8.225   -6.098  31.936 1.00 69.75 ?  114 GLN   A OE1 1 
ATOM   945  N NE2 . GLN   A 1 114 ? 10.396  -6.573  31.607 1.00 63.68 ?  114 GLN   A NE2 1 
ATOM   946  N N   . PRO   A 1 115 ? 8.136   -1.812  29.020 1.00 30.56 ?  115 PRO   A N   1 
ATOM   947  C CA  . PRO   A 1 115 ? 8.518   -0.406  29.143 1.00 29.38 ?  115 PRO   A CA  1 
ATOM   948  C C   . PRO   A 1 115 ? 9.630   -0.204  30.157 1.00 34.30 ?  115 PRO   A C   1 
ATOM   949  O O   . PRO   A 1 115 ? 9.910   -1.056  31.009 1.00 31.73 ?  115 PRO   A O   1 
ATOM   950  C CB  . PRO   A 1 115 ? 7.223   0.280   29.580 1.00 33.93 ?  115 PRO   A CB  1 
ATOM   951  C CG  . PRO   A 1 115 ? 6.416   -0.788  30.203 1.00 36.21 ?  115 PRO   A CG  1 
ATOM   952  C CD  . PRO   A 1 115 ? 6.765   -2.058  29.494 1.00 33.76 ?  115 PRO   A CD  1 
ATOM   953  N N   . TYR   A 1 116 ? 10.298  0.939   30.014 1.00 26.39 ?  116 TYR   A N   1 
ATOM   954  C CA  . TYR   A 1 116 ? 11.296  1.402   30.978 1.00 29.15 ?  116 TYR   A CA  1 
ATOM   955  C C   . TYR   A 1 116 ? 12.457  0.429   31.100 1.00 29.56 ?  116 TYR   A C   1 
ATOM   956  O O   . TYR   A 1 116 ? 13.075  0.310   32.161 1.00 32.60 ?  116 TYR   A O   1 
ATOM   957  C CB  . TYR   A 1 116 ? 10.656  1.660   32.341 1.00 32.37 ?  116 TYR   A CB  1 
ATOM   958  C CG  . TYR   A 1 116 ? 9.464   2.571   32.218 1.00 33.31 ?  116 TYR   A CG  1 
ATOM   959  C CD1 . TYR   A 1 116 ? 9.593   3.826   31.646 1.00 31.94 ?  116 TYR   A CD1 1 
ATOM   960  C CD2 . TYR   A 1 116 ? 8.206   2.160   32.626 1.00 41.17 ?  116 TYR   A CD2 1 
ATOM   961  C CE1 . TYR   A 1 116 ? 8.507   4.661   31.514 1.00 42.11 ?  116 TYR   A CE1 1 
ATOM   962  C CE2 . TYR   A 1 116 ? 7.114   2.988   32.500 1.00 41.42 ?  116 TYR   A CE2 1 
ATOM   963  C CZ  . TYR   A 1 116 ? 7.266   4.236   31.946 1.00 48.07 ?  116 TYR   A CZ  1 
ATOM   964  O OH  . TYR   A 1 116 ? 6.166   5.057   31.824 1.00 52.85 ?  116 TYR   A OH  1 
ATOM   965  N N   . ASN   A 1 117 ? 12.789  -0.236  29.996 1.00 31.64 ?  117 ASN   A N   1 
ATOM   966  C CA  . ASN   A 1 117 ? 13.775  -1.312  30.001 1.00 28.45 ?  117 ASN   A CA  1 
ATOM   967  C C   . ASN   A 1 117 ? 14.615  -1.142  28.744 1.00 29.15 ?  117 ASN   A C   1 
ATOM   968  O O   . ASN   A 1 117 ? 14.191  -1.531  27.650 1.00 28.04 ?  117 ASN   A O   1 
ATOM   969  C CB  . ASN   A 1 117 ? 13.091  -2.669  30.044 1.00 35.53 ?  117 ASN   A CB  1 
ATOM   970  C CG  . ASN   A 1 117 ? 14.070  -3.816  30.171 1.00 34.19 ?  117 ASN   A CG  1 
ATOM   971  O OD1 . ASN   A 1 117 ? 15.172  -3.783  29.625 1.00 33.18 ?  117 ASN   A OD1 1 
ATOM   972  N ND2 . ASN   A 1 117 ? 13.664  -4.848  30.895 1.00 40.85 ?  117 ASN   A ND2 1 
ATOM   973  N N   . GLU   A 1 118 ? 15.804  -0.559  28.902 1.00 30.00 ?  118 GLU   A N   1 
ATOM   974  C CA  . GLU   A 1 118 ? 16.627  -0.288  27.734 1.00 29.23 ?  118 GLU   A CA  1 
ATOM   975  C C   . GLU   A 1 118 ? 16.968  -1.576  27.006 1.00 31.91 ?  118 GLU   A C   1 
ATOM   976  O O   . GLU   A 1 118 ? 16.877  -1.645  25.773 1.00 29.34 ?  118 GLU   A O   1 
ATOM   977  C CB  . GLU   A 1 118 ? 17.898  0.442   28.138 1.00 30.44 ?  118 GLU   A CB  1 
ATOM   978  C CG  . GLU   A 1 118 ? 18.799  0.698   26.965 1.00 27.93 ?  118 GLU   A CG  1 
ATOM   979  C CD  . GLU   A 1 118 ? 19.907  1.668   27.312 1.00 30.21 ?  118 GLU   A CD  1 
ATOM   980  O OE1 . GLU   A 1 118 ? 19.591  2.801   27.730 1.00 27.01 ?  118 GLU   A OE1 1 
ATOM   981  O OE2 . GLU   A 1 118 ? 21.079  1.292   27.161 1.00 27.96 ?  118 GLU   A OE2 1 
ATOM   982  N N   . GLY   A 1 119 ? 17.326  -2.620  27.755 1.00 30.06 ?  119 GLY   A N   1 
ATOM   983  C CA  . GLY   A 1 119 ? 17.737  -3.859  27.115 1.00 29.71 ?  119 GLY   A CA  1 
ATOM   984  C C   . GLY   A 1 119 ? 16.627  -4.491  26.299 1.00 27.23 ?  119 GLY   A C   1 
ATOM   985  O O   . GLY   A 1 119 ? 16.869  -5.028  25.217 1.00 28.74 ?  119 GLY   A O   1 
ATOM   986  N N   . ALA   A 1 120 ? 15.398  -4.439  26.805 1.00 27.93 ?  120 ALA   A N   1 
ATOM   987  C CA  . ALA   A 1 120 ? 14.278  -4.999  26.060 1.00 28.40 ?  120 ALA   A CA  1 
ATOM   988  C C   . ALA   A 1 120 ? 14.088  -4.248  24.747 1.00 28.00 ?  120 ALA   A C   1 
ATOM   989  O O   . ALA   A 1 120 ? 13.801  -4.846  23.707 1.00 26.07 ?  120 ALA   A O   1 
ATOM   990  C CB  . ALA   A 1 120 ? 13.004  -4.945  26.910 1.00 27.87 ?  120 ALA   A CB  1 
ATOM   991  N N   . LEU   A 1 121 ? 14.261  -2.931  24.777 1.00 25.90 ?  121 LEU   A N   1 
ATOM   992  C CA  . LEU   A 1 121 ? 14.120  -2.162  23.552 1.00 25.99 ?  121 LEU   A CA  1 
ATOM   993  C C   . LEU   A 1 121 ? 15.215  -2.529  22.562 1.00 29.26 ?  121 LEU   A C   1 
ATOM   994  O O   . LEU   A 1 121 ? 14.946  -2.755  21.375 1.00 27.42 ?  121 LEU   A O   1 
ATOM   995  C CB  . LEU   A 1 121 ? 14.156  -0.672  23.873 1.00 26.61 ?  121 LEU   A CB  1 
ATOM   996  C CG  . LEU   A 1 121 ? 13.965  0.225   22.659 1.00 28.19 ?  121 LEU   A CG  1 
ATOM   997  C CD1 . LEU   A 1 121 ? 12.697  -0.183  21.926 1.00 26.04 ?  121 LEU   A CD1 1 
ATOM   998  C CD2 . LEU   A 1 121 ? 13.877  1.653   23.147 1.00 26.76 ?  121 LEU   A CD2 1 
ATOM   999  N N   . LEU   A 1 122 ? 16.464  -2.594  23.032 1.00 24.65 ?  122 LEU   A N   1 
ATOM   1000 C CA  . LEU   A 1 122 ? 17.556  -2.943  22.129 1.00 24.46 ?  122 LEU   A CA  1 
ATOM   1001 C C   . LEU   A 1 122 ? 17.348  -4.324  21.538 1.00 27.03 ?  122 LEU   A C   1 
ATOM   1002 O O   . LEU   A 1 122 ? 17.568  -4.544  20.344 1.00 27.03 ?  122 LEU   A O   1 
ATOM   1003 C CB  . LEU   A 1 122 ? 18.888  -2.891  22.869 1.00 27.87 ?  122 LEU   A CB  1 
ATOM   1004 C CG  . LEU   A 1 122 ? 19.274  -1.544  23.440 1.00 29.02 ?  122 LEU   A CG  1 
ATOM   1005 C CD1 . LEU   A 1 122 ? 20.575  -1.704  24.227 1.00 27.61 ?  122 LEU   A CD1 1 
ATOM   1006 C CD2 . LEU   A 1 122 ? 19.392  -0.529  22.321 1.00 30.67 ?  122 LEU   A CD2 1 
ATOM   1007 N N   . TYR   A 1 123 ? 16.922  -5.272  22.363 1.00 23.22 ?  123 TYR   A N   1 
ATOM   1008 C CA  . TYR   A 1 123 ? 16.690  -6.604  21.842 1.00 25.51 ?  123 TYR   A CA  1 
ATOM   1009 C C   . TYR   A 1 123 ? 15.657  -6.567  20.719 1.00 26.49 ?  123 TYR   A C   1 
ATOM   1010 O O   . TYR   A 1 123 ? 15.833  -7.213  19.677 1.00 29.74 ?  123 TYR   A O   1 
ATOM   1011 C CB  . TYR   A 1 123 ? 16.251  -7.521  22.980 1.00 25.26 ?  123 TYR   A CB  1 
ATOM   1012 C CG  . TYR   A 1 123 ? 15.927  -8.884  22.481 1.00 29.66 ?  123 TYR   A CG  1 
ATOM   1013 C CD1 . TYR   A 1 123 ? 16.942  -9.765  22.126 1.00 33.98 ?  123 TYR   A CD1 1 
ATOM   1014 C CD2 . TYR   A 1 123 ? 14.609  -9.292  22.318 1.00 45.59 ?  123 TYR   A CD2 1 
ATOM   1015 C CE1 . TYR   A 1 123 ? 16.657  -11.021 21.652 1.00 41.14 ?  123 TYR   A CE1 1 
ATOM   1016 C CE2 . TYR   A 1 123 ? 14.312  -10.554 21.837 1.00 41.64 ?  123 TYR   A CE2 1 
ATOM   1017 C CZ  . TYR   A 1 123 ? 15.340  -11.412 21.507 1.00 50.40 ?  123 TYR   A CZ  1 
ATOM   1018 O OH  . TYR   A 1 123 ? 15.055  -12.671 21.029 1.00 59.94 ?  123 TYR   A OH  1 
ATOM   1019 N N   . SER   A 1 124 ? 14.600  -5.773  20.893 1.00 27.20 ?  124 SER   A N   1 
ATOM   1020 C CA  . SER   A 1 124 ? 13.578  -5.681  19.854 1.00 28.31 ?  124 SER   A CA  1 
ATOM   1021 C C   . SER   A 1 124 ? 14.134  -5.037  18.593 1.00 26.32 ?  124 SER   A C   1 
ATOM   1022 O O   . SER   A 1 124 ? 13.884  -5.520  17.481 1.00 27.34 ?  124 SER   A O   1 
ATOM   1023 C CB  . SER   A 1 124 ? 12.383  -4.896  20.376 1.00 30.25 ?  124 SER   A CB  1 
ATOM   1024 O OG  . SER   A 1 124 ? 11.766  -5.598  21.431 1.00 43.07 ?  124 SER   A OG  1 
ATOM   1025 N N   . ILE   A 1 125 ? 14.897  -3.947  18.750 1.00 25.65 ?  125 ILE   A N   1 
ATOM   1026 C CA  . ILE   A 1 125 ? 15.479  -3.267  17.594 1.00 31.37 ?  125 ILE   A CA  1 
ATOM   1027 C C   . ILE   A 1 125 ? 16.395  -4.199  16.816 1.00 24.87 ?  125 ILE   A C   1 
ATOM   1028 O O   . ILE   A 1 125 ? 16.481  -4.131  15.582 1.00 27.03 ?  125 ILE   A O   1 
ATOM   1029 C CB  . ILE   A 1 125 ? 16.229  -2.003  18.050 1.00 24.93 ?  125 ILE   A CB  1 
ATOM   1030 C CG1 . ILE   A 1 125 ? 15.291  -1.046  18.794 1.00 24.29 ?  125 ILE   A CG1 1 
ATOM   1031 C CG2 . ILE   A 1 125 ? 16.932  -1.344  16.863 1.00 27.46 ?  125 ILE   A CG2 1 
ATOM   1032 C CD1 . ILE   A 1 125 ? 16.022  0.133   19.390 1.00 24.66 ?  125 ILE   A CD1 1 
ATOM   1033 N N   . ALA   A 1 126 ? 17.139  -5.051  17.517 1.00 25.46 ?  126 ALA   A N   1 
ATOM   1034 C CA  . ALA   A 1 126 ? 18.004  -5.978  16.803 1.00 23.51 ?  126 ALA   A CA  1 
ATOM   1035 C C   . ALA   A 1 126 ? 17.209  -6.937  15.936 1.00 27.96 ?  126 ALA   A C   1 
ATOM   1036 O O   . ALA   A 1 126 ? 17.776  -7.542  15.024 1.00 33.07 ?  126 ALA   A O   1 
ATOM   1037 C CB  . ALA   A 1 126 ? 18.874  -6.780  17.780 1.00 25.44 ?  126 ALA   A CB  1 
ATOM   1038 N N   . ASN   A 1 127 ? 15.924  -7.104  16.219 1.00 27.38 ?  127 ASN   A N   1 
ATOM   1039 C CA  . ASN   A 1 127 ? 15.060  -7.978  15.437 1.00 29.02 ?  127 ASN   A CA  1 
ATOM   1040 C C   . ASN   A 1 127 ? 14.304  -7.258  14.331 1.00 28.87 ?  127 ASN   A C   1 
ATOM   1041 O O   . ASN   A 1 127 ? 14.050  -7.854  13.275 1.00 31.54 ?  127 ASN   A O   1 
ATOM   1042 C CB  . ASN   A 1 127 ? 14.073  -8.667  16.375 1.00 32.49 ?  127 ASN   A CB  1 
ATOM   1043 C CG  . ASN   A 1 127 ? 14.733  -9.769  17.166 1.00 41.63 ?  127 ASN   A CG  1 
ATOM   1044 O OD1 . ASN   A 1 127 ? 14.757  -9.745  18.400 1.00 51.73 ?  127 ASN   A OD1 1 
ATOM   1045 N ND2 . ASN   A 1 127 ? 15.281  -10.748 16.453 1.00 43.38 ?  127 ASN   A ND2 1 
ATOM   1046 N N   . GLN   A 1 128 ? 13.953  -6.002  14.542 1.00 25.48 ?  128 GLN   A N   1 
ATOM   1047 C CA  . GLN   A 1 128 ? 13.147  -5.258  13.581 1.00 25.64 ?  128 GLN   A CA  1 
ATOM   1048 C C   . GLN   A 1 128 ? 13.008  -3.815  14.041 1.00 27.22 ?  128 GLN   A C   1 
ATOM   1049 O O   . GLN   A 1 128 ? 13.140  -3.526  15.237 1.00 28.97 ?  128 GLN   A O   1 
ATOM   1050 C CB  . GLN   A 1 128 ? 11.757  -5.873  13.455 1.00 29.04 ?  128 GLN   A CB  1 
ATOM   1051 C CG  . GLN   A 1 128 ? 10.977  -5.765  14.751 1.00 28.19 ?  128 GLN   A CG  1 
ATOM   1052 C CD  . GLN   A 1 128 ? 9.802   -6.681  14.759 1.00 38.51 ?  128 GLN   A CD  1 
