data_9NB2
# 
_entry.id   9NB2 
# 
_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   9NB2         pdb_00009nb2 10.2210/pdb9nb2/pdb 
WWPDB D_1000292958 ?            ?                   
# 
_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                        9NB2 
_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           Y 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB 'XRD structure of same protein complexed with a different ligand'     9NAT unspecified 
PDB 'MicroED structure of same protein in apo-form'                       9NAG unspecified 
PDB 'MicroED structure of same protein complexed with a different ligand' 9NAE unspecified 
PDB 'MicroED structure of same protein complexed with a different ligand' 9NAR unspecified 
PDB 'MicroED structure of same protein complexed with a different ligand' 9NAO unspecified 
PDB 'MicroED structure of same protein complexed with a different ligand' 9NAX unspecified 
PDB 'MicroED structure of same protein complexed with a different ligand' 9NAY unspecified 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.email              jrodriguez@mbi.ucla.edu 
_pdbx_contact_author.name_first         Jose 
_pdbx_contact_author.name_last          Rodriguez 
_pdbx_contact_author.name_mi            A 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-0248-4964 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Vlahakis, N.W.'  1 0000-0002-5092-0265 
'Rodriguez, J.A.' 2 0000-0002-0248-4964 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Biorxiv 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2692-8205 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
'Combining MicroED and native mass spectrometry for structural discovery of enzyme-biosynthetic inhibitor complexes.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1101/2025.02.20.638743 
_citation.pdbx_database_id_PubMed   40060639 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Vlahakis, N.W.'  1  0000-0002-5092-0265 
primary 'Flowers, C.W.'   2  ?                   
primary 'Liu, M.'         3  ?                   
primary 'Agdanowski, M.'  4  ?                   
primary 'Johnson, S.'     5  ?                   
primary 'Summers, J.A.'   6  ?                   
primary 'Keyser, C.'      7  ?                   
primary 'Russell, P.'     8  ?                   
primary 'Rose, S.'        9  ?                   
primary 'Orlans, J.'      10 ?                   
primary 'Adhami, N.'      11 ?                   
primary 'Chen, Y.'        12 ?                   
primary 'Sawaya, M.R.'    13 ?                   
primary 'Basu, S.'        14 ?                   
primary 'de Sanctis, D.'  15 ?                   
primary 'Wakatsuki, S.'   16 ?                   
primary 'Nelson, H.M.'    17 ?                   
primary 'Loo, J.A.'       18 ?                   
primary 'Tang, Y.'        19 ?                   
primary 'Rodriguez, J.A.' 20 0000-0002-0248-4964 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     nat Papain                                                              23452.301 1   3.4.22.2 ? ? ? 
2 non-polymer syn 'N-[N-[1-HYDROXYCARBOXYETHYL-CARBONYL]LEUCYLAMINO-BUTYL]-GUANIDINE' 360.429   1   ?        ? ? ? 
3 water       nat water                                                               18.015    223 ?        ? ? ? 
# 
_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 'N-[N-[1-HYDROXYCARBOXYETHYL-CARBONYL]LEUCYLAMINO-BUTYL]-GUANIDINE' E64 
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 
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 
E64 non-polymer         . 'N-[N-[1-HYDROXYCARBOXYETHYL-CARBONYL]LEUCYLAMINO-BUTYL]-GUANIDINE' ? 'C15 H30 N5 O5 1' 360.429 
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        E64 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   E64 
_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 E64 1   301 301 E64 E64 A . 
C 3 HOH 1   401 154 HOH HOH A . 
C 3 HOH 2   402 162 HOH HOH A . 
C 3 HOH 3   403 172 HOH HOH A . 
C 3 HOH 4   404 109 HOH HOH A . 
C 3 HOH 5   405 189 HOH HOH A . 
C 3 HOH 6   406 193 HOH HOH A . 
C 3 HOH 7   407 40  HOH HOH A . 
C 3 HOH 8   408 224 HOH HOH A . 
C 3 HOH 9   409 187 HOH HOH A . 
C 3 HOH 10  410 135 HOH HOH A . 
C 3 HOH 11  411 80  HOH HOH A . 
C 3 HOH 12  412 46  HOH HOH A . 
C 3 HOH 13  413 43  HOH HOH A . 
C 3 HOH 14  414 82  HOH HOH A . 
C 3 HOH 15  415 115 HOH HOH A . 
C 3 HOH 16  416 139 HOH HOH A . 
C 3 HOH 17  417 106 HOH HOH A . 
C 3 HOH 18  418 26  HOH HOH A . 
C 3 HOH 19  419 229 HOH HOH A . 
C 3 HOH 20  420 161 HOH HOH A . 
C 3 HOH 21  421 118 HOH HOH A . 
C 3 HOH 22  422 207 HOH HOH A . 
C 3 HOH 23  423 8   HOH HOH A . 
C 3 HOH 24  424 94  HOH HOH A . 
C 3 HOH 25  425 27  HOH HOH A . 
C 3 HOH 26  426 55  HOH HOH A . 
C 3 HOH 27  427 9   HOH HOH A . 
C 3 HOH 28  428 52  HOH HOH A . 
C 3 HOH 29  429 186 HOH HOH A . 
C 3 HOH 30  430 197 HOH HOH A . 
C 3 HOH 31  431 33  HOH HOH A . 
C 3 HOH 32  432 73  HOH HOH A . 
C 3 HOH 33  433 38  HOH HOH A . 
C 3 HOH 34  434 64  HOH HOH A . 
C 3 HOH 35  435 179 HOH HOH A . 
C 3 HOH 36  436 39  HOH HOH A . 
C 3 HOH 37  437 15  HOH HOH A . 
C 3 HOH 38  438 70  HOH HOH A . 
C 3 HOH 39  439 36  HOH HOH A . 
C 3 HOH 40  440 231 HOH HOH A . 
C 3 HOH 41  441 54  HOH HOH A . 
C 3 HOH 42  442 113 HOH HOH A . 
C 3 HOH 43  443 76  HOH HOH A . 
C 3 HOH 44  444 25  HOH HOH A . 
C 3 HOH 45  445 205 HOH HOH A . 
C 3 HOH 46  446 199 HOH HOH A . 
C 3 HOH 47  447 108 HOH HOH A . 
C 3 HOH 48  448 5   HOH HOH A . 
C 3 HOH 49  449 233 HOH HOH A . 
C 3 HOH 50  450 219 HOH HOH A . 
C 3 HOH 51  451 84  HOH HOH A . 
C 3 HOH 52  452 66  HOH HOH A . 
C 3 HOH 53  453 103 HOH HOH A . 
C 3 HOH 54  454 37  HOH HOH A . 
C 3 HOH 55  455 19  HOH HOH A . 
C 3 HOH 56  456 32  HOH HOH A . 
C 3 HOH 57  457 63  HOH HOH A . 
C 3 HOH 58  458 99  HOH HOH A . 
C 3 HOH 59  459 50  HOH HOH A . 
C 3 HOH 60  460 57  HOH HOH A . 
C 3 HOH 61  461 209 HOH HOH A . 
C 3 HOH 62  462 13  HOH HOH A . 
C 3 HOH 63  463 131 HOH HOH A . 
C 3 HOH 64  464 160 HOH HOH A . 
C 3 HOH 65  465 22  HOH HOH A . 
C 3 HOH 66  466 29  HOH HOH A . 
C 3 HOH 67  467 74  HOH HOH A . 
C 3 HOH 68  468 136 HOH HOH A . 
C 3 HOH 69  469 34  HOH HOH A . 
C 3 HOH 70  470 130 HOH HOH A . 
C 3 HOH 71  471 124 HOH HOH A . 
C 3 HOH 72  472 227 HOH HOH A . 
C 3 HOH 73  473 121 HOH HOH A . 
C 3 HOH 74  474 134 HOH HOH A . 
C 3 HOH 75  475 44  HOH HOH A . 
C 3 HOH 76  476 61  HOH HOH A . 
C 3 HOH 77  477 123 HOH HOH A . 
C 3 HOH 78  478 79  HOH HOH A . 
C 3 HOH 79  479 235 HOH HOH A . 
C 3 HOH 80  480 86  HOH HOH A . 
C 3 HOH 81  481 49  HOH HOH A . 
C 3 HOH 82  482 117 HOH HOH A . 
C 3 HOH 83  483 81  HOH HOH A . 
C 3 HOH 84  484 196 HOH HOH A . 
C 3 HOH 85  485 23  HOH HOH A . 
C 3 HOH 86  486 137 HOH HOH A . 
C 3 HOH 87  487 114 HOH HOH A . 
C 3 HOH 88  488 158 HOH HOH A . 
C 3 HOH 89  489 62  HOH HOH A . 
C 3 HOH 90  490 156 HOH HOH A . 
C 3 HOH 91  491 221 HOH HOH A . 
C 3 HOH 92  492 173 HOH HOH A . 
C 3 HOH 93  493 110 HOH HOH A . 
C 3 HOH 94  494 190 HOH HOH A . 
C 3 HOH 95  495 116 HOH HOH A . 
C 3 HOH 96  496 90  HOH HOH A . 
C 3 HOH 97  497 24  HOH HOH A . 
C 3 HOH 98  498 58  HOH HOH A . 
C 3 HOH 99  499 14  HOH HOH A . 
C 3 HOH 100 500 127 HOH HOH A . 
C 3 HOH 101 501 47  HOH HOH A . 
C 3 HOH 102 502 223 HOH HOH A . 
C 3 HOH 103 503 166 HOH HOH A . 
C 3 HOH 104 504 122 HOH HOH A . 
C 3 HOH 105 505 11  HOH HOH A . 
C 3 HOH 106 506 87  HOH HOH A . 
C 3 HOH 107 507 65  HOH HOH A . 
C 3 HOH 108 508 170 HOH HOH A . 
C 3 HOH 109 509 69  HOH HOH A . 
C 3 HOH 110 510 41  HOH HOH A . 
C 3 HOH 111 511 77  HOH HOH A . 
C 3 HOH 112 512 202 HOH HOH A . 
C 3 HOH 113 513 177 HOH HOH A . 
C 3 HOH 114 514 12  HOH HOH A . 
C 3 HOH 115 515 20  HOH HOH A . 
C 3 HOH 116 516 220 HOH HOH A . 
C 3 HOH 117 517 21  HOH HOH A . 
C 3 HOH 118 518 214 HOH HOH A . 
C 3 HOH 119 519 88  HOH HOH A . 
C 3 HOH 120 520 102 HOH HOH A . 
C 3 HOH 121 521 176 HOH HOH A . 
C 3 HOH 122 522 226 HOH HOH A . 
C 3 HOH 123 523 71  HOH HOH A . 
C 3 HOH 124 524 45  HOH HOH A . 
C 3 HOH 125 525 72  HOH HOH A . 
C 3 HOH 126 526 138 HOH HOH A . 
C 3 HOH 127 527 111 HOH HOH A . 
C 3 HOH 128 528 51  HOH HOH A . 
C 3 HOH 129 529 184 HOH HOH A . 
C 3 HOH 130 530 7   HOH HOH A . 
C 3 HOH 131 531 48  HOH HOH A . 
C 3 HOH 132 532 100 HOH HOH A . 
C 3 HOH 133 533 126 HOH HOH A . 
C 3 HOH 134 534 132 HOH HOH A . 
C 3 HOH 135 535 59  HOH HOH A . 
C 3 HOH 136 536 222 HOH HOH A . 
C 3 HOH 137 537 30  HOH HOH A . 
C 3 HOH 138 538 192 HOH HOH A . 
C 3 HOH 139 539 3   HOH HOH A . 
C 3 HOH 140 540 107 HOH HOH A . 
C 3 HOH 141 541 159 HOH HOH A . 
C 3 HOH 142 542 17  HOH HOH A . 
C 3 HOH 143 543 212 HOH HOH A . 
C 3 HOH 144 544 98  HOH HOH A . 
C 3 HOH 145 545 31  HOH HOH A . 
C 3 HOH 146 546 75  HOH HOH A . 
C 3 HOH 147 547 18  HOH HOH A . 
C 3 HOH 148 548 93  HOH HOH A . 
C 3 HOH 149 549 178 HOH HOH A . 
C 3 HOH 150 550 185 HOH HOH A . 
C 3 HOH 151 551 203 HOH HOH A . 
C 3 HOH 152 552 2   HOH HOH A . 
C 3 HOH 153 553 204 HOH HOH A . 
C 3 HOH 154 554 104 HOH HOH A . 
C 3 HOH 155 555 183 HOH HOH A . 
C 3 HOH 156 556 194 HOH HOH A . 
C 3 HOH 157 557 1   HOH HOH A . 
C 3 HOH 158 558 120 HOH HOH A . 
C 3 HOH 159 559 171 HOH HOH A . 
C 3 HOH 160 560 213 HOH HOH A . 
C 3 HOH 161 561 133 HOH HOH A . 
C 3 HOH 162 562 28  HOH HOH A . 
C 3 HOH 163 563 6   HOH HOH A . 
C 3 HOH 164 564 53  HOH HOH A . 
C 3 HOH 165 565 174 HOH HOH A . 
C 3 HOH 166 566 215 HOH HOH A . 
C 3 HOH 167 567 181 HOH HOH A . 
C 3 HOH 168 568 167 HOH HOH A . 
C 3 HOH 169 569 105 HOH HOH A . 
C 3 HOH 170 570 168 HOH HOH A . 
C 3 HOH 171 571 83  HOH HOH A . 
C 3 HOH 172 572 155 HOH HOH A . 
C 3 HOH 173 573 211 HOH HOH A . 
C 3 HOH 174 574 228 HOH HOH A . 
C 3 HOH 175 575 56  HOH HOH A . 
C 3 HOH 176 576 206 HOH HOH A . 
C 3 HOH 177 577 145 HOH HOH A . 
C 3 HOH 178 578 151 HOH HOH A . 
C 3 HOH 179 579 67  HOH HOH A . 
C 3 HOH 180 580 232 HOH HOH A . 
C 3 HOH 181 581 216 HOH HOH A . 
C 3 HOH 182 582 182 HOH HOH A . 
C 3 HOH 183 583 201 HOH HOH A . 
C 3 HOH 184 584 89  HOH HOH A . 
C 3 HOH 185 585 152 HOH HOH A . 
C 3 HOH 186 586 144 HOH HOH A . 
C 3 HOH 187 587 208 HOH HOH A . 
C 3 HOH 188 588 150 HOH HOH A . 
C 3 HOH 189 589 141 HOH HOH A . 
C 3 HOH 190 590 78  HOH HOH A . 
C 3 HOH 191 591 148 HOH HOH A . 
C 3 HOH 192 592 129 HOH HOH A . 
C 3 HOH 193 593 143 HOH HOH A . 
C 3 HOH 194 594 16  HOH HOH A . 
C 3 HOH 195 595 95  HOH HOH A . 
C 3 HOH 196 596 119 HOH HOH A . 
C 3 HOH 197 597 236 HOH HOH A . 
C 3 HOH 198 598 165 HOH HOH A . 
C 3 HOH 199 599 191 HOH HOH A . 
C 3 HOH 200 600 234 HOH HOH A . 
C 3 HOH 201 601 140 HOH HOH A . 
C 3 HOH 202 602 169 HOH HOH A . 
C 3 HOH 203 603 217 HOH HOH A . 
C 3 HOH 204 604 200 HOH HOH A . 
C 3 HOH 205 605 125 HOH HOH A . 
C 3 HOH 206 606 68  HOH HOH A . 
C 3 HOH 207 607 230 HOH HOH A . 
C 3 HOH 208 608 157 HOH HOH A . 
C 3 HOH 209 609 147 HOH HOH A . 
C 3 HOH 210 610 153 HOH HOH A . 
C 3 HOH 211 611 210 HOH HOH A . 
C 3 HOH 212 612 188 HOH HOH A . 
C 3 HOH 213 613 112 HOH HOH A . 
C 3 HOH 214 614 180 HOH HOH A . 
C 3 HOH 215 615 237 HOH HOH A . 
C 3 HOH 216 616 146 HOH HOH A . 
C 3 HOH 217 617 101 HOH HOH A . 
C 3 HOH 218 618 198 HOH HOH A . 
C 3 HOH 219 619 128 HOH HOH A . 
C 3 HOH 220 620 218 HOH HOH A . 
C 3 HOH 221 621 92  HOH HOH A . 
C 3 HOH 222 622 195 HOH HOH A . 
C 3 HOH 223 623 225 HOH HOH A . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? '(1.20.1_4487: ???)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XSCALE ? ? ? .                    2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9NB2 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     42.410 
_cell.length_a_esd                 ? 
_cell.length_b                     48.910 
_cell.length_b_esd                 ? 
_cell.length_c                     101.710 
_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                         9NB2 
_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                   9NB2 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.25 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          45.31 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '889 mM NaCl and 59% methanol in reservoir. 66% methanol in sitting drop.' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            298 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     'IMAGE PLATE' 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'RIGAKU RAXIS HTC' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-05-08 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.54 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      'ROTATING ANODE' 
_diffrn_source.target                      ? 
_diffrn_source.type                        'RIGAKU FR-E+' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.54 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ? 
_diffrn_source.pdbx_synchrotron_site       ? 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9NB2 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.5 
_reflns.d_resolution_low                               27.86 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     71570 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.4 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                12.1 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          18.22 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.078 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.5 
_reflns_shell.d_res_low                                     1.6 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           3.72 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             6000 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.850 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          100 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.71 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9NB2 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.50 
_refine.ls_d_res_low                             27.86 
_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                     34476 
_refine.ls_number_reflns_R_free                  1723 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.40 
_refine.ls_percent_reflns_R_free                 5.00 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1850 
_refine.ls_R_factor_R_free                       0.2124 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1835 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.36 
_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                 19.93 
_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                            0.18 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        1655 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         25 
_refine_hist.number_atoms_solvent             223 
_refine_hist.number_atoms_total               1903 
_refine_hist.d_res_high                       1.50 
_refine_hist.d_res_low                        27.86 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.006 ? 1802 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.838 ? 2458 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 7.013 ? 265  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.059 ? 243  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.007 ? 329  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.50 1.54  . . 142 2707 100.00 . . . . 0.2226 . . . . . . . . . . . 0.2476 
'X-RAY DIFFRACTION' 1.54 1.59  . . 142 2690 100.00 . . . . 0.2100 . . . . . . . . . . . 0.2394 
'X-RAY DIFFRACTION' 1.59 1.65  . . 142 2699 100.00 . . . . 0.1993 . . . . . . . . . . . 0.2971 
'X-RAY DIFFRACTION' 1.65 1.72  . . 142 2721 100.00 . . . . 0.1962 . . . . . . . . . . . 0.2586 
'X-RAY DIFFRACTION' 1.72 1.80  . . 143 2715 100.00 . . . . 0.1891 . . . . . . . . . . . 0.2073 
'X-RAY DIFFRACTION' 1.80 1.89  . . 143 2697 100.00 . . . . 0.1969 . . . . . . . . . . . 0.2566 
'X-RAY DIFFRACTION' 1.89 2.01  . . 138 2636 97.00  . . . . 0.2276 . . . . . . . . . . . 0.2694 
'X-RAY DIFFRACTION' 2.01 2.16  . . 145 2736 100.00 . . . . 0.1817 . . . . . . . . . . . 0.2131 
'X-RAY DIFFRACTION' 2.16 2.38  . . 140 2658 97.00  . . . . 0.2033 . . . . . . . . . . . 0.2313 
'X-RAY DIFFRACTION' 2.38 2.72  . . 145 2767 100.00 . . . . 0.1914 . . . . . . . . . . . 0.2109 
'X-RAY DIFFRACTION' 2.73 3.43  . . 147 2802 100.00 . . . . 0.1804 . . . . . . . . . . . 0.2171 
'X-RAY DIFFRACTION' 3.43 27.86 . . 154 2925 100.00 . . . . 0.1505 . . . . . . . . . . . 0.1584 
# 
_struct.entry_id                     9NB2 
_struct.title                        'X-ray diffraction structure of papain soaked with E-64' 
_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        9NB2 
_struct_keywords.text            'Inhibitor, Complex, Enzyme, 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              9NB2 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 212 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P00784 
_struct_ref_seq.db_align_beg                  134 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  345 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       212 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 ARG A 8   ? GLY A 11  ? ARG A 8   GLY A 11  5 ? 4  
HELX_P HELX_P2 AA2 SER A 24  ? GLY A 43  ? SER A 24  GLY A 43  1 ? 20 
HELX_P HELX_P3 AA3 SER A 49  ? ASP A 57  ? SER A 49  ASP A 57  1 ? 9  
HELX_P HELX_P4 AA4 TYR A 61  ? GLY A 65  ? TYR A 61  GLY A 65  5 ? 5  
HELX_P HELX_P5 AA5 TYR A 67  ? TYR A 78  ? TYR A 67  TYR A 78  1 ? 12 
HELX_P HELX_P6 AA6 SER A 97  ? GLY A 101 ? SER A 97  GLY A 101 5 ? 5  
HELX_P HELX_P7 AA7 ASN A 117 ? GLN A 128 ? ASN A 117 GLN A 128 1 ? 12 
HELX_P HELX_P8 AA8 GLY A 138 ? LEU A 143 ? GLY A 138 LEU A 143 1 ? 6  
HELX_P HELX_P9 AA9 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 ? ? ? ? ? ? ? 2.020 ? ? 
disulf2 disulf ?    ? A CYS 56  SG ? ? ? 1_555 A CYS 95  SG ? ? A CYS 56  A CYS 95  1_555 ? ? ? ? ? ? ? 2.040 ? ? 
disulf3 disulf ?    ? A CYS 153 SG ? ? ? 1_555 A CYS 200 SG ? ? A CYS 153 A CYS 200 1_555 ? ? ? ? ? ? ? 2.065 ? ? 
covale1 covale none ? A CYS 25  SG ? ? ? 1_555 B E64 .   C2 ? ? A CYS 25  A E64 301 1_555 ? ? ? ? ? ? ? 1.800 ? ? 
# 
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 E64 B .   ? CYS A 25  ? E64 A 301 ? 1_555 CYS A 25  ? 1_555 C2 SG CYS 1 E64 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       3.97 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 5 ? 
AA3 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? parallel      
AA3 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 VAL A 5   ? ASP A 6   ? VAL A 5   ASP A 6   
AA1 2 HIS A 159 ? GLY A 167 ? HIS A 159 GLY A 167 
AA1 3 VAL A 130 ? LEU A 134 ? VAL A 130 LEU A 134 
AA2 1 VAL A 5   ? ASP A 6   ? VAL A 5   ASP A 6   
AA2 2 HIS A 159 ? GLY A 167 ? HIS A 159 GLY A 167 
AA2 3 TYR A 170 ? LYS A 174 ? TYR A 170 LYS A 174 
AA2 4 TYR A 186 ? LYS A 190 ? TYR A 186 LYS A 190 
AA2 5 ILE A 148 ? PHE A 149 ? ILE A 148 PHE A 149 
AA3 1 GLY A 109 ? GLN A 112 ? GLY A 109 GLN A 112 
AA3 2 PHE A 207 ? VAL A 210 ? PHE A 207 VAL A 210 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N VAL A 5   ? N VAL A 5   O TYR A 166 ? O TYR A 166 
AA1 2 3 O ALA A 163 ? O ALA A 163 N VAL A 130 ? N VAL A 130 
AA2 1 2 N VAL A 5   ? N VAL A 5   O TYR A 166 ? O TYR A 166 
AA2 2 3 N ALA A 162 ? N ALA A 162 O LYS A 174 ? O LYS A 174 
AA2 3 4 N ILE A 173 ? N ILE A 173 O ILE A 187 ? O ILE A 187 
AA2 4 5 O ARG A 188 ? O ARG A 188 N PHE A 149 ? N PHE A 149 
AA3 1 2 N ARG A 111 ? N ARG A 111 O TYR A 208 ? O TYR A 208 
# 
_pdbx_entry_details.entry_id                   9NB2 
_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 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    ASP 
_pdbx_validate_torsion.auth_asym_id    A 
_pdbx_validate_torsion.auth_seq_id     158 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             -150.83 
_pdbx_validate_torsion.psi             6.59 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       623 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   6.54 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
E64 C1   C N N 88  
E64 O1   O N N 89  
E64 O2   O N N 90  
E64 C2   C N N 91  
E64 C3   C N S 92  
E64 O3   O N N 93  
E64 C4   C N N 94  
E64 O4   O N N 95  
E64 N1   N N N 96  
E64 C6   C N S 97  
E64 C7   C N N 98  
E64 C8   C N N 99  
E64 C9   C N N 100 
E64 C10  C N N 101 
E64 C11  C N N 102 
E64 O5   O N N 103 
E64 N2   N N N 104 
E64 C12  C N N 105 
E64 C13  C N N 106 
E64 C14  C N N 107 
E64 C15  C N N 108 
E64 N3   N N N 109 
E64 C16  C N N 110 
E64 N4   N N N 111 
E64 N5   N N N 112 
E64 HO2  H N N 113 
E64 H21  H N N 114 
E64 H22  H N N 115 
E64 H3   H N N 116 
E64 HO3  H N N 117 
E64 HN1  H N N 118 
E64 H6   H N N 119 
E64 H71  H N N 120 
E64 H72  H N N 121 
E64 H8   H N N 122 
E64 H91  H N N 123 
E64 H92  H N N 124 
E64 H93  H N N 125 
E64 H101 H N N 126 
E64 H102 H N N 127 
E64 H103 H N N 128 
E64 HN2  H N N 129 
E64 H121 H N N 130 
E64 H122 H N N 131 
E64 H131 H N N 132 
E64 H132 H N N 133 
E64 H141 H N N 134 
E64 H142 H N N 135 
E64 H151 H N N 136 
E64 H152 H N N 137 
E64 HN3  H N N 138 
E64 HN41 H N N 139 
E64 HN42 H N N 140 
