data_9NAY
# 
_entry.id   9NAY 
# 
_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   9NAY         pdb_00009nay 10.2210/pdb9nay/pdb 
WWPDB D_1000292945 ?            ?                   
# 
_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                        9NAY 
_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 apo-form of the same protein'                   9NAG unspecified 
PDB 'MicroED structure of papain crystals co-crystallized with pure E-64-A65' 9NAO unspecified 
PDB 'MicroED structure of the same protein complexed with a different ligand' 9N9D unspecified 
PDB 'MicroED structure of the same protein complexed with a different ligand' 9NAE unspecified 
PDB 'MicroED structure of the same protein complexed with a different ligand' 9NAR unspecified 
PDB 'XRD structure of the same protein complexed with a different ligand'     9NAT unspecified 
PDB 'MicroED structure of the same protein complexed with a different ligand' 9NAX unspecified 
# 
_pdbx_contact_author.id                 2 
_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 ? 
'Rodriguez, J.A.' 2 ? 
# 
_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 '(3S)-4-({(1S)-2-[(8-aminooctyl)amino]-1-cyclobutyl-2-oxoethyl}amino)-3-hydroxy-4-oxobutanoic acid' 371.472   1 
?        ? ? ? 
3 water       nat water                                                                                               18.015    4 
?        ? ? ? 
# 
_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 '(3S)-4-({(1S)-2-[(8-aminooctyl)amino]-1-cyclobutyl-2-oxoethyl}amino)-3-hydroxy-4-oxobutanoic acid' A1AXI 
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 
A1AXI non-polymer         . '(3S)-4-({(1S)-2-[(8-aminooctyl)amino]-1-cyclobutyl-2-oxoethyl}amino)-3-hydroxy-4-oxobutanoic acid' ? 
'C18 H33 N3 O5'  371.472 
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 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1AXI 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1AXI 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 A1AXI 1 301 301 A1AXI A65 A . 
C 3 HOH   1 401 5   HOH   HOH A . 
C 3 HOH   2 402 1   HOH   HOH A . 
C 3 HOH   3 403 6   HOH   HOH A . 
C 3 HOH   4 404 3   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.dependencies 
_software.description 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.pdbx_ordinal 
_software.type 
_software.version 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? 1 ? 1.20.1_4487 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? 2 ? .           
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XSCALE ? ? 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                     9NAY 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     42.200 
_cell.length_a_esd                 ? 
_cell.length_b                     48.780 
_cell.length_b_esd                 ? 
_cell.length_c                     100.100 
_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                         9NAY 
_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                   9NAY 
_exptl.crystals_number            ? 
_exptl.details                    ? 
_exptl.method                     'ELECTRON CRYSTALLOGRAPHY' 
_exptl.method_details             ? 
# 
_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                                 9NAY 
_refine.pdbx_refine_id                           'ELECTRON CRYSTALLOGRAPHY' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.50 
_refine.ls_d_res_low                             50.05 
_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                     6554 
_refine.ls_number_reflns_R_free                  656 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    86.45 
_refine.ls_percent_reflns_R_free                 10.01 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1847 
_refine.ls_R_factor_R_free                       0.2277 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1797 
_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                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 21.52 
_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                            0.32 
_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                    ? 
# 
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 
'ELECTRON CRYSTALLOGRAPHY' ? 0.007 ? 1765 ? f_bond_d           ? ? 
'ELECTRON CRYSTALLOGRAPHY' ? 1.119 ? 2401 ? f_angle_d          ? ? 
'ELECTRON CRYSTALLOGRAPHY' ? 8.249 ? 270  ? f_dihedral_angle_d ? ? 
'ELECTRON CRYSTALLOGRAPHY' ? 0.074 ? 239  ? f_chiral_restr     ? ? 
'ELECTRON CRYSTALLOGRAPHY' ? 0.009 ? 315  ? 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 
'ELECTRON CRYSTALLOGRAPHY' 2.50 2.69  . . 128 1157 86.00 . . . . 0.2859 . . . . . . . . . . . . . . . 0.3421 
'ELECTRON CRYSTALLOGRAPHY' 2.69 2.96  . . 128 1152 88.00 . . . . 0.2513 . . . . . . . . . . . . . . . 0.3135 
'ELECTRON CRYSTALLOGRAPHY' 2.97 3.39  . . 131 1177 87.00 . . . . 0.1880 . . . . . . . . . . . . . . . 0.2378 
'ELECTRON CRYSTALLOGRAPHY' 3.39 4.28  . . 133 1186 87.00 . . . . 0.1458 . . . . . . . . . . . . . . . 0.1920 
'ELECTRON CRYSTALLOGRAPHY' 4.28 50.05 . . 136 1226 85.00 . . . . 0.1417 . . . . . . . . . . . . . . . 0.1836 
# 
_struct.entry_id                     9NAY 
_struct.title                        
;MicroED structure of papain complexed with natural product E-64-A65 from microcrystals soaked in crude biosynthetic reaction mixture
;
_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        9NAY 
_struct_keywords.text            'Inhibitor, Complex, Protease, MicroED, 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              9NAY 
_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_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 ? ? ? ? ? ? ? 2.040 ? ? 
disulf2 disulf ?    ? A CYS 56  SG ? ? ? 1_555 A CYS   95  SG ? ? A CYS 56  A CYS   95  1_555 ? ? ? ? ? ? ? 2.049 ? ? 
disulf3 disulf ?    ? A CYS 153 SG ? ? ? 1_555 A CYS   200 SG ? ? A CYS 153 A CYS   200 1_555 ? ? ? ? ? ? ? 2.067 ? ? 
covale1 covale none ? A CYS 25  SG ? ? ? 1_555 B A1AXI .   C2 ? ? A CYS 25  A A1AXI 301 1_555 ? ? ? ? ? ? ? 1.808 ? ? 
# 
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 A1AXI B .   ? CYS A 25  ? A1AXI A 301 ? 1_555 CYS A 25  ? 1_555 C2 SG CYS 1 A1AXI 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       3.40 
# 
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 ? VAL A 113 ? GLY A 109 VAL A 113 
AA3 2 SER A 206 ? VAL A 210 ? SER A 206 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 VAL A 161 ? O VAL A 161 N VAL A 132 ? N VAL A 132 
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 VAL A 113 ? N VAL A 113 O SER A 206 ? O SER A 206 
# 
_pdbx_entry_details.entry_id                   9NAY 
_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  ? ? -104.74 -70.14 
2 1 ASP A 158 ? ? -152.33 7.04   
# 
_em_3d_fitting.id                1 
_em_3d_fitting.entry_id          9NAY 
_em_3d_fitting.method            ? 
_em_3d_fitting.target_criteria   ? 
_em_3d_fitting.details           ? 
_em_3d_fitting.overall_b_value   ? 
_em_3d_fitting.ref_space         ? 
_em_3d_fitting.ref_protocol      ? 
# 
_em_3d_fitting_list.id                            1 
_em_3d_fitting_list.3d_fitting_id                 1 
_em_3d_fitting_list.pdb_entry_id                  9PAP 
_em_3d_fitting_list.pdb_chain_id                  ? 
_em_3d_fitting_list.pdb_chain_residue_range       ? 
_em_3d_fitting_list.details                       ? 
_em_3d_fitting_list.chain_id                      ? 
_em_3d_fitting_list.chain_residue_range           ? 
_em_3d_fitting_list.source_name                   PDB 
_em_3d_fitting_list.type                          'experimental model' 
_em_3d_fitting_list.accession_code                9PAP 
_em_3d_fitting_list.initial_refinement_model_id   1 
# 
_em_3d_reconstruction.entry_id                    9NAY 
_em_3d_reconstruction.id                          1 
_em_3d_reconstruction.method                      ? 
_em_3d_reconstruction.algorithm                   ? 
_em_3d_reconstruction.citation_id                 ? 
_em_3d_reconstruction.details                     ? 
_em_3d_reconstruction.resolution                  2.5 
_em_3d_reconstruction.resolution_method           'DIFFRACTION PATTERN/LAYERLINES' 
_em_3d_reconstruction.magnification_calibration   ? 
_em_3d_reconstruction.nominal_pixel_size          ? 
_em_3d_reconstruction.actual_pixel_size           ? 
_em_3d_reconstruction.num_particles               ? 
_em_3d_reconstruction.euler_angles_details        ? 
_em_3d_reconstruction.num_class_averages          ? 
_em_3d_reconstruction.refinement_type             ? 
_em_3d_reconstruction.image_processing_id         1 
_em_3d_reconstruction.symmetry_type               '3D CRYSTAL' 
# 
_em_buffer.id            1 
_em_buffer.specimen_id   1 
_em_buffer.name          ? 
_em_buffer.details       ? 
_em_buffer.pH            7 
# 
_em_entity_assembly.id                   1 
_em_entity_assembly.parent_id            0 
_em_entity_assembly.source               NATURAL 
_em_entity_assembly.type                 COMPLEX 
_em_entity_assembly.name                 'Papain-E64-A65 complex' 
_em_entity_assembly.details              ? 
_em_entity_assembly.synonym              ? 
_em_entity_assembly.oligomeric_details   ? 
_em_entity_assembly.entity_id_list       1 
# 
_em_imaging.entry_id                        9NAY 
_em_imaging.id                              1 
_em_imaging.astigmatism                     ? 
_em_imaging.electron_beam_tilt_params       ? 
_em_imaging.residual_tilt                   ? 
_em_imaging.microscope_model                'TFS TALOS F200C' 
_em_imaging.specimen_holder_type            ? 
_em_imaging.specimen_holder_model           ? 
_em_imaging.details                         ? 
_em_imaging.date                            ? 
_em_imaging.accelerating_voltage            200 
_em_imaging.illumination_mode               'FLOOD BEAM' 
_em_imaging.mode                            DIFFRACTION 
_em_imaging.nominal_cs                      ? 
_em_imaging.nominal_defocus_min             10000 
_em_imaging.nominal_defocus_max             10000 
_em_imaging.calibrated_defocus_min          ? 
_em_imaging.calibrated_defocus_max          ? 
_em_imaging.tilt_angle_min                  ? 
_em_imaging.tilt_angle_max                  ? 
_em_imaging.nominal_magnification           ? 
_em_imaging.calibrated_magnification        ? 
_em_imaging.electron_source                 'FIELD EMISSION GUN' 
_em_imaging.citation_id                     ? 
_em_imaging.temperature                     ? 
_em_imaging.detector_distance               ? 
_em_imaging.recording_temperature_minimum   ? 
_em_imaging.recording_temperature_maximum   ? 
_em_imaging.alignment_procedure             ? 
_em_imaging.c2_aperture_diameter            70 
_em_imaging.specimen_id                     1 
_em_imaging.cryogen                         ? 
_em_imaging.objective_aperture              ? 
_em_imaging.microscope_serial_number        ? 
_em_imaging.microscope_version              ? 
# 
_em_vitrification.entry_id              9NAY 
_em_vitrification.id                    1 
_em_vitrification.specimen_id           1 
_em_vitrification.cryogen_name          ETHANE 
_em_vitrification.humidity              ? 
_em_vitrification.temp                  ? 
_em_vitrification.chamber_temperature   ? 
_em_vitrification.instrument            ? 
_em_vitrification.method                ? 
_em_vitrification.time_resolved_state   ? 
_em_vitrification.citation_id           ? 
_em_vitrification.details               ? 
# 
_em_experiment.entry_id                9NAY 
_em_experiment.id                      1 
_em_experiment.reconstruction_method   CRYSTALLOGRAPHY 
_em_experiment.aggregation_state       '3D ARRAY' 
_em_experiment.entity_assembly_id      1 
# 
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 
A1AXI N1   N N N 1   
A1AXI N3   N N N 2   
A1AXI C4   C N N 3   
A1AXI C5   C N S 4   
A1AXI C6   C N N 5   
A1AXI C7   C N N 6   
A1AXI C8   C N N 7   
A1AXI C10  C N N 8   
A1AXI C13  C N N 9   
A1AXI C15  C N N 10  
A1AXI C17  C N N 11  
A1AXI C1   C N N 12  
A1AXI C11  C N N 13  
A1AXI C12  C N N 14  
A1AXI C14  C N N 15  
A1AXI C16  C N N 16  
A1AXI C18  C N N 17  
A1AXI C2   C N N 18  
A1AXI C3   C N S 19  
A1AXI C9   C N N 20  
A1AXI N2   N N N 21  
A1AXI O1   O N N 22  
A1AXI O2   O N N 23  
A1AXI O3   O N N 24  
A1AXI O4   O N N 25  
A1AXI O5   O N N 26  
A1AXI H1   H N N 27  
A1AXI H2   H N N 28  
A1AXI H3   H N N 29  
A1AXI H5   H N N 30  
A1AXI H6   H N N 31  
A1AXI H7   H N N 32  
A1AXI H8   H N N 33  
A1AXI H9   H N N 34  
A1AXI H10  H N N 35  
A1AXI H11  H N N 36  
A1AXI H12  H N N 37  
A1AXI H13  H N N 38  
A1AXI H14  H N N 39  
A1AXI H15  H N N 40  
A1AXI H16  H N N 41  
A1AXI H17  H N N 42  
A1AXI H18  H N N 43  
A1AXI H19  H N N 44  
A1AXI H20  H N N 45  
A1AXI H21  H N N 46  
A1AXI H22  H N N 47  
A1AXI H23  H N N 48  
A1AXI H24  H N N 49  
A1AXI H25  H N N 50  
A1AXI H26  H N N 51  
A1AXI H27  H N N 52  
A1AXI H28  H N N 53  
A1AXI H29  H N N 54  
A1AXI H30  H N N 55  
A1AXI H31  H N N 56  
A1AXI H32  H N N 57  
A1AXI H33  H N N 58  
A1AXI H34  H N N 59  
ALA   N    N N N 60  
ALA   CA   C N S 61  
ALA   C    C N N 62  
ALA   O    O N N 63  
ALA   CB   C N N 64  
ALA   OXT  O N N 65  
ALA   H    H N N 66  
ALA   H2   H N N 67  
ALA   HA   H N N 68  
ALA   HB1  H N N 69  
ALA   HB2  H N N 70  
ALA   HB3  H N N 71  
ALA   HXT  H N N 72  
ARG   N    N N N 73  
ARG   CA   C N S 74  
ARG   C    C N N 75  
ARG   O    O N N 76  
ARG   CB   C N N 77  
ARG   CG   C N N 78  
ARG   CD   C N N 79  
ARG   NE   N N N 80  
ARG   CZ   C N N 81  
ARG   NH1  N N N 82  
ARG   NH2  N N N 83  
ARG   OXT  O N N 84  
ARG   H    H N N 85  
ARG   H2   H N N 86  
ARG   HA   H N N 87  
ARG   HB2  H N N 88  
ARG   HB3  H N N 89  
ARG   HG2  H N N 90  
ARG   HG3  H N N 91  
ARG   HD2  H N N 92  
ARG   HD3  H N N 93  
ARG   HE   H N N 94  
ARG   HH11 H N N 95  
ARG   HH12 H N N 96  
ARG   HH21 H N N 97  
ARG   HH22 H N N 98  
ARG   HXT  H N N 99  
ASN   N    N N N 100 
ASN   CA   C N S 101 
ASN   C    C N N 102 
ASN   O    O N N 103 
ASN   CB   C N N 104 
ASN   CG   C N N 105 
ASN   OD1  O N N 106 
ASN   ND2  N N N 107 
ASN   OXT  O N N 108 
ASN   H    H N N 109 
ASN   H2   H N N 110 
ASN   HA   H N N 111 
ASN   HB2  H N N 112 
ASN   HB3  H N N 113 
ASN   HD21 H N N 114 
ASN   HD22 H N N 115 
ASN   HXT  H N N 116 
ASP   N    N N N 117 
ASP   CA   C N S 118 
ASP   C    C N N 119 
ASP   O    O N N 120 
ASP   CB   C N N 121 
ASP   CG   C N N 122 
ASP   OD1  O N N 123 
ASP   OD2  O N N 124 
ASP   OXT  O N N 125 
ASP   H    H N N 126 
ASP   H2   H N N 127 
ASP   HA   H N N 128 
ASP   HB2  H N N 129 
ASP   HB3  H N N 130 
ASP   HD2  H N N 131 
ASP   HXT  H N N 132 
CYS   N    N N N 133 
CYS   CA   C N R 134 
CYS   C    C N N 135 
CYS   O    O N N 136 
CYS   CB   C N N 137 
CYS   SG   S N N 138 
CYS   OXT  O N N 139 
CYS   H    H N N 140 
CYS   H2   H N N 141 
CYS   HA   H N N 142 
CYS   HB2  H N N 143 
CYS   HB3  H N N 144 
CYS   HG   H N N 145 
CYS   HXT  H N N 146 
GLN   N    N N N 147 
GLN   CA   C N S 148 
GLN   C    C N N 149 
GLN   O    O N N 150 
GLN   CB   C N N 151 
GLN   CG   C N N 152 
GLN   CD   C N N 153 
GLN   OE1  O N N 154 
GLN   NE2  N N N 155 
GLN   OXT  O N N 156 
GLN   H    H N N 157 
GLN   H2   H N N 158 
GLN   HA   H N N 159 
GLN   HB2  H N N 160 
GLN   HB3  H N N 161 
GLN   HG2  H N N 162 
GLN   HG3  H N N 163 
GLN   HE21 H N N 164 
GLN   HE22 H N N 165 
GLN   HXT  H N N 166 
GLU   N    N N N 167 
GLU   CA   C N S 168 
GLU   C    C N N 169 
GLU   O    O N N 170 
GLU   CB   C N N 171 
GLU   CG   C N N 172 
GLU   CD   C N N 173 
GLU   OE1  O N N 174 
GLU   OE2  O N N 175 
GLU   OXT  O N N 176 
GLU   H    H N N 177 
GLU   H2   H N N 178 
GLU   HA   H N N 179 
GLU   HB2  H N N 180 
GLU   HB3  H N N 181 
GLU   HG2  H N N 182 
GLU   HG3  H N N 183 
GLU   HE2  H N N 184 
GLU   HXT  H N N 185 
GLY   N    N N N 186 
GLY   CA   C N N 187 
GLY   C    C N N 188 
GLY   O    O N N 189 
GLY   OXT  O N N 190 
GLY   H    H N N 191 
GLY   H2   H N N 192 
GLY   HA2  H N N 193 
GLY   HA3  H N N 194 
GLY   HXT  H N N 195 
HIS   N    N N N 196 
HIS   CA   C N S 197 
HIS   C    C N N 198 
HIS   O    O N N 199 
HIS   CB   C N N 200 
HIS   CG   C Y N 201 
HIS   ND1  N Y N 202 
HIS   CD2  C Y N 203 
HIS   CE1  C Y N 204 
HIS   NE2  N Y N 205 
HIS   OXT  O N N 206 
HIS   H    H N N 207 
HIS   H2   H N N 208 
HIS   HA   H N N 209 
HIS   HB2  H N N 210 
HIS   HB3  H N N 211 
HIS   HD1  H N N 212 
HIS   HD2  H N N 213 
HIS   HE1  H N N 214 
HIS   HE2  H N N 215 
HIS   HXT  H N N 216 
HOH   O    O N N 217 
HOH   H1   H N N 218 
HOH   H2   H N N 219 
ILE   N    N N N 220 
ILE   CA   C N S 221 
ILE   C    C N N 222 
ILE   O    O N N 223 
ILE   CB   C N S 224 
ILE   CG1  C N N 225 
ILE   CG2  C N N 226 
ILE   CD1  C N N 227 
ILE   OXT  O N N 228 
ILE   H    H N N 229 
ILE   H2   H N N 230 
ILE   HA   H N N 231 
ILE   HB   H N N 232 
ILE   HG12 H N N 233 
ILE   HG13 H N N 234 
ILE   HG21 H N N 235 
ILE   HG22 H N N 236 
ILE   HG23 H N N 237 
ILE   HD11 H N N 238 
ILE   HD12 H N N 239 
ILE   HD13 H N N 240 
ILE   HXT  H N N 241 
LEU   N    N N N 242 
LEU   CA   C N S 243 
LEU   C    C N N 244 
LEU   O    O N N 245 
LEU   CB   C N N 246 
LEU   CG   C N N 247 
LEU   CD1  C N N 248 
LEU   CD2  C N N 249 
LEU   OXT  O N N 250 
LEU   H    H N N 251 
LEU   H2   H N N 252 
LEU   HA   H N N 253 
LEU   HB2  H N N 254 
LEU   HB3  H N N 255 
LEU   HG   H N N 256 
LEU   HD11 H N N 257 
LEU   HD12 H N N 258 
LEU   HD13 H N N 259 
LEU   HD21 H N N 260 
LEU   HD22 H N N 261 
LEU   HD23 H N N 262 
LEU   HXT  H N N 263 
LYS   N    N N N 264 
LYS   CA   C N S 265 
LYS   C    C N N 266 
LYS   O    O N N 267 
LYS   CB   C N N 268 
LYS   CG   C N N 269 
LYS   CD   C N N 270 
LYS   CE   C N N 271 
LYS   NZ   N N N 272 
LYS   OXT  O N N 273 
LYS   H    H N N 274 
LYS   H2   H N N 275 
LYS   HA   H N N 276 
LYS   HB2  H N N 277 
LYS   HB3  H N N 278 
LYS   HG2  H N N 279 
LYS   HG3  H N N 280 
LYS   HD2  H N N 281 
LYS   HD3  H N N 282 
LYS   HE2  H N N 283 
LYS   HE3  H N N 284 
LYS   HZ1  H N N 285 
LYS   HZ2  H N N 286 
LYS   HZ3  H N N 287 
LYS   HXT  H N N 288 
PHE   N    N N N 289 
PHE   CA   C N S 290 
PHE   C    C N N 291 
PHE   O    O N N 292 
PHE   CB   C N N 293 
PHE   CG   C Y N 294 
PHE   CD1  C Y N 295 
PHE   CD2  C Y N 296 
PHE   CE1  C Y N 297 
PHE   CE2  C Y N 298 
PHE   CZ   C Y N 299 
PHE   OXT  O N N 300 
PHE   H    H N N 301 
PHE   H2   H N N 302 
PHE   HA   H N N 303 
PHE   HB2  H N N 304 
PHE   HB3  H N N 305 
PHE   HD1  H N N 306 
PHE   HD2  H N N 307 
PHE   HE1  H N N 308 
PHE   HE2  H N N 309 
PHE   HZ   H N N 310 
PHE   HXT  H N N 311 
PRO   N    N N N 312 
PRO   CA   C N S 313 
PRO   C    C N N 314 
PRO   O    O N N 315 
PRO   CB   C N N 316 
PRO   CG   C N N 317 
PRO   CD   C N N 318 
PRO   OXT  O N N 319 
PRO   H    H N N 320 
PRO   HA   H N N 321 
PRO   HB2  H N N 322 
PRO   HB3  H N N 323 
PRO   HG2  H N N 324 
PRO   HG3  H N N 325 
PRO   HD2  H N N 326 
PRO   HD3  H N N 327 
PRO   HXT  H N N 328 
SER   N    N N N 329 
SER   CA   C N S 330 
SER   C    C N N 331 
SER   O    O N N 332 
SER   CB   C N N 333 
SER   OG   O N N 334 
SER   OXT  O N N 335 
SER   H    H N N 336 
SER   H2   H N N 337 
SER   HA   H N N 338 
SER   HB2  H N N 339 
SER   HB3  H N N 340 
SER   HG   H N N 341 
SER   HXT  H N N 342 
THR   N    N N N 343 
THR   CA   C N S 344 
THR   C    C N N 345 
THR   O    O N N 346 
THR   CB   C N R 347 
THR   OG1  O N N 348 
THR   CG2  C N N 349 
THR   OXT  O N N 350 
THR   H    H N N 351 
THR   H2   H N N 352 
THR   HA   H N N 353 
THR   HB   H N N 354 
THR   HG1  H N N 355 
THR   HG21 H N N 356 
THR   HG22 H N N 357 
THR   HG23 H N N 358 
THR   HXT  H N N 359 
TRP   N    N N N 360 
TRP   CA   C N S 361 
TRP   C    C N N 362 
TRP   O    O N N 363 
TRP   CB   C N N 364 
TRP   CG   C Y N 365 
TRP   CD1  C Y N 366 
TRP   CD2  C Y N 367 
TRP   NE1  N Y N 368 
TRP   CE2  C Y N 369 
TRP   CE3  C Y N 370 
TRP   CZ2  C Y N 371 
TRP   CZ3  C Y N 372 
TRP   CH2  C Y N 373 
TRP   OXT  O N N 374 
TRP   H    H N N 375 
TRP   H2   H N N 376 
TRP   HA   H N N 377 
TRP   HB2  H N N 378 
TRP   HB3  H N N 379 
TRP   HD1  H N N 380 
TRP   HE1  H N N 381 
TRP   HE3  H N N 382 
TRP   HZ2  H N N 383 
TRP   HZ3  H N N 384 
TRP   HH2  H N N 385 
TRP   HXT  H N N 386 
TYR   N    N N N 387 
TYR   CA   C N S 388 
TYR   C    C N N 389 
TYR   O    O N N 390 
TYR   CB   C N N 391 
TYR   CG   C Y N 392 
TYR   CD1  C Y N 393 
TYR   CD2  C Y N 394 
TYR   CE1  C Y N 395 
TYR   CE2  C Y N 396 
TYR   CZ   C Y N 397 
TYR   OH   O N N 398 
TYR   OXT  O N N 399 
TYR   H    H N N 400 
TYR   H2   H N N 401 
TYR   HA   H N N 402 
TYR   HB2  H N N 403 
TYR   HB3  H N N 404 
TYR   HD1  H N N 405 
TYR   HD2  H N N 406 
TYR   HE1  H N N 407 
TYR   HE2  H N N 408 
TYR   HH   H N N 409 
TYR   HXT  H N N 410 
VAL   N    N N N 411 
VAL   CA   C N S 412 
VAL   C    C N N 413 
VAL   O    O N N 414 
VAL   CB   C N N 415 
VAL   CG1  C N N 416 
VAL   CG2  C N N 417 
VAL   OXT  O N N 418 
VAL   H    H N N 419 
VAL   H2   H N N 420 
VAL   HA   H N N 421 
VAL   HB   H N N 422 
VAL   HG11 H N N 423 
VAL   HG12 H N N 424 
VAL   HG13 H N N 425 
VAL   HG21 H N N 426 
VAL   HG22 H N N 427 
VAL   HG23 H N N 428 
VAL   HXT  H N N 429 
# 
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 
A1AXI O2  C1   doub N N 1   
A1AXI C1  O1   sing N N 2   
A1AXI C1  C2   sing N N 3   
A1AXI C2  C3   sing N N 4   
A1AXI C3  O3   sing N N 5   
A1AXI C3  C4   sing N N 6   
A1AXI O4  C4   doub N N 7   
A1AXI C4  N1   sing N N 8   
A1AXI N1  C5   sing N N 9   
A1AXI C5  C10  sing N N 10  
A1AXI C5  C6   sing N N 11  
A1AXI C8  C7   sing N N 12  
A1AXI C8  C9   sing N N 13  
A1AXI C7  C6   sing N N 14  
A1AXI C16 C17  sing N N 15  
A1AXI C16 C15  sing N N 16  
A1AXI N2  C10  sing N N 17  
A1AXI N2  C11  sing N N 18  
A1AXI C12 C11  sing N N 19  
A1AXI C12 C13  sing N N 20  
A1AXI C14 C13  sing N N 21  
A1AXI C14 C15  sing N N 22  
A1AXI C10 O5   doub N N 23  
A1AXI C6  C9   sing N N 24  
A1AXI C17 C18  sing N N 25  
A1AXI C18 N3   sing N N 26  
A1AXI N1  H1   sing N N 27  
A1AXI N3  H2   sing N N 28  
A1AXI N3  H3   sing N N 29  
A1AXI C5  H5   sing N N 30  
A1AXI C6  H6   sing N N 31  
A1AXI C7  H7   sing N N 32  
A1AXI C7  H8   sing N N 33  
A1AXI C8  H9   sing N N 34  
A1AXI C8  H10  sing N N 35  
A1AXI C13 H11  sing N N 36  
A1AXI C13 H12  sing N N 37  
A1AXI C15 H13  sing N N 38  
A1AXI C15 H14  sing N N 39  
A1AXI C17 H15  sing N N 40  
A1AXI C17 H16  sing N N 41  
A1AXI C11 H17  sing N N 42  
A1AXI C11 H18  sing N N 43  
A1AXI C12 H19  sing N N 44  
A1AXI C12 H20  sing N N 45  
A1AXI C14 H21  sing N N 46  
A1AXI C14 H22  sing N N 47  
A1AXI C16 H23  sing N N 48  
A1AXI C16 H24  sing N N 49  
A1AXI C18 H25  sing N N 50  
A1AXI C18 H26  sing N N 51  
A1AXI C2  H27  sing N N 52  
A1AXI C2  H28  sing N N 53  
A1AXI C3  H29  sing N N 54  
A1AXI C9  H30  sing N N 55  
A1AXI C9  H31  sing N N 56  
A1AXI N2  H32  sing N N 57  
A1AXI O1  H33  sing N N 58  
A1AXI O3  H34  sing N N 59  
ALA   N   CA   sing N N 60  
ALA   N   H    sing N N 61  
ALA   N   H2   sing N N 62  
ALA   CA  C    sing N N 63  
ALA   CA  CB   sing N N 64  
ALA   CA  HA   sing N N 65  
ALA   C   O    doub N N 66  
ALA   C   OXT  sing N N 67  
ALA   CB  HB1  sing N N 68  
ALA   CB  HB2  sing N N 69  
ALA   CB  HB3  sing N N 70  
ALA   OXT HXT  sing N N 71  
ARG   N   CA   sing N N 72  
ARG   N   H    sing N N 73  
ARG   N   H2   sing N N 74  
ARG   CA  C    sing N N 75  
ARG   CA  CB   sing N N 76  
ARG   CA  HA   sing N N 77  
ARG   C   O    doub N N 78  
ARG   C   OXT  sing N N 79  
ARG   CB  CG   sing N N 80  
ARG   CB  HB2  sing N N 81  
ARG   CB  HB3  sing N N 82  
ARG   CG  CD   sing N N 83  
ARG   CG  HG2  sing N N 84  
ARG   CG  HG3  sing N N 85  
ARG   CD  NE   sing N N 86  
ARG   CD  HD2  sing N N 87  
ARG   CD  HD3  sing N N 88  
ARG   NE  CZ   sing N N 89  
ARG   NE  HE   sing N N 90  
ARG   CZ  NH1  sing N N 91  
ARG   CZ  NH2  doub N N 92  
ARG   NH1 HH11 sing N N 93  
ARG   NH1 HH12 sing N N 94  
ARG   NH2 HH21 sing N N 95  
ARG   NH2 HH22 sing N N 96  
ARG   OXT HXT  sing N N 97  
ASN   N   CA   sing N N 98  
ASN   N   H    sing N N 99  
ASN   N   H2   sing N N 100 
ASN   CA  C    sing N N 101 
ASN   CA  CB   sing N N 102 
ASN   CA  HA   sing N N 103 
ASN   C   O    doub N N 104 
ASN   C   OXT  sing N N 105 
ASN   CB  CG   sing N N 106 
ASN   CB  HB2  sing N N 107 
ASN   CB  HB3  sing N N 108 
ASN   CG  OD1  doub N N 109 
ASN   CG  ND2  sing N N 110 
ASN   ND2 HD21 sing N N 111 
ASN   ND2 HD22 sing N N 112 
ASN   OXT HXT  sing N N 113 
ASP   N   CA   sing N N 114 
ASP   N   H    sing N N 115 
ASP   N   H2   sing N N 116 
ASP   CA  C    sing N N 117 
ASP   CA  CB   sing N N 118 
ASP   CA  HA   sing N N 119 
ASP   C   O    doub N N 120 
ASP   C   OXT  sing N N 121 
ASP   CB  CG   sing N N 122 
ASP   CB  HB2  sing N N 123 
ASP   CB  HB3  sing N N 124 
ASP   CG  OD1  doub N N 125 
ASP   CG  OD2  sing N N 126 
ASP   OD2 HD2  sing N N 127 
ASP   OXT HXT  sing N N 128 
CYS   N   CA   sing N N 129 
CYS   N   H    sing N N 130 
CYS   N   H2   sing N N 131 
CYS   CA  C    sing N N 132 
CYS   CA  CB   sing N N 133 
CYS   CA  HA   sing N N 134 
CYS   C   O    doub N N 135 
CYS   C   OXT  sing N N 136 
CYS   CB  SG   sing N N 137 
CYS   CB  HB2  sing N N 138 
CYS   CB  HB3  sing N N 139 
CYS   SG  HG   sing N N 140 
CYS   OXT HXT  sing N N 141 
GLN   N   CA   sing N N 142 
GLN   N   H    sing N N 143 
GLN   N   H2   sing N N 144 
GLN   CA  C    sing N N 145 
GLN   CA  CB   sing N N 146 
GLN   CA  HA   sing N N 147 
GLN   C   O    doub N N 148 
GLN   C   OXT  sing N N 149 
GLN   CB  CG   sing N N 150 
GLN   CB  HB2  sing N N 151 
GLN   CB  HB3  sing N N 152 
GLN   CG  CD   sing N N 153 
GLN   CG  HG2  sing N N 154 
GLN   CG  HG3  sing N N 155 
GLN   CD  OE1  doub N N 156 
GLN   CD  NE2  sing N N 157 
GLN   NE2 HE21 sing N N 158 
GLN   NE2 HE22 sing N N 159 
GLN   OXT HXT  sing N N 160 
GLU   N   CA   sing N N 161 
GLU   N   H    sing N N 162 
GLU   N   H2   sing N N 163 
GLU   CA  C    sing N N 164 
GLU   CA  CB   sing N N 165 
GLU   CA  HA   sing N N 166 
GLU   C   O    doub N N 167 
GLU   C   OXT  sing N N 168 
GLU   CB  CG   sing N N 169 
GLU   CB  HB2  sing N N 170 
GLU   CB  HB3  sing N N 171 
GLU   CG  CD   sing N N 172 
GLU   CG  HG2  sing N N 173 
GLU   CG  HG3  sing N N 174 
GLU   CD  OE1  doub N N 175 
GLU   CD  OE2  sing N N 176 
GLU   OE2 HE2  sing N N 177 
GLU   OXT HXT  sing N N 178 
GLY   N   CA   sing N N 179 
GLY   N   H    sing N N 180 
GLY   N   H2   sing N N 181 
GLY   CA  C    sing N N 182 
GLY   CA  HA2  sing N N 183 
GLY   CA  HA3  sing N N 184 
GLY   C   O    doub N N 185 
GLY   C   OXT  sing N N 186 
GLY   OXT HXT  sing N N 187 
HIS   N   CA   sing N N 188 
HIS   N   H    sing N N 189 
HIS   N   H2   sing N N 190 
HIS   CA  C    sing N N 191 
HIS   CA  CB   sing N N 192 
HIS   CA  HA   sing N N 193 
HIS   C   O    doub N N 194 
HIS   C   OXT  sing N N 195 
HIS   CB  CG   sing N N 196 
HIS   CB  HB2  sing N N 197 
HIS   CB  HB3  sing N N 198 
HIS   CG  ND1  sing Y N 199 
HIS   CG  CD2  doub Y N 200 
HIS   ND1 CE1  doub Y N 201 
HIS   ND1 HD1  sing N N 202 
HIS   CD2 NE2  sing Y N 203 
HIS   CD2 HD2  sing N N 204 
HIS   CE1 NE2  sing Y N 205 
HIS   CE1 HE1  sing N N 206 
HIS   NE2 HE2  sing N N 207 
HIS   OXT HXT  sing N N 208 
HOH   O   H1   sing N N 209 
HOH   O   H2   sing N N 210 
ILE   N   CA   sing N N 211 
ILE   N   H    sing N N 212 
ILE   N   H2   sing N N 213 
ILE   CA  C    sing N N 214 
ILE   CA  CB   sing N N 215 
ILE   CA  HA   sing N N 216 
ILE   C   O    doub N N 217 
ILE   C   OXT  sing N N 218 
ILE   CB  CG1  sing N N 219 
ILE   CB  CG2  sing N N 220 
ILE   CB  HB   sing N N 221 
ILE   CG1 CD1  sing N N 222 
ILE   CG1 HG12 sing N N 223 
ILE   CG1 HG13 sing N N 224 
ILE   CG2 HG21 sing N N 225 
ILE   CG2 HG22 sing N N 226 
ILE   CG2 HG23 sing N N 227 
ILE   CD1 HD11 sing N N 228 
ILE   CD1 HD12 sing N N 229 
ILE   CD1 HD13 sing N N 230 
ILE   OXT HXT  sing N N 231 
LEU   N   CA   sing N N 232 
LEU   N   H    sing N N 233 
LEU   N   H2   sing N N 234 
LEU   CA  C    sing N N 235 
LEU   CA  CB   sing N N 236 
LEU   CA  HA   sing N N 237 
LEU   C   O    doub N N 238 
LEU   C   OXT  sing N N 239 
LEU   CB  CG   sing N N 240 
LEU   CB  HB2  sing N N 241 
LEU   CB  HB3  sing N N 242 
LEU   CG  CD1  sing N N 243 
LEU   CG  CD2  sing N N 244 
LEU   CG  HG   sing N N 245 
LEU   CD1 HD11 sing N N 246 
LEU   CD1 HD12 sing N N 247 
LEU   CD1 HD13 sing N N 248 
LEU   CD2 HD21 sing N N 249 
LEU   CD2 HD22 sing N N 250 
LEU   CD2 HD23 sing N N 251 
LEU   OXT HXT  sing N N 252 
LYS   N   CA   sing N N 253 
LYS   N   H    sing N N 254 
LYS   N   H2   sing N N 255 
LYS   CA  C    sing N N 256 
LYS   CA  CB   sing N N 257 
LYS   CA  HA   sing N N 258 
LYS   C   O    doub N N 259 
LYS   C   OXT  sing N N 260 
LYS   CB  CG   sing N N 261 
LYS   CB  HB2  sing N N 262 
LYS   CB  HB3  sing N N 263 
LYS   CG  CD   sing N N 264 
LYS   CG  HG2  sing N N 265 
LYS   CG  HG3  sing N N 266 
LYS   CD  CE   sing N N 267 
LYS   CD  HD2  sing N N 268 
LYS   CD  HD3  sing N N 269 
LYS   CE  NZ   sing N N 270 
LYS   CE  HE2  sing N N 271 
LYS   CE  HE3  sing N N 272 
LYS   NZ  HZ1  sing N N 273 
LYS   NZ  HZ2  sing N N 274 
LYS   NZ  HZ3  sing N N 275 
LYS   OXT HXT  sing N N 276 
PHE   N   CA   sing N N 277 
PHE   N   H    sing N N 278 
PHE   N   H2   sing N N 279 
PHE   CA  C    sing N N 280 
PHE   CA  CB   sing N N 281 
PHE   CA  HA   sing N N 282 
PHE   C   O    doub N N 283 
PHE   C   OXT  sing N N 284 
PHE   CB  CG   sing N N 285 
PHE   CB  HB2  sing N N 286 
PHE   CB  HB3  sing N N 287 
PHE   CG  CD1  doub Y N 288 
PHE   CG  CD2  sing Y N 289 
PHE   CD1 CE1  sing Y N 290 
PHE   CD1 HD1  sing N N 291 
PHE   CD2 CE2  doub Y N 292 
PHE   CD2 HD2  sing N N 293 
PHE   CE1 CZ   doub Y N 294 
PHE   CE1 HE1  sing N N 295 
PHE   CE2 CZ   sing Y N 296 
PHE   CE2 HE2  sing N N 297 
PHE   CZ  HZ   sing N N 298 
PHE   OXT HXT  sing N N 299 
PRO   N   CA   sing N N 300 
PRO   N   CD   sing N N 301 
PRO   N   H    sing N N 302 
PRO   CA  C    sing N N 303 
PRO   CA  CB   sing N N 304 
PRO   CA  HA   sing N N 305 
PRO   C   O    doub N N 306 
PRO   C   OXT  sing N N 307 
PRO   CB  CG   sing N N 308 
PRO   CB  HB2  sing N N 309 
PRO   CB  HB3  sing N N 310 
PRO   CG  CD   sing N N 311 
PRO   CG  HG2  sing N N 312 
PRO   CG  HG3  sing N N 313 
PRO   CD  HD2  sing N N 314 
PRO   CD  HD3  sing N N 315 
PRO   OXT HXT  sing N N 316 
SER   N   CA   sing N N 317 
SER   N   H    sing N N 318 
SER   N   H2   sing N N 319 
SER   CA  C    sing N N 320 
SER   CA  CB   sing N N 321 
SER   CA  HA   sing N N 322 
SER   C   O    doub N N 323 
SER   C   OXT  sing N N 324 
SER   CB  OG   sing N N 325 
SER   CB  HB2  sing N N 326 
SER   CB  HB3  sing N N 327 
SER   OG  HG   sing N N 328 
SER   OXT HXT  sing N N 329 
THR   N   CA   sing N N 330 
THR   N   H    sing N N 331 
THR   N   H2   sing N N 332 
THR   CA  C    sing N N 333 
THR   CA  CB   sing N N 334 
THR   CA  HA   sing N N 335 
THR   C   O    doub N N 336 
THR   C   OXT  sing N N 337 
THR   CB  OG1  sing N N 338 
THR   CB  CG2  sing N N 339 
THR   CB  HB   sing N N 340 
THR   OG1 HG1  sing N N 341 
THR   CG2 HG21 sing N N 342 
THR   CG2 HG22 sing N N 343 
THR   CG2 HG23 sing N N 344 
THR   OXT HXT  sing N N 345 
TRP   N   CA   sing N N 346 
TRP   N   H    sing N N 347 
TRP   N   H2   sing N N 348 
TRP   CA  C    sing N N 349 
TRP   CA  CB   sing N N 350 
TRP   CA  HA   sing N N 351 
TRP   C   O    doub N N 352 
TRP   C   OXT  sing N N 353 
TRP   CB  CG   sing N N 354 
TRP   CB  HB2  sing N N 355 
TRP   CB  HB3  sing N N 356 
TRP   CG  CD1  doub Y N 357 
TRP   CG  CD2  sing Y N 358 
TRP   CD1 NE1  sing Y N 359 
TRP   CD1 HD1  sing N N 360 
TRP   CD2 CE2  doub Y N 361 
TRP   CD2 CE3  sing Y N 362 
TRP   NE1 CE2  sing Y N 363 
TRP   NE1 HE1  sing N N 364 
TRP   CE2 CZ2  sing Y N 365 
TRP   CE3 CZ3  doub Y N 366 
TRP   CE3 HE3  sing N N 367 
TRP   CZ2 CH2  doub Y N 368 
TRP   CZ2 HZ2  sing N N 369 
TRP   CZ3 CH2  sing Y N 370 
TRP   CZ3 HZ3  sing N N 371 
TRP   CH2 HH2  sing N N 372 
TRP   OXT HXT  sing N N 373 
TYR   N   CA   sing N N 374 
TYR   N   H    sing N N 375 
TYR   N   H2   sing N N 376 
TYR   CA  C    sing N N 377 
TYR   CA  CB   sing N N 378 
TYR   CA  HA   sing N N 379 
TYR   C   O    doub N N 380 
TYR   C   OXT  sing N N 381 
TYR   CB  CG   sing N N 382 
TYR   CB  HB2  sing N N 383 
TYR   CB  HB3  sing N N 384 
TYR   CG  CD1  doub Y N 385 
TYR   CG  CD2  sing Y N 386 
TYR   CD1 CE1  sing Y N 387 
TYR   CD1 HD1  sing N N 388 
TYR   CD2 CE2  doub Y N 389 
TYR   CD2 HD2  sing N N 390 
TYR   CE1 CZ   doub Y N 391 
TYR   CE1 HE1  sing N N 392 
TYR   CE2 CZ   sing Y N 393 
TYR   CE2 HE2  sing N N 394 
TYR   CZ  OH   sing N N 395 
TYR   OH  HH   sing N N 396 
TYR   OXT HXT  sing N N 397 
VAL   N   CA   sing N N 398 
VAL   N   H    sing N N 399 
VAL   N   H2   sing N N 400 
VAL   CA  C    sing N N 401 
VAL   CA  CB   sing N N 402 
VAL   CA  HA   sing N N 403 
VAL   C   O    doub N N 404 
VAL   C   OXT  sing N N 405 
VAL   CB  CG1  sing N N 406 
VAL   CB  CG2  sing N N 407 
VAL   CB  HB   sing N N 408 
VAL   CG1 HG11 sing N N 409 
VAL   CG1 HG12 sing N N 410 
VAL   CG1 HG13 sing N N 411 
VAL   CG2 HG21 sing N N 412 
VAL   CG2 HG22 sing N N 413 
VAL   CG2 HG23 sing N N 414 
VAL   OXT HXT  sing N N 415 
# 
_em_3d_crystal_entity.angle_alpha           90 
_em_3d_crystal_entity.angle_beta            90 
_em_3d_crystal_entity.angle_gamma           90 
_em_3d_crystal_entity.image_processing_id   1 
_em_3d_crystal_entity.id                    1 
_em_3d_crystal_entity.length_a              42.20 
_em_3d_crystal_entity.length_b              48.78 
_em_3d_crystal_entity.length_c              100.10 
_em_3d_crystal_entity.space_group_name      'P 21 21 21' 
_em_3d_crystal_entity.space_group_num       19 
# 
_em_ctf_correction.details                  ? 