ATOM   1053 O OE1 . GLN   A 1 128 ? 9.821   -7.711  15.418 1.00 37.64 ?  128 GLN   A OE1 1 
ATOM   1054 N NE2 . GLN   A 1 128 ? 8.777   -6.333  13.999 1.00 31.89 ?  128 GLN   A NE2 1 
ATOM   1055 N N   . PRO   A 1 129 ? 12.708  -2.892  13.131 1.00 30.08 ?  129 PRO   A N   1 
ATOM   1056 C CA  . PRO   A 1 129 ? 12.386  -1.525  13.554 1.00 23.58 ?  129 PRO   A CA  1 
ATOM   1057 C C   . PRO   A 1 129 ? 11.205  -1.510  14.512 1.00 25.24 ?  129 PRO   A C   1 
ATOM   1058 O O   . PRO   A 1 129 ? 10.268  -2.304  14.404 1.00 24.79 ?  129 PRO   A O   1 
ATOM   1059 C CB  . PRO   A 1 129 ? 12.059  -0.820  12.230 1.00 22.26 ?  129 PRO   A CB  1 
ATOM   1060 C CG  . PRO   A 1 129 ? 12.873  -1.584  11.229 1.00 26.41 ?  129 PRO   A CG  1 
ATOM   1061 C CD  . PRO   A 1 129 ? 12.765  -3.017  11.665 1.00 21.02 ?  129 PRO   A CD  1 
ATOM   1062 N N   . VAL   A 1 130 ? 11.261  -0.597  15.463 1.00 23.40 ?  130 VAL   A N   1 
ATOM   1063 C CA  . VAL   A 1 130 ? 10.311  -0.562  16.560 1.00 22.94 ?  130 VAL   A CA  1 
ATOM   1064 C C   . VAL   A 1 130 ? 9.739   0.835   16.622 1.00 26.26 ?  130 VAL   A C   1 
ATOM   1065 O O   . VAL   A 1 130 ? 10.466  1.821   16.447 1.00 27.15 ?  130 VAL   A O   1 
ATOM   1066 C CB  . VAL   A 1 130 ? 10.985  -0.923  17.904 1.00 24.64 ?  130 VAL   A CB  1 
ATOM   1067 C CG1 . VAL   A 1 130 ? 10.001  -0.776  19.059 1.00 26.65 ?  130 VAL   A CG1 1 
ATOM   1068 C CG2 . VAL   A 1 130 ? 11.563  -2.342  17.845 1.00 27.53 ?  130 VAL   A CG2 1 
ATOM   1069 N N   . SER   A 1 131 ? 8.442   0.916   16.861 1.00 23.47 ?  131 SER   A N   1 
ATOM   1070 C CA  . SER   A 1 131 ? 7.794   2.184   17.123 1.00 22.87 ?  131 SER   A CA  1 
ATOM   1071 C C   . SER   A 1 131 ? 8.051   2.606   18.566 1.00 25.92 ?  131 SER   A C   1 
ATOM   1072 O O   . SER   A 1 131 ? 7.790   1.843   19.499 1.00 25.81 ?  131 SER   A O   1 
ATOM   1073 C CB  . SER   A 1 131 ? 6.299   2.053   16.873 1.00 24.44 ?  131 SER   A CB  1 
ATOM   1074 O OG  . SER   A 1 131 ? 5.618   3.212   17.292 1.00 26.85 ?  131 SER   A OG  1 
ATOM   1075 N N   . VAL   A 1 132 ? 8.562   3.815   18.754 1.00 22.13 ?  132 VAL   A N   1 
ATOM   1076 C CA  . VAL   A 1 132 ? 8.885   4.320   20.080 1.00 22.97 ?  132 VAL   A CA  1 
ATOM   1077 C C   . VAL   A 1 132 ? 8.332   5.723   20.177 1.00 25.03 ?  132 VAL   A C   1 
ATOM   1078 O O   . VAL   A 1 132 ? 8.062   6.368   19.166 1.00 27.22 ?  132 VAL   A O   1 
ATOM   1079 C CB  . VAL   A 1 132 ? 10.402  4.330   20.371 1.00 28.27 ?  132 VAL   A CB  1 
ATOM   1080 C CG1 . VAL   A 1 132 ? 10.972  2.915   20.300 1.00 25.04 ?  132 VAL   A CG1 1 
ATOM   1081 C CG2 . VAL   A 1 132 ? 11.122  5.267   19.357 1.00 24.39 ?  132 VAL   A CG2 1 
ATOM   1082 N N   . VAL   A 1 133 ? 8.179   6.202   21.416 1.00 22.19 ?  133 VAL   A N   1 
ATOM   1083 C CA  . VAL   A 1 133 ? 7.714   7.564   21.619 1.00 21.90 ?  133 VAL   A CA  1 
ATOM   1084 C C   . VAL   A 1 133 ? 8.771   8.321   22.403 1.00 29.06 ?  133 VAL   A C   1 
ATOM   1085 O O   . VAL   A 1 133 ? 9.594   7.745   23.123 1.00 26.23 ?  133 VAL   A O   1 
ATOM   1086 C CB  . VAL   A 1 133 ? 6.353   7.626   22.334 1.00 25.69 ?  133 VAL   A CB  1 
ATOM   1087 C CG1 . VAL   A 1 133 ? 5.281   6.925   21.505 1.00 34.40 ?  133 VAL   A CG1 1 
ATOM   1088 C CG2 . VAL   A 1 133 ? 6.449   7.002   23.726 1.00 26.89 ?  133 VAL   A CG2 1 
ATOM   1089 N N   . LEU   A 1 134 ? 8.737   9.632   22.258 1.00 24.07 ?  134 LEU   A N   1 
ATOM   1090 C CA  . LEU   A 1 134 ? 9.658   10.482  22.984 1.00 23.18 ?  134 LEU   A CA  1 
ATOM   1091 C C   . LEU   A 1 134 ? 9.029   11.857  23.091 1.00 26.30 ?  134 LEU   A C   1 
ATOM   1092 O O   . LEU   A 1 134 ? 8.040   12.166  22.421 1.00 25.18 ?  134 LEU   A O   1 
ATOM   1093 C CB  . LEU   A 1 134 ? 11.022  10.553  22.291 1.00 24.94 ?  134 LEU   A CB  1 
ATOM   1094 C CG  . LEU   A 1 134 ? 11.031  10.719  20.771 1.00 28.52 ?  134 LEU   A CG  1 
ATOM   1095 C CD1 . LEU   A 1 134 ? 10.622  12.105  20.311 1.00 30.80 ?  134 LEU   A CD1 1 
ATOM   1096 C CD2 . LEU   A 1 134 ? 12.418  10.428  20.246 1.00 27.32 ?  134 LEU   A CD2 1 
ATOM   1097 N N   . GLU   A 1 135 ? 9.636   12.683  23.926 1.00 25.07 ?  135 GLU   A N   1 
ATOM   1098 C CA  . GLU   A 1 135 ? 9.254   14.080  24.058 1.00 22.19 ?  135 GLU   A CA  1 
ATOM   1099 C C   . GLU   A 1 135 ? 9.988   14.866  22.991 1.00 22.49 ?  135 GLU   A C   1 
ATOM   1100 O O   . GLU   A 1 135 ? 11.217  14.984  23.034 1.00 27.00 ?  135 GLU   A O   1 
ATOM   1101 C CB  . GLU   A 1 135 ? 9.603   14.600  25.440 1.00 24.40 ?  135 GLU   A CB  1 
ATOM   1102 C CG  . GLU   A 1 135 ? 9.232   16.039  25.646 1.00 27.76 ?  135 GLU   A CG  1 
ATOM   1103 C CD  . GLU   A 1 135 ? 9.953   16.605  26.836 1.00 29.70 ?  135 GLU   A CD  1 
ATOM   1104 O OE1 . GLU   A 1 135 ? 9.429   16.447  27.951 1.00 29.23 ?  135 GLU   A OE1 1 
ATOM   1105 O OE2 . GLU   A 1 135 ? 11.042  17.196  26.639 1.00 28.03 ?  135 GLU   A OE2 1 
ATOM   1106 N N   . ALA   A 1 136 ? 9.241   15.403  22.039 1.00 25.12 ?  136 ALA   A N   1 
ATOM   1107 C CA  . ALA   A 1 136 ? 9.815   16.171  20.949 1.00 29.06 ?  136 ALA   A CA  1 
ATOM   1108 C C   . ALA   A 1 136 ? 9.507   17.655  21.046 1.00 27.45 ?  136 ALA   A C   1 
ATOM   1109 O O   . ALA   A 1 136 ? 9.976   18.426  20.207 1.00 30.98 ?  136 ALA   A O   1 
ATOM   1110 C CB  . ALA   A 1 136 ? 9.312   15.627  19.611 1.00 25.93 ?  136 ALA   A CB  1 
ATOM   1111 N N   . ALA   A 1 137 ? 8.747   18.070  22.062 1.00 32.93 ?  137 ALA   A N   1 
ATOM   1112 C CA  . ALA   A 1 137 ? 8.302   19.458  22.184 1.00 41.76 ?  137 ALA   A CA  1 
ATOM   1113 C C   . ALA   A 1 137 ? 9.447   20.424  22.473 1.00 32.24 ?  137 ALA   A C   1 
ATOM   1114 O O   . ALA   A 1 137 ? 9.380   21.593  22.079 1.00 28.53 ?  137 ALA   A O   1 
ATOM   1115 C CB  . ALA   A 1 137 ? 7.260   19.560  23.295 1.00 30.33 ?  137 ALA   A CB  1 
ATOM   1116 N N   . GLY   A 1 138 ? 10.479  19.975  23.183 1.00 30.00 ?  138 GLY   A N   1 
ATOM   1117 C CA  . GLY   A 1 138 ? 11.551  20.871  23.561 1.00 29.73 ?  138 GLY   A CA  1 
ATOM   1118 C C   . GLY   A 1 138 ? 12.299  21.413  22.360 1.00 36.75 ?  138 GLY   A C   1 
ATOM   1119 O O   . GLY   A 1 138 ? 12.492  20.733  21.352 1.00 30.70 ?  138 GLY   A O   1 
ATOM   1120 N N   . LYS   A 1 139 ? 12.726  22.675  22.474 1.00 28.99 ?  139 LYS   A N   1 
ATOM   1121 C CA  . LYS   A 1 139 ? 13.471  23.307  21.393 1.00 31.05 ?  139 LYS   A CA  1 
ATOM   1122 C C   . LYS   A 1 139 ? 14.771  22.582  21.091 1.00 31.03 ?  139 LYS   A C   1 
ATOM   1123 O O   . LYS   A 1 139 ? 15.221  22.582  19.944 1.00 30.90 ?  139 LYS   A O   1 
ATOM   1124 C CB  . LYS   A 1 139 ? 13.777  24.775  21.721 1.00 28.37 ?  139 LYS   A CB  1 
ATOM   1125 C CG  . LYS   A 1 139 ? 12.555  25.673  21.832 1.00 47.55 ?  139 LYS   A CG  1 
ATOM   1126 C CD  . LYS   A 1 139 ? 12.823  27.013  21.133 1.00 60.74 ?  139 LYS   A CD  1 
ATOM   1127 C CE  . LYS   A 1 139 ? 13.028  28.166  22.118 1.00 69.83 ?  139 LYS   A CE  1 
ATOM   1128 N NZ  . LYS   A 1 139 ? 11.794  28.974  22.345 1.00 71.73 ?  139 LYS   A NZ  1 
ATOM   1129 N N   . ASP   A 1 140 ? 15.405  21.981  22.096 1.00 27.60 ?  140 ASP   A N   1 
ATOM   1130 C CA  . ASP   A 1 140 ? 16.647  21.271  21.825 1.00 25.80 ?  140 ASP   A CA  1 
ATOM   1131 C C   . ASP   A 1 140 ? 16.422  20.125  20.859 1.00 24.90 ?  140 ASP   A C   1 
ATOM   1132 O O   . ASP   A 1 140 ? 17.204  19.931  19.928 1.00 26.85 ?  140 ASP   A O   1 
ATOM   1133 C CB  . ASP   A 1 140 ? 17.253  20.773  23.123 1.00 26.63 ?  140 ASP   A CB  1 
ATOM   1134 C CG  . ASP   A 1 140 ? 17.646  21.906  24.000 1.00 24.64 ?  140 ASP   A CG  1 
ATOM   1135 O OD1 . ASP   A 1 140 ? 18.670  22.539  23.687 1.00 26.85 ?  140 ASP   A OD1 1 
ATOM   1136 O OD2 . ASP   A 1 140 ? 16.914  22.175  24.958 1.00 28.85 ?  140 ASP   A OD2 1 
ATOM   1137 N N   . PHE   A 1 141 ? 15.355  19.358  21.062 1.00 24.15 ?  141 PHE   A N   1 
ATOM   1138 C CA  . PHE   A 1 141 ? 15.033  18.318  20.091 1.00 23.75 ?  141 PHE   A CA  1 
ATOM   1139 C C   . PHE   A 1 141 ? 14.678  18.927  18.737 1.00 27.02 ?  141 PHE   A C   1 
ATOM   1140 O O   . PHE   A 1 141 ? 15.134  18.453  17.686 1.00 27.91 ?  141 PHE   A O   1 
ATOM   1141 C CB  . PHE   A 1 141 ? 13.886  17.470  20.622 1.00 22.88 ?  141 PHE   A CB  1 
ATOM   1142 C CG  . PHE   A 1 141 ? 13.572  16.294  19.770 1.00 28.22 ?  141 PHE   A CG  1 
ATOM   1143 C CD1 . PHE   A 1 141 ? 12.676  16.402  18.726 1.00 27.71 ?  141 PHE   A CD1 1 
ATOM   1144 C CD2 . PHE   A 1 141 ? 14.190  15.072  20.007 1.00 28.94 ?  141 PHE   A CD2 1 
ATOM   1145 C CE1 . PHE   A 1 141 ? 12.395  15.304  17.922 1.00 26.53 ?  141 PHE   A CE1 1 
ATOM   1146 C CE2 . PHE   A 1 141 ? 13.906  13.976  19.209 1.00 29.40 ?  141 PHE   A CE2 1 
ATOM   1147 C CZ  . PHE   A 1 141 ? 13.013  14.094  18.177 1.00 30.48 ?  141 PHE   A CZ  1 
ATOM   1148 N N   . GLN   A 1 142 ? 13.857  19.974  18.731 1.00 26.44 ?  142 GLN   A N   1 
ATOM   1149 C CA  . GLN   A 1 142 ? 13.400  20.490  17.444 1.00 28.30 ?  142 GLN   A CA  1 
ATOM   1150 C C   . GLN   A 1 142 ? 14.548  21.052  16.621 1.00 28.04 ?  142 GLN   A C   1 
ATOM   1151 O O   . GLN   A 1 142 ? 14.580  20.883  15.395 1.00 30.98 ?  142 GLN   A O   1 
ATOM   1152 C CB  . GLN   A 1 142 ? 12.317  21.535  17.648 1.00 33.35 ?  142 GLN   A CB  1 
ATOM   1153 C CG  . GLN   A 1 142 ? 11.025  20.914  18.097 1.00 33.28 ?  142 GLN   A CG  1 
ATOM   1154 C CD  . GLN   A 1 142 ? 10.027  21.950  18.504 1.00 48.82 ?  142 GLN   A CD  1 
ATOM   1155 O OE1 . GLN   A 1 142 ? 10.072  23.082  18.023 1.00 55.33 ?  142 GLN   A OE1 1 
ATOM   1156 N NE2 . GLN   A 1 142 ? 9.117   21.581  19.402 1.00 53.10 ?  142 GLN   A NE2 1 
ATOM   1157 N N   . LEU   A 1 143 ? 15.499  21.706  17.273 1.00 27.66 ?  143 LEU   A N   1 
ATOM   1158 C CA  . LEU   A 1 143 ? 16.641  22.297  16.601 1.00 30.57 ?  143 LEU   A CA  1 
ATOM   1159 C C   . LEU   A 1 143 ? 17.790  21.313  16.422 1.00 30.45 ?  143 LEU   A C   1 
ATOM   1160 O O   . LEU   A 1 143 ? 18.866  21.716  15.975 1.00 30.92 ?  143 LEU   A O   1 
ATOM   1161 C CB  . LEU   A 1 143 ? 17.117  23.540  17.366 1.00 36.91 ?  143 LEU   A CB  1 