E64 HN51 H N N 141 
E64 HN52 H N N 142 
GLN N    N N N 143 
GLN CA   C N S 144 
GLN C    C N N 145 
GLN O    O N N 146 
GLN CB   C N N 147 
GLN CG   C N N 148 
GLN CD   C N N 149 
GLN OE1  O N N 150 
GLN NE2  N N N 151 
GLN OXT  O N N 152 
GLN H    H N N 153 
GLN H2   H N N 154 
GLN HA   H N N 155 
GLN HB2  H N N 156 
GLN HB3  H N N 157 
GLN HG2  H N N 158 
GLN HG3  H N N 159 
GLN HE21 H N N 160 
GLN HE22 H N N 161 
GLN HXT  H N N 162 
GLU N    N N N 163 
GLU CA   C N S 164 
GLU C    C N N 165 
GLU O    O N N 166 
GLU CB   C N N 167 
GLU CG   C N N 168 
GLU CD   C N N 169 
GLU OE1  O N N 170 
GLU OE2  O N N 171 
GLU OXT  O N N 172 
GLU H    H N N 173 
GLU H2   H N N 174 
GLU HA   H N N 175 
GLU HB2  H N N 176 
GLU HB3  H N N 177 
GLU HG2  H N N 178 
GLU HG3  H N N 179 
GLU HE2  H N N 180 
GLU HXT  H N N 181 
GLY N    N N N 182 
GLY CA   C N N 183 
GLY C    C N N 184 
GLY O    O N N 185 
GLY OXT  O N N 186 
GLY H    H N N 187 
GLY H2   H N N 188 
GLY HA2  H N N 189 
GLY HA3  H N N 190 
GLY HXT  H N N 191 
HIS N    N N N 192 
HIS CA   C N S 193 
HIS C    C N N 194 
HIS O    O N N 195 
HIS CB   C N N 196 
HIS CG   C Y N 197 
HIS ND1  N Y N 198 
HIS CD2  C Y N 199 
HIS CE1  C Y N 200 
HIS NE2  N Y N 201 
HIS OXT  O N N 202 
HIS H    H N N 203 
HIS H2   H N N 204 
HIS HA   H N N 205 
HIS HB2  H N N 206 
HIS HB3  H N N 207 
HIS HD1  H N N 208 
HIS HD2  H N N 209 
HIS HE1  H N N 210 
HIS HE2  H N N 211 
HIS HXT  H N N 212 
HOH O    O N N 213 
HOH H1   H N N 214 
HOH H2   H N N 215 
ILE N    N N N 216 
ILE CA   C N S 217 
ILE C    C N N 218 
ILE O    O N N 219 
ILE CB   C N S 220 
ILE CG1  C N N 221 
ILE CG2  C N N 222 
ILE CD1  C N N 223 
ILE OXT  O N N 224 
ILE H    H N N 225 
ILE H2   H N N 226 
ILE HA   H N N 227 
ILE HB   H N N 228 
ILE HG12 H N N 229 
ILE HG13 H N N 230 
ILE HG21 H N N 231 
ILE HG22 H N N 232 
ILE HG23 H N N 233 
ILE HD11 H N N 234 
ILE HD12 H N N 235 
ILE HD13 H N N 236 
ILE HXT  H N N 237 
LEU N    N N N 238 
LEU CA   C N S 239 
LEU C    C N N 240 
LEU O    O N N 241 
LEU CB   C N N 242 
LEU CG   C N N 243 
LEU CD1  C N N 244 
LEU CD2  C N N 245 
LEU OXT  O N N 246 
LEU H    H N N 247 
LEU H2   H N N 248 
LEU HA   H N N 249 
LEU HB2  H N N 250 
LEU HB3  H N N 251 
LEU HG   H N N 252 
LEU HD11 H N N 253 
LEU HD12 H N N 254 
LEU HD13 H N N 255 
LEU HD21 H N N 256 
LEU HD22 H N N 257 
LEU HD23 H N N 258 
LEU HXT  H N N 259 
LYS N    N N N 260 
LYS CA   C N S 261 
LYS C    C N N 262 
LYS O    O N N 263 
LYS CB   C N N 264 
LYS CG   C N N 265 
LYS CD   C N N 266 
LYS CE   C N N 267 
LYS NZ   N N N 268 
LYS OXT  O N N 269 
LYS H    H N N 270 
LYS H2   H N N 271 
LYS HA   H N N 272 
LYS HB2  H N N 273 
LYS HB3  H N N 274 
LYS HG2  H N N 275 
LYS HG3  H N N 276 
LYS HD2  H N N 277 
LYS HD3  H N N 278 
LYS HE2  H N N 279 
LYS HE3  H N N 280 
LYS HZ1  H N N 281 
LYS HZ2  H N N 282 
LYS HZ3  H N N 283 
LYS HXT  H N N 284 
PHE N    N N N 285 
PHE CA   C N S 286 
PHE C    C N N 287 
PHE O    O N N 288 
PHE CB   C N N 289 
PHE CG   C Y N 290 
PHE CD1  C Y N 291 
PHE CD2  C Y N 292 
PHE CE1  C Y N 293 
PHE CE2  C Y N 294 
PHE CZ   C Y N 295 
PHE OXT  O N N 296 
PHE H    H N N 297 
PHE H2   H N N 298 
PHE HA   H N N 299 
PHE HB2  H N N 300 
PHE HB3  H N N 301 
PHE HD1  H N N 302 
PHE HD2  H N N 303 
PHE HE1  H N N 304 
PHE HE2  H N N 305 
PHE HZ   H N N 306 
PHE HXT  H N N 307 
PRO N    N N N 308 
PRO CA   C N S 309 
PRO C    C N N 310 
PRO O    O N N 311 
PRO CB   C N N 312 
PRO CG   C N N 313 
PRO CD   C N N 314 
PRO OXT  O N N 315 
PRO H    H N N 316 
PRO HA   H N N 317 
PRO HB2  H N N 318 
PRO HB3  H N N 319 
PRO HG2  H N N 320 
PRO HG3  H N N 321 
PRO HD2  H N N 322 
PRO HD3  H N N 323 
PRO HXT  H N N 324 
SER N    N N N 325 
SER CA   C N S 326 
SER C    C N N 327 
SER O    O N N 328 
SER CB   C N N 329 
SER OG   O N N 330 
SER OXT  O N N 331 
SER H    H N N 332 
SER H2   H N N 333 
SER HA   H N N 334 
SER HB2  H N N 335 
SER HB3  H N N 336 
SER HG   H N N 337 
SER HXT  H N N 338 
THR N    N N N 339 
THR CA   C N S 340 
THR C    C N N 341 
THR O    O N N 342 
THR CB   C N R 343 
THR OG1  O N N 344 
THR CG2  C N N 345 
THR OXT  O N N 346 
THR H    H N N 347 
THR H2   H N N 348 
THR HA   H N N 349 
THR HB   H N N 350 
THR HG1  H N N 351 
THR HG21 H N N 352 
THR HG22 H N N 353 
THR HG23 H N N 354 
THR HXT  H N N 355 
TRP N    N N N 356 
TRP CA   C N S 357 
TRP C    C N N 358 
TRP O    O N N 359 
TRP CB   C N N 360 
TRP CG   C Y N 361 
TRP CD1  C Y N 362 
TRP CD2  C Y N 363 
TRP NE1  N Y N 364 
TRP CE2  C Y N 365 
TRP CE3  C Y N 366 
TRP CZ2  C Y N 367 
TRP CZ3  C Y N 368 
TRP CH2  C Y N 369 
TRP OXT  O N N 370 
TRP H    H N N 371 
TRP H2   H N N 372 
TRP HA   H N N 373 
TRP HB2  H N N 374 
TRP HB3  H N N 375 
TRP HD1  H N N 376 
TRP HE1  H N N 377 
TRP HE3  H N N 378 
TRP HZ2  H N N 379 
TRP HZ3  H N N 380 
TRP HH2  H N N 381 
TRP HXT  H N N 382 
TYR N    N N N 383 
TYR CA   C N S 384 
TYR C    C N N 385 
TYR O    O N N 386 
TYR CB   C N N 387 
TYR CG   C Y N 388 
TYR CD1  C Y N 389 
TYR CD2  C Y N 390 
TYR CE1  C Y N 391 
TYR CE2  C Y N 392 
TYR CZ   C Y N 393 
TYR OH   O N N 394 
TYR OXT  O N N 395 
TYR H    H N N 396 
TYR H2   H N N 397 
TYR HA   H N N 398 
TYR HB2  H N N 399 
TYR HB3  H N N 400 
TYR HD1  H N N 401 
TYR HD2  H N N 402 
TYR HE1  H N N 403 
TYR HE2  H N N 404 
TYR HH   H N N 405 
TYR HXT  H N N 406 
VAL N    N N N 407 
VAL CA   C N S 408 
VAL C    C N N 409 
VAL O    O N N 410 
VAL CB   C N N 411 
VAL CG1  C N N 412 
VAL CG2  C N N 413 
VAL OXT  O N N 414 
VAL H    H N N 415 
VAL H2   H N N 416 
VAL HA   H N N 417 
VAL HB   H N N 418 
VAL HG11 H N N 419 
VAL HG12 H N N 420 
VAL HG13 H N N 421 
VAL HG21 H N N 422 
VAL HG22 H N N 423 
VAL HG23 H N N 424 
VAL HXT  H N N 425 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
E64 C1  O1   doub N N 83  
E64 C1  O2   sing N N 84  
E64 C1  C2   sing N N 85  
E64 O2  HO2  sing N N 86  
E64 C2  C3   sing N N 87  
E64 C2  H21  sing N N 88  
E64 C2  H22  sing N N 89  
E64 C3  O3   sing N N 90  
E64 C3  C4   sing N N 91  
E64 C3  H3   sing N N 92  
E64 O3  HO3  sing N N 93  
E64 C4  O4   doub N N 94  
E64 C4  N1   sing N N 95  
E64 N1  C6   sing N N 96  
E64 N1  HN1  sing N N 97  
E64 C6  C7   sing N N 98  
E64 C6  C11  sing N N 99  
E64 C6  H6   sing N N 100 
E64 C7  C8   sing N N 101 
E64 C7  H71  sing N N 102 
E64 C7  H72  sing N N 103 
E64 C8  C9   sing N N 104 
E64 C8  C10  sing N N 105 
E64 C8  H8   sing N N 106 
E64 C9  H91  sing N N 107 
E64 C9  H92  sing N N 108 
E64 C9  H93  sing N N 109 
E64 C10 H101 sing N N 110 
E64 C10 H102 sing N N 111 
E64 C10 H103 sing N N 112 
E64 C11 O5   doub N N 113 
E64 C11 N2   sing N N 114 
E64 N2  C12  sing N N 115 
E64 N2  HN2  sing N N 116 
E64 C12 C13  sing N N 117 
E64 C12 H121 sing N N 118 
E64 C12 H122 sing N N 119 
E64 C13 C14  sing N N 120 
E64 C13 H131 sing N N 121 
E64 C13 H132 sing N N 122 
E64 C14 C15  sing N N 123 
E64 C14 H141 sing N N 124 
E64 C14 H142 sing N N 125 
E64 C15 N3   sing N N 126 
E64 C15 H151 sing N N 127 
E64 C15 H152 sing N N 128 
E64 N3  C16  sing N N 129 
E64 N3  HN3  sing N N 130 
E64 C16 N4   sing N N 131 
E64 C16 N5   doub N N 132 
E64 N4  HN41 sing N N 133 
E64 N4  HN42 sing N N 134 
E64 N5  HN51 sing N N 135 
E64 N5  HN52 sing N N 136 
GLN N   CA   sing N N 137 
GLN N   H    sing N N 138 
GLN N   H2   sing N N 139 
GLN CA  C    sing N N 140 
GLN CA  CB   sing N N 141 
GLN CA  HA   sing N N 142 
GLN C   O    doub N N 143 
GLN C   OXT  sing N N 144 
GLN CB  CG   sing N N 145 
GLN CB  HB2  sing N N 146 
GLN CB  HB3  sing N N 147 
GLN CG  CD   sing N N 148 
GLN CG  HG2  sing N N 149 
GLN CG  HG3  sing N N 150 
GLN CD  OE1  doub N N 151 
GLN CD  NE2  sing N N 152 
GLN NE2 HE21 sing N N 153 
GLN NE2 HE22 sing N N 154 
GLN OXT HXT  sing N N 155 
GLU N   CA   sing N N 156 
GLU N   H    sing N N 157 
GLU N   H2   sing N N 158 
GLU CA  C    sing N N 159 
GLU CA  CB   sing N N 160 
GLU CA  HA   sing N N 161 
GLU C   O    doub N N 162 
GLU C   OXT  sing N N 163 
GLU CB  CG   sing N N 164 
GLU CB  HB2  sing N N 165 
GLU CB  HB3  sing N N 166 
GLU CG  CD   sing N N 167 
GLU CG  HG2  sing N N 168 
GLU CG  HG3  sing N N 169 
GLU CD  OE1  doub N N 170 
GLU CD  OE2  sing N N 171 
GLU OE2 HE2  sing N N 172 
GLU OXT HXT  sing N N 173 
GLY N   CA   sing N N 174 
GLY N   H    sing N N 175 
GLY N   H2   sing N N 176 
GLY CA  C    sing N N 177 
GLY CA  HA2  sing N N 178 
GLY CA  HA3  sing N N 179 
GLY C   O    doub N N 180 
GLY C   OXT  sing N N 181 
GLY OXT HXT  sing N N 182 
HIS N   CA   sing N N 183 
HIS N   H    sing N N 184 
HIS N   H2   sing N N 185 
HIS CA  C    sing N N 186 
HIS CA  CB   sing N N 187 
HIS CA  HA   sing N N 188 
HIS C   O    doub N N 189 
HIS C   OXT  sing N N 190 
HIS CB  CG   sing N N 191 
HIS CB  HB2  sing N N 192 
HIS CB  HB3  sing N N 193 
HIS CG  ND1  sing Y N 194 
HIS CG  CD2  doub Y N 195 
HIS ND1 CE1  doub Y N 196 
HIS ND1 HD1  sing N N 197 
HIS CD2 NE2  sing Y N 198 
HIS CD2 HD2  sing N N 199 
HIS CE1 NE2  sing Y N 200 
HIS CE1 HE1  sing N N 201 
HIS NE2 HE2  sing N N 202 
HIS OXT HXT  sing N N 203 
HOH O   H1   sing N N 204 
HOH O   H2   sing N N 205 
ILE N   CA   sing N N 206 
ILE N   H    sing N N 207 
ILE N   H2   sing N N 208 
ILE CA  C    sing N N 209 
ILE CA  CB   sing N N 210 
ILE CA  HA   sing N N 211 
ILE C   O    doub N N 212 
ILE C   OXT  sing N N 213 
ILE CB  CG1  sing N N 214 
ILE CB  CG2  sing N N 215 
ILE CB  HB   sing N N 216 
ILE CG1 CD1  sing N N 217 
ILE CG1 HG12 sing N N 218 
ILE CG1 HG13 sing N N 219 
ILE CG2 HG21 sing N N 220 
ILE CG2 HG22 sing N N 221 
ILE CG2 HG23 sing N N 222 
ILE CD1 HD11 sing N N 223 
ILE CD1 HD12 sing N N 224 
ILE CD1 HD13 sing N N 225 
ILE OXT HXT  sing N N 226 
LEU N   CA   sing N N 227 
LEU N   H    sing N N 228 
LEU N   H2   sing N N 229 
LEU CA  C    sing N N 230 
LEU CA  CB   sing N N 231 
LEU CA  HA   sing N N 232 
LEU C   O    doub N N 233 
LEU C   OXT  sing N N 234 
LEU CB  CG   sing N N 235 
LEU CB  HB2  sing N N 236 
LEU CB  HB3  sing N N 237 
LEU CG  CD1  sing N N 238 
LEU CG  CD2  sing N N 239 
LEU CG  HG   sing N N 240 
LEU CD1 HD11 sing N N 241 
LEU CD1 HD12 sing N N 242 
LEU CD1 HD13 sing N N 243 
LEU CD2 HD21 sing N N 244 
LEU CD2 HD22 sing N N 245 
LEU CD2 HD23 sing N N 246 
LEU OXT HXT  sing N N 247 
LYS N   CA   sing N N 248 
LYS N   H    sing N N 249 
LYS N   H2   sing N N 250 
LYS CA  C    sing N N 251 
LYS CA  CB   sing N N 252 
LYS CA  HA   sing N N 253 
LYS C   O    doub N N 254 
LYS C   OXT  sing N N 255 
LYS CB  CG   sing N N 256 
LYS CB  HB2  sing N N 257 
LYS CB  HB3  sing N N 258 
LYS CG  CD   sing N N 259 
LYS CG  HG2  sing N N 260 
LYS CG  HG3  sing N N 261 
LYS CD  CE   sing N N 262 
LYS CD  HD2  sing N N 263 
LYS CD  HD3  sing N N 264 
LYS CE  NZ   sing N N 265 
LYS CE  HE2  sing N N 266 
LYS CE  HE3  sing N N 267 
LYS NZ  HZ1  sing N N 268 
LYS NZ  HZ2  sing N N 269 
LYS NZ  HZ3  sing N N 270 
LYS OXT HXT  sing N N 271 
PHE N   CA   sing N N 272 
PHE N   H    sing N N 273 
PHE N   H2   sing N N 274 
PHE CA  C    sing N N 275 
PHE CA  CB   sing N N 276 
PHE CA  HA   sing N N 277 
PHE C   O    doub N N 278 
PHE C   OXT  sing N N 279 
PHE CB  CG   sing N N 280 
PHE CB  HB2  sing N N 281 
PHE CB  HB3  sing N N 282 
PHE CG  CD1  doub Y N 283 
PHE CG  CD2  sing Y N 284 
PHE CD1 CE1  sing Y N 285 
PHE CD1 HD1  sing N N 286 
PHE CD2 CE2  doub Y N 287 
PHE CD2 HD2  sing N N 288 
PHE CE1 CZ   doub Y N 289 
PHE CE1 HE1  sing N N 290 
PHE CE2 CZ   sing Y N 291 
PHE CE2 HE2  sing N N 292 
PHE CZ  HZ   sing N N 293 
PHE OXT HXT  sing N N 294 
PRO N   CA   sing N N 295 
PRO N   CD   sing N N 296 
PRO N   H    sing N N 297 
PRO CA  C    sing N N 298 
PRO CA  CB   sing N N 299 
PRO CA  HA   sing N N 300 
PRO C   O    doub N N 301 
PRO C   OXT  sing N N 302 
PRO CB  CG   sing N N 303 
PRO CB  HB2  sing N N 304 
PRO CB  HB3  sing N N 305 
PRO CG  CD   sing N N 306 
PRO CG  HG2  sing N N 307 
PRO CG  HG3  sing N N 308 
PRO CD  HD2  sing N N 309 
PRO CD  HD3  sing N N 310 
PRO OXT HXT  sing N N 311 
SER N   CA   sing N N 312 
SER N   H    sing N N 313 
SER N   H2   sing N N 314 
SER CA  C    sing N N 315 
SER CA  CB   sing N N 316 
SER CA  HA   sing N N 317 
SER C   O    doub N N 318 
SER C   OXT  sing N N 319 
SER CB  OG   sing N N 320 
SER CB  HB2  sing N N 321 
SER CB  HB3  sing N N 322 
SER OG  HG   sing N N 323 
SER OXT HXT  sing N N 324 
THR N   CA   sing N N 325 
THR N   H    sing N N 326 
THR N   H2   sing N N 327 
THR CA  C    sing N N 328 
THR CA  CB   sing N N 329 
THR CA  HA   sing N N 330 
THR C   O    doub N N 331 
THR C   OXT  sing N N 332 
THR CB  OG1  sing N N 333 
THR CB  CG2  sing N N 334 
THR CB  HB   sing N N 335 
THR OG1 HG1  sing N N 336 
THR CG2 HG21 sing N N 337 
THR CG2 HG22 sing N N 338 
THR CG2 HG23 sing N N 339 
THR OXT HXT  sing N N 340 
TRP N   CA   sing N N 341 
TRP N   H    sing N N 342 
TRP N   H2   sing N N 343 
TRP CA  C    sing N N 344 
TRP CA  CB   sing N N 345 
TRP CA  HA   sing N N 346 
TRP C   O    doub N N 347 
TRP C   OXT  sing N N 348 
TRP CB  CG   sing N N 349 
TRP CB  HB2  sing N N 350 
TRP CB  HB3  sing N N 351 
TRP CG  CD1  doub Y N 352 
TRP CG  CD2  sing Y N 353 
TRP CD1 NE1  sing Y N 354 
TRP CD1 HD1  sing N N 355 
TRP CD2 CE2  doub Y N 356 
TRP CD2 CE3  sing Y N 357 
TRP NE1 CE2  sing Y N 358 
TRP NE1 HE1  sing N N 359 
TRP CE2 CZ2  sing Y N 360 
TRP CE3 CZ3  doub Y N 361 
TRP CE3 HE3  sing N N 362 
TRP CZ2 CH2  doub Y N 363 
TRP CZ2 HZ2  sing N N 364 
TRP CZ3 CH2  sing Y N 365 
TRP CZ3 HZ3  sing N N 366 
TRP CH2 HH2  sing N N 367 
TRP OXT HXT  sing N N 368 
TYR N   CA   sing N N 369 
TYR N   H    sing N N 370 
TYR N   H2   sing N N 371 
TYR CA  C    sing N N 372 
TYR CA  CB   sing N N 373 
TYR CA  HA   sing N N 374 
TYR C   O    doub N N 375 
TYR C   OXT  sing N N 376 
TYR CB  CG   sing N N 377 
TYR CB  HB2  sing N N 378 
TYR CB  HB3  sing N N 379 
TYR CG  CD1  doub Y N 380 
TYR CG  CD2  sing Y N 381 
TYR CD1 CE1  sing Y N 382 
TYR CD1 HD1  sing N N 383 
TYR CD2 CE2  doub Y N 384 
TYR CD2 HD2  sing N N 385 
TYR CE1 CZ   doub Y N 386 
TYR CE1 HE1  sing N N 387 
TYR CE2 CZ   sing Y N 388 
TYR CE2 HE2  sing N N 389 
TYR CZ  OH   sing N N 390 
TYR OH  HH   sing N N 391 
TYR OXT HXT  sing N N 392 
VAL N   CA   sing N N 393 
VAL N   H    sing N N 394 
VAL N   H2   sing N N 395 
VAL CA  C    sing N N 396 
VAL CA  CB   sing N N 397 
VAL CA  HA   sing N N 398 
VAL C   O    doub N N 399 
VAL C   OXT  sing N N 400 
VAL CB  CG1  sing N N 401 
VAL CB  CG2  sing N N 402 
VAL CB  HB   sing N N 403 
VAL CG1 HG11 sing N N 404 
VAL CG1 HG12 sing N N 405 
VAL CG1 HG13 sing N N 406 
VAL CG2 HG21 sing N N 407 
VAL CG2 HG22 sing N N 408 
VAL CG2 HG23 sing N N 409 
VAL OXT HXT  sing N N 410 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Howard Hughes Medical Institute (HHMI)'           'United States' HHMI-EPI          1 
'National Science Foundation (NSF, United States)' 'United States' DMR-1548924       2 
'Department of Energy (DOE, United States)'        'United States' DE-FC02-02ER63421 3 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   9PAP 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9NB2 
_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]   0.023579 
_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]   0.020446 
_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]   0.009832 
_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   ? 22.774  -10.726 20.880 1.00 15.25 ? 1   ILE A N   1 
ATOM   2    C CA  . ILE A 1 1   ? 22.509  -9.777  19.802 1.00 15.62 ? 1   ILE A CA  1 
ATOM   3    C C   . ILE A 1 1   ? 23.779  -8.949  19.567 1.00 18.73 ? 1   ILE A C   1 
ATOM   4    O O   . ILE A 1 1   ? 24.625  -8.839  20.468 1.00 16.31 ? 1   ILE A O   1 
ATOM   5    C CB  . ILE A 1 1   ? 21.268  -8.895  20.121 1.00 14.79 ? 1   ILE A CB  1 
ATOM   6    C CG1 . ILE A 1 1   ? 21.519  -7.962  21.312 1.00 15.50 ? 1   ILE A CG1 1 
ATOM   7    C CG2 . ILE A 1 1   ? 20.039  -9.783  20.370 1.00 16.52 ? 1   ILE A CG2 1 
ATOM   8    C CD1 . ILE A 1 1   ? 20.298  -7.113  21.678 1.00 18.23 ? 1   ILE A CD1 1 
ATOM   9    N N   . PRO A 1 2   ? 23.937  -8.389  18.370 1.00 16.88 ? 2   PRO A N   1 
ATOM   10   C CA  . PRO A 1 2   ? 25.208  -7.755  18.008 1.00 18.94 ? 2   PRO A CA  1 
ATOM   11   C C   . PRO A 1 2   ? 25.329  -6.361  18.602 1.00 18.36 ? 2   PRO A C   1 
ATOM   12   O O   . PRO A 1 2   ? 24.379  -5.791  19.144 1.00 18.35 ? 2   PRO A O   1 
ATOM   13   C CB  . PRO A 1 2   ? 25.161  -7.659  16.477 1.00 23.21 ? 2   PRO A CB  1 
ATOM   14   C CG  . PRO A 1 2   ? 23.862  -8.211  16.053 1.00 22.64 ? 2   PRO A CG  1 
ATOM   15   C CD  . PRO A 1 2   ? 22.977  -8.335  17.254 1.00 19.13 ? 2   PRO A CD  1 
ATOM   16   N N   A GLU A 1 3   ? 26.535  -5.802  18.483 0.52 17.05 ? 3   GLU A N   1 
ATOM   17   N N   B GLU A 1 3   ? 26.529  -5.804  18.450 0.48 17.07 ? 3   GLU A N   1 
ATOM   18   C CA  A GLU A 1 3   ? 26.777  -4.467  19.018 0.52 18.00 ? 3   GLU A CA  1 
ATOM   19   C CA  B GLU A 1 3   ? 26.818  -4.483  18.983 0.48 18.00 ? 3   GLU A CA  1 
ATOM   20   C C   A GLU A 1 3   ? 26.215  -3.369  18.123 0.52 15.18 ? 3   GLU A C   1 
ATOM   21   C C   B GLU A 1 3   ? 26.241  -3.374  18.117 0.48 15.19 ? 3   GLU A C   1 
ATOM   22   O O   A GLU A 1 3   ? 25.875  -2.293  18.626 0.52 15.90 ? 3   GLU A O   1 
ATOM   23   O O   B GLU A 1 3   ? 25.920  -2.299  18.635 0.48 15.88 ? 3   GLU A O   1 
ATOM   24   C CB  A GLU A 1 3   ? 28.276  -4.248  19.249 0.52 19.46 ? 3   GLU A CB  1 
ATOM   25   C CB  B GLU A 1 3   ? 28.326  -4.312  19.136 0.48 19.48 ? 3   GLU A CB  1 
ATOM   26   C CG  A GLU A 1 3   ? 28.820  -4.914  20.517 0.52 23.60 ? 3   GLU A CG  1 
ATOM   27   C CG  B GLU A 1 3   ? 28.893  -5.162  20.251 0.48 23.26 ? 3   GLU A CG  1 
ATOM   28   C CD  A GLU A 1 3   ? 28.986  -3.947  21.686 0.52 23.37 ? 3   GLU A CD  1 
ATOM   29   C CD  B GLU A 1 3   ? 30.359  -4.911  20.480 0.48 22.46 ? 3   GLU A CD  1 
ATOM   30   O OE1 A GLU A 1 3   ? 28.003  -3.304  22.104 0.52 22.20 ? 3   GLU A OE1 1 
ATOM   31   O OE1 B GLU A 1 3   ? 31.193  -5.574  19.828 0.48 30.02 ? 3   GLU A OE1 1 
ATOM   32   O OE2 A GLU A 1 3   ? 30.125  -3.820  22.188 0.52 30.37 ? 3   GLU A OE2 1 
ATOM   33   O OE2 B GLU A 1 3   ? 30.669  -4.021  21.296 0.48 23.78 ? 3   GLU A OE2 1 
ATOM   34   N N   . TYR A 1 4   ? 26.092  -3.615  16.816 1.00 16.83 ? 4   TYR A N   1 
ATOM   35   C CA  . TYR A 1 4   ? 25.486  -2.657  15.897 1.00 13.90 ? 4   TYR A CA  1 
ATOM   36   C C   . TYR A 1 4   ? 24.363  -3.314  15.110 1.00 16.54 ? 4   TYR A C   1 
ATOM   37   O O   . TYR A 1 4   ? 24.510  -4.445  14.632 1.00 15.24 ? 4   TYR A O   1 
ATOM   38   C CB  . TYR A 1 4   ? 26.500  -2.086  14.900 1.00 16.45 ? 4   TYR A CB  1 
ATOM   39   C CG  . TYR A 1 4   ? 27.412  -1.058  15.505 1.00 17.57 ? 4   TYR A CG  1 
ATOM   40   C CD1 . TYR A 1 4   ? 27.014  0.266   15.623 1.00 14.88 ? 4   TYR A CD1 1 
ATOM   41   C CD2 . TYR A 1 4   ? 28.680  -1.404  15.949 1.00 19.67 ? 4   TYR A CD2 1 
ATOM   42   C CE1 . TYR A 1 4   ? 27.852  1.222   16.189 1.00 18.29 ? 4   TYR A CE1 1 
ATOM   43   C CE2 . TYR A 1 4   ? 29.520  -0.461  16.518 1.00 22.36 ? 4   TYR A CE2 1 
ATOM   44   C CZ  . TYR A 1 4   ? 29.109  0.847   16.623 1.00 16.17 ? 4   TYR A CZ  1 
ATOM   45   O OH  . TYR A 1 4   ? 29.957  1.778   17.191 1.00 21.30 ? 4   TYR A OH  1 
ATOM   46   N N   . VAL A 1 5   ? 23.249  -2.588  14.963 1.00 14.11 ? 5   VAL A N   1 
ATOM   47   C CA  . VAL A 1 5   ? 22.177  -2.937  14.038 1.00 13.23 ? 5   VAL A CA  1 
ATOM   48   C C   . VAL A 1 5   ? 21.809  -1.679  13.254 1.00 15.98 ? 5   VAL A C   1 
ATOM   49   O O   . VAL A 1 5   ? 21.763  -0.582  13.817 1.00 14.74 ? 5   VAL A O   1 
ATOM   50   C CB  . VAL A 1 5   ? 20.946  -3.507  14.774 1.00 14.04 ? 5   VAL A CB  1 
ATOM   51   C CG1 . VAL A 1 5   ? 19.764  -3.637  13.819 1.00 16.41 ? 5   VAL A CG1 1 
ATOM   52   C CG2 . VAL A 1 5   ? 21.269  -4.859  15.412 1.00 16.18 ? 5   VAL A CG2 1 
ATOM   53   N N   . ASP A 1 6   ? 21.597  -1.827  11.945 1.00 14.76 ? 6   ASP A N   1 
ATOM   54   C CA  . ASP A 1 6   ? 21.133  -0.718  11.105 1.00 12.86 ? 6   ASP A CA  1 
ATOM   55   C C   . ASP A 1 6   ? 20.307  -1.322  9.975  1.00 15.05 ? 6   ASP A C   1 
ATOM   56   O O   . ASP A 1 6   ? 20.863  -1.774  8.973  1.00 14.98 ? 6   ASP A O   1 
ATOM   57   C CB  . ASP A 1 6   ? 22.303  0.102   10.568 1.00 14.16 ? 6   ASP A CB  1 
ATOM   58   C CG  . ASP A 1 6   ? 21.853  1.387   9.873  1.00 16.64 ? 6   ASP A CG  1 
ATOM   59   O OD1 . ASP A 1 6   ? 20.683  1.476   9.416  1.00 14.19 ? 6   ASP A OD1 1 
ATOM   60   O OD2 . ASP A 1 6   ? 22.696  2.302   9.746  1.00 17.15 ? 6   ASP A OD2 1 
ATOM   61   N N   . TRP A 1 7   ? 18.987  -1.305  10.137 1.00 13.68 ? 7   TRP A N   1 
ATOM   62   C CA  . TRP A 1 7   ? 18.120  -1.912  9.134  1.00 12.79 ? 7   TRP A CA  1 
ATOM   63   C C   . TRP A 1 7   ? 18.190  -1.219  7.781  1.00 14.67 ? 7   TRP A C   1 
ATOM   64   O O   . TRP A 1 7   ? 17.809  -1.828  6.771  1.00 13.82 ? 7   TRP A O   1 
ATOM   65   C CB  . TRP A 1 7   ? 16.685  -1.949  9.669  1.00 10.87 ? 7   TRP A CB  1 
ATOM   66   C CG  . TRP A 1 7   ? 16.526  -3.100  10.630 1.00 12.66 ? 7   TRP A CG  1 
ATOM   67   C CD1 . TRP A 1 7   ? 16.388  -3.029  11.982 1.00 14.50 ? 7   TRP A CD1 1 