_em_ctf_correction.em_image_processing_id   1 
_em_ctf_correction.id                       1 
_em_ctf_correction.type                     NONE 
# 
_em_diffraction_shell.em_diffraction_stats_id   1 
_em_diffraction_shell.fourier_space_coverage    85.4 
_em_diffraction_shell.high_resolution           2.5 
_em_diffraction_shell.id                        1 
_em_diffraction_shell.low_resolution            2.6 
_em_diffraction_shell.multiplicity              6.1 
_em_diffraction_shell.num_structure_factors     688 
_em_diffraction_shell.phase_residual            34.1 
# 
_em_diffraction_stats.details                          ? 
_em_diffraction_stats.fourier_space_coverage           86.4 
_em_diffraction_stats.high_resolution                  2.5 
_em_diffraction_stats.id                               1 
_em_diffraction_stats.image_processing_id              1 
_em_diffraction_stats.num_intensities_measured         40867 
_em_diffraction_stats.num_structure_factors            6582 
_em_diffraction_stats.overall_phase_error              ? 
_em_diffraction_stats.overall_phase_residual           ? 
_em_diffraction_stats.phase_error_rejection_criteria   NULL 
_em_diffraction_stats.r_merge                          27.5 
_em_diffraction_stats.r_sym                            ? 
# 
_em_entity_assembly_naturalsource.cell                 ? 
_em_entity_assembly_naturalsource.cellular_location    ? 
_em_entity_assembly_naturalsource.entity_assembly_id   1 
_em_entity_assembly_naturalsource.id                   2 
_em_entity_assembly_naturalsource.ncbi_tax_id          3649 
_em_entity_assembly_naturalsource.organism             'Carica papaya' 
_em_entity_assembly_naturalsource.organelle            ? 
_em_entity_assembly_naturalsource.organ                ? 
_em_entity_assembly_naturalsource.strain               ? 
_em_entity_assembly_naturalsource.tissue               ? 
_em_entity_assembly_naturalsource.details              ? 
# 
_em_image_processing.details              ? 
_em_image_processing.id                   1 
_em_image_processing.image_recording_id   1 
# 
_em_image_recording.average_exposure_time               ? 
_em_image_recording.avg_electron_dose_per_subtomogram   ? 
_em_image_recording.avg_electron_dose_per_image         0.045 
_em_image_recording.details                             ? 
_em_image_recording.detector_mode                       ? 
_em_image_recording.film_or_detector_model              'DIRECT ELECTRON APOLLO (4k x 4k)' 
_em_image_recording.id                                  1 
_em_image_recording.imaging_id                          1 
_em_image_recording.num_diffraction_images              ? 
_em_image_recording.num_grids_imaged                    ? 
_em_image_recording.num_real_images                     ? 
# 
loop_
_em_software.category 
_em_software.details 
_em_software.id 
_em_software.image_processing_id 
_em_software.fitting_id 
_em_software.imaging_id 
_em_software.name 
_em_software.version 
'IMAGE ACQUISITION'             ? 1  ? ? 1 ? ? 
MASKING                         ? 2  ? ? ? ? ? 
'CTF CORRECTION'                ? 3  1 ? ? ? ? 
'LAYERLINE INDEXING'            ? 4  ? ? ? ? ? 
'DIFFRACTION INDEXING'          ? 5  ? ? ? ? ? 
'MODEL FITTING'                 ? 6  ? 1 ? ? ? 
OTHER                           ? 7  ? ? ? ? ? 
'MOLECULAR REPLACEMENT'         ? 8  1 ? ? ? ? 
'LATTICE DISTORTION CORRECTION' ? 9  1 ? ? ? ? 
'SYMMETRY DETERMINATION'        ? 10 1 ? ? ? ? 
'CRYSTALLOGRAPHY MERGING'       ? 11 1 ? ? ? ? 
RECONSTRUCTION                  ? 12 1 ? ? ? ? 
'MODEL REFINEMENT'              ? 13 ? 1 ? ? ? 
'PARTICLE SELECTION'            ? 14 1 1 1 ? ? 
'VOLUME SELECTION'              ? 15 1 1 1 ? ? 
CLASSIFICATION                  ? 16 1 1 1 ? ? 
'INITIAL EULER ASSIGNMENT'      ? 17 1 1 1 ? ? 
'FINAL EULER ASSIGNMENT'        ? 18 1 1 1 ? ? 
'SERIES ALIGNMENT'              ? 19 1 1 1 ? ? 
# 
_em_specimen.concentration           ? 
_em_specimen.details                 ? 
_em_specimen.embedding_applied       NO 
_em_specimen.experiment_id           1 
_em_specimen.id                      1 
_em_specimen.shadowing_applied       NO 
_em_specimen.staining_applied        NO 
_em_specimen.vitrification_applied   YES 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Science Foundation (NSF, United States)' 'United States' DMR-1548924       1 
'Department of Energy (DOE, United States)'        'United States' DE-FC02-02ER63421 2 
'Howard Hughes Medical Institute (HHMI)'           'United States' HHMI-EPI          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          ? 
# 
_atom_sites.entry_id                    9NAY 
_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]   0.023697 
_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]   0.020500 
_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]   0.009990 
_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   ? 22.504  -10.486 20.473 1.00 20.82 ? 1   ILE   A N   1 
ATOM   2    C CA  . ILE   A 1 1   ? 22.254  -9.441  19.485 1.00 30.92 ? 1   ILE   A CA  1 
ATOM   3    C C   . ILE   A 1 1   ? 23.535  -8.651  19.230 1.00 27.33 ? 1   ILE   A C   1 
ATOM   4    O O   . ILE   A 1 1   ? 24.395  -8.555  20.103 1.00 21.69 ? 1   ILE   A O   1 
ATOM   5    C CB  . ILE   A 1 1   ? 21.091  -8.537  19.916 1.00 24.77 ? 1   ILE   A CB  1 
ATOM   6    C CG1 . ILE   A 1 1   ? 21.467  -7.718  21.153 1.00 29.83 ? 1   ILE   A CG1 1 
ATOM   7    C CG2 . ILE   A 1 1   ? 19.851  -9.374  20.158 1.00 27.79 ? 1   ILE   A CG2 1 
ATOM   8    C CD1 . ILE   A 1 1   ? 20.333  -6.821  21.676 1.00 27.80 ? 1   ILE   A CD1 1 
ATOM   9    N N   . PRO   A 1 2   ? 23.672  -8.066  18.044 1.00 40.49 ? 2   PRO   A N   1 
ATOM   10   C CA  . PRO   A 1 2   ? 24.963  -7.489  17.662 1.00 27.84 ? 2   PRO   A CA  1 
ATOM   11   C C   . PRO   A 1 2   ? 25.175  -6.108  18.264 1.00 22.62 ? 2   PRO   A C   1 
ATOM   12   O O   . PRO   A 1 2   ? 24.285  -5.497  18.853 1.00 32.39 ? 2   PRO   A O   1 
ATOM   13   C CB  . PRO   A 1 2   ? 24.876  -7.408  16.130 1.00 20.45 ? 2   PRO   A CB  1 
ATOM   14   C CG  . PRO   A 1 2   ? 23.425  -7.257  15.839 1.00 33.15 ? 2   PRO   A CG  1 
ATOM   15   C CD  . PRO   A 1 2   ? 22.698  -8.028  16.932 1.00 27.70 ? 2   PRO   A CD  1 
ATOM   16   N N   . GLU   A 1 3   ? 26.414  -5.646  18.128 1.00 26.59 ? 3   GLU   A N   1 
ATOM   17   C CA  . GLU   A 1 3   ? 26.808  -4.357  18.672 1.00 24.36 ? 3   GLU   A CA  1 
ATOM   18   C C   . GLU   A 1 3   ? 26.158  -3.213  17.903 1.00 28.81 ? 3   GLU   A C   1 
ATOM   19   O O   . GLU   A 1 3   ? 25.896  -2.149  18.476 1.00 31.56 ? 3   GLU   A O   1 
ATOM   20   C CB  . GLU   A 1 3   ? 28.333  -4.249  18.627 1.00 22.68 ? 3   GLU   A CB  1 
ATOM   21   C CG  . GLU   A 1 3   ? 28.974  -3.515  19.771 1.00 45.33 ? 3   GLU   A CG  1 
ATOM   22   C CD  . GLU   A 1 3   ? 28.935  -4.304  21.049 1.00 62.93 ? 3   GLU   A CD  1 
ATOM   23   O OE1 . GLU   A 1 3   ? 29.489  -5.424  21.062 1.00 52.84 ? 3   GLU   A OE1 1 
ATOM   24   O OE2 . GLU   A 1 3   ? 28.350  -3.802  22.035 1.00 41.99 ? 3   GLU   A OE2 1 
ATOM   25   N N   . TYR   A 1 4   ? 25.887  -3.415  16.614 1.00 25.75 ? 4   TYR   A N   1 
ATOM   26   C CA  . TYR   A 1 4   ? 25.300  -2.396  15.759 1.00 25.17 ? 4   TYR   A CA  1 
ATOM   27   C C   . TYR   A 1 4   ? 24.157  -2.991  14.956 1.00 25.21 ? 4   TYR   A C   1 
ATOM   28   O O   . TYR   A 1 4   ? 24.264  -4.106  14.437 1.00 26.84 ? 4   TYR   A O   1 
ATOM   29   C CB  . TYR   A 1 4   ? 26.330  -1.828  14.786 1.00 20.63 ? 4   TYR   A CB  1 
ATOM   30   C CG  . TYR   A 1 4   ? 27.319  -0.907  15.432 1.00 32.87 ? 4   TYR   A CG  1 
ATOM   31   C CD1 . TYR   A 1 4   ? 27.044  0.453   15.565 1.00 27.84 ? 4   TYR   A CD1 1 
ATOM   32   C CD2 . TYR   A 1 4   ? 28.536  -1.387  15.903 1.00 38.38 ? 4   TYR   A CD2 1 
ATOM   33   C CE1 . TYR   A 1 4   ? 27.960  1.305   16.166 1.00 33.06 ? 4   TYR   A CE1 1 
ATOM   34   C CE2 . TYR   A 1 4   ? 29.451  -0.544  16.499 1.00 38.75 ? 4   TYR   A CE2 1 
ATOM   35   C CZ  . TYR   A 1 4   ? 29.157  0.797   16.626 1.00 23.14 ? 4   TYR   A CZ  1 
ATOM   36   O OH  . TYR   A 1 4   ? 30.058  1.637   17.226 1.00 37.21 ? 4   TYR   A OH  1 
ATOM   37   N N   . VAL   A 1 5   ? 23.063  -2.246  14.856 1.00 31.44 ? 5   VAL   A N   1 
ATOM   38   C CA  . VAL   A 1 5   ? 21.964  -2.565  13.950 1.00 29.97 ? 5   VAL   A CA  1 
ATOM   39   C C   . VAL   A 1 5   ? 21.607  -1.293  13.191 1.00 23.48 ? 5   VAL   A C   1 
ATOM   40   O O   . VAL   A 1 5   ? 21.626  -0.191  13.755 1.00 20.20 ? 5   VAL   A O   1 
ATOM   41   C CB  . VAL   A 1 5   ? 20.733  -3.158  14.669 1.00 25.04 ? 5   VAL   A CB  1 
ATOM   42   C CG1 . VAL   A 1 5   ? 19.561  -3.248  13.705 1.00 20.18 ? 5   VAL   A CG1 1 
ATOM   43   C CG2 . VAL   A 1 5   ? 21.061  -4.529  15.212 1.00 13.41 ? 5   VAL   A CG2 1 
ATOM   44   N N   . ASP   A 1 6   ? 21.347  -1.441  11.899 1.00 25.08 ? 6   ASP   A N   1 
ATOM   45   C CA  . ASP   A 1 6   ? 20.929  -0.315  11.075 1.00 28.86 ? 6   ASP   A CA  1 
ATOM   46   C C   . ASP   A 1 6   ? 20.091  -0.921  9.959  1.00 26.55 ? 6   ASP   A C   1 
ATOM   47   O O   . ASP   A 1 6   ? 20.630  -1.393  8.954  1.00 34.66 ? 6   ASP   A O   1 
ATOM   48   C CB  . ASP   A 1 6   ? 22.138  0.443   10.536 1.00 36.16 ? 6   ASP   A CB  1 
ATOM   49   C CG  . ASP   A 1 6   ? 21.762  1.715   9.789  1.00 36.13 ? 6   ASP   A CG  1 
ATOM   50   O OD1 . ASP   A 1 6   ? 20.583  1.871   9.398  1.00 29.73 ? 6   ASP   A OD1 1 
ATOM   51   O OD2 . ASP   A 1 6   ? 22.660  2.565   9.591  1.00 34.35 ? 6   ASP   A OD2 1 
ATOM   52   N N   . TRP   A 1 7   ? 18.780  -0.913  10.148 1.00 25.56 ? 7   TRP   A N   1 
ATOM   53   C CA  . TRP   A 1 7   ? 17.926  -1.546  9.163  1.00 25.86 ? 7   TRP   A CA  1 
ATOM   54   C C   . TRP   A 1 7   ? 18.000  -0.857  7.814  1.00 23.48 ? 7   TRP   A C   1 
ATOM   55   O O   . TRP   A 1 7   ? 17.598  -1.459  6.813  1.00 28.82 ? 7   TRP   A O   1 
ATOM   56   C CB  . TRP   A 1 7   ? 16.496  -1.581  9.698  1.00 29.03 ? 7   TRP   A CB  1 
ATOM   57   C CG  . TRP   A 1 7   ? 16.375  -2.671  10.688 1.00 19.77 ? 7   TRP   A CG  1 
ATOM   58   C CD1 . TRP   A 1 7   ? 16.245  -2.542  12.044 1.00 23.41 ? 7   TRP   A CD1 1 
ATOM   59   C CD2 . TRP   A 1 7   ? 16.412  -4.076  10.415 1.00 23.74 ? 7   TRP   A CD2 1 
ATOM   60   N NE1 . TRP   A 1 7   ? 16.196  -3.787  12.634 1.00 22.47 ? 7   TRP   A NE1 1 
ATOM   61   C CE2 . TRP   A 1 7   ? 16.298  -4.747  11.658 1.00 23.37 ? 7   TRP   A CE2 1 
ATOM   62   C CE3 . TRP   A 1 7   ? 16.522  -4.837  9.240  1.00 19.28 ? 7   TRP   A CE3 1 
ATOM   63   C CZ2 . TRP   A 1 7   ? 16.291  -6.147  11.760 1.00 19.91 ? 7   TRP   A CZ2 1 
ATOM   64   C CZ3 . TRP   A 1 7   ? 16.515  -6.235  9.341  1.00 21.42 ? 7   TRP   A CZ3 1 
ATOM   65   C CH2 . TRP   A 1 7   ? 16.403  -6.872  10.594 1.00 28.84 ? 7   TRP   A CH2 1 
ATOM   66   N N   . ARG   A 1 8   ? 18.503  0.382   7.753  1.00 24.16 ? 8   ARG   A N   1 
ATOM   67   C CA  . ARG   A 1 8   ? 18.706  1.005   6.450  1.00 19.79 ? 8   ARG   A CA  1 
ATOM   68   C C   . ARG   A 1 8   ? 19.733  0.241   5.629  1.00 22.67 ? 8   ARG   A C   1 
ATOM   69   O O   . ARG   A 1 8   ? 19.567  0.066   4.417  1.00 30.00 ? 8   ARG   A O   1 
ATOM   70   C CB  . ARG   A 1 8   ? 19.178  2.447   6.635  1.00 19.12 ? 8   ARG   A CB  1 
ATOM   71   C CG  . ARG   A 1 8   ? 18.229  3.327   7.392  1.00 26.69 ? 8   ARG   A CG  1 
ATOM   72   C CD  . ARG   A 1 8   ? 18.829  4.696   7.642  1.00 19.21 ? 8   ARG   A CD  1 
ATOM   73   N NE  . ARG   A 1 8   ? 19.973  4.634   8.542  1.00 27.37 ? 8   ARG   A NE  1 
ATOM   74   C CZ  . ARG   A 1 8   ? 20.632  5.699   8.977  1.00 31.99 ? 8   ARG   A CZ  1 
ATOM   75   N NH1 . ARG   A 1 8   ? 20.292  6.924   8.599  1.00 15.95 ? 8   ARG   A NH1 1 
ATOM   76   N NH2 . ARG   A 1 8   ? 21.642  5.533   9.830  1.00 21.21 ? 8   ARG   A NH2 1 
ATOM   77   N N   . GLN   A 1 9   ? 20.788  -0.250  6.279  1.00 30.27 ? 9   GLN   A N   1 
ATOM   78   C CA  . GLN   A 1 9   ? 21.821  -0.980  5.555  1.00 31.93 ? 9   GLN   A CA  1 
ATOM   79   C C   . GLN   A 1 9   ? 21.332  -2.354  5.137  1.00 25.76 ? 9   GLN   A C   1 
ATOM   80   O O   . GLN   A 1 9   ? 21.861  -2.933  4.184  1.00 36.04 ? 9   GLN   A O   1 
ATOM   81   C CB  . GLN   A 1 9   ? 23.095  -1.026  6.391  1.00 31.74 ? 9   GLN   A CB  1 
ATOM   82   C CG  . GLN   A 1 9   ? 23.630  0.394   6.635  1.00 32.84 ? 9   GLN   A CG  1 
ATOM   83   C CD  . GLN   A 1 9   ? 24.884  0.451   7.482  1.00 50.20 ? 9   GLN   A CD  1 
ATOM   84   O OE1 . GLN   A 1 9   ? 25.166  -0.461  8.261  1.00 41.38 ? 9   GLN   A OE1 1 
ATOM   85   N NE2 . GLN   A 1 9   ? 25.638  1.538   7.345  1.00 66.04 ? 9   GLN   A NE2 1 
ATOM   86   N N   . LYS   A 1 10  ? 20.339  -2.884  5.838  1.00 32.07 ? 10  LYS   A N   1 
ATOM   87   C CA  . LYS   A 1 10  ? 19.695  -4.132  5.474  1.00 34.10 ? 10  LYS   A CA  1 
ATOM   88   C C   . LYS   A 1 10  ? 18.593  -3.934  4.443  1.00 29.68 ? 10  LYS   A C   1 
ATOM   89   O O   . LYS   A 1 10  ? 17.937  -4.911  4.060  1.00 38.01 ? 10  LYS   A O   1 
ATOM   90   C CB  . LYS   A 1 10  ? 19.142  -4.803  6.733  1.00 32.16 ? 10  LYS   A CB  1 
ATOM   91   C CG  . LYS   A 1 10  ? 20.210  -5.501  7.558  1.00 36.36 ? 10  LYS   A CG  1 
ATOM   92   C CD  . LYS   A 1 10  ? 20.539  -6.866  6.977  1.00 42.64 ? 10  LYS   A CD  1 
ATOM   93   C CE  . LYS   A 1 10  ? 21.415  -7.653  7.921  1.00 53.90 ? 10  LYS   A CE  1 
ATOM   94   N NZ  . LYS   A 1 10  ? 22.616  -6.857  8.279  1.00 42.74 ? 10  LYS   A NZ  1 
ATOM   95   N N   . GLY   A 1 11  ? 18.381  -2.703  3.982  1.00 26.57 ? 11  GLY   A N   1 
ATOM   96   C CA  . GLY   A 1 11  ? 17.380  -2.427  2.965  1.00 20.49 ? 11  GLY   A CA  1 
ATOM   97   C C   . GLY   A 1 11  ? 15.940  -2.562  3.410  1.00 34.46 ? 11  GLY   A C   1 
ATOM   98   O O   . GLY   A 1 11  ? 15.078  -2.888  2.591  1.00 39.29 ? 11  GLY   A O   1 
ATOM   99   N N   . ALA   A 1 12  ? 15.649  -2.277  4.681  1.00 30.84 ? 12  ALA   A N   1 
ATOM   100  C CA  . ALA   A 1 12  ? 14.332  -2.474  5.278  1.00 21.09 ? 12  ALA   A CA  1 
ATOM   101  C C   . ALA   A 1 12  ? 13.652  -1.161  5.627  1.00 25.11 ? 12  ALA   A C   1 
ATOM   102  O O   . ALA   A 1 12  ? 12.639  -1.167  6.331  1.00 31.41 ? 12  ALA   A O   1 
ATOM   103  C CB  . ALA   A 1 12  ? 14.416  -3.357  6.521  1.00 24.72 ? 12  ALA   A CB  1 
ATOM   104  N N   . VAL   A 1 13  ? 14.188  -0.038  5.165  1.00 23.98 ? 13  VAL   A N   1 
ATOM   105  C CA  . VAL   A 1 13  ? 13.685  1.285   5.511  1.00 24.06 ? 13  VAL   A CA  1 
ATOM   106  C C   . VAL   A 1 13  ? 13.487  2.076   4.230  1.00 20.50 ? 13  VAL   A C   1 
ATOM   107  O O   . VAL   A 1 13  ? 14.410  2.199   3.420  1.00 24.32 ? 13  VAL   A O   1 
ATOM   108  C CB  . VAL   A 1 13  ? 14.635  2.024   6.480  1.00 21.20 ? 13  VAL   A CB  1 
ATOM   109  C CG1 . VAL   A 1 13  ? 14.032  3.343   6.925  1.00 23.35 ? 13  VAL   A CG1 1 
ATOM   110  C CG2 . VAL   A 1 13  ? 14.900  1.164   7.712  1.00 17.93 ? 13  VAL   A CG2 1 
ATOM   111  N N   . THR   A 1 14  ? 12.292  2.624   4.062  1.00 27.53 ? 14  THR   A N   1 
ATOM   112  C CA  . THR   A 1 14  ? 11.984  3.436   2.898  1.00 31.95 ? 14  THR   A CA  1 
ATOM   113  C C   . THR   A 1 14  ? 12.493  4.850   3.134  1.00 20.51 ? 14  THR   A C   1 
ATOM   114  O O   . THR   A 1 14  ? 12.956  5.180   4.229  1.00 21.45 ? 14  THR   A O   1 
ATOM   115  C CB  . THR   A 1 14  ? 10.468  3.443   2.664  1.00 33.25 ? 14  THR   A CB  1 
ATOM   116  O OG1 . THR   A 1 14  ? 9.818   4.206   3.688  1.00 26.95 ? 14  THR   A OG1 1 
ATOM   117  C CG2 . THR   A 1 14  ? 9.923   2.031   2.717  1.00 24.83 ? 14  THR   A CG2 1 
ATOM   118  N N   . PRO   A 1 15  ? 12.461  5.708   2.116  1.00 21.94 ? 15  PRO   A N   1 
ATOM   119  C CA  . PRO   A 1 15  ? 12.933  7.077   2.320  1.00 20.24 ? 15  PRO   A CA  1 
ATOM   120  C C   . PRO   A 1 15  ? 12.175  7.757   3.449  1.00 26.02 ? 15  PRO   A C   1 
ATOM   121  O O   . PRO   A 1 15  ? 11.030  7.423   3.758  1.00 25.13 ? 15  PRO   A O   1 
ATOM   122  C CB  . PRO   A 1 15  ? 12.647  7.749   0.977  1.00 29.18 ? 15  PRO   A CB  1 
ATOM   123  C CG  . PRO   A 1 15  ? 12.758  6.648   0.004  1.00 23.90 ? 15  PRO   A CG  1 
ATOM   124  C CD  . PRO   A 1 15  ? 12.187  5.443   0.689  1.00 19.75 ? 15  PRO   A CD  1 
ATOM   125  N N   . VAL   A 1 16  ? 12.849  8.714   4.079  1.00 22.69 ? 16  VAL   A N   1 
ATOM   126  C CA  . VAL   A 1 16  ? 12.239  9.494   5.143  1.00 20.14 ? 16  VAL   A CA  1 
ATOM   127  C C   . VAL   A 1 16  ? 11.068  10.335  4.621  1.00 20.63 ? 16  VAL   A C   1 
ATOM   128  O O   . VAL   A 1 16  ? 11.132  10.936  3.540  1.00 28.35 ? 16  VAL   A O   1 
ATOM   129  C CB  . VAL   A 1 16  ? 13.321  10.362  5.802  1.00 15.75 ? 16  VAL   A CB  1 
ATOM   130  C CG1 . VAL   A 1 16  ? 12.681  11.479  6.619  1.00 18.45 ? 16  VAL   A CG1 1 
ATOM   131  C CG2 . VAL   A 1 16  ? 14.187  9.497   6.676  1.00 9.72  ? 16  VAL   A CG2 1 
ATOM   132  N N   . LYS   A 1 17  ? 9.985   10.377  5.394  1.00 27.50 ? 17  LYS   A N   1 
ATOM   133  C CA  . LYS   A 1 17  ? 8.779   11.108  5.027  1.00 22.34 ? 17  LYS   A CA  1 
ATOM   134  C C   . LYS   A 1 17  ? 8.634   12.353  5.895  1.00 18.90 ? 17  LYS   A C   1 
ATOM   135  O O   . LYS   A 1 17  ? 9.282   12.500  6.933  1.00 27.48 ? 17  LYS   A O   1 
ATOM   136  C CB  . LYS   A 1 17  ? 7.530   10.230  5.183  1.00 23.63 ? 17  LYS   A CB  1 
ATOM   137  C CG  . LYS   A 1 17  ? 7.576   8.886   4.495  1.00 33.89 ? 17  LYS   A CG  1 
ATOM   138  C CD  . LYS   A 1 17  ? 7.903   9.020   3.019  1.00 45.56 ? 17  LYS   A CD  1 
ATOM   139  C CE  . LYS   A 1 17  ? 7.646   7.703   2.305  1.00 28.34 ? 17  LYS   A CE  1 
ATOM   140  N NZ  . LYS   A 1 17  ? 8.374   6.579   2.969  1.00 35.04 ? 17  LYS   A NZ  1 
ATOM   141  N N   . ASN   A 1 18  ? 7.719   13.224  5.484  1.00 22.91 ? 18  ASN   A N   1 
ATOM   142  C CA  . ASN   A 1 18  ? 7.373   14.430  6.224  1.00 29.55 ? 18  ASN   A CA  1 
ATOM   143  C C   . ASN   A 1 18  ? 5.877   14.430  6.478  1.00 32.06 ? 18  ASN   A C   1 
ATOM   144  O O   . ASN   A 1 18  ? 5.079   14.465  5.535  1.00 25.90 ? 18  ASN   A O   1 
ATOM   145  C CB  . ASN   A 1 18  ? 7.800   15.696  5.473  1.00 27.39 ? 18  ASN   A CB  1 
ATOM   146  C CG  . ASN   A 1 18  ? 7.587   16.965  6.297  1.00 21.96 ? 18  ASN   A CG  1 
ATOM   147  O OD1 . ASN   A 1 18  ? 7.116   16.912  7.436  1.00 34.07 ? 18  ASN   A OD1 1 
ATOM   148  N ND2 . ASN   A 1 18  ? 7.978   18.106  5.737  1.00 28.52 ? 18  ASN   A ND2 1 
ATOM   149  N N   . GLN   A 1 19  ? 5.506   14.373  7.754  1.00 24.46 ? 19  GLN   A N   1 
ATOM   150  C CA  . GLN   A 1 19  ? 4.102   14.376  8.118  1.00 24.44 ? 19  GLN   A CA  1 
ATOM   151  C C   . GLN   A 1 19  ? 3.463   15.743  7.935  1.00 29.97 ? 19  GLN   A C   1 
ATOM   152  O O   . GLN   A 1 19  ? 2.232   15.829  7.906  1.00 35.61 ? 19  GLN   A O   1 
ATOM   153  C CB  . GLN   A 1 19  ? 3.956   13.901  9.560  1.00 26.82 ? 19  GLN   A CB  1 
ATOM   154  C CG  . GLN   A 1 19  ? 4.537   14.870  10.561 1.00 29.29 ? 19  GLN   A CG  1 
ATOM   155  C CD  . GLN   A 1 19  ? 4.525   14.320  11.965 1.00 28.39 ? 19  GLN   A CD  1 
ATOM   156  O OE1 . GLN   A 1 19  ? 5.422   13.567  12.344 1.00 35.12 ? 19  GLN   A OE1 1 
ATOM   157  N NE2 . GLN   A 1 19  ? 3.542   14.718  12.760 1.00 22.44 ? 19  GLN   A NE2 1 
ATOM   158  N N   . GLY   A 1 20  ? 4.254   16.806  7.803  1.00 25.10 ? 20  GLY   A N   1 
ATOM   159  C CA  . GLY   A 1 20  ? 3.592   18.087  7.672  1.00 16.21 ? 20  GLY   A CA  1 
ATOM   160  C C   . GLY   A 1 20  ? 2.996   18.576  8.978  1.00 20.82 ? 20  GLY   A C   1 
ATOM   161  O O   . GLY   A 1 20  ? 3.406   18.185  10.069 1.00 31.60 ? 20  GLY   A O   1 
ATOM   162  N N   . SER   A 1 21  ? 1.988   19.448  8.846  1.00 29.47 ? 21  SER   A N   1 
ATOM   163  C CA  . SER   A 1 21  ? 1.365   20.074  10.010 1.00 26.25 ? 21  SER   A CA  1 
ATOM   164  C C   . SER   A 1 21  ? 0.452   19.115  10.755 1.00 36.37 ? 21  SER   A C   1 
ATOM   165  O O   . SER   A 1 21  ? 0.203   19.308  11.950 1.00 65.18 ? 21  SER   A O   1 
ATOM   166  C CB  . SER   A 1 21  ? 0.569   21.303  9.551  1.00 35.96 ? 21  SER   A CB  1 
ATOM   167  O OG  . SER   A 1 21  ? 1.448   22.386  9.287  1.00 58.15 ? 21  SER   A OG  1 
ATOM   168  N N   . CYS   A 1 22  ? 0.035   18.049  10.086 1.00 32.70 ? 22  CYS   A N   1 
ATOM   169  C CA  . CYS   A 1 22  ? -0.889  17.061  10.618 1.00 37.24 ? 22  CYS   A CA  1 
ATOM   170  C C   . CYS   A 1 22  ? -0.259  16.269  11.756 1.00 34.83 ? 22  CYS   A C   1 
ATOM   171  O O   . CYS   A 1 22  ? 0.914   15.882  11.697 1.00 26.26 ? 22  CYS   A O   1 
ATOM   172  C CB  . CYS   A 1 22  ? -1.312  16.098  9.502  1.00 31.73 ? 22  CYS   A CB  1 
ATOM   173  S SG  . CYS   A 1 22  ? -2.338  14.714  10.060 1.00 59.39 ? 22  CYS   A SG  1 
ATOM   174  N N   . GLY   A 1 23  ? -1.030  16.062  12.817 1.00 24.34 ? 23  GLY   A N   1 
ATOM   175  C CA  . GLY   A 1 23  ? -0.542  15.242  13.909 1.00 28.62 ? 23  GLY   A CA  1 
ATOM   176  C C   . GLY   A 1 23  ? -0.664  13.763  13.589 1.00 25.97 ? 23  GLY   A C   1 
ATOM   177  O O   . GLY   A 1 23  ? -1.332  13.029  14.319 1.00 24.51 ? 23  GLY   A O   1 
ATOM   178  N N   . SER   A 1 24  ? 0.001   13.293  12.534 1.00 32.43 ? 24  SER   A N   1 
ATOM   179  C CA  . SER   A 1 24  ? -0.162  11.917  12.077 1.00 27.91 ? 24  SER   A CA  1 
ATOM   180  C C   . SER   A 1 24  ? 1.030   11.019  12.373 1.00 21.37 ? 24  SER   A C   1 
ATOM   181  O O   . SER   A 1 24  ? 1.121   9.931   11.793 1.00 20.01 ? 24  SER   A O   1 
ATOM   182  C CB  . SER   A 1 24  ? -0.425  11.899  10.572 1.00 29.53 ? 24  SER   A CB  1 
ATOM   183  O OG  . SER   A 1 24  ? 0.562   12.651  9.883  1.00 29.95 ? 24  SER   A OG  1 
ATOM   184  N N   . CYS   A 1 25  ? 1.940   11.434  13.255 1.00 24.56 ? 25  CYS   A N   1 
ATOM   185  C CA  . CYS   A 1 25  ? 3.175   10.674  13.443 1.00 28.08 ? 25  CYS   A CA  1 
ATOM   186  C C   . CYS   A 1 25  ? 2.905   9.235   13.859 1.00 18.61 ? 25  CYS   A C   1 
ATOM   187  O O   . CYS   A 1 25  ? 3.710   8.347   13.564 1.00 16.31 ? 25  CYS   A O   1 
ATOM   188  C CB  . CYS   A 1 25  ? 4.050   11.350  14.495 1.00 19.66 ? 25  CYS   A CB  1 
ATOM   189  S SG  . CYS   A 1 25  ? 3.105   11.690  16.002 1.00 33.02 ? 25  CYS   A SG  1 
ATOM   190  N N   . TRP   A 1 26  ? 1.809   8.988   14.581 1.00 18.85 ? 26  TRP   A N   1 
ATOM   191  C CA  . TRP   A 1 26  ? 1.492   7.622   14.973 1.00 18.84 ? 26  TRP   A CA  1 
ATOM   192  C C   . TRP   A 1 26  ? 1.337   6.736   13.750 1.00 24.54 ? 26  TRP   A C   1 
ATOM   193  O O   . TRP   A 1 26  ? 1.837   5.602   13.714 1.00 28.63 ? 26  TRP   A O   1 
ATOM   194  C CB  . TRP   A 1 26  ? 0.206   7.609   15.795 1.00 19.95 ? 26  TRP   A CB  1 
ATOM   195  C CG  . TRP   A 1 26  ? -0.964  8.263   15.087 1.00 29.72 ? 26  TRP   A CG  1 
ATOM   196  C CD1 . TRP   A 1 26  ? -1.280  9.603   15.069 1.00 32.10 ? 26  TRP   A CD1 1 
ATOM   197  C CD2 . TRP   A 1 26  ? -1.981  7.607   14.316 1.00 25.69 ? 26  TRP   A CD2 1 
ATOM   198  N NE1 . TRP   A 1 26  ? -2.424  9.812   14.328 1.00 23.54 ? 26  TRP   A NE1 1 
ATOM   199  C CE2 . TRP   A 1 26  ? -2.874  8.605   13.859 1.00 25.64 ? 26  TRP   A CE2 1 
ATOM   200  C CE3 . TRP   A 1 26  ? -2.219  6.275   13.957 1.00 28.00 ? 26  TRP   A CE3 1 