ATOM   1162 C CG  . LEU   A 1 143 ? 16.292  24.820  17.149 1.00 39.47 ?  143 LEU   A CG  1 
ATOM   1163 C CD1 . LEU   A 1 143 ? 15.961  24.967  15.696 1.00 37.70 ?  143 LEU   A CD1 1 
ATOM   1164 C CD2 . LEU   A 1 143 ? 15.014  24.874  17.966 1.00 49.18 ?  143 LEU   A CD2 1 
ATOM   1165 N N   . TYR   A 1 144 ? 17.581  20.034  16.736 1.00 28.93 ?  144 TYR   A N   1 
ATOM   1166 C CA  . TYR   A 1 144 ? 18.642  19.041  16.582 1.00 28.62 ?  144 TYR   A CA  1 
ATOM   1167 C C   . TYR   A 1 144 ? 19.171  19.020  15.155 1.00 29.20 ?  144 TYR   A C   1 
ATOM   1168 O O   . TYR   A 1 144 ? 18.410  18.905  14.194 1.00 29.44 ?  144 TYR   A O   1 
ATOM   1169 C CB  . TYR   A 1 144 ? 18.128  17.656  16.973 1.00 29.94 ?  144 TYR   A CB  1 
ATOM   1170 C CG  . TYR   A 1 144 ? 19.056  16.503  16.647 1.00 25.83 ?  144 TYR   A CG  1 
ATOM   1171 C CD1 . TYR   A 1 144 ? 20.125  16.185  17.482 1.00 24.87 ?  144 TYR   A CD1 1 
ATOM   1172 C CD2 . TYR   A 1 144 ? 18.831  15.700  15.526 1.00 25.36 ?  144 TYR   A CD2 1 
ATOM   1173 C CE1 . TYR   A 1 144 ? 20.955  15.127  17.193 1.00 27.06 ?  144 TYR   A CE1 1 
ATOM   1174 C CE2 . TYR   A 1 144 ? 19.655  14.647  15.224 1.00 23.45 ?  144 TYR   A CE2 1 
ATOM   1175 C CZ  . TYR   A 1 144 ? 20.710  14.354  16.065 1.00 28.56 ?  144 TYR   A CZ  1 
ATOM   1176 O OH  . TYR   A 1 144 ? 21.522  13.295  15.787 1.00 26.45 ?  144 TYR   A OH  1 
ATOM   1177 N N   . ARG   A 1 145 ? 20.483  19.127  15.011 1.00 27.12 ?  145 ARG   A N   1 
ATOM   1178 C CA  . ARG   A 1 145 ? 21.063  19.056  13.681 1.00 31.76 ?  145 ARG   A CA  1 
ATOM   1179 C C   . ARG   A 1 145 ? 22.067  17.926  13.525 1.00 32.47 ?  145 ARG   A C   1 
ATOM   1180 O O   . ARG   A 1 145 ? 22.584  17.729  12.421 1.00 37.66 ?  145 ARG   A O   1 
ATOM   1181 C CB  . ARG   A 1 145 ? 21.715  20.396  13.300 1.00 43.01 ?  145 ARG   A CB  1 
ATOM   1182 C CG  . ARG   A 1 145 ? 23.001  20.734  14.037 1.00 55.71 ?  145 ARG   A CG  1 
ATOM   1183 C CD  . ARG   A 1 145 ? 23.129  22.235  14.358 1.00 63.62 ?  145 ARG   A CD  1 
ATOM   1184 N NE  . ARG   A 1 145 ? 22.592  22.570  15.674 1.00 77.34 ?  145 ARG   A NE  1 
ATOM   1185 C CZ  . ARG   A 1 145 ? 21.480  23.264  15.889 1.00 72.19 ?  145 ARG   A CZ  1 
ATOM   1186 N NH1 . ARG   A 1 145 ? 20.775  23.774  14.888 1.00 70.10 ?  145 ARG   A NH1 1 
ATOM   1187 N NH2 . ARG   A 1 145 ? 21.066  23.453  17.141 1.00 61.06 ?  145 ARG   A NH2 1 
ATOM   1188 N N   . GLY   A 1 146 ? 22.348  17.176  14.577 1.00 33.26 ?  146 GLY   A N   1 
ATOM   1189 C CA  . GLY   A 1 146 ? 23.256  16.050  14.468 1.00 27.57 ?  146 GLY   A CA  1 
ATOM   1190 C C   . GLY   A 1 146 ? 23.997  15.822  15.765 1.00 29.90 ?  146 GLY   A C   1 
ATOM   1191 O O   . GLY   A 1 146 ? 23.984  16.644  16.678 1.00 31.65 ?  146 GLY   A O   1 
ATOM   1192 N N   . GLY   A 1 147 ? 24.681  14.689  15.818 1.00 30.67 ?  147 GLY   A N   1 
ATOM   1193 C CA  . GLY   A 1 147 ? 25.348  14.278  17.031 1.00 30.74 ?  147 GLY   A CA  1 
ATOM   1194 C C   . GLY   A 1 147 ? 24.490  13.334  17.842 1.00 33.76 ?  147 GLY   A C   1 
ATOM   1195 O O   . GLY   A 1 147 ? 23.347  13.000  17.502 1.00 31.03 ?  147 GLY   A O   1 
ATOM   1196 N N   . ILE   A 1 148 ? 25.069  12.863  18.938 1.00 26.07 ?  148 ILE   A N   1 
ATOM   1197 C CA  . ILE   A 1 148 ? 24.318  12.031  19.862 1.00 29.03 ?  148 ILE   A CA  1 
ATOM   1198 C C   . ILE   A 1 148 ? 23.539  12.959  20.776 1.00 31.05 ?  148 ILE   A C   1 
ATOM   1199 O O   . ILE   A 1 148 ? 24.116  13.792  21.482 1.00 30.00 ?  148 ILE   A O   1 
ATOM   1200 C CB  . ILE   A 1 148 ? 25.239  11.099  20.649 1.00 27.35 ?  148 ILE   A CB  1 
ATOM   1201 C CG1 . ILE   A 1 148 ? 25.765  10.028  19.694 1.00 35.11 ?  148 ILE   A CG1 1 
ATOM   1202 C CG2 . ILE   A 1 148 ? 24.467  10.451  21.774 1.00 29.03 ?  148 ILE   A CG2 1 
ATOM   1203 C CD1 . ILE   A 1 148 ? 26.326  8.868   20.381 1.00 39.23 ?  148 ILE   A CD1 1 
ATOM   1204 N N   . PHE   A 1 149 ? 22.226  12.847  20.734 1.00 25.21 ?  149 PHE   A N   1 
ATOM   1205 C CA  . PHE   A 1 149 ? 21.376  13.783  21.438 1.00 24.06 ?  149 PHE   A CA  1 
ATOM   1206 C C   . PHE   A 1 149 ? 21.167  13.293  22.862 1.00 24.42 ?  149 PHE   A C   1 
ATOM   1207 O O   . PHE   A 1 149 ? 20.757  12.152  23.084 1.00 28.52 ?  149 PHE   A O   1 
ATOM   1208 C CB  . PHE   A 1 149 ? 20.059  13.959  20.694 1.00 25.35 ?  149 PHE   A CB  1 
ATOM   1209 C CG  . PHE   A 1 149 ? 19.162  14.965  21.314 1.00 24.52 ?  149 PHE   A CG  1 
ATOM   1210 C CD1 . PHE   A 1 149 ? 19.415  16.321  21.162 1.00 23.49 ?  149 PHE   A CD1 1 
ATOM   1211 C CD2 . PHE   A 1 149 ? 18.059  14.563  22.029 1.00 22.71 ?  149 PHE   A CD2 1 
ATOM   1212 C CE1 . PHE   A 1 149 ? 18.576  17.255  21.729 1.00 29.05 ?  149 PHE   A CE1 1 
ATOM   1213 C CE2 . PHE   A 1 149 ? 17.206  15.499  22.595 1.00 25.72 ?  149 PHE   A CE2 1 
ATOM   1214 C CZ  . PHE   A 1 149 ? 17.462  16.837  22.440 1.00 28.37 ?  149 PHE   A CZ  1 
ATOM   1215 N N   . VAL   A 1 150 ? 21.511  14.143  23.826 1.00 24.96 ?  150 VAL   A N   1 
ATOM   1216 C CA  . VAL   A 1 150 ? 21.372  13.833  25.243 1.00 28.39 ?  150 VAL   A CA  1 
ATOM   1217 C C   . VAL   A 1 150 ? 20.261  14.632  25.883 1.00 33.95 ?  150 VAL   A C   1 
ATOM   1218 O O   . VAL   A 1 150 ? 20.037  14.519  27.097 1.00 33.77 ?  150 VAL   A O   1 
ATOM   1219 C CB  . VAL   A 1 150 ? 22.698  14.070  25.994 1.00 28.50 ?  150 VAL   A CB  1 
ATOM   1220 C CG1 . VAL   A 1 150 ? 23.809  13.213  25.390 1.00 29.89 ?  150 VAL   A CG1 1 
ATOM   1221 C CG2 . VAL   A 1 150 ? 23.089  15.548  25.949 1.00 28.93 ?  150 VAL   A CG2 1 
ATOM   1222 N N   . GLY   A 1 151 ? 19.550  15.428  25.107 1.00 26.74 ?  151 GLY   A N   1 
ATOM   1223 C CA  . GLY   A 1 151 ? 18.632  16.374  25.669 1.00 27.92 ?  151 GLY   A CA  1 
ATOM   1224 C C   . GLY   A 1 151 ? 19.220  17.765  25.595 1.00 27.98 ?  151 GLY   A C   1 
ATOM   1225 O O   . GLY   A 1 151 ? 20.097  18.055  24.772 1.00 30.55 ?  151 GLY   A O   1 
ATOM   1226 N N   . PRO   A 1 152 ? 18.756  18.654  26.464 1.00 27.00 ?  152 PRO   A N   1 
ATOM   1227 C CA  . PRO   A 1 152 ? 17.767  18.409  27.520 1.00 26.36 ?  152 PRO   A CA  1 
ATOM   1228 C C   . PRO   A 1 152 ? 16.388  18.123  26.981 1.00 29.11 ?  152 PRO   A C   1 
ATOM   1229 O O   . PRO   A 1 152 ? 15.977  18.585  25.909 1.00 28.99 ?  152 PRO   A O   1 
ATOM   1230 C CB  . PRO   A 1 152 ? 17.794  19.699  28.355 1.00 29.76 ?  152 PRO   A CB  1 
ATOM   1231 C CG  . PRO   A 1 152 ? 18.794  20.604  27.770 1.00 28.40 ?  152 PRO   A CG  1 
ATOM   1232 C CD  . PRO   A 1 152 ? 19.310  20.016  26.491 1.00 28.36 ?  152 PRO   A CD  1 
ATOM   1233 N N   . CYS   A 1 153 ? 15.684  17.292  27.735 1.00 27.35 ?  153 CYS   A N   1 
ATOM   1234 C CA  . CYS   A 1 153 ? 14.300  16.968  27.463 1.00 32.16 ?  153 CYS   A CA  1 
ATOM   1235 C C   . CYS   A 1 153 ? 13.747  16.267  28.687 1.00 31.62 ?  153 CYS   A C   1 
ATOM   1236 O O   . CYS   A 1 153 ? 14.493  15.656  29.456 1.00 32.29 ?  153 CYS   A O   1 
ATOM   1237 C CB  . CYS   A 1 153 ? 14.179  16.081  26.224 1.00 29.01 ?  153 CYS   A CB  1 
ATOM   1238 S SG  . CYS   A 1 153 ? 15.242  14.638  26.384 1.00 31.51 ?  153 CYS   A SG  1 
ATOM   1239 N N   . GLY   A 1 154 ? 12.443  16.392  28.873 1.00 35.30 ?  154 GLY   A N   1 
ATOM   1240 C CA  . GLY   A 1 154 ? 11.738  15.673  29.906 1.00 37.92 ?  154 GLY   A CA  1 
ATOM   1241 C C   . GLY   A 1 154 ? 11.217  14.364  29.357 1.00 34.97 ?  154 GLY   A C   1 
ATOM   1242 O O   . GLY   A 1 154 ? 11.622  13.899  28.291 1.00 34.17 ?  154 GLY   A O   1 
ATOM   1243 N N   A ASN   A 1 155 ? 10.299  13.758  30.108 0.50 33.47 ?  155 ASN   A N   1 
ATOM   1244 N N   B ASN   A 1 155 ? 10.283  13.770  30.101 0.50 33.47 ?  155 ASN   A N   1 
ATOM   1245 C CA  A ASN   A 1 155 ? 9.666   12.508  29.710 0.50 34.17 ?  155 ASN   A CA  1 
ATOM   1246 C CA  B ASN   A 1 155 ? 9.660   12.507  29.732 0.50 34.17 ?  155 ASN   A CA  1 
ATOM   1247 C C   A ASN   A 1 155 ? 8.197   12.692  29.338 0.50 35.21 ?  155 ASN   A C   1 
ATOM   1248 C C   B ASN   A 1 155 ? 8.202   12.687  29.316 0.50 35.21 ?  155 ASN   A C   1 
ATOM   1249 O O   A ASN   A 1 155 ? 7.430   11.723  29.355 0.50 35.02 ?  155 ASN   A O   1 
ATOM   1250 O O   B ASN   A 1 155 ? 7.444   11.711  29.284 0.50 35.02 ?  155 ASN   A O   1 
ATOM   1251 C CB  A ASN   A 1 155 ? 9.826   11.455  30.814 0.50 37.51 ?  155 ASN   A CB  1 
ATOM   1252 C CB  B ASN   A 1 155 ? 9.761   11.504  30.885 0.50 37.53 ?  155 ASN   A CB  1 
ATOM   1253 C CG  A ASN   A 1 155 ? 9.044   11.793  32.072 0.50 37.42 ?  155 ASN   A CG  1 
ATOM   1254 C CG  B ASN   A 1 155 ? 11.185  11.318  31.379 0.50 36.68 ?  155 ASN   A CG  1 
ATOM   1255 O OD1 A ASN   A 1 155 ? 8.454   12.863  32.181 0.50 37.95 ?  155 ASN   A OD1 1 
ATOM   1256 O OD1 B ASN   A 1 155 ? 12.115  11.154  30.592 0.50 38.84 ?  155 ASN   A OD1 1 
ATOM   1257 N ND2 A ASN   A 1 155 ? 9.014   10.862  33.016 0.50 39.76 ?  155 ASN   A ND2 1 
ATOM   1258 N ND2 B ASN   A 1 155 ? 11.357  11.328  32.694 0.50 42.65 ?  155 ASN   A ND2 1 
ATOM   1259 N N   . LYS   A 1 156 ? 7.791   13.920  29.008 1.00 27.08 ?  156 LYS   A N   1 
ATOM   1260 C CA  . LYS   A 1 156 ? 6.428   14.198  28.536 1.00 34.40 ?  156 LYS   A CA  1 
ATOM   1261 C C   . LYS   A 1 156 ? 6.304   13.799  27.064 1.00 26.02 ?  156 LYS   A C   1 
ATOM   1262 O O   . LYS   A 1 156 ? 6.218   14.636  26.156 1.00 31.73 ?  156 LYS   A O   1 
ATOM   1263 C CB  . LYS   A 1 156 ? 6.054   15.664  28.720 1.00 31.08 ?  156 LYS   A CB  1 
ATOM   1264 C CG  . LYS   A 1 156 ? 6.416   16.322  30.050 1.00 45.44 ?  156 LYS   A CG  1 
ATOM   1265 C CD  . LYS   A 1 156 ? 6.129   15.407  31.233 1.00 50.21 ?  156 LYS   A CD  1 
ATOM   1266 C CE  . LYS   A 1 156 ? 6.858   15.884  32.492 1.00 63.80 ?  156 LYS   A CE  1 
ATOM   1267 N NZ  . LYS   A 1 156 ? 6.854   14.861  33.580 1.00 59.79 ?  156 LYS   A NZ  1 
ATOM   1268 N N   . VAL   A 1 157 ? 6.261   12.484  26.842 1.00 29.37 ?  157 VAL   A N   1 
ATOM   1269 C CA  . VAL   A 1 157 ? 6.331   11.967  25.481 1.00 28.43 ?  157 VAL   A CA  1 
ATOM   1270 C C   . VAL   A 1 157 ? 5.135   12.454  24.681 1.00 30.66 ?  157 VAL   A C   1 