ATOM   68   C CD2 . TRP A 1 7   ? 16.539  -4.495  10.298 1.00 15.66 ? 7   TRP A CD2 1 
ATOM   69   N NE1 . TRP A 1 7   ? 16.293  -4.292  12.517 1.00 14.99 ? 7   TRP A NE1 1 
ATOM   70   C CE2 . TRP A 1 7   ? 16.382  -5.210  11.503 1.00 14.56 ? 7   TRP A CE2 1 
ATOM   71   C CE3 . TRP A 1 7   ? 16.663  -5.204  9.097  1.00 18.03 ? 7   TRP A CE3 1 
ATOM   72   C CZ2 . TRP A 1 7   ? 16.360  -6.598  11.546 1.00 15.97 ? 7   TRP A CZ2 1 
ATOM   73   C CZ3 . TRP A 1 7   ? 16.623  -6.591  9.135  1.00 19.14 ? 7   TRP A CZ3 1 
ATOM   74   C CH2 . TRP A 1 7   ? 16.481  -7.272  10.356 1.00 17.04 ? 7   TRP A CH2 1 
ATOM   75   N N   . ARG A 1 8   ? 18.672  0.023   7.722  1.00 13.98 ? 8   ARG A N   1 
ATOM   76   C CA  . ARG A 1 8   ? 18.876  0.658   6.423  1.00 14.47 ? 8   ARG A CA  1 
ATOM   77   C C   . ARG A 1 8   ? 19.894  -0.117  5.596  1.00 13.82 ? 8   ARG A C   1 
ATOM   78   O O   . ARG A 1 8   ? 19.750  -0.245  4.372  1.00 16.03 ? 8   ARG A O   1 
ATOM   79   C CB  . ARG A 1 8   ? 19.334  2.104   6.602  1.00 13.57 ? 8   ARG A CB  1 
ATOM   80   C CG  . ARG A 1 8   ? 18.441  2.974   7.454  1.00 15.07 ? 8   ARG A CG  1 
ATOM   81   C CD  . ARG A 1 8   ? 19.074  4.341   7.626  1.00 15.87 ? 8   ARG A CD  1 
ATOM   82   N NE  . ARG A 1 8   ? 20.257  4.254   8.485  1.00 14.49 ? 8   ARG A NE  1 
ATOM   83   C CZ  . ARG A 1 8   ? 20.954  5.300   8.915  1.00 14.96 ? 8   ARG A CZ  1 
ATOM   84   N NH1 . ARG A 1 8   ? 20.632  6.539   8.574  1.00 16.72 ? 8   ARG A NH1 1 
ATOM   85   N NH2 . ARG A 1 8   ? 22.018  5.094   9.688  1.00 15.54 ? 8   ARG A NH2 1 
ATOM   86   N N   . GLN A 1 9   ? 20.926  -0.648  6.255  1.00 14.85 ? 9   GLN A N   1 
ATOM   87   C CA  . GLN A 1 9   ? 21.985  -1.382  5.576  1.00 15.26 ? 9   GLN A CA  1 
ATOM   88   C C   . GLN A 1 9   ? 21.504  -2.709  5.019  1.00 16.22 ? 9   GLN A C   1 
ATOM   89   O O   . GLN A 1 9   ? 22.136  -3.254  4.107  1.00 21.33 ? 9   GLN A O   1 
ATOM   90   C CB  . GLN A 1 9   ? 23.134  -1.598  6.556  1.00 19.45 ? 9   GLN A CB  1 
ATOM   91   C CG  . GLN A 1 9   ? 23.985  -0.369  6.743  1.00 21.11 ? 9   GLN A CG  1 
ATOM   92   C CD  . GLN A 1 9   ? 24.980  -0.514  7.877  1.00 37.28 ? 9   GLN A CD  1 
ATOM   93   O OE1 . GLN A 1 9   ? 25.074  -1.572  8.510  1.00 32.08 ? 9   GLN A OE1 1 
ATOM   94   N NE2 . GLN A 1 9   ? 25.736  0.550   8.138  1.00 26.43 ? 9   GLN A NE2 1 
ATOM   95   N N   . LYS A 1 10  ? 20.401  -3.240  5.535  1.00 18.50 ? 10  LYS A N   1 
ATOM   96   C CA  . LYS A 1 10  ? 19.806  -4.456  5.006  1.00 20.62 ? 10  LYS A CA  1 
ATOM   97   C C   . LYS A 1 10  ? 18.695  -4.163  4.006  1.00 20.53 ? 10  LYS A C   1 
ATOM   98   O O   . LYS A 1 10  ? 17.991  -5.088  3.593  1.00 22.17 ? 10  LYS A O   1 
ATOM   99   C CB  . LYS A 1 10  ? 19.275  -5.323  6.150  1.00 19.71 ? 10  LYS A CB  1 
ATOM   100  C CG  . LYS A 1 10  ? 20.275  -5.540  7.276  1.00 22.25 ? 10  LYS A CG  1 
ATOM   101  C CD  . LYS A 1 10  ? 21.254  -6.645  6.949  1.00 36.22 ? 10  LYS A CD  1 
ATOM   102  C CE  . LYS A 1 10  ? 21.456  -7.575  8.140  1.00 35.17 ? 10  LYS A CE  1 
ATOM   103  N NZ  . LYS A 1 10  ? 20.160  -8.082  8.674  1.00 38.06 ? 10  LYS A NZ  1 
ATOM   104  N N   . GLY A 1 11  ? 18.523  -2.903  3.607  1.00 17.77 ? 11  GLY A N   1 
ATOM   105  C CA  . GLY A 1 11  ? 17.522  -2.574  2.603  1.00 14.70 ? 11  GLY A CA  1 
ATOM   106  C C   . GLY A 1 11  ? 16.095  -2.693  3.084  1.00 15.96 ? 11  GLY A C   1 
ATOM   107  O O   . GLY A 1 11  ? 15.199  -2.976  2.286  1.00 17.28 ? 11  GLY A O   1 
ATOM   108  N N   . ALA A 1 12  ? 15.859  -2.475  4.372  1.00 15.72 ? 12  ALA A N   1 
ATOM   109  C CA  . ALA A 1 12  ? 14.554  -2.683  4.973  1.00 16.34 ? 12  ALA A CA  1 
ATOM   110  C C   . ALA A 1 12  ? 13.903  -1.380  5.406  1.00 12.27 ? 12  ALA A C   1 
ATOM   111  O O   . ALA A 1 12  ? 12.887  -1.417  6.107  1.00 14.81 ? 12  ALA A O   1 
ATOM   112  C CB  . ALA A 1 12  ? 14.668  -3.643  6.163  1.00 15.86 ? 12  ALA A CB  1 
ATOM   113  N N   . VAL A 1 13  ? 14.431  -0.236  4.978  1.00 14.90 ? 13  VAL A N   1 
ATOM   114  C CA  . VAL A 1 13  ? 13.936  1.077   5.385  1.00 12.49 ? 13  VAL A CA  1 
ATOM   115  C C   . VAL A 1 13  ? 13.754  1.951   4.147  1.00 13.46 ? 13  VAL A C   1 
ATOM   116  O O   . VAL A 1 13  ? 14.690  2.129   3.358  1.00 13.61 ? 13  VAL A O   1 
ATOM   117  C CB  . VAL A 1 13  ? 14.883  1.771   6.385  1.00 14.00 ? 13  VAL A CB  1 
ATOM   118  C CG1 . VAL A 1 13  ? 14.253  3.064   6.878  1.00 15.13 ? 13  VAL A CG1 1 
ATOM   119  C CG2 . VAL A 1 13  ? 15.188  0.855   7.569  1.00 14.36 ? 13  VAL A CG2 1 
ATOM   120  N N   . THR A 1 14  ? 12.563  2.522   3.998  1.00 12.30 ? 14  THR A N   1 
ATOM   121  C CA  . THR A 1 14  ? 12.263  3.393   2.864  1.00 14.02 ? 14  THR A CA  1 
ATOM   122  C C   . THR A 1 14  ? 12.714  4.825   3.152  1.00 12.61 ? 14  THR A C   1 
ATOM   123  O O   . THR A 1 14  ? 13.162  5.145   4.260  1.00 13.27 ? 14  THR A O   1 
ATOM   124  C CB  . THR A 1 14  ? 10.766  3.365   2.569  1.00 13.90 ? 14  THR A CB  1 
ATOM   125  O OG1 . THR A 1 14  ? 10.094  4.030   3.634  1.00 13.25 ? 14  THR A OG1 1 
ATOM   126  C CG2 . THR A 1 14  ? 10.245  1.938   2.424  1.00 12.73 ? 14  THR A CG2 1 
ATOM   127  N N   . PRO A 1 15  ? 12.661  5.720   2.162  1.00 12.06 ? 15  PRO A N   1 
ATOM   128  C CA  . PRO A 1 15  ? 13.108  7.097   2.410  1.00 12.10 ? 15  PRO A CA  1 
ATOM   129  C C   . PRO A 1 15  ? 12.337  7.783   3.532  1.00 12.62 ? 15  PRO A C   1 
ATOM   130  O O   . PRO A 1 15  ? 11.194  7.447   3.853  1.00 13.74 ? 15  PRO A O   1 
ATOM   131  C CB  . PRO A 1 15  ? 12.846  7.793   1.072  1.00 12.91 ? 15  PRO A CB  1 
ATOM   132  C CG  . PRO A 1 15  ? 13.079  6.704   0.084  1.00 13.82 ? 15  PRO A CG  1 
ATOM   133  C CD  . PRO A 1 15  ? 12.368  5.528   0.722  1.00 12.25 ? 15  PRO A CD  1 
ATOM   134  N N   . VAL A 1 16  ? 13.002  8.773   4.130  1.00 11.09 ? 16  VAL A N   1 
ATOM   135  C CA  . VAL A 1 16  ? 12.437  9.536   5.229  1.00 10.53 ? 16  VAL A CA  1 
ATOM   136  C C   . VAL A 1 16  ? 11.267  10.374  4.739  1.00 11.98 ? 16  VAL A C   1 
ATOM   137  O O   . VAL A 1 16  ? 11.329  11.015  3.681  1.00 13.53 ? 16  VAL A O   1 
ATOM   138  C CB  . VAL A 1 16  ? 13.524  10.426  5.853  1.00 10.66 ? 16  VAL A CB  1 
ATOM   139  C CG1 . VAL A 1 16  ? 12.928  11.539  6.709  1.00 10.71 ? 16  VAL A CG1 1 
ATOM   140  C CG2 . VAL A 1 16  ? 14.525  9.581   6.627  1.00 14.50 ? 16  VAL A CG2 1 
ATOM   141  N N   . LYS A 1 17  ? 10.195  10.380  5.524  1.00 12.22 ? 17  LYS A N   1 
ATOM   142  C CA  . LYS A 1 17  ? 8.979   11.099  5.186  1.00 12.62 ? 17  LYS A CA  1 
ATOM   143  C C   . LYS A 1 17  ? 8.823   12.348  6.036  1.00 11.86 ? 17  LYS A C   1 
ATOM   144  O O   . LYS A 1 17  ? 9.483   12.536  7.060  1.00 10.97 ? 17  LYS A O   1 
ATOM   145  C CB  . LYS A 1 17  ? 7.752   10.201  5.368  1.00 11.89 ? 17  LYS A CB  1 
ATOM   146  C CG  . LYS A 1 17  ? 7.887   8.852   4.716  1.00 13.32 ? 17  LYS A CG  1 
ATOM   147  C CD  . LYS A 1 17  ? 8.230   9.010   3.238  1.00 13.60 ? 17  LYS A CD  1 
ATOM   148  C CE  . LYS A 1 17  ? 7.878   7.760   2.437  1.00 14.64 ? 17  LYS A CE  1 
ATOM   149  N NZ  . LYS A 1 17  ? 8.676   6.560   2.848  1.00 14.30 ? 17  LYS A NZ  1 
ATOM   150  N N   . ASN A 1 18  ? 7.883   13.193  5.617  1.00 13.36 ? 18  ASN A N   1 
ATOM   151  C CA  . ASN A 1 18  ? 7.522   14.401  6.349  1.00 13.52 ? 18  ASN A CA  1 
ATOM   152  C C   . ASN A 1 18  ? 6.025   14.358  6.607  1.00 13.65 ? 18  ASN A C   1 
ATOM   153  O O   . ASN A 1 18  ? 5.227   14.416  5.662  1.00 13.87 ? 18  ASN A O   1 
ATOM   154  C CB  . ASN A 1 18  ? 7.884   15.670  5.572  1.00 14.21 ? 18  ASN A CB  1 
ATOM   155  C CG  . ASN A 1 18  ? 7.766   16.929  6.420  1.00 20.15 ? 18  ASN A CG  1 
ATOM   156  O OD1 . ASN A 1 18  ? 7.192   16.919  7.512  1.00 16.27 ? 18  ASN A OD1 1 
ATOM   157  N ND2 . ASN A 1 18  ? 8.300   18.030  5.908  1.00 33.86 ? 18  ASN A ND2 1 
ATOM   158  N N   . GLN A 1 19  ? 5.647   14.281  7.879  1.00 12.45 ? 19  GLN A N   1 
ATOM   159  C CA  . GLN A 1 19  ? 4.235   14.246  8.219  1.00 14.80 ? 19  GLN A CA  1 
ATOM   160  C C   . GLN A 1 19  ? 3.569   15.608  8.091  1.00 15.67 ? 19  GLN A C   1 
ATOM   161  O O   . GLN A 1 19  ? 2.345   15.667  8.040  1.00 13.77 ? 19  GLN A O   1 
ATOM   162  C CB  . GLN A 1 19  ? 4.045   13.726  9.641  1.00 14.27 ? 19  GLN A CB  1 
ATOM   163  C CG  . GLN A 1 19  ? 4.571   14.669  10.719 1.00 12.87 ? 19  GLN A CG  1 
ATOM   164  C CD  . GLN A 1 19  ? 4.431   14.085  12.116 1.00 13.15 ? 19  GLN A CD  1 
ATOM   165  O OE1 . GLN A 1 19  ? 5.262   13.300  12.578 1.00 14.92 ? 19  GLN A OE1 1 
ATOM   166  N NE2 . GLN A 1 19  ? 3.349   14.458  12.788 1.00 17.41 ? 19  GLN A NE2 1 
ATOM   167  N N   . GLY A 1 20  ? 4.335   16.690  8.029  1.00 14.92 ? 20  GLY A N   1 
ATOM   168  C CA  . GLY A 1 20  ? 3.689   17.987  7.998  1.00 14.34 ? 20  GLY A CA  1 
ATOM   169  C C   . GLY A 1 20  ? 3.049   18.348  9.333  1.00 18.70 ? 20  GLY A C   1 
ATOM   170  O O   . GLY A 1 20  ? 3.396   17.822  10.392 1.00 19.79 ? 20  GLY A O   1 
ATOM   171  N N   . SER A 1 21  ? 2.094   19.278  9.272  1.00 20.51 ? 21  SER A N   1 
ATOM   172  C CA  . SER A 1 21  ? 1.514   19.801  10.503 1.00 18.91 ? 21  SER A CA  1 
ATOM   173  C C   . SER A 1 21  ? 0.530   18.834  11.150 1.00 25.51 ? 21  SER A C   1 
ATOM   174  O O   . SER A 1 21  ? 0.224   18.974  12.342 1.00 27.21 ? 21  SER A O   1 
ATOM   175  C CB  . SER A 1 21  ? 0.834   21.142  10.223 1.00 22.15 ? 21  SER A CB  1 
ATOM   176  O OG  . SER A 1 21  ? 0.076   21.081  9.033  1.00 27.47 ? 21  SER A OG  1 
ATOM   177  N N   . CYS A 1 22  ? 0.064   17.849  10.400 1.00 18.41 ? 22  CYS A N   1 
ATOM   178  C CA  . CYS A 1 22  ? -0.889  16.867  10.894 1.00 17.17 ? 22  CYS A CA  1 
ATOM   179  C C   . CYS A 1 22  ? -0.265  16.001  11.993 1.00 17.03 ? 22  CYS A C   1 
ATOM   180  O O   . CYS A 1 22  ? 0.887   15.571  11.886 1.00 17.11 ? 22  CYS A O   1 
ATOM   181  C CB  . CYS A 1 22  ? -1.348  16.022  9.702  1.00 16.03 ? 22  CYS A CB  1 
ATOM   182  S SG  . CYS A 1 22  ? -2.372  14.588  10.031 1.00 16.12 ? 22  CYS A SG  1 
ATOM   183  N N   . GLY A 1 23  ? -1.028  15.747  13.055 1.00 18.12 ? 23  GLY A N   1 
ATOM   184  C CA  . GLY A 1 23  ? -0.568  14.864  14.111 1.00 17.57 ? 23  GLY A CA  1 
ATOM   185  C C   . GLY A 1 23  ? -0.693  13.387  13.779 1.00 17.94 ? 23  GLY A C   1 
ATOM   186  O O   . GLY A 1 23  ? -1.385  12.639  14.478 1.00 17.35 ? 23  GLY A O   1 
ATOM   187  N N   . SER A 1 24  ? 0.018   12.959  12.737 1.00 10.98 ? 24  SER A N   1 
ATOM   188  C CA  . SER A 1 24  ? -0.086  11.616  12.174 1.00 14.43 ? 24  SER A CA  1 
ATOM   189  C C   . SER A 1 24  ? 1.141   10.757  12.469 1.00 13.52 ? 24  SER A C   1 
ATOM   190  O O   . SER A 1 24  ? 1.292   9.686   11.867 1.00 14.71 ? 24  SER A O   1 
ATOM   191  C CB  . SER A 1 24  ? -0.302  11.708  10.664 1.00 12.45 ? 24  SER A CB  1 
ATOM   192  O OG  . SER A 1 24  ? 0.704   12.541  10.118 1.00 13.37 ? 24  SER A OG  1 
ATOM   193  N N   . CYS A 1 25  ? 2.007   11.194  13.395 1.00 13.04 ? 25  CYS A N   1 
ATOM   194  C CA  . CYS A 1 25  ? 3.226   10.444  13.711 1.00 14.22 ? 25  CYS A CA  1 
ATOM   195  C C   . CYS A 1 25  ? 2.935   8.974   14.021 1.00 12.98 ? 25  CYS A C   1 
ATOM   196  O O   . CYS A 1 25  ? 3.702   8.086   13.629 1.00 14.55 ? 25  CYS A O   1 
ATOM   197  C CB  . CYS A 1 25  ? 3.949   11.098  14.891 1.00 16.88 ? 25  CYS A CB  1 
ATOM   198  S SG  . CYS A 1 25  ? 2.936   11.238  16.386 1.00 22.89 ? 25  CYS A SG  1 
ATOM   199  N N   . TRP A 1 26  ? 1.818   8.702   14.708 1.00 11.65 ? 26  TRP A N   1 
ATOM   200  C CA  . TRP A 1 26  ? 1.466   7.331   15.064 1.00 13.93 ? 26  TRP A CA  1 
ATOM   201  C C   . TRP A 1 26  ? 1.342   6.455   13.823 1.00 11.79 ? 26  TRP A C   1 
ATOM   202  O O   . TRP A 1 26  ? 1.738   5.281   13.839 1.00 13.93 ? 26  TRP A O   1 
ATOM   203  C CB  . TRP A 1 26  ? 0.171   7.338   15.887 1.00 11.75 ? 26  TRP A CB  1 
ATOM   204  C CG  . TRP A 1 26  ? -0.967  8.031   15.195 1.00 13.18 ? 26  TRP A CG  1 
ATOM   205  C CD1 . TRP A 1 26  ? -1.242  9.371   15.192 1.00 14.41 ? 26  TRP A CD1 1 
ATOM   206  C CD2 . TRP A 1 26  ? -1.979  7.410   14.409 1.00 12.44 ? 26  TRP A CD2 1 
ATOM   207  N NE1 . TRP A 1 26  ? -2.375  9.621   14.445 1.00 14.52 ? 26  TRP A NE1 1 
ATOM   208  C CE2 . TRP A 1 26  ? -2.838  8.434   13.943 1.00 12.33 ? 26  TRP A CE2 1 
ATOM   209  C CE3 . TRP A 1 26  ? -2.232  6.090   14.032 1.00 13.55 ? 26  TRP A CE3 1 
ATOM   210  C CZ2 . TRP A 1 26  ? -3.947  8.170   13.146 1.00 15.35 ? 26  TRP A CZ2 1 
ATOM   211  C CZ3 . TRP A 1 26  ? -3.335  5.824   13.246 1.00 13.73 ? 26  TRP A CZ3 1 
ATOM   212  C CH2 . TRP A 1 26  ? -4.172  6.865   12.797 1.00 14.51 ? 26  TRP A CH2 1 
ATOM   213  N N   . ALA A 1 27  ? 0.797   7.016   12.731 1.00 13.52 ? 27  ALA A N   1 
ATOM   214  C CA  . ALA A 1 27  ? 0.663   6.273   11.483 1.00 12.67 ? 27  ALA A CA  1 
ATOM   215  C C   . ALA A 1 27  ? 2.001   6.108   10.768 1.00 10.39 ? 27  ALA A C   1 
ATOM   216  O O   . ALA A 1 27  ? 2.271   5.051   10.191 1.00 12.75 ? 27  ALA A O   1 
ATOM   217  C CB  . ALA A 1 27  ? -0.344  6.975   10.565 1.00 13.81 ? 27  ALA A CB  1 
ATOM   218  N N   . PHE A 1 28  ? 2.832   7.155   10.771 1.00 13.18 ? 28  PHE A N   1 
ATOM   219  C CA  . PHE A 1 28  ? 4.144   7.054   10.140 1.00 12.84 ? 28  PHE A CA  1 
ATOM   220  C C   . PHE A 1 28  ? 4.991   6.008   10.843 1.00 11.60 ? 28  PHE A C   1 
ATOM   221  O O   . PHE A 1 28  ? 5.611   5.156   10.196 1.00 11.10 ? 28  PHE A O   1 
ATOM   222  C CB  . PHE A 1 28  ? 4.819   8.431   10.147 1.00 13.14 ? 28  PHE A CB  1 
ATOM   223  C CG  . PHE A 1 28  ? 4.333   9.312   9.033  1.00 11.88 ? 28  PHE A CG  1 
ATOM   224  C CD1 . PHE A 1 28  ? 3.158   10.035  9.171  1.00 12.37 ? 28  PHE A CD1 1 
ATOM   225  C CD2 . PHE A 1 28  ? 5.018   9.379   7.837  1.00 13.44 ? 28  PHE A CD2 1 
ATOM   226  C CE1 . PHE A 1 28  ? 2.685   10.824  8.116  1.00 11.87 ? 28  PHE A CE1 1 
ATOM   227  C CE2 . PHE A 1 28  ? 4.543   10.168  6.786  1.00 14.26 ? 28  PHE A CE2 1 
ATOM   228  C CZ  . PHE A 1 28  ? 3.370   10.875  6.932  1.00 12.28 ? 28  PHE A CZ  1 
ATOM   229  N N   . SER A 1 29  ? 4.991   6.053   12.179 1.00 14.47 ? 29  SER A N   1 
ATOM   230  C CA  . SER A 1 29  ? 5.697   5.085   13.010 1.00 11.75 ? 29  SER A CA  1 
ATOM   231  C C   . SER A 1 29  ? 5.275   3.659   12.677 1.00 11.94 ? 29  SER A C   1 
ATOM   232  O O   . SER A 1 29  ? 6.114   2.788   12.424 1.00 13.35 ? 29  SER A O   1 
ATOM   233  C CB  . SER A 1 29  ? 5.414   5.429   14.479 1.00 12.22 ? 29  SER A CB  1 
ATOM   234  O OG  . SER A 1 29  ? 5.909   4.445   15.371 1.00 17.27 ? 29  SER A OG  1 
ATOM   235  N N   . ALA A 1 30  ? 3.958   3.402   12.669 1.00 11.61 ? 30  ALA A N   1 
ATOM   236  C CA  . ALA A 1 30  ? 3.479   2.060   12.340 1.00 13.73 ? 30  ALA A CA  1 
ATOM   237  C C   . ALA A 1 30  ? 3.946   1.621   10.957 1.00 12.43 ? 30  ALA A C   1 
ATOM   238  O O   . ALA A 1 30  ? 4.400   0.484   10.778 1.00 13.51 ? 30  ALA A O   1 
ATOM   239  C CB  . ALA A 1 30  ? 1.949   2.008   12.428 1.00 13.78 ? 30  ALA A CB  1 
ATOM   240  N N   . VAL A 1 31  ? 3.858   2.511   9.961  1.00 12.27 ? 31  VAL A N   1 
ATOM   241  C CA  . VAL A 1 31  ? 4.205   2.124   8.595  1.00 13.45 ? 31  VAL A CA  1 
ATOM   242  C C   . VAL A 1 31  ? 5.680   1.745   8.484  1.00 14.75 ? 31  VAL A C   1 
ATOM   243  O O   . VAL A 1 31  ? 6.027   0.794   7.775  1.00 12.67 ? 31  VAL A O   1 
ATOM   244  C CB  . VAL A 1 31  ? 3.818   3.238   7.601  1.00 11.60 ? 31  VAL A CB  1 
ATOM   245  C CG1 . VAL A 1 31  ? 4.564   3.072   6.297  1.00 11.65 ? 31  VAL A CG1 1 
ATOM   246  C CG2 . VAL A 1 31  ? 2.295   3.214   7.337  1.00 10.94 ? 31  VAL A CG2 1 
ATOM   247  N N   . VAL A 1 32  ? 6.575   2.454   9.188  1.00 11.53 ? 32  VAL A N   1 
ATOM   248  C CA  . VAL A 1 32  ? 7.978   2.042   9.145  1.00 13.29 ? 32  VAL A CA  1 
ATOM   249  C C   . VAL A 1 32  ? 8.112   0.574   9.530  1.00 12.39 ? 32  VAL A C   1 
ATOM   250  O O   . VAL A 1 32  ? 8.835   -0.192  8.880  1.00 13.22 ? 32  VAL A O   1 
ATOM   251  C CB  . VAL A 1 32  ? 8.840   2.934   10.056 1.00 9.91  ? 32  VAL A CB  1 
ATOM   252  C CG1 . VAL A 1 32  ? 10.280  2.443   10.058 1.00 11.48 ? 32  VAL A CG1 1 
ATOM   253  C CG2 . VAL A 1 32  ? 8.803   4.369   9.583  1.00 12.88 ? 32  VAL A CG2 1 
ATOM   254  N N   . THR A 1 33  ? 7.406   0.152   10.582 1.00 13.68 ? 33  THR A N   1 
ATOM   255  C CA  . THR A 1 33  ? 7.562   -1.225  11.029 1.00 12.84 ? 33  THR A CA  1 
ATOM   256  C C   . THR A 1 33  ? 6.943   -2.207  10.049 1.00 14.29 ? 33  THR A C   1 
ATOM   257  O O   . THR A 1 33  ? 7.446   -3.321  9.911  1.00 13.51 ? 33  THR A O   1 
ATOM   258  C CB  . THR A 1 33  ? 6.977   -1.418  12.429 1.00 15.10 ? 33  THR A CB  1 
ATOM   259  O OG1 . THR A 1 33  ? 5.542   -1.426  12.370 1.00 13.49 ? 33  THR A OG1 1 
ATOM   260  C CG2 . THR A 1 33  ? 7.457   -0.330  13.389 1.00 12.11 ? 33  THR A CG2 1 
ATOM   261  N N   . ILE A 1 34  ? 5.874   -1.815  9.350  1.00 12.73 ? 34  ILE A N   1 
ATOM   262  C CA  . ILE A 1 34  ? 5.303   -2.691  8.331  1.00 15.20 ? 34  ILE A CA  1 
ATOM   263  C C   . ILE A 1 34  ? 6.263   -2.836  7.161  1.00 14.51 ? 34  ILE A C   1 
ATOM   264  O O   . ILE A 1 34  ? 6.556   -3.949  6.703  1.00 16.58 ? 34  ILE A O   1 
ATOM   265  C CB  . ILE A 1 34  ? 3.945   -2.147  7.860  1.00 13.72 ? 34  ILE A CB  1 
ATOM   266  C CG1 . ILE A 1 34  ? 2.907   -2.137  8.985  1.00 17.25 ? 34  ILE A CG1 1 
ATOM   267  C CG2 . ILE A 1 34  ? 3.454   -2.999  6.692  1.00 15.92 ? 34  ILE A CG2 1 
ATOM   268  C CD1 . ILE A 1 34  ? 2.811   -3.420  9.739  1.00 20.46 ? 34  ILE A CD1 1 
ATOM   269  N N   . GLU A 1 35  ? 6.770   -1.711  6.652  1.00 13.51 ? 35  GLU A N   1 
ATOM   270  C CA  . GLU A 1 35  ? 7.727   -1.769  5.554  1.00 13.32 ? 35  GLU A CA  1 
ATOM   271  C C   . GLU A 1 35  ? 8.901   -2.671  5.910  1.00 15.80 ? 35  GLU A C   1 
ATOM   272  O O   . GLU A 1 35  ? 9.361   -3.462  5.078  1.00 17.09 ? 35  GLU A O   1 
ATOM   273  C CB  . GLU A 1 35  ? 8.199   -0.351  5.204  1.00 14.14 ? 35  GLU A CB  1 
ATOM   274  C CG  . GLU A 1 35  ? 7.037   0.521   4.698  1.00 15.15 ? 35  GLU A CG  1 
ATOM   275  C CD  . GLU A 1 35  ? 7.345   2.002   4.538  1.00 14.56 ? 35  GLU A CD  1 
ATOM   276  O OE1 . GLU A 1 35  ? 8.328   2.515   5.133  1.00 14.42 ? 35  GLU A OE1 1 
ATOM   277  O OE2 . GLU A 1 35  ? 6.557   2.673   3.819  1.00 14.86 ? 35  GLU A OE2 1 
ATOM   278  N N   . GLY A 1 36  ? 9.357   -2.598  7.165  1.00 12.89 ? 36  GLY A N   1 
ATOM   279  C CA  . GLY A 1 36  ? 10.483  -3.417  7.596  1.00 14.96 ? 36  GLY A CA  1 
ATOM   280  C C   . GLY A 1 36  ? 10.170  -4.903  7.652  1.00 15.30 ? 36  GLY A C   1 
ATOM   281  O O   . GLY A 1 36  ? 10.911  -5.717  7.101  1.00 16.98 ? 36  GLY A O   1 
ATOM   282  N N   . ILE A 1 37  ? 9.069   -5.277  8.310  1.00 14.24 ? 37  ILE A N   1 
ATOM   283  C CA  . ILE A 1 37  ? 8.795   -6.705  8.480  1.00 14.22 ? 37  ILE A CA  1 
ATOM   284  C C   . ILE A 1 37  ? 8.478   -7.357  7.137  1.00 18.23 ? 37  ILE A C   1 
ATOM   285  O O   . ILE A 1 37  ? 8.842   -8.514  6.918  1.00 18.42 ? 37  ILE A O   1 
ATOM   286  C CB  . ILE A 1 37  ? 7.685   -6.946  9.524  1.00 15.84 ? 37  ILE A CB  1 
ATOM   287  C CG1 . ILE A 1 37  ? 7.680   -8.419  9.979  1.00 19.37 ? 37  ILE A CG1 1 
ATOM   288  C CG2 . ILE A 1 37  ? 6.327   -6.560  8.979  1.00 15.69 ? 37  ILE A CG2 1 
ATOM   289  C CD1 . ILE A 1 37  ? 8.978   -8.882  10.595 1.00 25.01 ? 37  ILE A CD1 1 
ATOM   290  N N   . ILE A 1 38  ? 7.849   -6.630  6.204  1.00 17.22 ? 38  ILE A N   1 
ATOM   291  C CA  . ILE A 1 38  ? 7.558   -7.210  4.893  1.00 17.07 ? 38  ILE A CA  1 
ATOM   292  C C   . ILE A 1 38  ? 8.850   -7.456  4.121  1.00 20.67 ? 38  ILE A C   1 
ATOM   293  O O   . ILE A 1 38  ? 8.992   -8.470  3.428  1.00 21.01 ? 38  ILE A O   1 
ATOM   294  C CB  . ILE A 1 38  ? 6.577   -6.315  4.104  1.00 16.32 ? 38  ILE A CB  1 
ATOM   295  C CG1 . ILE A 1 38  ? 5.222   -6.276  4.795  1.00 17.08 ? 38  ILE A CG1 1 
ATOM   296  C CG2 . ILE A 1 38  ? 6.435   -6.796  2.643  1.00 18.33 ? 38  ILE A CG2 1 
ATOM   297  C CD1 . ILE A 1 38  ? 4.624   -7.650  5.006  1.00 20.07 ? 38  ILE A CD1 1 
ATOM   298  N N   . LYS A 1 39  ? 9.820   -6.546  4.228  1.00 17.99 ? 39  LYS A N   1 
ATOM   299  C CA  . LYS A 1 39  ? 11.113  -6.805  3.602  1.00 15.11 ? 39  LYS A CA  1 
ATOM   300  C C   . LYS A 1 39  ? 11.799  -7.990  4.257  1.00 20.49 ? 39  LYS A C   1 
ATOM   301  O O   . LYS A 1 39  ? 12.335  -8.868  3.572  1.00 21.11 ? 39  LYS A O   1 
ATOM   302  C CB  . LYS A 1 39  ? 12.006  -5.564  3.680  1.00 16.19 ? 39  LYS A CB  1 
ATOM   303  C CG  . LYS A 1 39  ? 13.484  -5.820  3.372  1.00 19.05 ? 39  LYS A CG  1 
ATOM   304  C CD  . LYS A 1 39  ? 13.699  -6.250  1.934  1.00 21.07 ? 39  LYS A CD  1 
ATOM   305  C CE  . LYS A 1 39  ? 15.188  -6.329  1.603  1.00 19.90 ? 39  LYS A CE  1 
ATOM   306  N NZ  . LYS A 1 39  ? 15.372  -6.472  0.127  1.00 29.59 ? 39  LYS A NZ  1 
ATOM   307  N N   . ILE A 1 40  ? 11.783  -8.031  5.587  1.00 21.84 ? 40  ILE A N   1 
ATOM   308  C CA  . ILE A 1 40  ? 12.415  -9.127  6.316  1.00 19.28 ? 40  ILE A CA  1 
ATOM   309  C C   . ILE A 1 40  ? 11.801  -10.470 5.927  1.00 23.85 ? 40  ILE A C   1 