ATOM   201  C CZ2 . TRP   A 1 26  ? -3.984  8.308   13.071 1.00 22.96 ? 26  TRP   A CZ2 1 
ATOM   202  C CZ3 . TRP   A 1 26  ? -3.333  5.987   13.162 1.00 25.95 ? 26  TRP   A CZ3 1 
ATOM   203  C CH2 . TRP   A 1 26  ? -4.191  7.000   12.733 1.00 21.79 ? 26  TRP   A CH2 1 
ATOM   204  N N   . ALA   A 1 27  ? 0.769   7.290   12.689 1.00 24.50 ? 27  ALA   A N   1 
ATOM   205  C CA  . ALA   A 1 27  ? 0.635   6.519   11.469 1.00 22.26 ? 27  ALA   A CA  1 
ATOM   206  C C   . ALA   A 1 27  ? 1.960   6.387   10.728 1.00 23.46 ? 27  ALA   A C   1 
ATOM   207  O O   . ALA   A 1 27  ? 2.277   5.301   10.245 1.00 23.24 ? 27  ALA   A O   1 
ATOM   208  C CB  . ALA   A 1 27  ? -0.415  7.159   10.565 1.00 25.56 ? 27  ALA   A CB  1 
ATOM   209  N N   . PHE   A 1 28  ? 2.784   7.440   10.696 1.00 14.47 ? 28  PHE   A N   1 
ATOM   210  C CA  . PHE   A 1 28  ? 4.083   7.325   10.038 1.00 23.25 ? 28  PHE   A CA  1 
ATOM   211  C C   . PHE   A 1 28  ? 4.959   6.294   10.733 1.00 16.10 ? 28  PHE   A C   1 
ATOM   212  O O   . PHE   A 1 28  ? 5.567   5.443   10.078 1.00 17.58 ? 28  PHE   A O   1 
ATOM   213  C CB  . PHE   A 1 28  ? 4.766   8.689   10.000 1.00 20.60 ? 28  PHE   A CB  1 
ATOM   214  C CG  . PHE   A 1 28  ? 4.268   9.557   8.902  1.00 17.67 ? 28  PHE   A CG  1 
ATOM   215  C CD1 . PHE   A 1 28  ? 3.094   10.262  9.049  1.00 19.57 ? 28  PHE   A CD1 1 
ATOM   216  C CD2 . PHE   A 1 28  ? 4.952   9.632   7.693  1.00 28.15 ? 28  PHE   A CD2 1 
ATOM   217  C CE1 . PHE   A 1 28  ? 2.609   11.043  8.022  1.00 30.35 ? 28  PHE   A CE1 1 
ATOM   218  C CE2 . PHE   A 1 28  ? 4.477   10.419  6.666  1.00 28.77 ? 28  PHE   A CE2 1 
ATOM   219  C CZ  . PHE   A 1 28  ? 3.305   11.125  6.830  1.00 23.96 ? 28  PHE   A CZ  1 
ATOM   220  N N   . SER   A 1 29  ? 5.023   6.359   12.063 1.00 17.22 ? 29  SER   A N   1 
ATOM   221  C CA  . SER   A 1 29  ? 5.761   5.391   12.873 1.00 18.30 ? 29  SER   A CA  1 
ATOM   222  C C   . SER   A 1 29  ? 5.285   3.966   12.592 1.00 18.27 ? 29  SER   A C   1 
ATOM   223  O O   . SER   A 1 29  ? 6.090   3.053   12.316 1.00 21.59 ? 29  SER   A O   1 
ATOM   224  C CB  . SER   A 1 29  ? 5.582   5.747   14.347 1.00 9.53  ? 29  SER   A CB  1 
ATOM   225  O OG  . SER   A 1 29  ? 6.117   4.760   15.199 1.00 19.92 ? 29  SER   A OG  1 
ATOM   226  N N   . ALA   A 1 30  ? 3.964   3.763   12.643 1.00 16.66 ? 30  ALA   A N   1 
ATOM   227  C CA  . ALA   A 1 30  ? 3.422   2.446   12.363 1.00 23.92 ? 30  ALA   A CA  1 
ATOM   228  C C   . ALA   A 1 30  ? 3.836   1.965   10.967 1.00 27.58 ? 30  ALA   A C   1 
ATOM   229  O O   . ALA   A 1 30  ? 4.302   0.825   10.802 1.00 22.06 ? 30  ALA   A O   1 
ATOM   230  C CB  . ALA   A 1 30  ? 1.898   2.526   12.490 1.00 13.50 ? 30  ALA   A CB  1 
ATOM   231  N N   . VAL   A 1 31  ? 3.708   2.836   9.953  1.00 24.14 ? 31  VAL   A N   1 
ATOM   232  C CA  . VAL   A 1 31  ? 4.048   2.443   8.586  1.00 19.00 ? 31  VAL   A CA  1 
ATOM   233  C C   . VAL   A 1 31  ? 5.520   2.088   8.458  1.00 27.75 ? 31  VAL   A C   1 
ATOM   234  O O   . VAL   A 1 31  ? 5.879   1.169   7.716  1.00 30.78 ? 31  VAL   A O   1 
ATOM   235  C CB  . VAL   A 1 31  ? 3.652   3.523   7.569  1.00 23.11 ? 31  VAL   A CB  1 
ATOM   236  C CG1 . VAL   A 1 31  ? 3.791   2.956   6.172  1.00 39.53 ? 31  VAL   A CG1 1 
ATOM   237  C CG2 . VAL   A 1 31  ? 2.198   3.862   7.734  1.00 33.72 ? 31  VAL   A CG2 1 
ATOM   238  N N   . VAL   A 1 32  ? 6.403   2.837   9.128  1.00 22.91 ? 32  VAL   A N   1 
ATOM   239  C CA  . VAL   A 1 32  ? 7.826   2.495   9.070  1.00 34.45 ? 32  VAL   A CA  1 
ATOM   240  C C   . VAL   A 1 32  ? 8.021   1.069   9.532  1.00 24.39 ? 32  VAL   A C   1 
ATOM   241  O O   . VAL   A 1 32  ? 8.719   0.261   8.891  1.00 23.41 ? 32  VAL   A O   1 
ATOM   242  C CB  . VAL   A 1 32  ? 8.676   3.447   9.931  1.00 35.10 ? 32  VAL   A CB  1 
ATOM   243  C CG1 . VAL   A 1 32  ? 10.134  2.984   9.891  1.00 13.48 ? 32  VAL   A CG1 1 
ATOM   244  C CG2 . VAL   A 1 32  ? 8.521   4.908   9.504  1.00 23.17 ? 32  VAL   A CG2 1 
ATOM   245  N N   . THR   A 1 33  ? 7.325   0.715   10.608 1.00 25.45 ? 33  THR   A N   1 
ATOM   246  C CA  . THR   A 1 33  ? 7.493   -0.619  11.153 1.00 27.85 ? 33  THR   A CA  1 
ATOM   247  C C   . THR   A 1 33  ? 6.907   -1.697  10.235 1.00 19.63 ? 33  THR   A C   1 
ATOM   248  O O   . THR   A 1 33  ? 7.489   -2.787  10.101 1.00 19.35 ? 33  THR   A O   1 
ATOM   249  C CB  . THR   A 1 33  ? 6.811   -0.623  12.515 1.00 30.03 ? 33  THR   A CB  1 
ATOM   250  O OG1 . THR   A 1 33  ? 6.954   0.678   13.103 1.00 26.32 ? 33  THR   A OG1 1 
ATOM   251  C CG2 . THR   A 1 33  ? 7.467   -1.559  13.405 1.00 39.30 ? 33  THR   A CG2 1 
ATOM   252  N N   . ILE   A 1 34  ? 5.836   -1.371  9.507  1.00 26.67 ? 34  ILE   A N   1 
ATOM   253  C CA  . ILE   A 1 34  ? 5.253   -2.335  8.568  1.00 26.46 ? 34  ILE   A CA  1 
ATOM   254  C C   . ILE   A 1 34  ? 6.154   -2.531  7.354  1.00 30.92 ? 34  ILE   A C   1 
ATOM   255  O O   . ILE   A 1 34  ? 6.389   -3.662  6.916  1.00 34.64 ? 34  ILE   A O   1 
ATOM   256  C CB  . ILE   A 1 34  ? 3.827   -1.927  8.156  1.00 27.10 ? 34  ILE   A CB  1 
ATOM   257  C CG1 . ILE   A 1 34  ? 2.911   -1.890  9.374  1.00 23.44 ? 34  ILE   A CG1 1 
ATOM   258  C CG2 . ILE   A 1 34  ? 3.271   -2.858  7.082  1.00 18.21 ? 34  ILE   A CG2 1 
ATOM   259  C CD1 . ILE   A 1 34  ? 1.761   -0.937  9.195  1.00 46.50 ? 34  ILE   A CD1 1 
ATOM   260  N N   . GLU   A 1 35  ? 6.629   -1.431  6.766  1.00 27.62 ? 35  GLU   A N   1 
ATOM   261  C CA  . GLU   A 1 35  ? 7.566   -1.501  5.644  1.00 31.71 ? 35  GLU   A CA  1 
ATOM   262  C C   . GLU   A 1 35  ? 8.760   -2.372  6.010  1.00 33.13 ? 35  GLU   A C   1 
ATOM   263  O O   . GLU   A 1 35  ? 9.187   -3.241  5.229  1.00 31.49 ? 35  GLU   A O   1 
ATOM   264  C CB  . GLU   A 1 35  ? 8.028   -0.087  5.296  1.00 27.96 ? 35  GLU   A CB  1 
ATOM   265  C CG  . GLU   A 1 35  ? 6.904   0.830   4.823  1.00 33.19 ? 35  GLU   A CG  1 
ATOM   266  C CD  . GLU   A 1 35  ? 7.312   2.306   4.787  1.00 44.02 ? 35  GLU   A CD  1 
ATOM   267  O OE1 . GLU   A 1 35  ? 6.662   3.090   4.058  1.00 43.28 ? 35  GLU   A OE1 1 
ATOM   268  O OE2 . GLU   A 1 35  ? 8.258   2.692   5.516  1.00 43.06 ? 35  GLU   A OE2 1 
ATOM   269  N N   . GLY   A 1 36  ? 9.237   -2.224  7.250  1.00 25.81 ? 36  GLY   A N   1 
ATOM   270  C CA  . GLY   A 1 36  ? 10.394  -2.990  7.667  1.00 31.16 ? 36  GLY   A CA  1 
ATOM   271  C C   . GLY   A 1 36  ? 10.082  -4.468  7.759  1.00 24.63 ? 36  GLY   A C   1 
ATOM   272  O O   . GLY   A 1 36  ? 10.853  -5.304  7.277  1.00 26.59 ? 36  GLY   A O   1 
ATOM   273  N N   . ILE   A 1 37  ? 8.985   -4.818  8.436  1.00 22.19 ? 37  ILE   A N   1 
ATOM   274  C CA  . ILE   A 1 37  ? 8.718   -6.245  8.601  1.00 28.14 ? 37  ILE   A CA  1 
ATOM   275  C C   . ILE   A 1 37  ? 8.338   -6.890  7.268  1.00 34.94 ? 37  ILE   A C   1 
ATOM   276  O O   . ILE   A 1 37  ? 8.650   -8.067  7.037  1.00 40.58 ? 37  ILE   A O   1 
ATOM   277  C CB  . ILE   A 1 37  ? 7.676   -6.536  9.689  1.00 31.26 ? 37  ILE   A CB  1 
ATOM   278  C CG1 . ILE   A 1 37  ? 7.791   -8.031  10.036 1.00 23.75 ? 37  ILE   A CG1 1 
ATOM   279  C CG2 . ILE   A 1 37  ? 6.283   -6.139  9.222  1.00 32.24 ? 37  ILE   A CG2 1 
ATOM   280  C CD1 . ILE   A 1 37  ? 7.817   -8.374  11.447 1.00 34.62 ? 37  ILE   A CD1 1 
ATOM   281  N N   . ILE   A 1 38  ? 7.714   -6.142  6.353  1.00 30.25 ? 38  ILE   A N   1 
ATOM   282  C CA  . ILE   A 1 38  ? 7.412   -6.733  5.056  1.00 35.74 ? 38  ILE   A CA  1 
ATOM   283  C C   . ILE   A 1 38  ? 8.709   -7.002  4.300  1.00 34.61 ? 38  ILE   A C   1 
ATOM   284  O O   . ILE   A 1 38  ? 8.866   -8.058  3.679  1.00 35.26 ? 38  ILE   A O   1 
ATOM   285  C CB  . ILE   A 1 38  ? 6.464   -5.830  4.249  1.00 41.31 ? 38  ILE   A CB  1 
ATOM   286  C CG1 . ILE   A 1 38  ? 5.080   -5.707  4.901  1.00 35.99 ? 38  ILE   A CG1 1 
ATOM   287  C CG2 . ILE   A 1 38  ? 6.242   -6.416  2.851  1.00 31.69 ? 38  ILE   A CG2 1 
ATOM   288  C CD1 . ILE   A 1 38  ? 4.420   -6.998  5.197  1.00 31.38 ? 38  ILE   A CD1 1 
ATOM   289  N N   . LYS   A 1 39  ? 9.685   -6.091  4.390  1.00 26.37 ? 39  LYS   A N   1 
ATOM   290  C CA  . LYS   A 1 39  ? 10.987  -6.353  3.772  1.00 40.81 ? 39  LYS   A CA  1 
ATOM   291  C C   . LYS   A 1 39  ? 11.697  -7.538  4.425  1.00 33.68 ? 39  LYS   A C   1 
ATOM   292  O O   . LYS   A 1 39  ? 12.270  -8.386  3.734  1.00 35.19 ? 39  LYS   A O   1 
ATOM   293  C CB  . LYS   A 1 39  ? 11.878  -5.111  3.853  1.00 43.30 ? 39  LYS   A CB  1 
ATOM   294  C CG  . LYS   A 1 39  ? 13.346  -5.382  3.509  1.00 32.85 ? 39  LYS   A CG  1 
ATOM   295  C CD  . LYS   A 1 39  ? 13.495  -5.747  2.028  1.00 45.72 ? 39  LYS   A CD  1 
ATOM   296  C CE  . LYS   A 1 39  ? 14.952  -6.005  1.650  1.00 41.06 ? 39  LYS   A CE  1 
ATOM   297  N NZ  . LYS   A 1 39  ? 15.521  -7.141  2.425  1.00 48.34 ? 39  LYS   A NZ  1 
ATOM   298  N N   . ILE   A 1 40  ? 11.698  -7.592  5.761  1.00 30.32 ? 40  ILE   A N   1 
ATOM   299  C CA  . ILE   A 1 40  ? 12.375  -8.678  6.474  1.00 49.36 ? 40  ILE   A CA  1 
ATOM   300  C C   . ILE   A 1 40  ? 11.791  -10.038 6.110  1.00 37.20 ? 40  ILE   A C   1 
ATOM   301  O O   . ILE   A 1 40  ? 12.532  -10.998 5.857  1.00 23.89 ? 40  ILE   A O   1 
ATOM   302  C CB  . ILE   A 1 40  ? 12.315  -8.428  8.002  1.00 40.24 ? 40  ILE   A CB  1 
ATOM   303  C CG1 . ILE   A 1 40  ? 13.274  -7.307  8.416  1.00 28.26 ? 40  ILE   A CG1 1 
ATOM   304  C CG2 . ILE   A 1 40  ? 12.576  -9.696  8.810  1.00 34.68 ? 40  ILE   A CG2 1 
ATOM   305  C CD1 . ILE   A 1 40  ? 12.950  -6.705  9.752  1.00 27.06 ? 40  ILE   A CD1 1 
ATOM   306  N N   . ARG   A 1 41  ? 10.462  -10.137 6.041  1.00 29.95 ? 41  ARG   A N   1 
ATOM   307  C CA  . ARG   A 1 41  ? 9.819   -11.426 5.794  1.00 29.08 ? 41  ARG   A CA  1 
ATOM   308  C C   . ARG   A 1 41  ? 9.704   -11.807 4.321  1.00 30.86 ? 41  ARG   A C   1 
ATOM   309  O O   . ARG   A 1 41  ? 9.717   -13.003 4.010  1.00 36.82 ? 41  ARG   A O   1 
ATOM   310  C CB  . ARG   A 1 41  ? 8.460   -11.466 6.474  1.00 35.39 ? 41  ARG   A CB  1 
ATOM   311  C CG  . ARG   A 1 41  ? 8.646   -11.484 7.959  1.00 46.35 ? 41  ARG   A CG  1 
ATOM   312  C CD  . ARG   A 1 41  ? 8.249   -12.841 8.461  1.00 51.78 ? 41  ARG   A CD  1 
ATOM   313  N NE  . ARG   A 1 41  ? 8.463   -12.982 9.892  1.00 47.30 ? 41  ARG   A NE  1 
ATOM   314  C CZ  . ARG   A 1 41  ? 9.539   -13.553 10.415 1.00 72.68 ? 41  ARG   A CZ  1 
ATOM   315  N NH1 . ARG   A 1 41  ? 10.473  -14.095 9.647  1.00 66.16 ? 41  ARG   A NH1 1 
ATOM   316  N NH2 . ARG   A 1 41  ? 9.670   -13.601 11.738 1.00 60.60 ? 41  ARG   A NH2 1 
ATOM   317  N N   . THR   A 1 42  ? 9.585   -10.842 3.399  1.00 32.49 ? 42  THR   A N   1 
ATOM   318  C CA  . THR   A 1 42  ? 9.293   -11.169 2.009  1.00 39.15 ? 42  THR   A CA  1 
ATOM   319  C C   . THR   A 1 42  ? 10.403  -10.792 1.045  1.00 35.09 ? 42  THR   A C   1 
ATOM   320  O O   . THR   A 1 42  ? 10.380  -11.259 -0.101 1.00 37.67 ? 42  THR   A O   1 
ATOM   321  C CB  . THR   A 1 42  ? 8.003   -10.474 1.532  1.00 35.44 ? 42  THR   A CB  1 
ATOM   322  O OG1 . THR   A 1 42  ? 8.267   -9.089  1.267  1.00 31.81 ? 42  THR   A OG1 1 
ATOM   323  C CG2 . THR   A 1 42  ? 6.913   -10.585 2.584  1.00 40.15 ? 42  THR   A CG2 1 
ATOM   324  N N   . GLY   A 1 43  ? 11.363  -9.967  1.461  1.00 27.67 ? 43  GLY   A N   1 
ATOM   325  C CA  . GLY   A 1 43  ? 12.437  -9.549  0.591  1.00 23.17 ? 43  GLY   A CA  1 
ATOM   326  C C   . GLY   A 1 43  ? 12.158  -8.303  -0.214 1.00 30.97 ? 43  GLY   A C   1 
ATOM   327  O O   . GLY   A 1 43  ? 13.070  -7.801  -0.883 1.00 31.31 ? 43  GLY   A O   1 
ATOM   328  N N   . ASN   A 1 44  ? 10.945  -7.765  -0.148 1.00 33.49 ? 44  ASN   A N   1 
ATOM   329  C CA  . ASN   A 1 44  ? 10.555  -6.603  -0.931 1.00 26.07 ? 44  ASN   A CA  1 
ATOM   330  C C   . ASN   A 1 44  ? 10.356  -5.406  -0.017 1.00 30.95 ? 44  ASN   A C   1 
ATOM   331  O O   . ASN   A 1 44  ? 9.695   -5.506  1.020  1.00 29.23 ? 44  ASN   A O   1 
ATOM   332  C CB  . ASN   A 1 44  ? 9.271   -6.876  -1.721 1.00 41.97 ? 44  ASN   A CB  1 
ATOM   333  C CG  . ASN   A 1 44  ? 9.373   -8.114  -2.619 1.00 51.85 ? 44  ASN   A CG  1 
ATOM   334  O OD1 . ASN   A 1 44  ? 10.441  -8.724  -2.763 1.00 32.09 ? 44  ASN   A OD1 1 
ATOM   335  N ND2 . ASN   A 1 44  ? 8.250   -8.486  -3.224 1.00 40.64 ? 44  ASN   A ND2 1 
ATOM   336  N N   . LEU   A 1 45  ? 10.934  -4.283  -0.406 1.00 35.64 ? 45  LEU   A N   1 
ATOM   337  C CA  . LEU   A 1 45  ? 10.722  -3.013  0.271  1.00 32.83 ? 45  LEU   A CA  1 
ATOM   338  C C   . LEU   A 1 45  ? 9.638   -2.240  -0.468 1.00 34.32 ? 45  LEU   A C   1 
ATOM   339  O O   . LEU   A 1 45  ? 9.802   -1.893  -1.643 1.00 34.03 ? 45  LEU   A O   1 
ATOM   340  C CB  . LEU   A 1 45  ? 12.010  -2.197  0.342  1.00 25.04 ? 45  LEU   A CB  1 
ATOM   341  C CG  . LEU   A 1 45  ? 11.859  -0.900  1.145  1.00 22.70 ? 45  LEU   A CG  1 
ATOM   342  C CD1 . LEU   A 1 45  ? 11.515  -1.187  2.611  1.00 20.39 ? 45  LEU   A CD1 1 
ATOM   343  C CD2 . LEU   A 1 45  ? 13.128  -0.045  1.022  1.00 29.48 ? 45  LEU   A CD2 1 
ATOM   344  N N   . ASN   A 1 46  ? 8.530   -1.984  0.211  1.00 23.39 ? 46  ASN   A N   1 
ATOM   345  C CA  . ASN   A 1 46  ? 7.446   -1.208  -0.368 1.00 36.64 ? 46  ASN   A CA  1 
ATOM   346  C C   . ASN   A 1 46  ? 7.123   -0.050  0.550  1.00 25.18 ? 46  ASN   A C   1 
ATOM   347  O O   . ASN   A 1 46  ? 7.443   -0.068  1.737  1.00 29.59 ? 46  ASN   A O   1 
ATOM   348  C CB  . ASN   A 1 46  ? 6.177   -2.010  -0.554 1.00 39.44 ? 46  ASN   A CB  1 
ATOM   349  C CG  . ASN   A 1 46  ? 6.409   -3.311  -1.243 1.00 31.88 ? 46  ASN   A CG  1 
ATOM   350  O OD1 . ASN   A 1 46  ? 6.351   -4.371  -0.621 1.00 32.62 ? 46  ASN   A OD1 1 
ATOM   351  N ND2 . ASN   A 1 46  ? 6.629   -3.252  -2.555 1.00 33.27 ? 46  ASN   A ND2 1 
ATOM   352  N N   . GLU   A 1 47  ? 6.484   0.960   -0.008 1.00 20.14 ? 47  GLU   A N   1 
ATOM   353  C CA  . GLU   A 1 47  ? 5.958   2.039   0.805  1.00 33.22 ? 47  GLU   A CA  1 
ATOM   354  C C   . GLU   A 1 47  ? 4.480   1.790   1.031  1.00 25.06 ? 47  GLU   A C   1 
ATOM   355  O O   . GLU   A 1 47  ? 3.748   1.420   0.108  1.00 27.42 ? 47  GLU   A O   1 
ATOM   356  C CB  . GLU   A 1 47  ? 6.216   3.408   0.171  1.00 35.43 ? 47  GLU   A CB  1 
ATOM   357  C CG  . GLU   A 1 47  ? 7.679   3.779   0.349  1.00 35.43 ? 47  GLU   A CG  1 
ATOM   358  C CD  . GLU   A 1 47  ? 8.095   5.076   -0.295 1.00 35.43 ? 47  GLU   A CD  1 
ATOM   359  O OE1 . GLU   A 1 47  ? 9.181   5.597   0.046  1.00 35.43 ? 47  GLU   A OE1 1 
ATOM   360  O OE2 . GLU   A 1 47  ? 7.343   5.562   -1.167 1.00 35.43 ? 47  GLU   A OE2 1 
ATOM   361  N N   . TYR   A 1 48  ? 4.046   1.992   2.267  1.00 23.01 ? 48  TYR   A N   1 
ATOM   362  C CA  . TYR   A 1 48  ? 2.661   1.759   2.612  1.00 26.25 ? 48  TYR   A CA  1 
ATOM   363  C C   . TYR   A 1 48  ? 2.016   3.070   3.027  1.00 22.51 ? 48  TYR   A C   1 
ATOM   364  O O   . TYR   A 1 48  ? 2.682   4.095   3.216  1.00 24.83 ? 48  TYR   A O   1 
ATOM   365  C CB  . TYR   A 1 48  ? 2.554   0.685   3.691  1.00 28.25 ? 48  TYR   A CB  1 
ATOM   366  C CG  . TYR   A 1 48  ? 3.042   -0.641  3.156  1.00 33.03 ? 48  TYR   A CG  1 
ATOM   367  C CD1 . TYR   A 1 48  ? 2.264   -1.359  2.246  1.00 32.99 ? 48  TYR   A CD1 1 
ATOM   368  C CD2 . TYR   A 1 48  ? 4.290   -1.157  3.509  1.00 21.65 ? 48  TYR   A CD2 1 
ATOM   369  C CE1 . TYR   A 1 48  ? 2.703   -2.558  1.716  1.00 24.73 ? 48  TYR   A CE1 1 
ATOM   370  C CE2 . TYR   A 1 48  ? 4.731   -2.357  2.985  1.00 30.26 ? 48  TYR   A CE2 1 
ATOM   371  C CZ  . TYR   A 1 48  ? 3.928   -3.054  2.081  1.00 26.38 ? 48  TYR   A CZ  1 
ATOM   372  O OH  . TYR   A 1 48  ? 4.339   -4.250  1.524  1.00 26.32 ? 48  TYR   A OH  1 
ATOM   373  N N   . SER   A 1 49  ? 0.694   3.008   3.179  1.00 26.20 ? 49  SER   A N   1 
ATOM   374  C CA  . SER   A 1 49  ? -0.138  4.202   3.204  1.00 26.86 ? 49  SER   A CA  1 
ATOM   375  C C   . SER   A 1 49  ? -0.281  4.690   4.635  1.00 29.12 ? 49  SER   A C   1 
ATOM   376  O O   . SER   A 1 49  ? -1.025  4.108   5.427  1.00 34.48 ? 49  SER   A O   1 
ATOM   377  C CB  . SER   A 1 49  ? -1.497  3.881   2.587  1.00 27.45 ? 49  SER   A CB  1 
ATOM   378  O OG  . SER   A 1 49  ? -2.352  5.010   2.589  1.00 25.50 ? 49  SER   A OG  1 
ATOM   379  N N   . GLU   A 1 50  ? 0.387   5.801   4.942  1.00 27.97 ? 50  GLU   A N   1 
ATOM   380  C CA  . GLU   A 1 50  ? 0.090   6.514   6.178  1.00 25.23 ? 50  GLU   A CA  1 
ATOM   381  C C   . GLU   A 1 50  ? -1.325  7.053   6.152  1.00 22.47 ? 50  GLU   A C   1 
ATOM   382  O O   . GLU   A 1 50  ? -2.026  7.042   7.177  1.00 25.04 ? 50  GLU   A O   1 
ATOM   383  C CB  . GLU   A 1 50  ? 1.092   7.650   6.377  1.00 23.37 ? 50  GLU   A CB  1 
ATOM   384  C CG  . GLU   A 1 50  ? 2.516   7.146   6.484  1.00 35.77 ? 50  GLU   A CG  1 
ATOM   385  C CD  . GLU   A 1 50  ? 3.246   7.101   5.140  1.00 51.44 ? 50  GLU   A CD  1 
ATOM   386  O OE1 . GLU   A 1 50  ? 2.623   7.404   4.091  1.00 56.68 ? 50  GLU   A OE1 1 
ATOM   387  O OE2 . GLU   A 1 50  ? 4.453   6.760   5.139  1.00 52.46 ? 50  GLU   A OE2 1 
ATOM   388  N N   . GLN   A 1 51  ? -1.761  7.525   4.982  1.00 24.78 ? 51  GLN   A N   1 
ATOM   389  C CA  . GLN   A 1 51  ? -3.083  8.116   4.868  1.00 27.09 ? 51  GLN   A CA  1 
ATOM   390  C C   . GLN   A 1 51  ? -4.164  7.101   5.206  1.00 19.44 ? 51  GLN   A C   1 
ATOM   391  O O   . GLN   A 1 51  ? -5.164  7.450   5.835  1.00 18.31 ? 51  GLN   A O   1 
ATOM   392  C CB  . GLN   A 1 51  ? -3.300  8.711   3.470  1.00 26.08 ? 51  GLN   A CB  1 
ATOM   393  C CG  . GLN   A 1 51  ? -4.639  9.440   3.364  1.00 24.60 ? 51  GLN   A CG  1 
ATOM   394  C CD  . GLN   A 1 51  ? -4.680  10.754  4.158  1.00 28.74 ? 51  GLN   A CD  1 
ATOM   395  O OE1 . GLN   A 1 51  ? -5.721  11.408  4.231  1.00 30.11 ? 51  GLN   A OE1 1 
ATOM   396  N NE2 . GLN   A 1 51  ? -3.535  11.190  4.658  1.00 30.06 ? 51  GLN   A NE2 1 
ATOM   397  N N   . GLU   A 1 52  ? -3.980  5.840   4.795  1.00 21.43 ? 52  GLU   A N   1 
ATOM   398  C CA  . GLU   A 1 52  ? -4.974  4.811   5.093  1.00 20.55 ? 52  GLU   A CA  1 
ATOM   399  C C   . GLU   A 1 52  ? -5.162  4.635   6.591  1.00 24.99 ? 52  GLU   A C   1 
ATOM   400  O O   . GLU   A 1 52  ? -6.297  4.565   7.073  1.00 33.10 ? 52  GLU   A O   1 
ATOM   401  C CB  . GLU   A 1 52  ? -4.536  3.486   4.481  1.00 24.19 ? 52  GLU   A CB  1 
ATOM   402  C CG  . GLU   A 1 52  ? -5.525  2.340   4.592  1.00 28.03 ? 52  GLU   A CG  1 
ATOM   403  C CD  . GLU   A 1 52  ? -5.127  1.195   3.679  1.00 37.49 ? 52  GLU   A CD  1 
ATOM   404  O OE1 . GLU   A 1 52  ? -3.924  1.100   3.360  1.00 42.55 ? 52  GLU   A OE1 1 
ATOM   405  O OE2 . GLU   A 1 52  ? -5.997  0.394   3.275  1.00 40.60 ? 52  GLU   A OE2 1 
ATOM   406  N N   . LEU   A 1 53  ? -4.067  4.595   7.350  1.00 19.74 ? 53  LEU   A N   1 
ATOM   407  C CA  . LEU   A 1 53  ? -4.196  4.467   8.796  1.00 28.76 ? 53  LEU   A CA  1 
ATOM   408  C C   . LEU   A 1 53  ? -4.812  5.726   9.382  1.00 30.67 ? 53  LEU   A C   1 
ATOM   409  O O   . LEU   A 1 53  ? -5.667  5.661   10.274 1.00 29.16 ? 53  LEU   A O   1 
ATOM   410  C CB  . LEU   A 1 53  ? -2.821  4.234   9.426  1.00 23.67 ? 53  LEU   A CB  1 
ATOM   411  C CG  . LEU   A 1 53  ? -1.975  3.064   8.930  1.00 27.47 ? 53  LEU   A CG  1 
ATOM   412  C CD1 . LEU   A 1 53  ? -0.653  3.026   9.667  1.00 21.13 ? 53  LEU   A CD1 1 
ATOM   413  C CD2 . LEU   A 1 53  ? -2.763  1.802   9.219  1.00 26.03 ? 53  LEU   A CD2 1 
ATOM   414  N N   . LEU   A 1 54  ? -4.381  6.881   8.878  1.00 24.75 ? 54  LEU   A N   1 
ATOM   415  C CA  . LEU   A 1 54  ? -4.928  8.156   9.312  1.00 28.97 ? 54  LEU   A CA  1 
ATOM   416  C C   . LEU   A 1 54  ? -6.451  8.200   9.138  1.00 31.13 ? 54  LEU   A C   1 
ATOM   417  O O   . LEU   A 1 54  ? -7.179  8.615   10.044 1.00 32.84 ? 54  LEU   A O   1 
ATOM   418  C CB  . LEU   A 1 54  ? -4.210  9.261   8.544  1.00 37.61 ? 54  LEU   A CB  1 
ATOM   419  C CG  . LEU   A 1 54  ? -4.489  10.707  8.882  1.00 39.51 ? 54  LEU   A CG  1 
ATOM   420  C CD1 . LEU   A 1 54  ? -3.954  10.877  10.278 1.00 33.09 ? 54  LEU   A CD1 1 
ATOM   421  C CD2 . LEU   A 1 54  ? -3.722  11.596  7.933  1.00 40.63 ? 54  LEU   A CD2 1 
ATOM   422  N N   . ASP   A 1 55  ? -6.952  7.758   7.978  1.00 23.38 ? 55  ASP   A N   1 
ATOM   423  C CA  . ASP   A 1 55  ? -8.386  7.828   7.705  1.00 28.55 ? 55  ASP   A CA  1 
ATOM   424  C C   . ASP   A 1 55  ? -9.149  6.741   8.434  1.00 27.08 ? 55  ASP   A C   1 
ATOM   425  O O   . ASP   A 1 55  ? -10.288 6.953   8.862  1.00 32.20 ? 55  ASP   A O   1 
ATOM   426  C CB  . ASP   A 1 55  ? -8.700  7.686   6.205  1.00 30.43 ? 55  ASP   A CB  1 
ATOM   427  C CG  . ASP   A 1 55  ? -8.159  8.826   5.356  1.00 26.25 ? 55  ASP   A CG  1 
ATOM   428  O OD1 . ASP   A 1 55  ? -7.815  9.898   5.908  1.00 18.91 ? 55  ASP   A OD1 1 
ATOM   429  O OD2 . ASP   A 1 55  ? -8.145  8.663   4.111  1.00 28.79 ? 55  ASP   A OD2 1 
ATOM   430  N N   . CYS   A 1 56  ? -8.564  5.554   8.530  1.00 32.23 ? 56  CYS   A N   1 
ATOM   431  C CA  . CYS   A 1 56  ? -9.345  4.376   8.850  1.00 29.39 ? 56  CYS   A CA  1 
ATOM   432  C C   . CYS   A 1 56  ? -9.141  3.857   10.257 1.00 32.14 ? 56  CYS   A C   1 
ATOM   433  O O   . CYS   A 1 56  ? -9.964  3.058   10.715 1.00 31.28 ? 56  CYS   A O   1 
ATOM   434  C CB  . CYS   A 1 56  ? -9.031  3.248   7.856  1.00 29.20 ? 56  CYS   A CB  1 
ATOM   435  S SG  . CYS   A 1 56  ? -9.326  3.725   6.143  1.00 37.97 ? 56  CYS   A SG  1 
ATOM   436  N N   . ASP   A 1 57  ? -8.082  4.257   10.958 1.00 42.48 ? 57  ASP   A N   1 
ATOM   437  C CA  . ASP   A 1 57  ? -7.968  3.736   12.311 1.00 34.25 ? 57  ASP   A CA  1 
ATOM   438  C C   . ASP   A 1 57  ? -8.910  4.561   13.165 1.00 41.43 ? 57  ASP   A C   1 
ATOM   439  O O   . ASP   A 1 57  ? -8.572  5.665   13.602 1.00 40.34 ? 57  ASP   A O   1 
ATOM   440  C CB  . ASP   A 1 57  ? -6.535  3.823   12.810 1.00 36.75 ? 57  ASP   A CB  1 
ATOM   441  C CG  . ASP   A 1 57  ? -6.372  3.268   14.211 1.00 26.75 ? 57  ASP   A CG  1 
ATOM   442  O OD1 . ASP   A 1 57  ? -7.354  2.729   14.776 1.00 27.59 ? 57  ASP   A OD1 1 
ATOM   443  O OD2 . ASP   A 1 57  ? -5.254  3.382   14.747 1.00 32.72 ? 57  ASP   A OD2 1 
ATOM   444  N N   . ARG   A 1 58  ? -10.109 4.026   13.389 1.00 37.65 ? 58  ARG   A N   1 
ATOM   445  C CA  . ARG   A 1 58  ? -11.124 4.739   14.149 1.00 42.50 ? 58  ARG   A CA  1 
ATOM   446  C C   . ARG   A 1 58  ? -10.814 4.808   15.641 1.00 34.64 ? 58  ARG   A C   1 
ATOM   447  O O   . ARG   A 1 58  ? -11.469 5.579   16.352 1.00 43.37 ? 58  ARG   A O   1 
ATOM   448  C CB  . ARG   A 1 58  ? -12.501 4.168   13.797 1.00 35.03 ? 58  ARG   A CB  1 
ATOM   449  C CG  . ARG   A 1 58  ? -12.424 2.838   13.108 1.00 43.40 ? 58  ARG   A CG  1 
ATOM   450  C CD  . ARG   A 1 58  ? -13.792 2.233   12.862 1.00 30.32 ? 58  ARG   A CD  1 
ATOM   451  N NE  . ARG   A 1 58  ? -13.655 0.843   12.456 1.00 38.24 ? 58  ARG   A NE  1 
ATOM   452  C CZ  . ARG   A 1 58  ? -14.645 0.103   11.983 1.00 32.31 ? 58  ARG   A CZ  1 
ATOM   453  N NH1 . ARG   A 1 58  ? -15.871 0.589   11.853 1.00 35.88 ? 58  ARG   A NH1 1 