ATOM   1271 O O   . VAL   A 1 157 ? 4.002   12.520  25.176 1.00 28.97 ?  157 VAL   A O   1 
ATOM   1272 C CB  . VAL   A 1 157 ? 6.447   10.434  25.490 1.00 31.77 ?  157 VAL   A CB  1 
ATOM   1273 C CG1 . VAL   A 1 157 ? 7.733   10.016  26.213 1.00 28.62 ?  157 VAL   A CG1 1 
ATOM   1274 C CG2 . VAL   A 1 157 ? 5.240   9.807   26.164 1.00 31.84 ?  157 VAL   A CG2 1 
ATOM   1275 N N   . ASP   A 1 158 ? 5.403   12.841  23.432 1.00 26.40 ?  158 ASP   A N   1 
ATOM   1276 C CA  . ASP   A 1 158 ? 4.392   13.498  22.610 1.00 26.82 ?  158 ASP   A CA  1 
ATOM   1277 C C   . ASP   A 1 158 ? 4.575   13.191  21.130 1.00 29.35 ?  158 ASP   A C   1 
ATOM   1278 O O   . ASP   A 1 158 ? 3.837   13.741  20.299 1.00 28.09 ?  158 ASP   A O   1 
ATOM   1279 C CB  . ASP   A 1 158 ? 4.446   15.008  22.886 1.00 21.58 ?  158 ASP   A CB  1 
ATOM   1280 C CG  . ASP   A 1 158 ? 5.749   15.625  22.468 1.00 32.20 ?  158 ASP   A CG  1 
ATOM   1281 O OD1 . ASP   A 1 158 ? 6.634   14.911  21.936 1.00 29.80 ?  158 ASP   A OD1 1 
ATOM   1282 O OD2 . ASP   A 1 158 ? 5.944   16.818  22.767 1.00 38.69 ?  158 ASP   A OD2 1 
ATOM   1283 N N   . HIS   A 1 159 ? 5.508   12.321  20.769 1.00 21.98 ?  159 HIS   A N   1 
ATOM   1284 C CA  . HIS   A 1 159 ? 5.903   12.188  19.371 1.00 21.11 ?  159 HIS   A CA  1 
ATOM   1285 C C   . HIS   A 1 159 ? 6.342   10.756  19.146 1.00 26.62 ?  159 HIS   A C   1 
ATOM   1286 O O   . HIS   A 1 159 ? 7.243   10.274  19.838 1.00 29.01 ?  159 HIS   A O   1 
ATOM   1287 C CB  . HIS   A 1 159 ? 7.036   13.139  19.041 1.00 21.57 ?  159 HIS   A CB  1 
ATOM   1288 C CG  . HIS   A 1 159 ? 7.414   13.146  17.591 1.00 22.09 ?  159 HIS   A CG  1 
ATOM   1289 N ND1 . HIS   A 1 159 ? 6.504   13.416  16.594 1.00 27.13 ?  159 HIS   A ND1 1 
ATOM   1290 C CD2 . HIS   A 1 159 ? 8.605   12.964  16.976 1.00 24.68 ?  159 HIS   A CD2 1 
ATOM   1291 C CE1 . HIS   A 1 159 ? 7.116   13.386  15.420 1.00 26.52 ?  159 HIS   A CE1 1 
ATOM   1292 N NE2 . HIS   A 1 159 ? 8.394   13.124  15.625 1.00 22.59 ?  159 HIS   A NE2 1 
ATOM   1293 N N   . ALA   A 1 160 ? 5.703   10.085  18.200 1.00 21.86 ?  160 ALA   A N   1 
ATOM   1294 C CA  . ALA   A 1 160 ? 6.049   8.717   17.859 1.00 22.93 ?  160 ALA   A CA  1 
ATOM   1295 C C   . ALA   A 1 160 ? 7.042   8.734   16.711 1.00 20.75 ?  160 ALA   A C   1 
ATOM   1296 O O   . ALA   A 1 160 ? 6.848   9.451   15.727 1.00 24.68 ?  160 ALA   A O   1 
ATOM   1297 C CB  . ALA   A 1 160 ? 4.805   7.927   17.461 1.00 25.10 ?  160 ALA   A CB  1 
ATOM   1298 N N   . VAL   A 1 161 ? 8.091   7.938   16.835 1.00 20.38 ?  161 VAL   A N   1 
ATOM   1299 C CA  . VAL   A 1 161 ? 9.103   7.810   15.795 1.00 22.41 ?  161 VAL   A CA  1 
ATOM   1300 C C   . VAL   A 1 161 ? 9.381   6.319   15.698 1.00 20.69 ?  161 VAL   A C   1 
ATOM   1301 O O   . VAL   A 1 161 ? 8.638   5.511   16.259 1.00 22.84 ?  161 VAL   A O   1 
ATOM   1302 C CB  . VAL   A 1 161 ? 10.362  8.626   16.136 1.00 25.72 ?  161 VAL   A CB  1 
ATOM   1303 C CG1 . VAL   A 1 161 ? 10.093  10.108  15.961 1.00 22.66 ?  161 VAL   A CG1 1 
ATOM   1304 C CG2 . VAL   A 1 161 ? 10.774  8.359   17.573 1.00 25.68 ?  161 VAL   A CG2 1 
ATOM   1305 N N   . ALA   A 1 162 ? 10.429  5.935   14.990 1.00 22.69 ?  162 ALA   A N   1 
ATOM   1306 C CA  . ALA   A 1 162 ? 10.746  4.532   14.833 1.00 26.46 ?  162 ALA   A CA  1 
ATOM   1307 C C   . ALA   A 1 162 ? 12.225  4.360   15.104 1.00 24.90 ?  162 ALA   A C   1 
ATOM   1308 O O   . ALA   A 1 162 ? 13.049  5.099   14.561 1.00 24.77 ?  162 ALA   A O   1 
ATOM   1309 C CB  . ALA   A 1 162 ? 10.392  4.025   13.431 1.00 25.30 ?  162 ALA   A CB  1 
ATOM   1310 N N   . ALA   A 1 163 ? 12.552  3.410   15.964 1.00 22.19 ?  163 ALA   A N   1 
ATOM   1311 C CA  . ALA   A 1 163 ? 13.939  3.059   16.205 1.00 27.29 ?  163 ALA   A CA  1 
ATOM   1312 C C   . ALA   A 1 163 ? 14.340  2.044   15.162 1.00 27.23 ?  163 ALA   A C   1 
ATOM   1313 O O   . ALA   A 1 163 ? 13.716  0.985   15.062 1.00 25.25 ?  163 ALA   A O   1 
ATOM   1314 C CB  . ALA   A 1 163 ? 14.115  2.489   17.609 1.00 27.06 ?  163 ALA   A CB  1 
ATOM   1315 N N   . VAL   A 1 164 ? 15.349  2.382   14.365 1.00 21.60 ?  164 VAL   A N   1 
ATOM   1316 C CA  . VAL   A 1 164 ? 15.802  1.535   13.277 1.00 22.28 ?  164 VAL   A CA  1 
ATOM   1317 C C   . VAL   A 1 164 ? 17.235  1.078   13.497 1.00 23.13 ?  164 VAL   A C   1 
ATOM   1318 O O   . VAL   A 1 164 ? 17.845  0.506   12.603 1.00 27.12 ?  164 VAL   A O   1 
ATOM   1319 C CB  . VAL   A 1 164 ? 15.654  2.245   11.918 1.00 23.24 ?  164 VAL   A CB  1 
ATOM   1320 C CG1 . VAL   A 1 164 ? 14.187  2.540   11.622 1.00 27.35 ?  164 VAL   A CG1 1 
ATOM   1321 C CG2 . VAL   A 1 164 ? 16.513  3.494   11.874 1.00 25.46 ?  164 VAL   A CG2 1 
ATOM   1322 N N   . GLY   A 1 165 ? 17.789  1.332   14.675 1.00 23.69 ?  165 GLY   A N   1 
ATOM   1323 C CA  . GLY   A 1 165 ? 19.138  0.883   14.935 1.00 25.24 ?  165 GLY   A CA  1 
ATOM   1324 C C   . GLY   A 1 165 ? 19.584  1.341   16.304 1.00 21.03 ?  165 GLY   A C   1 
ATOM   1325 O O   . GLY   A 1 165 ? 18.839  1.982   17.049 1.00 21.73 ?  165 GLY   A O   1 
ATOM   1326 N N   . TYR   A 1 166 ? 20.823  0.995   16.619 1.00 23.68 ?  166 TYR   A N   1 
ATOM   1327 C CA  . TYR   A 1 166 ? 21.447  1.441   17.851 1.00 23.13 ?  166 TYR   A CA  1 
ATOM   1328 C C   . TYR   A 1 166 ? 22.936  1.192   17.725 1.00 24.15 ?  166 TYR   A C   1 
ATOM   1329 O O   . TYR   A 1 166 ? 23.403  0.471   16.833 1.00 27.01 ?  166 TYR   A O   1 
ATOM   1330 C CB  . TYR   A 1 166 ? 20.883  0.737   19.088 1.00 22.44 ?  166 TYR   A CB  1 
ATOM   1331 C CG  . TYR   A 1 166 ? 21.146  -0.747  19.115 1.00 23.56 ?  166 TYR   A CG  1 
ATOM   1332 C CD1 . TYR   A 1 166 ? 22.394  -1.250  19.514 1.00 26.72 ?  166 TYR   A CD1 1 
ATOM   1333 C CD2 . TYR   A 1 166 ? 20.142  -1.652  18.782 1.00 26.25 ?  166 TYR   A CD2 1 
ATOM   1334 C CE1 . TYR   A 1 166 ? 22.646  -2.610  19.531 1.00 27.72 ?  166 TYR   A CE1 1 
ATOM   1335 C CE2 . TYR   A 1 166 ? 20.379  -3.029  18.811 1.00 27.46 ?  166 TYR   A CE2 1 
ATOM   1336 C CZ  . TYR   A 1 166 ? 21.636  -3.494  19.184 1.00 28.07 ?  166 TYR   A CZ  1 
ATOM   1337 O OH  . TYR   A 1 166 ? 21.905  -4.844  19.217 1.00 27.56 ?  166 TYR   A OH  1 
ATOM   1338 N N   . GLY   A 1 167 ? 23.667  1.796   18.639 1.00 25.69 ?  167 GLY   A N   1 
ATOM   1339 C CA  . GLY   A 1 167 ? 25.078  1.570   18.775 1.00 24.43 ?  167 GLY   A CA  1 
ATOM   1340 C C   . GLY   A 1 167 ? 25.380  1.560   20.248 1.00 24.54 ?  167 GLY   A C   1 
ATOM   1341 O O   . GLY   A 1 167 ? 24.472  1.564   21.089 1.00 28.87 ?  167 GLY   A O   1 
ATOM   1342 N N   . PRO   A 1 168 ? 26.664  1.522   20.593 1.00 27.21 ?  168 PRO   A N   1 
ATOM   1343 C CA  . PRO   A 1 168 ? 27.045  1.487   22.012 1.00 29.26 ?  168 PRO   A CA  1 
ATOM   1344 C C   . PRO   A 1 168 ? 26.444  2.600   22.842 1.00 30.26 ?  168 PRO   A C   1 
ATOM   1345 O O   . PRO   A 1 168 ? 26.104  2.386   24.010 1.00 32.93 ?  168 PRO   A O   1 
ATOM   1346 C CB  . PRO   A 1 168 ? 28.577  1.615   21.956 1.00 35.52 ?  168 PRO   A CB  1 
ATOM   1347 C CG  . PRO   A 1 168 ? 28.974  1.171   20.597 1.00 34.69 ?  168 PRO   A CG  1 
ATOM   1348 C CD  . PRO   A 1 168 ? 27.755  1.091   19.709 1.00 28.68 ?  168 PRO   A CD  1 
ATOM   1349 N N   A ASN   A 1 169 ? 26.299  3.794   22.264 0.59 29.09 ?  169 ASN   A N   1 
ATOM   1350 N N   B ASN   A 1 169 ? 26.300  3.802   22.290 0.41 29.16 ?  169 ASN   A N   1 
ATOM   1351 C CA  A ASN   A 1 169 ? 25.929  4.969   23.043 0.59 31.55 ?  169 ASN   A CA  1 
ATOM   1352 C CA  B ASN   A 1 169 ? 25.884  4.939   23.105 0.41 31.51 ?  169 ASN   A CA  1 
ATOM   1353 C C   A ASN   A 1 169 ? 24.688  5.670   22.494 0.59 26.69 ?  169 ASN   A C   1 
ATOM   1354 C C   B ASN   A 1 169 ? 24.604  5.601   22.611 0.41 26.80 ?  169 ASN   A C   1 
ATOM   1355 O O   A ASN   A 1 169 ? 24.416  6.815   22.859 0.59 28.18 ?  169 ASN   A O   1 
ATOM   1356 O O   B ASN   A 1 169 ? 24.231  6.660   23.125 0.41 27.65 ?  169 ASN   A O   1 
ATOM   1357 C CB  A ASN   A 1 169 ? 27.122  5.933   23.129 0.59 35.31 ?  169 ASN   A CB  1 
ATOM   1358 C CB  B ASN   A 1 169 ? 27.016  5.969   23.182 0.41 35.31 ?  169 ASN   A CB  1 
ATOM   1359 C CG  A ASN   A 1 169 ? 27.787  6.197   21.774 0.59 37.03 ?  169 ASN   A CG  1 
ATOM   1360 C CG  B ASN   A 1 169 ? 28.170  5.493   24.034 0.41 34.33 ?  169 ASN   A CG  1 
ATOM   1361 O OD1 A ASN   A 1 169 ? 27.623  5.443   20.801 0.59 34.61 ?  169 ASN   A OD1 1 
ATOM   1362 O OD1 B ASN   A 1 169 ? 28.000  4.644   24.905 0.41 41.40 ?  169 ASN   A OD1 1 
ATOM   1363 N ND2 A ASN   A 1 169 ? 28.592  7.259   21.726 0.59 40.46 ?  169 ASN   A ND2 1 
ATOM   1364 N ND2 B ASN   A 1 169 ? 29.353  6.032   23.783 0.41 43.86 ?  169 ASN   A ND2 1 
ATOM   1365 N N   . TYR   A 1 170 ? 23.904  5.002   21.654 1.00 23.98 ?  170 TYR   A N   1 
ATOM   1366 C CA  . TYR   A 1 170 ? 22.772  5.684   21.053 1.00 25.08 ?  170 TYR   A CA  1 
ATOM   1367 C C   . TYR   A 1 170 ? 21.767  4.691   20.516 1.00 23.87 ?  170 TYR   A C   1 
ATOM   1368 O O   . TYR   A 1 170 ? 22.078  3.532   20.239 1.00 25.90 ?  170 TYR   A O   1 
ATOM   1369 C CB  . TYR   A 1 170 ? 23.209  6.603   19.910 1.00 25.62 ?  170 TYR   A CB  1 
ATOM   1370 C CG  . TYR   A 1 170 ? 23.795  5.862   18.731 1.00 25.57 ?  170 TYR   A CG  1 
ATOM   1371 C CD1 . TYR   A 1 170 ? 22.993  5.380   17.680 1.00 23.69 ?  170 TYR   A CD1 1 
ATOM   1372 C CD2 . TYR   A 1 170 ? 25.161  5.625   18.675 1.00 33.66 ?  170 TYR   A CD2 1 
ATOM   1373 C CE1 . TYR   A 1 170 ? 23.558  4.696   16.616 1.00 24.66 ?  170 TYR   A CE1 1 
ATOM   1374 C CE2 . TYR   A 1 170 ? 25.724  4.947   17.623 1.00 32.86 ?  170 TYR   A CE2 1 
ATOM   1375 C CZ  . TYR   A 1 170 ? 24.921  4.483   16.601 1.00 31.02 ?  170 TYR   A CZ  1 
ATOM   1376 O OH  . TYR   A 1 170 ? 25.511  3.818   15.561 1.00 28.32 ?  170 TYR   A OH  1 
ATOM   1377 N N   . ILE   A 1 171 ? 20.544  5.175   20.389 1.00 25.34 ?  171 ILE   A N   1 
ATOM   1378 C CA  . ILE   A 1 171 ? 19.510  4.506   19.628 1.00 22.25 ?  171 ILE   A CA  1 
ATOM   1379 C C   . ILE   A 1 171 ? 19.263  5.354   18.388 1.00 26.93 ?  171 ILE   A C   1 