ATOM   310  O O   . ILE A 1 40  ? 12.521  -11.455 5.715  1.00 25.05 ? 40  ILE A O   1 
ATOM   311  C CB  . ILE A 1 40  ? 12.316  -8.866  7.828  1.00 21.57 ? 40  ILE A CB  1 
ATOM   312  C CG1 . ILE A 1 40  ? 13.280  -7.748  8.218  1.00 18.41 ? 40  ILE A CG1 1 
ATOM   313  C CG2 . ILE A 1 40  ? 12.615  -10.136 8.618  1.00 21.90 ? 40  ILE A CG2 1 
ATOM   314  C CD1 . ILE A 1 40  ? 13.004  -7.141  9.579  1.00 17.55 ? 40  ILE A CD1 1 
ATOM   315  N N   . ARG A 1 41  ? 10.469  -10.536 5.806  1.00 19.87 ? 41  ARG A N   1 
ATOM   316  C CA  . ARG A 1 41  ? 9.822   -11.821 5.566  1.00 23.25 ? 41  ARG A CA  1 
ATOM   317  C C   . ARG A 1 41  ? 9.709   -12.202 4.095  1.00 28.54 ? 41  ARG A C   1 
ATOM   318  O O   . ARG A 1 41  ? 9.641   -13.400 3.791  1.00 27.51 ? 41  ARG A O   1 
ATOM   319  C CB  . ARG A 1 41  ? 8.433   -11.840 6.202  1.00 24.81 ? 41  ARG A CB  1 
ATOM   320  C CG  . ARG A 1 41  ? 8.502   -11.757 7.704  1.00 30.21 ? 41  ARG A CG  1 
ATOM   321  C CD  . ARG A 1 41  ? 8.678   -13.140 8.316  1.00 30.66 ? 41  ARG A CD  1 
ATOM   322  N NE  . ARG A 1 41  ? 8.782   -13.045 9.763  1.00 36.18 ? 41  ARG A NE  1 
ATOM   323  C CZ  . ARG A 1 41  ? 9.928   -12.895 10.411 1.00 33.30 ? 41  ARG A CZ  1 
ATOM   324  N NH1 . ARG A 1 41  ? 11.086  -12.920 9.773  1.00 41.05 ? 41  ARG A NH1 1 
ATOM   325  N NH2 . ARG A 1 41  ? 9.911   -12.717 11.728 1.00 35.46 ? 41  ARG A NH2 1 
ATOM   326  N N   . THR A 1 42  ? 9.701   -11.232 3.177  1.00 26.00 ? 42  THR A N   1 
ATOM   327  C CA  . THR A 1 42  ? 9.432   -11.498 1.772  1.00 25.51 ? 42  THR A CA  1 
ATOM   328  C C   . THR A 1 42  ? 10.557  -11.103 0.828  1.00 29.43 ? 42  THR A C   1 
ATOM   329  O O   . THR A 1 42  ? 10.501  -11.469 -0.352 1.00 32.01 ? 42  THR A O   1 
ATOM   330  C CB  . THR A 1 42  ? 8.161   -10.767 1.312  1.00 28.45 ? 42  THR A CB  1 
ATOM   331  O OG1 . THR A 1 42  ? 8.486   -9.397  1.018  1.00 27.15 ? 42  THR A OG1 1 
ATOM   332  C CG2 . THR A 1 42  ? 7.066   -10.842 2.374  1.00 24.68 ? 42  THR A CG2 1 
ATOM   333  N N   . GLY A 1 43  ? 11.546  -10.349 1.287  1.00 22.24 ? 43  GLY A N   1 
ATOM   334  C CA  . GLY A 1 43  ? 12.625  -9.916  0.433  1.00 24.61 ? 43  GLY A CA  1 
ATOM   335  C C   . GLY A 1 43  ? 12.360  -8.655  -0.357 1.00 18.82 ? 43  GLY A C   1 
ATOM   336  O O   . GLY A 1 43  ? 13.267  -8.181  -1.054 1.00 24.43 ? 43  GLY A O   1 
ATOM   337  N N   . ASN A 1 44  ? 11.166  -8.075  -0.243 1.00 22.96 ? 44  ASN A N   1 
ATOM   338  C CA  . ASN A 1 44  ? 10.758  -6.938  -1.055 1.00 21.70 ? 44  ASN A CA  1 
ATOM   339  C C   . ASN A 1 44  ? 10.514  -5.732  -0.157 1.00 18.25 ? 44  ASN A C   1 
ATOM   340  O O   . ASN A 1 44  ? 9.773   -5.835  0.819  1.00 18.60 ? 44  ASN A O   1 
ATOM   341  C CB  . ASN A 1 44  ? 9.488   -7.275  -1.833 1.00 24.74 ? 44  ASN A CB  1 
ATOM   342  C CG  . ASN A 1 44  ? 9.721   -8.339  -2.893 1.00 31.84 ? 44  ASN A CG  1 
ATOM   343  O OD1 . ASN A 1 44  ? 10.823  -8.480  -3.424 1.00 30.58 ? 44  ASN A OD1 1 
ATOM   344  N ND2 . ASN A 1 44  ? 8.689   -9.120  -3.170 1.00 40.99 ? 44  ASN A ND2 1 
ATOM   345  N N   . LEU A 1 45  ? 11.121  -4.599  -0.507 1.00 20.06 ? 45  LEU A N   1 
ATOM   346  C CA  . LEU A 1 45  ? 10.905  -3.324  0.171  1.00 17.09 ? 45  LEU A CA  1 
ATOM   347  C C   . LEU A 1 45  ? 9.869   -2.493  -0.586 1.00 18.36 ? 45  LEU A C   1 
ATOM   348  O O   . LEU A 1 45  ? 10.104  -2.096  -1.736 1.00 19.75 ? 45  LEU A O   1 
ATOM   349  C CB  . LEU A 1 45  ? 12.211  -2.536  0.278  1.00 17.52 ? 45  LEU A CB  1 
ATOM   350  C CG  . LEU A 1 45  ? 12.107  -1.223  1.055  1.00 18.51 ? 45  LEU A CG  1 
ATOM   351  C CD1 . LEU A 1 45  ? 11.676  -1.491  2.504  1.00 17.14 ? 45  LEU A CD1 1 
ATOM   352  C CD2 . LEU A 1 45  ? 13.406  -0.393  0.984  1.00 18.64 ? 45  LEU A CD2 1 
ATOM   353  N N   . ASN A 1 46  ? 8.755   -2.196  0.074  1.00 15.76 ? 46  ASN A N   1 
ATOM   354  C CA  . ASN A 1 46  ? 7.681   -1.388  -0.489 1.00 16.55 ? 46  ASN A CA  1 
ATOM   355  C C   . ASN A 1 46  ? 7.326   -0.277  0.487  1.00 17.22 ? 46  ASN A C   1 
ATOM   356  O O   . ASN A 1 46  ? 7.560   -0.396  1.692  1.00 18.90 ? 46  ASN A O   1 
ATOM   357  C CB  . ASN A 1 46  ? 6.421   -2.228  -0.765 1.00 20.37 ? 46  ASN A CB  1 
ATOM   358  C CG  . ASN A 1 46  ? 6.727   -3.508  -1.509 1.00 23.82 ? 46  ASN A CG  1 
ATOM   359  O OD1 . ASN A 1 46  ? 6.578   -4.609  -0.969 1.00 27.02 ? 46  ASN A OD1 1 
ATOM   360  N ND2 . ASN A 1 46  ? 7.151   -3.371  -2.755 1.00 19.72 ? 46  ASN A ND2 1 
ATOM   361  N N   . GLU A 1 47  ? 6.735   0.798   -0.041 1.00 14.99 ? 47  GLU A N   1 
ATOM   362  C CA  . GLU A 1 47  ? 6.146   1.843   0.791  1.00 13.12 ? 47  GLU A CA  1 
ATOM   363  C C   . GLU A 1 47  ? 4.661   1.577   0.984  1.00 12.71 ? 47  GLU A C   1 
ATOM   364  O O   . GLU A 1 47  ? 3.947   1.294   0.014  1.00 16.45 ? 47  GLU A O   1 
ATOM   365  C CB  . GLU A 1 47  ? 6.339   3.223   0.173  1.00 13.59 ? 47  GLU A CB  1 
ATOM   366  C CG  . GLU A 1 47  ? 7.756   3.726   0.387  1.00 14.78 ? 47  GLU A CG  1 
ATOM   367  C CD  . GLU A 1 47  ? 8.059   5.033   -0.306 1.00 16.22 ? 47  GLU A CD  1 
ATOM   368  O OE1 . GLU A 1 47  ? 7.378   5.386   -1.290 1.00 21.28 ? 47  GLU A OE1 1 
ATOM   369  O OE2 . GLU A 1 47  ? 8.947   5.747   0.184  1.00 19.10 ? 47  GLU A OE2 1 
ATOM   370  N N   . TYR A 1 48  ? 4.198   1.677   2.227  1.00 12.70 ? 48  TYR A N   1 
ATOM   371  C CA  . TYR A 1 48  ? 2.791   1.468   2.552  1.00 11.66 ? 48  TYR A CA  1 
ATOM   372  C C   . TYR A 1 48  ? 2.159   2.773   3.034  1.00 12.20 ? 48  TYR A C   1 
ATOM   373  O O   . TYR A 1 48  ? 2.825   3.782   3.257  1.00 13.60 ? 48  TYR A O   1 
ATOM   374  C CB  . TYR A 1 48  ? 2.645   0.328   3.573  1.00 14.47 ? 48  TYR A CB  1 
ATOM   375  C CG  . TYR A 1 48  ? 3.092   -0.990  2.973  1.00 14.34 ? 48  TYR A CG  1 
ATOM   376  C CD1 . TYR A 1 48  ? 2.318   -1.635  2.008  1.00 14.12 ? 48  TYR A CD1 1 
ATOM   377  C CD2 . TYR A 1 48  ? 4.330   -1.549  3.303  1.00 17.40 ? 48  TYR A CD2 1 
ATOM   378  C CE1 . TYR A 1 48  ? 2.745   -2.810  1.417  1.00 15.88 ? 48  TYR A CE1 1 
ATOM   379  C CE2 . TYR A 1 48  ? 4.765   -2.724  2.712  1.00 18.21 ? 48  TYR A CE2 1 
ATOM   380  C CZ  . TYR A 1 48  ? 3.966   -3.354  1.779  1.00 17.74 ? 48  TYR A CZ  1 
ATOM   381  O OH  . TYR A 1 48  ? 4.404   -4.523  1.192  1.00 19.85 ? 48  TYR A OH  1 
ATOM   382  N N   . SER A 1 49  ? 0.833   2.751   3.165  1.00 13.24 ? 49  SER A N   1 
ATOM   383  C CA  . SER A 1 49  ? 0.050   3.983   3.251  1.00 13.03 ? 49  SER A CA  1 
ATOM   384  C C   . SER A 1 49  ? -0.160  4.443   4.696  1.00 13.11 ? 49  SER A C   1 
ATOM   385  O O   . SER A 1 49  ? -0.980  3.874   5.431  1.00 14.26 ? 49  SER A O   1 
ATOM   386  C CB  . SER A 1 49  ? -1.302  3.790   2.573  1.00 11.40 ? 49  SER A CB  1 
ATOM   387  O OG  . SER A 1 49  ? -2.041  4.992   2.730  1.00 13.34 ? 49  SER A OG  1 
ATOM   388  N N   . GLU A 1 50  ? 0.513   5.535   5.069  1.00 12.37 ? 50  GLU A N   1 
ATOM   389  C CA  . GLU A 1 50  ? 0.178   6.240   6.303  1.00 12.39 ? 50  GLU A CA  1 
ATOM   390  C C   . GLU A 1 50  ? -1.230  6.820   6.237  1.00 13.59 ? 50  GLU A C   1 
ATOM   391  O O   . GLU A 1 50  ? -1.953  6.842   7.243  1.00 13.26 ? 50  GLU A O   1 
ATOM   392  C CB  . GLU A 1 50  ? 1.178   7.373   6.564  1.00 13.09 ? 50  GLU A CB  1 
ATOM   393  C CG  . GLU A 1 50  ? 2.620   6.934   6.745  1.00 12.43 ? 50  GLU A CG  1 
ATOM   394  C CD  . GLU A 1 50  ? 3.380   6.945   5.442  1.00 15.68 ? 50  GLU A CD  1 
ATOM   395  O OE1 . GLU A 1 50  ? 2.772   7.237   4.384  1.00 13.87 ? 50  GLU A OE1 1 
ATOM   396  O OE2 . GLU A 1 50  ? 4.589   6.643   5.474  1.00 14.83 ? 50  GLU A OE2 1 
ATOM   397  N N   . GLN A 1 51  ? -1.626  7.319   5.063  1.00 12.52 ? 51  GLN A N   1 
ATOM   398  C CA  . GLN A 1 51  ? -2.928  7.964   4.926  1.00 13.67 ? 51  GLN A CA  1 
ATOM   399  C C   . GLN A 1 51  ? -4.053  6.991   5.241  1.00 14.03 ? 51  GLN A C   1 
ATOM   400  O O   . GLN A 1 51  ? -5.062  7.366   5.863  1.00 12.26 ? 51  GLN A O   1 
ATOM   401  C CB  . GLN A 1 51  ? -3.088  8.527   3.508  1.00 13.75 ? 51  GLN A CB  1 
ATOM   402  C CG  . GLN A 1 51  ? -4.399  9.295   3.285  1.00 13.42 ? 51  GLN A CG  1 
ATOM   403  C CD  . GLN A 1 51  ? -4.389  10.647  3.964  1.00 14.47 ? 51  GLN A CD  1 
ATOM   404  O OE1 . GLN A 1 51  ? -3.350  11.316  4.033  1.00 14.02 ? 51  GLN A OE1 1 
ATOM   405  N NE2 . GLN A 1 51  ? -5.528  11.045  4.507  1.00 15.40 ? 51  GLN A NE2 1 
ATOM   406  N N   . GLU A 1 52  ? -3.890  5.733   4.826  1.00 13.19 ? 52  GLU A N   1 
ATOM   407  C CA  . GLU A 1 52  ? -4.908  4.721   5.086  1.00 13.08 ? 52  GLU A CA  1 
ATOM   408  C C   . GLU A 1 52  ? -5.111  4.515   6.580  1.00 13.44 ? 52  GLU A C   1 
ATOM   409  O O   . GLU A 1 52  ? -6.247  4.439   7.050  1.00 14.86 ? 52  GLU A O   1 
ATOM   410  C CB  . GLU A 1 52  ? -4.508  3.417   4.416  1.00 13.80 ? 52  GLU A CB  1 
ATOM   411  C CG  . GLU A 1 52  ? -5.550  2.324   4.529  1.00 14.35 ? 52  GLU A CG  1 
ATOM   412  C CD  . GLU A 1 52  ? -5.275  1.214   3.527  1.00 19.55 ? 52  GLU A CD  1 
ATOM   413  O OE1 . GLU A 1 52  ? -4.096  0.983   3.199  1.00 21.52 ? 52  GLU A OE1 1 
ATOM   414  O OE2 . GLU A 1 52  ? -6.224  0.618   3.002  1.00 28.11 ? 52  GLU A OE2 1 
ATOM   415  N N   . LEU A 1 53  ? -4.026  4.442   7.348  1.00 14.55 ? 53  LEU A N   1 
ATOM   416  C CA  . LEU A 1 53  ? -4.163  4.324   8.798  1.00 12.86 ? 53  LEU A CA  1 
ATOM   417  C C   . LEU A 1 53  ? -4.786  5.580   9.398  1.00 12.88 ? 53  LEU A C   1 
ATOM   418  O O   . LEU A 1 53  ? -5.697  5.499   10.236 1.00 13.88 ? 53  LEU A O   1 
ATOM   419  C CB  . LEU A 1 53  ? -2.799  4.041   9.423  1.00 12.75 ? 53  LEU A CB  1 
ATOM   420  C CG  . LEU A 1 53  ? -2.077  2.832   8.831  1.00 12.97 ? 53  LEU A CG  1 
ATOM   421  C CD1 . LEU A 1 53  ? -0.725  2.664   9.547  1.00 12.53 ? 53  LEU A CD1 1 
ATOM   422  C CD2 . LEU A 1 53  ? -2.880  1.538   8.894  1.00 17.42 ? 53  LEU A CD2 1 
ATOM   423  N N   . LEU A 1 54  ? -4.310  6.752   8.974  1.00 11.49 ? 54  LEU A N   1 
ATOM   424  C CA  . LEU A 1 54  ? -4.898  8.031   9.360  1.00 14.02 ? 54  LEU A CA  1 
ATOM   425  C C   . LEU A 1 54  ? -6.413  8.040   9.204  1.00 14.34 ? 54  LEU A C   1 
ATOM   426  O O   . LEU A 1 54  ? -7.142  8.432   10.120 1.00 13.99 ? 54  LEU A O   1 
ATOM   427  C CB  . LEU A 1 54  ? -4.310  9.148   8.495  1.00 14.71 ? 54  LEU A CB  1 
ATOM   428  C CG  . LEU A 1 54  ? -4.519  10.590  8.959  1.00 15.57 ? 54  LEU A CG  1 
ATOM   429  C CD1 . LEU A 1 54  ? -4.112  10.799  10.406 1.00 19.58 ? 54  LEU A CD1 1 
ATOM   430  C CD2 . LEU A 1 54  ? -3.862  11.582  8.033  1.00 15.33 ? 54  LEU A CD2 1 
ATOM   431  N N   . ASP A 1 55  ? -6.891  7.627   8.030  1.00 12.06 ? 55  ASP A N   1 
ATOM   432  C CA  . ASP A 1 55  ? -8.314  7.689   7.705  1.00 13.25 ? 55  ASP A CA  1 
ATOM   433  C C   . ASP A 1 55  ? -9.101  6.581   8.392  1.00 14.83 ? 55  ASP A C   1 
ATOM   434  O O   . ASP A 1 55  ? -10.265 6.780   8.763  1.00 16.03 ? 55  ASP A O   1 
ATOM   435  C CB  . ASP A 1 55  ? -8.506  7.552   6.197  1.00 14.40 ? 55  ASP A CB  1 
ATOM   436  C CG  . ASP A 1 55  ? -7.994  8.744   5.404  1.00 13.54 ? 55  ASP A CG  1 
ATOM   437  O OD1 . ASP A 1 55  ? -7.725  9.816   5.976  1.00 15.47 ? 55  ASP A OD1 1 
ATOM   438  O OD2 . ASP A 1 55  ? -7.843  8.554   4.179  1.00 14.66 ? 55  ASP A OD2 1 
ATOM   439  N N   . CYS A 1 56  ? -8.504  5.395   8.519  1.00 13.67 ? 56  CYS A N   1 
ATOM   440  C CA  . CYS A 1 56  ? -9.267  4.185   8.789  1.00 11.83 ? 56  CYS A CA  1 
ATOM   441  C C   . CYS A 1 56  ? -9.147  3.648   10.207 1.00 14.91 ? 56  CYS A C   1 
ATOM   442  O O   . CYS A 1 56  ? -9.964  2.801   10.592 1.00 15.10 ? 56  CYS A O   1 
ATOM   443  C CB  . CYS A 1 56  ? -8.872  3.073   7.813  1.00 14.36 ? 56  CYS A CB  1 
ATOM   444  S SG  . CYS A 1 56  ? -9.111  3.548   6.063  1.00 14.87 ? 56  CYS A SG  1 
ATOM   445  N N   . ASP A 1 57  ? -8.153  4.071   10.985 1.00 15.18 ? 57  ASP A N   1 
ATOM   446  C CA  . ASP A 1 57  ? -8.047  3.574   12.358 1.00 13.28 ? 57  ASP A CA  1 
ATOM   447  C C   . ASP A 1 57  ? -9.041  4.323   13.233 1.00 16.15 ? 57  ASP A C   1 
ATOM   448  O O   . ASP A 1 57  ? -8.792  5.449   13.673 1.00 15.24 ? 57  ASP A O   1 
ATOM   449  C CB  . ASP A 1 57  ? -6.621  3.708   12.872 1.00 14.72 ? 57  ASP A CB  1 
ATOM   450  C CG  . ASP A 1 57  ? -6.487  3.264   14.320 1.00 18.29 ? 57  ASP A CG  1 
ATOM   451  O OD1 . ASP A 1 57  ? -7.444  2.676   14.865 1.00 18.30 ? 57  ASP A OD1 1 
ATOM   452  O OD2 . ASP A 1 57  ? -5.430  3.539   14.924 1.00 15.25 ? 57  ASP A OD2 1 
ATOM   453  N N   . ARG A 1 58  ? -10.181 3.674   13.493 1.00 15.02 ? 58  ARG A N   1 
ATOM   454  C CA  . ARG A 1 58  ? -11.256 4.290   14.252 1.00 14.63 ? 58  ARG A CA  1 
ATOM   455  C C   . ARG A 1 58  ? -10.905 4.519   15.719 1.00 18.08 ? 58  ARG A C   1 
ATOM   456  O O   . ARG A 1 58  ? -11.575 5.326   16.372 1.00 18.84 ? 58  ARG A O   1 
ATOM   457  C CB  . ARG A 1 58  ? -12.527 3.441   14.128 1.00 14.11 ? 58  ARG A CB  1 
ATOM   458  C CG  . ARG A 1 58  ? -13.204 3.560   12.765 1.00 17.52 ? 58  ARG A CG  1 
ATOM   459  C CD  . ARG A 1 58  ? -14.335 2.548   12.541 1.00 14.50 ? 58  ARG A CD  1 
ATOM   460  N NE  . ARG A 1 58  ? -13.841 1.179   12.452 1.00 15.57 ? 58  ARG A NE  1 
ATOM   461  C CZ  . ARG A 1 58  ? -14.596 0.126   12.172 1.00 14.85 ? 58  ARG A CZ  1 
ATOM   462  N NH1 . ARG A 1 58  ? -15.889 0.255   11.897 1.00 17.72 ? 58  ARG A NH1 1 
ATOM   463  N NH2 . ARG A 1 58  ? -14.039 -1.086  12.152 1.00 18.20 ? 58  ARG A NH2 1 
ATOM   464  N N   . ARG A 1 59  ? -9.874  3.848   16.250 1.00 16.83 ? 59  ARG A N   1 
ATOM   465  C CA  . ARG A 1 59  ? -9.469  4.087   17.633 1.00 16.62 ? 59  ARG A CA  1 
ATOM   466  C C   . ARG A 1 59  ? -8.602  5.331   17.771 1.00 18.76 ? 59  ARG A C   1 
ATOM   467  O O   . ARG A 1 59  ? -8.477  5.869   18.876 1.00 24.71 ? 59  ARG A O   1 
ATOM   468  C CB  . ARG A 1 59  ? -8.713  2.881   18.187 1.00 18.79 ? 59  ARG A CB  1 
ATOM   469  C CG  . ARG A 1 59  ? -9.576  1.646   18.367 1.00 29.86 ? 59  ARG A CG  1 
ATOM   470  C CD  . ARG A 1 59  ? -8.823  0.508   19.040 1.00 32.68 ? 59  ARG A CD  1 
ATOM   471  N NE  . ARG A 1 59  ? -9.340  -0.782  18.597 1.00 32.76 ? 59  ARG A NE  1 
ATOM   472  C CZ  . ARG A 1 59  ? -9.903  -1.680  19.394 1.00 39.48 ? 59  ARG A CZ  1 
ATOM   473  N NH1 . ARG A 1 59  ? -10.046 -1.460  20.693 1.00 35.55 ? 59  ARG A NH1 1 
ATOM   474  N NH2 . ARG A 1 59  ? -10.353 -2.820  18.870 1.00 33.31 ? 59  ARG A NH2 1 
ATOM   475  N N   . SER A 1 60  ? -7.994  5.793   16.681 1.00 13.98 ? 60  SER A N   1 
ATOM   476  C CA  . SER A 1 60  ? -7.176  6.988   16.713 1.00 14.31 ? 60  SER A CA  1 
ATOM   477  C C   . SER A 1 60  ? -8.003  8.211   16.329 1.00 16.60 ? 60  SER A C   1 
ATOM   478  O O   . SER A 1 60  ? -9.191  8.114   16.011 1.00 16.71 ? 60  SER A O   1 
ATOM   479  C CB  . SER A 1 60  ? -5.974  6.826   15.784 1.00 14.83 ? 60  SER A CB  1 
ATOM   480  O OG  . SER A 1 60  ? -5.045  5.891   16.303 1.00 13.80 ? 60  SER A OG  1 
ATOM   481  N N   . TYR A 1 61  ? -7.351  9.383   16.324 1.00 17.44 ? 61  TYR A N   1 
ATOM   482  C CA  . TYR A 1 61  ? -8.026  10.671  16.200 1.00 18.55 ? 61  TYR A CA  1 
ATOM   483  C C   . TYR A 1 61  ? -7.504  11.476  15.013 1.00 17.42 ? 61  TYR A C   1 
ATOM   484  O O   . TYR A 1 61  ? -7.464  12.707  15.060 1.00 17.41 ? 61  TYR A O   1 
ATOM   485  C CB  . TYR A 1 61  ? -7.859  11.464  17.494 1.00 18.69 ? 61  TYR A CB  1 
ATOM   486  C CG  . TYR A 1 61  ? -8.529  10.796  18.669 1.00 25.83 ? 61  TYR A CG  1 
ATOM   487  C CD1 . TYR A 1 61  ? -9.911  10.837  18.830 1.00 24.52 ? 61  TYR A CD1 1 
ATOM   488  C CD2 . TYR A 1 61  ? -7.782  10.064  19.585 1.00 25.61 ? 61  TYR A CD2 1 
ATOM   489  C CE1 . TYR A 1 61  ? -10.524 10.212  19.898 1.00 24.16 ? 61  TYR A CE1 1 
ATOM   490  C CE2 . TYR A 1 61  ? -8.392  9.426   20.657 1.00 29.22 ? 61  TYR A CE2 1 
ATOM   491  C CZ  . TYR A 1 61  ? -9.759  9.509   20.804 1.00 29.12 ? 61  TYR A CZ  1 
ATOM   492  O OH  . TYR A 1 61  ? -10.378 8.880   21.860 1.00 37.90 ? 61  TYR A OH  1 
ATOM   493  N N   . GLY A 1 62  ? -7.099  10.794  13.947 1.00 18.99 ? 62  GLY A N   1 
ATOM   494  C CA  . GLY A 1 62  ? -6.711  11.503  12.735 1.00 15.58 ? 62  GLY A CA  1 
ATOM   495  C C   . GLY A 1 62  ? -5.481  12.365  12.962 1.00 16.44 ? 62  GLY A C   1 
ATOM   496  O O   . GLY A 1 62  ? -4.473  11.925  13.529 1.00 17.18 ? 62  GLY A O   1 
ATOM   497  N N   . CYS A 1 63  ? -5.562  13.617  12.526 1.00 18.37 ? 63  CYS A N   1 
ATOM   498  C CA  . CYS A 1 63  ? -4.468  14.558  12.719 1.00 17.36 ? 63  CYS A CA  1 
ATOM   499  C C   . CYS A 1 63  ? -4.403  15.095  14.145 1.00 21.07 ? 63  CYS A C   1 
ATOM   500  O O   . CYS A 1 63  ? -3.508  15.891  14.453 1.00 19.80 ? 63  CYS A O   1 
ATOM   501  C CB  . CYS A 1 63  ? -4.596  15.720  11.725 1.00 18.22 ? 63  CYS A CB  1 
ATOM   502  S SG  . CYS A 1 63  ? -4.273  15.269  9.990  1.00 18.11 ? 63  CYS A SG  1 
ATOM   503  N N   . ASN A 1 64  ? -5.325  14.689  15.017 1.00 17.04 ? 64  ASN A N   1 
ATOM   504  C CA  . ASN A 1 64  ? -5.271  15.043  16.428 1.00 19.05 ? 64  ASN A CA  1 
ATOM   505  C C   . ASN A 1 64  ? -4.599  13.958  17.259 1.00 22.13 ? 64  ASN A C   1 
ATOM   506  O O   . ASN A 1 64  ? -4.712  13.967  18.489 1.00 24.27 ? 64  ASN A O   1 
ATOM   507  C CB  . ASN A 1 64  ? -6.679  15.324  16.968 1.00 20.32 ? 64  ASN A CB  1 
ATOM   508  C CG  . ASN A 1 64  ? -7.309  16.554  16.341 1.00 31.02 ? 64  ASN A CG  1 
ATOM   509  O OD1 . ASN A 1 64  ? -6.700  17.622  16.287 1.00 34.51 ? 64  ASN A OD1 1 
ATOM   510  N ND2 . ASN A 1 64  ? -8.539  16.405  15.861 1.00 33.81 ? 64  ASN A ND2 1 
ATOM   511  N N   . GLY A 1 65  ? -3.910  13.025  16.622 1.00 19.04 ? 65  GLY A N   1 
ATOM   512  C CA  . GLY A 1 65  ? -3.111  12.040  17.318 1.00 16.69 ? 65  GLY A CA  1 
ATOM   513  C C   . GLY A 1 65  ? -3.754  10.668  17.284 1.00 15.37 ? 65  GLY A C   1 
ATOM   514  O O   . GLY A 1 65  ? -4.892  10.487  16.853 1.00 16.12 ? 65  GLY A O   1 
ATOM   515  N N   . GLY A 1 66  ? -3.001  9.693   17.774 1.00 16.42 ? 66  GLY A N   1 
ATOM   516  C CA  . GLY A 1 66  ? -3.416  8.315   17.611 1.00 14.64 ? 66  GLY A CA  1 
ATOM   517  C C   . GLY A 1 66  ? -2.484  7.357   18.315 1.00 16.92 ? 66  GLY A C   1 
ATOM   518  O O   . GLY A 1 66  ? -1.613  7.755   19.100 1.00 17.78 ? 66  GLY A O   1 
ATOM   519  N N   . TYR A 1 67  ? -2.659  6.076   17.996 1.00 17.35 ? 67  TYR A N   1 
ATOM   520  C CA  . TYR A 1 67  ? -2.006  4.995   18.732 1.00 18.61 ? 67  TYR A CA  1 
ATOM   521  C C   . TYR A 1 67  ? -1.300  4.052   17.773 1.00 17.93 ? 67  TYR A C   1 
ATOM   522  O O   . TYR A 1 67  ? -1.967  3.383   16.962 1.00 15.36 ? 67  TYR A O   1 
ATOM   523  C CB  . TYR A 1 67  ? -3.013  4.221   19.585 1.00 17.31 ? 67  TYR A CB  1 
ATOM   524  C CG  . TYR A 1 67  ? -3.838  5.087   20.487 1.00 21.63 ? 67  TYR A CG  1 
ATOM   525  C CD1 . TYR A 1 67  ? -3.342  5.489   21.715 1.00 20.77 ? 67  TYR A CD1 1 
ATOM   526  C CD2 . TYR A 1 67  ? -5.118  5.489   20.126 1.00 19.52 ? 67  TYR A CD2 1 
ATOM   527  C CE1 . TYR A 1 67  ? -4.086  6.279   22.560 1.00 21.95 ? 67  TYR A CE1 1 
ATOM   528  C CE2 . TYR A 1 67  ? -5.872  6.286   20.967 1.00 23.73 ? 67  TYR A CE2 1 
ATOM   529  C CZ  . TYR A 1 67  ? -5.349  6.676   22.183 1.00 23.65 ? 67  TYR A CZ  1 
ATOM   530  O OH  . TYR A 1 67  ? -6.092  7.463   23.033 1.00 30.36 ? 67  TYR A OH  1 
ATOM   531  N N   . PRO A 1 68  ? 0.027   3.943   17.832 1.00 13.08 ? 68  PRO A N   1 
ATOM   532  C CA  . PRO A 1 68  ? 0.708   2.940   17.003 1.00 17.07 ? 68  PRO A CA  1 
ATOM   533  C C   . PRO A 1 68  ? 0.153   1.532   17.159 1.00 15.14 ? 68  PRO A C   1 
ATOM   534  O O   . PRO A 1 68  ? 0.072   0.796   16.169 1.00 17.06 ? 68  PRO A O   1 
ATOM   535  C CB  . PRO A 1 68  ? 2.161   3.046   17.484 1.00 17.79 ? 68  PRO A CB  1 
ATOM   536  C CG  . PRO A 1 68  ? 2.291   4.470   17.907 1.00 17.95 ? 68  PRO A CG  1 
ATOM   537  C CD  . PRO A 1 68  ? 0.974   4.809   18.556 1.00 16.47 ? 68  PRO A CD  1 
ATOM   538  N N   A TRP A 1 69  ? -0.219  1.123   18.369 0.50 15.82 ? 69  TRP A N   1 
ATOM   539  N N   B TRP A 1 69  ? -0.268  1.159   18.374 0.50 15.83 ? 69  TRP A N   1 
ATOM   540  C CA  A TRP A 1 69  ? -0.680  -0.250  18.540 0.50 16.93 ? 69  TRP A CA  1 
ATOM   541  C CA  B TRP A 1 69  ? -0.809  -0.178  18.603 0.50 17.08 ? 69  TRP A CA  1 
ATOM   542  C C   A TRP A 1 69  ? -2.016  -0.485  17.836 0.50 15.92 ? 69  TRP A C   1 
ATOM   543  C C   B TRP A 1 69  ? -2.056  -0.422  17.761 0.50 15.82 ? 69  TRP A C   1 
ATOM   544  O O   A TRP A 1 69  ? -2.230  -1.555  17.260 0.50 17.56 ? 69  TRP A O   1 
ATOM   545  O O   B TRP A 1 69  ? -2.167  -1.451  17.088 0.50 17.39 ? 69  TRP A O   1 
ATOM   546  C CB  A TRP A 1 69  ? -0.752  -0.601  20.030 0.50 17.54 ? 69  TRP A CB  1 
ATOM   547  C CB  B TRP A 1 69  ? -1.135  -0.386  20.089 0.50 17.36 ? 69  TRP A CB  1 
ATOM   548  C CG  A TRP A 1 69  ? -1.573  0.334   20.859 0.50 15.71 ? 69  TRP A CG  1 
ATOM   549  C CG  B TRP A 1 69  ? -2.010  -1.602  20.321 0.50 19.87 ? 69  TRP A CG  1 
ATOM   550  C CD1 A TRP A 1 69  ? -1.114  1.398   21.582 0.50 21.41 ? 69  TRP A CD1 1 
ATOM   551  C CD1 B TRP A 1 69  ? -1.601  -2.907  20.370 0.50 22.13 ? 69  TRP A CD1 1 