ATOM   454  N NH2 . ARG   A 1 58  ? -14.404 -1.161  11.642 1.00 29.75 ? 58  ARG   A NH2 1 
ATOM   455  N N   . ARG   A 1 59  ? -9.852  4.023   16.137 1.00 33.94 ? 59  ARG   A N   1 
ATOM   456  C CA  . ARG   A 1 59  ? -9.408  4.216   17.516 1.00 32.42 ? 59  ARG   A CA  1 
ATOM   457  C C   . ARG   A 1 59  ? -8.555  5.466   17.656 1.00 37.26 ? 59  ARG   A C   1 
ATOM   458  O O   . ARG   A 1 59  ? -8.485  6.045   18.746 1.00 49.08 ? 59  ARG   A O   1 
ATOM   459  C CB  . ARG   A 1 59  ? -8.625  3.005   18.023 1.00 36.29 ? 59  ARG   A CB  1 
ATOM   460  C CG  . ARG   A 1 59  ? -9.482  1.881   18.559 1.00 40.73 ? 59  ARG   A CG  1 
ATOM   461  C CD  . ARG   A 1 59  ? -8.632  0.772   19.149 1.00 52.61 ? 59  ARG   A CD  1 
ATOM   462  N NE  . ARG   A 1 59  ? -8.599  -0.387  18.265 1.00 69.86 ? 59  ARG   A NE  1 
ATOM   463  C CZ  . ARG   A 1 59  ? -9.353  -1.468  18.414 1.00 73.23 ? 59  ARG   A CZ  1 
ATOM   464  N NH1 . ARG   A 1 59  ? -10.211 -1.581  19.418 1.00 48.56 ? 59  ARG   A NH1 1 
ATOM   465  N NH2 . ARG   A 1 59  ? -9.246  -2.458  17.532 1.00 61.46 ? 59  ARG   A NH2 1 
ATOM   466  N N   . SER   A 1 60  ? -7.893  5.886   16.579 1.00 30.46 ? 60  SER   A N   1 
ATOM   467  C CA  . SER   A 1 60  ? -7.067  7.082   16.591 1.00 31.69 ? 60  SER   A CA  1 
ATOM   468  C C   . SER   A 1 60  ? -7.929  8.296   16.264 1.00 25.77 ? 60  SER   A C   1 
ATOM   469  O O   . SER   A 1 60  ? -9.154  8.208   16.187 1.00 25.07 ? 60  SER   A O   1 
ATOM   470  C CB  . SER   A 1 60  ? -5.903  6.932   15.620 1.00 26.02 ? 60  SER   A CB  1 
ATOM   471  O OG  . SER   A 1 60  ? -4.958  6.003   16.110 1.00 29.19 ? 60  SER   A OG  1 
ATOM   472  N N   . TYR   A 1 61  ? -7.305  9.450   16.063 1.00 24.96 ? 61  TYR   A N   1 
ATOM   473  C CA  . TYR   A 1 61  ? -8.071  10.682  15.908 1.00 31.72 ? 61  TYR   A CA  1 
ATOM   474  C C   . TYR   A 1 61  ? -7.582  11.496  14.718 1.00 25.10 ? 61  TYR   A C   1 
ATOM   475  O O   . TYR   A 1 61  ? -7.557  12.732  14.762 1.00 19.37 ? 61  TYR   A O   1 
ATOM   476  C CB  . TYR   A 1 61  ? -8.046  11.529  17.188 1.00 40.47 ? 61  TYR   A CB  1 
ATOM   477  C CG  . TYR   A 1 61  ? -8.328  10.764  18.474 1.00 60.16 ? 61  TYR   A CG  1 
ATOM   478  C CD1 . TYR   A 1 61  ? -7.379  9.910   19.030 1.00 61.32 ? 61  TYR   A CD1 1 
ATOM   479  C CD2 . TYR   A 1 61  ? -9.569  10.856  19.099 1.00 76.41 ? 61  TYR   A CD2 1 
ATOM   480  C CE1 . TYR   A 1 61  ? -7.641  9.204   20.185 1.00 78.70 ? 61  TYR   A CE1 1 
ATOM   481  C CE2 . TYR   A 1 61  ? -9.841  10.146  20.251 1.00 67.73 ? 61  TYR   A CE2 1 
ATOM   482  C CZ  . TYR   A 1 61  ? -8.871  9.320   20.790 1.00 73.31 ? 61  TYR   A CZ  1 
ATOM   483  O OH  . TYR   A 1 61  ? -9.116  8.604   21.940 1.00 74.19 ? 61  TYR   A OH  1 
ATOM   484  N N   . GLY   A 1 62  ? -7.214  10.820  13.630 1.00 21.67 ? 62  GLY   A N   1 
ATOM   485  C CA  . GLY   A 1 62  ? -6.761  11.540  12.451 1.00 31.53 ? 62  GLY   A CA  1 
ATOM   486  C C   . GLY   A 1 62  ? -5.568  12.425  12.760 1.00 25.33 ? 62  GLY   A C   1 
ATOM   487  O O   . GLY   A 1 62  ? -4.585  11.993  13.371 1.00 29.66 ? 62  GLY   A O   1 
ATOM   488  N N   . CYS   A 1 63  ? -5.656  13.688  12.338 1.00 39.61 ? 63  CYS   A N   1 
ATOM   489  C CA  . CYS   A 1 63  ? -4.591  14.654  12.576 1.00 45.92 ? 63  CYS   A CA  1 
ATOM   490  C C   . CYS   A 1 63  ? -4.557  15.199  13.991 1.00 28.93 ? 63  CYS   A C   1 
ATOM   491  O O   . CYS   A 1 63  ? -3.657  15.981  14.313 1.00 22.81 ? 63  CYS   A O   1 
ATOM   492  C CB  . CYS   A 1 63  ? -4.698  15.817  11.583 1.00 29.76 ? 63  CYS   A CB  1 
ATOM   493  S SG  . CYS   A 1 63  ? -4.275  15.332  9.893  1.00 61.08 ? 63  CYS   A SG  1 
ATOM   494  N N   . ASN   A 1 64  ? -5.467  14.796  14.855 1.00 30.66 ? 64  ASN   A N   1 
ATOM   495  C CA  . ASN   A 1 64  ? -5.374  15.221  16.238 1.00 38.79 ? 64  ASN   A CA  1 
ATOM   496  C C   . ASN   A 1 64  ? -4.618  14.215  17.097 1.00 30.37 ? 64  ASN   A C   1 
ATOM   497  O O   . ASN   A 1 64  ? -4.641  14.322  18.328 1.00 52.11 ? 64  ASN   A O   1 
ATOM   498  C CB  . ASN   A 1 64  ? -6.769  15.495  16.794 1.00 36.97 ? 64  ASN   A CB  1 
ATOM   499  C CG  . ASN   A 1 64  ? -7.402  16.733  16.174 1.00 41.75 ? 64  ASN   A CG  1 
ATOM   500  O OD1 . ASN   A 1 64  ? -8.489  16.672  15.595 1.00 43.30 ? 64  ASN   A OD1 1 
ATOM   501  N ND2 . ASN   A 1 64  ? -6.714  17.864  16.289 1.00 42.54 ? 64  ASN   A ND2 1 
ATOM   502  N N   . GLY   A 1 65  ? -3.938  13.258  16.474 1.00 30.28 ? 65  GLY   A N   1 
ATOM   503  C CA  . GLY   A 1 65  ? -3.113  12.290  17.171 1.00 32.80 ? 65  GLY   A CA  1 
ATOM   504  C C   . GLY   A 1 65  ? -3.745  10.908  17.132 1.00 31.75 ? 65  GLY   A C   1 
ATOM   505  O O   . GLY   A 1 65  ? -4.854  10.709  16.632 1.00 32.26 ? 65  GLY   A O   1 
ATOM   506  N N   . GLY   A 1 66  ? -3.022  9.948   17.694 1.00 21.93 ? 66  GLY   A N   1 
ATOM   507  C CA  . GLY   A 1 66  ? -3.461  8.573   17.575 1.00 23.04 ? 66  GLY   A CA  1 
ATOM   508  C C   . GLY   A 1 66  ? -2.477  7.615   18.207 1.00 26.46 ? 66  GLY   A C   1 
ATOM   509  O O   . GLY   A 1 66  ? -1.550  8.017   18.914 1.00 35.85 ? 66  GLY   A O   1 
ATOM   510  N N   . TYR   A 1 67  ? -2.673  6.330   17.915 1.00 19.60 ? 67  TYR   A N   1 
ATOM   511  C CA  . TYR   A 1 67  ? -1.996  5.265   18.643 1.00 28.64 ? 67  TYR   A CA  1 
ATOM   512  C C   . TYR   A 1 67  ? -1.306  4.375   17.626 1.00 30.51 ? 67  TYR   A C   1 
ATOM   513  O O   . TYR   A 1 67  ? -1.989  3.773   16.771 1.00 25.54 ? 67  TYR   A O   1 
ATOM   514  C CB  . TYR   A 1 67  ? -2.967  4.446   19.493 1.00 22.17 ? 67  TYR   A CB  1 
ATOM   515  C CG  . TYR   A 1 67  ? -3.776  5.305   20.416 1.00 34.05 ? 67  TYR   A CG  1 
ATOM   516  C CD1 . TYR   A 1 67  ? -3.228  5.814   21.587 1.00 43.80 ? 67  TYR   A CD1 1 
ATOM   517  C CD2 . TYR   A 1 67  ? -5.093  5.618   20.113 1.00 26.43 ? 67  TYR   A CD2 1 
ATOM   518  C CE1 . TYR   A 1 67  ? -3.979  6.620   22.438 1.00 34.66 ? 67  TYR   A CE1 1 
ATOM   519  C CE2 . TYR   A 1 67  ? -5.848  6.416   20.955 1.00 46.37 ? 67  TYR   A CE2 1 
ATOM   520  C CZ  . TYR   A 1 67  ? -5.288  6.916   22.115 1.00 38.38 ? 67  TYR   A CZ  1 
ATOM   521  O OH  . TYR   A 1 67  ? -6.041  7.708   22.951 1.00 52.49 ? 67  TYR   A OH  1 
ATOM   522  N N   . PRO   A 1 68  ? 0.023   4.299   17.643 1.00 23.23 ? 68  PRO   A N   1 
ATOM   523  C CA  . PRO   A 1 68  ? 0.705   3.328   16.774 1.00 28.27 ? 68  PRO   A CA  1 
ATOM   524  C C   . PRO   A 1 68  ? 0.182   1.920   16.982 1.00 23.33 ? 68  PRO   A C   1 
ATOM   525  O O   . PRO   A 1 68  ? 0.073   1.145   16.019 1.00 24.80 ? 68  PRO   A O   1 
ATOM   526  C CB  . PRO   A 1 68  ? 2.179   3.471   17.192 1.00 22.16 ? 68  PRO   A CB  1 
ATOM   527  C CG  . PRO   A 1 68  ? 2.287   4.894   17.695 1.00 18.64 ? 68  PRO   A CG  1 
ATOM   528  C CD  . PRO   A 1 68  ? 0.966   5.158   18.384 1.00 22.33 ? 68  PRO   A CD  1 
ATOM   529  N N   A TRP   A 1 69  ? -0.162  1.576   18.226 0.42 27.56 ? 69  TRP   A N   1 
ATOM   530  N N   B TRP   A 1 69  ? -0.161  1.569   18.226 0.58 27.74 ? 69  TRP   A N   1 
ATOM   531  C CA  A TRP   A 1 69  ? -0.689  0.250   18.524 0.42 32.09 ? 69  TRP   A CA  1 
ATOM   532  C CA  B TRP   A 1 69  ? -0.676  0.232   18.497 0.58 32.11 ? 69  TRP   A CA  1 
ATOM   533  C C   A TRP   A 1 69  ? -1.971  -0.020  17.742 0.42 31.26 ? 69  TRP   A C   1 
ATOM   534  C C   B TRP   A 1 69  ? -1.970  -0.021  17.728 0.58 31.24 ? 69  TRP   A C   1 
ATOM   535  O O   A TRP   A 1 69  ? -2.138  -1.096  17.156 0.42 32.80 ? 69  TRP   A O   1 
ATOM   536  O O   B TRP   A 1 69  ? -2.143  -1.093  17.136 0.58 32.85 ? 69  TRP   A O   1 
ATOM   537  C CB  A TRP   A 1 69  ? -0.927  0.110   20.029 0.42 33.08 ? 69  TRP   A CB  1 
ATOM   538  C CB  B TRP   A 1 69  ? -0.853  0.025   20.011 0.58 33.07 ? 69  TRP   A CB  1 
ATOM   539  C CG  A TRP   A 1 69  ? -1.986  -0.888  20.374 0.42 36.87 ? 69  TRP   A CG  1 
ATOM   540  C CG  B TRP   A 1 69  ? -2.225  0.305   20.574 0.58 38.57 ? 69  TRP   A CG  1 
ATOM   541  C CD1 A TRP   A 1 69  ? -1.835  -2.241  20.485 0.42 33.57 ? 69  TRP   A CD1 1 
ATOM   542  C CD1 B TRP   A 1 69  ? -2.583  1.356   21.378 0.58 42.64 ? 69  TRP   A CD1 1 
ATOM   543  C CD2 A TRP   A 1 69  ? -3.365  -0.614  20.651 0.42 44.64 ? 69  TRP   A CD2 1 
ATOM   544  C CD2 B TRP   A 1 69  ? -3.415  -0.489  20.404 0.58 44.45 ? 69  TRP   A CD2 1 
ATOM   545  N NE1 A TRP   A 1 69  ? -3.033  -2.825  20.814 0.42 42.94 ? 69  TRP   A NE1 1 
ATOM   546  N NE1 B TRP   A 1 69  ? -3.922  1.276   21.696 0.58 41.39 ? 69  TRP   A NE1 1 
ATOM   547  C CE2 A TRP   A 1 69  ? -3.989  -1.849  20.924 0.42 46.91 ? 69  TRP   A CE2 1 
ATOM   548  C CE2 B TRP   A 1 69  ? -4.453  0.154   21.113 0.58 46.78 ? 69  TRP   A CE2 1 
ATOM   549  C CE3 A TRP   A 1 69  ? -4.133  0.557   20.699 0.42 44.67 ? 69  TRP   A CE3 1 
ATOM   550  C CE3 B TRP   A 1 69  ? -3.704  -1.675  19.714 0.58 44.33 ? 69  TRP   A CE3 1 
ATOM   551  C CZ2 A TRP   A 1 69  ? -5.346  -1.948  21.237 0.42 51.13 ? 69  TRP   A CZ2 1 
ATOM   552  C CZ2 B TRP   A 1 69  ? -5.757  -0.352  21.151 0.58 50.09 ? 69  TRP   A CZ2 1 
ATOM   553  C CZ3 A TRP   A 1 69  ? -5.481  0.458   21.011 0.42 44.45 ? 69  TRP   A CZ3 1 
ATOM   554  C CZ3 B TRP   A 1 69  ? -4.998  -2.170  19.746 0.58 46.52 ? 69  TRP   A CZ3 1 
ATOM   555  C CH2 A TRP   A 1 69  ? -6.073  -0.787  21.275 0.42 49.92 ? 69  TRP   A CH2 1 
ATOM   556  C CH2 B TRP   A 1 69  ? -6.008  -1.512  20.462 0.58 50.65 ? 69  TRP   A CH2 1 
ATOM   557  N N   . SER   A 1 70  ? -2.883  0.954   17.705 1.00 28.05 ? 70  SER   A N   1 
ATOM   558  C CA  . SER   A 1 70  ? -4.140  0.745   16.985 1.00 31.21 ? 70  SER   A CA  1 
ATOM   559  C C   . SER   A 1 70  ? -3.931  0.728   15.473 1.00 30.22 ? 70  SER   A C   1 
ATOM   560  O O   . SER   A 1 70  ? -4.659  0.027   14.761 1.00 30.64 ? 70  SER   A O   1 
ATOM   561  C CB  . SER   A 1 70  ? -5.174  1.805   17.373 1.00 20.35 ? 70  SER   A CB  1 
ATOM   562  O OG  . SER   A 1 70  ? -4.780  3.087   16.928 1.00 48.87 ? 70  SER   A OG  1 
ATOM   563  N N   . ALA   A 1 71  ? -2.926  1.450   14.963 1.00 22.84 ? 71  ALA   A N   1 
ATOM   564  C CA  . ALA   A 1 71  ? -2.635  1.373   13.534 1.00 22.89 ? 71  ALA   A CA  1 
ATOM   565  C C   . ALA   A 1 71  ? -2.085  -0.001  13.158 1.00 25.52 ? 71  ALA   A C   1 
ATOM   566  O O   . ALA   A 1 71  ? -2.435  -0.551  12.101 1.00 28.75 ? 71  ALA   A O   1 
ATOM   567  C CB  . ALA   A 1 71  ? -1.660  2.478   13.143 1.00 21.86 ? 71  ALA   A CB  1 
ATOM   568  N N   . LEU   A 1 72  ? -1.216  -0.578  13.997 1.00 20.12 ? 72  LEU   A N   1 
ATOM   569  C CA  . LEU   A 1 72  ? -0.727  -1.914  13.665 1.00 32.09 ? 72  LEU   A CA  1 
ATOM   570  C C   . LEU   A 1 72  ? -1.829  -2.942  13.840 1.00 27.15 ? 72  LEU   A C   1 
ATOM   571  O O   . LEU   A 1 72  ? -1.910  -3.910  13.076 1.00 29.06 ? 72  LEU   A O   1 
ATOM   572  C CB  . LEU   A 1 72  ? 0.504   -2.320  14.485 1.00 32.03 ? 72  LEU   A CB  1 
ATOM   573  C CG  . LEU   A 1 72  ? 1.928   -1.776  14.287 1.00 23.10 ? 72  LEU   A CG  1 
ATOM   574  C CD1 . LEU   A 1 72  ? 1.905   -0.368  13.935 1.00 40.07 ? 72  LEU   A CD1 1 
ATOM   575  C CD2 . LEU   A 1 72  ? 2.780   -1.963  15.545 1.00 27.39 ? 72  LEU   A CD2 1 
ATOM   576  N N   . GLN   A 1 73  ? -2.683  -2.751  14.845 1.00 24.91 ? 73  GLN   A N   1 
ATOM   577  C CA  . GLN   A 1 73  ? -3.842  -3.614  14.995 1.00 33.26 ? 73  GLN   A CA  1 
ATOM   578  C C   . GLN   A 1 73  ? -4.703  -3.576  13.738 1.00 31.78 ? 73  GLN   A C   1 
ATOM   579  O O   . GLN   A 1 73  ? -5.163  -4.619  13.252 1.00 38.12 ? 73  GLN   A O   1 
ATOM   580  C CB  . GLN   A 1 73  ? -4.638  -3.183  16.226 1.00 36.85 ? 73  GLN   A CB  1 
ATOM   581  C CG  . GLN   A 1 73  ? -5.590  -4.248  16.716 1.00 49.05 ? 73  GLN   A CG  1 
ATOM   582  C CD  . GLN   A 1 73  ? -4.856  -5.527  17.045 1.00 66.08 ? 73  GLN   A CD  1 
ATOM   583  O OE1 . GLN   A 1 73  ? -4.088  -5.589  18.009 1.00 55.93 ? 73  GLN   A OE1 1 
ATOM   584  N NE2 . GLN   A 1 73  ? -5.052  -6.549  16.215 1.00 53.11 ? 73  GLN   A NE2 1 
ATOM   585  N N   . LEU   A 1 74  ? -4.897  -2.379  13.177 1.00 27.64 ? 74  LEU   A N   1 
ATOM   586  C CA  . LEU   A 1 74  ? -5.668  -2.234  11.946 1.00 37.92 ? 74  LEU   A CA  1 
ATOM   587  C C   . LEU   A 1 74  ? -5.008  -2.968  10.781 1.00 31.67 ? 74  LEU   A C   1 
ATOM   588  O O   . LEU   A 1 74  ? -5.690  -3.629  9.991  1.00 31.47 ? 74  LEU   A O   1 
ATOM   589  C CB  . LEU   A 1 74  ? -5.829  -0.748  11.622 1.00 36.88 ? 74  LEU   A CB  1 
ATOM   590  C CG  . LEU   A 1 74  ? -6.725  -0.328  10.453 1.00 37.90 ? 74  LEU   A CG  1 
ATOM   591  C CD1 . LEU   A 1 74  ? -8.158  -0.778  10.665 1.00 40.68 ? 74  LEU   A CD1 1 
ATOM   592  C CD2 . LEU   A 1 74  ? -6.644  1.171   10.229 1.00 36.37 ? 74  LEU   A CD2 1 
ATOM   593  N N   . VAL   A 1 75  ? -3.679  -2.871  10.659 1.00 32.34 ? 75  VAL   A N   1 
ATOM   594  C CA  . VAL   A 1 75  ? -2.998  -3.566  9.560  1.00 30.77 ? 75  VAL   A CA  1 
ATOM   595  C C   . VAL   A 1 75  ? -3.030  -5.089  9.742  1.00 26.31 ? 75  VAL   A C   1 
ATOM   596  O O   . VAL   A 1 75  ? -3.056  -5.839  8.756  1.00 26.45 ? 75  VAL   A O   1 
ATOM   597  C CB  . VAL   A 1 75  ? -1.565  -3.021  9.398  1.00 28.77 ? 75  VAL   A CB  1 
ATOM   598  C CG1 . VAL   A 1 75  ? -0.829  -3.713  8.258  1.00 21.21 ? 75  VAL   A CG1 1 
ATOM   599  C CG2 . VAL   A 1 75  ? -1.634  -1.545  9.107  1.00 35.97 ? 75  VAL   A CG2 1 
ATOM   600  N N   . ALA   A 1 76  ? -3.047  -5.575  10.984 1.00 40.29 ? 76  ALA   A N   1 
ATOM   601  C CA  . ALA   A 1 76  ? -3.120  -7.017  11.211 1.00 37.24 ? 76  ALA   A CA  1 
ATOM   602  C C   . ALA   A 1 76  ? -4.524  -7.567  11.012 1.00 34.69 ? 76  ALA   A C   1 
ATOM   603  O O   . ALA   A 1 76  ? -4.674  -8.737  10.638 1.00 30.34 ? 76  ALA   A O   1 
ATOM   604  C CB  . ALA   A 1 76  ? -2.640  -7.365  12.624 1.00 23.12 ? 76  ALA   A CB  1 
ATOM   605  N N   . GLN   A 1 77  ? -5.556  -6.758  11.275 1.00 22.17 ? 77  GLN   A N   1 
ATOM   606  C CA  . GLN   A 1 77  ? -6.928  -7.239  11.129 1.00 42.54 ? 77  GLN   A CA  1 
ATOM   607  C C   . GLN   A 1 77  ? -7.379  -7.158  9.678  1.00 43.07 ? 77  GLN   A C   1 
ATOM   608  O O   . GLN   A 1 77  ? -7.923  -8.124  9.127  1.00 31.86 ? 77  GLN   A O   1 
ATOM   609  C CB  . GLN   A 1 77  ? -7.869  -6.429  12.023 1.00 45.12 ? 77  GLN   A CB  1 
ATOM   610  C CG  . GLN   A 1 77  ? -9.241  -7.059  12.206 1.00 76.37 ? 77  GLN   A CG  1 
ATOM   611  C CD  . GLN   A 1 77  ? -10.346 -6.031  12.359 1.00 62.21 ? 77  GLN   A CD  1 
ATOM   612  O OE1 . GLN   A 1 77  ? -11.474 -6.246  11.919 1.00 66.22 ? 77  GLN   A OE1 1 
ATOM   613  N NE2 . GLN   A 1 77  ? -10.019 -4.896  12.965 1.00 63.59 ? 77  GLN   A NE2 1 
ATOM   614  N N   . TYR   A 1 78  ? -7.150  -6.008  9.051  1.00 29.70 ? 78  TYR   A N   1 
ATOM   615  C CA  . TYR   A 1 78  ? -7.524  -5.774  7.665  1.00 33.02 ? 78  TYR   A CA  1 
ATOM   616  C C   . TYR   A 1 78  ? -6.317  -5.816  6.748  1.00 34.32 ? 78  TYR   A C   1 
ATOM   617  O O   . TYR   A 1 78  ? -6.178  -6.733  5.932  1.00 44.32 ? 78  TYR   A O   1 
ATOM   618  C CB  . TYR   A 1 78  ? -8.262  -4.444  7.528  1.00 43.99 ? 78  TYR   A CB  1 
ATOM   619  C CG  . TYR   A 1 78  ? -9.555  -4.396  8.319  1.00 50.43 ? 78  TYR   A CG  1 
ATOM   620  C CD1 . TYR   A 1 78  ? -10.474 -5.437  8.242  1.00 65.80 ? 78  TYR   A CD1 1 
ATOM   621  C CD2 . TYR   A 1 78  ? -9.869  -3.307  9.115  1.00 63.01 ? 78  TYR   A CD2 1 
ATOM   622  C CE1 . TYR   A 1 78  ? -11.657 -5.400  8.949  1.00 65.32 ? 78  TYR   A CE1 1 
ATOM   623  C CE2 . TYR   A 1 78  ? -11.060 -3.256  9.824  1.00 65.29 ? 78  TYR   A CE2 1 
ATOM   624  C CZ  . TYR   A 1 78  ? -11.947 -4.305  9.737  1.00 68.30 ? 78  TYR   A CZ  1 
ATOM   625  O OH  . TYR   A 1 78  ? -13.125 -4.258  10.446 1.00 56.08 ? 78  TYR   A OH  1 
ATOM   626  N N   . GLY   A 1 79  ? -5.462  -4.826  6.842  1.00 32.36 ? 79  GLY   A N   1 
ATOM   627  C CA  . GLY   A 1 79  ? -4.328  -4.749  5.955  1.00 28.86 ? 79  GLY   A CA  1 
ATOM   628  C C   . GLY   A 1 79  ? -4.002  -3.301  5.693  1.00 26.93 ? 79  GLY   A C   1 
ATOM   629  O O   . GLY   A 1 79  ? -4.516  -2.402  6.354  1.00 31.64 ? 79  GLY   A O   1 
ATOM   630  N N   . ILE   A 1 80  ? -3.156  -3.092  4.692  1.00 21.73 ? 80  ILE   A N   1 
ATOM   631  C CA  . ILE   A 1 80  ? -2.730  -1.748  4.343  1.00 27.52 ? 80  ILE   A CA  1 
ATOM   632  C C   . ILE   A 1 80  ? -2.447  -1.727  2.853  1.00 32.31 ? 80  ILE   A C   1 
ATOM   633  O O   . ILE   A 1 80  ? -2.056  -2.735  2.257  1.00 35.76 ? 80  ILE   A O   1 
ATOM   634  C CB  . ILE   A 1 80  ? -1.489  -1.313  5.160  1.00 15.70 ? 80  ILE   A CB  1 
ATOM   635  C CG1 . ILE   A 1 80  ? -1.231  0.186   5.015  1.00 24.93 ? 80  ILE   A CG1 1 
ATOM   636  C CG2 . ILE   A 1 80  ? -0.261  -2.081  4.720  1.00 42.83 ? 80  ILE   A CG2 1 
ATOM   637  C CD1 . ILE   A 1 80  ? -0.233  0.736   6.060  1.00 26.91 ? 80  ILE   A CD1 1 
ATOM   638  N N   . HIS   A 1 81  ? -2.718  -0.584  2.242  1.00 29.48 ? 81  HIS   A N   1 
ATOM   639  C CA  . HIS   A 1 81  ? -2.453  -0.394  0.831  1.00 30.60 ? 81  HIS   A CA  1 
ATOM   640  C C   . HIS   A 1 81  ? -1.081  0.224   0.642  1.00 31.74 ? 81  HIS   A C   1 
ATOM   641  O O   . HIS   A 1 81  ? -0.511  0.832   1.553  1.00 31.35 ? 81  HIS   A O   1 
ATOM   642  C CB  . HIS   A 1 81  ? -3.524  0.490   0.188  1.00 28.49 ? 81  HIS   A CB  1 
ATOM   643  C CG  . HIS   A 1 81  ? -4.834  -0.203  -0.000 1.00 30.98 ? 81  HIS   A CG  1 
ATOM   644  N ND1 . HIS   A 1 81  ? -5.834  -0.166  0.947  1.00 27.03 ? 81  HIS   A ND1 1 
ATOM   645  C CD2 . HIS   A 1 81  ? -5.299  -0.972  -1.012 1.00 40.39 ? 81  HIS   A CD2 1 
ATOM   646  C CE1 . HIS   A 1 81  ? -6.867  -0.868  0.518  1.00 42.22 ? 81  HIS   A CE1 1 
ATOM   647  N NE2 . HIS   A 1 81  ? -6.568  -1.370  -0.668 1.00 36.48 ? 81  HIS   A NE2 1 
ATOM   648  N N   . TYR   A 1 82  ? -0.562  0.075   -0.567 1.00 31.98 ? 82  TYR   A N   1 
ATOM   649  C CA  . TYR   A 1 82  ? 0.665   0.758   -0.929 1.00 31.79 ? 82  TYR   A CA  1 
ATOM   650  C C   . TYR   A 1 82  ? 0.459   2.263   -0.840 1.00 31.12 ? 82  TYR   A C   1 
ATOM   651  O O   . TYR   A 1 82  ? -0.651  2.769   -1.027 1.00 37.65 ? 82  TYR   A O   1 
ATOM   652  C CB  . TYR   A 1 82  ? 1.076   0.396   -2.352 1.00 29.72 ? 82  TYR   A CB  1 
ATOM   653  C CG  . TYR   A 1 82  ? 1.589   -1.003  -2.517 1.00 29.86 ? 82  TYR   A CG  1 
ATOM   654  C CD1 . TYR   A 1 82  ? 2.579   -1.499  -1.688 1.00 28.48 ? 82  TYR   A CD1 1 
ATOM   655  C CD2 . TYR   A 1 82  ? 1.117   -1.815  -3.538 1.00 25.09 ? 82  TYR   A CD2 1 
ATOM   656  C CE1 . TYR   A 1 82  ? 3.070   -2.778  -1.850 1.00 37.56 ? 82  TYR   A CE1 1 
ATOM   657  C CE2 . TYR   A 1 82  ? 1.598   -3.094  -3.705 1.00 28.57 ? 82  TYR   A CE2 1 
ATOM   658  C CZ  . TYR   A 1 82  ? 2.580   -3.571  -2.861 1.00 32.32 ? 82  TYR   A CZ  1 
ATOM   659  O OH  . TYR   A 1 82  ? 3.070   -4.849  -3.012 1.00 35.94 ? 82  TYR   A OH  1 
ATOM   660  N N   . ARG   A 1 83  ? 1.542   2.983   -0.549 1.00 25.88 ? 83  ARG   A N   1 
ATOM   661  C CA  . ARG   A 1 83  ? 1.454   4.436   -0.461 1.00 23.74 ? 83  ARG   A CA  1 
ATOM   662  C C   . ARG   A 1 83  ? 1.005   5.048   -1.785 1.00 27.82 ? 83  ARG   A C   1 
ATOM   663  O O   . ARG   A 1 83  ? 0.250   6.025   -1.797 1.00 19.66 ? 83  ARG   A O   1 
ATOM   664  C CB  . ARG   A 1 83  ? 2.801   5.004   -0.033 1.00 25.02 ? 83  ARG   A CB  1 
ATOM   665  C CG  . ARG   A 1 83  ? 2.711   6.380   0.581  1.00 34.74 ? 83  ARG   A CG  1 
ATOM   666  C CD  . ARG   A 1 83  ? 4.083   6.859   1.008  1.00 46.22 ? 83  ARG   A CD  1 
ATOM   667  N NE  . ARG   A 1 83  ? 3.964   7.902   2.019  1.00 41.64 ? 83  ARG   A NE  1 
ATOM   668  C CZ  . ARG   A 1 83  ? 4.460   9.123   1.883  1.00 40.86 ? 83  ARG   A CZ  1 
ATOM   669  N NH1 . ARG   A 1 83  ? 5.157   9.468   0.812  1.00 33.52 ? 83  ARG   A NH1 1 
ATOM   670  N NH2 . ARG   A 1 83  ? 4.245   10.021  2.841  1.00 36.61 ? 83  ARG   A NH2 1 
ATOM   671  N N   A ASN   A 1 84  ? 1.454   4.484   -2.911 0.33 29.16 ? 84  ASN   A N   1 
ATOM   672  N N   B ASN   A 1 84  ? 1.456   4.481   -2.908 0.67 29.20 ? 84  ASN   A N   1 
ATOM   673  C CA  A ASN   A 1 84  ? 1.075   5.028   -4.213 0.33 29.23 ? 84  ASN   A CA  1 
ATOM   674  C CA  B ASN   A 1 84  ? 1.084   5.009   -4.220 0.67 29.21 ? 84  ASN   A CA  1 
ATOM   675  C C   A ASN   A 1 84  ? -0.411  4.838   -4.496 0.33 30.15 ? 84  ASN   A C   1 
ATOM   676  C C   B ASN   A 1 84  ? -0.404  4.829   -4.505 0.67 30.26 ? 84  ASN   A C   1 
ATOM   677  O O   A ASN   A 1 84  ? -1.014  5.647   -5.211 0.33 26.01 ? 84  ASN   A O   1 
ATOM   678  O O   B ASN   A 1 84  ? -0.999  5.633   -5.233 0.67 26.03 ? 84  ASN   A O   1 
ATOM   679  C CB  A ASN   A 1 84  ? 1.909   4.382   -5.322 0.33 31.89 ? 84  ASN   A CB  1 
ATOM   680  C CB  B ASN   A 1 84  ? 1.918   4.327   -5.307 0.67 31.89 ? 84  ASN   A CB  1 
ATOM   681  C CG  A ASN   A 1 84  ? 2.131   2.896   -5.097 0.33 38.09 ? 84  ASN   A CG  1 
ATOM   682  C CG  B ASN   A 1 84  ? 2.058   5.172   -6.548 0.67 38.09 ? 84  ASN   A CG  1 
ATOM   683  O OD1 A ASN   A 1 84  ? 2.869   2.495   -4.193 0.33 31.70 ? 84  ASN   A OD1 1 
ATOM   684  O OD1 B ASN   A 1 84  ? 1.101   5.340   -7.303 0.67 31.29 ? 84  ASN   A OD1 1 
ATOM   685  N ND2 A ASN   A 1 84  ? 1.492   2.070   -5.922 0.33 29.57 ? 84  ASN   A ND2 1 
ATOM   686  N ND2 B ASN   A 1 84  ? 3.256   5.710   -6.770 0.67 28.51 ? 84  ASN   A ND2 1 
ATOM   687  N N   . THR   A 1 85  ? -1.011  3.776   -3.958 1.00 31.34 ? 85  THR   A N   1 
ATOM   688  C CA  . THR   A 1 85  ? -2.439  3.550   -4.132 1.00 27.98 ? 85  THR   A CA  1 
ATOM   689  C C   . THR   A 1 85  ? -3.261  4.498   -3.269 1.00 35.49 ? 85  THR   A C   1 
ATOM   690  O O   . THR   A 1 85  ? -4.396  4.843   -3.626 1.00 36.45 ? 85  THR   A O   1 
ATOM   691  C CB  . THR   A 1 85  ? -2.790  2.099   -3.779 1.00 30.94 ? 85  THR   A CB  1 
ATOM   692  O OG1 . THR   A 1 85  ? -1.939  1.201   -4.499 1.00 28.36 ? 85  THR   A OG1 1 
ATOM   693  C CG2 . THR   A 1 85  ? -4.256  1.793   -4.126 1.00 30.17 ? 85  THR   A CG2 1 
ATOM   694  N N   . TYR   A 1 86  ? -2.701  4.918   -2.137 1.00 31.56 ? 86  TYR   A N   1 
ATOM   695  C CA  . TYR   A 1 86  ? -3.418  5.647   -1.087 1.00 23.76 ? 86  TYR   A CA  1 
ATOM   696  C C   . TYR   A 1 86  ? -2.453  6.691   -0.540 1.00 19.05 ? 86  TYR   A C   1 
ATOM   697  O O   . TYR   A 1 86  ? -1.957  6.583   0.586  1.00 23.69 ? 86  TYR   A O   1 
ATOM   698  C CB  . TYR   A 1 86  ? -3.887  4.658   -0.015 1.00 18.67 ? 86  TYR   A CB  1 
ATOM   699  C CG  . TYR   A 1 86  ? -5.079  5.038   0.831  1.00 23.90 ? 86  TYR   A CG  1 
ATOM   700  C CD1 . TYR   A 1 86  ? -5.346  6.358   1.144  1.00 31.61 ? 86  TYR   A CD1 1 
ATOM   701  C CD2 . TYR   A 1 86  ? -5.930  4.056   1.341  1.00 58.42 ? 86  TYR   A CD2 1 
ATOM   702  C CE1 . TYR   A 1 86  ? -6.442  6.694   1.930  1.00 23.86 ? 86  TYR   A CE1 1 
ATOM   703  C CE2 . TYR   A 1 86  ? -7.022  4.380   2.126  1.00 61.01 ? 86  TYR   A CE2 1 
ATOM   704  C CZ  . TYR   A 1 86  ? -7.277  5.701   2.413  1.00 27.15 ? 86  TYR   A CZ  1 
ATOM   705  O OH  . TYR   A 1 86  ? -8.356  6.054   3.193  1.00 37.46 ? 86  TYR   A OH  1 
ATOM   706  N N   . PRO   A 1 87  ? -2.160  7.725   -1.331 1.00 27.45 ? 87  PRO   A N   1 