ATOM   1380 O O   . ILE   A 1 171 ? 19.204  6.586   18.475 1.00 23.17 ?  171 ILE   A O   1 
ATOM   1381 C CB  . ILE   A 1 171 ? 18.251  4.306   20.484 1.00 23.54 ?  171 ILE   A CB  1 
ATOM   1382 C CG1 . ILE   A 1 171 ? 18.540  3.207   21.512 1.00 26.75 ?  171 ILE   A CG1 1 
ATOM   1383 C CG2 . ILE   A 1 171 ? 17.078  3.881   19.604 1.00 25.22 ?  171 ILE   A CG2 1 
ATOM   1384 C CD1 . ILE   A 1 171 ? 17.579  3.163   22.654 1.00 34.40 ?  171 ILE   A CD1 1 
ATOM   1385 N N   . LEU   A 1 172 ? 19.209  4.703   17.225 1.00 22.72 ?  172 LEU   A N   1 
ATOM   1386 C CA  . LEU   A 1 172 ? 19.077  5.391   15.950 1.00 22.92 ?  172 LEU   A CA  1 
ATOM   1387 C C   . LEU   A 1 172 ? 17.604  5.488   15.596 1.00 21.47 ?  172 LEU   A C   1 
ATOM   1388 O O   . LEU   A 1 172 ? 16.909  4.467   15.538 1.00 24.08 ?  172 LEU   A O   1 
ATOM   1389 C CB  . LEU   A 1 172 ? 19.839  4.650   14.857 1.00 26.39 ?  172 LEU   A CB  1 
ATOM   1390 C CG  . LEU   A 1 172 ? 19.596  5.209   13.466 1.00 27.43 ?  172 LEU   A CG  1 
ATOM   1391 C CD1 . LEU   A 1 172 ? 20.250  6.548   13.393 1.00 20.66 ?  172 LEU   A CD1 1 
ATOM   1392 C CD2 . LEU   A 1 172 ? 20.168  4.252   12.397 1.00 30.29 ?  172 LEU   A CD2 1 
ATOM   1393 N N   . ILE   A 1 173 ? 17.130  6.706   15.353 1.00 20.97 ?  173 ILE   A N   1 
ATOM   1394 C CA  . ILE   A 1 173 ? 15.704  6.979   15.233 1.00 21.44 ?  173 ILE   A CA  1 
ATOM   1395 C C   . ILE   A 1 173 ? 15.429  7.615   13.883 1.00 22.48 ?  173 ILE   A C   1 
ATOM   1396 O O   . ILE   A 1 173 ? 16.064  8.609   13.524 1.00 24.60 ?  173 ILE   A O   1 
ATOM   1397 C CB  . ILE   A 1 173 ? 15.223  7.918   16.350 1.00 25.72 ?  173 ILE   A CB  1 
ATOM   1398 C CG1 . ILE   A 1 173 ? 15.319  7.272   17.741 1.00 31.18 ?  173 ILE   A CG1 1 
ATOM   1399 C CG2 . ILE   A 1 173 ? 13.833  8.410   16.046 1.00 23.16 ?  173 ILE   A CG2 1 
ATOM   1400 C CD1 . ILE   A 1 173 ? 14.535  6.005   17.859 1.00 29.79 ?  173 ILE   A CD1 1 
ATOM   1401 N N   . LYS   A 1 174 ? 14.461  7.061   13.160 1.00 19.24 ?  174 LYS   A N   1 
ATOM   1402 C CA  . LYS   A 1 174 ? 13.905  7.680   11.962 1.00 16.88 ?  174 LYS   A CA  1 
ATOM   1403 C C   . LYS   A 1 174 ? 12.793  8.621   12.385 1.00 21.41 ?  174 LYS   A C   1 
ATOM   1404 O O   . LYS   A 1 174 ? 11.791  8.186   12.962 1.00 21.29 ?  174 LYS   A O   1 
ATOM   1405 C CB  . LYS   A 1 174 ? 13.357  6.618   11.008 1.00 23.44 ?  174 LYS   A CB  1 
ATOM   1406 C CG  . LYS   A 1 174 ? 12.961  7.149   9.623  1.00 22.63 ?  174 LYS   A CG  1 
ATOM   1407 C CD  . LYS   A 1 174 ? 12.291  6.067   8.799  1.00 19.84 ?  174 LYS   A CD  1 
ATOM   1408 C CE  . LYS   A 1 174 ? 12.123  6.488   7.349  1.00 22.67 ?  174 LYS   A CE  1 
ATOM   1409 N NZ  . LYS   A 1 174 ? 11.410  5.429   6.547  1.00 22.12 ?  174 LYS   A NZ  1 
ATOM   1410 N N   . ASN   A 1 175 ? 12.974  9.902   12.125 1.00 22.51 ?  175 ASN   A N   1 
ATOM   1411 C CA  . ASN   A 1 175 ? 11.923  10.865  12.381 1.00 21.66 ?  175 ASN   A CA  1 
ATOM   1412 C C   . ASN   A 1 175 ? 11.141  11.105  11.095 1.00 24.55 ?  175 ASN   A C   1 
ATOM   1413 O O   . ASN   A 1 175 ? 11.536  10.672  10.012 1.00 22.04 ?  175 ASN   A O   1 
ATOM   1414 C CB  . ASN   A 1 175 ? 12.519  12.167  12.930 1.00 21.10 ?  175 ASN   A CB  1 
ATOM   1415 C CG  . ASN   A 1 175 ? 11.504  12.997  13.700 1.00 24.08 ?  175 ASN   A CG  1 
ATOM   1416 O OD1 . ASN   A 1 175 ? 10.343  12.613  13.835 1.00 25.13 ?  175 ASN   A OD1 1 
ATOM   1417 N ND2 . ASN   A 1 175 ? 11.941  14.133  14.213 1.00 23.16 ?  175 ASN   A ND2 1 
ATOM   1418 N N   . SER   A 1 176 ? 10.019  11.804  11.224 1.00 22.70 ?  176 SER   A N   1 
ATOM   1419 C CA  . SER   A 1 176 ? 9.136   12.078  10.095 1.00 19.18 ?  176 SER   A CA  1 
ATOM   1420 C C   . SER   A 1 176 ? 9.065   13.561  9.838  1.00 22.09 ?  176 SER   A C   1 
ATOM   1421 O O   . SER   A 1 176 ? 8.001   14.108  9.528  1.00 24.46 ?  176 SER   A O   1 
ATOM   1422 C CB  . SER   A 1 176 ? 7.741   11.534  10.349 1.00 21.57 ?  176 SER   A CB  1 
ATOM   1423 O OG  . SER   A 1 176 ? 7.349   11.929  11.650 1.00 22.50 ?  176 SER   A OG  1 
ATOM   1424 N N   . TRP   A 1 177 ? 10.201  14.238  9.969  1.00 18.59 ?  177 TRP   A N   1 
ATOM   1425 C CA  . TRP   A 1 177 ? 10.237  15.677  9.795  1.00 21.04 ?  177 TRP   A CA  1 
ATOM   1426 C C   . TRP   A 1 177 ? 11.015  16.072  8.553  1.00 23.84 ?  177 TRP   A C   1 
ATOM   1427 O O   . TRP   A 1 177 ? 11.521  17.194  8.477  1.00 21.65 ?  177 TRP   A O   1 
ATOM   1428 C CB  . TRP   A 1 177 ? 10.831  16.346  11.039 1.00 20.28 ?  177 TRP   A CB  1 
ATOM   1429 C CG  . TRP   A 1 177 ? 9.903   16.341  12.217 1.00 23.64 ?  177 TRP   A CG  1 
ATOM   1430 C CD1 . TRP   A 1 177 ? 8.605   15.882  12.260 1.00 25.81 ?  177 TRP   A CD1 1 
ATOM   1431 C CD2 . TRP   A 1 177 ? 10.211  16.798  13.534 1.00 22.91 ?  177 TRP   A CD2 1 
ATOM   1432 N NE1 . TRP   A 1 177 ? 8.091   16.037  13.538 1.00 27.11 ?  177 TRP   A NE1 1 
ATOM   1433 C CE2 . TRP   A 1 177 ? 9.058   16.595  14.336 1.00 26.94 ?  177 TRP   A CE2 1 
ATOM   1434 C CE3 . TRP   A 1 177 ? 11.348  17.363  14.119 1.00 22.56 ?  177 TRP   A CE3 1 
ATOM   1435 C CZ2 . TRP   A 1 177 ? 9.020   16.938  15.694 1.00 25.66 ?  177 TRP   A CZ2 1 
ATOM   1436 C CZ3 . TRP   A 1 177 ? 11.299  17.718  15.479 1.00 23.92 ?  177 TRP   A CZ3 1 
ATOM   1437 C CH2 . TRP   A 1 177 ? 10.148  17.502  16.242 1.00 24.00 ?  177 TRP   A CH2 1 
ATOM   1438 N N   . GLY   A 1 178 ? 11.130  15.159  7.584  1.00 22.92 ?  178 GLY   A N   1 
ATOM   1439 C CA  . GLY   A 1 178 ? 11.843  15.427  6.356  1.00 22.78 ?  178 GLY   A CA  1 
ATOM   1440 C C   . GLY   A 1 178 ? 13.342  15.222  6.498  1.00 22.71 ?  178 GLY   A C   1 
ATOM   1441 O O   . GLY   A 1 178 ? 13.889  15.019  7.587  1.00 22.19 ?  178 GLY   A O   1 
ATOM   1442 N N   . THR   A 1 179 ? 14.025  15.310  5.357  1.00 22.07 ?  179 THR   A N   1 
ATOM   1443 C CA  . THR   A 1 179 ? 15.441  14.982  5.307  1.00 21.43 ?  179 THR   A CA  1 
ATOM   1444 C C   . THR   A 1 179 ? 16.300  16.126  5.779  1.00 26.75 ?  179 THR   A C   1 
ATOM   1445 O O   . THR   A 1 179 ? 17.505  15.925  5.950  1.00 30.23 ?  179 THR   A O   1 
ATOM   1446 C CB  . THR   A 1 179 ? 15.865  14.631  3.876  1.00 26.27 ?  179 THR   A CB  1 
ATOM   1447 O OG1 . THR   A 1 179 ? 15.436  15.669  2.984  1.00 25.70 ?  179 THR   A OG1 1 
ATOM   1448 C CG2 . THR   A 1 179 ? 15.155  13.356  3.445  1.00 26.97 ?  179 THR   A CG2 1 
ATOM   1449 N N   . GLY   A 1 180 ? 15.718  17.323  5.943  1.00 25.43 ?  180 GLY   A N   1 
ATOM   1450 C CA  . GLY   A 1 180 ? 16.468  18.478  6.403  1.00 29.68 ?  180 GLY   A CA  1 
ATOM   1451 C C   . GLY   A 1 180 ? 16.661  18.534  7.901  1.00 32.42 ?  180 GLY   A C   1 
ATOM   1452 O O   . GLY   A 1 180 ? 17.515  19.281  8.385  1.00 36.44 ?  180 GLY   A O   1 
ATOM   1453 N N   . TRP   A 1 181 ? 15.898  17.759  8.648  1.00 26.60 ?  181 TRP   A N   1 
ATOM   1454 C CA  . TRP   A 1 181 ? 16.006  17.777  10.100 1.00 22.73 ?  181 TRP   A CA  1 
ATOM   1455 C C   . TRP   A 1 181 ? 17.018  16.742  10.560 1.00 26.71 ?  181 TRP   A C   1 
ATOM   1456 O O   . TRP   A 1 181 ? 17.091  15.643  10.007 1.00 26.80 ?  181 TRP   A O   1 
ATOM   1457 C CB  . TRP   A 1 181 ? 14.649  17.498  10.745 1.00 23.71 ?  181 TRP   A CB  1 
ATOM   1458 C CG  . TRP   A 1 181 ? 14.716  17.458  12.265 1.00 22.92 ?  181 TRP   A CG  1 
ATOM   1459 C CD1 . TRP   A 1 181 ? 14.568  18.514  13.119 1.00 22.06 ?  181 TRP   A CD1 1 
ATOM   1460 C CD2 . TRP   A 1 181 ? 14.942  16.306  13.080 1.00 25.93 ?  181 TRP   A CD2 1 
ATOM   1461 N NE1 . TRP   A 1 181 ? 14.698  18.091  14.435 1.00 21.42 ?  181 TRP   A NE1 1 
ATOM   1462 C CE2 . TRP   A 1 181 ? 14.928  16.739  14.434 1.00 24.72 ?  181 TRP   A CE2 1 
ATOM   1463 C CE3 . TRP   A 1 181 ? 15.175  14.949  12.805 1.00 21.34 ?  181 TRP   A CE3 1 
ATOM   1464 C CZ2 . TRP   A 1 181 ? 15.104  15.867  15.496 1.00 25.12 ?  181 TRP   A CZ2 1 
ATOM   1465 C CZ3 . TRP   A 1 181 ? 15.364  14.083  13.876 1.00 26.54 ?  181 TRP   A CZ3 1 
ATOM   1466 C CH2 . TRP   A 1 181 ? 15.315  14.549  15.207 1.00 23.52 ?  181 TRP   A CH2 1 
ATOM   1467 N N   . GLY   A 1 182 ? 17.784  17.093  11.590 1.00 23.86 ?  182 GLY   A N   1 
ATOM   1468 C CA  . GLY   A 1 182 ? 18.670  16.116  12.190 1.00 24.09 ?  182 GLY   A CA  1 
ATOM   1469 C C   . GLY   A 1 182 ? 19.690  15.612  11.198 1.00 28.48 ?  182 GLY   A C   1 
ATOM   1470 O O   . GLY   A 1 182 ? 20.194  16.354  10.358 1.00 27.94 ?  182 GLY   A O   1 
ATOM   1471 N N   . GLU   A 1 183 ? 19.994  14.322  11.284 1.00 23.29 ?  183 GLU   A N   1 
ATOM   1472 C CA  . GLU   A 1 183 ? 21.022  13.719  10.431 1.00 24.38 ?  183 GLU   A CA  1 
ATOM   1473 C C   . GLU   A 1 183 ? 20.325  13.094  9.229  1.00 25.34 ?  183 GLU   A C   1 
ATOM   1474 O O   . GLU   A 1 183 ? 20.046  11.896  9.185  1.00 25.21 ?  183 GLU   A O   1 
ATOM   1475 C CB  . GLU   A 1 183 ? 21.835  12.705  11.224 1.00 26.06 ?  183 GLU   A CB  1 
ATOM   1476 C CG  . GLU   A 1 183 ? 22.464  13.303  12.465 1.00 23.74 ?  183 GLU   A CG  1 
ATOM   1477 C CD  . GLU   A 1 183 ? 23.422  12.361  13.183 1.00 30.03 ?  183 GLU   A CD  1 
ATOM   1478 O OE1 . GLU   A 1 183 ? 23.151  11.144  13.231 1.00 29.76 ?  183 GLU   A OE1 1 
ATOM   1479 O OE2 . GLU   A 1 183 ? 24.432  12.844  13.737 1.00 29.06 ?  183 GLU   A OE2 1 
ATOM   1480 N N   . ASN   A 1 184 ? 20.029  13.939  8.240  1.00 25.14 ?  184 ASN   A N   1 
ATOM   1481 C CA  . ASN   A 1 184 ? 19.288  13.510  7.048  1.00 25.60 ?  184 ASN   A CA  1 
ATOM   1482 C C   . ASN   A 1 184 ? 17.946  12.885  7.427  1.00 23.09 ?  184 ASN   A C   1 
ATOM   1483 O O   . ASN   A 1 184 ? 17.482  11.925  6.794  1.00 25.42 ?  184 ASN   A O   1 
ATOM   1484 C CB  . ASN   A 1 184 ? 20.097  12.536  6.182  1.00 23.98 ?  184 ASN   A CB  1 
ATOM   1485 C CG  . ASN   A 1 184 ? 21.410  13.114  5.739  1.00 35.23 ?  184 ASN   A CG  1 
ATOM   1486 O OD1 . ASN   A 1 184 ? 21.549  14.333  5.619  1.00 31.88 ?  184 ASN   A OD1 1 
ATOM   1487 N ND2 . ASN   A 1 184 ? 22.377  12.247  5.464  1.00 40.29 ?  184 ASN   A ND2 1 
ATOM   1488 N N   . GLY   A 1 185 ? 17.329  13.418  8.482  1.00 22.03 ?  185 GLY   A N   1 