ATOM   552  C CD2 A TRP A 1 69  ? -2.990  0.288   21.067 0.50 19.84 ? 69  TRP A CD2 1 
ATOM   553  C CD2 B TRP A 1 69  ? -3.438  -1.626  20.489 0.50 16.71 ? 69  TRP A CD2 1 
ATOM   554  N NE1 A TRP A 1 69  ? -2.156  2.020   22.223 0.50 22.68 ? 69  TRP A NE1 1 
ATOM   555  N NE1 B TRP A 1 69  ? -2.677  -3.736  20.576 0.50 24.47 ? 69  TRP A NE1 1 
ATOM   556  C CE2 A TRP A 1 69  ? -3.319  1.361   21.922 0.50 18.19 ? 69  TRP A CE2 1 
ATOM   557  C CE2 B TRP A 1 69  ? -3.815  -2.977  20.653 0.50 23.11 ? 69  TRP A CE2 1 
ATOM   558  C CE3 A TRP A 1 69  ? -4.010  -0.554  20.617 0.50 21.96 ? 69  TRP A CE3 1 
ATOM   559  C CE3 B TRP A 1 69  ? -4.428  -0.641  20.531 0.50 21.32 ? 69  TRP A CE3 1 
ATOM   560  C CZ2 A TRP A 1 69  ? -4.625  1.615   22.330 0.50 21.16 ? 69  TRP A CZ2 1 
ATOM   561  C CZ2 B TRP A 1 69  ? -5.144  -3.363  20.850 0.50 25.52 ? 69  TRP A CZ2 1 
ATOM   562  C CZ3 A TRP A 1 69  ? -5.304  -0.300  21.024 0.50 23.83 ? 69  TRP A CZ3 1 
ATOM   563  C CZ3 B TRP A 1 69  ? -5.747  -1.029  20.730 0.50 24.82 ? 69  TRP A CZ3 1 
ATOM   564  C CH2 A TRP A 1 69  ? -5.602  0.776   21.872 0.50 24.54 ? 69  TRP A CH2 1 
ATOM   565  C CH2 B TRP A 1 69  ? -6.090  -2.376  20.886 0.50 27.31 ? 69  TRP A CH2 1 
ATOM   566  N N   A SER A 1 70  ? -2.912  0.504   17.847 0.50 15.33 ? 70  SER A N   1 
ATOM   567  N N   B SER A 1 70  ? -3.015  0.506   17.804 0.50 15.28 ? 70  SER A N   1 
ATOM   568  C CA  A SER A 1 70  ? -4.170  0.352   17.123 0.50 14.40 ? 70  SER A CA  1 
ATOM   569  C CA  B SER A 1 70  ? -4.254  0.294   17.065 0.50 14.46 ? 70  SER A CA  1 
ATOM   570  C C   A SER A 1 70  ? -3.946  0.319   15.616 0.50 16.29 ? 70  SER A C   1 
ATOM   571  C C   B SER A 1 70  ? -4.032  0.381   15.561 0.50 16.28 ? 70  SER A C   1 
ATOM   572  O O   A SER A 1 70  ? -4.578  -0.471  14.903 0.50 16.54 ? 70  SER A O   1 
ATOM   573  O O   B SER A 1 70  ? -4.736  -0.286  14.795 0.50 16.98 ? 70  SER A O   1 
ATOM   574  C CB  A SER A 1 70  ? -5.134  1.477   17.492 0.50 15.20 ? 70  SER A CB  1 
ATOM   575  C CB  B SER A 1 70  ? -5.330  1.286   17.514 0.50 14.79 ? 70  SER A CB  1 
ATOM   576  O OG  A SER A 1 70  ? -6.432  1.189   17.009 0.50 21.40 ? 70  SER A OG  1 
ATOM   577  O OG  B SER A 1 70  ? -4.928  2.632   17.341 0.50 13.44 ? 70  SER A OG  1 
ATOM   578  N N   . ALA A 1 71  ? -3.055  1.173   15.111 1.00 15.77 ? 71  ALA A N   1 
ATOM   579  C CA  . ALA A 1 71  ? -2.755  1.172   13.683 1.00 14.61 ? 71  ALA A CA  1 
ATOM   580  C C   . ALA A 1 71  ? -2.185  -0.170  13.250 1.00 16.35 ? 71  ALA A C   1 
ATOM   581  O O   . ALA A 1 71  ? -2.527  -0.691  12.182 1.00 15.02 ? 71  ALA A O   1 
ATOM   582  C CB  . ALA A 1 71  ? -1.787  2.312   13.358 1.00 17.48 ? 71  ALA A CB  1 
ATOM   583  N N   . LEU A 1 72  ? -1.310  -0.745  14.073 1.00 14.67 ? 72  LEU A N   1 
ATOM   584  C CA  . LEU A 1 72  ? -0.732  -2.045  13.770 1.00 14.83 ? 72  LEU A CA  1 
ATOM   585  C C   . LEU A 1 72  ? -1.781  -3.150  13.847 1.00 15.72 ? 72  LEU A C   1 
ATOM   586  O O   . LEU A 1 72  ? -1.765  -4.080  13.030 1.00 17.21 ? 72  LEU A O   1 
ATOM   587  C CB  . LEU A 1 72  ? 0.425   -2.301  14.731 1.00 16.08 ? 72  LEU A CB  1 
ATOM   588  C CG  . LEU A 1 72  ? 1.680   -1.472  14.426 1.00 15.13 ? 72  LEU A CG  1 
ATOM   589  C CD1 . LEU A 1 72  ? 2.745   -1.775  15.460 1.00 18.64 ? 72  LEU A CD1 1 
ATOM   590  C CD2 . LEU A 1 72  ? 2.176   -1.765  13.029 1.00 16.91 ? 72  LEU A CD2 1 
ATOM   591  N N   A GLN A 1 73  ? -2.694  -3.074  14.822 0.43 17.12 ? 73  GLN A N   1 
ATOM   592  N N   B GLN A 1 73  ? -2.700  -3.058  14.812 0.57 17.10 ? 73  GLN A N   1 
ATOM   593  C CA  A GLN A 1 73  ? -3.786  -4.044  14.879 0.43 19.93 ? 73  GLN A CA  1 
ATOM   594  C CA  B GLN A 1 73  ? -3.788  -4.026  14.894 0.57 19.93 ? 73  GLN A CA  1 
ATOM   595  C C   A GLN A 1 73  ? -4.656  -3.961  13.632 0.43 19.57 ? 73  GLN A C   1 
ATOM   596  C C   B GLN A 1 73  ? -4.672  -3.953  13.657 0.57 19.54 ? 73  GLN A C   1 
ATOM   597  O O   A GLN A 1 73  ? -5.126  -4.987  13.126 0.43 20.94 ? 73  GLN A O   1 
ATOM   598  O O   B GLN A 1 73  ? -5.152  -4.985  13.174 0.57 20.98 ? 73  GLN A O   1 
ATOM   599  C CB  A GLN A 1 73  ? -4.628  -3.834  16.139 0.43 19.11 ? 73  GLN A CB  1 
ATOM   600  C CB  B GLN A 1 73  ? -4.602  -3.781  16.165 0.57 19.08 ? 73  GLN A CB  1 
ATOM   601  C CG  A GLN A 1 73  ? -3.915  -4.178  17.444 0.43 19.59 ? 73  GLN A CG  1 
ATOM   602  C CG  B GLN A 1 73  ? -5.803  -4.687  16.351 0.57 22.35 ? 73  GLN A CG  1 
ATOM   603  C CD  A GLN A 1 73  ? -4.754  -3.864  18.672 0.43 27.62 ? 73  GLN A CD  1 
ATOM   604  C CD  B GLN A 1 73  ? -6.753  -4.165  17.417 0.57 28.51 ? 73  GLN A CD  1 
ATOM   605  O OE1 A GLN A 1 73  ? -5.633  -3.002  18.635 0.43 29.08 ? 73  GLN A OE1 1 
ATOM   606  O OE1 B GLN A 1 73  ? -7.149  -3.000  17.389 0.57 30.80 ? 73  GLN A OE1 1 
ATOM   607  N NE2 A GLN A 1 73  ? -4.492  -4.570  19.767 0.43 26.90 ? 73  GLN A NE2 1 
ATOM   608  N NE2 B GLN A 1 73  ? -7.123  -5.026  18.363 0.57 27.81 ? 73  GLN A NE2 1 
ATOM   609  N N   . LEU A 1 74  ? -4.861  -2.749  13.110 1.00 19.97 ? 74  LEU A N   1 
ATOM   610  C CA  . LEU A 1 74  ? -5.638  -2.595  11.885 1.00 20.16 ? 74  LEU A CA  1 
ATOM   611  C C   . LEU A 1 74  ? -5.008  -3.351  10.718 1.00 21.24 ? 74  LEU A C   1 
ATOM   612  O O   . LEU A 1 74  ? -5.711  -4.033  9.960  1.00 20.67 ? 74  LEU A O   1 
ATOM   613  C CB  . LEU A 1 74  ? -5.785  -1.111  11.556 1.00 19.04 ? 74  LEU A CB  1 
ATOM   614  C CG  . LEU A 1 74  ? -6.713  -0.772  10.384 1.00 23.21 ? 74  LEU A CG  1 
ATOM   615  C CD1 . LEU A 1 74  ? -8.152  -1.126  10.700 1.00 26.40 ? 74  LEU A CD1 1 
ATOM   616  C CD2 . LEU A 1 74  ? -6.603  0.709   10.030 1.00 22.85 ? 74  LEU A CD2 1 
ATOM   617  N N   . VAL A 1 75  ? -3.681  -3.267  10.571 1.00 15.85 ? 75  VAL A N   1 
ATOM   618  C CA  . VAL A 1 75  ? -3.002  -3.966  9.487  1.00 14.69 ? 75  VAL A CA  1 
ATOM   619  C C   . VAL A 1 75  ? -3.073  -5.474  9.690  1.00 19.66 ? 75  VAL A C   1 
ATOM   620  O O   . VAL A 1 75  ? -3.113  -6.239  8.717  1.00 23.49 ? 75  VAL A O   1 
ATOM   621  C CB  . VAL A 1 75  ? -1.544  -3.477  9.368  1.00 17.89 ? 75  VAL A CB  1 
ATOM   622  C CG1 . VAL A 1 75  ? -0.802  -4.249  8.272  1.00 17.74 ? 75  VAL A CG1 1 
ATOM   623  C CG2 . VAL A 1 75  ? -1.529  -1.989  9.095  1.00 18.61 ? 75  VAL A CG2 1 
ATOM   624  N N   . ALA A 1 76  ? -3.077  -5.926  10.945 1.00 20.09 ? 76  ALA A N   1 
ATOM   625  C CA  . ALA A 1 76  ? -3.171  -7.355  11.211 1.00 21.68 ? 76  ALA A CA  1 
ATOM   626  C C   . ALA A 1 76  ? -4.583  -7.868  10.980 1.00 21.43 ? 76  ALA A C   1 
ATOM   627  O O   . ALA A 1 76  ? -4.765  -9.013  10.550 1.00 27.90 ? 76  ALA A O   1 
ATOM   628  C CB  . ALA A 1 76  ? -2.725  -7.648  12.646 1.00 20.23 ? 76  ALA A CB  1 
ATOM   629  N N   A GLN A 1 77  ? -5.595  -7.051  11.251 0.47 21.96 ? 77  GLN A N   1 
ATOM   630  N N   B GLN A 1 77  ? -5.589  -7.040  11.265 0.53 21.95 ? 77  GLN A N   1 
ATOM   631  C CA  A GLN A 1 77  ? -6.961  -7.526  11.095 0.47 23.10 ? 77  GLN A CA  1 
ATOM   632  C CA  B GLN A 1 77  ? -6.973  -7.464  11.113 0.53 23.09 ? 77  GLN A CA  1 
ATOM   633  C C   A GLN A 1 77  ? -7.471  -7.367  9.669  0.47 27.46 ? 77  GLN A C   1 
ATOM   634  C C   B GLN A 1 77  ? -7.425  -7.387  9.661  0.53 27.46 ? 77  GLN A C   1 
ATOM   635  O O   A GLN A 1 77  ? -8.235  -8.217  9.198  0.47 26.44 ? 77  GLN A O   1 
ATOM   636  O O   B GLN A 1 77  ? -8.104  -8.295  9.172  0.53 26.56 ? 77  GLN A O   1 
ATOM   637  C CB  A GLN A 1 77  ? -7.883  -6.805  12.083 0.47 21.87 ? 77  GLN A CB  1 
ATOM   638  C CB  B GLN A 1 77  ? -7.876  -6.618  12.013 0.53 21.50 ? 77  GLN A CB  1 
ATOM   639  C CG  A GLN A 1 77  ? -9.366  -6.872  11.741 0.47 26.46 ? 77  GLN A CG  1 
ATOM   640  C CG  B GLN A 1 77  ? -7.779  -6.991  13.493 0.53 23.35 ? 77  GLN A CG  1 
ATOM   641  C CD  A GLN A 1 77  ? -10.028 -8.168  12.150 0.47 34.22 ? 77  GLN A CD  1 
ATOM   642  C CD  B GLN A 1 77  ? -8.529  -6.034  14.413 0.53 32.97 ? 77  GLN A CD  1 
ATOM   643  O OE1 A GLN A 1 77  ? -9.509  -9.256  11.900 0.47 38.90 ? 77  GLN A OE1 1 
ATOM   644  O OE1 B GLN A 1 77  ? -8.312  -4.821  14.386 0.53 33.91 ? 77  GLN A OE1 1 
ATOM   645  N NE2 A GLN A 1 77  ? -11.204 -8.058  12.763 0.47 30.86 ? 77  GLN A NE2 1 
ATOM   646  N NE2 B GLN A 1 77  ? -9.403  -6.585  15.248 0.53 32.98 ? 77  GLN A NE2 1 
ATOM   647  N N   . TYR A 1 78  ? -7.057  -6.320  8.951  1.00 18.01 ? 78  TYR A N   1 
ATOM   648  C CA  . TYR A 1 78  ? -7.448  -6.153  7.556  1.00 23.25 ? 78  TYR A CA  1 
ATOM   649  C C   . TYR A 1 78  ? -6.252  -6.230  6.614  1.00 25.84 ? 78  TYR A C   1 
ATOM   650  O O   . TYR A 1 78  ? -6.147  -7.175  5.833  1.00 27.50 ? 78  TYR A O   1 
ATOM   651  C CB  . TYR A 1 78  ? -8.242  -4.865  7.320  1.00 20.81 ? 78  TYR A CB  1 
ATOM   652  C CG  . TYR A 1 78  ? -9.448  -4.663  8.222  1.00 29.86 ? 78  TYR A CG  1 
ATOM   653  C CD1 . TYR A 1 78  ? -9.316  -4.331  9.561  1.00 29.49 ? 78  TYR A CD1 1 
ATOM   654  C CD2 . TYR A 1 78  ? -10.726 -4.905  7.737  1.00 34.87 ? 78  TYR A CD2 1 
ATOM   655  C CE1 . TYR A 1 78  ? -10.435 -4.159  10.370 1.00 30.90 ? 78  TYR A CE1 1 
ATOM   656  C CE2 . TYR A 1 78  ? -11.840 -4.755  8.535  1.00 37.33 ? 78  TYR A CE2 1 
ATOM   657  C CZ  . TYR A 1 78  ? -11.692 -4.388  9.850  1.00 33.20 ? 78  TYR A CZ  1 
ATOM   658  O OH  . TYR A 1 78  ? -12.807 -4.238  10.641 1.00 41.22 ? 78  TYR A OH  1 
ATOM   659  N N   . GLY A 1 79  ? -5.361  -5.265  6.653  1.00 19.35 ? 79  GLY A N   1 
ATOM   660  C CA  . GLY A 1 79  ? -4.279  -5.192  5.701  1.00 18.24 ? 79  GLY A CA  1 
ATOM   661  C C   . GLY A 1 79  ? -3.951  -3.736  5.457  1.00 14.71 ? 79  GLY A C   1 
ATOM   662  O O   . GLY A 1 79  ? -4.484  -2.853  6.121  1.00 18.44 ? 79  GLY A O   1 
ATOM   663  N N   . ILE A 1 80  ? -3.051  -3.508  4.500  1.00 16.50 ? 80  ILE A N   1 
ATOM   664  C CA  . ILE A 1 80  ? -2.642  -2.153  4.142  1.00 15.84 ? 80  ILE A CA  1 
ATOM   665  C C   . ILE A 1 80  ? -2.359  -2.102  2.647  1.00 16.13 ? 80  ILE A C   1 
ATOM   666  O O   . ILE A 1 80  ? -1.928  -3.085  2.040  1.00 17.31 ? 80  ILE A O   1 
ATOM   667  C CB  . ILE A 1 80  ? -1.433  -1.679  4.996  1.00 14.78 ? 80  ILE A CB  1 
ATOM   668  C CG1 . ILE A 1 80  ? -1.265  -0.154  4.893  1.00 12.30 ? 80  ILE A CG1 1 
ATOM   669  C CG2 . ILE A 1 80  ? -0.145  -2.443  4.668  1.00 16.32 ? 80  ILE A CG2 1 
ATOM   670  C CD1 . ILE A 1 80  ? -0.371  0.441   6.005  1.00 16.64 ? 80  ILE A CD1 1 
ATOM   671  N N   . HIS A 1 81  ? -2.630  -0.944  2.053  1.00 14.08 ? 81  HIS A N   1 
ATOM   672  C CA  . HIS A 1 81  ? -2.377  -0.670  0.648  1.00 14.46 ? 81  HIS A CA  1 
ATOM   673  C C   . HIS A 1 81  ? -1.010  -0.016  0.471  1.00 13.88 ? 81  HIS A C   1 
ATOM   674  O O   . HIS A 1 81  ? -0.443  0.552   1.409  1.00 16.01 ? 81  HIS A O   1 
ATOM   675  C CB  . HIS A 1 81  ? -3.463  0.252   0.105  1.00 15.10 ? 81  HIS A CB  1 
ATOM   676  C CG  . HIS A 1 81  ? -4.759  -0.445  -0.154 1.00 14.17 ? 81  HIS A CG  1 
ATOM   677  N ND1 . HIS A 1 81  ? -5.790  -0.448  0.761  1.00 19.36 ? 81  HIS A ND1 1 
ATOM   678  C CD2 . HIS A 1 81  ? -5.198  -1.153  -1.220 1.00 16.71 ? 81  HIS A CD2 1 
ATOM   679  C CE1 . HIS A 1 81  ? -6.810  -1.131  0.269  1.00 22.17 ? 81  HIS A CE1 1 
ATOM   680  N NE2 . HIS A 1 81  ? -6.476  -1.568  -0.931 1.00 18.38 ? 81  HIS A NE2 1 
ATOM   681  N N   . TYR A 1 82  ? -0.491  -0.100  -0.748 1.00 14.81 ? 82  TYR A N   1 
ATOM   682  C CA  . TYR A 1 82  ? 0.721   0.624   -1.102 1.00 12.64 ? 82  TYR A CA  1 
ATOM   683  C C   . TYR A 1 82  ? 0.513   2.128   -0.967 1.00 14.76 ? 82  TYR A C   1 
ATOM   684  O O   . TYR A 1 82  ? -0.591  2.647   -1.154 1.00 14.70 ? 82  TYR A O   1 
ATOM   685  C CB  . TYR A 1 82  ? 1.159   0.303   -2.538 1.00 19.83 ? 82  TYR A CB  1 
ATOM   686  C CG  . TYR A 1 82  ? 1.661   -1.102  -2.751 1.00 19.67 ? 82  TYR A CG  1 
ATOM   687  C CD1 . TYR A 1 82  ? 2.660   -1.621  -1.950 1.00 16.41 ? 82  TYR A CD1 1 
ATOM   688  C CD2 . TYR A 1 82  ? 1.159   -1.899  -3.782 1.00 22.24 ? 82  TYR A CD2 1 
ATOM   689  C CE1 . TYR A 1 82  ? 3.132   -2.911  -2.140 1.00 19.04 ? 82  TYR A CE1 1 
ATOM   690  C CE2 . TYR A 1 82  ? 1.633   -3.192  -3.985 1.00 20.81 ? 82  TYR A CE2 1 
ATOM   691  C CZ  . TYR A 1 82  ? 2.614   -3.689  -3.153 1.00 19.86 ? 82  TYR A CZ  1 
ATOM   692  O OH  . TYR A 1 82  ? 3.092   -4.964  -3.320 1.00 23.47 ? 82  TYR A OH  1 
ATOM   693  N N   . ARG A 1 83  ? 1.596   2.829   -0.626 1.00 14.76 ? 83  ARG A N   1 
ATOM   694  C CA  . ARG A 1 83  ? 1.540   4.283   -0.530 1.00 11.57 ? 83  ARG A CA  1 
ATOM   695  C C   . ARG A 1 83  ? 1.094   4.907   -1.855 1.00 15.60 ? 83  ARG A C   1 
ATOM   696  O O   . ARG A 1 83  ? 0.339   5.884   -1.864 1.00 15.28 ? 83  ARG A O   1 
ATOM   697  C CB  . ARG A 1 83  ? 2.908   4.831   -0.115 1.00 13.11 ? 83  ARG A CB  1 
ATOM   698  C CG  . ARG A 1 83  ? 2.878   6.253   0.457  1.00 13.76 ? 83  ARG A CG  1 
ATOM   699  C CD  . ARG A 1 83  ? 4.264   6.643   0.989  1.00 13.75 ? 83  ARG A CD  1 
ATOM   700  N NE  . ARG A 1 83  ? 4.166   7.641   2.051  1.00 15.67 ? 83  ARG A NE  1 
ATOM   701  C CZ  . ARG A 1 83  ? 4.601   8.894   1.992  1.00 13.83 ? 83  ARG A CZ  1 
ATOM   702  N NH1 . ARG A 1 83  ? 5.271   9.355   0.944  1.00 16.44 ? 83  ARG A NH1 1 
ATOM   703  N NH2 . ARG A 1 83  ? 4.404   9.697   3.036  1.00 17.43 ? 83  ARG A NH2 1 
ATOM   704  N N   . ASN A 1 84  ? 1.563   4.362   -2.981 1.00 14.98 ? 84  ASN A N   1 
ATOM   705  C CA  . ASN A 1 84  ? 1.191   4.874   -4.298 1.00 16.82 ? 84  ASN A CA  1 
ATOM   706  C C   . ASN A 1 84  ? -0.308  4.802   -4.546 1.00 16.68 ? 84  ASN A C   1 
ATOM   707  O O   . ASN A 1 84  ? -0.874  5.690   -5.196 1.00 19.87 ? 84  ASN A O   1 
ATOM   708  C CB  . ASN A 1 84  ? 1.957   4.091   -5.367 1.00 18.84 ? 84  ASN A CB  1 
ATOM   709  C CG  . ASN A 1 84  ? 1.675   4.578   -6.770 1.00 29.35 ? 84  ASN A CG  1 
ATOM   710  O OD1 . ASN A 1 84  ? 1.720   5.779   -7.064 1.00 26.62 ? 84  ASN A OD1 1 
ATOM   711  N ND2 . ASN A 1 84  ? 1.379   3.635   -7.654 1.00 40.04 ? 84  ASN A ND2 1 
ATOM   712  N N   . THR A 1 85  ? -0.965  3.770   -4.026 1.00 14.62 ? 85  THR A N   1 
ATOM   713  C CA  . THR A 1 85  ? -2.401  3.612   -4.193 1.00 14.30 ? 85  THR A CA  1 
ATOM   714  C C   . THR A 1 85  ? -3.174  4.575   -3.299 1.00 14.92 ? 85  THR A C   1 
ATOM   715  O O   . THR A 1 85  ? -4.315  4.956   -3.611 1.00 16.99 ? 85  THR A O   1 
ATOM   716  C CB  . THR A 1 85  ? -2.766  2.162   -3.860 1.00 19.95 ? 85  THR A CB  1 
ATOM   717  O OG1 . THR A 1 85  ? -2.033  1.282   -4.717 1.00 22.09 ? 85  THR A OG1 1 
ATOM   718  C CG2 . THR A 1 85  ? -4.280  1.908   -4.021 1.00 20.77 ? 85  THR A CG2 1 
ATOM   719  N N   . TYR A 1 86  ? -2.586  4.959   -2.177 1.00 13.78 ? 86  TYR A N   1 
ATOM   720  C CA  . TYR A 1 86  ? -3.278  5.699   -1.120 1.00 14.78 ? 86  TYR A CA  1 
ATOM   721  C C   . TYR A 1 86  ? -2.275  6.700   -0.567 1.00 13.20 ? 86  TYR A C   1 
ATOM   722  O O   . TYR A 1 86  ? -1.772  6.557   0.559  1.00 13.58 ? 86  TYR A O   1 
ATOM   723  C CB  . TYR A 1 86  ? -3.802  4.725   -0.060 1.00 13.29 ? 86  TYR A CB  1 
ATOM   724  C CG  . TYR A 1 86  ? -5.011  5.137   0.766  1.00 12.16 ? 86  TYR A CG  1 
ATOM   725  C CD1 . TYR A 1 86  ? -5.263  6.467   1.083  1.00 13.79 ? 86  TYR A CD1 1 
ATOM   726  C CD2 . TYR A 1 86  ? -5.867  4.174   1.276  1.00 16.04 ? 86  TYR A CD2 1 
ATOM   727  C CE1 . TYR A 1 86  ? -6.367  6.822   1.871  1.00 14.04 ? 86  TYR A CE1 1 
ATOM   728  C CE2 . TYR A 1 86  ? -6.962  4.517   2.049  1.00 12.07 ? 86  TYR A CE2 1 
ATOM   729  C CZ  . TYR A 1 86  ? -7.204  5.837   2.348  1.00 12.46 ? 86  TYR A CZ  1 
ATOM   730  O OH  . TYR A 1 86  ? -8.281  6.186   3.126  1.00 14.29 ? 86  TYR A OH  1 
ATOM   731  N N   . PRO A 1 87  ? -1.940  7.723   -1.356 1.00 12.26 ? 87  PRO A N   1 
ATOM   732  C CA  . PRO A 1 87  ? -0.827  8.612   -1.001 1.00 12.47 ? 87  PRO A CA  1 
ATOM   733  C C   . PRO A 1 87  ? -1.180  9.567   0.130  1.00 11.90 ? 87  PRO A C   1 
ATOM   734  O O   . PRO A 1 87  ? -2.334  9.757   0.503  1.00 11.79 ? 87  PRO A O   1 
ATOM   735  C CB  . PRO A 1 87  ? -0.542  9.370   -2.302 1.00 13.49 ? 87  PRO A CB  1 
ATOM   736  C CG  . PRO A 1 87  ? -1.854  9.330   -3.065 1.00 13.96 ? 87  PRO A CG  1 
ATOM   737  C CD  . PRO A 1 87  ? -2.470  8.009   -2.707 1.00 13.33 ? 87  PRO A CD  1 
ATOM   738  N N   . TYR A 1 88  ? -0.135  10.173  0.698  1.00 10.99 ? 88  TYR A N   1 
ATOM   739  C CA  . TYR A 1 88  ? -0.293  10.992  1.894  1.00 10.91 ? 88  TYR A CA  1 
ATOM   740  C C   . TYR A 1 88  ? -0.771  12.397  1.546  1.00 11.44 ? 88  TYR A C   1 
ATOM   741  O O   . TYR A 1 88  ? -0.161  13.087  0.725  1.00 15.90 ? 88  TYR A O   1 
ATOM   742  C CB  . TYR A 1 88  ? 1.026   11.079  2.663  1.00 11.22 ? 88  TYR A CB  1 
ATOM   743  C CG  . TYR A 1 88  ? 0.905   11.821  3.983  1.00 13.05 ? 88  TYR A CG  1 
ATOM   744  C CD1 . TYR A 1 88  ? 0.055   11.361  4.993  1.00 12.19 ? 88  TYR A CD1 1 
ATOM   745  C CD2 . TYR A 1 88  ? 1.621   12.986  4.215  1.00 11.30 ? 88  TYR A CD2 1 
ATOM   746  C CE1 . TYR A 1 88  ? -0.047  12.028  6.195  1.00 15.74 ? 88  TYR A CE1 1 
ATOM   747  C CE2 . TYR A 1 88  ? 1.526   13.672  5.422  1.00 11.45 ? 88  TYR A CE2 1 
ATOM   748  C CZ  . TYR A 1 88  ? 0.684   13.176  6.411  1.00 12.83 ? 88  TYR A CZ  1 
ATOM   749  O OH  . TYR A 1 88  ? 0.572   13.837  7.620  1.00 13.29 ? 88  TYR A OH  1 
ATOM   750  N N   . GLU A 1 89  ? -1.844  12.829  2.200  1.00 12.38 ? 89  GLU A N   1 
ATOM   751  C CA  . GLU A 1 89  ? -2.430  14.147  1.970  1.00 13.38 ? 89  GLU A CA  1 
ATOM   752  C C   . GLU A 1 89  ? -2.311  15.094  3.159  1.00 15.59 ? 89  GLU A C   1 
ATOM   753  O O   . GLU A 1 89  ? -2.647  16.274  3.025  1.00 17.08 ? 89  GLU A O   1 
ATOM   754  C CB  . GLU A 1 89  ? -3.910  13.995  1.573  1.00 16.56 ? 89  GLU A CB  1 
ATOM   755  C CG  . GLU A 1 89  ? -4.192  12.745  0.739  1.00 14.42 ? 89  GLU A CG  1 
ATOM   756  C CD  . GLU A 1 89  ? -5.607  12.708  0.190  1.00 14.50 ? 89  GLU A CD  1 
ATOM   757  O OE1 . GLU A 1 89  ? -6.179  13.773  -0.125 1.00 15.96 ? 89  GLU A OE1 1 
ATOM   758  O OE2 . GLU A 1 89  ? -6.195  11.615  0.214  1.00 14.36 ? 89  GLU A OE2 1 
ATOM   759  N N   . GLY A 1 90  ? -1.867  14.619  4.320  1.00 13.17 ? 90  GLY A N   1 
ATOM   760  C CA  . GLY A 1 90  ? -1.691  15.526  5.430  1.00 13.93 ? 90  GLY A CA  1 
ATOM   761  C C   . GLY A 1 90  ? -2.961  16.021  6.091  1.00 13.15 ? 90  GLY A C   1 
ATOM   762  O O   . GLY A 1 90  ? -2.913  16.993  6.837  1.00 16.73 ? 90  GLY A O   1 
ATOM   763  N N   . VAL A 1 91  ? -4.097  15.383  5.825  1.00 15.23 ? 91  VAL A N   1 
ATOM   764  C CA  . VAL A 1 91  ? -5.377  15.731  6.428  1.00 16.80 ? 91  VAL A CA  1 
ATOM   765  C C   . VAL A 1 91  ? -6.179  14.441  6.510  1.00 14.81 ? 91  VAL A C   1 
ATOM   766  O O   . VAL A 1 91  ? -6.067  13.588  5.630  1.00 16.55 ? 91  VAL A O   1 
ATOM   767  C CB  . VAL A 1 91  ? -6.100  16.823  5.599  1.00 16.53 ? 91  VAL A CB  1 
ATOM   768  C CG1 . VAL A 1 91  ? -6.244  16.397  4.142  1.00 18.78 ? 91  VAL A CG1 1 
ATOM   769  C CG2 . VAL A 1 91  ? -7.454  17.162  6.189  1.00 17.80 ? 91  VAL A CG2 1 
ATOM   770  N N   . GLN A 1 92  ? -6.973  14.271  7.564  1.00 13.15 ? 92  GLN A N   1 
ATOM   771  C CA  . GLN A 1 92  ? -7.786  13.066  7.660  1.00 12.46 ? 92  GLN A CA  1 
ATOM   772  C C   . GLN A 1 92  ? -8.995  13.200  6.743  1.00 13.37 ? 92  GLN A C   1 
ATOM   773  O O   . GLN A 1 92  ? -9.661  14.241  6.727  1.00 17.78 ? 92  GLN A O   1 
ATOM   774  C CB  . GLN A 1 92  ? -8.257  12.805  9.094  1.00 16.52 ? 92  GLN A CB  1 
ATOM   775  C CG  . GLN A 1 92  ? -9.055  11.511  9.185  1.00 18.13 ? 92  GLN A CG  1 
ATOM   776  C CD  . GLN A 1 92  ? -9.565  11.198  10.582 1.00 16.31 ? 92  GLN A CD  1 
ATOM   777  O OE1 . GLN A 1 92  ? -9.321  10.111  11.129 1.00 18.71 ? 92  GLN A OE1 1 
ATOM   778  N NE2 . GLN A 1 92  ? -10.302 12.131  11.152 1.00 20.46 ? 92  GLN A NE2 1 
ATOM   779  N N   . ARG A 1 93  ? -9.273  12.145  5.983  1.00 13.22 ? 93  ARG A N   1 
ATOM   780  C CA  . ARG A 1 93  ? -10.442 12.102  5.120  1.00 13.36 ? 93  ARG A CA  1 
ATOM   781  C C   . ARG A 1 93  ? -11.198 10.809  5.412  1.00 16.34 ? 93  ARG A C   1 
ATOM   782  O O   . ARG A 1 93  ? -10.861 10.091  6.361  1.00 21.27 ? 93  ARG A O   1 
ATOM   783  C CB  . ARG A 1 93  ? -10.024 12.216  3.648  1.00 13.09 ? 93  ARG A CB  1 
ATOM   784  C CG  . ARG A 1 93  ? -9.350  13.549  3.300  1.00 15.39 ? 93  ARG A CG  1 
ATOM   785  C CD  . ARG A 1 93  ? -8.918  13.580  1.843  1.00 14.55 ? 93  ARG A CD  1 
ATOM   786  N NE  . ARG A 1 93  ? -10.078 13.542  0.960  1.00 14.80 ? 93  ARG A NE  1 
ATOM   787  C CZ  . ARG A 1 93  ? -10.012 13.423  -0.359 1.00 15.05 ? 93  ARG A CZ  1 
ATOM   788  N NH1 . ARG A 1 93  ? -8.857  13.305  -0.988 1.00 12.81 ? 93  ARG A NH1 1 
ATOM   789  N NH2 . ARG A 1 93  ? -11.133 13.428  -1.066 1.00 17.09 ? 93  ARG A NH2 1 
ATOM   790  N N   . TYR A 1 94  ? -12.222 10.501  4.620  1.00 18.02 ? 94  TYR A N   1 
ATOM   791  C CA  . TYR A 1 94  ? -12.950 9.254   4.797  1.00 16.87 ? 94  TYR A CA  1 
ATOM   792  C C   . TYR A 1 94  ? -12.036 8.068   4.528  1.00 16.43 ? 94  TYR A C   1 
ATOM   793  O O   . TYR A 1 94  ? -11.118 8.145   3.709  1.00 16.90 ? 94  TYR A O   1 