ATOM   707  C CA  . PRO   A 1 87  ? -1.082  8.653   -0.974 1.00 21.02 ? 87  PRO   A CA  1 
ATOM   708  C C   . PRO   A 1 87  ? -1.458  9.566   0.176  1.00 23.04 ? 87  PRO   A C   1 
ATOM   709  O O   . PRO   A 1 87  ? -2.629  9.755   0.511  1.00 27.69 ? 87  PRO   A O   1 
ATOM   710  C CB  . PRO   A 1 87  ? -0.874  9.468   -2.258 1.00 26.96 ? 87  PRO   A CB  1 
ATOM   711  C CG  . PRO   A 1 87  ? -2.184  9.371   -2.965 1.00 20.73 ? 87  PRO   A CG  1 
ATOM   712  C CD  . PRO   A 1 87  ? -2.660  7.978   -2.696 1.00 21.91 ? 87  PRO   A CD  1 
ATOM   713  N N   . TYR   A 1 88  ? -0.424  10.179  0.742  1.00 24.12 ? 88  TYR   A N   1 
ATOM   714  C CA  . TYR   A 1 88  ? -0.553  11.000  1.936  1.00 20.61 ? 88  TYR   A CA  1 
ATOM   715  C C   . TYR   A 1 88  ? -1.065  12.389  1.590  1.00 18.55 ? 88  TYR   A C   1 
ATOM   716  O O   . TYR   A 1 88  ? -0.586  13.020  0.642  1.00 28.60 ? 88  TYR   A O   1 
ATOM   717  C CB  . TYR   A 1 88  ? 0.791   11.115  2.657  1.00 20.82 ? 88  TYR   A CB  1 
ATOM   718  C CG  . TYR   A 1 88  ? 0.706   11.860  3.974  1.00 19.94 ? 88  TYR   A CG  1 
ATOM   719  C CD1 . TYR   A 1 88  ? -0.071  11.371  5.028  1.00 27.95 ? 88  TYR   A CD1 1 
ATOM   720  C CD2 . TYR   A 1 88  ? 1.401   13.050  4.169  1.00 14.60 ? 88  TYR   A CD2 1 
ATOM   721  C CE1 . TYR   A 1 88  ? -0.147  12.048  6.241  1.00 31.08 ? 88  TYR   A CE1 1 
ATOM   722  C CE2 . TYR   A 1 88  ? 1.324   13.741  5.382  1.00 27.92 ? 88  TYR   A CE2 1 
ATOM   723  C CZ  . TYR   A 1 88  ? 0.555   13.230  6.414  1.00 27.71 ? 88  TYR   A CZ  1 
ATOM   724  O OH  . TYR   A 1 88  ? 0.482   13.903  7.613  1.00 25.36 ? 88  TYR   A OH  1 
ATOM   725  N N   . GLU   A 1 89  ? -2.092  12.829  2.308  1.00 27.75 ? 89  GLU   A N   1 
ATOM   726  C CA  . GLU   A 1 89  ? -2.719  14.110  2.040  1.00 36.22 ? 89  GLU   A CA  1 
ATOM   727  C C   . GLU   A 1 89  ? -2.573  15.114  3.176  1.00 41.35 ? 89  GLU   A C   1 
ATOM   728  O O   . GLU   A 1 89  ? -2.853  16.301  2.968  1.00 40.72 ? 89  GLU   A O   1 
ATOM   729  C CB  . GLU   A 1 89  ? -4.206  13.909  1.721  1.00 36.91 ? 89  GLU   A CB  1 
ATOM   730  C CG  . GLU   A 1 89  ? -4.424  12.906  0.610  1.00 39.70 ? 89  GLU   A CG  1 
ATOM   731  C CD  . GLU   A 1 89  ? -5.874  12.777  0.214  1.00 31.97 ? 89  GLU   A CD  1 
ATOM   732  O OE1 . GLU   A 1 89  ? -6.490  13.797  -0.173 1.00 45.38 ? 89  GLU   A OE1 1 
ATOM   733  O OE2 . GLU   A 1 89  ? -6.398  11.646  0.291  1.00 49.11 ? 89  GLU   A OE2 1 
ATOM   734  N N   . GLY   A 1 90  ? -2.122  14.687  4.352  1.00 29.80 ? 90  GLY   A N   1 
ATOM   735  C CA  . GLY   A 1 90  ? -1.881  15.623  5.427  1.00 27.90 ? 90  GLY   A CA  1 
ATOM   736  C C   . GLY   A 1 90  ? -3.133  16.124  6.100  1.00 31.69 ? 90  GLY   A C   1 
ATOM   737  O O   . GLY   A 1 90  ? -3.074  17.106  6.848  1.00 40.13 ? 90  GLY   A O   1 
ATOM   738  N N   . VAL   A 1 91  ? -4.262  15.452  5.882  1.00 29.29 ? 91  VAL   A N   1 
ATOM   739  C CA  . VAL   A 1 91  ? -5.551  15.772  6.495  1.00 34.62 ? 91  VAL   A CA  1 
ATOM   740  C C   . VAL   A 1 91  ? -6.339  14.475  6.575  1.00 33.66 ? 91  VAL   A C   1 
ATOM   741  O O   . VAL   A 1 91  ? -6.204  13.605  5.712  1.00 37.45 ? 91  VAL   A O   1 
ATOM   742  C CB  . VAL   A 1 91  ? -6.368  16.838  5.718  1.00 35.10 ? 91  VAL   A CB  1 
ATOM   743  C CG1 . VAL   A 1 91  ? -5.771  18.238  5.862  1.00 39.57 ? 91  VAL   A CG1 1 
ATOM   744  C CG2 . VAL   A 1 91  ? -6.514  16.453  4.247  1.00 40.32 ? 91  VAL   A CG2 1 
ATOM   745  N N   . GLN   A 1 92  ? -7.118  14.317  7.635  1.00 26.54 ? 92  GLN   A N   1 
ATOM   746  C CA  . GLN   A 1 92  ? -7.937  13.123  7.736  1.00 31.80 ? 92  GLN   A CA  1 
ATOM   747  C C   . GLN   A 1 92  ? -9.107  13.251  6.772  1.00 34.59 ? 92  GLN   A C   1 
ATOM   748  O O   . GLN   A 1 92  ? -9.740  14.307  6.671  1.00 33.05 ? 92  GLN   A O   1 
ATOM   749  C CB  . GLN   A 1 92  ? -8.459  12.903  9.155  1.00 31.25 ? 92  GLN   A CB  1 
ATOM   750  C CG  . GLN   A 1 92  ? -9.182  11.561  9.276  1.00 24.44 ? 92  GLN   A CG  1 
ATOM   751  C CD  . GLN   A 1 92  ? -9.801  11.330  10.629 1.00 33.96 ? 92  GLN   A CD  1 
ATOM   752  O OE1 . GLN   A 1 92  ? -10.486 12.202  11.169 1.00 30.49 ? 92  GLN   A OE1 1 
ATOM   753  N NE2 . GLN   A 1 92  ? -9.594  10.138  11.176 1.00 36.20 ? 92  GLN   A NE2 1 
ATOM   754  N N   . ARG   A 1 93  ? -9.400  12.165  6.060  1.00 31.14 ? 93  ARG   A N   1 
ATOM   755  C CA  . ARG   A 1 93  ? -10.509 12.143  5.120  1.00 27.69 ? 93  ARG   A CA  1 
ATOM   756  C C   . ARG   A 1 93  ? -11.325 10.909  5.485  1.00 22.46 ? 93  ARG   A C   1 
ATOM   757  O O   . ARG   A 1 93  ? -11.003 10.206  6.446  1.00 29.42 ? 93  ARG   A O   1 
ATOM   758  C CB  . ARG   A 1 93  ? -9.947  12.064  3.693  1.00 24.79 ? 93  ARG   A CB  1 
ATOM   759  C CG  . ARG   A 1 93  ? -9.013  13.254  3.419  1.00 25.99 ? 93  ARG   A CG  1 
ATOM   760  C CD  . ARG   A 1 93  ? -9.148  14.181  2.224  1.00 29.06 ? 93  ARG   A CD  1 
ATOM   761  N NE  . ARG   A 1 93  ? -9.217  13.529  0.930  1.00 52.07 ? 93  ARG   A NE  1 
ATOM   762  C CZ  . ARG   A 1 93  ? -10.214 13.704  0.077  1.00 49.26 ? 93  ARG   A CZ  1 
ATOM   763  N NH1 . ARG   A 1 93  ? -11.230 14.511  0.355  1.00 52.80 ? 93  ARG   A NH1 1 
ATOM   764  N NH2 . ARG   A 1 93  ? -10.186 13.068  -1.089 1.00 42.11 ? 93  ARG   A NH2 1 
ATOM   765  N N   A TYR   A 1 94  ? -12.384 10.639  4.733  0.47 30.35 ? 94  TYR   A N   1 
ATOM   766  N N   B TYR   A 1 94  ? -12.382 10.629  4.729  0.53 28.97 ? 94  TYR   A N   1 
ATOM   767  C CA  A TYR   A 1 94  ? -13.150 9.432   5.004  0.47 34.00 ? 94  TYR   A CA  1 
ATOM   768  C CA  B TYR   A 1 94  ? -13.163 9.431   5.014  0.53 33.48 ? 94  TYR   A CA  1 
ATOM   769  C C   A TYR   A 1 94  ? -12.322 8.205   4.637  0.47 30.07 ? 94  TYR   A C   1 
ATOM   770  C C   B TYR   A 1 94  ? -12.392 8.187   4.582  0.53 29.25 ? 94  TYR   A C   1 
ATOM   771  O O   A TYR   A 1 94  ? -11.455 8.256   3.761  0.47 33.05 ? 94  TYR   A O   1 
ATOM   772  O O   B TYR   A 1 94  ? -11.629 8.210   3.614  0.53 33.13 ? 94  TYR   A O   1 
ATOM   773  C CB  A TYR   A 1 94  ? -14.473 9.429   4.230  0.47 34.29 ? 94  TYR   A CB  1 
ATOM   774  C CB  B TYR   A 1 94  ? -14.538 9.484   4.326  0.53 34.32 ? 94  TYR   A CB  1 
ATOM   775  C CG  A TYR   A 1 94  ? -15.331 10.675  4.389  0.47 29.57 ? 94  TYR   A CG  1 
ATOM   776  C CG  B TYR   A 1 94  ? -14.516 9.461   2.806  0.53 32.14 ? 94  TYR   A CG  1 
ATOM   777  C CD1 A TYR   A 1 94  ? -15.212 11.503  5.498  0.47 31.29 ? 94  TYR   A CD1 1 
ATOM   778  C CD1 B TYR   A 1 94  ? -14.168 10.593  2.078  0.53 37.73 ? 94  TYR   A CD1 1 
ATOM   779  C CD2 A TYR   A 1 94  ? -16.281 11.001  3.432  0.47 35.51 ? 94  TYR   A CD2 1 
ATOM   780  C CD2 B TYR   A 1 94  ? -14.852 8.312   2.103  0.53 29.62 ? 94  TYR   A CD2 1 
ATOM   781  C CE1 A TYR   A 1 94  ? -16.002 12.630  5.635  0.47 33.56 ? 94  TYR   A CE1 1 
ATOM   782  C CE1 B TYR   A 1 94  ? -14.145 10.580  0.696  0.53 37.93 ? 94  TYR   A CE1 1 
ATOM   783  C CE2 A TYR   A 1 94  ? -17.076 12.120  3.563  0.47 39.07 ? 94  TYR   A CE2 1 
ATOM   784  C CE2 B TYR   A 1 94  ? -14.834 8.290   0.721  0.53 28.24 ? 94  TYR   A CE2 1 
ATOM   785  C CZ  A TYR   A 1 94  ? -16.935 12.930  4.662  0.47 34.35 ? 94  TYR   A CZ  1 
ATOM   786  C CZ  B TYR   A 1 94  ? -14.476 9.428   0.020  0.53 35.05 ? 94  TYR   A CZ  1 
ATOM   787  O OH  A TYR   A 1 94  ? -17.734 14.045  4.782  0.47 30.79 ? 94  TYR   A OH  1 
ATOM   788  O OH  B TYR   A 1 94  ? -14.449 9.420   -1.360 0.53 31.87 ? 94  TYR   A OH  1 
ATOM   789  N N   . CYS   A 1 95  ? -12.583 7.098   5.327  1.00 28.57 ? 95  CYS   A N   1 
ATOM   790  C CA  . CYS   A 1 95  ? -11.853 5.855   5.064  1.00 32.84 ? 95  CYS   A CA  1 
ATOM   791  C C   . CYS   A 1 95  ? -12.115 5.309   3.661  1.00 33.16 ? 95  CYS   A C   1 
ATOM   792  O O   . CYS   A 1 95  ? -13.254 4.992   3.304  1.00 30.60 ? 95  CYS   A O   1 
ATOM   793  C CB  . CYS   A 1 95  ? -12.217 4.798   6.101  1.00 32.59 ? 95  CYS   A CB  1 
ATOM   794  S SG  . CYS   A 1 95  ? -11.299 3.256   5.850  1.00 40.44 ? 95  CYS   A SG  1 
ATOM   795  N N   . ARG   A 1 96  ? -11.055 5.176   2.868  1.00 30.42 ? 96  ARG   A N   1 
ATOM   796  C CA  . ARG   A 1 96  ? -11.204 4.767   1.478  1.00 27.04 ? 96  ARG   A CA  1 
ATOM   797  C C   . ARG   A 1 96  ? -10.556 3.422   1.195  1.00 24.70 ? 96  ARG   A C   1 
ATOM   798  O O   . ARG   A 1 96  ? -10.338 3.091   0.030  1.00 30.47 ? 96  ARG   A O   1 
ATOM   799  C CB  . ARG   A 1 96  ? -10.635 5.836   0.551  1.00 24.43 ? 96  ARG   A CB  1 
ATOM   800  C CG  . ARG   A 1 96  ? -11.424 7.111   0.627  1.00 22.78 ? 96  ARG   A CG  1 
ATOM   801  C CD  . ARG   A 1 96  ? -10.653 8.297   0.124  1.00 24.76 ? 96  ARG   A CD  1 
ATOM   802  N NE  . ARG   A 1 96  ? -9.753  8.795   1.156  1.00 28.03 ? 96  ARG   A NE  1 
ATOM   803  C CZ  . ARG   A 1 96  ? -8.738  9.614   0.922  1.00 33.18 ? 96  ARG   A CZ  1 
ATOM   804  N NH1 . ARG   A 1 96  ? -8.444  10.013  -0.309 1.00 20.28 ? 96  ARG   A NH1 1 
ATOM   805  N NH2 . ARG   A 1 96  ? -7.981  10.016  1.943  1.00 30.93 ? 96  ARG   A NH2 1 
ATOM   806  N N   . SER   A 1 97  ? -10.266 2.628   2.231  1.00 29.47 ? 97  SER   A N   1 
ATOM   807  C CA  . SER   A 1 97  ? -9.754  1.277   2.009  1.00 26.70 ? 97  SER   A CA  1 
ATOM   808  C C   . SER   A 1 97  ? -10.688 0.472   1.114  1.00 35.79 ? 97  SER   A C   1 
ATOM   809  O O   . SER   A 1 97  ? -10.238 -0.348  0.307  1.00 48.89 ? 97  SER   A O   1 
ATOM   810  C CB  . SER   A 1 97  ? -9.579  0.556   3.344  1.00 33.44 ? 97  SER   A CB  1 
ATOM   811  O OG  . SER   A 1 97  ? -8.786  1.310   4.234  1.00 31.80 ? 97  SER   A OG  1 
ATOM   812  N N   . ARG   A 1 98  ? -11.997 0.687   1.257  1.00 41.12 ? 98  ARG   A N   1 
ATOM   813  C CA  . ARG   A 1 98  ? -12.973 -0.067  0.479  1.00 52.62 ? 98  ARG   A CA  1 
ATOM   814  C C   . ARG   A 1 98  ? -12.806 0.194   -1.011 1.00 42.03 ? 98  ARG   A C   1 
ATOM   815  O O   . ARG   A 1 98  ? -12.680 -0.736  -1.816 1.00 42.37 ? 98  ARG   A O   1 
ATOM   816  C CB  . ARG   A 1 98  ? -14.380 0.311   0.936  1.00 61.52 ? 98  ARG   A CB  1 
ATOM   817  C CG  . ARG   A 1 98  ? -14.666 -0.048  2.387  1.00 74.00 ? 98  ARG   A CG  1 
ATOM   818  C CD  . ARG   A 1 98  ? -14.933 -1.536  2.526  1.00 80.42 ? 98  ARG   A CD  1 
ATOM   819  N NE  . ARG   A 1 98  ? -15.335 -2.118  1.249  1.00 73.86 ? 98  ARG   A NE  1 
ATOM   820  C CZ  . ARG   A 1 98  ? -15.926 -3.296  1.112  1.00 78.44 ? 98  ARG   A CZ  1 
ATOM   821  N NH1 . ARG   A 1 98  ? -16.238 -4.040  2.162  1.00 81.52 ? 98  ARG   A NH1 1 
ATOM   822  N NH2 . ARG   A 1 98  ? -16.216 -3.738  -0.109 1.00 75.80 ? 98  ARG   A NH2 1 
ATOM   823  N N   . GLU   A 1 99  ? -12.784 1.463   -1.388 1.00 38.66 ? 99  GLU   A N   1 
ATOM   824  C CA  . GLU   A 1 99  ? -12.678 1.912   -2.764 1.00 26.74 ? 99  GLU   A CA  1 
ATOM   825  C C   . GLU   A 1 99  ? -11.285 1.747   -3.361 1.00 26.80 ? 99  GLU   A C   1 
ATOM   826  O O   . GLU   A 1 99  ? -11.123 2.081   -4.539 1.00 31.37 ? 99  GLU   A O   1 
ATOM   827  C CB  . GLU   A 1 99  ? -13.042 3.391   -2.827 1.00 33.33 ? 99  GLU   A CB  1 
ATOM   828  C CG  . GLU   A 1 99  ? -13.943 3.845   -1.701 1.00 63.81 ? 99  GLU   A CG  1 
ATOM   829  C CD  . GLU   A 1 99  ? -14.437 5.260   -1.902 1.00 65.61 ? 99  GLU   A CD  1 
ATOM   830  O OE1 . GLU   A 1 99  ? -14.136 5.850   -2.964 1.00 46.45 ? 99  GLU   A OE1 1 
ATOM   831  O OE2 . GLU   A 1 99  ? -15.123 5.777   -0.995 1.00 70.96 ? 99  GLU   A OE2 1 
ATOM   832  N N   . LYS   A 1 100 ? -10.282 1.234   -2.636 1.00 33.68 ? 100 LYS   A N   1 
ATOM   833  C CA  . LYS   A 1 100 ? -8.935  1.169   -3.195 1.00 30.72 ? 100 LYS   A CA  1 
ATOM   834  C C   . LYS   A 1 100 ? -8.507  -0.257  -3.524 1.00 36.35 ? 100 LYS   A C   1 
ATOM   835  O O   . LYS   A 1 100 ? -7.310  -0.508  -3.701 1.00 37.39 ? 100 LYS   A O   1 
ATOM   836  C CB  . LYS   A 1 100 ? -7.928  1.687   -2.161 1.00 33.36 ? 100 LYS   A CB  1 
ATOM   837  C CG  . LYS   A 1 100 ? -7.860  3.150   -1.755 1.00 37.11 ? 100 LYS   A CG  1 
ATOM   838  C CD  . LYS   A 1 100 ? -7.721  4.197   -2.788 1.00 35.43 ? 100 LYS   A CD  1 
ATOM   839  C CE  . LYS   A 1 100 ? -7.664  5.533   -2.034 1.00 22.54 ? 100 LYS   A CE  1 
ATOM   840  N NZ  . LYS   A 1 100 ? -6.823  6.540   -2.735 1.00 22.75 ? 100 LYS   A NZ  1 
ATOM   841  N N   . GLY   A 1 101 ? -9.439  -1.193  -3.650 1.00 35.31 ? 101 GLY   A N   1 
ATOM   842  C CA  . GLY   A 1 101 ? -9.060  -2.515  -4.081 1.00 38.67 ? 101 GLY   A CA  1 
ATOM   843  C C   . GLY   A 1 101 ? -8.485  -3.318  -2.928 1.00 35.96 ? 101 GLY   A C   1 
ATOM   844  O O   . GLY   A 1 101 ? -8.520  -2.897  -1.768 1.00 38.04 ? 101 GLY   A O   1 
ATOM   845  N N   . PRO   A 1 102 ? -7.962  -4.504  -3.228 1.00 40.87 ? 102 PRO   A N   1 
ATOM   846  C CA  . PRO   A 1 102 ? -7.422  -5.361  -2.165 1.00 43.50 ? 102 PRO   A CA  1 
ATOM   847  C C   . PRO   A 1 102 ? -6.224  -4.715  -1.476 1.00 39.46 ? 102 PRO   A C   1 
ATOM   848  O O   . PRO   A 1 102 ? -5.466  -3.952  -2.078 1.00 39.66 ? 102 PRO   A O   1 
ATOM   849  C CB  . PRO   A 1 102 ? -7.040  -6.647  -2.905 1.00 45.86 ? 102 PRO   A CB  1 
ATOM   850  C CG  . PRO   A 1 102 ? -7.045  -6.290  -4.399 1.00 49.29 ? 102 PRO   A CG  1 
ATOM   851  C CD  . PRO   A 1 102 ? -7.378  -4.833  -4.537 1.00 41.64 ? 102 PRO   A CD  1 
ATOM   852  N N   . TYR   A 1 103 ? -6.054  -5.045  -0.198 1.00 37.40 ? 103 TYR   A N   1 
ATOM   853  C CA  . TYR   A 1 103 ? -4.904  -4.581  0.568  1.00 32.96 ? 103 TYR   A CA  1 
ATOM   854  C C   . TYR   A 1 103 ? -3.598  -5.061  -0.058 1.00 32.49 ? 103 TYR   A C   1 
ATOM   855  O O   . TYR   A 1 103 ? -3.539  -6.103  -0.714 1.00 30.62 ? 103 TYR   A O   1 
ATOM   856  C CB  . TYR   A 1 103 ? -5.008  -5.084  2.006  1.00 28.52 ? 103 TYR   A CB  1 
ATOM   857  C CG  . TYR   A 1 103 ? -6.110  -4.408  2.780  1.00 41.61 ? 103 TYR   A CG  1 
ATOM   858  C CD1 . TYR   A 1 103 ? -6.026  -3.058  3.135  1.00 39.96 ? 103 TYR   A CD1 1 
ATOM   859  C CD2 . TYR   A 1 103 ? -7.269  -5.103  3.114  1.00 55.62 ? 103 TYR   A CD2 1 
ATOM   860  C CE1 . TYR   A 1 103 ? -7.056  -2.434  3.838  1.00 46.52 ? 103 TYR   A CE1 1 
ATOM   861  C CE2 . TYR   A 1 103 ? -8.307  -4.485  3.814  1.00 50.47 ? 103 TYR   A CE2 1 
ATOM   862  C CZ  . TYR   A 1 103 ? -8.195  -3.154  4.173  1.00 48.65 ? 103 TYR   A CZ  1 
ATOM   863  O OH  . TYR   A 1 103 ? -9.223  -2.551  4.866  1.00 40.67 ? 103 TYR   A OH  1 
ATOM   864  N N   . ALA   A 1 104 ? -2.529  -4.302  0.179  1.00 27.36 ? 104 ALA   A N   1 
ATOM   865  C CA  . ALA   A 1 104 ? -1.222  -4.678  -0.347 1.00 29.14 ? 104 ALA   A CA  1 
ATOM   866  C C   . ALA   A 1 104 ? -0.472  -5.606  0.590  1.00 23.76 ? 104 ALA   A C   1 
ATOM   867  O O   . ALA   A 1 104 ? 0.252   -6.497  0.126  1.00 24.14 ? 104 ALA   A O   1 
ATOM   868  C CB  . ALA   A 1 104 ? -0.376  -3.432  -0.618 1.00 27.08 ? 104 ALA   A CB  1 
ATOM   869  N N   . ALA   A 1 105 ? -0.647  -5.430  1.897  1.00 21.54 ? 105 ALA   A N   1 
ATOM   870  C CA  . ALA   A 1 105 ? 0.040   -6.252  2.877  1.00 25.36 ? 105 ALA   A CA  1 
ATOM   871  C C   . ALA   A 1 105 ? -0.882  -6.388  4.074  1.00 29.09 ? 105 ALA   A C   1 
ATOM   872  O O   . ALA   A 1 105 ? -1.778  -5.565  4.290  1.00 36.29 ? 105 ALA   A O   1 
ATOM   873  C CB  . ALA   A 1 105 ? 1.393   -5.652  3.303  1.00 22.33 ? 105 ALA   A CB  1 
ATOM   874  N N   . LYS   A 1 106 ? -0.662  -7.445  4.845  1.00 14.64 ? 106 LYS   A N   1 
ATOM   875  C CA  . LYS   A 1 106 ? -1.436  -7.671  6.051  1.00 24.36 ? 106 LYS   A CA  1 
ATOM   876  C C   . LYS   A 1 106 ? -0.500  -8.356  7.031  1.00 27.06 ? 106 LYS   A C   1 
ATOM   877  O O   . LYS   A 1 106 ? 0.282   -9.227  6.638  1.00 27.49 ? 106 LYS   A O   1 
ATOM   878  C CB  . LYS   A 1 106 ? -2.689  -8.517  5.762  1.00 25.91 ? 106 LYS   A CB  1 
ATOM   879  C CG  . LYS   A 1 106 ? -3.625  -8.720  6.964  1.00 40.25 ? 106 LYS   A CG  1 
ATOM   880  C CD  . LYS   A 1 106 ? -4.789  -9.621  6.596  1.00 39.73 ? 106 LYS   A CD  1 
ATOM   881  C CE  . LYS   A 1 106 ? -5.585  -10.035 7.815  1.00 38.57 ? 106 LYS   A CE  1 
ATOM   882  N NZ  . LYS   A 1 106 ? -4.694  -10.499 8.916  1.00 41.86 ? 106 LYS   A NZ  1 
ATOM   883  N N   . THR   A 1 107 ? -0.613  -8.014  8.303  1.00 20.00 ? 107 THR   A N   1 
ATOM   884  C CA  . THR   A 1 107 ? 0.225   -8.654  9.304  1.00 22.54 ? 107 THR   A CA  1 
ATOM   885  C C   . THR   A 1 107 ? -0.624  -9.620  10.112 1.00 41.05 ? 107 THR   A C   1 
ATOM   886  O O   . THR   A 1 107 ? -1.831  -9.767  9.895  1.00 45.53 ? 107 THR   A O   1 
ATOM   887  C CB  . THR   A 1 107 ? 0.916   -7.629  10.215 1.00 31.75 ? 107 THR   A CB  1 
ATOM   888  O OG1 . THR   A 1 107 ? -0.056  -6.793  10.855 1.00 29.25 ? 107 THR   A OG1 1 
ATOM   889  C CG2 . THR   A 1 107 ? 1.902   -6.759  9.409  1.00 18.39 ? 107 THR   A CG2 1 
ATOM   890  N N   . ASP   A 1 108 ? 0.015   -10.258 11.079 1.00 36.25 ? 108 ASP   A N   1 
ATOM   891  C CA  . ASP   A 1 108 ? -0.627  -11.304 11.840 1.00 25.89 ? 108 ASP   A CA  1 
ATOM   892  C C   . ASP   A 1 108 ? -0.834  -10.881 13.275 1.00 37.56 ? 108 ASP   A C   1 
ATOM   893  O O   . ASP   A 1 108 ? -1.477  -11.612 14.037 1.00 46.93 ? 108 ASP   A O   1 
ATOM   894  C CB  . ASP   A 1 108 ? 0.185   -12.608 11.799 1.00 48.47 ? 108 ASP   A CB  1 
ATOM   895  C CG  . ASP   A 1 108 ? 0.322   -13.186 10.384 1.00 72.26 ? 108 ASP   A CG  1 
ATOM   896  O OD1 . ASP   A 1 108 ? 0.445   -12.399 9.418  1.00 62.45 ? 108 ASP   A OD1 1 
ATOM   897  O OD2 . ASP   A 1 108 ? 0.300   -14.427 10.237 1.00 62.40 ? 108 ASP   A OD2 1 
ATOM   898  N N   . GLY   A 1 109 ? -0.333  -9.713  13.656 1.00 25.23 ? 109 GLY   A N   1 
ATOM   899  C CA  . GLY   A 1 109 ? -0.576  -9.224  14.994 1.00 20.50 ? 109 GLY   A CA  1 
ATOM   900  C C   . GLY   A 1 109 ? 0.313   -8.043  15.323 1.00 26.54 ? 109 GLY   A C   1 
ATOM   901  O O   . GLY   A 1 109 ? 1.010   -7.496  14.470 1.00 26.90 ? 109 GLY   A O   1 
ATOM   902  N N   . VAL   A 1 110 ? 0.293   -7.702  16.605 1.00 29.97 ? 110 VAL   A N   1 
ATOM   903  C CA  . VAL   A 1 110 ? 1.005   -6.566  17.172 1.00 29.95 ? 110 VAL   A CA  1 
ATOM   904  C C   . VAL   A 1 110 ? 1.514   -6.985  18.534 1.00 24.39 ? 110 VAL   A C   1 
ATOM   905  O O   . VAL   A 1 110 ? 0.778   -7.587  19.323 1.00 31.04 ? 110 VAL   A O   1 
ATOM   906  C CB  . VAL   A 1 110 ? 0.086   -5.340  17.336 1.00 26.25 ? 110 VAL   A CB  1 
ATOM   907  C CG1 . VAL   A 1 110 ? 0.876   -4.123  17.795 1.00 48.52 ? 110 VAL   A CG1 1 
ATOM   908  C CG2 . VAL   A 1 110 ? -0.664  -5.074  16.059 1.00 34.86 ? 110 VAL   A CG2 1 
ATOM   909  N N   . ARG   A 1 111 ? 2.757   -6.664  18.824 1.00 25.84 ? 111 ARG   A N   1 
ATOM   910  C CA  . ARG   A 1 111 ? 3.281   -6.943  20.142 1.00 32.56 ? 111 ARG   A CA  1 
ATOM   911  C C   . ARG   A 1 111 ? 3.912   -5.681  20.695 1.00 29.10 ? 111 ARG   A C   1 
ATOM   912  O O   . ARG   A 1 111 ? 4.323   -4.789  19.944 1.00 31.90 ? 111 ARG   A O   1 
ATOM   913  C CB  . ARG   A 1 111 ? 4.246   -8.129  20.115 1.00 19.71 ? 111 ARG   A CB  1 
ATOM   914  C CG  . ARG   A 1 111 ? 3.458   -9.422  20.376 1.00 35.93 ? 111 ARG   A CG  1 
ATOM   915  C CD  . ARG   A 1 111 ? 4.111   -10.655 19.813 1.00 41.79 ? 111 ARG   A CD  1 
ATOM   916  N NE  . ARG   A 1 111 ? 5.565   -10.549 19.792 1.00 78.98 ? 111 ARG   A NE  1 
ATOM   917  C CZ  . ARG   A 1 111 ? 6.376   -11.259 20.566 1.00 82.37 ? 111 ARG   A CZ  1 
ATOM   918  N NH1 . ARG   A 1 111 ? 5.906   -12.136 21.441 1.00 72.87 ? 111 ARG   A NH1 1 
ATOM   919  N NH2 . ARG   A 1 111 ? 7.691   -11.086 20.459 1.00 68.50 ? 111 ARG   A NH2 1 
ATOM   920  N N   . GLN   A 1 112 ? 3.901   -5.582  22.017 1.00 14.75 ? 112 GLN   A N   1 
ATOM   921  C CA  . GLN   A 1 112 ? 4.490   -4.460  22.728 1.00 21.04 ? 112 GLN   A CA  1 
ATOM   922  C C   . GLN   A 1 112 ? 5.819   -4.885  23.340 1.00 28.62 ? 112 GLN   A C   1 
ATOM   923  O O   . GLN   A 1 112 ? 5.948   -5.993  23.870 1.00 28.06 ? 112 GLN   A O   1 
ATOM   924  C CB  . GLN   A 1 112 ? 3.548   -3.920  23.811 1.00 17.78 ? 112 GLN   A CB  1 
ATOM   925  C CG  . GLN   A 1 112 ? 4.055   -2.642  24.478 1.00 28.07 ? 112 GLN   A CG  1 
ATOM   926  C CD  . GLN   A 1 112 ? 3.081   -2.057  25.486 1.00 35.46 ? 112 GLN   A CD  1 
ATOM   927  O OE1 . GLN   A 1 112 ? 1.977   -2.569  25.675 1.00 35.93 ? 112 GLN   A OE1 1 
ATOM   928  N NE2 . GLN   A 1 112 ? 3.488   -0.973  26.135 1.00 28.17 ? 112 GLN   A NE2 1 
ATOM   929  N N   . VAL   A 1 113 ? 6.818   -4.013  23.223 1.00 21.58 ? 113 VAL   A N   1 
ATOM   930  C CA  . VAL   A 1 113 ? 8.050   -4.194  23.978 1.00 13.54 ? 113 VAL   A CA  1 
ATOM   931  C C   . VAL   A 1 113 ? 7.773   -3.918  25.446 1.00 20.09 ? 113 VAL   A C   1 
ATOM   932  O O   . VAL   A 1 113 ? 7.011   -2.998  25.790 1.00 13.59 ? 113 VAL   A O   1 
ATOM   933  C CB  . VAL   A 1 113 ? 9.134   -3.240  23.461 1.00 24.20 ? 113 VAL   A CB  1 
ATOM   934  C CG1 . VAL   A 1 113 ? 10.426  -3.497  24.207 1.00 20.37 ? 113 VAL   A CG1 1 
ATOM   935  C CG2 . VAL   A 1 113 ? 9.294   -3.370  21.946 1.00 35.96 ? 113 VAL   A CG2 1 
ATOM   936  N N   . GLN   A 1 114 ? 8.359   -4.734  26.319 1.00 30.15 ? 114 GLN   A N   1 
ATOM   937  C CA  . GLN   A 1 114 ? 8.270   -4.471  27.744 1.00 39.24 ? 114 GLN   A CA  1 
ATOM   938  C C   . GLN   A 1 114 ? 8.737   -3.040  28.002 1.00 19.66 ? 114 GLN   A C   1 
ATOM   939  O O   . GLN   A 1 114 ? 9.893   -2.713  27.704 1.00 30.66 ? 114 GLN   A O   1 
ATOM   940  C CB  . GLN   A 1 114 ? 9.116   -5.474  28.528 1.00 44.56 ? 114 GLN   A CB  1 
ATOM   941  C CG  . GLN   A 1 114 ? 9.688   -4.949  29.836 1.00 39.98 ? 114 GLN   A CG  1 
ATOM   942  C CD  . GLN   A 1 114 ? 8.837   -5.315  31.031 1.00 64.28 ? 114 GLN   A CD  1 
ATOM   943  O OE1 . GLN   A 1 114 ? 8.800   -6.473  31.444 1.00 58.68 ? 114 GLN   A OE1 1 
ATOM   944  N NE2 . GLN   A 1 114 ? 8.142   -4.327  31.597 1.00 71.02 ? 114 GLN   A NE2 1 
ATOM   945  N N   . PRO   A 1 115 ? 7.867   -2.155  28.481 1.00 27.99 ? 115 PRO   A N   1 
ATOM   946  C CA  . PRO   A 1 115 ? 8.249   -0.744  28.590 1.00 33.07 ? 115 PRO   A CA  1 
ATOM   947  C C   . PRO   A 1 115 ? 9.320   -0.524  29.645 1.00 28.77 ? 115 PRO   A C   1 
ATOM   948  O O   . PRO   A 1 115 ? 9.540   -1.342  30.540 1.00 28.82 ? 115 PRO   A O   1 
ATOM   949  C CB  . PRO   A 1 115 ? 6.938   -0.038  28.960 1.00 19.04 ? 115 PRO   A CB  1 
ATOM   950  C CG  . PRO   A 1 115 ? 6.088   -1.094  29.549 1.00 30.23 ? 115 PRO   A CG  1 
ATOM   951  C CD  . PRO   A 1 115 ? 6.473   -2.393  28.889 1.00 27.14 ? 115 PRO   A CD  1 
ATOM   952  N N   . TYR   A 1 116 ? 10.005  0.611   29.504 1.00 26.67 ? 116 TYR   A N   1 
ATOM   953  C CA  . TYR   A 1 116 ? 10.980  1.074   30.485 1.00 31.40 ? 116 TYR   A CA  1 
ATOM   954  C C   . TYR   A 1 116 ? 12.106  0.055   30.642 1.00 25.72 ? 116 TYR   A C   1 
ATOM   955  O O   . TYR   A 1 116 ? 12.602  -0.191  31.742 1.00 38.71 ? 116 TYR   A O   1 
ATOM   956  C CB  . TYR   A 1 116 ? 10.310  1.388   31.824 1.00 21.96 ? 116 TYR   A CB  1 
ATOM   957  C CG  . TYR   A 1 116 ? 9.109   2.287   31.692 1.00 33.69 ? 116 TYR   A CG  1 
ATOM   958  C CD1 . TYR   A 1 116 ? 9.240   3.579   31.184 1.00 43.71 ? 116 TYR   A CD1 1 
ATOM   959  C CD2 . TYR   A 1 116 ? 7.851   1.880   32.130 1.00 30.01 ? 116 TYR   A CD2 1 