ATOM   1489 C CA  . GLY   A 1 185 ? 16.042  12.947  8.942  1.00 23.20 ?  185 GLY   A CA  1 
ATOM   1490 C C   . GLY   A 1 185 ? 16.096  12.021  10.137 1.00 26.08 ?  185 GLY   A C   1 
ATOM   1491 O O   . GLY   A 1 185 ? 15.037  11.659  10.659 1.00 24.73 ?  185 GLY   A O   1 
ATOM   1492 N N   . TYR   A 1 186 ? 17.290  11.627  10.574 1.00 21.90 ?  186 TYR   A N   1 
ATOM   1493 C CA  . TYR   A 1 186 ? 17.489  10.719  11.691 1.00 19.77 ?  186 TYR   A CA  1 
ATOM   1494 C C   . TYR   A 1 186 ? 18.041  11.469  12.889 1.00 20.18 ?  186 TYR   A C   1 
ATOM   1495 O O   . TYR   A 1 186 ? 18.623  12.549  12.762 1.00 24.92 ?  186 TYR   A O   1 
ATOM   1496 C CB  . TYR   A 1 186 ? 18.460  9.605   11.310 1.00 22.45 ?  186 TYR   A CB  1 
ATOM   1497 C CG  . TYR   A 1 186 ? 17.839  8.685   10.295 1.00 21.97 ?  186 TYR   A CG  1 
ATOM   1498 C CD1 . TYR   A 1 186 ? 17.877  8.997   8.938  1.00 26.44 ?  186 TYR   A CD1 1 
ATOM   1499 C CD2 . TYR   A 1 186 ? 17.246  7.497   10.682 1.00 22.17 ?  186 TYR   A CD2 1 
ATOM   1500 C CE1 . TYR   A 1 186 ? 17.307  8.157   8.001  1.00 25.71 ?  186 TYR   A CE1 1 
ATOM   1501 C CE2 . TYR   A 1 186 ? 16.684  6.653   9.754  1.00 25.77 ?  186 TYR   A CE2 1 
ATOM   1502 C CZ  . TYR   A 1 186 ? 16.714  6.985   8.421  1.00 27.05 ?  186 TYR   A CZ  1 
ATOM   1503 O OH  . TYR   A 1 186 ? 16.157  6.136   7.492  1.00 32.43 ?  186 TYR   A OH  1 
ATOM   1504 N N   . ILE   A 1 187 ? 17.847  10.874  14.059 1.00 20.54 ?  187 ILE   A N   1 
ATOM   1505 C CA  . ILE   A 1 187 ? 18.494  11.333  15.274 1.00 23.32 ?  187 ILE   A CA  1 
ATOM   1506 C C   . ILE   A 1 187 ? 19.084  10.127  15.984 1.00 23.91 ?  187 ILE   A C   1 
ATOM   1507 O O   . ILE   A 1 187 ? 18.481  9.051   16.024 1.00 26.98 ?  187 ILE   A O   1 
ATOM   1508 C CB  . ILE   A 1 187 ? 17.512  12.095  16.185 1.00 24.60 ?  187 ILE   A CB  1 
ATOM   1509 C CG1 . ILE   A 1 187 ? 18.165  12.443  17.519 1.00 25.32 ?  187 ILE   A CG1 1 
ATOM   1510 C CG2 . ILE   A 1 187 ? 16.219  11.292  16.393 1.00 20.12 ?  187 ILE   A CG2 1 
ATOM   1511 C CD1 . ILE   A 1 187 ? 17.399  13.538  18.248 1.00 26.78 ?  187 ILE   A CD1 1 
ATOM   1512 N N   . ARG   A 1 188 ? 20.279  10.303  16.522 1.00 22.43 ?  188 ARG   A N   1 
ATOM   1513 C CA  . ARG   A 1 188 ? 20.868  9.339   17.429 1.00 23.55 ?  188 ARG   A CA  1 
ATOM   1514 C C   . ARG   A 1 188 ? 20.659  9.862   18.845 1.00 25.73 ?  188 ARG   A C   1 
ATOM   1515 O O   . ARG   A 1 188 ? 21.123  10.955  19.187 1.00 27.05 ?  188 ARG   A O   1 
ATOM   1516 C CB  . ARG   A 1 188 ? 22.343  9.124   17.104 1.00 23.81 ?  188 ARG   A CB  1 
ATOM   1517 C CG  . ARG   A 1 188 ? 22.545  8.425   15.756 1.00 26.61 ?  188 ARG   A CG  1 
ATOM   1518 C CD  . ARG   A 1 188 ? 24.008  8.289   15.484 1.00 28.43 ?  188 ARG   A CD  1 
ATOM   1519 N NE  . ARG   A 1 188 ? 24.544  9.609   15.187 1.00 29.22 ?  188 ARG   A NE  1 
ATOM   1520 C CZ  . ARG   A 1 188 ? 25.794  9.981   15.411 1.00 37.95 ?  188 ARG   A CZ  1 
ATOM   1521 N NH1 . ARG   A 1 188 ? 26.643  9.191   16.049 1.00 32.56 ?  188 ARG   A NH1 1 
ATOM   1522 N NH2 . ARG   A 1 188 ? 26.189  11.188  15.012 1.00 29.42 ?  188 ARG   A NH2 1 
ATOM   1523 N N   . ILE   A 1 189 ? 19.916  9.113   19.642 1.00 23.93 ?  189 ILE   A N   1 
ATOM   1524 C CA  . ILE   A 1 189 ? 19.596  9.511   21.003 1.00 29.90 ?  189 ILE   A CA  1 
ATOM   1525 C C   . ILE   A 1 189 ? 20.418  8.673   21.962 1.00 26.36 ?  189 ILE   A C   1 
ATOM   1526 O O   . ILE   A 1 189 ? 20.501  7.449   21.813 1.00 24.28 ?  189 ILE   A O   1 
ATOM   1527 C CB  . ILE   A 1 189 ? 18.095  9.380   21.285 1.00 28.55 ?  189 ILE   A CB  1 
ATOM   1528 C CG1 . ILE   A 1 189 ? 17.364  10.425  20.449 1.00 28.25 ?  189 ILE   A CG1 1 
ATOM   1529 C CG2 . ILE   A 1 189 ? 17.830  9.590   22.756 1.00 27.71 ?  189 ILE   A CG2 1 
ATOM   1530 C CD1 . ILE   A 1 189 ? 15.889  10.447  20.639 1.00 37.42 ?  189 ILE   A CD1 1 
ATOM   1531 N N   . LYS   A 1 190 ? 21.022  9.335   22.948 1.00 24.21 ?  190 LYS   A N   1 
ATOM   1532 C CA  . LYS   A 1 190 ? 21.905  8.642   23.878 1.00 27.09 ?  190 LYS   A CA  1 
ATOM   1533 C C   . LYS   A 1 190 ? 21.163  7.542   24.634 1.00 26.20 ?  190 LYS   A C   1 
ATOM   1534 O O   . LYS   A 1 190 ? 20.008  7.705   25.035 1.00 25.71 ?  190 LYS   A O   1 
ATOM   1535 C CB  . LYS   A 1 190 ? 22.513  9.651   24.853 1.00 26.79 ?  190 LYS   A CB  1 
ATOM   1536 C CG  . LYS   A 1 190 ? 23.386  9.033   25.937 1.00 31.04 ?  190 LYS   A CG  1 
ATOM   1537 C CD  . LYS   A 1 190 ? 24.838  9.032   25.514 1.00 41.23 ?  190 LYS   A CD  1 
ATOM   1538 C CE  . LYS   A 1 190 ? 25.756  8.600   26.658 1.00 40.22 ?  190 LYS   A CE  1 
ATOM   1539 N NZ  . LYS   A 1 190 ? 26.114  9.787   27.472 1.00 52.13 ?  190 LYS   A NZ  1 
ATOM   1540 N N   . ARG   A 1 191 ? 21.822  6.403   24.798 1.00 25.42 ?  191 ARG   A N   1 
ATOM   1541 C CA  . ARG   A 1 191 ? 21.314  5.339   25.645 1.00 26.17 ?  191 ARG   A CA  1 
ATOM   1542 C C   . ARG   A 1 191 ? 22.336  5.069   26.745 1.00 29.10 ?  191 ARG   A C   1 
ATOM   1543 O O   . ARG   A 1 191 ? 23.420  5.654   26.764 1.00 29.21 ?  191 ARG   A O   1 
ATOM   1544 C CB  . ARG   A 1 191 ? 21.034  4.066   24.841 1.00 25.18 ?  191 ARG   A CB  1 
ATOM   1545 C CG  . ARG   A 1 191 ? 22.276  3.367   24.300 1.00 26.26 ?  191 ARG   A CG  1 
ATOM   1546 C CD  . ARG   A 1 191 ? 21.894  2.025   23.686 1.00 22.42 ?  191 ARG   A CD  1 
ATOM   1547 N NE  . ARG   A 1 191 ? 23.037  1.153   23.471 1.00 28.72 ?  191 ARG   A NE  1 
ATOM   1548 C CZ  . ARG   A 1 191 ? 23.499  0.298   24.373 1.00 27.50 ?  191 ARG   A CZ  1 
ATOM   1549 N NH1 . ARG   A 1 191 ? 23.031  0.283   25.607 1.00 23.52 ?  191 ARG   A NH1 1 
ATOM   1550 N NH2 . ARG   A 1 191 ? 24.442  -0.572  24.021 1.00 26.41 ?  191 ARG   A NH2 1 
ATOM   1551 N N   . GLY   A 1 192 ? 21.978  4.171   27.658 1.00 29.57 ?  192 GLY   A N   1 
ATOM   1552 C CA  . GLY   A 1 192 ? 22.902  3.750   28.691 1.00 32.92 ?  192 GLY   A CA  1 
ATOM   1553 C C   . GLY   A 1 192 ? 23.126  4.746   29.801 1.00 38.52 ?  192 GLY   A C   1 
ATOM   1554 O O   . GLY   A 1 192 ? 24.195  4.739   30.416 1.00 43.52 ?  192 GLY   A O   1 
ATOM   1555 N N   . THR   A 1 193 ? 22.159  5.616   30.072 1.00 38.21 ?  193 THR   A N   1 
ATOM   1556 C CA  . THR   A 1 193 ? 22.294  6.604   31.131 1.00 43.64 ?  193 THR   A CA  1 
ATOM   1557 C C   . THR   A 1 193 ? 21.740  6.130   32.467 1.00 39.31 ?  193 THR   A C   1 
ATOM   1558 O O   . THR   A 1 193 ? 21.856  6.854   33.460 1.00 49.62 ?  193 THR   A O   1 
ATOM   1559 C CB  . THR   A 1 193 ? 21.602  7.907   30.722 1.00 36.41 ?  193 THR   A CB  1 
ATOM   1560 O OG1 . THR   A 1 193 ? 20.181  7.746   30.848 1.00 39.63 ?  193 THR   A OG1 1 
ATOM   1561 C CG2 . THR   A 1 193 ? 21.959  8.288   29.300 1.00 39.33 ?  193 THR   A CG2 1 
ATOM   1562 N N   . GLY   A 1 194 ? 21.154  4.937   32.526 1.00 40.06 ?  194 GLY   A N   1 
ATOM   1563 C CA  . GLY   A 1 194 ? 20.526  4.470   33.738 1.00 41.70 ?  194 GLY   A CA  1 
ATOM   1564 C C   . GLY   A 1 194 ? 19.181  5.095   34.034 1.00 54.75 ?  194 GLY   A C   1 
ATOM   1565 O O   . GLY   A 1 194 ? 18.473  4.611   34.928 1.00 53.77 ?  194 GLY   A O   1 
ATOM   1566 N N   . ASN   A 1 195 ? 18.817  6.167   33.332 1.00 45.57 ?  195 ASN   A N   1 
ATOM   1567 C CA  . ASN   A 1 195 ? 17.466  6.710   33.355 1.00 44.42 ?  195 ASN   A CA  1 
ATOM   1568 C C   . ASN   A 1 195 ? 16.492  5.671   32.824 1.00 49.04 ?  195 ASN   A C   1 
ATOM   1569 O O   . ASN   A 1 195 ? 16.515  5.337   31.633 1.00 45.35 ?  195 ASN   A O   1 
ATOM   1570 C CB  . ASN   A 1 195 ? 17.402  7.995   32.525 1.00 48.92 ?  195 ASN   A CB  1 
ATOM   1571 C CG  . ASN   A 1 195 ? 16.071  8.708   32.641 1.00 51.37 ?  195 ASN   A CG  1 
ATOM   1572 O OD1 . ASN   A 1 195 ? 15.150  8.234   33.309 1.00 51.20 ?  195 ASN   A OD1 1 
ATOM   1573 N ND2 . ASN   A 1 195 ? 15.962  9.859   31.983 1.00 51.47 ?  195 ASN   A ND2 1 
ATOM   1574 N N   . SER   A 1 196 ? 15.632  5.156   33.704 1.00 39.38 ?  196 SER   A N   1 
ATOM   1575 C CA  . SER   A 1 196 ? 14.677  4.131   33.313 1.00 41.24 ?  196 SER   A CA  1 
ATOM   1576 C C   . SER   A 1 196 ? 13.654  4.647   32.313 1.00 35.60 ?  196 SER   A C   1 
ATOM   1577 O O   . SER   A 1 196 ? 13.079  3.850   31.567 1.00 35.29 ?  196 SER   A O   1 
ATOM   1578 C CB  . SER   A 1 196 ? 13.967  3.578   34.551 1.00 53.15 ?  196 SER   A CB  1 
ATOM   1579 O OG  . SER   A 1 196 ? 14.908  3.108   35.505 1.00 63.38 ?  196 SER   A OG  1 
ATOM   1580 N N   . TYR   A 1 197 ? 13.406  5.953   32.278 1.00 34.43 ?  197 TYR   A N   1 
ATOM   1581 C CA  . TYR   A 1 197 ? 12.485  6.490   31.284 1.00 37.50 ?  197 TYR   A CA  1 
ATOM   1582 C C   . TYR   A 1 197 ? 13.081  6.527   29.887 1.00 34.70 ?  197 TYR   A C   1 
ATOM   1583 O O   . TYR   A 1 197 ? 12.322  6.638   28.914 1.00 30.81 ?  197 TYR   A O   1 
ATOM   1584 C CB  . TYR   A 1 197 ? 12.034  7.901   31.670 1.00 33.56 ?  197 TYR   A CB  1 
ATOM   1585 C CG  . TYR   A 1 197 ? 11.293  7.952   32.980 1.00 42.49 ?  197 TYR   A CG  1 
ATOM   1586 C CD1 . TYR   A 1 197 ? 9.910   7.817   33.021 1.00 47.71 ?  197 TYR   A CD1 1 
ATOM   1587 C CD2 . TYR   A 1 197 ? 11.971  8.138   34.178 1.00 52.09 ?  197 TYR   A CD2 1 
ATOM   1588 C CE1 . TYR   A 1 197 ? 9.223   7.861   34.220 1.00 48.01 ?  197 TYR   A CE1 1 
ATOM   1589 C CE2 . TYR   A 1 197 ? 11.292  8.186   35.383 1.00 50.99 ?  197 TYR   A CE2 1 
ATOM   1590 C CZ  . TYR   A 1 197 ? 9.919   8.050   35.396 1.00 55.99 ?  197 TYR   A CZ  1 
ATOM   1591 O OH  . TYR   A 1 197 ? 9.243   8.096   36.597 1.00 62.51 ?  197 TYR   A OH  1 
ATOM   1592 N N   . GLY   A 1 198 ? 14.404  6.423   29.772 1.00 29.71 ?  198 GLY   A N   1 
ATOM   1593 C CA  . GLY   A 1 198 ? 15.103  6.718   28.530 1.00 34.40 ?  198 GLY   A CA  1 
ATOM   1594 C C   . GLY   A 1 198 ? 15.252  8.215   28.363 1.00 31.21 ?  198 GLY   A C   1 
ATOM   1595 O O   . GLY   A 1 198 ? 14.462  8.978   28.939 1.00 30.06 ?  198 GLY   A O   1 
ATOM   1596 N N   . VAL   A 1 199 ? 16.234  8.691   27.601 1.00 27.39 ?  199 VAL   A N   1 