ATOM   794  C CB  . TYR A 1 94  ? -14.144 9.197   3.844  1.00 19.60 ? 94  TYR A CB  1 
ATOM   795  C CG  . TYR A 1 94  ? -15.083 10.384  3.953  1.00 24.21 ? 94  TYR A CG  1 
ATOM   796  C CD1 . TYR A 1 94  ? -15.657 10.740  5.171  1.00 29.17 ? 94  TYR A CD1 1 
ATOM   797  C CD2 . TYR A 1 94  ? -15.363 11.169  2.839  1.00 30.21 ? 94  TYR A CD2 1 
ATOM   798  C CE1 . TYR A 1 94  ? -16.506 11.837  5.267  1.00 36.80 ? 94  TYR A CE1 1 
ATOM   799  C CE2 . TYR A 1 94  ? -16.206 12.267  2.925  1.00 30.61 ? 94  TYR A CE2 1 
ATOM   800  C CZ  . TYR A 1 94  ? -16.771 12.596  4.138  1.00 30.57 ? 94  TYR A CZ  1 
ATOM   801  O OH  . TYR A 1 94  ? -17.610 13.686  4.216  1.00 28.39 ? 94  TYR A OH  1 
ATOM   802  N N   . CYS A 1 95  ? -12.312 6.951   5.204  1.00 17.62 ? 95  CYS A N   1 
ATOM   803  C CA  . CYS A 1 95  ? -11.592 5.717   4.933  1.00 16.88 ? 95  CYS A CA  1 
ATOM   804  C C   . CYS A 1 95  ? -11.963 5.200   3.545  1.00 19.92 ? 95  CYS A C   1 
ATOM   805  O O   . CYS A 1 95  ? -13.138 4.934   3.267  1.00 19.22 ? 95  CYS A O   1 
ATOM   806  C CB  . CYS A 1 95  ? -11.912 4.669   5.996  1.00 18.82 ? 95  CYS A CB  1 
ATOM   807  S SG  . CYS A 1 95  ? -11.073 3.103   5.727  1.00 19.87 ? 95  CYS A SG  1 
ATOM   808  N N   . ARG A 1 96  ? -10.964 5.050   2.675  1.00 12.99 ? 96  ARG A N   1 
ATOM   809  C CA  . ARG A 1 96  ? -11.187 4.655   1.288  1.00 14.56 ? 96  ARG A CA  1 
ATOM   810  C C   . ARG A 1 96  ? -10.582 3.295   0.955  1.00 15.36 ? 96  ARG A C   1 
ATOM   811  O O   . ARG A 1 96  ? -10.410 2.973   -0.224 1.00 19.63 ? 96  ARG A O   1 
ATOM   812  C CB  . ARG A 1 96  ? -10.646 5.734   0.353  1.00 15.05 ? 96  ARG A CB  1 
ATOM   813  C CG  . ARG A 1 96  ? -11.421 7.043   0.468  1.00 16.11 ? 96  ARG A CG  1 
ATOM   814  C CD  . ARG A 1 96  ? -10.586 8.195   -0.044 1.00 17.38 ? 96  ARG A CD  1 
ATOM   815  N NE  . ARG A 1 96  ? -9.707  8.708   1.001  1.00 15.13 ? 96  ARG A NE  1 
ATOM   816  C CZ  . ARG A 1 96  ? -8.724  9.566   0.773  1.00 16.75 ? 96  ARG A CZ  1 
ATOM   817  N NH1 . ARG A 1 96  ? -8.433  9.976   -0.452 1.00 15.52 ? 96  ARG A NH1 1 
ATOM   818  N NH2 . ARG A 1 96  ? -7.991  9.995   1.792  1.00 12.54 ? 96  ARG A NH2 1 
ATOM   819  N N   A SER A 1 97  ? -10.268 2.486   1.972  0.53 16.46 ? 97  SER A N   1 
ATOM   820  N N   B SER A 1 97  ? -10.297 2.477   1.974  0.47 16.49 ? 97  SER A N   1 
ATOM   821  C CA  A SER A 1 97  ? -9.660  1.179   1.730  0.53 21.79 ? 97  SER A CA  1 
ATOM   822  C CA  B SER A 1 97  ? -9.654  1.183   1.751  0.47 21.80 ? 97  SER A CA  1 
ATOM   823  C C   A SER A 1 97  ? -10.511 0.334   0.796  0.53 24.01 ? 97  SER A C   1 
ATOM   824  C C   B SER A 1 97  ? -10.499 0.275   0.862  0.47 23.96 ? 97  SER A C   1 
ATOM   825  O O   A SER A 1 97  ? -9.992  -0.288  -0.139 0.53 25.80 ? 97  SER A O   1 
ATOM   826  O O   B SER A 1 97  ? -9.962  -0.454  0.019  0.47 26.27 ? 97  SER A O   1 
ATOM   827  C CB  A SER A 1 97  ? -9.462  0.441   3.050  0.53 23.15 ? 97  SER A CB  1 
ATOM   828  C CB  B SER A 1 97  ? -9.371  0.507   3.095  0.47 23.11 ? 97  SER A CB  1 
ATOM   829  O OG  A SER A 1 97  ? -8.802  1.262   3.980  0.53 20.64 ? 97  SER A OG  1 
ATOM   830  O OG  B SER A 1 97  ? -10.551 0.382   3.872  0.47 23.23 ? 97  SER A OG  1 
ATOM   831  N N   . ARG A 1 98  ? -11.825 0.312   1.026  1.00 27.18 ? 98  ARG A N   1 
ATOM   832  C CA  . ARG A 1 98  ? -12.697 -0.536  0.221  1.00 28.17 ? 98  ARG A CA  1 
ATOM   833  C C   . ARG A 1 98  ? -12.714 -0.109  -1.240 1.00 31.51 ? 98  ARG A C   1 
ATOM   834  O O   . ARG A 1 98  ? -12.853 -0.955  -2.131 1.00 36.64 ? 98  ARG A O   1 
ATOM   835  C CB  . ARG A 1 98  ? -14.112 -0.518  0.804  1.00 28.78 ? 98  ARG A CB  1 
ATOM   836  C CG  . ARG A 1 98  ? -14.247 -1.281  2.114  1.00 34.74 ? 98  ARG A CG  1 
ATOM   837  C CD  . ARG A 1 98  ? -15.658 -1.811  2.286  1.00 48.43 ? 98  ARG A CD  1 
ATOM   838  N NE  . ARG A 1 98  ? -16.362 -1.890  1.011  1.00 54.74 ? 98  ARG A NE  1 
ATOM   839  C CZ  . ARG A 1 98  ? -17.645 -2.198  0.880  1.00 60.30 ? 98  ARG A CZ  1 
ATOM   840  N NH1 . ARG A 1 98  ? -18.401 -2.476  1.932  1.00 42.92 ? 98  ARG A NH1 1 
ATOM   841  N NH2 . ARG A 1 98  ? -18.187 -2.219  -0.336 1.00 57.78 ? 98  ARG A NH2 1 
ATOM   842  N N   . GLU A 1 99  ? -12.556 1.186   -1.508 1.00 24.88 ? 99  GLU A N   1 
ATOM   843  C CA  . GLU A 1 99  ? -12.610 1.693   -2.872 1.00 27.58 ? 99  GLU A CA  1 
ATOM   844  C C   . GLU A 1 99  ? -11.328 1.442   -3.651 1.00 25.01 ? 99  GLU A C   1 
ATOM   845  O O   . GLU A 1 99  ? -11.297 1.697   -4.858 1.00 29.71 ? 99  GLU A O   1 
ATOM   846  C CB  . GLU A 1 99  ? -12.881 3.199   -2.867 1.00 26.70 ? 99  GLU A CB  1 
ATOM   847  C CG  . GLU A 1 99  ? -14.153 3.612   -2.183 1.00 37.21 ? 99  GLU A CG  1 
ATOM   848  C CD  . GLU A 1 99  ? -14.169 5.096   -1.863 1.00 42.02 ? 99  GLU A CD  1 
ATOM   849  O OE1 . GLU A 1 99  ? -13.433 5.868   -2.525 1.00 41.14 ? 99  GLU A OE1 1 
ATOM   850  O OE2 . GLU A 1 99  ? -14.899 5.486   -0.924 1.00 51.24 ? 99  GLU A OE2 1 
ATOM   851  N N   . LYS A 1 100 ? -10.267 0.966   -3.003 1.00 22.22 ? 100 LYS A N   1 
ATOM   852  C CA  . LYS A 1 100 ? -8.945  0.971   -3.610 1.00 17.49 ? 100 LYS A CA  1 
ATOM   853  C C   . LYS A 1 100 ? -8.411  -0.431  -3.900 1.00 23.26 ? 100 LYS A C   1 
ATOM   854  O O   . LYS A 1 100 ? -7.199  -0.612  -4.059 1.00 25.59 ? 100 LYS A O   1 
ATOM   855  C CB  . LYS A 1 100 ? -7.982  1.763   -2.720 1.00 17.52 ? 100 LYS A CB  1 
ATOM   856  C CG  . LYS A 1 100 ? -8.213  3.279   -2.786 1.00 17.52 ? 100 LYS A CG  1 
ATOM   857  C CD  . LYS A 1 100 ? -7.339  4.026   -1.777 1.00 17.68 ? 100 LYS A CD  1 
ATOM   858  C CE  . LYS A 1 100 ? -7.479  5.544   -1.844 1.00 15.87 ? 100 LYS A CE  1 
ATOM   859  N NZ  . LYS A 1 100 ? -6.851  6.071   -3.093 1.00 16.02 ? 100 LYS A NZ  1 
ATOM   860  N N   . GLY A 1 101 ? -9.292  -1.418  -4.013 1.00 27.79 ? 101 GLY A N   1 
ATOM   861  C CA  . GLY A 1 101 ? -8.891  -2.734  -4.440 1.00 24.59 ? 101 GLY A CA  1 
ATOM   862  C C   . GLY A 1 101 ? -8.355  -3.564  -3.294 1.00 25.99 ? 101 GLY A C   1 
ATOM   863  O O   . GLY A 1 101 ? -8.416  -3.168  -2.125 1.00 23.04 ? 101 GLY A O   1 
ATOM   864  N N   . PRO A 1 102 ? -7.826  -4.745  -3.615 1.00 27.58 ? 102 PRO A N   1 
ATOM   865  C CA  . PRO A 1 102 ? -7.317  -5.637  -2.569 1.00 21.97 ? 102 PRO A CA  1 
ATOM   866  C C   . PRO A 1 102 ? -6.135  -5.013  -1.846 1.00 22.46 ? 102 PRO A C   1 
ATOM   867  O O   . PRO A 1 102 ? -5.399  -4.207  -2.408 1.00 22.07 ? 102 PRO A O   1 
ATOM   868  C CB  . PRO A 1 102 ? -6.889  -6.879  -3.360 1.00 30.76 ? 102 PRO A CB  1 
ATOM   869  C CG  . PRO A 1 102 ? -7.826  -6.865  -4.537 1.00 35.60 ? 102 PRO A CG  1 
ATOM   870  C CD  . PRO A 1 102 ? -7.784  -5.408  -4.932 1.00 31.22 ? 102 PRO A CD  1 
ATOM   871  N N   . TYR A 1 103 ? -5.964  -5.402  -0.587 1.00 21.81 ? 103 TYR A N   1 
ATOM   872  C CA  . TYR A 1 103 ? -4.823  -4.932  0.184  1.00 20.55 ? 103 TYR A CA  1 
ATOM   873  C C   . TYR A 1 103 ? -3.527  -5.424  -0.436 1.00 23.88 ? 103 TYR A C   1 
ATOM   874  O O   . TYR A 1 103 ? -3.478  -6.472  -1.083 1.00 22.34 ? 103 TYR A O   1 
ATOM   875  C CB  . TYR A 1 103 ? -4.920  -5.415  1.626  1.00 20.38 ? 103 TYR A CB  1 
ATOM   876  C CG  . TYR A 1 103 ? -5.963  -4.694  2.444  1.00 22.16 ? 103 TYR A CG  1 
ATOM   877  C CD1 . TYR A 1 103 ? -5.819  -3.343  2.771  1.00 20.61 ? 103 TYR A CD1 1 
ATOM   878  C CD2 . TYR A 1 103 ? -7.114  -5.354  2.873  1.00 27.56 ? 103 TYR A CD2 1 
ATOM   879  C CE1 . TYR A 1 103 ? -6.776  -2.685  3.517  1.00 21.65 ? 103 TYR A CE1 1 
ATOM   880  C CE2 . TYR A 1 103 ? -8.081  -4.697  3.617  1.00 26.50 ? 103 TYR A CE2 1 
ATOM   881  C CZ  . TYR A 1 103 ? -7.905  -3.363  3.938  1.00 24.96 ? 103 TYR A CZ  1 
ATOM   882  O OH  . TYR A 1 103 ? -8.866  -2.708  4.679  1.00 28.08 ? 103 TYR A OH  1 
ATOM   883  N N   . ALA A 1 104 ? -2.463  -4.650  -0.235 1.00 18.88 ? 104 ALA A N   1 
ATOM   884  C CA  . ALA A 1 104 ? -1.149  -5.018  -0.741 1.00 18.65 ? 104 ALA A CA  1 
ATOM   885  C C   . ALA A 1 104 ? -0.398  -5.940  0.214  1.00 20.17 ? 104 ALA A C   1 
ATOM   886  O O   . ALA A 1 104 ? 0.268   -6.879  -0.235 1.00 22.83 ? 104 ALA A O   1 
ATOM   887  C CB  . ALA A 1 104 ? -0.322  -3.759  -1.017 1.00 17.47 ? 104 ALA A CB  1 
ATOM   888  N N   . ALA A 1 105 ? -0.505  -5.703  1.521  1.00 18.73 ? 105 ALA A N   1 
ATOM   889  C CA  . ALA A 1 105 ? 0.218   -6.492  2.504  1.00 19.74 ? 105 ALA A CA  1 
ATOM   890  C C   . ALA A 1 105 ? -0.665  -6.737  3.714  1.00 18.41 ? 105 ALA A C   1 
ATOM   891  O O   . ALA A 1 105 ? -1.592  -5.972  3.997  1.00 19.86 ? 105 ALA A O   1 
ATOM   892  C CB  . ALA A 1 105 ? 1.510   -5.803  2.948  1.00 21.32 ? 105 ALA A CB  1 
ATOM   893  N N   . LYS A 1 106 ? -0.365  -7.816  4.431  1.00 21.72 ? 106 LYS A N   1 
ATOM   894  C CA  . LYS A 1 106 ? -1.099  -8.146  5.638  1.00 19.60 ? 106 LYS A CA  1 
ATOM   895  C C   . LYS A 1 106 ? -0.137  -8.731  6.662  1.00 22.59 ? 106 LYS A C   1 
ATOM   896  O O   . LYS A 1 106 ? 0.802   -9.448  6.306  1.00 27.36 ? 106 LYS A O   1 
ATOM   897  C CB  . LYS A 1 106 ? -2.237  -9.132  5.333  1.00 25.57 ? 106 LYS A CB  1 
ATOM   898  C CG  . LYS A 1 106 ? -2.798  -9.803  6.566  1.00 36.26 ? 106 LYS A CG  1 
ATOM   899  C CD  . LYS A 1 106 ? -4.122  -9.199  6.980  1.00 35.25 ? 106 LYS A CD  1 
ATOM   900  C CE  . LYS A 1 106 ? -4.937  -10.215 7.751  1.00 33.28 ? 106 LYS A CE  1 
ATOM   901  N NZ  . LYS A 1 106 ? -4.113  -10.744 8.882  1.00 27.35 ? 106 LYS A NZ  1 
ATOM   902  N N   . THR A 1 107 ? -0.361  -8.404  7.929  1.00 19.61 ? 107 THR A N   1 
ATOM   903  C CA  . THR A 1 107 ? 0.404   -8.962  9.033  1.00 18.82 ? 107 THR A CA  1 
ATOM   904  C C   . THR A 1 107 ? -0.491  -9.891  9.848  1.00 25.34 ? 107 THR A C   1 
ATOM   905  O O   . THR A 1 107 ? -1.692  -10.018 9.594  1.00 24.19 ? 107 THR A O   1 
ATOM   906  C CB  . THR A 1 107 ? 0.975   -7.844  9.909  1.00 16.62 ? 107 THR A CB  1 
ATOM   907  O OG1 . THR A 1 107 ? -0.096  -7.034  10.405 1.00 19.97 ? 107 THR A OG1 1 
ATOM   908  C CG2 . THR A 1 107 ? 1.956   -6.975  9.108  1.00 20.98 ? 107 THR A CG2 1 
ATOM   909  N N   . ASP A 1 108 ? 0.106   -10.552 10.841 1.00 22.38 ? 108 ASP A N   1 
ATOM   910  C CA  . ASP A 1 108 ? -0.588  -11.584 11.599 1.00 22.52 ? 108 ASP A CA  1 
ATOM   911  C C   . ASP A 1 108 ? -0.815  -11.245 13.063 1.00 25.79 ? 108 ASP A C   1 
ATOM   912  O O   . ASP A 1 108 ? -1.505  -12.001 13.752 1.00 32.43 ? 108 ASP A O   1 
ATOM   913  C CB  . ASP A 1 108 ? 0.178   -12.907 11.484 1.00 26.85 ? 108 ASP A CB  1 
ATOM   914  C CG  . ASP A 1 108 ? 0.257   -13.394 10.052 1.00 27.18 ? 108 ASP A CG  1 
ATOM   915  O OD1 . ASP A 1 108 ? -0.816  -13.534 9.430  1.00 31.49 ? 108 ASP A OD1 1 
ATOM   916  O OD2 . ASP A 1 108 ? 1.369   -13.611 9.541  1.00 30.88 ? 108 ASP A OD2 1 
ATOM   917  N N   . GLY A 1 109 ? -0.277  -10.135 13.552 1.00 20.18 ? 109 GLY A N   1 
ATOM   918  C CA  . GLY A 1 109 ? -0.522  -9.731  14.918 1.00 20.12 ? 109 GLY A CA  1 
ATOM   919  C C   . GLY A 1 109 ? 0.354   -8.549  15.279 1.00 21.00 ? 109 GLY A C   1 
ATOM   920  O O   . GLY A 1 109 ? 1.041   -7.978  14.426 1.00 19.48 ? 109 GLY A O   1 
ATOM   921  N N   . VAL A 1 110 ? 0.313   -8.202  16.565 1.00 19.25 ? 110 VAL A N   1 
ATOM   922  C CA  . VAL A 1 110 ? 1.060   -7.086  17.141 1.00 19.54 ? 110 VAL A CA  1 
ATOM   923  C C   . VAL A 1 110 ? 1.526   -7.512  18.525 1.00 23.38 ? 110 VAL A C   1 
ATOM   924  O O   . VAL A 1 110 ? 0.758   -8.109  19.283 1.00 21.96 ? 110 VAL A O   1 
ATOM   925  C CB  . VAL A 1 110 ? 0.201   -5.811  17.261 1.00 21.81 ? 110 VAL A CB  1 
ATOM   926  C CG1 . VAL A 1 110 ? 1.010   -4.673  17.898 1.00 22.98 ? 110 VAL A CG1 1 
ATOM   927  C CG2 . VAL A 1 110 ? -0.381  -5.424  15.925 1.00 23.99 ? 110 VAL A CG2 1 
ATOM   928  N N   . ARG A 1 111 ? 2.775   -7.201  18.866 1.00 20.77 ? 111 ARG A N   1 
ATOM   929  C CA  . ARG A 1 111 ? 3.281   -7.438  20.215 1.00 20.47 ? 111 ARG A CA  1 
ATOM   930  C C   . ARG A 1 111 ? 3.856   -6.159  20.805 1.00 21.79 ? 111 ARG A C   1 
ATOM   931  O O   . ARG A 1 111 ? 4.332   -5.282  20.084 1.00 19.29 ? 111 ARG A O   1 
ATOM   932  C CB  . ARG A 1 111 ? 4.353   -8.535  20.260 1.00 23.00 ? 111 ARG A CB  1 
ATOM   933  C CG  . ARG A 1 111 ? 4.069   -9.729  19.390 1.00 33.54 ? 111 ARG A CG  1 
ATOM   934  C CD  . ARG A 1 111 ? 3.949   -11.021 20.187 1.00 40.07 ? 111 ARG A CD  1 
ATOM   935  N NE  . ARG A 1 111 ? 2.697   -11.096 20.933 1.00 48.71 ? 111 ARG A NE  1 
ATOM   936  C CZ  . ARG A 1 111 ? 1.499   -11.270 20.389 1.00 53.65 ? 111 ARG A CZ  1 
ATOM   937  N NH1 . ARG A 1 111 ? 1.345   -11.414 19.080 1.00 47.64 ? 111 ARG A NH1 1 
ATOM   938  N NH2 . ARG A 1 111 ? 0.427   -11.307 21.178 1.00 53.78 ? 111 ARG A NH2 1 
ATOM   939  N N   . GLN A 1 112 ? 3.808   -6.071  22.131 1.00 20.95 ? 112 GLN A N   1 
ATOM   940  C CA  . GLN A 1 112 ? 4.410   -4.979  22.870 1.00 21.22 ? 112 GLN A CA  1 
ATOM   941  C C   . GLN A 1 112 ? 5.727   -5.444  23.480 1.00 19.16 ? 112 GLN A C   1 
ATOM   942  O O   . GLN A 1 112 ? 5.832   -6.572  23.970 1.00 19.96 ? 112 GLN A O   1 
ATOM   943  C CB  . GLN A 1 112 ? 3.461   -4.471  23.962 1.00 21.23 ? 112 GLN A CB  1 
ATOM   944  C CG  . GLN A 1 112 ? 3.980   -3.250  24.707 1.00 21.29 ? 112 GLN A CG  1 
ATOM   945  C CD  . GLN A 1 112 ? 3.002   -2.739  25.743 1.00 25.43 ? 112 GLN A CD  1 
ATOM   946  O OE1 . GLN A 1 112 ? 2.026   -3.410  26.067 1.00 33.81 ? 112 GLN A OE1 1 
ATOM   947  N NE2 . GLN A 1 112 ? 3.271   -1.556  26.285 1.00 32.84 ? 112 GLN A NE2 1 
ATOM   948  N N   . VAL A 1 113 ? 6.745   -4.585  23.393 1.00 17.78 ? 113 VAL A N   1 
ATOM   949  C CA  . VAL A 1 113 ? 7.971   -4.784  24.157 1.00 16.73 ? 113 VAL A CA  1 
ATOM   950  C C   . VAL A 1 113 ? 7.688   -4.507  25.624 1.00 16.33 ? 113 VAL A C   1 
ATOM   951  O O   . VAL A 1 113 ? 6.925   -3.593  25.963 1.00 17.40 ? 113 VAL A O   1 
ATOM   952  C CB  . VAL A 1 113 ? 9.087   -3.860  23.638 1.00 15.96 ? 113 VAL A CB  1 
ATOM   953  C CG1 . VAL A 1 113 ? 10.434  -4.237  24.254 1.00 15.81 ? 113 VAL A CG1 1 
ATOM   954  C CG2 . VAL A 1 113 ? 9.197   -3.945  22.130 1.00 17.23 ? 113 VAL A CG2 1 
ATOM   955  N N   A GLN A 1 114 ? 8.296   -5.291  26.505 0.56 16.99 ? 114 GLN A N   1 
ATOM   956  N N   B GLN A 1 114 ? 8.303   -5.295  26.510 0.44 17.00 ? 114 GLN A N   1 
ATOM   957  C CA  A GLN A 1 114 ? 8.186   -4.999  27.926 0.56 18.26 ? 114 GLN A CA  1 
ATOM   958  C CA  B GLN A 1 114 ? 8.228   -4.989  27.931 0.44 18.31 ? 114 GLN A CA  1 
ATOM   959  C C   A GLN A 1 114 ? 8.688   -3.578  28.173 0.56 19.42 ? 114 GLN A C   1 
ATOM   960  C C   B GLN A 1 114 ? 8.696   -3.555  28.156 0.44 19.43 ? 114 GLN A C   1 
ATOM   961  O O   A GLN A 1 114 ? 9.840   -3.267  27.823 0.56 17.93 ? 114 GLN A O   1 
ATOM   962  O O   B GLN A 1 114 ? 9.834   -3.218  27.788 0.44 17.93 ? 114 GLN A O   1 
ATOM   963  C CB  A GLN A 1 114 ? 8.982   -6.018  28.744 0.56 22.48 ? 114 GLN A CB  1 
ATOM   964  C CB  B GLN A 1 114 ? 9.082   -5.942  28.769 0.44 22.32 ? 114 GLN A CB  1 
ATOM   965  C CG  A GLN A 1 114 ? 8.492   -6.243  30.181 0.56 29.74 ? 114 GLN A CG  1 
ATOM   966  C CG  B GLN A 1 114 ? 9.042   -5.629  30.274 0.44 24.35 ? 114 GLN A CG  1 
ATOM   967  C CD  A GLN A 1 114 ? 7.075   -6.813  30.270 0.56 27.33 ? 114 GLN A CD  1 
ATOM   968  C CD  B GLN A 1 114 ? 10.196  -6.245  31.051 0.44 23.63 ? 114 GLN A CD  1 
ATOM   969  O OE1 A GLN A 1 114 ? 6.275   -6.374  31.094 0.56 30.52 ? 114 GLN A OE1 1 
ATOM   970  O OE1 B GLN A 1 114 ? 10.869  -7.154  30.570 0.44 30.68 ? 114 GLN A OE1 1 
ATOM   971  N NE2 A GLN A 1 114 ? 6.755   -7.771  29.403 0.56 26.32 ? 114 GLN A NE2 1 
ATOM   972  N NE2 B GLN A 1 114 ? 10.424  -5.753  32.262 0.44 28.44 ? 114 GLN A NE2 1 
ATOM   973  N N   . PRO A 1 115 ? 7.862   -2.687  28.723 1.00 18.87 ? 115 PRO A N   1 
ATOM   974  C CA  . PRO A 1 115 ? 8.249   -1.280  28.849 1.00 18.14 ? 115 PRO A CA  1 
ATOM   975  C C   . PRO A 1 115 ? 9.333   -1.088  29.895 1.00 22.10 ? 115 PRO A C   1 
ATOM   976  O O   . PRO A 1 115 ? 9.539   -1.925  30.775 1.00 22.51 ? 115 PRO A O   1 
ATOM   977  C CB  . PRO A 1 115 ? 6.955   -0.577  29.273 1.00 23.76 ? 115 PRO A CB  1 
ATOM   978  C CG  . PRO A 1 115 ? 6.061   -1.647  29.768 1.00 26.08 ? 115 PRO A CG  1 
ATOM   979  C CD  . PRO A 1 115 ? 6.498   -2.956  29.204 1.00 22.38 ? 115 PRO A CD  1 
ATOM   980  N N   . TYR A 1 116 ? 10.027  0.047   29.778 1.00 18.47 ? 116 TYR A N   1 
ATOM   981  C CA  . TYR A 1 116 ? 11.017  0.488   30.763 1.00 18.22 ? 116 TYR A CA  1 
ATOM   982  C C   . TYR A 1 116 ? 12.146  -0.527  30.917 1.00 20.12 ? 116 TYR A C   1 
ATOM   983  O O   . TYR A 1 116 ? 12.648  -0.771  32.019 1.00 20.32 ? 116 TYR A O   1 
ATOM   984  C CB  . TYR A 1 116 ? 10.351  0.784   32.109 1.00 17.77 ? 116 TYR A CB  1 
ATOM   985  C CG  . TYR A 1 116 ? 9.187   1.724   31.984 1.00 19.88 ? 116 TYR A CG  1 
ATOM   986  C CD1 . TYR A 1 116 ? 9.341   2.990   31.423 1.00 19.54 ? 116 TYR A CD1 1 
ATOM   987  C CD2 . TYR A 1 116 ? 7.926   1.339   32.404 1.00 26.20 ? 116 TYR A CD2 1 
ATOM   988  C CE1 . TYR A 1 116 ? 8.256   3.854   31.303 1.00 22.76 ? 116 TYR A CE1 1 
ATOM   989  C CE2 . TYR A 1 116 ? 6.843   2.181   32.286 1.00 24.84 ? 116 TYR A CE2 1 
ATOM   990  C CZ  . TYR A 1 116 ? 7.009   3.438   31.740 1.00 27.78 ? 116 TYR A CZ  1 
ATOM   991  O OH  . TYR A 1 116 ? 5.914   4.261   31.628 1.00 30.36 ? 116 TYR A OH  1 
ATOM   992  N N   . ASN A 1 117 ? 12.567  -1.099  29.790 1.00 14.78 ? 117 ASN A N   1 
ATOM   993  C CA  . ASN A 1 117 ? 13.546  -2.189  29.777 1.00 17.09 ? 117 ASN A CA  1 
ATOM   994  C C   . ASN A 1 117 ? 14.381  -2.009  28.510 1.00 14.90 ? 117 ASN A C   1 
ATOM   995  O O   . ASN A 1 117 ? 13.948  -2.380  27.415 1.00 16.88 ? 117 ASN A O   1 
ATOM   996  C CB  . ASN A 1 117 ? 12.841  -3.544  29.828 1.00 19.89 ? 117 ASN A CB  1 
ATOM   997  C CG  . ASN A 1 117 ? 13.804  -4.718  29.914 1.00 19.90 ? 117 ASN A CG  1 
ATOM   998  O OD1 . ASN A 1 117 ? 14.906  -4.678  29.382 1.00 20.20 ? 117 ASN A OD1 1 
ATOM   999  N ND2 . ASN A 1 117 ? 13.364  -5.795  30.559 1.00 24.97 ? 117 ASN A ND2 1 
ATOM   1000 N N   . GLU A 1 118 ? 15.566  -1.424  28.667 1.00 16.62 ? 118 GLU A N   1 
ATOM   1001 C CA  . GLU A 1 118 ? 16.413  -1.136  27.514 1.00 16.80 ? 118 GLU A CA  1 
ATOM   1002 C C   . GLU A 1 118 ? 16.738  -2.406  26.733 1.00 14.16 ? 118 GLU A C   1 
ATOM   1003 O O   . GLU A 1 118 ? 16.580  -2.456  25.509 1.00 15.53 ? 118 GLU A O   1 
ATOM   1004 C CB  . GLU A 1 118 ? 17.689  -0.432  27.981 1.00 14.24 ? 118 GLU A CB  1 
ATOM   1005 C CG  . GLU A 1 118 ? 18.673  -0.154  26.863 1.00 16.40 ? 118 GLU A CG  1 
ATOM   1006 C CD  . GLU A 1 118 ? 19.773  0.799   27.291 1.00 18.39 ? 118 GLU A CD  1 
ATOM   1007 O OE1 . GLU A 1 118 ? 19.461  1.935   27.714 1.00 20.54 ? 118 GLU A OE1 1 
ATOM   1008 O OE2 . GLU A 1 118 ? 20.952  0.414   27.201 1.00 17.38 ? 118 GLU A OE2 1 
ATOM   1009 N N   . GLY A 1 119 ? 17.186  -3.449  27.427 1.00 17.93 ? 119 GLY A N   1 
ATOM   1010 C CA  . GLY A 1 119 ? 17.594  -4.663  26.741 1.00 13.96 ? 119 GLY A CA  1 
ATOM   1011 C C   . GLY A 1 119 ? 16.476  -5.308  25.945 1.00 14.56 ? 119 GLY A C   1 
ATOM   1012 O O   . GLY A 1 119 ? 16.708  -5.829  24.854 1.00 16.19 ? 119 GLY A O   1 
ATOM   1013 N N   . ALA A 1 120 ? 15.251  -5.293  26.484 1.00 15.19 ? 120 ALA A N   1 
ATOM   1014 C CA  . ALA A 1 120 ? 14.124  -5.865  25.751 1.00 14.00 ? 120 ALA A CA  1 
ATOM   1015 C C   . ALA A 1 120 ? 13.895  -5.111  24.448 1.00 15.77 ? 120 ALA A C   1 
ATOM   1016 O O   . ALA A 1 120 ? 13.606  -5.718  23.411 1.00 15.80 ? 120 ALA A O   1 
ATOM   1017 C CB  . ALA A 1 120 ? 12.861  -5.842  26.611 1.00 18.00 ? 120 ALA A CB  1 
ATOM   1018 N N   . LEU A 1 121 ? 14.040  -3.785  24.483 1.00 16.63 ? 121 LEU A N   1 
ATOM   1019 C CA  . LEU A 1 121 ? 13.896  -3.001  23.262 1.00 12.71 ? 121 LEU A CA  1 
ATOM   1020 C C   . LEU A 1 121 ? 15.004  -3.311  22.263 1.00 16.49 ? 121 LEU A C   1 
ATOM   1021 O O   . LEU A 1 121 ? 14.729  -3.499  21.070 1.00 14.42 ? 121 LEU A O   1 
ATOM   1022 C CB  . LEU A 1 121 ? 13.870  -1.515  23.598 1.00 12.44 ? 121 LEU A CB  1 
ATOM   1023 C CG  . LEU A 1 121 ? 13.702  -0.621  22.369 1.00 13.08 ? 121 LEU A CG  1 
ATOM   1024 C CD1 . LEU A 1 121 ? 12.445  -0.993  21.599 1.00 14.99 ? 121 LEU A CD1 1 
ATOM   1025 C CD2 . LEU A 1 121 ? 13.640  0.837   22.787 1.00 16.41 ? 121 LEU A CD2 1 
ATOM   1026 N N   . LEU A 1 122 ? 16.261  -3.383  22.728 1.00 13.38 ? 122 LEU A N   1 
ATOM   1027 C CA  . LEU A 1 122 ? 17.349  -3.728  21.829 1.00 14.13 ? 122 LEU A CA  1 
ATOM   1028 C C   . LEU A 1 122 ? 17.128  -5.099  21.211 1.00 13.64 ? 122 LEU A C   1 
ATOM   1029 O O   . LEU A 1 122 ? 17.354  -5.290  20.013 1.00 13.45 ? 122 LEU A O   1 
ATOM   1030 C CB  . LEU A 1 122 ? 18.680  -3.681  22.584 1.00 14.58 ? 122 LEU A CB  1 
ATOM   1031 C CG  . LEU A 1 122 ? 19.034  -2.323  23.179 1.00 14.74 ? 122 LEU A CG  1 
ATOM   1032 C CD1 . LEU A 1 122 ? 20.408  -2.395  23.860 1.00 13.06 ? 122 LEU A CD1 1 
ATOM   1033 C CD2 . LEU A 1 122 ? 19.058  -1.242  22.104 1.00 17.18 ? 122 LEU A CD2 1 
ATOM   1034 N N   . TYR A 1 123 ? 16.662  -6.061  22.014 1.00 13.35 ? 123 TYR A N   1 
ATOM   1035 C CA  . TYR A 1 123 ? 16.385  -7.387  21.476 1.00 14.88 ? 123 TYR A CA  1 