ATOM   960  C CE1 . TYR   A 1 116 ? 8.146   4.431   31.070 1.00 41.60 ? 116 TYR   A CE1 1 
ATOM   961  C CE2 . TYR   A 1 116 ? 6.740   2.733   32.027 1.00 25.40 ? 116 TYR   A CE2 1 
ATOM   962  C CZ  . TYR   A 1 116 ? 6.901   4.004   31.493 1.00 37.30 ? 116 TYR   A CZ  1 
ATOM   963  O OH  . TYR   A 1 116 ? 5.822   4.852   31.380 1.00 44.57 ? 116 TYR   A OH  1 
ATOM   964  N N   . ASN   A 1 117 ? 12.527  -0.527  29.521 1.00 21.90 ? 117 ASN   A N   1 
ATOM   965  C CA  . ASN   A 1 117 ? 13.494  -1.625  29.538 1.00 30.34 ? 117 ASN   A CA  1 
ATOM   966  C C   . ASN   A 1 117 ? 14.357  -1.510  28.283 1.00 32.87 ? 117 ASN   A C   1 
ATOM   967  O O   . ASN   A 1 117 ? 13.917  -1.875  27.189 1.00 29.94 ? 117 ASN   A O   1 
ATOM   968  C CB  . ASN   A 1 117 ? 12.779  -2.968  29.612 1.00 16.06 ? 117 ASN   A CB  1 
ATOM   969  C CG  . ASN   A 1 117 ? 13.738  -4.142  29.760 1.00 28.04 ? 117 ASN   A CG  1 
ATOM   970  O OD1 . ASN   A 1 117 ? 14.846  -4.139  29.220 1.00 25.28 ? 117 ASN   A OD1 1 
ATOM   971  N ND2 . ASN   A 1 117 ? 13.299  -5.168  30.483 1.00 47.36 ? 117 ASN   A ND2 1 
ATOM   972  N N   . GLU   A 1 118 ? 15.581  -1.014  28.449 1.00 29.02 ? 118 GLU   A N   1 
ATOM   973  C CA  . GLU   A 1 118 ? 16.433  -0.764  27.292 1.00 33.41 ? 118 GLU   A CA  1 
ATOM   974  C C   . GLU   A 1 118 ? 16.747  -2.042  26.523 1.00 33.30 ? 118 GLU   A C   1 
ATOM   975  O O   . GLU   A 1 118 ? 16.619  -2.081  25.294 1.00 26.05 ? 118 GLU   A O   1 
ATOM   976  C CB  . GLU   A 1 118 ? 17.723  -0.074  27.725 1.00 34.97 ? 118 GLU   A CB  1 
ATOM   977  C CG  . GLU   A 1 118 ? 18.703  0.139   26.575 1.00 34.97 ? 118 GLU   A CG  1 
ATOM   978  C CD  . GLU   A 1 118 ? 19.871  1.037   26.949 1.00 34.97 ? 118 GLU   A CD  1 
ATOM   979  O OE1 . GLU   A 1 118 ? 19.602  2.180   27.397 1.00 34.97 ? 118 GLU   A OE1 1 
ATOM   980  O OE2 . GLU   A 1 118 ? 21.041  0.603   26.804 1.00 34.97 ? 118 GLU   A OE2 1 
ATOM   981  N N   . GLY   A 1 119 ? 17.146  -3.103  27.219 1.00 28.59 ? 119 GLY   A N   1 
ATOM   982  C CA  . GLY   A 1 119 ? 17.508  -4.323  26.514 1.00 25.65 ? 119 GLY   A CA  1 
ATOM   983  C C   . GLY   A 1 119 ? 16.354  -4.916  25.728 1.00 26.78 ? 119 GLY   A C   1 
ATOM   984  O O   . GLY   A 1 119 ? 16.548  -5.447  24.632 1.00 30.01 ? 119 GLY   A O   1 
ATOM   985  N N   . ALA   A 1 120 ? 15.133  -4.812  26.267 1.00 19.99 ? 120 ALA   A N   1 
ATOM   986  C CA  . ALA   A 1 120 ? 13.966  -5.328  25.560 1.00 10.57 ? 120 ALA   A CA  1 
ATOM   987  C C   . ALA   A 1 120 ? 13.739  -4.579  24.256 1.00 24.21 ? 120 ALA   A C   1 
ATOM   988  O O   . ALA   A 1 120 ? 13.384  -5.184  23.236 1.00 24.20 ? 120 ALA   A O   1 
ATOM   989  C CB  . ALA   A 1 120 ? 12.724  -5.213  26.448 1.00 20.74 ? 120 ALA   A CB  1 
ATOM   990  N N   . LEU   A 1 121 ? 13.923  -3.256  24.274 1.00 21.57 ? 121 LEU   A N   1 
ATOM   991  C CA  . LEU   A 1 121 ? 13.750  -2.483  23.055 1.00 23.12 ? 121 LEU   A CA  1 
ATOM   992  C C   . LEU   A 1 121 ? 14.859  -2.772  22.051 1.00 32.21 ? 121 LEU   A C   1 
ATOM   993  O O   . LEU   A 1 121 ? 14.588  -2.943  20.855 1.00 25.64 ? 121 LEU   A O   1 
ATOM   994  C CB  . LEU   A 1 121 ? 13.705  -0.992  23.379 1.00 29.09 ? 121 LEU   A CB  1 
ATOM   995  C CG  . LEU   A 1 121 ? 13.619  -0.131  22.123 1.00 18.56 ? 121 LEU   A CG  1 
ATOM   996  C CD1 . LEU   A 1 121 ? 12.341  -0.502  21.368 1.00 22.08 ? 121 LEU   A CD1 1 
ATOM   997  C CD2 . LEU   A 1 121 ? 13.658  1.328   22.469 1.00 29.53 ? 121 LEU   A CD2 1 
ATOM   998  N N   . LEU   A 1 122 ? 16.115  -2.845  22.519 1.00 34.32 ? 122 LEU   A N   1 
ATOM   999  C CA  . LEU   A 1 122 ? 17.212  -3.194  21.621 1.00 20.74 ? 122 LEU   A CA  1 
ATOM   1000 C C   . LEU   A 1 122 ? 16.982  -4.571  21.021 1.00 21.75 ? 122 LEU   A C   1 
ATOM   1001 O O   . LEU   A 1 122 ? 17.192  -4.782  19.817 1.00 26.08 ? 122 LEU   A O   1 
ATOM   1002 C CB  . LEU   A 1 122 ? 18.547  -3.138  22.356 1.00 21.62 ? 122 LEU   A CB  1 
ATOM   1003 C CG  . LEU   A 1 122 ? 18.959  -1.795  22.949 1.00 23.82 ? 122 LEU   A CG  1 
ATOM   1004 C CD1 . LEU   A 1 122 ? 20.278  -1.961  23.706 1.00 22.10 ? 122 LEU   A CD1 1 
ATOM   1005 C CD2 . LEU   A 1 122 ? 19.081  -0.755  21.861 1.00 19.83 ? 122 LEU   A CD2 1 
ATOM   1006 N N   . TYR   A 1 123 ? 16.509  -5.510  21.844 1.00 16.23 ? 123 TYR   A N   1 
ATOM   1007 C CA  . TYR   A 1 123 ? 16.216  -6.848  21.349 1.00 32.47 ? 123 TYR   A CA  1 
ATOM   1008 C C   . TYR   A 1 123 ? 15.185  -6.797  20.231 1.00 23.79 ? 123 TYR   A C   1 
ATOM   1009 O O   . TYR   A 1 123 ? 15.306  -7.509  19.229 1.00 29.15 ? 123 TYR   A O   1 
ATOM   1010 C CB  . TYR   A 1 123 ? 15.714  -7.738  22.490 1.00 24.80 ? 123 TYR   A CB  1 
ATOM   1011 C CG  . TYR   A 1 123 ? 15.410  -9.144  22.041 1.00 30.71 ? 123 TYR   A CG  1 
ATOM   1012 C CD1 . TYR   A 1 123 ? 16.425  -10.012 21.653 1.00 36.07 ? 123 TYR   A CD1 1 
ATOM   1013 C CD2 . TYR   A 1 123 ? 14.096  -9.587  21.955 1.00 32.20 ? 123 TYR   A CD2 1 
ATOM   1014 C CE1 . TYR   A 1 123 ? 16.135  -11.299 21.216 1.00 41.11 ? 123 TYR   A CE1 1 
ATOM   1015 C CE2 . TYR   A 1 123 ? 13.794  -10.863 21.516 1.00 46.54 ? 123 TYR   A CE2 1 
ATOM   1016 C CZ  . TYR   A 1 123 ? 14.810  -11.716 21.149 1.00 46.84 ? 123 TYR   A CZ  1 
ATOM   1017 O OH  . TYR   A 1 123 ? 14.495  -12.985 20.718 1.00 53.36 ? 123 TYR   A OH  1 
ATOM   1018 N N   . SER   A 1 124 ? 14.172  -5.950  20.376 1.00 18.06 ? 124 SER   A N   1 
ATOM   1019 C CA  . SER   A 1 124 ? 13.173  -5.835  19.322 1.00 28.69 ? 124 SER   A CA  1 
ATOM   1020 C C   . SER   A 1 124 ? 13.760  -5.175  18.086 1.00 25.31 ? 124 SER   A C   1 
ATOM   1021 O O   . SER   A 1 124 ? 13.444  -5.571  16.960 1.00 21.61 ? 124 SER   A O   1 
ATOM   1022 C CB  . SER   A 1 124 ? 11.951  -5.066  19.829 1.00 27.14 ? 124 SER   A CB  1 
ATOM   1023 O OG  . SER   A 1 124 ? 11.217  -5.835  20.764 1.00 22.32 ? 124 SER   A OG  1 
ATOM   1024 N N   . ILE   A 1 125 ? 14.634  -4.183  18.272 1.00 25.03 ? 125 ILE   A N   1 
ATOM   1025 C CA  . ILE   A 1 125 ? 15.205  -3.503  17.120 1.00 18.62 ? 125 ILE   A CA  1 
ATOM   1026 C C   . ILE   A 1 125 ? 16.124  -4.440  16.353 1.00 23.63 ? 125 ILE   A C   1 
ATOM   1027 O O   . ILE   A 1 125 ? 16.214  -4.363  15.120 1.00 23.47 ? 125 ILE   A O   1 
ATOM   1028 C CB  . ILE   A 1 125 ? 15.959  -2.232  17.542 1.00 28.27 ? 125 ILE   A CB  1 
ATOM   1029 C CG1 . ILE   A 1 125 ? 15.038  -1.236  18.231 1.00 25.03 ? 125 ILE   A CG1 1 
ATOM   1030 C CG2 . ILE   A 1 125 ? 16.533  -1.547  16.315 1.00 18.06 ? 125 ILE   A CG2 1 
ATOM   1031 C CD1 . ILE   A 1 125 ? 15.797  -0.127  18.938 1.00 27.07 ? 125 ILE   A CD1 1 
ATOM   1032 N N   . ALA   A 1 126 ? 16.826  -5.332  17.054 1.00 20.08 ? 126 ALA   A N   1 
ATOM   1033 C CA  . ALA   A 1 126 ? 17.660  -6.310  16.359 1.00 22.96 ? 126 ALA   A CA  1 
ATOM   1034 C C   . ALA   A 1 126 ? 16.843  -7.214  15.437 1.00 19.68 ? 126 ALA   A C   1 
ATOM   1035 O O   . ALA   A 1 126 ? 17.363  -7.700  14.430 1.00 23.26 ? 126 ALA   A O   1 
ATOM   1036 C CB  . ALA   A 1 126 ? 18.433  -7.145  17.382 1.00 22.84 ? 126 ALA   A CB  1 
ATOM   1037 N N   . ASN   A 1 127 ? 15.574  -7.453  15.761 1.00 23.56 ? 127 ASN   A N   1 
ATOM   1038 C CA  . ASN   A 1 127 ? 14.717  -8.296  14.935 1.00 26.58 ? 127 ASN   A CA  1 
ATOM   1039 C C   . ASN   A 1 127 ? 14.010  -7.527  13.828 1.00 29.07 ? 127 ASN   A C   1 
ATOM   1040 O O   . ASN   A 1 127 ? 13.774  -8.090  12.751 1.00 35.17 ? 127 ASN   A O   1 
ATOM   1041 C CB  . ASN   A 1 127 ? 13.665  -8.991  15.800 1.00 25.88 ? 127 ASN   A CB  1 
ATOM   1042 C CG  . ASN   A 1 127 ? 14.279  -9.828  16.911 1.00 43.06 ? 127 ASN   A CG  1 
ATOM   1043 O OD1 . ASN   A 1 127 ? 15.308  -9.470  17.481 1.00 38.23 ? 127 ASN   A OD1 1 
ATOM   1044 N ND2 . ASN   A 1 127 ? 13.635  -10.943 17.234 1.00 67.49 ? 127 ASN   A ND2 1 
ATOM   1045 N N   . GLN   A 1 128 ? 13.683  -6.251  14.057 1.00 22.25 ? 128 GLN   A N   1 
ATOM   1046 C CA  . GLN   A 1 128 ? 12.883  -5.463  13.124 1.00 19.88 ? 128 GLN   A CA  1 
ATOM   1047 C C   . GLN   A 1 128 ? 12.761  -4.013  13.578 1.00 16.38 ? 128 GLN   A C   1 
ATOM   1048 O O   . GLN   A 1 128 ? 12.972  -3.711  14.761 1.00 20.10 ? 128 GLN   A O   1 
ATOM   1049 C CB  . GLN   A 1 128 ? 11.495  -6.077  12.987 1.00 27.49 ? 128 GLN   A CB  1 
ATOM   1050 C CG  . GLN   A 1 128 ? 10.672  -5.957  14.254 1.00 18.46 ? 128 GLN   A CG  1 
ATOM   1051 C CD  . GLN   A 1 128 ? 9.524   -6.900  14.238 1.00 27.80 ? 128 GLN   A CD  1 
ATOM   1052 O OE1 . GLN   A 1 128 ? 8.456   -6.577  13.722 1.00 32.33 ? 128 GLN   A OE1 1 
ATOM   1053 N NE2 . GLN   A 1 128 ? 9.728   -8.090  14.788 1.00 37.70 ? 128 GLN   A NE2 1 
ATOM   1054 N N   . PRO   A 1 129 ? 12.403  -3.091  12.682 1.00 22.82 ? 129 PRO   A N   1 
ATOM   1055 C CA  . PRO   A 1 129 ? 12.075  -1.730  13.127 1.00 24.14 ? 129 PRO   A CA  1 
ATOM   1056 C C   . PRO   A 1 129 ? 10.894  -1.764  14.090 1.00 21.10 ? 129 PRO   A C   1 
ATOM   1057 O O   . PRO   A 1 129 ? 10.021  -2.626  13.990 1.00 23.79 ? 129 PRO   A O   1 
ATOM   1058 C CB  . PRO   A 1 129 ? 11.720  -1.010  11.822 1.00 25.65 ? 129 PRO   A CB  1 
ATOM   1059 C CG  . PRO   A 1 129 ? 12.490  -1.757  10.786 1.00 30.88 ? 129 PRO   A CG  1 
ATOM   1060 C CD  . PRO   A 1 129 ? 12.452  -3.191  11.213 1.00 21.33 ? 129 PRO   A CD  1 
ATOM   1061 N N   . VAL   A 1 130 ? 10.921  -0.868  15.080 1.00 17.97 ? 130 VAL   A N   1 
ATOM   1062 C CA  . VAL   A 1 130 ? 9.966   -0.862  16.186 1.00 20.82 ? 130 VAL   A CA  1 
ATOM   1063 C C   . VAL   A 1 130 ? 9.357   0.525   16.248 1.00 19.66 ? 130 VAL   A C   1 
ATOM   1064 O O   . VAL   A 1 130 ? 10.052  1.526   16.066 1.00 18.57 ? 130 VAL   A O   1 
ATOM   1065 C CB  . VAL   A 1 130 ? 10.642  -1.219  17.538 1.00 13.00 ? 130 VAL   A CB  1 
ATOM   1066 C CG1 . VAL   A 1 130 ? 9.669   -1.113  18.726 1.00 16.51 ? 130 VAL   A CG1 1 
ATOM   1067 C CG2 . VAL   A 1 130 ? 11.195  -2.624  17.493 1.00 15.42 ? 130 VAL   A CG2 1 
ATOM   1068 N N   . SER   A 1 131 ? 8.066   0.593   16.507 1.00 14.57 ? 131 SER   A N   1 
ATOM   1069 C CA  . SER   A 1 131 ? 7.430   1.881   16.729 1.00 19.97 ? 131 SER   A CA  1 
ATOM   1070 C C   . SER   A 1 131 ? 7.686   2.285   18.168 1.00 13.20 ? 131 SER   A C   1 
ATOM   1071 O O   . SER   A 1 131 ? 7.416   1.507   19.083 1.00 21.38 ? 131 SER   A O   1 
ATOM   1072 C CB  . SER   A 1 131 ? 5.935   1.803   16.438 1.00 13.94 ? 131 SER   A CB  1 
ATOM   1073 O OG  . SER   A 1 131 ? 5.271   2.948   16.923 1.00 19.99 ? 131 SER   A OG  1 
ATOM   1074 N N   . VAL   A 1 132 ? 8.221   3.488   18.379 1.00 10.92 ? 132 VAL   A N   1 
ATOM   1075 C CA  . VAL   A 1 132 ? 8.536   3.966   19.720 1.00 17.11 ? 132 VAL   A CA  1 
ATOM   1076 C C   . VAL   A 1 132 ? 7.989   5.381   19.835 1.00 19.69 ? 132 VAL   A C   1 
ATOM   1077 O O   . VAL   A 1 132 ? 7.651   6.018   18.837 1.00 25.44 ? 132 VAL   A O   1 
ATOM   1078 C CB  . VAL   A 1 132 ? 10.060  3.944   20.010 1.00 17.98 ? 132 VAL   A CB  1 
ATOM   1079 C CG1 . VAL   A 1 132 ? 10.613  2.505   19.898 1.00 11.81 ? 132 VAL   A CG1 1 
ATOM   1080 C CG2 . VAL   A 1 132 ? 10.815  4.906   19.072 1.00 16.96 ? 132 VAL   A CG2 1 
ATOM   1081 N N   . VAL   A 1 133 ? 7.881   5.872   21.064 1.00 16.27 ? 133 VAL   A N   1 
ATOM   1082 C CA  . VAL   A 1 133 ? 7.412   7.231   21.275 1.00 18.25 ? 133 VAL   A CA  1 
ATOM   1083 C C   . VAL   A 1 133 ? 8.468   7.977   22.072 1.00 27.34 ? 133 VAL   A C   1 
ATOM   1084 O O   . VAL   A 1 133 ? 9.300   7.388   22.770 1.00 21.54 ? 133 VAL   A O   1 
ATOM   1085 C CB  . VAL   A 1 133 ? 6.039   7.301   22.000 1.00 23.30 ? 133 VAL   A CB  1 
ATOM   1086 C CG1 . VAL   A 1 133 ? 4.929   6.618   21.164 1.00 15.46 ? 133 VAL   A CG1 1 
ATOM   1087 C CG2 . VAL   A 1 133 ? 6.127   6.720   23.406 1.00 20.86 ? 133 VAL   A CG2 1 
ATOM   1088 N N   . LEU   A 1 134 ? 8.415   9.296   21.974 1.00 18.06 ? 134 LEU   A N   1 
ATOM   1089 C CA  . LEU   A 1 134 ? 9.360   10.139  22.684 1.00 19.89 ? 134 LEU   A CA  1 
ATOM   1090 C C   . LEU   A 1 134 ? 8.766   11.534  22.826 1.00 27.57 ? 134 LEU   A C   1 
ATOM   1091 O O   . LEU   A 1 134 ? 7.741   11.873  22.226 1.00 28.01 ? 134 LEU   A O   1 
ATOM   1092 C CB  . LEU   A 1 134 ? 10.723  10.160  21.986 1.00 20.84 ? 134 LEU   A CB  1 
ATOM   1093 C CG  . LEU   A 1 134 ? 10.803  10.458  20.490 1.00 26.90 ? 134 LEU   A CG  1 
ATOM   1094 C CD1 . LEU   A 1 134 ? 10.507  11.915  20.173 1.00 27.95 ? 134 LEU   A CD1 1 
ATOM   1095 C CD2 . LEU   A 1 134 ? 12.194  10.063  19.981 1.00 18.69 ? 134 LEU   A CD2 1 
ATOM   1096 N N   . GLU   A 1 135 ? 9.426   12.329  23.651 1.00 33.16 ? 135 GLU   A N   1 
ATOM   1097 C CA  . GLU   A 1 135 ? 9.110   13.738  23.816 1.00 29.30 ? 135 GLU   A CA  1 
ATOM   1098 C C   . GLU   A 1 135 ? 9.855   14.541  22.764 1.00 31.15 ? 135 GLU   A C   1 
ATOM   1099 O O   . GLU   A 1 135 ? 11.079  14.686  22.829 1.00 31.90 ? 135 GLU   A O   1 
ATOM   1100 C CB  . GLU   A 1 135 ? 9.480   14.205  25.213 1.00 36.81 ? 135 GLU   A CB  1 
ATOM   1101 C CG  . GLU   A 1 135 ? 9.158   15.638  25.410 1.00 36.81 ? 135 GLU   A CG  1 
ATOM   1102 C CD  . GLU   A 1 135 ? 9.802   16.197  26.651 1.00 36.81 ? 135 GLU   A CD  1 
ATOM   1103 O OE1 . GLU   A 1 135 ? 10.627  17.130  26.507 1.00 36.81 ? 135 GLU   A OE1 1 
ATOM   1104 O OE2 . GLU   A 1 135 ? 9.449   15.736  27.764 1.00 36.81 ? 135 GLU   A OE2 1 
ATOM   1105 N N   . ALA   A 1 136 ? 9.109   15.087  21.812 1.00 31.15 ? 136 ALA   A N   1 
ATOM   1106 C CA  . ALA   A 1 136 ? 9.677   15.890  20.746 1.00 23.35 ? 136 ALA   A CA  1 
ATOM   1107 C C   . ALA   A 1 136 ? 9.383   17.373  20.900 1.00 25.59 ? 136 ALA   A C   1 
ATOM   1108 O O   . ALA   A 1 136 ? 9.785   18.165  20.037 1.00 35.91 ? 136 ALA   A O   1 
ATOM   1109 C CB  . ALA   A 1 136 ? 9.146   15.392  19.400 1.00 26.91 ? 136 ALA   A CB  1 
ATOM   1110 N N   . ALA   A 1 137 ? 8.675   17.769  21.963 1.00 32.23 ? 137 ALA   A N   1 
ATOM   1111 C CA  . ALA   A 1 137 ? 8.226   19.151  22.108 1.00 34.60 ? 137 ALA   A CA  1 
ATOM   1112 C C   . ALA   A 1 137 ? 9.373   20.087  22.444 1.00 33.30 ? 137 ALA   A C   1 
ATOM   1113 O O   . ALA   A 1 137 ? 9.292   21.281  22.140 1.00 33.98 ? 137 ALA   A O   1 
ATOM   1114 C CB  . ALA   A 1 137 ? 7.142   19.254  23.185 1.00 23.79 ? 137 ALA   A CB  1 
ATOM   1115 N N   . GLY   A 1 138 ? 10.437  19.571  23.052 1.00 32.14 ? 138 GLY   A N   1 
ATOM   1116 C CA  . GLY   A 1 138 ? 11.541  20.423  23.442 1.00 26.20 ? 138 GLY   A CA  1 
ATOM   1117 C C   . GLY   A 1 138 ? 12.263  20.995  22.234 1.00 30.81 ? 138 GLY   A C   1 
ATOM   1118 O O   . GLY   A 1 138 ? 12.418  20.337  21.204 1.00 28.04 ? 138 GLY   A O   1 
ATOM   1119 N N   . LYS   A 1 139 ? 12.714  22.246  22.375 1.00 38.08 ? 139 LYS   A N   1 
ATOM   1120 C CA  . LYS   A 1 139 ? 13.437  22.912  21.297 1.00 36.78 ? 139 LYS   A CA  1 
ATOM   1121 C C   . LYS   A 1 139 ? 14.728  22.195  20.948 1.00 45.85 ? 139 LYS   A C   1 
ATOM   1122 O O   . LYS   A 1 139 ? 15.151  22.198  19.787 1.00 55.19 ? 139 LYS   A O   1 
ATOM   1123 C CB  . LYS   A 1 139 ? 13.760  24.343  21.682 1.00 44.82 ? 139 LYS   A CB  1 
ATOM   1124 C CG  . LYS   A 1 139 ? 12.676  25.353  21.440 1.00 44.82 ? 139 LYS   A CG  1 
ATOM   1125 C CD  . LYS   A 1 139 ? 13.338  26.725  21.522 1.00 44.82 ? 139 LYS   A CD  1 
ATOM   1126 C CE  . LYS   A 1 139 ? 14.633  26.734  20.673 1.00 44.82 ? 139 LYS   A CE  1 
ATOM   1127 N NZ  . LYS   A 1 139 ? 15.444  28.001  20.708 1.00 44.82 ? 139 LYS   A NZ  1 
ATOM   1128 N N   . ASP   A 1 140 ? 15.394  21.616  21.943 1.00 24.99 ? 140 ASP   A N   1 
ATOM   1129 C CA  . ASP   A 1 140 ? 16.631  20.891  21.680 1.00 32.89 ? 140 ASP   A CA  1 
ATOM   1130 C C   . ASP   A 1 140 ? 16.387  19.744  20.711 1.00 37.00 ? 140 ASP   A C   1 
ATOM   1131 O O   . ASP   A 1 140 ? 17.190  19.504  19.801 1.00 40.80 ? 140 ASP   A O   1 
ATOM   1132 C CB  . ASP   A 1 140 ? 17.191  20.393  23.006 1.00 35.16 ? 140 ASP   A CB  1 
ATOM   1133 C CG  . ASP   A 1 140 ? 17.627  21.534  23.878 1.00 52.99 ? 140 ASP   A CG  1 
ATOM   1134 O OD1 . ASP   A 1 140 ? 17.811  22.633  23.315 1.00 42.41 ? 140 ASP   A OD1 1 
ATOM   1135 O OD2 . ASP   A 1 140 ? 17.622  21.392  25.118 1.00 39.31 ? 140 ASP   A OD2 1 
ATOM   1136 N N   . PHE   A 1 141 ? 15.284  19.011  20.896 1.00 35.69 ? 141 PHE   A N   1 
ATOM   1137 C CA  . PHE   A 1 141 ? 14.931  17.967  19.941 1.00 34.19 ? 141 PHE   A CA  1 
ATOM   1138 C C   . PHE   A 1 141 ? 14.504  18.573  18.609 1.00 23.72 ? 141 PHE   A C   1 
ATOM   1139 O O   . PHE   A 1 141 ? 14.899  18.091  17.543 1.00 31.75 ? 141 PHE   A O   1 
ATOM   1140 C CB  . PHE   A 1 141 ? 13.805  17.103  20.527 1.00 27.24 ? 141 PHE   A CB  1 
ATOM   1141 C CG  . PHE   A 1 141 ? 13.467  15.897  19.706 1.00 25.45 ? 141 PHE   A CG  1 
ATOM   1142 C CD1 . PHE   A 1 141 ? 12.586  15.989  18.634 1.00 33.61 ? 141 PHE   A CD1 1 
ATOM   1143 C CD2 . PHE   A 1 141 ? 14.006  14.661  20.021 1.00 31.58 ? 141 PHE   A CD2 1 
ATOM   1144 C CE1 . PHE   A 1 141 ? 12.268  14.872  17.871 1.00 43.32 ? 141 PHE   A CE1 1 
ATOM   1145 C CE2 . PHE   A 1 141 ? 13.688  13.531  19.262 1.00 35.06 ? 141 PHE   A CE2 1 
ATOM   1146 C CZ  . PHE   A 1 141 ? 12.817  13.643  18.182 1.00 32.15 ? 141 PHE   A CZ  1 
ATOM   1147 N N   . GLN   A 1 142 ? 13.687  19.626  18.654 1.00 16.27 ? 142 GLN   A N   1 
ATOM   1148 C CA  . GLN   A 1 142 ? 13.222  20.243  17.418 1.00 29.04 ? 142 GLN   A CA  1 
ATOM   1149 C C   . GLN   A 1 142 ? 14.384  20.772  16.585 1.00 28.72 ? 142 GLN   A C   1 
ATOM   1150 O O   . GLN   A 1 142 ? 14.366  20.674  15.353 1.00 29.89 ? 142 GLN   A O   1 
ATOM   1151 C CB  . GLN   A 1 142 ? 12.196  21.325  17.721 1.00 22.58 ? 142 GLN   A CB  1 
ATOM   1152 C CG  . GLN   A 1 142 ? 11.013  20.748  18.408 1.00 28.54 ? 142 GLN   A CG  1 
ATOM   1153 C CD  . GLN   A 1 142 ? 9.801   21.605  18.271 1.00 52.00 ? 142 GLN   A CD  1 
ATOM   1154 O OE1 . GLN   A 1 142 ? 9.393   21.941  17.156 1.00 47.59 ? 142 GLN   A OE1 1 
ATOM   1155 N NE2 . GLN   A 1 142 ? 9.191   21.959  19.403 1.00 49.14 ? 142 GLN   A NE2 1 
ATOM   1156 N N   . LEU   A 1 143 ? 15.407  21.324  17.237 1.00 31.95 ? 143 LEU   A N   1 
ATOM   1157 C CA  . LEU   A 1 143 ? 16.508  21.974  16.536 1.00 29.15 ? 143 LEU   A CA  1 
ATOM   1158 C C   . LEU   A 1 143 ? 17.673  21.036  16.312 1.00 28.94 ? 143 LEU   A C   1 
ATOM   1159 O O   . LEU   A 1 143 ? 18.729  21.476  15.843 1.00 43.89 ? 143 LEU   A O   1 
ATOM   1160 C CB  . LEU   A 1 143 ? 17.002  23.211  17.291 1.00 41.91 ? 143 LEU   A CB  1 
ATOM   1161 C CG  . LEU   A 1 143 ? 16.097  24.442  17.389 1.00 41.18 ? 143 LEU   A CG  1 
ATOM   1162 C CD1 . LEU   A 1 143 ? 16.794  25.539  18.198 1.00 53.93 ? 143 LEU   A CD1 1 
ATOM   1163 C CD2 . LEU   A 1 143 ? 15.710  24.941  16.007 1.00 34.57 ? 143 LEU   A CD2 1 
ATOM   1164 N N   . TYR   A 1 144 ? 17.514  19.766  16.662 1.00 27.79 ? 144 TYR   A N   1 
ATOM   1165 C CA  . TYR   A 1 144 ? 18.604  18.815  16.536 1.00 30.31 ? 144 TYR   A CA  1 
ATOM   1166 C C   . TYR   A 1 144 ? 19.139  18.793  15.114 1.00 22.54 ? 144 TYR   A C   1 
ATOM   1167 O O   . TYR   A 1 144 ? 18.377  18.669  14.150 1.00 30.97 ? 144 TYR   A O   1 
ATOM   1168 C CB  . TYR   A 1 144 ? 18.101  17.427  16.914 1.00 33.97 ? 144 TYR   A CB  1 
ATOM   1169 C CG  . TYR   A 1 144 ? 19.011  16.266  16.554 1.00 25.88 ? 144 TYR   A CG  1 
ATOM   1170 C CD1 . TYR   A 1 144 ? 20.086  15.905  17.369 1.00 25.29 ? 144 TYR   A CD1 1 
ATOM   1171 C CD2 . TYR   A 1 144 ? 18.772  15.506  15.411 1.00 20.52 ? 144 TYR   A CD2 1 
ATOM   1172 C CE1 . TYR   A 1 144 ? 20.904  14.818  17.046 1.00 25.29 ? 144 TYR   A CE1 1 
ATOM   1173 C CE2 . TYR   A 1 144 ? 19.582  14.429  15.080 1.00 24.47 ? 144 TYR   A CE2 1 
ATOM   1174 C CZ  . TYR   A 1 144 ? 20.642  14.083  15.903 1.00 25.52 ? 144 TYR   A CZ  1 
ATOM   1175 O OH  . TYR   A 1 144 ? 21.429  13.006  15.571 1.00 23.44 ? 144 TYR   A OH  1 
ATOM   1176 N N   . ARG   A 1 145 ? 20.456  18.883  14.986 1.00 34.59 ? 145 ARG   A N   1 
ATOM   1177 C CA  . ARG   A 1 145 ? 21.093  18.797  13.683 1.00 36.05 ? 145 ARG   A CA  1 
ATOM   1178 C C   . ARG   A 1 145 ? 21.937  17.550  13.503 1.00 32.46 ? 145 ARG   A C   1 
ATOM   1179 O O   . ARG   A 1 145 ? 22.156  17.127  12.364 1.00 44.35 ? 145 ARG   A O   1 
ATOM   1180 C CB  . ARG   A 1 145 ? 21.906  20.048  13.331 1.00 33.45 ? 145 ARG   A CB  1 
ATOM   1181 C CG  . ARG   A 1 145 ? 21.099  21.332  13.312 1.00 46.12 ? 145 ARG   A CG  1 
ATOM   1182 C CD  . ARG   A 1 145 ? 22.002  22.526  13.063 1.00 54.59 ? 145 ARG   A CD  1 
ATOM   1183 N NE  . ARG   A 1 145 ? 21.501  23.271  11.907 1.00 76.53 ? 145 ARG   A NE  1 
ATOM   1184 C CZ  . ARG   A 1 145 ? 21.691  22.915  10.638 1.00 81.90 ? 145 ARG   A CZ  1 
ATOM   1185 N NH1 . ARG   A 1 145 ? 22.373  21.824  10.317 1.00 73.56 ? 145 ARG   A NH1 1 
ATOM   1186 N NH2 . ARG   A 1 145 ? 21.171  23.663  9.666  1.00 71.99 ? 145 ARG   A NH2 1 
ATOM   1187 N N   . GLY   A 1 146 ? 22.435  16.958  14.572 1.00 27.48 ? 146 GLY   A N   1 
ATOM   1188 C CA  . GLY   A 1 146 ? 23.252  15.782  14.382 1.00 31.19 ? 146 GLY   A CA  1 
ATOM   1189 C C   . GLY   A 1 146 ? 24.013  15.446  15.632 1.00 30.85 ? 146 GLY   A C   1 
ATOM   1190 O O   . GLY   A 1 146 ? 24.024  16.192  16.616 1.00 30.06 ? 146 GLY   A O   1 
ATOM   1191 N N   . GLY   A 1 147 ? 24.614  14.273  15.592 1.00 30.48 ? 147 GLY   A N   1 
ATOM   1192 C CA  . GLY   A 1 147 ? 25.323  13.765  16.740 1.00 16.13 ? 147 GLY   A CA  1 
ATOM   1193 C C   . GLY   A 1 147 ? 24.431  12.853  17.542 1.00 34.04 ? 147 GLY   A C   1 
ATOM   1194 O O   . GLY   A 1 147 ? 23.256  12.630  17.235 1.00 32.07 ? 147 GLY   A O   1 
ATOM   1195 N N   . ILE   A 1 148 ? 25.002  12.337  18.619 1.00 32.14 ? 148 ILE   A N   1 
ATOM   1196 C CA  . ILE   A 1 148 ? 24.234  11.494  19.520 1.00 34.92 ? 148 ILE   A CA  1 
ATOM   1197 C C   . ILE   A 1 148 ? 23.484  12.423  20.472 1.00 27.68 ? 148 ILE   A C   1 
ATOM   1198 O O   . ILE   A 1 148 ? 24.095  13.128  21.281 1.00 26.47 ? 148 ILE   A O   1 
ATOM   1199 C CB  . ILE   A 1 148 ? 25.133  10.497  20.259 1.00 36.24 ? 148 ILE   A CB  1 
ATOM   1200 C CG1 . ILE   A 1 148 ? 25.689  9.496   19.239 1.00 24.05 ? 148 ILE   A CG1 1 
ATOM   1201 C CG2 . ILE   A 1 148 ? 24.377  9.795   21.400 1.00 27.49 ? 148 ILE   A CG2 1 
ATOM   1202 C CD1 . ILE   A 1 148 ? 26.762  8.625   19.771 1.00 34.47 ? 148 ILE   A CD1 1 
ATOM   1203 N N   . PHE   A 1 149 ? 22.157  12.462  20.333 1.00 17.52 ? 149 PHE   A N   1 
ATOM   1204 C CA  . PHE   A 1 149 ? 21.328  13.402  21.077 1.00 27.24 ? 149 PHE   A CA  1 
ATOM   1205 C C   . PHE   A 1 149 ? 21.144  12.932  22.508 1.00 28.19 ? 149 PHE   A C   1 
ATOM   1206 O O   . PHE   A 1 149 ? 20.723  11.798  22.748 1.00 31.11 ? 149 PHE   A O   1 
ATOM   1207 C CB  . PHE   A 1 149 ? 19.957  13.545  20.411 1.00 19.42 ? 149 PHE   A CB  1 
ATOM   1208 C CG  . PHE   A 1 149 ? 19.076  14.593  21.045 1.00 20.71 ? 149 PHE   A CG  1 
ATOM   1209 C CD1 . PHE   A 1 149 ? 19.349  15.947  20.905 1.00 23.13 ? 149 PHE   A CD1 1 
ATOM   1210 C CD2 . PHE   A 1 149 ? 17.982  14.212  21.813 1.00 27.25 ? 149 PHE   A CD2 1 
ATOM   1211 C CE1 . PHE   A 1 149 ? 18.521  16.906  21.498 1.00 19.40 ? 149 PHE   A CE1 1 
ATOM   1212 C CE2 . PHE   A 1 149 ? 17.157  15.161  22.401 1.00 28.78 ? 149 PHE   A CE2 1 
ATOM   1213 C CZ  . PHE   A 1 149 ? 17.427  16.510  22.240 1.00 22.42 ? 149 PHE   A CZ  1 