ATOM   1597 C CA  . VAL   A 1 199 ? 16.314  10.135  27.488 1.00 29.36 ?  199 VAL   A CA  1 
ATOM   1598 C C   . VAL   A 1 199 ? 15.183  10.594  26.580 1.00 28.81 ?  199 VAL   A C   1 
ATOM   1599 O O   . VAL   A 1 199 ? 14.824  9.910   25.606 1.00 29.92 ?  199 VAL   A O   1 
ATOM   1600 C CB  . VAL   A 1 199 ? 17.704  10.622  27.032 1.00 35.90 ?  199 VAL   A CB  1 
ATOM   1601 C CG1 . VAL   A 1 199 ? 18.772  9.560   27.166 1.00 35.23 ?  199 VAL   A CG1 1 
ATOM   1602 C CG2 . VAL   A 1 199 ? 17.677  11.282  25.714 1.00 29.79 ?  199 VAL   A CG2 1 
ATOM   1603 N N   . CYS   A 1 200 ? 14.555  11.712  26.963 1.00 29.92 ?  200 CYS   A N   1 
ATOM   1604 C CA  . CYS   A 1 200 ? 13.319  12.213  26.351 1.00 31.83 ?  200 CYS   A CA  1 
ATOM   1605 C C   . CYS   A 1 200 ? 12.177  11.203  26.433 1.00 28.58 ?  200 CYS   A C   1 
ATOM   1606 O O   . CYS   A 1 200 ? 11.250  11.243  25.618 1.00 30.88 ?  200 CYS   A O   1 
ATOM   1607 C CB  . CYS   A 1 200 ? 13.534  12.651  24.896 1.00 27.31 ?  200 CYS   A CB  1 
ATOM   1608 S SG  . CYS   A 1 200 ? 15.010  13.641  24.620 1.00 30.38 ?  200 CYS   A SG  1 
ATOM   1609 N N   . GLY   A 1 201 ? 12.216  10.303  27.421 1.00 26.40 ?  201 GLY   A N   1 
ATOM   1610 C CA  . GLY   A 1 201 ? 11.123  9.372   27.639 1.00 28.73 ?  201 GLY   A CA  1 
ATOM   1611 C C   . GLY   A 1 201 ? 11.080  8.226   26.661 1.00 30.58 ?  201 GLY   A C   1 
ATOM   1612 O O   . GLY   A 1 201 ? 10.039  7.572   26.535 1.00 27.77 ?  201 GLY   A O   1 
ATOM   1613 N N   . LEU   A 1 202 ? 12.208  7.935   26.005 1.00 24.95 ?  202 LEU   A N   1 
ATOM   1614 C CA  . LEU   A 1 202 ? 12.261  7.022   24.874 1.00 26.82 ?  202 LEU   A CA  1 
ATOM   1615 C C   . LEU   A 1 202 ? 11.794  5.615   25.218 1.00 30.02 ?  202 LEU   A C   1 
ATOM   1616 O O   . LEU   A 1 202 ? 11.415  4.871   24.314 1.00 24.80 ?  202 LEU   A O   1 
ATOM   1617 C CB  . LEU   A 1 202 ? 13.694  6.978   24.327 1.00 25.99 ?  202 LEU   A CB  1 
ATOM   1618 C CG  . LEU   A 1 202 ? 14.002  6.225   23.029 1.00 31.42 ?  202 LEU   A CG  1 
ATOM   1619 C CD1 . LEU   A 1 202 ? 13.206  6.832   21.890 1.00 29.07 ?  202 LEU   A CD1 1 
ATOM   1620 C CD2 . LEU   A 1 202 ? 15.500  6.259   22.706 1.00 27.06 ?  202 LEU   A CD2 1 
ATOM   1621 N N   . TYR   A 1 203 ? 11.826  5.207   26.491 1.00 28.01 ?  203 TYR   A N   1 
ATOM   1622 C CA  . TYR   A 1 203 ? 11.434  3.838   26.808 1.00 31.92 ?  203 TYR   A CA  1 
ATOM   1623 C C   . TYR   A 1 203 ? 9.999   3.734   27.289 1.00 27.99 ?  203 TYR   A C   1 
ATOM   1624 O O   . TYR   A 1 203 ? 9.610   2.689   27.824 1.00 29.66 ?  203 TYR   A O   1 
ATOM   1625 C CB  . TYR   A 1 203 ? 12.385  3.220   27.833 1.00 26.41 ?  203 TYR   A CB  1 
ATOM   1626 C CG  . TYR   A 1 203 ? 13.833  3.374   27.457 1.00 27.17 ?  203 TYR   A CG  1 
ATOM   1627 C CD1 . TYR   A 1 203 ? 14.215  3.466   26.114 1.00 29.07 ?  203 TYR   A CD1 1 
ATOM   1628 C CD2 . TYR   A 1 203 ? 14.827  3.371   28.430 1.00 26.42 ?  203 TYR   A CD2 1 
ATOM   1629 C CE1 . TYR   A 1 203 ? 15.528  3.606   25.760 1.00 26.69 ?  203 TYR   A CE1 1 
ATOM   1630 C CE2 . TYR   A 1 203 ? 16.148  3.497   28.089 1.00 25.26 ?  203 TYR   A CE2 1 
ATOM   1631 C CZ  . TYR   A 1 203 ? 16.496  3.612   26.755 1.00 26.14 ?  203 TYR   A CZ  1 
ATOM   1632 O OH  . TYR   A 1 203 ? 17.806  3.752   26.414 1.00 27.64 ?  203 TYR   A OH  1 
ATOM   1633 N N   . THR   A 1 204 ? 9.201   4.786   27.089 1.00 30.05 ?  204 THR   A N   1 
ATOM   1634 C CA  . THR   A 1 204 ? 7.871   4.846   27.683 1.00 27.25 ?  204 THR   A CA  1 
ATOM   1635 C C   . THR   A 1 204 ? 6.907   3.861   27.032 1.00 31.08 ?  204 THR   A C   1 
ATOM   1636 O O   . THR   A 1 204 ? 6.156   3.173   27.730 1.00 26.33 ?  204 THR   A O   1 
ATOM   1637 C CB  . THR   A 1 204 ? 7.309   6.256   27.573 1.00 29.26 ?  204 THR   A CB  1 
ATOM   1638 O OG1 . THR   A 1 204 ? 8.148   7.158   28.302 1.00 30.94 ?  204 THR   A OG1 1 
ATOM   1639 C CG2 . THR   A 1 204 ? 5.867   6.301   28.128 1.00 28.55 ?  204 THR   A CG2 1 
ATOM   1640 N N   . SER   A 1 205 ? 6.898   3.773   25.700 1.00 29.85 ?  205 SER   A N   1 
ATOM   1641 C CA  . SER   A 1 205 ? 5.802   3.062   25.028 1.00 28.26 ?  205 SER   A CA  1 
ATOM   1642 C C   . SER   A 1 205 ? 6.271   2.637   23.636 1.00 30.03 ?  205 SER   A C   1 
ATOM   1643 O O   . SER   A 1 205 ? 6.234   3.440   22.700 1.00 26.66 ?  205 SER   A O   1 
ATOM   1644 C CB  . SER   A 1 205 ? 4.559   3.940   24.942 1.00 31.80 ?  205 SER   A CB  1 
ATOM   1645 O OG  . SER   A 1 205 ? 3.445   3.185   24.474 1.00 36.06 ?  205 SER   A OG  1 
ATOM   1646 N N   . SER   A 1 206 ? 6.661   1.374   23.503 1.00 25.41 ?  206 SER   A N   1 
ATOM   1647 C CA  . SER   A 1 206 ? 7.321   0.887   22.298 1.00 26.37 ?  206 SER   A CA  1 
ATOM   1648 C C   . SER   A 1 206 ? 6.592   -0.348  21.800 1.00 30.52 ?  206 SER   A C   1 
ATOM   1649 O O   . SER   A 1 206 ? 6.277   -1.237  22.595 1.00 30.08 ?  206 SER   A O   1 
ATOM   1650 C CB  . SER   A 1 206 ? 8.780   0.559   22.586 1.00 25.81 ?  206 SER   A CB  1 
ATOM   1651 O OG  . SER   A 1 206 ? 9.385   1.682   23.209 1.00 27.67 ?  206 SER   A OG  1 
ATOM   1652 N N   . PHE   A 1 207 ? 6.319   -0.397  20.497 1.00 26.59 ?  207 PHE   A N   1 
ATOM   1653 C CA  . PHE   A 1 207 ? 5.531   -1.469  19.906 1.00 28.77 ?  207 PHE   A CA  1 
ATOM   1654 C C   . PHE   A 1 207 ? 6.127   -1.879  18.576 1.00 32.42 ?  207 PHE   A C   1 
ATOM   1655 O O   . PHE   A 1 207 ? 6.702   -1.064  17.856 1.00 27.87 ?  207 PHE   A O   1 
ATOM   1656 C CB  . PHE   A 1 207 ? 4.073   -1.065  19.666 1.00 29.79 ?  207 PHE   A CB  1 
ATOM   1657 C CG  . PHE   A 1 207 ? 3.312   -0.752  20.921 1.00 28.98 ?  207 PHE   A CG  1 
ATOM   1658 C CD1 . PHE   A 1 207 ? 3.426   0.484   21.527 1.00 28.32 ?  207 PHE   A CD1 1 
ATOM   1659 C CD2 . PHE   A 1 207 ? 2.455   -1.696  21.477 1.00 32.13 ?  207 PHE   A CD2 1 
ATOM   1660 C CE1 . PHE   A 1 207 ? 2.722   0.778   22.668 1.00 31.58 ?  207 PHE   A CE1 1 
ATOM   1661 C CE2 . PHE   A 1 207 ? 1.743   -1.404  22.625 1.00 31.77 ?  207 PHE   A CE2 1 
ATOM   1662 C CZ  . PHE   A 1 207 ? 1.874   -0.168  23.221 1.00 37.18 ?  207 PHE   A CZ  1 
ATOM   1663 N N   . TYR   A 1 208 ? 5.950   -3.144  18.236 1.00 29.19 ?  208 TYR   A N   1 
ATOM   1664 C CA  . TYR   A 1 208 ? 6.399   -3.613  16.945 1.00 27.49 ?  208 TYR   A CA  1 
ATOM   1665 C C   . TYR   A 1 208 ? 5.370   -4.579  16.376 1.00 29.27 ?  208 TYR   A C   1 
ATOM   1666 O O   . TYR   A 1 208 ? 4.620   -5.220  17.131 1.00 30.11 ?  208 TYR   A O   1 
ATOM   1667 C CB  . TYR   A 1 208 ? 7.786   -4.272  17.039 1.00 29.02 ?  208 TYR   A CB  1 
ATOM   1668 C CG  . TYR   A 1 208 ? 7.892   -5.386  18.047 1.00 37.23 ?  208 TYR   A CG  1 
ATOM   1669 C CD1 . TYR   A 1 208 ? 8.231   -5.122  19.371 1.00 37.17 ?  208 TYR   A CD1 1 
ATOM   1670 C CD2 . TYR   A 1 208 ? 7.672   -6.707  17.674 1.00 34.39 ?  208 TYR   A CD2 1 
ATOM   1671 C CE1 . TYR   A 1 208 ? 8.337   -6.148  20.300 1.00 38.43 ?  208 TYR   A CE1 1 
ATOM   1672 C CE2 . TYR   A 1 208 ? 7.782   -7.729  18.584 1.00 35.92 ?  208 TYR   A CE2 1 
ATOM   1673 C CZ  . TYR   A 1 208 ? 8.115   -7.450  19.893 1.00 41.82 ?  208 TYR   A CZ  1 
ATOM   1674 O OH  . TYR   A 1 208 ? 8.211   -8.475  20.801 1.00 43.33 ?  208 TYR   A OH  1 
ATOM   1675 N N   . PRO   A 1 209 ? 5.270   -4.658  15.056 1.00 28.83 ?  209 PRO   A N   1 
ATOM   1676 C CA  . PRO   A 1 209 ? 4.365   -5.630  14.438 1.00 28.55 ?  209 PRO   A CA  1 
ATOM   1677 C C   . PRO   A 1 209 ? 4.997   -7.006  14.410 1.00 30.30 ?  209 PRO   A C   1 
ATOM   1678 O O   . PRO   A 1 209 ? 6.218   -7.164  14.352 1.00 34.65 ?  209 PRO   A O   1 
ATOM   1679 C CB  . PRO   A 1 209 ? 4.176   -5.091  13.013 1.00 28.12 ?  209 PRO   A CB  1 
ATOM   1680 C CG  . PRO   A 1 209 ? 5.511   -4.405  12.715 1.00 32.18 ?  209 PRO   A CG  1 
ATOM   1681 C CD  . PRO   A 1 209 ? 6.063   -3.918  14.052 1.00 30.17 ?  209 PRO   A CD  1 
ATOM   1682 N N   . VAL   A 1 210 ? 4.137   -8.011  14.447 1.00 31.26 ?  210 VAL   A N   1 
ATOM   1683 C CA  . VAL   A 1 210 ? 4.543   -9.397  14.303 1.00 32.34 ?  210 VAL   A CA  1 
ATOM   1684 C C   . VAL   A 1 210 ? 4.100   -9.857  12.928 1.00 37.51 ?  210 VAL   A C   1 
ATOM   1685 O O   . VAL   A 1 210 ? 2.983   -9.550  12.499 1.00 38.53 ?  210 VAL   A O   1 
ATOM   1686 C CB  . VAL   A 1 210 ? 3.928   -10.266 15.417 1.00 35.08 ?  210 VAL   A CB  1 
ATOM   1687 C CG1 . VAL   A 1 210 ? 4.032   -11.742 15.062 1.00 43.82 ?  210 VAL   A CG1 1 
ATOM   1688 C CG2 . VAL   A 1 210 ? 4.628   -9.980  16.724 1.00 43.75 ?  210 VAL   A CG2 1 
ATOM   1689 N N   . LYS   A 1 211 ? 4.984   -10.554 12.222 1.00 34.57 ?  211 LYS   A N   1 
ATOM   1690 C CA  . LYS   A 1 211 ? 4.648   -11.127 10.925 1.00 47.27 ?  211 LYS   A CA  1 
ATOM   1691 C C   . LYS   A 1 211 ? 5.258   -12.511 10.831 1.00 49.70 ?  211 LYS   A C   1 
ATOM   1692 O O   . LYS   A 1 211 ? 6.483   -12.649 10.864 1.00 45.62 ?  211 LYS   A O   1 
ATOM   1693 C CB  . LYS   A 1 211 ? 5.130   -10.255 9.761  1.00 41.41 ?  211 LYS   A CB  1 
ATOM   1694 C CG  . LYS   A 1 211 ? 4.888   -10.938 8.408  1.00 43.64 ?  211 LYS   A CG  1 
ATOM   1695 C CD  . LYS   A 1 211 ? 3.930   -10.168 7.524  1.00 52.99 ?  211 LYS   A CD  1 
ATOM   1696 C CE  . LYS   A 1 211 ? 3.505   -11.005 6.309  1.00 44.34 ?  211 LYS   A CE  1 
ATOM   1697 N NZ  . LYS   A 1 211 ? 2.057   -11.375 6.364  1.00 50.84 ?  211 LYS   A NZ  1 
ATOM   1698 N N   . ASN   A 1 212 ? 4.407   -13.523 10.699 1.00 53.83 ?  212 ASN   A N   1 
ATOM   1699 C CA  . ASN   A 1 212 ? 4.847   -14.907 10.564 1.00 61.79 ?  212 ASN   A CA  1 
ATOM   1700 C C   . ASN   A 1 212 ? 5.308   -15.191 9.145  1.00 65.62 ?  212 ASN   A C   1 
ATOM   1701 O O   . ASN   A 1 212 ? 6.159   -16.050 8.915  1.00 69.45 ?  212 ASN   A O   1 
ATOM   1702 C CB  . ASN   A 1 212 ? 3.722   -15.864 10.937 1.00 55.39 ?  212 ASN   A CB  1 
ATOM   1703 C CG  . ASN   A 1 212 ? 3.454   -15.887 12.420 1.00 59.45 ?  212 ASN   A CG  1 
ATOM   1704 O OD1 . ASN   A 1 212 ? 4.336   -15.583 13.226 1.00 64.57 ?  212 ASN   A OD1 1 
ATOM   1705 N ND2 . ASN   A 1 212 ? 2.225   -16.228 12.794 1.00 72.81 ?  212 ASN   A ND2 1 