ATOM   1036 C C   . TYR A 1 123 ? 15.365  -7.321  20.345 1.00 13.83 ? 123 TYR A C   1 
ATOM   1037 O O   . TYR A 1 123 ? 15.546  -7.953  19.298 1.00 15.21 ? 123 TYR A O   1 
ATOM   1038 C CB  . TYR A 1 123 ? 15.886  -8.314  22.588 1.00 14.79 ? 123 TYR A CB  1 
ATOM   1039 C CG  . TYR A 1 123 ? 15.579  -9.706  22.097 1.00 19.53 ? 123 TYR A CG  1 
ATOM   1040 C CD1 . TYR A 1 123 ? 16.603  -10.621 21.899 1.00 22.71 ? 123 TYR A CD1 1 
ATOM   1041 C CD2 . TYR A 1 123 ? 14.273  -10.110 21.829 1.00 19.99 ? 123 TYR A CD2 1 
ATOM   1042 C CE1 . TYR A 1 123 ? 16.343  -11.897 21.450 1.00 31.40 ? 123 TYR A CE1 1 
ATOM   1043 C CE2 . TYR A 1 123 ? 14.009  -11.388 21.378 1.00 23.63 ? 123 TYR A CE2 1 
ATOM   1044 C CZ  . TYR A 1 123 ? 15.046  -12.275 21.193 1.00 29.87 ? 123 TYR A CZ  1 
ATOM   1045 O OH  . TYR A 1 123 ? 14.791  -13.550 20.741 1.00 36.97 ? 123 TYR A OH  1 
ATOM   1046 N N   . SER A 1 124 ? 14.309  -6.537  20.523 1.00 15.66 ? 124 SER A N   1 
ATOM   1047 C CA  . SER A 1 124 ? 13.313  -6.429  19.462 1.00 17.22 ? 124 SER A CA  1 
ATOM   1048 C C   . SER A 1 124 ? 13.885  -5.747  18.222 1.00 14.18 ? 124 SER A C   1 
ATOM   1049 O O   . SER A 1 124 ? 13.605  -6.172  17.098 1.00 16.44 ? 124 SER A O   1 
ATOM   1050 C CB  . SER A 1 124 ? 12.085  -5.682  19.975 1.00 14.62 ? 124 SER A CB  1 
ATOM   1051 O OG  . SER A 1 124 ? 11.470  -6.368  21.056 1.00 25.28 ? 124 SER A OG  1 
ATOM   1052 N N   . ILE A 1 125 ? 14.693  -4.694  18.404 1.00 13.02 ? 125 ILE A N   1 
ATOM   1053 C CA  . ILE A 1 125 ? 15.269  -3.980  17.265 1.00 13.12 ? 125 ILE A CA  1 
ATOM   1054 C C   . ILE A 1 125 ? 16.212  -4.875  16.478 1.00 15.64 ? 125 ILE A C   1 
ATOM   1055 O O   . ILE A 1 125 ? 16.312  -4.773  15.250 1.00 16.37 ? 125 ILE A O   1 
ATOM   1056 C CB  . ILE A 1 125 ? 15.984  -2.703  17.743 1.00 14.32 ? 125 ILE A CB  1 
ATOM   1057 C CG1 . ILE A 1 125 ? 15.019  -1.728  18.418 1.00 14.80 ? 125 ILE A CG1 1 
ATOM   1058 C CG2 . ILE A 1 125 ? 16.799  -2.061  16.595 1.00 16.55 ? 125 ILE A CG2 1 
ATOM   1059 C CD1 . ILE A 1 125 ? 15.741  -0.587  19.145 1.00 13.72 ? 125 ILE A CD1 1 
ATOM   1060 N N   . ALA A 1 126 ? 16.930  -5.764  17.167 1.00 13.44 ? 126 ALA A N   1 
ATOM   1061 C CA  . ALA A 1 126 ? 17.782  -6.696  16.452 1.00 14.00 ? 126 ALA A CA  1 
ATOM   1062 C C   . ALA A 1 126 ? 16.972  -7.598  15.537 1.00 15.95 ? 126 ALA A C   1 
ATOM   1063 O O   . ALA A 1 126 ? 17.514  -8.121  14.562 1.00 17.76 ? 126 ALA A O   1 
ATOM   1064 C CB  . ALA A 1 126 ? 18.598  -7.521  17.453 1.00 16.86 ? 126 ALA A CB  1 
ATOM   1065 N N   . ASN A 1 127 ? 15.686  -7.770  15.809 1.00 16.09 ? 127 ASN A N   1 
ATOM   1066 C CA  . ASN A 1 127 ? 14.873  -8.617  14.958 1.00 15.17 ? 127 ASN A CA  1 
ATOM   1067 C C   . ASN A 1 127 ? 14.087  -7.854  13.907 1.00 18.41 ? 127 ASN A C   1 
ATOM   1068 O O   . ASN A 1 127 ? 13.851  -8.414  12.834 1.00 16.26 ? 127 ASN A O   1 
ATOM   1069 C CB  . ASN A 1 127 ? 13.929  -9.481  15.799 1.00 18.98 ? 127 ASN A CB  1 
ATOM   1070 C CG  . ASN A 1 127 ? 14.676  -10.586 16.527 1.00 26.72 ? 127 ASN A CG  1 
ATOM   1071 O OD1 . ASN A 1 127 ? 15.079  -11.575 15.912 1.00 33.21 ? 127 ASN A OD1 1 
ATOM   1072 N ND2 . ASN A 1 127 ? 14.877  -10.422 17.834 1.00 35.66 ? 127 ASN A ND2 1 
ATOM   1073 N N   . GLN A 1 128 ? 13.743  -6.589  14.142 1.00 14.73 ? 128 GLN A N   1 
ATOM   1074 C CA  . GLN A 1 128 ? 12.947  -5.832  13.177 1.00 16.32 ? 128 GLN A CA  1 
ATOM   1075 C C   . GLN A 1 128 ? 12.822  -4.390  13.657 1.00 15.58 ? 128 GLN A C   1 
ATOM   1076 O O   . GLN A 1 128 ? 12.977  -4.121  14.844 1.00 15.66 ? 128 GLN A O   1 
ATOM   1077 C CB  . GLN A 1 128 ? 11.546  -6.435  13.013 1.00 16.03 ? 128 GLN A CB  1 
ATOM   1078 C CG  . GLN A 1 128 ? 10.725  -6.290  14.271 1.00 15.88 ? 128 GLN A CG  1 
ATOM   1079 C CD  . GLN A 1 128 ? 9.572   -7.215  14.278 1.00 21.04 ? 128 GLN A CD  1 
ATOM   1080 O OE1 . GLN A 1 128 ? 9.589   -8.235  14.968 1.00 23.91 ? 128 GLN A OE1 1 
ATOM   1081 N NE2 . GLN A 1 128 ? 8.532   -6.871  13.514 1.00 22.64 ? 128 GLN A NE2 1 
ATOM   1082 N N   . PRO A 1 129 ? 12.491  -3.461  12.755 1.00 13.53 ? 129 PRO A N   1 
ATOM   1083 C CA  . PRO A 1 129 ? 12.152  -2.106  13.200 1.00 13.34 ? 129 PRO A CA  1 
ATOM   1084 C C   . PRO A 1 129 ? 10.974  -2.117  14.173 1.00 14.63 ? 129 PRO A C   1 
ATOM   1085 O O   . PRO A 1 129 ? 10.017  -2.887  14.027 1.00 14.84 ? 129 PRO A O   1 
ATOM   1086 C CB  . PRO A 1 129 ? 11.809  -1.381  11.896 1.00 13.01 ? 129 PRO A CB  1 
ATOM   1087 C CG  . PRO A 1 129 ? 12.606  -2.092  10.863 1.00 14.17 ? 129 PRO A CG  1 
ATOM   1088 C CD  . PRO A 1 129 ? 12.515  -3.555  11.286 1.00 15.93 ? 129 PRO A CD  1 
ATOM   1089 N N   . VAL A 1 130 ? 11.057  -1.255  15.188 1.00 13.64 ? 130 VAL A N   1 
ATOM   1090 C CA  . VAL A 1 130 ? 10.094  -1.209  16.286 1.00 12.34 ? 130 VAL A CA  1 
ATOM   1091 C C   . VAL A 1 130 ? 9.497   0.191   16.371 1.00 13.69 ? 130 VAL A C   1 
ATOM   1092 O O   . VAL A 1 130 ? 10.205  1.192   16.221 1.00 14.31 ? 130 VAL A O   1 
ATOM   1093 C CB  . VAL A 1 130 ? 10.767  -1.605  17.617 1.00 12.65 ? 130 VAL A CB  1 
ATOM   1094 C CG1 . VAL A 1 130 ? 9.780   -1.502  18.774 1.00 12.58 ? 130 VAL A CG1 1 
ATOM   1095 C CG2 . VAL A 1 130 ? 11.323  -3.021  17.515 1.00 15.16 ? 130 VAL A CG2 1 
ATOM   1096 N N   . SER A 1 131 ? 8.187   0.262   16.602 1.00 11.91 ? 131 SER A N   1 
ATOM   1097 C CA  . SER A 1 131 ? 7.539   1.540   16.883 1.00 11.24 ? 131 SER A CA  1 
ATOM   1098 C C   . SER A 1 131 ? 7.796   1.949   18.331 1.00 14.30 ? 131 SER A C   1 
ATOM   1099 O O   . SER A 1 131 ? 7.505   1.185   19.245 1.00 15.09 ? 131 SER A O   1 
ATOM   1100 C CB  . SER A 1 131 ? 6.037   1.432   16.634 1.00 12.53 ? 131 SER A CB  1 
ATOM   1101 O OG  . SER A 1 131 ? 5.365   2.576   17.139 1.00 14.43 ? 131 SER A OG  1 
ATOM   1102 N N   . VAL A 1 132 ? 8.327   3.154   18.544 1.00 12.90 ? 132 VAL A N   1 
ATOM   1103 C CA  . VAL A 1 132 ? 8.653   3.648   19.879 1.00 15.66 ? 132 VAL A CA  1 
ATOM   1104 C C   . VAL A 1 132 ? 8.132   5.070   20.017 1.00 13.34 ? 132 VAL A C   1 
ATOM   1105 O O   . VAL A 1 132 ? 7.795   5.728   19.030 1.00 14.79 ? 132 VAL A O   1 
ATOM   1106 C CB  . VAL A 1 132 ? 10.171  3.603   20.186 1.00 15.53 ? 132 VAL A CB  1 
ATOM   1107 C CG1 . VAL A 1 132 ? 10.704  2.173   20.039 1.00 14.23 ? 132 VAL A CG1 1 
ATOM   1108 C CG2 . VAL A 1 132 ? 10.938  4.575   19.284 1.00 14.22 ? 132 VAL A CG2 1 
ATOM   1109 N N   . VAL A 1 133 ? 8.048   5.545   21.266 1.00 13.44 ? 133 VAL A N   1 
ATOM   1110 C CA  . VAL A 1 133 ? 7.589   6.904   21.526 1.00 13.57 ? 133 VAL A CA  1 
ATOM   1111 C C   . VAL A 1 133 ? 8.631   7.651   22.349 1.00 14.35 ? 133 VAL A C   1 
ATOM   1112 O O   . VAL A 1 133 ? 9.451   7.063   23.064 1.00 13.76 ? 133 VAL A O   1 
ATOM   1113 C CB  . VAL A 1 133 ? 6.212   6.940   22.223 1.00 13.36 ? 133 VAL A CB  1 
ATOM   1114 C CG1 . VAL A 1 133 ? 5.169   6.277   21.346 1.00 15.16 ? 133 VAL A CG1 1 
ATOM   1115 C CG2 . VAL A 1 133 ? 6.266   6.235   23.577 1.00 16.09 ? 133 VAL A CG2 1 
ATOM   1116 N N   . LEU A 1 134 ? 8.597   8.974   22.233 1.00 14.14 ? 134 LEU A N   1 
ATOM   1117 C CA  . LEU A 1 134 ? 9.507   9.803   22.997 1.00 14.97 ? 134 LEU A CA  1 
ATOM   1118 C C   . LEU A 1 134 ? 8.891   11.181  23.185 1.00 13.80 ? 134 LEU A C   1 
ATOM   1119 O O   . LEU A 1 134 ? 7.880   11.523  22.571 1.00 13.22 ? 134 LEU A O   1 
ATOM   1120 C CB  . LEU A 1 134 ? 10.883  9.903   22.319 1.00 14.54 ? 134 LEU A CB  1 
ATOM   1121 C CG  . LEU A 1 134 ? 10.883  10.230  20.819 1.00 15.99 ? 134 LEU A CG  1 
ATOM   1122 C CD1 . LEU A 1 134 ? 10.615  11.698  20.528 1.00 15.98 ? 134 LEU A CD1 1 
ATOM   1123 C CD2 . LEU A 1 134 ? 12.219  9.803   20.220 1.00 16.71 ? 134 LEU A CD2 1 
ATOM   1124 N N   . GLU A 1 135 ? 9.533   11.977  24.035 1.00 13.98 ? 135 GLU A N   1 
ATOM   1125 C CA  . GLU A 1 135 ? 9.186   13.382  24.226 1.00 11.90 ? 135 GLU A CA  1 
ATOM   1126 C C   . GLU A 1 135 ? 9.899   14.246  23.195 1.00 12.29 ? 135 GLU A C   1 
ATOM   1127 O O   . GLU A 1 135 ? 11.120  14.435  23.268 1.00 15.38 ? 135 GLU A O   1 
ATOM   1128 C CB  . GLU A 1 135 ? 9.570   13.833  25.629 1.00 13.03 ? 135 GLU A CB  1 
ATOM   1129 C CG  . GLU A 1 135 ? 9.029   15.199  25.966 1.00 16.26 ? 135 GLU A CG  1 
ATOM   1130 C CD  . GLU A 1 135 ? 9.772   15.828  27.130 1.00 19.42 ? 135 GLU A CD  1 
ATOM   1131 O OE1 . GLU A 1 135 ? 9.335   15.552  28.262 1.00 18.33 ? 135 GLU A OE1 1 
ATOM   1132 O OE2 . GLU A 1 135 ? 10.761  16.588  26.932 1.00 20.45 ? 135 GLU A OE2 1 
ATOM   1133 N N   . ALA A 1 136 ? 9.133   14.824  22.273 1.00 14.65 ? 136 ALA A N   1 
ATOM   1134 C CA  . ALA A 1 136 ? 9.678   15.668  21.222 1.00 15.56 ? 136 ALA A CA  1 
ATOM   1135 C C   . ALA A 1 136 ? 9.395   17.153  21.404 1.00 14.24 ? 136 ALA A C   1 
ATOM   1136 O O   . ALA A 1 136 ? 9.856   17.953  20.582 1.00 19.97 ? 136 ALA A O   1 
ATOM   1137 C CB  . ALA A 1 136 ? 9.118   15.221  19.868 1.00 17.14 ? 136 ALA A CB  1 
ATOM   1138 N N   . ALA A 1 137 ? 8.647   17.545  22.435 1.00 16.33 ? 137 ALA A N   1 
ATOM   1139 C CA  . ALA A 1 137 ? 8.203   18.934  22.549 1.00 18.76 ? 137 ALA A CA  1 
ATOM   1140 C C   . ALA A 1 137 ? 9.339   19.883  22.909 1.00 21.59 ? 137 ALA A C   1 
ATOM   1141 O O   . ALA A 1 137 ? 9.257   21.079  22.611 1.00 19.37 ? 137 ALA A O   1 
ATOM   1142 C CB  . ALA A 1 137 ? 7.086   19.049  23.589 1.00 23.21 ? 137 ALA A CB  1 
ATOM   1143 N N   . GLY A 1 138 ? 10.393  19.389  23.547 1.00 18.37 ? 138 GLY A N   1 
ATOM   1144 C CA  . GLY A 1 138 ? 11.464  20.269  23.973 1.00 16.63 ? 138 GLY A CA  1 
ATOM   1145 C C   . GLY A 1 138 ? 12.220  20.864  22.803 1.00 17.12 ? 138 GLY A C   1 
ATOM   1146 O O   . GLY A 1 138 ? 12.395  20.243  21.756 1.00 16.93 ? 138 GLY A O   1 
ATOM   1147 N N   . LYS A 1 139 ? 12.707  22.088  22.994 1.00 16.26 ? 139 LYS A N   1 
ATOM   1148 C CA  . LYS A 1 139 ? 13.375  22.766  21.894 1.00 17.22 ? 139 LYS A CA  1 
ATOM   1149 C C   . LYS A 1 139 ? 14.697  22.083  21.541 1.00 16.54 ? 139 LYS A C   1 
ATOM   1150 O O   . LYS A 1 139 ? 15.123  22.125  20.387 1.00 14.86 ? 139 LYS A O   1 
ATOM   1151 C CB  . LYS A 1 139 ? 13.547  24.249  22.247 1.00 20.90 ? 139 LYS A CB  1 
ATOM   1152 C CG  . LYS A 1 139 ? 14.654  24.985  21.553 1.00 29.76 ? 139 LYS A CG  1 
ATOM   1153 C CD  . LYS A 1 139 ? 14.584  26.479  21.885 1.00 37.20 ? 139 LYS A CD  1 
ATOM   1154 C CE  . LYS A 1 139 ? 15.880  27.204  21.539 1.00 31.98 ? 139 LYS A CE  1 
ATOM   1155 N NZ  . LYS A 1 139 ? 15.844  28.653  21.895 1.00 46.65 ? 139 LYS A NZ  1 
ATOM   1156 N N   . ASP A 1 140 ? 15.338  21.406  22.498 1.00 16.14 ? 140 ASP A N   1 
ATOM   1157 C CA  . ASP A 1 140 ? 16.561  20.676  22.161 1.00 13.57 ? 140 ASP A CA  1 
ATOM   1158 C C   . ASP A 1 140 ? 16.290  19.579  21.138 1.00 14.07 ? 140 ASP A C   1 
ATOM   1159 O O   . ASP A 1 140 ? 17.067  19.394  20.196 1.00 16.26 ? 140 ASP A O   1 
ATOM   1160 C CB  . ASP A 1 140 ? 17.188  20.084  23.416 1.00 15.26 ? 140 ASP A CB  1 
ATOM   1161 C CG  . ASP A 1 140 ? 17.678  21.142  24.358 1.00 16.29 ? 140 ASP A CG  1 
ATOM   1162 O OD1 . ASP A 1 140 ? 18.779  21.655  24.123 1.00 19.46 ? 140 ASP A OD1 1 
ATOM   1163 O OD2 . ASP A 1 140 ? 16.947  21.472  25.309 1.00 17.74 ? 140 ASP A OD2 1 
ATOM   1164 N N   . PHE A 1 141 ? 15.192  18.839  21.304 1.00 13.97 ? 141 PHE A N   1 
ATOM   1165 C CA  . PHE A 1 141 ? 14.856  17.834  20.306 1.00 12.67 ? 141 PHE A CA  1 
ATOM   1166 C C   . PHE A 1 141 ? 14.454  18.492  18.991 1.00 15.96 ? 141 PHE A C   1 
ATOM   1167 O O   . PHE A 1 141 ? 14.846  18.032  17.915 1.00 17.40 ? 141 PHE A O   1 
ATOM   1168 C CB  . PHE A 1 141 ? 13.737  16.928  20.839 1.00 15.07 ? 141 PHE A CB  1 
ATOM   1169 C CG  . PHE A 1 141 ? 13.429  15.754  19.954 1.00 15.58 ? 141 PHE A CG  1 
ATOM   1170 C CD1 . PHE A 1 141 ? 12.553  15.884  18.884 1.00 17.34 ? 141 PHE A CD1 1 
ATOM   1171 C CD2 . PHE A 1 141 ? 14.015  14.521  20.189 1.00 17.57 ? 141 PHE A CD2 1 
ATOM   1172 C CE1 . PHE A 1 141 ? 12.268  14.803  18.063 1.00 17.56 ? 141 PHE A CE1 1 
ATOM   1173 C CE2 . PHE A 1 141 ? 13.745  13.439  19.362 1.00 12.98 ? 141 PHE A CE2 1 
ATOM   1174 C CZ  . PHE A 1 141 ? 12.875  13.579  18.308 1.00 16.34 ? 141 PHE A CZ  1 
ATOM   1175 N N   . GLN A 1 142 ? 13.658  19.562  19.055 1.00 16.05 ? 142 GLN A N   1 
ATOM   1176 C CA  . GLN A 1 142 ? 13.191  20.193  17.825 1.00 17.66 ? 142 GLN A CA  1 
ATOM   1177 C C   . GLN A 1 142 ? 14.356  20.701  16.984 1.00 17.28 ? 142 GLN A C   1 
ATOM   1178 O O   . GLN A 1 142 ? 14.354  20.564  15.753 1.00 20.57 ? 142 GLN A O   1 
ATOM   1179 C CB  . GLN A 1 142 ? 12.216  21.327  18.148 1.00 16.05 ? 142 GLN A CB  1 
ATOM   1180 C CG  . GLN A 1 142 ? 11.005  20.879  18.944 1.00 23.18 ? 142 GLN A CG  1 
ATOM   1181 C CD  . GLN A 1 142 ? 9.765   20.713  18.094 1.00 28.33 ? 142 GLN A CD  1 
ATOM   1182 O OE1 . GLN A 1 142 ? 9.637   21.328  17.036 1.00 36.03 ? 142 GLN A OE1 1 
ATOM   1183 N NE2 . GLN A 1 142 ? 8.848   19.857  18.545 1.00 30.08 ? 142 GLN A NE2 1 
ATOM   1184 N N   . LEU A 1 143 ? 15.375  21.259  17.630 1.00 17.78 ? 143 LEU A N   1 
ATOM   1185 C CA  . LEU A 1 143 ? 16.499  21.869  16.939 1.00 19.34 ? 143 LEU A CA  1 
ATOM   1186 C C   . LEU A 1 143 ? 17.633  20.896  16.662 1.00 19.98 ? 143 LEU A C   1 
ATOM   1187 O O   . LEU A 1 143 ? 18.667  21.318  16.136 1.00 22.25 ? 143 LEU A O   1 
ATOM   1188 C CB  . LEU A 1 143 ? 17.039  23.052  17.753 1.00 19.28 ? 143 LEU A CB  1 
ATOM   1189 C CG  . LEU A 1 143 ? 16.093  24.221  18.005 1.00 24.90 ? 143 LEU A CG  1 
ATOM   1190 C CD1 . LEU A 1 143 ? 16.862  25.302  18.728 1.00 32.17 ? 143 LEU A CD1 1 
ATOM   1191 C CD2 . LEU A 1 143 ? 15.540  24.747  16.697 1.00 24.56 ? 143 LEU A CD2 1 
ATOM   1192 N N   . TYR A 1 144 ? 17.478  19.623  17.020 1.00 16.52 ? 144 TYR A N   1 
ATOM   1193 C CA  . TYR A 1 144 ? 18.554  18.653  16.862 1.00 15.64 ? 144 TYR A CA  1 
ATOM   1194 C C   . TYR A 1 144 ? 19.129  18.680  15.450 1.00 14.52 ? 144 TYR A C   1 
ATOM   1195 O O   . TYR A 1 144 ? 18.389  18.638  14.460 1.00 17.36 ? 144 TYR A O   1 
ATOM   1196 C CB  . TYR A 1 144 ? 18.021  17.258  17.193 1.00 14.46 ? 144 TYR A CB  1 
ATOM   1197 C CG  . TYR A 1 144 ? 18.971  16.137  16.841 1.00 12.72 ? 144 TYR A CG  1 
ATOM   1198 C CD1 . TYR A 1 144 ? 20.034  15.809  17.672 1.00 14.24 ? 144 TYR A CD1 1 
ATOM   1199 C CD2 . TYR A 1 144 ? 18.773  15.374  15.696 1.00 15.48 ? 144 TYR A CD2 1 
ATOM   1200 C CE1 . TYR A 1 144 ? 20.886  14.774  17.359 1.00 13.71 ? 144 TYR A CE1 1 
ATOM   1201 C CE2 . TYR A 1 144 ? 19.619  14.346  15.375 1.00 12.75 ? 144 TYR A CE2 1 
ATOM   1202 C CZ  . TYR A 1 144 ? 20.671  14.044  16.207 1.00 13.56 ? 144 TYR A CZ  1 
ATOM   1203 O OH  . TYR A 1 144 ? 21.490  12.994  15.871 1.00 14.09 ? 144 TYR A OH  1 
ATOM   1204 N N   . ARG A 1 145 ? 20.459  18.734  15.367 1.00 17.60 ? 145 ARG A N   1 
ATOM   1205 C CA  . ARG A 1 145 ? 21.158  18.688  14.087 1.00 17.56 ? 145 ARG A CA  1 
ATOM   1206 C C   . ARG A 1 145 ? 22.019  17.456  13.891 1.00 16.10 ? 145 ARG A C   1 
ATOM   1207 O O   . ARG A 1 145 ? 22.233  17.058  12.747 1.00 24.02 ? 145 ARG A O   1 
ATOM   1208 C CB  . ARG A 1 145 ? 22.034  19.935  13.884 1.00 21.61 ? 145 ARG A CB  1 
ATOM   1209 C CG  . ARG A 1 145 ? 21.269  21.245  13.902 1.00 25.20 ? 145 ARG A CG  1 
ATOM   1210 C CD  . ARG A 1 145 ? 22.210  22.443  13.848 1.00 36.03 ? 145 ARG A CD  1 
ATOM   1211 N NE  . ARG A 1 145 ? 22.695  22.827  15.167 1.00 55.88 ? 145 ARG A NE  1 
ATOM   1212 C CZ  . ARG A 1 145 ? 23.245  24.001  15.449 1.00 62.12 ? 145 ARG A CZ  1 
ATOM   1213 N NH1 . ARG A 1 145 ? 23.407  24.930  14.519 1.00 63.79 ? 145 ARG A NH1 1 
ATOM   1214 N NH2 . ARG A 1 145 ? 23.636  24.251  16.695 1.00 54.40 ? 145 ARG A NH2 1 
ATOM   1215 N N   . GLY A 1 146 ? 22.519  16.840  14.948 1.00 15.23 ? 146 GLY A N   1 
ATOM   1216 C CA  . GLY A 1 146 ? 23.347  15.665  14.766 1.00 14.05 ? 146 GLY A CA  1 
ATOM   1217 C C   . GLY A 1 146 ? 24.093  15.328  16.032 1.00 13.88 ? 146 GLY A C   1 
ATOM   1218 O O   . GLY A 1 146 ? 24.121  16.096  16.995 1.00 17.22 ? 146 GLY A O   1 
ATOM   1219 N N   . GLY A 1 147 ? 24.709  14.151  16.007 1.00 16.43 ? 147 GLY A N   1 
ATOM   1220 C CA  . GLY A 1 147 ? 25.387  13.627  17.171 1.00 13.71 ? 147 GLY A CA  1 
ATOM   1221 C C   . GLY A 1 147 ? 24.491  12.707  17.973 1.00 15.11 ? 147 GLY A C   1 
ATOM   1222 O O   . GLY A 1 147 ? 23.329  12.452  17.651 1.00 15.76 ? 147 GLY A O   1 
ATOM   1223 N N   . ILE A 1 148 ? 25.049  12.175  19.049 1.00 14.72 ? 148 ILE A N   1 
ATOM   1224 C CA  . ILE A 1 148 ? 24.297  11.299  19.932 1.00 13.98 ? 148 ILE A CA  1 
ATOM   1225 C C   . ILE A 1 148 ? 23.556  12.196  20.917 1.00 15.74 ? 148 ILE A C   1 
ATOM   1226 O O   . ILE A 1 148 ? 24.173  12.884  21.738 1.00 20.40 ? 148 ILE A O   1 
ATOM   1227 C CB  . ILE A 1 148 ? 25.215  10.297  20.636 1.00 16.40 ? 148 ILE A CB  1 
ATOM   1228 C CG1 . ILE A 1 148 ? 25.875  9.397   19.585 1.00 22.44 ? 148 ILE A CG1 1 
ATOM   1229 C CG2 . ILE A 1 148 ? 24.415  9.494   21.655 1.00 18.90 ? 148 ILE A CG2 1 
ATOM   1230 C CD1 . ILE A 1 148 ? 26.563  8.186   20.137 1.00 21.76 ? 148 ILE A CD1 1 
ATOM   1231 N N   . PHE A 1 149 ? 22.228  12.198  20.830 1.00 13.26 ? 149 PHE A N   1 
ATOM   1232 C CA  . PHE A 1 149 ? 21.402  13.141  21.569 1.00 11.21 ? 149 PHE A CA  1 
ATOM   1233 C C   . PHE A 1 149 ? 21.183  12.678  23.006 1.00 14.57 ? 149 PHE A C   1 
ATOM   1234 O O   . PHE A 1 149 ? 20.677  11.577  23.247 1.00 15.04 ? 149 PHE A O   1 
ATOM   1235 C CB  . PHE A 1 149 ? 20.066  13.300  20.838 1.00 11.70 ? 149 PHE A CB  1 
ATOM   1236 C CG  . PHE A 1 149 ? 19.143  14.308  21.458 1.00 13.42 ? 149 PHE A CG  1 
ATOM   1237 C CD1 . PHE A 1 149 ? 19.408  15.669  21.319 1.00 15.45 ? 149 PHE A CD1 1 
ATOM   1238 C CD2 . PHE A 1 149 ? 17.994  13.909  22.136 1.00 14.02 ? 149 PHE A CD2 1 
ATOM   1239 C CE1 . PHE A 1 149 ? 18.567  16.617  21.865 1.00 16.95 ? 149 PHE A CE1 1 
ATOM   1240 C CE2 . PHE A 1 149 ? 17.141  14.853  22.689 1.00 15.69 ? 149 PHE A CE2 1 
ATOM   1241 C CZ  . PHE A 1 149 ? 17.428  16.214  22.542 1.00 16.84 ? 149 PHE A CZ  1 
ATOM   1242 N N   . VAL A 1 150 ? 21.518  13.534  23.969 1.00 15.54 ? 150 VAL A N   1 
ATOM   1243 C CA  . VAL A 1 150 ? 21.345  13.211  25.381 1.00 15.92 ? 150 VAL A CA  1 
ATOM   1244 C C   . VAL A 1 150 ? 20.269  14.057  26.026 1.00 16.01 ? 150 VAL A C   1 
ATOM   1245 O O   . VAL A 1 150 ? 20.062  13.958  27.247 1.00 19.28 ? 150 VAL A O   1 
ATOM   1246 C CB  . VAL A 1 150 ? 22.665  13.360  26.161 1.00 16.41 ? 150 VAL A CB  1 
ATOM   1247 C CG1 . VAL A 1 150 ? 23.756  12.496  25.555 1.00 20.30 ? 150 VAL A CG1 1 
ATOM   1248 C CG2 . VAL A 1 150 ? 23.095  14.818  26.194 1.00 20.30 ? 150 VAL A CG2 1 
ATOM   1249 N N   . GLY A 1 151 ? 19.575  14.881  25.252 1.00 15.82 ? 151 GLY A N   1 
ATOM   1250 C CA  . GLY A 1 151 ? 18.684  15.855  25.806 1.00 18.14 ? 151 GLY A CA  1 
ATOM   1251 C C   . GLY A 1 151 ? 19.330  17.226  25.835 1.00 15.32 ? 151 GLY A C   1 
ATOM   1252 O O   . GLY A 1 151 ? 20.264  17.517  25.077 1.00 16.38 ? 151 GLY A O   1 
ATOM   1253 N N   . PRO A 1 152 ? 18.863  18.094  26.736 1.00 15.46 ? 152 PRO A N   1 
ATOM   1254 C CA  . PRO A 1 152 ? 17.844  17.861  27.768 1.00 14.62 ? 152 PRO A CA  1 
ATOM   1255 C C   . PRO A 1 152 ? 16.476  17.489  27.232 1.00 16.43 ? 152 PRO A C   1 
ATOM   1256 O O   . PRO A 1 152 ? 16.081  17.870  26.139 1.00 17.17 ? 152 PRO A O   1 
ATOM   1257 C CB  . PRO A 1 152 ? 17.782  19.210  28.500 1.00 17.68 ? 152 PRO A CB  1 
ATOM   1258 C CG  . PRO A 1 152 ? 19.140  19.791  28.333 1.00 16.69 ? 152 PRO A CG  1 
ATOM   1259 C CD  . PRO A 1 152 ? 19.547  19.384  26.930 1.00 16.60 ? 152 PRO A CD  1 
ATOM   1260 N N   . CYS A 1 153 ? 15.762  16.703  28.019 1.00 15.93 ? 153 CYS A N   1 
ATOM   1261 C CA  . CYS A 1 153 ? 14.385  16.343  27.722 1.00 18.63 ? 153 CYS A CA  1 
ATOM   1262 C C   . CYS A 1 153 ? 13.833  15.619  28.930 1.00 19.07 ? 153 CYS A C   1 
ATOM   1263 O O   . CYS A 1 153 ? 14.581  15.000  29.689 1.00 19.62 ? 153 CYS A O   1 
ATOM   1264 C CB  . CYS A 1 153 ? 14.264  15.457  26.467 1.00 18.97 ? 153 CYS A CB  1 
ATOM   1265 S SG  . CYS A 1 153 ? 15.255  13.937  26.488 1.00 21.11 ? 153 CYS A SG  1 
ATOM   1266 N N   . GLY A 1 154 ? 12.525  15.713  29.102 1.00 16.80 ? 154 GLY A N   1 
ATOM   1267 C CA  . GLY A 1 154 ? 11.816  14.957  30.110 1.00 18.59 ? 154 GLY A CA  1 
ATOM   1268 C C   . GLY A 1 154 ? 11.262  13.677  29.528 1.00 19.15 ? 154 GLY A C   1 
ATOM   1269 O O   . GLY A 1 154 ? 11.655  13.233  28.446 1.00 18.91 ? 154 GLY A O   1 
ATOM   1270 N N   . ASN A 1 155 ? 10.311  13.087  30.250 1.00 19.57 ? 155 ASN A N   1 
ATOM   1271 C CA  . ASN A 1 155 ? 9.738   11.798  29.894 1.00 19.28 ? 155 ASN A CA  1 
ATOM   1272 C C   . ASN A 1 155 ? 8.272   11.897  29.486 1.00 16.20 ? 155 ASN A C   1 
ATOM   1273 O O   . ASN A 1 155 ? 7.583   10.876  29.418 1.00 20.18 ? 155 ASN A O   1 
ATOM   1274 C CB  . ASN A 1 155 ? 9.924   10.811  31.052 1.00 23.37 ? 155 ASN A CB  1 
ATOM   1275 C CG  . ASN A 1 155 ? 8.824   10.922  32.115 1.00 27.73 ? 155 ASN A CG  1 
ATOM   1276 O OD1 . ASN A 1 155 ? 8.323   12.010  32.405 1.00 37.46 ? 155 ASN A OD1 1 
ATOM   1277 N ND2 . ASN A 1 155 ? 8.459   9.796   32.703 1.00 43.64 ? 155 ASN A ND2 1 