ATOM   1214 N N   . VAL   A 1 150 ? 21.462  13.801  23.464 1.00 27.20 ? 150 VAL   A N   1 
ATOM   1215 C CA  . VAL   A 1 150 ? 21.313  13.452  24.871 1.00 37.85 ? 150 VAL   A CA  1 
ATOM   1216 C C   . VAL   A 1 150 ? 20.245  14.278  25.555 1.00 33.07 ? 150 VAL   A C   1 
ATOM   1217 O O   . VAL   A 1 150 ? 20.039  14.129  26.769 1.00 30.45 ? 150 VAL   A O   1 
ATOM   1218 C CB  . VAL   A 1 150 ? 22.655  13.580  25.620 1.00 36.89 ? 150 VAL   A CB  1 
ATOM   1219 C CG1 . VAL   A 1 150 ? 23.737  12.791  24.882 1.00 30.80 ? 150 VAL   A CG1 1 
ATOM   1220 C CG2 . VAL   A 1 150 ? 23.054  15.038  25.795 1.00 36.37 ? 150 VAL   A CG2 1 
ATOM   1221 N N   . GLY   A 1 151 ? 19.559  15.150  24.817 1.00 27.96 ? 151 GLY   A N   1 
ATOM   1222 C CA  . GLY   A 1 151 ? 18.691  16.148  25.397 1.00 24.19 ? 151 GLY   A CA  1 
ATOM   1223 C C   . GLY   A 1 151 ? 19.328  17.531  25.418 1.00 23.42 ? 151 GLY   A C   1 
ATOM   1224 O O   . GLY   A 1 151 ? 20.244  17.839  24.645 1.00 19.99 ? 151 GLY   A O   1 
ATOM   1225 N N   . PRO   A 1 152 ? 18.851  18.403  26.303 1.00 19.09 ? 152 PRO   A N   1 
ATOM   1226 C CA  . PRO   A 1 152 ? 17.823  18.191  27.324 1.00 26.39 ? 152 PRO   A CA  1 
ATOM   1227 C C   . PRO   A 1 152 ? 16.467  17.799  26.785 1.00 33.86 ? 152 PRO   A C   1 
ATOM   1228 O O   . PRO   A 1 152 ? 16.036  18.221  25.714 1.00 37.39 ? 152 PRO   A O   1 
ATOM   1229 C CB  . PRO   A 1 152 ? 17.742  19.564  28.017 1.00 35.21 ? 152 PRO   A CB  1 
ATOM   1230 C CG  . PRO   A 1 152 ? 19.088  20.144  27.834 1.00 29.53 ? 152 PRO   A CG  1 
ATOM   1231 C CD  . PRO   A 1 152 ? 19.500  19.713  26.460 1.00 25.11 ? 152 PRO   A CD  1 
ATOM   1232 N N   . CYS   A 1 153 ? 15.787  16.959  27.549 1.00 35.96 ? 153 CYS   A N   1 
ATOM   1233 C CA  . CYS   A 1 153 ? 14.406  16.627  27.260 1.00 41.87 ? 153 CYS   A CA  1 
ATOM   1234 C C   . CYS   A 1 153 ? 13.862  15.940  28.490 1.00 43.51 ? 153 CYS   A C   1 
ATOM   1235 O O   . CYS   A 1 153 ? 14.615  15.337  29.262 1.00 39.04 ? 153 CYS   A O   1 
ATOM   1236 C CB  . CYS   A 1 153 ? 14.218  15.726  26.024 1.00 49.80 ? 153 CYS   A CB  1 
ATOM   1237 S SG  . CYS   A 1 153 ? 15.158  14.174  25.874 1.00 56.25 ? 153 CYS   A SG  1 
ATOM   1238 N N   . GLY   A 1 154 ? 12.551  16.040  28.664 1.00 32.98 ? 154 GLY   A N   1 
ATOM   1239 C CA  . GLY   A 1 154 ? 11.863  15.292  29.683 1.00 25.58 ? 154 GLY   A CA  1 
ATOM   1240 C C   . GLY   A 1 154 ? 11.339  14.013  29.082 1.00 33.64 ? 154 GLY   A C   1 
ATOM   1241 O O   . GLY   A 1 154 ? 11.668  13.639  27.955 1.00 39.72 ? 154 GLY   A O   1 
ATOM   1242 N N   . ASN   A 1 155 ? 10.487  13.341  29.846 1.00 45.44 ? 155 ASN   A N   1 
ATOM   1243 C CA  . ASN   A 1 155 ? 9.907   12.073  29.434 1.00 34.55 ? 155 ASN   A CA  1 
ATOM   1244 C C   . ASN   A 1 155 ? 8.410   12.191  29.139 1.00 39.54 ? 155 ASN   A C   1 
ATOM   1245 O O   . ASN   A 1 155 ? 7.678   11.201  29.229 1.00 43.77 ? 155 ASN   A O   1 
ATOM   1246 C CB  . ASN   A 1 155 ? 10.165  11.023  30.509 1.00 36.76 ? 155 ASN   A CB  1 
ATOM   1247 C CG  . ASN   A 1 155 ? 9.642   11.462  31.855 1.00 66.68 ? 155 ASN   A CG  1 
ATOM   1248 O OD1 . ASN   A 1 155 ? 10.022  12.520  32.362 1.00 55.30 ? 155 ASN   A OD1 1 
ATOM   1249 N ND2 . ASN   A 1 155 ? 8.711   10.696  32.409 1.00 76.34 ? 155 ASN   A ND2 1 
ATOM   1250 N N   . LYS   A 1 156 ? 7.939   13.395  28.786 1.00 35.58 ? 156 LYS   A N   1 
ATOM   1251 C CA  . LYS   A 1 156 ? 6.517   13.623  28.496 1.00 39.59 ? 156 LYS   A CA  1 
ATOM   1252 C C   . LYS   A 1 156 ? 6.329   13.338  27.004 1.00 32.07 ? 156 LYS   A C   1 
ATOM   1253 O O   . LYS   A 1 156 ? 6.378   14.222  26.141 1.00 27.30 ? 156 LYS   A O   1 
ATOM   1254 C CB  . LYS   A 1 156 ? 6.105   15.042  28.906 1.00 36.69 ? 156 LYS   A CB  1 
ATOM   1255 C CG  . LYS   A 1 156 ? 4.858   15.653  28.230 1.00 56.86 ? 156 LYS   A CG  1 
ATOM   1256 C CD  . LYS   A 1 156 ? 3.579   14.863  28.555 1.00 62.10 ? 156 LYS   A CD  1 
ATOM   1257 C CE  . LYS   A 1 156 ? 2.303   15.717  28.457 1.00 43.47 ? 156 LYS   A CE  1 
ATOM   1258 N NZ  . LYS   A 1 156 ? 2.404   17.044  29.145 1.00 40.68 ? 156 LYS   A NZ  1 
ATOM   1259 N N   . VAL   A 1 157 ? 6.150   12.054  26.692 1.00 29.43 ? 157 VAL   A N   1 
ATOM   1260 C CA  . VAL   A 1 157 ? 6.203   11.639  25.297 1.00 33.28 ? 157 VAL   A CA  1 
ATOM   1261 C C   . VAL   A 1 157 ? 4.974   12.157  24.569 1.00 30.43 ? 157 VAL   A C   1 
ATOM   1262 O O   . VAL   A 1 157 ? 3.873   12.231  25.133 1.00 23.03 ? 157 VAL   A O   1 
ATOM   1263 C CB  . VAL   A 1 157 ? 6.337   10.113  25.167 1.00 25.09 ? 157 VAL   A CB  1 
ATOM   1264 C CG1 . VAL   A 1 157 ? 7.634   9.659   25.796 1.00 28.47 ? 157 VAL   A CG1 1 
ATOM   1265 C CG2 . VAL   A 1 157 ? 5.145   9.398   25.783 1.00 24.36 ? 157 VAL   A CG2 1 
ATOM   1266 N N   . ASP   A 1 158 ? 5.175   12.552  23.315 1.00 26.26 ? 158 ASP   A N   1 
ATOM   1267 C CA  . ASP   A 1 158 ? 4.134   13.225  22.549 1.00 19.85 ? 158 ASP   A CA  1 
ATOM   1268 C C   . ASP   A 1 158 ? 4.297   12.980  21.057 1.00 24.66 ? 158 ASP   A C   1 
ATOM   1269 O O   . ASP   A 1 158 ? 3.516   13.532  20.268 1.00 26.35 ? 158 ASP   A O   1 
ATOM   1270 C CB  . ASP   A 1 158 ? 4.163   14.732  22.834 1.00 17.18 ? 158 ASP   A CB  1 
ATOM   1271 C CG  . ASP   A 1 158 ? 5.532   15.368  22.537 1.00 35.31 ? 158 ASP   A CG  1 
ATOM   1272 O OD1 . ASP   A 1 158 ? 6.278   14.867  21.669 1.00 26.56 ? 158 ASP   A OD1 1 
ATOM   1273 O OD2 . ASP   A 1 158 ? 5.882   16.367  23.206 1.00 41.19 ? 158 ASP   A OD2 1 
ATOM   1274 N N   . HIS   A 1 159 ? 5.219   12.114  20.647 1.00 22.85 ? 159 HIS   A N   1 
ATOM   1275 C CA  . HIS   A 1 159 ? 5.592   12.027  19.244 1.00 25.15 ? 159 HIS   A CA  1 
ATOM   1276 C C   . HIS   A 1 159 ? 6.016   10.602  18.985 1.00 18.13 ? 159 HIS   A C   1 
ATOM   1277 O O   . HIS   A 1 159 ? 6.928   10.106  19.648 1.00 28.98 ? 159 HIS   A O   1 
ATOM   1278 C CB  . HIS   A 1 159 ? 6.743   12.970  18.926 1.00 20.84 ? 159 HIS   A CB  1 
ATOM   1279 C CG  . HIS   A 1 159 ? 7.064   13.060  17.473 1.00 24.46 ? 159 HIS   A CG  1 
ATOM   1280 N ND1 . HIS   A 1 159 ? 6.110   13.341  16.518 1.00 21.35 ? 159 HIS   A ND1 1 
ATOM   1281 C CD2 . HIS   A 1 159 ? 8.230   12.896  16.806 1.00 27.02 ? 159 HIS   A CD2 1 
ATOM   1282 C CE1 . HIS   A 1 159 ? 6.678   13.355  15.325 1.00 24.94 ? 159 HIS   A CE1 1 
ATOM   1283 N NE2 . HIS   A 1 159 ? 7.964   13.084  15.471 1.00 23.04 ? 159 HIS   A NE2 1 
ATOM   1284 N N   . ALA   A 1 160 ? 5.383   9.965   18.008 1.00 21.44 ? 160 ALA   A N   1 
ATOM   1285 C CA  . ALA   A 1 160 ? 5.699   8.590   17.662 1.00 19.68 ? 160 ALA   A CA  1 
ATOM   1286 C C   . ALA   A 1 160 ? 6.651   8.578   16.477 1.00 13.05 ? 160 ALA   A C   1 
ATOM   1287 O O   . ALA   A 1 160 ? 6.445   9.295   15.494 1.00 19.91 ? 160 ALA   A O   1 
ATOM   1288 C CB  . ALA   A 1 160 ? 4.432   7.794   17.346 1.00 16.20 ? 160 ALA   A CB  1 
ATOM   1289 N N   . VAL   A 1 161 ? 7.690   7.755   16.575 1.00 10.10 ? 161 VAL   A N   1 
ATOM   1290 C CA  . VAL   A 1 161 ? 8.735   7.662   15.562 1.00 16.73 ? 161 VAL   A CA  1 
ATOM   1291 C C   . VAL   A 1 161 ? 9.084   6.191   15.459 1.00 14.34 ? 161 VAL   A C   1 
ATOM   1292 O O   . VAL   A 1 161 ? 8.451   5.350   16.115 1.00 14.70 ? 161 VAL   A O   1 
ATOM   1293 C CB  . VAL   A 1 161 ? 9.974   8.501   15.918 1.00 14.96 ? 161 VAL   A CB  1 
ATOM   1294 C CG1 . VAL   A 1 161 ? 9.644   9.964   15.916 1.00 16.44 ? 161 VAL   A CG1 1 
ATOM   1295 C CG2 . VAL   A 1 161 ? 10.445  8.116   17.292 1.00 30.69 ? 161 VAL   A CG2 1 
ATOM   1296 N N   . ALA   A 1 162 ? 10.143  5.858   14.729 1.00 12.17 ? 162 ALA   A N   1 
ATOM   1297 C CA  . ALA   A 1 162 ? 10.458  4.447   14.595 1.00 12.78 ? 162 ALA   A CA  1 
ATOM   1298 C C   . ALA   A 1 162 ? 11.932  4.220   14.845 1.00 13.11 ? 162 ALA   A C   1 
ATOM   1299 O O   . ALA   A 1 162 ? 12.781  4.922   14.292 1.00 14.63 ? 162 ALA   A O   1 
ATOM   1300 C CB  . ALA   A 1 162 ? 10.055  3.921   13.216 1.00 14.89 ? 162 ALA   A CB  1 
ATOM   1301 N N   . ALA   A 1 163 ? 12.236  3.221   15.664 1.00 19.92 ? 163 ALA   A N   1 
ATOM   1302 C CA  . ALA   A 1 163 ? 13.613  2.825   15.916 1.00 21.47 ? 163 ALA   A CA  1 
ATOM   1303 C C   . ALA   A 1 163 ? 13.999  1.785   14.875 1.00 29.36 ? 163 ALA   A C   1 
ATOM   1304 O O   . ALA   A 1 163 ? 13.323  0.758   14.728 1.00 29.46 ? 163 ALA   A O   1 
ATOM   1305 C CB  . ALA   A 1 163 ? 13.761  2.260   17.327 1.00 23.85 ? 163 ALA   A CB  1 
ATOM   1306 N N   . VAL   A 1 164 ? 15.047  2.086   14.116 1.00 21.50 ? 164 VAL   A N   1 
ATOM   1307 C CA  . VAL   A 1 164 ? 15.501  1.243   13.024 1.00 20.67 ? 164 VAL   A CA  1 
ATOM   1308 C C   . VAL   A 1 164 ? 16.934  0.771   13.228 1.00 25.27 ? 164 VAL   A C   1 
ATOM   1309 O O   . VAL   A 1 164 ? 17.512  0.160   12.331 1.00 26.75 ? 164 VAL   A O   1 
ATOM   1310 C CB  . VAL   A 1 164 ? 15.354  1.968   11.677 1.00 26.45 ? 164 VAL   A CB  1 
ATOM   1311 C CG1 . VAL   A 1 164 ? 13.886  2.273   11.423 1.00 22.82 ? 164 VAL   A CG1 1 
ATOM   1312 C CG2 . VAL   A 1 164 ? 16.200  3.233   11.691 1.00 25.83 ? 164 VAL   A CG2 1 
ATOM   1313 N N   . GLY   A 1 165 ? 17.521  1.035   14.390 1.00 24.87 ? 165 GLY   A N   1 
ATOM   1314 C CA  . GLY   A 1 165 ? 18.861  0.545   14.669 1.00 15.03 ? 165 GLY   A CA  1 
ATOM   1315 C C   . GLY   A 1 165 ? 19.354  1.025   16.015 1.00 18.37 ? 165 GLY   A C   1 
ATOM   1316 O O   . GLY   A 1 165 ? 18.643  1.701   16.765 1.00 20.91 ? 165 GLY   A O   1 
ATOM   1317 N N   . TYR   A 1 166 ? 20.609  0.702   16.295 1.00 23.30 ? 166 TYR   A N   1 
ATOM   1318 C CA  . TYR   A 1 166 ? 21.238  1.116   17.543 1.00 17.49 ? 166 TYR   A CA  1 
ATOM   1319 C C   . TYR   A 1 166 ? 22.736  0.907   17.405 1.00 18.51 ? 166 TYR   A C   1 
ATOM   1320 O O   . TYR   A 1 166 ? 23.213  0.235   16.485 1.00 22.11 ? 166 TYR   A O   1 
ATOM   1321 C CB  . TYR   A 1 166 ? 20.674  0.357   18.761 1.00 15.89 ? 166 TYR   A CB  1 
ATOM   1322 C CG  . TYR   A 1 166 ? 20.918  -1.142  18.781 1.00 30.23 ? 166 TYR   A CG  1 
ATOM   1323 C CD1 . TYR   A 1 166 ? 22.165  -1.662  19.148 1.00 30.18 ? 166 TYR   A CD1 1 
ATOM   1324 C CD2 . TYR   A 1 166 ? 19.910  -2.042  18.420 1.00 23.09 ? 166 TYR   A CD2 1 
ATOM   1325 C CE1 . TYR   A 1 166 ? 22.414  -3.026  19.153 1.00 18.01 ? 166 TYR   A CE1 1 
ATOM   1326 C CE2 . TYR   A 1 166 ? 20.146  -3.408  18.424 1.00 20.23 ? 166 TYR   A CE2 1 
ATOM   1327 C CZ  . TYR   A 1 166 ? 21.411  -3.892  18.801 1.00 32.87 ? 166 TYR   A CZ  1 
ATOM   1328 O OH  . TYR   A 1 166 ? 21.690  -5.240  18.821 1.00 27.18 ? 166 TYR   A OH  1 
ATOM   1329 N N   . GLY   A 1 167 ? 23.465  1.475   18.353 1.00 22.68 ? 167 GLY   A N   1 
ATOM   1330 C CA  . GLY   A 1 167 ? 24.881  1.239   18.496 1.00 33.77 ? 167 GLY   A CA  1 
ATOM   1331 C C   . GLY   A 1 167 ? 25.192  1.158   19.974 1.00 29.82 ? 167 GLY   A C   1 
ATOM   1332 O O   . GLY   A 1 167 ? 24.279  1.102   20.811 1.00 23.07 ? 167 GLY   A O   1 
ATOM   1333 N N   . PRO   A 1 168 ? 26.473  1.077   20.328 1.00 30.24 ? 168 PRO   A N   1 
ATOM   1334 C CA  . PRO   A 1 168 ? 26.814  0.936   21.752 1.00 24.39 ? 168 PRO   A CA  1 
ATOM   1335 C C   . PRO   A 1 168 ? 26.209  2.026   22.617 1.00 20.24 ? 168 PRO   A C   1 
ATOM   1336 O O   . PRO   A 1 168 ? 25.785  1.737   23.740 1.00 22.77 ? 168 PRO   A O   1 
ATOM   1337 C CB  . PRO   A 1 168 ? 28.348  0.990   21.746 1.00 22.02 ? 168 PRO   A CB  1 
ATOM   1338 C CG  . PRO   A 1 168 ? 28.721  0.399   20.410 1.00 26.98 ? 168 PRO   A CG  1 
ATOM   1339 C CD  . PRO   A 1 168 ? 27.635  0.844   19.452 1.00 32.58 ? 168 PRO   A CD  1 
ATOM   1340 N N   . ASN   A 1 169 ? 26.106  3.260   22.118 1.00 23.71 ? 169 ASN   A N   1 
ATOM   1341 C CA  . ASN   A 1 169 ? 25.681  4.387   22.944 1.00 27.03 ? 169 ASN   A CA  1 
ATOM   1342 C C   . ASN   A 1 169 ? 24.458  5.118   22.385 1.00 34.13 ? 169 ASN   A C   1 
ATOM   1343 O O   . ASN   A 1 169 ? 24.173  6.245   22.813 1.00 34.47 ? 169 ASN   A O   1 
ATOM   1344 C CB  . ASN   A 1 169 ? 26.848  5.368   23.152 1.00 16.83 ? 169 ASN   A CB  1 
ATOM   1345 C CG  . ASN   A 1 169 ? 27.536  5.766   21.839 1.00 29.04 ? 169 ASN   A CG  1 
ATOM   1346 O OD1 . ASN   A 1 169 ? 27.211  5.247   20.766 1.00 32.33 ? 169 ASN   A OD1 1 
ATOM   1347 N ND2 . ASN   A 1 169 ? 28.499  6.669   21.929 1.00 43.33 ? 169 ASN   A ND2 1 
ATOM   1348 N N   . TYR   A 1 170 ? 23.705  4.510   21.470 1.00 27.16 ? 170 TYR   A N   1 
ATOM   1349 C CA  . TYR   A 1 170 ? 22.558  5.222   20.922 1.00 29.51 ? 170 TYR   A CA  1 
ATOM   1350 C C   . TYR   A 1 170 ? 21.557  4.238   20.329 1.00 24.85 ? 170 TYR   A C   1 
ATOM   1351 O O   . TYR   A 1 170 ? 21.849  3.060   20.098 1.00 24.59 ? 170 TYR   A O   1 
ATOM   1352 C CB  . TYR   A 1 170 ? 22.956  6.212   19.821 1.00 22.33 ? 170 TYR   A CB  1 
ATOM   1353 C CG  . TYR   A 1 170 ? 23.518  5.539   18.589 1.00 27.29 ? 170 TYR   A CG  1 
ATOM   1354 C CD1 . TYR   A 1 170 ? 24.879  5.242   18.495 1.00 27.66 ? 170 TYR   A CD1 1 
ATOM   1355 C CD2 . TYR   A 1 170 ? 22.695  5.204   17.511 1.00 27.16 ? 170 TYR   A CD2 1 
ATOM   1356 C CE1 . TYR   A 1 170 ? 25.397  4.618   17.358 1.00 23.85 ? 170 TYR   A CE1 1 
ATOM   1357 C CE2 . TYR   A 1 170 ? 23.204  4.589   16.371 1.00 31.64 ? 170 TYR   A CE2 1 
ATOM   1358 C CZ  . TYR   A 1 170 ? 24.554  4.295   16.303 1.00 25.31 ? 170 TYR   A CZ  1 
ATOM   1359 O OH  . TYR   A 1 170 ? 25.064  3.681   15.183 1.00 26.62 ? 170 TYR   A OH  1 
ATOM   1360 N N   . ILE   A 1 171 ? 20.362  4.765   20.083 1.00 21.40 ? 171 ILE   A N   1 
ATOM   1361 C CA  . ILE   A 1 171 ? 19.328  4.132   19.276 1.00 22.02 ? 171 ILE   A CA  1 
ATOM   1362 C C   . ILE   A 1 171 ? 19.056  5.039   18.087 1.00 23.54 ? 171 ILE   A C   1 
ATOM   1363 O O   . ILE   A 1 171 ? 18.956  6.264   18.234 1.00 25.02 ? 171 ILE   A O   1 
ATOM   1364 C CB  . ILE   A 1 171 ? 18.050  3.866   20.092 1.00 18.04 ? 171 ILE   A CB  1 
ATOM   1365 C CG1 . ILE   A 1 171 ? 18.324  2.696   21.037 1.00 24.59 ? 171 ILE   A CG1 1 
ATOM   1366 C CG2 . ILE   A 1 171 ? 16.872  3.572   19.189 1.00 25.38 ? 171 ILE   A CG2 1 
ATOM   1367 C CD1 . ILE   A 1 171 ? 17.236  2.438   22.047 1.00 36.98 ? 171 ILE   A CD1 1 
ATOM   1368 N N   . LEU   A 1 172 ? 18.946  4.428   16.912 1.00 23.27 ? 172 LEU   A N   1 
ATOM   1369 C CA  . LEU   A 1 172 ? 18.814  5.139   15.650 1.00 20.77 ? 172 LEU   A CA  1 
ATOM   1370 C C   . LEU   A 1 172 ? 17.338  5.268   15.320 1.00 23.43 ? 172 LEU   A C   1 
ATOM   1371 O O   . LEU   A 1 172 ? 16.631  4.257   15.248 1.00 26.02 ? 172 LEU   A O   1 
ATOM   1372 C CB  . LEU   A 1 172 ? 19.546  4.400   14.526 1.00 18.34 ? 172 LEU   A CB  1 
ATOM   1373 C CG  . LEU   A 1 172 ? 19.390  4.947   13.107 1.00 27.69 ? 172 LEU   A CG  1 
ATOM   1374 C CD1 . LEU   A 1 172 ? 19.997  6.335   12.963 1.00 28.39 ? 172 LEU   A CD1 1 
ATOM   1375 C CD2 . LEU   A 1 172 ? 19.961  3.957   12.095 1.00 20.98 ? 172 LEU   A CD2 1 
ATOM   1376 N N   . ILE   A 1 173 ? 16.874  6.501   15.119 1.00 24.51 ? 173 ILE   A N   1 
ATOM   1377 C CA  . ILE   A 1 173 ? 15.459  6.819   15.018 1.00 23.88 ? 173 ILE   A CA  1 
ATOM   1378 C C   . ILE   A 1 173 ? 15.187  7.446   13.655 1.00 26.56 ? 173 ILE   A C   1 
ATOM   1379 O O   . ILE   A 1 173 ? 15.841  8.421   13.267 1.00 18.00 ? 173 ILE   A O   1 
ATOM   1380 C CB  . ILE   A 1 173 ? 15.015  7.778   16.138 1.00 22.65 ? 173 ILE   A CB  1 
ATOM   1381 C CG1 . ILE   A 1 173 ? 15.203  7.158   17.527 1.00 21.65 ? 173 ILE   A CG1 1 
ATOM   1382 C CG2 . ILE   A 1 173 ? 13.583  8.223   15.917 1.00 16.66 ? 173 ILE   A CG2 1 
ATOM   1383 C CD1 . ILE   A 1 173 ? 14.355  5.902   17.777 1.00 23.10 ? 173 ILE   A CD1 1 
ATOM   1384 N N   . LYS   A 1 174 ? 14.203  6.892   12.950 1.00 22.73 ? 174 LYS   A N   1 
ATOM   1385 C CA  . LYS   A 1 174 ? 13.631  7.475   11.748 1.00 19.02 ? 174 LYS   A CA  1 
ATOM   1386 C C   . LYS   A 1 174 ? 12.484  8.351   12.204 1.00 19.00 ? 174 LYS   A C   1 
ATOM   1387 O O   . LYS   A 1 174 ? 11.496  7.860   12.782 1.00 27.09 ? 174 LYS   A O   1 
ATOM   1388 C CB  . LYS   A 1 174 ? 13.133  6.409   10.775 1.00 24.48 ? 174 LYS   A CB  1 
ATOM   1389 C CG  . LYS   A 1 174 ? 12.631  6.981   9.459  1.00 24.62 ? 174 LYS   A CG  1 
ATOM   1390 C CD  . LYS   A 1 174 ? 12.105  5.899   8.533  1.00 21.62 ? 174 LYS   A CD  1 
ATOM   1391 C CE  . LYS   A 1 174 ? 11.833  6.439   7.151  1.00 12.44 ? 174 LYS   A CE  1 
ATOM   1392 N NZ  . LYS   A 1 174 ? 11.017  5.462   6.388  1.00 28.96 ? 174 LYS   A NZ  1 
ATOM   1393 N N   . ASN   A 1 175 ? 12.646  9.641   11.995 1.00 22.27 ? 175 ASN   A N   1 
ATOM   1394 C CA  . ASN   A 1 175 ? 11.618  10.613  12.292 1.00 20.25 ? 175 ASN   A CA  1 
ATOM   1395 C C   . ASN   A 1 175 ? 10.786  10.845  11.034 1.00 23.90 ? 175 ASN   A C   1 
ATOM   1396 O O   . ASN   A 1 175 ? 11.118  10.389  9.937  1.00 14.99 ? 175 ASN   A O   1 
ATOM   1397 C CB  . ASN   A 1 175 ? 12.265  11.911  12.781 1.00 16.08 ? 175 ASN   A CB  1 
ATOM   1398 C CG  . ASN   A 1 175 ? 11.315  12.783  13.565 1.00 23.40 ? 175 ASN   A CG  1 
ATOM   1399 O OD1 . ASN   A 1 175 ? 10.154  12.420  13.790 1.00 19.85 ? 175 ASN   A OD1 1 
ATOM   1400 N ND2 . ASN   A 1 175 ? 11.803  13.952  13.994 1.00 21.60 ? 175 ASN   A ND2 1 
ATOM   1401 N N   . SER   A 1 176 ? 9.668   11.521  11.211 1.00 28.08 ? 176 SER   A N   1 
ATOM   1402 C CA  . SER   A 1 176 ? 8.762   11.791  10.114 1.00 26.42 ? 176 SER   A CA  1 
ATOM   1403 C C   . SER   A 1 176 ? 8.643   13.289  9.891  1.00 25.81 ? 176 SER   A C   1 
ATOM   1404 O O   . SER   A 1 176 ? 7.560   13.805  9.603  1.00 27.56 ? 176 SER   A O   1 
ATOM   1405 C CB  . SER   A 1 176 ? 7.402   11.160  10.373 1.00 25.27 ? 176 SER   A CB  1 
ATOM   1406 O OG  . SER   A 1 176 ? 6.956   11.526  11.668 1.00 21.67 ? 176 SER   A OG  1 
ATOM   1407 N N   . TRP   A 1 177 ? 9.776   13.995  9.956  1.00 23.11 ? 177 TRP   A N   1 
ATOM   1408 C CA  . TRP   A 1 177 ? 9.806   15.440  9.763  1.00 18.78 ? 177 TRP   A CA  1 
ATOM   1409 C C   . TRP   A 1 177 ? 10.557  15.832  8.497  1.00 20.01 ? 177 TRP   A C   1 
ATOM   1410 O O   . TRP   A 1 177 ? 10.979  16.981  8.363  1.00 22.76 ? 177 TRP   A O   1 
ATOM   1411 C CB  . TRP   A 1 177 ? 10.436  16.147  10.971 1.00 22.66 ? 177 TRP   A CB  1 
ATOM   1412 C CG  . TRP   A 1 177 ? 9.584   16.181  12.236 1.00 34.62 ? 177 TRP   A CG  1 
ATOM   1413 C CD1 . TRP   A 1 177 ? 8.292   15.740  12.376 1.00 32.27 ? 177 TRP   A CD1 1 
ATOM   1414 C CD2 . TRP   A 1 177 ? 9.969   16.704  13.523 1.00 32.74 ? 177 TRP   A CD2 1 
ATOM   1415 N NE1 . TRP   A 1 177 ? 7.861   15.940  13.673 1.00 32.58 ? 177 TRP   A NE1 1 
ATOM   1416 C CE2 . TRP   A 1 177 ? 8.866   16.534  14.394 1.00 31.70 ? 177 TRP   A CE2 1 
ATOM   1417 C CE3 . TRP   A 1 177 ? 11.140  17.289  14.024 1.00 23.96 ? 177 TRP   A CE3 1 
ATOM   1418 C CZ2 . TRP   A 1 177 ? 8.899   16.934  15.738 1.00 25.79 ? 177 TRP   A CZ2 1 
ATOM   1419 C CZ3 . TRP   A 1 177 ? 11.169  17.696  15.359 1.00 31.74 ? 177 TRP   A CZ3 1 
ATOM   1420 C CH2 . TRP   A 1 177 ? 10.055  17.511  16.202 1.00 32.30 ? 177 TRP   A CH2 1 
ATOM   1421 N N   . GLY   A 1 178 ? 10.681  14.918  7.546  1.00 21.74 ? 178 GLY   A N   1 
ATOM   1422 C CA  . GLY   A 1 178 ? 11.365  15.194  6.303  1.00 22.19 ? 178 GLY   A CA  1 
ATOM   1423 C C   . GLY   A 1 178 ? 12.859  14.927  6.395  1.00 22.26 ? 178 GLY   A C   1 
ATOM   1424 O O   . GLY   A 1 178 ? 13.429  14.708  7.469  1.00 21.27 ? 178 GLY   A O   1 
ATOM   1425 N N   . THR   A 1 179 ? 13.506  14.935  5.229  1.00 16.95 ? 179 THR   A N   1 
ATOM   1426 C CA  . THR   A 1 179 ? 14.930  14.618  5.157  1.00 17.59 ? 179 THR   A CA  1 
ATOM   1427 C C   . THR   A 1 179 ? 15.834  15.768  5.602  1.00 22.25 ? 179 THR   A C   1 
ATOM   1428 O O   . THR   A 1 179 ? 17.043  15.557  5.762  1.00 23.66 ? 179 THR   A O   1 
ATOM   1429 C CB  . THR   A 1 179 ? 15.313  14.191  3.735  1.00 20.53 ? 179 THR   A CB  1 
ATOM   1430 O OG1 . THR   A 1 179 ? 14.980  15.228  2.803  1.00 23.56 ? 179 THR   A OG1 1 
ATOM   1431 C CG2 . THR   A 1 179 ? 14.600  12.896  3.344  1.00 18.19 ? 179 THR   A CG2 1 
ATOM   1432 N N   . GLY   A 1 180 ? 15.289  16.968  5.816  1.00 21.67 ? 180 GLY   A N   1 
ATOM   1433 C CA  . GLY   A 1 180 ? 16.072  18.112  6.250  1.00 23.14 ? 180 GLY   A CA  1 
ATOM   1434 C C   . GLY   A 1 180 ? 16.274  18.268  7.736  1.00 24.93 ? 180 GLY   A C   1 
ATOM   1435 O O   . GLY   A 1 180 ? 16.990  19.174  8.165  1.00 23.25 ? 180 GLY   A O   1 
ATOM   1436 N N   . TRP   A 1 181 ? 15.601  17.464  8.537  1.00 23.07 ? 181 TRP   A N   1 
ATOM   1437 C CA  . TRP   A 1 181 ? 15.746  17.503  9.983  1.00 26.13 ? 181 TRP   A CA  1 
ATOM   1438 C C   . TRP   A 1 181 ? 16.794  16.505  10.449 1.00 24.34 ? 181 TRP   A C   1 
ATOM   1439 O O   . TRP   A 1 181 ? 16.895  15.405  9.901  1.00 27.18 ? 181 TRP   A O   1 
ATOM   1440 C CB  . TRP   A 1 181 ? 14.413  17.214  10.679 1.00 20.95 ? 181 TRP   A CB  1 
ATOM   1441 C CG  . TRP   A 1 181 ? 14.523  17.243  12.171 1.00 22.93 ? 181 TRP   A CG  1 
ATOM   1442 C CD1 . TRP   A 1 181 ? 14.426  18.340  12.981 1.00 16.47 ? 181 TRP   A CD1 1 
ATOM   1443 C CD2 . TRP   A 1 181 ? 14.716  16.115  13.039 1.00 22.91 ? 181 TRP   A CD2 1 
ATOM   1444 N NE1 . TRP   A 1 181 ? 14.559  17.966  14.296 1.00 14.40 ? 181 TRP   A NE1 1 
ATOM   1445 C CE2 . TRP   A 1 181 ? 14.737  16.606  14.361 1.00 20.36 ? 181 TRP   A CE2 1 
ATOM   1446 C CE3 . TRP   A 1 181 ? 14.884  14.739  12.827 1.00 22.90 ? 181 TRP   A CE3 1 
ATOM   1447 C CZ2 . TRP   A 1 181 ? 14.928  15.767  15.473 1.00 16.48 ? 181 TRP   A CZ2 1 
ATOM   1448 C CZ3 . TRP   A 1 181 ? 15.064  13.908  13.932 1.00 20.75 ? 181 TRP   A CZ3 1 
ATOM   1449 C CH2 . TRP   A 1 181 ? 15.081  14.430  15.237 1.00 15.02 ? 181 TRP   A CH2 1 
ATOM   1450 N N   . GLY   A 1 182 ? 17.621  16.921  11.406 1.00 20.37 ? 182 GLY   A N   1 
ATOM   1451 C CA  . GLY   A 1 182 ? 18.519  15.953  12.018 1.00 18.34 ? 182 GLY   A CA  1 
ATOM   1452 C C   . GLY   A 1 182 ? 19.539  15.433  11.028 1.00 17.09 ? 182 GLY   A C   1 
ATOM   1453 O O   . GLY   A 1 182 ? 20.019  16.157  10.146 1.00 26.04 ? 182 GLY   A O   1 
ATOM   1454 N N   . GLU   A 1 183 ? 19.862  14.146  11.160 1.00 23.11 ? 183 GLU   A N   1 
ATOM   1455 C CA  . GLU   A 1 183 ? 20.864  13.489  10.318 1.00 19.56 ? 183 GLU   A CA  1 
ATOM   1456 C C   . GLU   A 1 183 ? 20.152  12.853  9.129  1.00 22.30 ? 183 GLU   A C   1 
ATOM   1457 O O   . GLU   A 1 183 ? 19.814  11.666  9.116  1.00 16.27 ? 183 GLU   A O   1 
ATOM   1458 C CB  . GLU   A 1 183 ? 21.671  12.480  11.122 1.00 21.46 ? 183 GLU   A CB  1 
ATOM   1459 C CG  . GLU   A 1 183 ? 22.389  13.112  12.294 1.00 33.65 ? 183 GLU   A CG  1 
ATOM   1460 C CD  . GLU   A 1 183 ? 23.294  12.149  13.045 1.00 45.19 ? 183 GLU   A CD  1 
ATOM   1461 O OE1 . GLU   A 1 183 ? 24.329  12.607  13.575 1.00 48.21 ? 183 GLU   A OE1 1 
ATOM   1462 O OE2 . GLU   A 1 183 ? 22.974  10.938  13.105 1.00 44.62 ? 183 GLU   A OE2 1 
ATOM   1463 N N   . ASN   A 1 184 ? 19.872  13.703  8.139  1.00 19.87 ? 184 ASN   A N   1 
ATOM   1464 C CA  . ASN   A 1 184 ? 19.124  13.336  6.938  1.00 21.01 ? 184 ASN   A CA  1 
ATOM   1465 C C   . ASN   A 1 184 ? 17.784  12.714  7.297  1.00 30.66 ? 184 ASN   A C   1 
ATOM   1466 O O   . ASN   A 1 184 ? 17.303  11.790  6.635  1.00 26.59 ? 184 ASN   A O   1 