ATOM   1706 O OXT . ASN   A 1 212 ? 4.829   -14.567 8.196  1.00 65.41 ?  212 ASN   A OXT 1 
HETATM 1707 N N1  . A1BWT B 2 .   ? 1.464   11.970  19.863 0.64 41.40 ?  301 A1BWT A N1  1 
HETATM 1708 N N3  . A1BWT B 2 .   ? -4.969  14.372  21.289 0.64 55.67 ?  301 A1BWT A N3  1 
HETATM 1709 C C4  . A1BWT B 2 .   ? 1.053   12.186  18.607 0.64 37.68 ?  301 A1BWT A C4  1 
HETATM 1710 C C5  . A1BWT B 2 .   ? 1.067   10.824  20.660 0.64 45.23 ?  301 A1BWT A C5  1 
HETATM 1711 C C7  . A1BWT B 2 .   ? 0.556   11.343  22.003 0.64 39.98 ?  301 A1BWT A C7  1 
HETATM 1712 C C8  . A1BWT B 2 .   ? -1.668  10.207  21.652 0.64 43.33 ?  301 A1BWT A C8  1 
HETATM 1713 C C10 . A1BWT B 2 .   ? -3.232  12.048  20.823 0.64 46.96 ?  301 A1BWT A C10 1 
HETATM 1714 C C13 . A1BWT B 2 .   ? 2.266   9.878   20.818 0.64 38.49 ?  301 A1BWT A C13 1 
HETATM 1715 C C15 . A1BWT B 2 .   ? 1.409   7.629   21.569 0.64 41.81 ?  301 A1BWT A C15 1 
HETATM 1716 C C17 . A1BWT B 2 .   ? 1.761   6.827   23.797 0.64 43.06 ?  301 A1BWT A C17 1 
HETATM 1717 C C20 . A1BWT B 2 .   ? -6.045  15.067  21.659 0.64 57.37 ?  301 A1BWT A C20 1 
HETATM 1718 C C21 . A1BWT B 2 .   ? -7.203  15.079  20.688 0.64 46.30 ?  301 A1BWT A C21 1 
HETATM 1719 C C1  . A1BWT B 2 .   ? 3.023   14.138  15.971 0.64 33.21 ?  301 A1BWT A C1  1 
HETATM 1720 C C11 . A1BWT B 2 .   ? -2.702  13.374  21.361 0.64 47.76 ?  301 A1BWT A C11 1 
HETATM 1721 C C12 . A1BWT B 2 .   ? -3.766  14.189  22.092 0.64 51.60 ?  301 A1BWT A C12 1 
HETATM 1722 C C14 . A1BWT B 2 .   ? 2.084   8.808   21.864 0.64 44.14 ?  301 A1BWT A C14 1 
HETATM 1723 C C16 . A1BWT B 2 .   ? 1.246   6.647   22.534 0.64 41.25 ?  301 A1BWT A C16 1 
HETATM 1724 C C18 . A1BWT B 2 .   ? 2.438   7.984   24.104 0.64 42.48 ?  301 A1BWT A C18 1 
HETATM 1725 C C19 . A1BWT B 2 .   ? 2.600   8.972   23.145 0.64 42.34 ?  301 A1BWT A C19 1 
HETATM 1726 C C2  . A1BWT B 2 .   ? 2.539   13.069  16.898 0.64 35.04 ?  301 A1BWT A C2  1 
HETATM 1727 C C3  . A1BWT B 2 .   ? 1.552   13.487  17.974 0.64 36.30 ?  301 A1BWT A C3  1 
HETATM 1728 C C9  . A1BWT B 2 .   ? -3.065  10.811  21.698 0.64 39.47 ?  301 A1BWT A C9  1 
HETATM 1729 N N2  . A1BWT B 2 .   ? -0.689  11.015  22.363 0.64 54.45 ?  301 A1BWT A N2  1 
HETATM 1730 O O1  . A1BWT B 2 .   ? 3.808   15.023  16.372 0.64 39.53 -1 301 A1BWT A O1  1 
HETATM 1731 O O2  . A1BWT B 2 .   ? 2.622   14.054  14.800 0.64 31.58 ?  301 A1BWT A O2  1 
HETATM 1732 O O3  . A1BWT B 2 .   ? 0.508   14.303  17.468 0.64 40.76 ?  301 A1BWT A O3  1 
HETATM 1733 O O4  . A1BWT B 2 .   ? 0.375   11.377  17.967 0.64 29.20 ?  301 A1BWT A O4  1 
HETATM 1734 O O5  . A1BWT B 2 .   ? 1.288   12.032  22.717 0.64 53.17 ?  301 A1BWT A O5  1 
HETATM 1735 O O6  . A1BWT B 2 .   ? -6.093  15.675  22.739 0.64 57.08 ?  301 A1BWT A O6  1 
HETATM 1736 O O   . HOH   C 3 .   ? 14.613  21.427  25.330 1.00 42.49 ?  401 HOH   A O   1 
HETATM 1737 O O   . HOH   C 3 .   ? 15.922  6.438   5.049  1.00 35.08 ?  402 HOH   A O   1 
HETATM 1738 O O   . HOH   C 3 .   ? -5.380  17.694  24.020 1.00 48.72 ?  403 HOH   A O   1 
HETATM 1739 O O   . HOH   C 3 .   ? 6.948   -0.136  25.885 1.00 32.85 ?  404 HOH   A O   1 
HETATM 1740 O O   . HOH   C 3 .   ? -9.635  16.308  8.338  1.00 50.67 ?  405 HOH   A O   1 
HETATM 1741 O O   . HOH   C 3 .   ? 6.540   3.848   -3.055 1.00 44.18 ?  406 HOH   A O   1 
HETATM 1742 O O   . HOH   C 3 .   ? -9.310  6.257   21.283 1.00 45.44 ?  407 HOH   A O   1 
HETATM 1743 O O   . HOH   C 3 .   ? 22.186  19.375  16.967 1.00 38.71 ?  408 HOH   A O   1 
HETATM 1744 O O   . HOH   C 3 .   ? -10.383 6.486   -3.409 1.00 36.78 ?  409 HOH   A O   1 
HETATM 1745 O O   . HOH   C 3 .   ? 0.976   -5.117  13.140 1.00 29.27 ?  410 HOH   A O   1 
HETATM 1746 O O   . HOH   C 3 .   ? 19.711  20.700  19.612 1.00 39.00 ?  411 HOH   A O   1 
HETATM 1747 O O   . HOH   C 3 .   ? 8.916   4.426   23.583 1.00 29.85 ?  412 HOH   A O   1 
HETATM 1748 O O   . HOH   C 3 .   ? -11.586 9.331   8.811  1.00 39.06 ?  413 HOH   A O   1 
HETATM 1749 O O   . HOH   C 3 .   ? 24.699  -11.744 20.362 1.00 43.87 ?  414 HOH   A O   1 
HETATM 1750 O O   . HOH   C 3 .   ? 6.480   5.516   3.823  1.00 27.00 ?  415 HOH   A O   1 
HETATM 1751 O O   . HOH   C 3 .   ? 5.507   17.149  25.648 1.00 37.63 ?  416 HOH   A O   1 
HETATM 1752 O O   . HOH   C 3 .   ? 11.662  0.636   8.094  1.00 24.05 ?  417 HOH   A O   1 
HETATM 1753 O O   . HOH   C 3 .   ? -8.131  -7.970  5.866  1.00 47.89 ?  418 HOH   A O   1 
HETATM 1754 O O   . HOH   C 3 .   ? -4.653  9.371   -0.561 1.00 24.94 ?  419 HOH   A O   1 
HETATM 1755 O O   . HOH   C 3 .   ? 10.952  2.714   6.583  1.00 22.74 ?  420 HOH   A O   1 
HETATM 1756 O O   . HOH   C 3 .   ? 6.505   6.415   7.510  1.00 23.74 ?  421 HOH   A O   1 
HETATM 1757 O O   . HOH   C 3 .   ? 9.834   0.956   25.748 1.00 32.42 ?  422 HOH   A O   1 
HETATM 1758 O O   . HOH   C 3 .   ? 11.745  -0.463  27.101 1.00 30.38 ?  423 HOH   A O   1 
HETATM 1759 O O   . HOH   C 3 .   ? 8.756   5.565   6.184  1.00 26.65 ?  424 HOH   A O   1 
HETATM 1760 O O   . HOH   C 3 .   ? 10.320  9.405   7.913  1.00 24.23 ?  425 HOH   A O   1 
HETATM 1761 O O   . HOH   C 3 .   ? 28.274  -2.177  22.674 1.00 44.56 ?  426 HOH   A O   1 
HETATM 1762 O O   . HOH   C 3 .   ? 17.043  0.791   3.829  1.00 35.95 ?  427 HOH   A O   1 
HETATM 1763 O O   . HOH   C 3 .   ? 19.247  6.048   28.952 1.00 34.40 ?  428 HOH   A O   1 
HETATM 1764 O O   . HOH   C 3 .   ? 17.857  6.652   26.310 1.00 28.85 ?  429 HOH   A O   1 
HETATM 1765 O O   . HOH   C 3 .   ? 15.235  12.606  29.434 1.00 37.45 ?  430 HOH   A O   1 
HETATM 1766 O O   . HOH   C 3 .   ? -13.422 11.244  -2.383 1.00 33.85 ?  431 HOH   A O   1 
HETATM 1767 O O   . HOH   C 3 .   ? 9.259   -3.962  12.502 1.00 31.74 ?  432 HOH   A O   1 
HETATM 1768 O O   . HOH   C 3 .   ? 17.738  10.183  4.720  1.00 39.10 ?  433 HOH   A O   1 
HETATM 1769 O O   . HOH   C 3 .   ? 7.568   9.594   13.092 1.00 27.05 ?  434 HOH   A O   1 
HETATM 1770 O O   . HOH   C 3 .   ? 23.937  -4.925  3.904  1.00 52.05 ?  435 HOH   A O   1 
HETATM 1771 O O   . HOH   C 3 .   ? 3.315   -5.732  -0.215 1.00 42.40 ?  436 HOH   A O   1 
HETATM 1772 O O   . HOH   C 3 .   ? 15.005  -10.315 12.512 1.00 49.04 ?  437 HOH   A O   1 
HETATM 1773 O O   . HOH   C 3 .   ? 9.826   7.852   -1.184 1.00 37.70 ?  438 HOH   A O   1 
HETATM 1774 O O   . HOH   C 3 .   ? 5.528   16.565  14.868 1.00 35.55 ?  439 HOH   A O   1 
HETATM 1775 O O   . HOH   C 3 .   ? 23.575  2.330   14.233 1.00 34.44 ?  440 HOH   A O   1 
HETATM 1776 O O   . HOH   C 3 .   ? -7.107  8.403   12.957 1.00 28.78 ?  441 HOH   A O   1 
HETATM 1777 O O   . HOH   C 3 .   ? 25.880  -1.566  21.629 1.00 31.96 ?  442 HOH   A O   1 
HETATM 1778 O O   . HOH   C 3 .   ? 15.641  9.562   3.085  1.00 27.72 ?  443 HOH   A O   1 
HETATM 1779 O O   . HOH   C 3 .   ? 14.251  18.920  23.742 1.00 28.74 ?  444 HOH   A O   1 
HETATM 1780 O O   . HOH   C 3 .   ? 5.020   3.343   20.189 1.00 33.27 ?  445 HOH   A O   1 
HETATM 1781 O O   . HOH   C 3 .   ? -7.606  15.099  12.125 1.00 31.74 ?  446 HOH   A O   1 
HETATM 1782 O O   . HOH   C 3 .   ? 8.606   -3.573  2.825  1.00 31.56 ?  447 HOH   A O   1 
HETATM 1783 O O   . HOH   C 3 .   ? 12.973  13.732  9.962  1.00 22.78 ?  448 HOH   A O   1 
HETATM 1784 O O   . HOH   C 3 .   ? 6.550   7.899   -1.413 1.00 37.25 ?  449 HOH   A O   1 
HETATM 1785 O O   . HOH   C 3 .   ? -8.054  5.725   -5.307 1.00 29.32 ?  450 HOH   A O   1 
HETATM 1786 O O   . HOH   C 3 .   ? 16.688  0.562   31.349 1.00 41.63 ?  451 HOH   A O   1 
HETATM 1787 O O   . HOH   C 3 .   ? 7.280   8.490   30.660 1.00 44.90 ?  452 HOH   A O   1 
HETATM 1788 O O   . HOH   C 3 .   ? 2.594   -7.437  23.841 1.00 44.09 ?  453 HOH   A O   1 
HETATM 1789 O O   . HOH   C 3 .   ? 9.837   -6.832  25.968 1.00 35.52 ?  454 HOH   A O   1 
HETATM 1790 O O   . HOH   C 3 .   ? 2.891   4.142   21.840 1.00 36.04 ?  455 HOH   A O   1 
HETATM 1791 O O   . HOH   C 3 .   ? 22.093  16.945  23.045 1.00 37.24 ?  456 HOH   A O   1 
HETATM 1792 O O   . HOH   C 3 .   ? -14.027 6.852   7.266  1.00 35.40 ?  457 HOH   A O   1 
HETATM 1793 O O   . HOH   C 3 .   ? 9.356   20.775  6.917  1.00 49.83 ?  458 HOH   A O   1 
HETATM 1794 O O   . HOH   C 3 .   ? 21.138  -12.286 20.572 1.00 46.62 ?  459 HOH   A O   1 
HETATM 1795 O O   . HOH   C 3 .   ? 2.584   9.872   -0.676 1.00 29.46 ?  460 HOH   A O   1 
HETATM 1796 O O   . HOH   C 3 .   ? 19.916  16.821  7.320  1.00 39.10 ?  461 HOH   A O   1 
HETATM 1797 O O   . HOH   C 3 .   ? -1.923  -1.149  -2.483 1.00 26.11 ?  462 HOH   A O   1 
HETATM 1798 O O   . HOH   C 3 .   ? 9.900   15.391  32.530 1.00 46.86 ?  463 HOH   A O   1 
HETATM 1799 O O   . HOH   C 3 .   ? -7.193  16.616  9.311  1.00 30.29 ?  464 HOH   A O   1 
HETATM 1800 O O   . HOH   C 3 .   ? 4.273   2.558   -2.711 1.00 31.90 ?  465 HOH   A O   1 
HETATM 1801 O O   . HOH   C 3 .   ? 0.505   7.673   2.818  1.00 26.87 ?  466 HOH   A O   1 
HETATM 1802 O O   . HOH   C 3 .   ? -7.234  -7.601  0.656  1.00 43.57 ?  467 HOH   A O   1 
HETATM 1803 O O   . HOH   C 3 .   ? 6.494   0.745   -2.706 1.00 39.05 ?  468 HOH   A O   1 
HETATM 1804 O O   . HOH   C 3 .   ? 19.103  10.500  31.294 1.00 40.88 ?  469 HOH   A O   1 
HETATM 1805 O O   . HOH   C 3 .   ? 12.081  15.768  3.118  1.00 29.09 ?  470 HOH   A O   1 
HETATM 1806 O O   . HOH   C 3 .   ? 12.560  24.109  25.121 1.00 41.62 ?  471 HOH   A O   1 
HETATM 1807 O O   . HOH   C 3 .   ? -2.349  -3.537  -3.389 1.00 48.25 ?  472 HOH   A O   1 
HETATM 1808 O O   . HOH   C 3 .   ? 19.122  3.621   30.645 1.00 48.64 ?  473 HOH   A O   1 
HETATM 1809 O O   . HOH   C 3 .   ? -1.999  -8.393  18.469 1.00 52.30 ?  474 HOH   A O   1 
HETATM 1810 O O   . HOH   C 3 .   ? 8.889   7.629   11.908 1.00 29.40 ?  475 HOH   A O   1 
HETATM 1811 O O   . HOH   C 3 .   ? -2.000  -13.630 16.302 1.00 71.15 ?  476 HOH   A O   1 
HETATM 1812 O O   . HOH   C 3 .   ? 24.178  6.922   11.689 1.00 49.01 ?  477 HOH   A O   1 
HETATM 1813 O O   . HOH   C 3 .   ? 0.292   -2.254  29.533 1.00 70.69 ?  478 HOH   A O   1 
HETATM 1814 O O   . HOH   C 3 .   ? 8.529   7.909   8.986  1.00 29.68 ?  479 HOH   A O   1 
# 