ATOM   1467 C CB  . ASN   A 1 184 ? 19.924  12.383  6.056  1.00 21.50 ? 184 ASN   A CB  1 
ATOM   1468 C CG  . ASN   A 1 184 ? 21.149  13.024  5.470  1.00 34.69 ? 184 ASN   A CG  1 
ATOM   1469 O OD1 . ASN   A 1 184 ? 21.271  14.247  5.420  1.00 31.41 ? 184 ASN   A OD1 1 
ATOM   1470 N ND2 . ASN   A 1 184 ? 22.074  12.194  5.012  1.00 36.50 ? 184 ASN   A ND2 1 
ATOM   1471 N N   . GLY   A 1 185 ? 17.182  13.217  8.364  1.00 21.71 ? 185 GLY   A N   1 
ATOM   1472 C CA  . GLY   A 1 185 ? 15.879  12.774  8.779  1.00 25.06 ? 185 GLY   A CA  1 
ATOM   1473 C C   . GLY   A 1 185 ? 15.911  11.823  9.948  1.00 18.54 ? 185 GLY   A C   1 
ATOM   1474 O O   . GLY   A 1 185 ? 14.844  11.458  10.456 1.00 21.51 ? 185 GLY   A O   1 
ATOM   1475 N N   . TYR   A 1 186 ? 17.102  11.423  10.385 1.00 18.26 ? 186 TYR   A N   1 
ATOM   1476 C CA  . TYR   A 1 186 ? 17.286  10.480  11.476 1.00 17.32 ? 186 TYR   A CA  1 
ATOM   1477 C C   . TYR   A 1 186 ? 17.830  11.217  12.693 1.00 13.18 ? 186 TYR   A C   1 
ATOM   1478 O O   . TYR   A 1 186 ? 18.364  12.325  12.598 1.00 20.92 ? 186 TYR   A O   1 
ATOM   1479 C CB  . TYR   A 1 186 ? 18.222  9.334   11.061 1.00 20.05 ? 186 TYR   A CB  1 
ATOM   1480 C CG  . TYR   A 1 186 ? 17.582  8.425   10.032 1.00 30.31 ? 186 TYR   A CG  1 
ATOM   1481 C CD1 . TYR   A 1 186 ? 17.582  8.772   8.676  1.00 24.81 ? 186 TYR   A CD1 1 
ATOM   1482 C CD2 . TYR   A 1 186 ? 16.939  7.246   10.410 1.00 22.29 ? 186 TYR   A CD2 1 
ATOM   1483 C CE1 . TYR   A 1 186 ? 16.990  7.955   7.726  1.00 17.15 ? 186 TYR   A CE1 1 
ATOM   1484 C CE2 . TYR   A 1 186 ? 16.336  6.430   9.466  1.00 24.93 ? 186 TYR   A CE2 1 
ATOM   1485 C CZ  . TYR   A 1 186 ? 16.356  6.792   8.130  1.00 21.36 ? 186 TYR   A CZ  1 
ATOM   1486 O OH  . TYR   A 1 186 ? 15.760  5.982   7.192  1.00 25.27 ? 186 TYR   A OH  1 
ATOM   1487 N N   . ILE   A 1 187 ? 17.671  10.598  13.846 1.00 13.91 ? 187 ILE   A N   1 
ATOM   1488 C CA  . ILE   A 1 187 ? 18.319  11.074  15.056 1.00 15.15 ? 187 ILE   A CA  1 
ATOM   1489 C C   . ILE   A 1 187 ? 18.917  9.885   15.787 1.00 23.11 ? 187 ILE   A C   1 
ATOM   1490 O O   . ILE   A 1 187 ? 18.334  8.799   15.832 1.00 17.66 ? 187 ILE   A O   1 
ATOM   1491 C CB  . ILE   A 1 187 ? 17.347  11.886  15.942 1.00 27.17 ? 187 ILE   A CB  1 
ATOM   1492 C CG1 . ILE   A 1 187 ? 18.035  12.376  17.219 1.00 23.41 ? 187 ILE   A CG1 1 
ATOM   1493 C CG2 . ILE   A 1 187 ? 16.096  11.091  16.254 1.00 17.61 ? 187 ILE   A CG2 1 
ATOM   1494 C CD1 . ILE   A 1 187 ? 17.251  13.456  17.959 1.00 14.90 ? 187 ILE   A CD1 1 
ATOM   1495 N N   . ARG   A 1 188 ? 20.100  10.077  16.327 1.00 24.01 ? 188 ARG   A N   1 
ATOM   1496 C CA  . ARG   A 1 188 ? 20.684  9.098   17.220 1.00 18.79 ? 188 ARG   A CA  1 
ATOM   1497 C C   . ARG   A 1 188 ? 20.467  9.598   18.634 1.00 16.34 ? 188 ARG   A C   1 
ATOM   1498 O O   . ARG   A 1 188 ? 20.932  10.686  18.996 1.00 21.04 ? 188 ARG   A O   1 
ATOM   1499 C CB  . ARG   A 1 188 ? 22.162  8.870   16.912 1.00 14.75 ? 188 ARG   A CB  1 
ATOM   1500 C CG  . ARG   A 1 188 ? 22.361  8.107   15.615 1.00 21.13 ? 188 ARG   A CG  1 
ATOM   1501 C CD  . ARG   A 1 188 ? 23.816  7.971   15.278 1.00 20.99 ? 188 ARG   A CD  1 
ATOM   1502 N NE  . ARG   A 1 188 ? 24.434  9.251   14.969 1.00 19.25 ? 188 ARG   A NE  1 
ATOM   1503 C CZ  . ARG   A 1 188 ? 25.663  9.583   15.327 1.00 23.38 ? 188 ARG   A CZ  1 
ATOM   1504 N NH1 . ARG   A 1 188 ? 26.450  8.727   15.961 1.00 32.11 ? 188 ARG   A NH1 1 
ATOM   1505 N NH2 . ARG   A 1 188 ? 26.129  10.787  15.004 1.00 18.79 ? 188 ARG   A NH2 1 
ATOM   1506 N N   . ILE   A 1 189 ? 19.766  8.805   19.432 1.00 17.65 ? 189 ILE   A N   1 
ATOM   1507 C CA  . ILE   A 1 189 ? 19.381  9.210   20.769 1.00 23.16 ? 189 ILE   A CA  1 
ATOM   1508 C C   . ILE   A 1 189 ? 20.264  8.410   21.709 1.00 29.77 ? 189 ILE   A C   1 
ATOM   1509 O O   . ILE   A 1 189 ? 20.355  7.184   21.582 1.00 31.80 ? 189 ILE   A O   1 
ATOM   1510 C CB  . ILE   A 1 189 ? 17.896  8.865   21.008 1.00 24.58 ? 189 ILE   A CB  1 
ATOM   1511 C CG1 . ILE   A 1 189 ? 16.971  9.580   20.005 1.00 19.53 ? 189 ILE   A CG1 1 
ATOM   1512 C CG2 . ILE   A 1 189 ? 17.492  9.159   22.434 1.00 17.28 ? 189 ILE   A CG2 1 
ATOM   1513 C CD1 . ILE   A 1 189 ? 16.367  10.876  20.494 1.00 25.36 ? 189 ILE   A CD1 1 
ATOM   1514 N N   . LYS   A 1 190 ? 20.929  9.096   22.635 1.00 21.61 ? 190 LYS   A N   1 
ATOM   1515 C CA  . LYS   A 1 190 ? 21.827  8.402   23.550 1.00 29.11 ? 190 LYS   A CA  1 
ATOM   1516 C C   . LYS   A 1 190 ? 21.066  7.302   24.279 1.00 25.43 ? 190 LYS   A C   1 
ATOM   1517 O O   . LYS   A 1 190 ? 19.913  7.486   24.681 1.00 30.47 ? 190 LYS   A O   1 
ATOM   1518 C CB  . LYS   A 1 190 ? 22.506  9.365   24.526 1.00 38.71 ? 190 LYS   A CB  1 
ATOM   1519 C CG  . LYS   A 1 190 ? 23.446  8.661   25.513 1.00 35.48 ? 190 LYS   A CG  1 
ATOM   1520 C CD  . LYS   A 1 190 ? 24.017  9.607   26.554 1.00 47.01 ? 190 LYS   A CD  1 
ATOM   1521 C CE  . LYS   A 1 190 ? 25.509  9.401   26.719 1.00 40.86 ? 190 LYS   A CE  1 
ATOM   1522 N NZ  . LYS   A 1 190 ? 26.243  10.004  25.580 1.00 50.93 ? 190 LYS   A NZ  1 
ATOM   1523 N N   . ARG   A 1 191 ? 21.715  6.160   24.463 1.00 26.32 ? 191 ARG   A N   1 
ATOM   1524 C CA  . ARG   A 1 191 ? 21.174  5.106   25.302 1.00 32.60 ? 191 ARG   A CA  1 
ATOM   1525 C C   . ARG   A 1 191 ? 22.238  4.751   26.318 1.00 20.66 ? 191 ARG   A C   1 
ATOM   1526 O O   . ARG   A 1 191 ? 23.358  5.256   26.268 1.00 30.49 ? 191 ARG   A O   1 
ATOM   1527 C CB  . ARG   A 1 191 ? 20.791  3.857   24.499 1.00 30.86 ? 191 ARG   A CB  1 
ATOM   1528 C CG  . ARG   A 1 191 ? 21.988  3.014   24.045 1.00 30.65 ? 191 ARG   A CG  1 
ATOM   1529 C CD  . ARG   A 1 191 ? 21.506  1.762   23.340 1.00 26.47 ? 191 ARG   A CD  1 
ATOM   1530 N NE  . ARG   A 1 191 ? 22.596  0.851   23.016 1.00 32.50 ? 191 ARG   A NE  1 
ATOM   1531 C CZ  . ARG   A 1 191 ? 23.098  -0.039  23.860 1.00 28.64 ? 191 ARG   A CZ  1 
ATOM   1532 N NH1 . ARG   A 1 191 ? 22.681  -0.115  25.111 1.00 23.34 ? 191 ARG   A NH1 1 
ATOM   1533 N NH2 . ARG   A 1 191 ? 24.058  -0.860  23.442 1.00 24.19 ? 191 ARG   A NH2 1 
ATOM   1534 N N   . GLY   A 1 192 ? 21.883  3.896   27.263 1.00 27.02 ? 192 GLY   A N   1 
ATOM   1535 C CA  . GLY   A 1 192 ? 22.862  3.467   28.232 1.00 21.54 ? 192 GLY   A CA  1 
ATOM   1536 C C   . GLY   A 1 192 ? 23.064  4.445   29.363 1.00 32.83 ? 192 GLY   A C   1 
ATOM   1537 O O   . GLY   A 1 192 ? 24.092  4.381   30.047 1.00 34.05 ? 192 GLY   A O   1 
ATOM   1538 N N   . THR   A 1 193 ? 22.116  5.362   29.572 1.00 29.90 ? 193 THR   A N   1 
ATOM   1539 C CA  . THR   A 1 193 ? 22.217  6.368   30.620 1.00 31.34 ? 193 THR   A CA  1 
ATOM   1540 C C   . THR   A 1 193 ? 21.745  5.853   31.970 1.00 37.15 ? 193 THR   A C   1 
ATOM   1541 O O   . THR   A 1 193 ? 21.944  6.538   32.981 1.00 43.95 ? 193 THR   A O   1 
ATOM   1542 C CB  . THR   A 1 193 ? 21.405  7.624   30.246 1.00 31.76 ? 193 THR   A CB  1 
ATOM   1543 O OG1 . THR   A 1 193 ? 19.998  7.354   30.359 1.00 33.61 ? 193 THR   A OG1 1 
ATOM   1544 C CG2 . THR   A 1 193 ? 21.717  8.088   28.845 1.00 16.55 ? 193 THR   A CG2 1 
ATOM   1545 N N   . GLY   A 1 194 ? 21.107  4.685   32.012 1.00 33.88 ? 194 GLY   A N   1 
ATOM   1546 C CA  . GLY   A 1 194 ? 20.624  4.165   33.268 1.00 30.94 ? 194 GLY   A CA  1 
ATOM   1547 C C   . GLY   A 1 194 ? 19.306  4.753   33.683 1.00 36.55 ? 194 GLY   A C   1 
ATOM   1548 O O   . GLY   A 1 194 ? 18.783  4.393   34.748 1.00 33.84 ? 194 GLY   A O   1 
ATOM   1549 N N   . ASN   A 1 195 ? 18.753  5.647   32.871 1.00 43.66 ? 195 ASN   A N   1 
ATOM   1550 C CA  . ASN   A 1 195 ? 17.441  6.223   33.117 1.00 44.54 ? 195 ASN   A CA  1 
ATOM   1551 C C   . ASN   A 1 195 ? 16.402  5.258   32.556 1.00 47.05 ? 195 ASN   A C   1 
ATOM   1552 O O   . ASN   A 1 195 ? 16.337  5.036   31.342 1.00 44.44 ? 195 ASN   A O   1 
ATOM   1553 C CB  . ASN   A 1 195 ? 17.366  7.598   32.463 1.00 39.32 ? 195 ASN   A CB  1 
ATOM   1554 C CG  . ASN   A 1 195 ? 15.961  8.123   32.356 1.00 36.03 ? 195 ASN   A CG  1 
ATOM   1555 O OD1 . ASN   A 1 195 ? 15.074  7.747   33.128 1.00 39.86 ? 195 ASN   A OD1 1 
ATOM   1556 N ND2 . ASN   A 1 195 ? 15.738  8.988   31.375 1.00 38.25 ? 195 ASN   A ND2 1 
ATOM   1557 N N   . SER   A 1 196 ? 15.605  4.665   33.446 1.00 46.59 ? 196 SER   A N   1 
ATOM   1558 C CA  . SER   A 1 196 ? 14.659  3.634   33.030 1.00 43.45 ? 196 SER   A CA  1 
ATOM   1559 C C   . SER   A 1 196 ? 13.687  4.142   31.971 1.00 42.44 ? 196 SER   A C   1 
ATOM   1560 O O   . SER   A 1 196 ? 13.183  3.358   31.158 1.00 40.34 ? 196 SER   A O   1 
ATOM   1561 C CB  . SER   A 1 196 ? 13.887  3.126   34.245 1.00 47.71 ? 196 SER   A CB  1 
ATOM   1562 O OG  . SER   A 1 196 ? 13.060  2.033   33.887 1.00 52.90 ? 196 SER   A OG  1 
ATOM   1563 N N   . TYR   A 1 197 ? 13.400  5.440   31.977 1.00 36.23 ? 197 TYR   A N   1 
ATOM   1564 C CA  . TYR   A 1 197 ? 12.459  6.009   31.023 1.00 35.32 ? 197 TYR   A CA  1 
ATOM   1565 C C   . TYR   A 1 197 ? 13.053  6.075   29.621 1.00 36.87 ? 197 TYR   A C   1 
ATOM   1566 O O   . TYR   A 1 197 ? 12.299  6.112   28.643 1.00 29.99 ? 197 TYR   A O   1 
ATOM   1567 C CB  . TYR   A 1 197 ? 12.024  7.402   31.501 1.00 43.89 ? 197 TYR   A CB  1 
ATOM   1568 C CG  . TYR   A 1 197 ? 11.104  7.394   32.711 1.00 46.92 ? 197 TYR   A CG  1 
ATOM   1569 C CD1 . TYR   A 1 197 ? 10.696  6.197   33.304 1.00 57.75 ? 197 TYR   A CD1 1 
ATOM   1570 C CD2 . TYR   A 1 197 ? 10.717  8.583   33.320 1.00 73.11 ? 197 TYR   A CD2 1 
ATOM   1571 C CE1 . TYR   A 1 197 ? 9.879   6.187   34.437 1.00 71.28 ? 197 TYR   A CE1 1 
ATOM   1572 C CE2 . TYR   A 1 197 ? 9.896   8.585   34.454 1.00 74.93 ? 197 TYR   A CE2 1 
ATOM   1573 C CZ  . TYR   A 1 197 ? 9.484   7.385   35.005 1.00 84.69 ? 197 TYR   A CZ  1 
ATOM   1574 O OH  . TYR   A 1 197 ? 8.676   7.386   36.120 1.00 76.04 ? 197 TYR   A OH  1 
ATOM   1575 N N   . GLY   A 1 198 ? 14.383  6.095   29.504 1.00 40.35 ? 198 GLY   A N   1 
ATOM   1576 C CA  . GLY   A 1 198 ? 15.048  6.435   28.258 1.00 26.94 ? 198 GLY   A CA  1 
ATOM   1577 C C   . GLY   A 1 198 ? 15.212  7.919   28.027 1.00 31.06 ? 198 GLY   A C   1 
ATOM   1578 O O   . GLY   A 1 198 ? 14.442  8.723   28.562 1.00 38.44 ? 198 GLY   A O   1 
ATOM   1579 N N   . VAL   A 1 199 ? 16.223  8.306   27.250 1.00 22.24 ? 199 VAL   A N   1 
ATOM   1580 C CA  . VAL   A 1 199 ? 16.322  9.702   26.850 1.00 32.92 ? 199 VAL   A CA  1 
ATOM   1581 C C   . VAL   A 1 199 ? 15.044  10.097  26.111 1.00 30.99 ? 199 VAL   A C   1 
ATOM   1582 O O   . VAL   A 1 199 ? 14.619  9.416   25.169 1.00 30.59 ? 199 VAL   A O   1 
ATOM   1583 C CB  . VAL   A 1 199 ? 17.597  9.907   26.017 1.00 32.73 ? 199 VAL   A CB  1 
ATOM   1584 C CG1 . VAL   A 1 199 ? 17.670  11.313  25.448 1.00 32.40 ? 199 VAL   A CG1 1 
ATOM   1585 C CG2 . VAL   A 1 199 ? 18.819  9.593   26.862 1.00 25.80 ? 199 VAL   A CG2 1 
ATOM   1586 N N   . CYS   A 1 200 ? 14.446  11.229  26.520 1.00 32.04 ? 200 CYS   A N   1 
ATOM   1587 C CA  . CYS   A 1 200 ? 13.152  11.704  25.998 1.00 34.19 ? 200 CYS   A CA  1 
ATOM   1588 C C   . CYS   A 1 200 ? 12.036  10.673  26.175 1.00 28.80 ? 200 CYS   A C   1 
ATOM   1589 O O   . CYS   A 1 200 ? 11.111  10.608  25.361 1.00 35.37 ? 200 CYS   A O   1 
ATOM   1590 C CB  . CYS   A 1 200 ? 13.210  12.162  24.528 1.00 29.62 ? 200 CYS   A CB  1 
ATOM   1591 S SG  . CYS   A 1 200 ? 14.511  13.364  24.086 1.00 26.32 ? 200 CYS   A SG  1 
ATOM   1592 N N   . GLY   A 1 201 ? 12.106  9.833   27.207 1.00 29.96 ? 201 GLY   A N   1 
ATOM   1593 C CA  . GLY   A 1 201 ? 11.036  8.871   27.387 1.00 28.50 ? 201 GLY   A CA  1 
ATOM   1594 C C   . GLY   A 1 201 ? 11.012  7.783   26.346 1.00 27.48 ? 201 GLY   A C   1 
ATOM   1595 O O   . GLY   A 1 201 ? 9.959   7.176   26.128 1.00 21.13 ? 201 GLY   A O   1 
ATOM   1596 N N   . LEU   A 1 202 ? 12.153  7.513   25.695 1.00 27.84 ? 202 LEU   A N   1 
ATOM   1597 C CA  . LEU   A 1 202 ? 12.202  6.613   24.542 1.00 20.46 ? 202 LEU   A CA  1 
ATOM   1598 C C   . LEU   A 1 202 ? 11.695  5.202   24.808 1.00 25.09 ? 202 LEU   A C   1 
ATOM   1599 O O   . LEU   A 1 202 ? 11.299  4.521   23.859 1.00 29.55 ? 202 LEU   A O   1 
ATOM   1600 C CB  . LEU   A 1 202 ? 13.643  6.554   24.019 1.00 29.33 ? 202 LEU   A CB  1 
ATOM   1601 C CG  . LEU   A 1 202 ? 13.837  5.819   22.691 1.00 27.51 ? 202 LEU   A CG  1 
ATOM   1602 C CD1 . LEU   A 1 202 ? 13.061  6.467   21.542 1.00 29.46 ? 202 LEU   A CD1 1 
ATOM   1603 C CD2 . LEU   A 1 202 ? 15.312  5.727   22.361 1.00 32.19 ? 202 LEU   A CD2 1 
ATOM   1604 N N   . TYR   A 1 203 ? 11.655  4.747   26.056 1.00 21.04 ? 203 TYR   A N   1 
ATOM   1605 C CA  . TYR   A 1 203 ? 11.221  3.391   26.359 1.00 24.29 ? 203 TYR   A CA  1 
ATOM   1606 C C   . TYR   A 1 203 ? 9.790   3.334   26.866 1.00 16.86 ? 203 TYR   A C   1 
ATOM   1607 O O   . TYR   A 1 203 ? 9.396   2.326   27.456 1.00 30.19 ? 203 TYR   A O   1 
ATOM   1608 C CB  . TYR   A 1 203 ? 12.159  2.680   27.327 1.00 23.10 ? 203 TYR   A CB  1 
ATOM   1609 C CG  . TYR   A 1 203 ? 13.600  2.732   26.908 1.00 41.92 ? 203 TYR   A CG  1 
ATOM   1610 C CD1 . TYR   A 1 203 ? 14.016  2.068   25.768 1.00 34.80 ? 203 TYR   A CD1 1 
ATOM   1611 C CD2 . TYR   A 1 203 ? 14.573  3.304   27.722 1.00 37.26 ? 203 TYR   A CD2 1 
ATOM   1612 C CE1 . TYR   A 1 203 ? 15.336  2.065   25.386 1.00 40.62 ? 203 TYR   A CE1 1 
ATOM   1613 C CE2 . TYR   A 1 203 ? 15.918  3.302   27.353 1.00 28.64 ? 203 TYR   A CE2 1 
ATOM   1614 C CZ  . TYR   A 1 203 ? 16.289  2.677   26.186 1.00 35.69 ? 203 TYR   A CZ  1 
ATOM   1615 O OH  . TYR   A 1 203 ? 17.609  2.678   25.797 1.00 39.60 ? 203 TYR   A OH  1 
ATOM   1616 N N   . THR   A 1 204 ? 9.013   4.400   26.670 1.00 20.05 ? 204 THR   A N   1 
ATOM   1617 C CA  . THR   A 1 204 ? 7.697   4.481   27.297 1.00 30.44 ? 204 THR   A CA  1 
ATOM   1618 C C   . THR   A 1 204 ? 6.699   3.500   26.690 1.00 32.55 ? 204 THR   A C   1 
ATOM   1619 O O   . THR   A 1 204 ? 5.957   2.834   27.420 1.00 34.15 ? 204 THR   A O   1 
ATOM   1620 C CB  . THR   A 1 204 ? 7.174   5.917   27.168 1.00 24.19 ? 204 THR   A CB  1 
ATOM   1621 O OG1 . THR   A 1 204 ? 8.048   6.817   27.854 1.00 21.97 ? 204 THR   A OG1 1 
ATOM   1622 C CG2 . THR   A 1 204 ? 5.757   6.058   27.688 1.00 20.69 ? 204 THR   A CG2 1 
ATOM   1623 N N   . SER   A 1 205 ? 6.679   3.371   25.365 1.00 17.81 ? 205 SER   A N   1 
ATOM   1624 C CA  . SER   A 1 205 ? 5.578   2.660   24.720 1.00 31.28 ? 205 SER   A CA  1 
ATOM   1625 C C   . SER   A 1 205 ? 6.049   2.232   23.328 1.00 19.95 ? 205 SER   A C   1 
ATOM   1626 O O   . SER   A 1 205 ? 6.085   3.052   22.406 1.00 19.94 ? 205 SER   A O   1 
ATOM   1627 C CB  . SER   A 1 205 ? 4.334   3.535   24.659 1.00 26.24 ? 205 SER   A CB  1 
ATOM   1628 O OG  . SER   A 1 205 ? 3.233   2.819   24.126 1.00 27.68 ? 205 SER   A OG  1 
ATOM   1629 N N   . SER   A 1 206 ? 6.400   0.962   23.181 1.00 10.13 ? 206 SER   A N   1 
ATOM   1630 C CA  . SER   A 1 206 ? 7.014   0.513   21.947 1.00 19.07 ? 206 SER   A CA  1 
ATOM   1631 C C   . SER   A 1 206 ? 6.291   -0.718  21.428 1.00 17.17 ? 206 SER   A C   1 
ATOM   1632 O O   . SER   A 1 206 ? 6.094   -1.685  22.167 1.00 24.18 ? 206 SER   A O   1 
ATOM   1633 C CB  . SER   A 1 206 ? 8.505   0.217   22.157 1.00 27.18 ? 206 SER   A CB  1 
ATOM   1634 O OG  . SER   A 1 206 ? 9.152   1.324   22.764 1.00 22.17 ? 206 SER   A OG  1 
ATOM   1635 N N   . PHE   A 1 207 ? 5.965   -0.705  20.136 1.00 20.78 ? 207 PHE   A N   1 
ATOM   1636 C CA  . PHE   A 1 207 ? 5.176   -1.752  19.511 1.00 20.27 ? 207 PHE   A CA  1 
ATOM   1637 C C   . PHE   A 1 207 ? 5.819   -2.103  18.187 1.00 19.20 ? 207 PHE   A C   1 
ATOM   1638 O O   . PHE   A 1 207 ? 6.505   -1.283  17.572 1.00 26.45 ? 207 PHE   A O   1 
ATOM   1639 C CB  . PHE   A 1 207 ? 3.716   -1.310  19.223 1.00 25.89 ? 207 PHE   A CB  1 
ATOM   1640 C CG  . PHE   A 1 207 ? 2.871   -1.101  20.454 1.00 22.40 ? 207 PHE   A CG  1 
ATOM   1641 C CD1 . PHE   A 1 207 ? 2.856   0.120   21.102 1.00 22.90 ? 207 PHE   A CD1 1 
ATOM   1642 C CD2 . PHE   A 1 207 ? 2.056   -2.110  20.931 1.00 32.00 ? 207 PHE   A CD2 1 
ATOM   1643 C CE1 . PHE   A 1 207 ? 2.081   0.311   22.238 1.00 32.42 ? 207 PHE   A CE1 1 
ATOM   1644 C CE2 . PHE   A 1 207 ? 1.272   -1.920  22.062 1.00 34.04 ? 207 PHE   A CE2 1 
ATOM   1645 C CZ  . PHE   A 1 207 ? 1.286   -0.714  22.713 1.00 26.86 ? 207 PHE   A CZ  1 
ATOM   1646 N N   . TYR   A 1 208 ? 5.601   -3.340  17.765 1.00 23.40 ? 208 TYR   A N   1 
ATOM   1647 C CA  . TYR   A 1 208 ? 6.055   -3.784  16.460 1.00 26.46 ? 208 TYR   A CA  1 
ATOM   1648 C C   . TYR   A 1 208 ? 5.022   -4.771  15.946 1.00 30.41 ? 208 TYR   A C   1 
ATOM   1649 O O   . TYR   A 1 208 ? 4.377   -5.465  16.744 1.00 30.11 ? 208 TYR   A O   1 
ATOM   1650 C CB  . TYR   A 1 208 ? 7.455   -4.427  16.509 1.00 24.29 ? 208 TYR   A CB  1 
ATOM   1651 C CG  . TYR   A 1 208 ? 7.575   -5.557  17.506 1.00 26.65 ? 208 TYR   A CG  1 
ATOM   1652 C CD1 . TYR   A 1 208 ? 7.453   -6.882  17.102 1.00 28.57 ? 208 TYR   A CD1 1 
ATOM   1653 C CD2 . TYR   A 1 208 ? 7.824   -5.303  18.851 1.00 33.98 ? 208 TYR   A CD2 1 
ATOM   1654 C CE1 . TYR   A 1 208 ? 7.552   -7.926  18.017 1.00 26.54 ? 208 TYR   A CE1 1 
ATOM   1655 C CE2 . TYR   A 1 208 ? 7.930   -6.340  19.780 1.00 29.99 ? 208 TYR   A CE2 1 
ATOM   1656 C CZ  . TYR   A 1 208 ? 7.795   -7.648  19.354 1.00 36.74 ? 208 TYR   A CZ  1 
ATOM   1657 O OH  . TYR   A 1 208 ? 7.913   -8.673  20.270 1.00 45.77 ? 208 TYR   A OH  1 
ATOM   1658 N N   . PRO   A 1 209 ? 4.855   -4.878  14.634 1.00 28.39 ? 209 PRO   A N   1 
ATOM   1659 C CA  . PRO   A 1 209 ? 3.934   -5.874  14.091 1.00 32.19 ? 209 PRO   A CA  1 
ATOM   1660 C C   . PRO   A 1 209 ? 4.565   -7.253  14.060 1.00 28.78 ? 209 PRO   A C   1 
ATOM   1661 O O   . PRO   A 1 209 ? 5.784   -7.416  13.949 1.00 28.67 ? 209 PRO   A O   1 
ATOM   1662 C CB  . PRO   A 1 209 ? 3.668   -5.357  12.669 1.00 38.83 ? 209 PRO   A CB  1 
ATOM   1663 C CG  . PRO   A 1 209 ? 4.986   -4.742  12.285 1.00 30.41 ? 209 PRO   A CG  1 
ATOM   1664 C CD  . PRO   A 1 209 ? 5.415   -4.029  13.563 1.00 23.45 ? 209 PRO   A CD  1 
ATOM   1665 N N   . VAL   A 1 210 ? 3.713   -8.258  14.145 1.00 30.53 ? 210 VAL   A N   1 
ATOM   1666 C CA  . VAL   A 1 210 ? 4.139   -9.639  14.023 1.00 34.83 ? 210 VAL   A CA  1 
ATOM   1667 C C   . VAL   A 1 210 ? 3.574   -10.158 12.716 1.00 44.10 ? 210 VAL   A C   1 
ATOM   1668 O O   . VAL   A 1 210 ? 2.381   -9.973  12.427 1.00 45.58 ? 210 VAL   A O   1 
ATOM   1669 C CB  . VAL   A 1 210 ? 3.666   -10.497 15.207 1.00 36.52 ? 210 VAL   A CB  1 
ATOM   1670 C CG1 . VAL   A 1 210 ? 3.854   -11.994 14.900 1.00 43.28 ? 210 VAL   A CG1 1 
ATOM   1671 C CG2 . VAL   A 1 210 ? 4.416   -10.100 16.455 1.00 41.89 ? 210 VAL   A CG2 1 
ATOM   1672 N N   . LYS   A 1 211 ? 4.420   -10.845 11.956 1.00 38.15 ? 211 LYS   A N   1 
ATOM   1673 C CA  . LYS   A 1 211 ? 4.051   -11.381 10.659 1.00 49.86 ? 211 LYS   A CA  1 
ATOM   1674 C C   . LYS   A 1 211 ? 4.746   -12.723 10.526 1.00 56.68 ? 211 LYS   A C   1 
ATOM   1675 O O   . LYS   A 1 211 ? 5.976   -12.793 10.509 1.00 47.15 ? 211 LYS   A O   1 
ATOM   1676 C CB  . LYS   A 1 211 ? 4.481   -10.425 9.552  1.00 50.88 ? 211 LYS   A CB  1 
ATOM   1677 C CG  . LYS   A 1 211 ? 4.362   -10.980 8.154  1.00 43.49 ? 211 LYS   A CG  1 
ATOM   1678 C CD  . LYS   A 1 211 ? 3.070   -10.485 7.569  1.00 46.42 ? 211 LYS   A CD  1 
ATOM   1679 C CE  . LYS   A 1 211 ? 3.254   -9.993  6.164  1.00 46.71 ? 211 LYS   A CE  1 
ATOM   1680 N NZ  . LYS   A 1 211 ? 3.700   -11.041 5.209  1.00 66.54 ? 211 LYS   A NZ  1 
ATOM   1681 N N   . ASN   A 1 212 ? 3.955   -13.779 10.435 1.00 60.18 ? 212 ASN   A N   1 
ATOM   1682 C CA  . ASN   A 1 212 ? 4.464   -15.136 10.301 1.00 53.43 ? 212 ASN   A CA  1 
ATOM   1683 C C   . ASN   A 1 212 ? 4.934   -15.490 8.892  1.00 74.42 ? 212 ASN   A C   1 
ATOM   1684 O O   . ASN   A 1 212 ? 5.824   -16.329 8.727  1.00 70.96 ? 212 ASN   A O   1 
ATOM   1685 C CB  . ASN   A 1 212 ? 3.391   -16.105 10.770 1.00 50.39 ? 212 ASN   A CB  1 
ATOM   1686 C CG  . ASN   A 1 212 ? 2.914   -15.789 12.182 1.00 74.10 ? 212 ASN   A CG  1 
ATOM   1687 O OD1 . ASN   A 1 212 ? 3.703   -15.356 13.032 1.00 44.27 ? 212 ASN   A OD1 1 
ATOM   1688 N ND2 . ASN   A 1 212 ? 1.616   -15.980 12.431 1.00 52.14 ? 212 ASN   A ND2 1 
ATOM   1689 O OXT . ASN   A 1 212 ? 4.449   -14.953 7.894  1.00 73.73 ? 212 ASN   A OXT 1 
HETATM 1690 N N1  . A1AXI B 2 .   ? 0.782   11.765  19.555 0.75 43.51 ? 301 A1AXI A N1  1 
HETATM 1691 N N3  . A1AXI B 2 .   ? -8.597  15.935  23.883 0.75 43.51 ? 301 A1AXI A N3  1 
HETATM 1692 C C4  . A1AXI B 2 .   ? 0.340   11.854  18.288 0.75 43.51 ? 301 A1AXI A C4  1 
HETATM 1693 C C5  . A1AXI B 2 .   ? 0.159   10.717  20.362 0.75 43.51 ? 301 A1AXI A C5  1 
HETATM 1694 C C6  . A1AXI B 2 .   ? 0.986   9.785   21.238 0.75 43.51 ? 301 A1AXI A C6  1 
HETATM 1695 C C7  . A1AXI B 2 .   ? 1.839   8.765   20.476 0.75 43.51 ? 301 A1AXI A C7  1 
HETATM 1696 C C8  . A1AXI B 2 .   ? 2.978   9.782   20.563 0.75 43.51 ? 301 A1AXI A C8  1 
HETATM 1697 C C10 . A1AXI B 2 .   ? -1.072  11.192  21.135 0.75 43.51 ? 301 A1AXI A C10 1 
HETATM 1698 C C13 . A1AXI B 2 .   ? -5.674  11.969  21.308 0.75 43.51 ? 301 A1AXI A C13 1 
HETATM 1699 C C15 . A1AXI B 2 .   ? -7.259  13.673  20.089 0.75 43.51 ? 301 A1AXI A C15 1 
HETATM 1700 C C17 . A1AXI B 2 .   ? -8.876  15.180  21.472 0.75 43.51 ? 301 A1AXI A C17 1 
HETATM 1701 C C1  . A1AXI B 2 .   ? 2.733   13.911  15.995 0.75 43.51 ? 301 A1AXI A C1  1 
HETATM 1702 C C11 . A1AXI B 2 .   ? -3.502  10.683  21.489 0.75 43.51 ? 301 A1AXI A C11 1 
HETATM 1703 C C12 . A1AXI B 2 .   ? -4.224  11.861  20.848 0.75 43.51 ? 301 A1AXI A C12 1 
HETATM 1704 C C14 . A1AXI B 2 .   ? -6.254  13.374  21.197 0.75 43.51 ? 301 A1AXI A C14 1 
HETATM 1705 C C16 . A1AXI B 2 .   ? -8.689  14.011  20.505 0.75 43.51 ? 301 A1AXI A C16 1 
HETATM 1706 C C18 . A1AXI B 2 .   ? -8.667  14.813  22.931 0.75 43.51 ? 301 A1AXI A C18 1 
HETATM 1707 C C2  . A1AXI B 2 .   ? 2.279   12.913  17.047 0.75 43.51 ? 301 A1AXI A C2  1 
HETATM 1708 C C3  . A1AXI B 2 .   ? 0.801   13.034  17.429 0.75 43.51 ? 301 A1AXI A C3  1 
HETATM 1709 C C9  . A1AXI B 2 .   ? 2.295   10.308  21.831 0.75 43.51 ? 301 A1AXI A C9  1 
HETATM 1710 N N2  . A1AXI B 2 .   ? -2.174  10.460  20.935 0.75 43.51 ? 301 A1AXI A N2  1 
HETATM 1711 O O1  . A1AXI B 2 .   ? 2.209   13.858  14.860 0.75 43.51 ? 301 A1AXI A O1  1 
HETATM 1712 O O2  . A1AXI B 2 .   ? 3.621   14.743  16.294 0.75 43.51 ? 301 A1AXI A O2  1 
HETATM 1713 O O3  . A1AXI B 2 .   ? 0.524   14.273  18.063 0.75 43.51 ? 301 A1AXI A O3  1 
HETATM 1714 O O4  . A1AXI B 2 .   ? -0.427  11.032  17.804 0.75 43.51 ? 301 A1AXI A O4  1 
HETATM 1715 O O5  . A1AXI B 2 .   ? -1.016  12.153  21.912 0.75 43.51 ? 301 A1AXI A O5  1 
HETATM 1716 O O   . HOH   C 3 .   ? 15.869  14.887  0.612  1.00 16.17 ? 401 HOH   A O   1 
HETATM 1717 O O   . HOH   C 3 .   ? 8.802   4.013   23.041 1.00 15.98 ? 402 HOH   A O   1 
HETATM 1718 O O   . HOH   C 3 .   ? 12.726  13.683  10.146 1.00 15.06 ? 403 HOH   A O   1 
HETATM 1719 O O   . HOH   C 3 .   ? 11.386  15.496  3.155  1.00 15.69 ? 404 HOH   A O   1 
# 