ATOM   1278 N N   . LYS A 1 156 ? 7.785   13.097  29.169 1.00 16.72 ? 156 LYS A N   1 
ATOM   1279 C CA  . LYS A 1 156 ? 6.369   13.256  28.824 1.00 18.52 ? 156 LYS A CA  1 
ATOM   1280 C C   . LYS A 1 156 ? 6.195   12.975  27.333 1.00 16.92 ? 156 LYS A C   1 
ATOM   1281 O O   . LYS A 1 156 ? 6.139   13.873  26.490 1.00 18.73 ? 156 LYS A O   1 
ATOM   1282 C CB  . LYS A 1 156 ? 5.817   14.625  29.233 1.00 23.57 ? 156 LYS A CB  1 
ATOM   1283 C CG  . LYS A 1 156 ? 6.183   15.129  30.651 1.00 33.40 ? 156 LYS A CG  1 
ATOM   1284 C CD  . LYS A 1 156 ? 7.564   15.760  30.833 1.00 43.60 ? 156 LYS A CD  1 
ATOM   1285 C CE  . LYS A 1 156 ? 7.684   17.074  30.059 1.00 41.21 ? 156 LYS A CE  1 
ATOM   1286 N NZ  . LYS A 1 156 ? 9.056   17.653  30.175 1.00 37.58 ? 156 LYS A NZ  1 
ATOM   1287 N N   . VAL A 1 157 ? 6.079   11.682  27.015 1.00 17.32 ? 157 VAL A N   1 
ATOM   1288 C CA  . VAL A 1 157 ? 6.125   11.263  25.619 1.00 16.00 ? 157 VAL A CA  1 
ATOM   1289 C C   . VAL A 1 157 ? 4.949   11.839  24.843 1.00 14.72 ? 157 VAL A C   1 
ATOM   1290 O O   . VAL A 1 157 ? 3.822   11.957  25.348 1.00 18.19 ? 157 VAL A O   1 
ATOM   1291 C CB  . VAL A 1 157 ? 6.202   9.730   25.490 1.00 17.62 ? 157 VAL A CB  1 
ATOM   1292 C CG1 . VAL A 1 157 ? 7.497   9.205   26.138 1.00 15.41 ? 157 VAL A CG1 1 
ATOM   1293 C CG2 . VAL A 1 157 ? 4.969   9.042   26.052 1.00 15.44 ? 157 VAL A CG2 1 
ATOM   1294 N N   . ASP A 1 158 ? 5.226   12.238  23.595 1.00 13.49 ? 158 ASP A N   1 
ATOM   1295 C CA  . ASP A 1 158 ? 4.224   12.933  22.796 1.00 14.33 ? 158 ASP A CA  1 
ATOM   1296 C C   . ASP A 1 158 ? 4.410   12.677  21.301 1.00 14.55 ? 158 ASP A C   1 
ATOM   1297 O O   . ASP A 1 158 ? 3.711   13.302  20.495 1.00 14.54 ? 158 ASP A O   1 
ATOM   1298 C CB  . ASP A 1 158 ? 4.289   14.454  23.071 1.00 15.47 ? 158 ASP A CB  1 
ATOM   1299 C CG  . ASP A 1 158 ? 5.658   15.044  22.793 1.00 18.24 ? 158 ASP A CG  1 
ATOM   1300 O OD1 . ASP A 1 158 ? 6.444   14.443  22.037 1.00 17.48 ? 158 ASP A OD1 1 
ATOM   1301 O OD2 . ASP A 1 158 ? 5.960   16.126  23.332 1.00 22.50 ? 158 ASP A OD2 1 
ATOM   1302 N N   . HIS A 1 159 ? 5.318   11.793  20.895 1.00 15.37 ? 159 HIS A N   1 
ATOM   1303 C CA  . HIS A 1 159 ? 5.688   11.713  19.487 1.00 15.40 ? 159 HIS A CA  1 
ATOM   1304 C C   . HIS A 1 159 ? 6.101   10.287  19.182 1.00 13.38 ? 159 HIS A C   1 
ATOM   1305 O O   . HIS A 1 159 ? 7.038   9.776   19.798 1.00 15.06 ? 159 HIS A O   1 
ATOM   1306 C CB  . HIS A 1 159 ? 6.825   12.694  19.191 1.00 13.47 ? 159 HIS A CB  1 
ATOM   1307 C CG  . HIS A 1 159 ? 7.223   12.756  17.751 1.00 13.27 ? 159 HIS A CG  1 
ATOM   1308 N ND1 . HIS A 1 159 ? 6.321   13.026  16.741 1.00 15.64 ? 159 HIS A ND1 1 
ATOM   1309 C CD2 . HIS A 1 159 ? 8.428   12.597  17.153 1.00 11.78 ? 159 HIS A CD2 1 
ATOM   1310 C CE1 . HIS A 1 159 ? 6.957   13.023  15.580 1.00 18.04 ? 159 HIS A CE1 1 
ATOM   1311 N NE2 . HIS A 1 159 ? 8.235   12.762  15.802 1.00 14.13 ? 159 HIS A NE2 1 
ATOM   1312 N N   . ALA A 1 160 ? 5.427   9.649   18.236 1.00 12.29 ? 160 ALA A N   1 
ATOM   1313 C CA  . ALA A 1 160 ? 5.770   8.286   17.845 1.00 10.39 ? 160 ALA A CA  1 
ATOM   1314 C C   . ALA A 1 160 ? 6.750   8.286   16.679 1.00 14.49 ? 160 ALA A C   1 
ATOM   1315 O O   . ALA A 1 160 ? 6.558   9.004   15.697 1.00 15.57 ? 160 ALA A O   1 
ATOM   1316 C CB  . ALA A 1 160 ? 4.517   7.500   17.450 1.00 13.06 ? 160 ALA A CB  1 
ATOM   1317 N N   . VAL A 1 161 ? 7.773   7.439   16.780 1.00 13.24 ? 161 VAL A N   1 
ATOM   1318 C CA  . VAL A 1 161 ? 8.834   7.333   15.781 1.00 13.16 ? 161 VAL A CA  1 
ATOM   1319 C C   . VAL A 1 161 ? 9.165   5.858   15.609 1.00 12.47 ? 161 VAL A C   1 
ATOM   1320 O O   . VAL A 1 161 ? 8.444   4.993   16.122 1.00 14.80 ? 161 VAL A O   1 
ATOM   1321 C CB  . VAL A 1 161 ? 10.082  8.130   16.194 1.00 12.14 ? 161 VAL A CB  1 
ATOM   1322 C CG1 . VAL A 1 161 ? 9.811   9.639   16.147 1.00 14.60 ? 161 VAL A CG1 1 
ATOM   1323 C CG2 . VAL A 1 161 ? 10.528  7.712   17.584 1.00 13.82 ? 161 VAL A CG2 1 
ATOM   1324 N N   . ALA A 1 162 ? 10.249  5.541   14.899 1.00 11.32 ? 162 ALA A N   1 
ATOM   1325 C CA  . ALA A 1 162 ? 10.587  4.143   14.665 1.00 11.99 ? 162 ALA A CA  1 
ATOM   1326 C C   . ALA A 1 162 ? 12.054  3.916   14.955 1.00 14.27 ? 162 ALA A C   1 
ATOM   1327 O O   . ALA A 1 162 ? 12.908  4.651   14.450 1.00 13.78 ? 162 ALA A O   1 
ATOM   1328 C CB  . ALA A 1 162 ? 10.276  3.729   13.230 1.00 14.33 ? 162 ALA A CB  1 
ATOM   1329 N N   . ALA A 1 163 ? 12.346  2.896   15.754 1.00 10.98 ? 163 ALA A N   1 
ATOM   1330 C CA  . ALA A 1 163 ? 13.726  2.512   16.007 1.00 10.32 ? 163 ALA A CA  1 
ATOM   1331 C C   . ALA A 1 163 ? 14.152  1.530   14.928 1.00 12.32 ? 163 ALA A C   1 
ATOM   1332 O O   . ALA A 1 163 ? 13.545  0.461   14.784 1.00 14.48 ? 163 ALA A O   1 
ATOM   1333 C CB  . ALA A 1 163 ? 13.867  1.903   17.401 1.00 13.52 ? 163 ALA A CB  1 
ATOM   1334 N N   . VAL A 1 164 ? 15.194  1.887   14.171 1.00 11.52 ? 164 VAL A N   1 
ATOM   1335 C CA  . VAL A 1 164 ? 15.643  1.064   13.059 1.00 11.50 ? 164 VAL A CA  1 
ATOM   1336 C C   . VAL A 1 164 ? 17.063  0.553   13.260 1.00 14.80 ? 164 VAL A C   1 
ATOM   1337 O O   . VAL A 1 164 ? 17.632  -0.059  12.352 1.00 15.54 ? 164 VAL A O   1 
ATOM   1338 C CB  . VAL A 1 164 ? 15.514  1.808   11.714 1.00 13.13 ? 164 VAL A CB  1 
ATOM   1339 C CG1 . VAL A 1 164 ? 14.052  2.091   11.383 1.00 13.51 ? 164 VAL A CG1 1 
ATOM   1340 C CG2 . VAL A 1 164 ? 16.348  3.093   11.723 1.00 12.75 ? 164 VAL A CG2 1 
ATOM   1341 N N   . GLY A 1 165 ? 17.637  0.773   14.436 1.00 11.69 ? 165 GLY A N   1 
ATOM   1342 C CA  . GLY A 1 165 ? 18.958  0.251   14.725 1.00 12.56 ? 165 GLY A CA  1 
ATOM   1343 C C   . GLY A 1 165 ? 19.423  0.686   16.095 1.00 12.51 ? 165 GLY A C   1 
ATOM   1344 O O   . GLY A 1 165 ? 18.685  1.299   16.864 1.00 12.00 ? 165 GLY A O   1 
ATOM   1345 N N   . TYR A 1 166 ? 20.677  0.367   16.388 1.00 13.22 ? 166 TYR A N   1 
ATOM   1346 C CA  . TYR A 1 166 ? 21.293  0.783   17.641 1.00 13.48 ? 166 TYR A CA  1 
ATOM   1347 C C   . TYR A 1 166 ? 22.793  0.578   17.524 1.00 12.31 ? 166 TYR A C   1 
ATOM   1348 O O   . TYR A 1 166 ? 23.284  -0.100  16.617 1.00 13.11 ? 166 TYR A O   1 
ATOM   1349 C CB  . TYR A 1 166 ? 20.740  0.022   18.862 1.00 13.07 ? 166 TYR A CB  1 
ATOM   1350 C CG  . TYR A 1 166 ? 20.991  -1.473  18.857 1.00 15.19 ? 166 TYR A CG  1 
ATOM   1351 C CD1 . TYR A 1 166 ? 22.238  -1.996  19.206 1.00 14.98 ? 166 TYR A CD1 1 
ATOM   1352 C CD2 . TYR A 1 166 ? 19.965  -2.365  18.556 1.00 12.97 ? 166 TYR A CD2 1 
ATOM   1353 C CE1 . TYR A 1 166 ? 22.479  -3.360  19.195 1.00 15.37 ? 166 TYR A CE1 1 
ATOM   1354 C CE2 . TYR A 1 166 ? 20.197  -3.731  18.551 1.00 15.34 ? 166 TYR A CE2 1 
ATOM   1355 C CZ  . TYR A 1 166 ? 21.449  -4.215  18.877 1.00 16.32 ? 166 TYR A CZ  1 
ATOM   1356 O OH  . TYR A 1 166 ? 21.669  -5.573  18.862 1.00 16.58 ? 166 TYR A OH  1 
ATOM   1357 N N   . GLY A 1 167 ? 23.510  1.156   18.481 1.00 13.33 ? 167 GLY A N   1 
ATOM   1358 C CA  . GLY A 1 167 ? 24.927  0.921   18.645 1.00 13.22 ? 167 GLY A CA  1 
ATOM   1359 C C   . GLY A 1 167 ? 25.264  0.912   20.118 1.00 13.22 ? 167 GLY A C   1 
ATOM   1360 O O   . GLY A 1 167 ? 24.378  0.995   20.969 1.00 13.92 ? 167 GLY A O   1 
ATOM   1361 N N   . PRO A 1 168 ? 26.554  0.827   20.450 1.00 15.68 ? 168 PRO A N   1 
ATOM   1362 C CA  . PRO A 1 168 ? 26.952  0.765   21.867 1.00 14.48 ? 168 PRO A CA  1 
ATOM   1363 C C   . PRO A 1 168 ? 26.382  1.873   22.727 1.00 15.52 ? 168 PRO A C   1 
ATOM   1364 O O   . PRO A 1 168 ? 26.057  1.632   23.900 1.00 19.08 ? 168 PRO A O   1 
ATOM   1365 C CB  . PRO A 1 168 ? 28.486  0.838   21.784 1.00 16.08 ? 168 PRO A CB  1 
ATOM   1366 C CG  . PRO A 1 168 ? 28.801  0.140   20.496 1.00 14.09 ? 168 PRO A CG  1 
ATOM   1367 C CD  . PRO A 1 168 ? 27.694  0.614   19.551 1.00 13.00 ? 168 PRO A CD  1 
ATOM   1368 N N   A ASN A 1 169 ? 26.206  3.085   22.207 0.65 15.47 ? 169 ASN A N   1 
ATOM   1369 N N   B ASN A 1 169 ? 26.239  3.079   22.164 0.35 15.51 ? 169 ASN A N   1 
ATOM   1370 C CA  A ASN A 1 169 ? 25.779  4.184   23.063 0.65 13.92 ? 169 ASN A CA  1 
ATOM   1371 C CA  B ASN A 1 169 ? 25.883  4.264   22.931 0.35 14.13 ? 169 ASN A CA  1 
ATOM   1372 C C   A ASN A 1 169 ? 24.491  4.845   22.596 0.65 13.87 ? 169 ASN A C   1 
ATOM   1373 C C   B ASN A 1 169 ? 24.624  4.955   22.416 0.35 13.72 ? 169 ASN A C   1 
ATOM   1374 O O   A ASN A 1 169 ? 24.095  5.864   23.168 0.65 14.29 ? 169 ASN A O   1 
ATOM   1375 O O   B ASN A 1 169 ? 24.379  6.109   22.776 0.35 14.58 ? 169 ASN A O   1 
ATOM   1376 C CB  A ASN A 1 169 ? 26.882  5.240   23.182 0.65 17.03 ? 169 ASN A CB  1 
ATOM   1377 C CB  B ASN A 1 169 ? 27.039  5.275   22.967 0.35 17.40 ? 169 ASN A CB  1 
ATOM   1378 C CG  A ASN A 1 169 ? 28.096  4.728   23.931 0.65 16.35 ? 169 ASN A CG  1 
ATOM   1379 C CG  B ASN A 1 169 ? 27.908  5.296   21.687 0.35 24.52 ? 169 ASN A CG  1 
ATOM   1380 O OD1 A ASN A 1 169 ? 29.148  4.481   23.338 0.65 25.50 ? 169 ASN A OD1 1 
ATOM   1381 O OD1 B ASN A 1 169 ? 27.684  4.581   20.699 0.35 18.69 ? 169 ASN A OD1 1 
ATOM   1382 N ND2 A ASN A 1 169 ? 27.947  4.541   25.236 0.65 21.46 ? 169 ASN A ND2 1 
ATOM   1383 N ND2 B ASN A 1 169 ? 28.919  6.156   21.719 0.35 27.18 ? 169 ASN A ND2 1 
ATOM   1384 N N   . TYR A 1 170 ? 23.809  4.286   21.602 1.00 12.49 ? 170 TYR A N   1 
ATOM   1385 C CA  . TYR A 1 170 ? 22.633  4.966   21.067 1.00 12.95 ? 170 TYR A CA  1 
ATOM   1386 C C   . TYR A 1 170 ? 21.628  3.977   20.512 1.00 12.75 ? 170 TYR A C   1 
ATOM   1387 O O   . TYR A 1 170 ? 21.935  2.808   20.251 1.00 13.22 ? 170 TYR A O   1 
ATOM   1388 C CB  . TYR A 1 170 ? 22.990  5.957   19.950 1.00 13.00 ? 170 TYR A CB  1 
ATOM   1389 C CG  . TYR A 1 170 ? 23.549  5.251   18.747 1.00 13.23 ? 170 TYR A CG  1 
ATOM   1390 C CD1 . TYR A 1 170 ? 24.904  4.970   18.665 1.00 12.76 ? 170 TYR A CD1 1 
ATOM   1391 C CD2 . TYR A 1 170 ? 22.722  4.831   17.703 1.00 15.08 ? 170 TYR A CD2 1 
ATOM   1392 C CE1 . TYR A 1 170 ? 25.415  4.305   17.594 1.00 13.47 ? 170 TYR A CE1 1 
ATOM   1393 C CE2 . TYR A 1 170 ? 23.229  4.145   16.623 1.00 14.66 ? 170 TYR A CE2 1 
ATOM   1394 C CZ  . TYR A 1 170 ? 24.587  3.903   16.564 1.00 15.78 ? 170 TYR A CZ  1 
ATOM   1395 O OH  . TYR A 1 170 ? 25.133  3.225   15.495 1.00 17.70 ? 170 TYR A OH  1 
ATOM   1396 N N   . ILE A 1 171 ? 20.416  4.488   20.319 1.00 13.00 ? 171 ILE A N   1 
ATOM   1397 C CA  . ILE A 1 171 ? 19.396  3.833   19.517 1.00 10.75 ? 171 ILE A CA  1 
ATOM   1398 C C   . ILE A 1 171 ? 19.112  4.727   18.317 1.00 13.36 ? 171 ILE A C   1 
ATOM   1399 O O   . ILE A 1 171 ? 19.000  5.950   18.459 1.00 13.31 ? 171 ILE A O   1 
ATOM   1400 C CB  . ILE A 1 171 ? 18.129  3.567   20.347 1.00 12.04 ? 171 ILE A CB  1 
ATOM   1401 C CG1 . ILE A 1 171 ? 18.422  2.462   21.367 1.00 16.23 ? 171 ILE A CG1 1 
ATOM   1402 C CG2 . ILE A 1 171 ? 16.982  3.130   19.455 1.00 12.82 ? 171 ILE A CG2 1 
ATOM   1403 C CD1 . ILE A 1 171 ? 17.355  2.329   22.444 1.00 15.51 ? 171 ILE A CD1 1 
ATOM   1404 N N   . LEU A 1 172 ? 19.010  4.115   17.136 1.00 11.37 ? 172 LEU A N   1 
ATOM   1405 C CA  . LEU A 1 172 ? 18.869  4.844   15.876 1.00 10.77 ? 172 LEU A CA  1 
ATOM   1406 C C   . LEU A 1 172 ? 17.391  4.976   15.521 1.00 12.56 ? 172 LEU A C   1 
ATOM   1407 O O   . LEU A 1 172 ? 16.686  3.969   15.398 1.00 14.29 ? 172 LEU A O   1 
ATOM   1408 C CB  . LEU A 1 172 ? 19.626  4.128   14.764 1.00 13.48 ? 172 LEU A CB  1 
ATOM   1409 C CG  . LEU A 1 172 ? 19.423  4.612   13.330 1.00 12.57 ? 172 LEU A CG  1 
ATOM   1410 C CD1 . LEU A 1 172 ? 20.007  6.003   13.139 1.00 14.62 ? 172 LEU A CD1 1 
ATOM   1411 C CD2 . LEU A 1 172 ? 20.065  3.622   12.342 1.00 16.66 ? 172 LEU A CD2 1 
ATOM   1412 N N   . ILE A 1 173 ? 16.940  6.212   15.327 1.00 10.91 ? 173 ILE A N   1 
ATOM   1413 C CA  . ILE A 1 173 ? 15.525  6.546   15.185 1.00 12.07 ? 173 ILE A CA  1 
ATOM   1414 C C   . ILE A 1 173 ? 15.273  7.184   13.823 1.00 11.89 ? 173 ILE A C   1 
ATOM   1415 O O   . ILE A 1 173 ? 15.910  8.182   13.472 1.00 11.84 ? 173 ILE A O   1 
ATOM   1416 C CB  . ILE A 1 173 ? 15.067  7.511   16.293 1.00 11.16 ? 173 ILE A CB  1 
ATOM   1417 C CG1 . ILE A 1 173 ? 15.181  6.897   17.697 1.00 14.55 ? 173 ILE A CG1 1 
ATOM   1418 C CG2 . ILE A 1 173 ? 13.664  7.985   16.003 1.00 12.88 ? 173 ILE A CG2 1 
ATOM   1419 C CD1 . ILE A 1 173 ? 14.426  5.599   17.926 1.00 15.63 ? 173 ILE A CD1 1 
ATOM   1420 N N   . LYS A 1 174 ? 14.271  6.666   13.104 1.00 11.66 ? 174 LYS A N   1 
ATOM   1421 C CA  . LYS A 1 174 ? 13.740  7.310   11.903 1.00 9.74  ? 174 LYS A CA  1 
ATOM   1422 C C   . LYS A 1 174 ? 12.594  8.234   12.316 1.00 10.79 ? 174 LYS A C   1 
ATOM   1423 O O   . LYS A 1 174 ? 11.550  7.763   12.786 1.00 11.39 ? 174 LYS A O   1 
ATOM   1424 C CB  . LYS A 1 174 ? 13.281  6.253   10.897 1.00 12.24 ? 174 LYS A CB  1 
ATOM   1425 C CG  . LYS A 1 174 ? 12.895  6.802   9.497  1.00 12.29 ? 174 LYS A CG  1 
ATOM   1426 C CD  . LYS A 1 174 ? 12.233  5.747   8.642  1.00 12.31 ? 174 LYS A CD  1 
ATOM   1427 C CE  . LYS A 1 174 ? 11.984  6.268   7.234  1.00 12.84 ? 174 LYS A CE  1 
ATOM   1428 N NZ  . LYS A 1 174 ? 11.206  5.312   6.387  1.00 13.13 ? 174 LYS A NZ  1 
ATOM   1429 N N   . ASN A 1 175 ? 12.790  9.544   12.165 1.00 11.30 ? 175 ASN A N   1 
ATOM   1430 C CA  . ASN A 1 175 ? 11.747  10.529  12.437 1.00 11.14 ? 175 ASN A CA  1 
ATOM   1431 C C   . ASN A 1 175 ? 10.968  10.821  11.156 1.00 10.64 ? 175 ASN A C   1 
ATOM   1432 O O   . ASN A 1 175 ? 11.381  10.457  10.054 1.00 11.67 ? 175 ASN A O   1 
ATOM   1433 C CB  . ASN A 1 175 ? 12.375  11.803  13.011 1.00 12.15 ? 175 ASN A CB  1 
ATOM   1434 C CG  . ASN A 1 175 ? 11.390  12.676  13.780 1.00 11.94 ? 175 ASN A CG  1 
ATOM   1435 O OD1 . ASN A 1 175 ? 10.219  12.330  13.983 1.00 11.58 ? 175 ASN A OD1 1 
ATOM   1436 N ND2 . ASN A 1 175 ? 11.880  13.824  14.232 1.00 13.77 ? 175 ASN A ND2 1 
ATOM   1437 N N   . SER A 1 176 ? 9.814   11.471  11.312 1.00 11.17 ? 176 SER A N   1 
ATOM   1438 C CA  . SER A 1 176 ? 8.936   11.810  10.195 1.00 13.09 ? 176 SER A CA  1 
ATOM   1439 C C   . SER A 1 176 ? 8.845   13.323  9.990  1.00 11.63 ? 176 SER A C   1 
ATOM   1440 O O   . SER A 1 176 ? 7.760   13.869  9.719  1.00 12.26 ? 176 SER A O   1 
ATOM   1441 C CB  . SER A 1 176 ? 7.546   11.214  10.406 1.00 12.44 ? 176 SER A CB  1 
ATOM   1442 O OG  . SER A 1 176 ? 7.091   11.485  11.729 1.00 14.65 ? 176 SER A OG  1 
ATOM   1443 N N   . TRP A 1 177 ? 9.979   14.021  10.113 1.00 12.73 ? 177 TRP A N   1 
ATOM   1444 C CA  . TRP A 1 177 ? 10.019  15.474  9.980  1.00 10.88 ? 177 TRP A CA  1 
ATOM   1445 C C   . TRP A 1 177 ? 10.807  15.924  8.749  1.00 12.42 ? 177 TRP A C   1 
ATOM   1446 O O   . TRP A 1 177 ? 11.281  17.065  8.701  1.00 13.34 ? 177 TRP A O   1 
ATOM   1447 C CB  . TRP A 1 177 ? 10.607  16.106  11.243 1.00 13.50 ? 177 TRP A CB  1 
ATOM   1448 C CG  . TRP A 1 177 ? 9.691   16.080  12.457 1.00 10.73 ? 177 TRP A CG  1 
ATOM   1449 C CD1 . TRP A 1 177 ? 8.371   15.696  12.511 1.00 13.09 ? 177 TRP A CD1 1 
ATOM   1450 C CD2 . TRP A 1 177 ? 10.046  16.486  13.775 1.00 11.71 ? 177 TRP A CD2 1 
ATOM   1451 N NE1 . TRP A 1 177 ? 7.895   15.835  13.802 1.00 13.46 ? 177 TRP A NE1 1 
ATOM   1452 C CE2 . TRP A 1 177 ? 8.907   16.316  14.593 1.00 13.71 ? 177 TRP A CE2 1 
ATOM   1453 C CE3 . TRP A 1 177 ? 11.225  16.977  14.349 1.00 11.33 ? 177 TRP A CE3 1 
ATOM   1454 C CZ2 . TRP A 1 177 ? 8.905   16.637  15.956 1.00 15.46 ? 177 TRP A CZ2 1 
ATOM   1455 C CZ3 . TRP A 1 177 ? 11.225  17.292  15.705 1.00 14.69 ? 177 TRP A CZ3 1 
ATOM   1456 C CH2 . TRP A 1 177 ? 10.072  17.113  16.492 1.00 15.51 ? 177 TRP A CH2 1 
ATOM   1457 N N   . GLY A 1 178 ? 10.947  15.053  7.755  1.00 11.90 ? 178 GLY A N   1 
ATOM   1458 C CA  . GLY A 1 178 ? 11.665  15.375  6.540  1.00 11.61 ? 178 GLY A CA  1 
ATOM   1459 C C   . GLY A 1 178 ? 13.162  15.123  6.641  1.00 11.73 ? 178 GLY A C   1 
ATOM   1460 O O   . GLY A 1 178 ? 13.724  14.876  7.711  1.00 13.39 ? 178 GLY A O   1 
ATOM   1461 N N   . THR A 1 179 ? 13.820  15.206  5.480  1.00 12.59 ? 179 THR A N   1 
ATOM   1462 C CA  . THR A 1 179 ? 15.252  14.901  5.410  1.00 12.71 ? 179 THR A CA  1 
ATOM   1463 C C   . THR A 1 179 ? 16.147  16.049  5.866  1.00 14.82 ? 179 THR A C   1 
ATOM   1464 O O   . THR A 1 179 ? 17.352  15.837  6.023  1.00 14.31 ? 179 THR A O   1 
ATOM   1465 C CB  . THR A 1 179 ? 15.645  14.496  3.983  1.00 12.77 ? 179 THR A CB  1 
ATOM   1466 O OG1 . THR A 1 179 ? 15.351  15.578  3.082  1.00 13.95 ? 179 THR A OG1 1 
ATOM   1467 C CG2 . THR A 1 179 ? 14.893  13.228  3.540  1.00 15.36 ? 179 THR A CG2 1 
ATOM   1468 N N   . GLY A 1 180 ? 15.607  17.241  6.102  1.00 14.82 ? 180 GLY A N   1 
ATOM   1469 C CA  . GLY A 1 180 ? 16.427  18.333  6.579  1.00 16.83 ? 180 GLY A CA  1 
ATOM   1470 C C   . GLY A 1 180 ? 16.594  18.395  8.074  1.00 18.45 ? 180 GLY A C   1 
ATOM   1471 O O   . GLY A 1 180 ? 17.422  19.166  8.567  1.00 22.99 ? 180 GLY A O   1 
ATOM   1472 N N   . TRP A 1 181 ? 15.845  17.585  8.815  1.00 15.19 ? 181 TRP A N   1 
ATOM   1473 C CA  . TRP A 1 181 ? 15.953  17.541  10.267 1.00 14.08 ? 181 TRP A CA  1 
ATOM   1474 C C   . TRP A 1 181 ? 16.951  16.473  10.690 1.00 13.84 ? 181 TRP A C   1 
ATOM   1475 O O   . TRP A 1 181 ? 16.965  15.375  10.135 1.00 13.11 ? 181 TRP A O   1 
ATOM   1476 C CB  . TRP A 1 181 ? 14.590  17.240  10.891 1.00 12.54 ? 181 TRP A CB  1 
ATOM   1477 C CG  . TRP A 1 181 ? 14.603  17.188  12.395 1.00 12.09 ? 181 TRP A CG  1 
ATOM   1478 C CD1 . TRP A 1 181 ? 14.427  18.231  13.235 1.00 14.98 ? 181 TRP A CD1 1 
ATOM   1479 C CD2 . TRP A 1 181 ? 14.801  16.029  13.230 1.00 11.91 ? 181 TRP A CD2 1 
ATOM   1480 N NE1 . TRP A 1 181 ? 14.491  17.814  14.535 1.00 13.78 ? 181 TRP A NE1 1 
ATOM   1481 C CE2 . TRP A 1 181 ? 14.730  16.466  14.563 1.00 11.53 ? 181 TRP A CE2 1 
ATOM   1482 C CE3 . TRP A 1 181 ? 15.032  14.674  12.982 1.00 13.33 ? 181 TRP A CE3 1 
ATOM   1483 C CZ2 . TRP A 1 181 ? 14.859  15.597  15.649 1.00 11.25 ? 181 TRP A CZ2 1 
ATOM   1484 C CZ3 . TRP A 1 181 ? 15.174  13.815  14.058 1.00 12.05 ? 181 TRP A CZ3 1 
ATOM   1485 C CH2 . TRP A 1 181 ? 15.095  14.280  15.378 1.00 12.44 ? 181 TRP A CH2 1 
ATOM   1486 N N   . GLY A 1 182 ? 17.784  16.806  11.672 1.00 13.05 ? 182 GLY A N   1 
ATOM   1487 C CA  . GLY A 1 182 ? 18.695  15.820  12.232 1.00 12.39 ? 182 GLY A CA  1 
ATOM   1488 C C   . GLY A 1 182 ? 19.707  15.300  11.234 1.00 12.05 ? 182 GLY A C   1 
ATOM   1489 O O   . GLY A 1 182 ? 20.215  16.029  10.370 1.00 14.40 ? 182 GLY A O   1 
ATOM   1490 N N   . GLU A 1 183 ? 20.007  14.006  11.351 1.00 10.72 ? 183 GLU A N   1 
ATOM   1491 C CA  . GLU A 1 183 ? 21.003  13.362  10.489 1.00 10.68 ? 183 GLU A CA  1 
ATOM   1492 C C   . GLU A 1 183 ? 20.261  12.781  9.288  1.00 11.18 ? 183 GLU A C   1 
ATOM   1493 O O   . GLU A 1 183 ? 19.921  11.598  9.222  1.00 13.71 ? 183 GLU A O   1 
ATOM   1494 C CB  . GLU A 1 183 ? 21.800  12.314  11.268 1.00 12.90 ? 183 GLU A CB  1 
ATOM   1495 C CG  . GLU A 1 183 ? 22.455  12.908  12.527 1.00 16.69 ? 183 GLU A CG  1 
ATOM   1496 C CD  . GLU A 1 183 ? 23.377  11.965  13.272 1.00 17.19 ? 183 GLU A CD  1 
ATOM   1497 O OE1 . GLU A 1 183 ? 23.071  10.753  13.348 1.00 15.64 ? 183 GLU A OE1 1 
ATOM   1498 O OE2 . GLU A 1 183 ? 24.383  12.452  13.844 1.00 16.53 ? 183 GLU A OE2 1 
ATOM   1499 N N   . ASN A 1 184 ? 19.979  13.668  8.335  1.00 13.83 ? 184 ASN A N   1 
ATOM   1500 C CA  . ASN A 1 184 ? 19.195  13.342  7.140  1.00 12.85 ? 184 ASN A CA  1 
ATOM   1501 C C   . ASN A 1 184 ? 17.866  12.673  7.497  1.00 14.10 ? 184 ASN A C   1 
ATOM   1502 O O   . ASN A 1 184 ? 17.418  11.745  6.819  1.00 13.89 ? 184 ASN A O   1 
ATOM   1503 C CB  . ASN A 1 184 ? 20.001  12.469  6.177  1.00 13.92 ? 184 ASN A CB  1 
ATOM   1504 C CG  . ASN A 1 184 ? 21.253  13.169  5.682  1.00 15.30 ? 184 ASN A CG  1 
ATOM   1505 O OD1 . ASN A 1 184 ? 21.310  14.393  5.655  1.00 16.27 ? 184 ASN A OD1 1 
ATOM   1506 N ND2 . ASN A 1 184 ? 22.249  12.395  5.270  1.00 22.29 ? 184 ASN A ND2 1 
ATOM   1507 N N   . GLY A 1 185 ? 17.244  13.133  8.587  1.00 12.06 ? 185 GLY A N   1 
ATOM   1508 C CA  . GLY A 1 185 ? 15.936  12.656  9.007  1.00 13.14 ? 185 GLY A CA  1 
ATOM   1509 C C   . GLY A 1 185 ? 15.970  11.752  10.217 1.00 12.74 ? 185 GLY A C   1 
ATOM   1510 O O   . GLY A 1 185 ? 14.906  11.410  10.748 1.00 11.41 ? 185 GLY A O   1 
ATOM   1511 N N   . TYR A 1 186 ? 17.153  11.349  10.654 1.00 11.94 ? 186 TYR A N   1 
ATOM   1512 C CA  . TYR A 1 186 ? 17.358  10.396  11.737 1.00 11.02 ? 186 TYR A CA  1 
ATOM   1513 C C   . TYR A 1 186 ? 17.890  11.109  12.971 1.00 12.54 ? 186 TYR A C   1 
ATOM   1514 O O   . TYR A 1 186 ? 18.454  12.206  12.898 1.00 13.90 ? 186 TYR A O   1 
ATOM   1515 C CB  . TYR A 1 186 ? 18.332  9.289   11.295 1.00 12.35 ? 186 TYR A CB  1 
ATOM   1516 C CG  . TYR A 1 186 ? 17.720  8.371   10.261 1.00 10.43 ? 186 TYR A CG  1 
ATOM   1517 C CD1 . TYR A 1 186 ? 17.714  8.710   8.913  1.00 12.67 ? 186 TYR A CD1 1 
ATOM   1518 C CD2 . TYR A 1 186 ? 17.157  7.154   10.631 1.00 12.15 ? 186 TYR A CD2 1 
ATOM   1519 C CE1 . TYR A 1 186 ? 17.139  7.863   7.962  1.00 14.26 ? 186 TYR A CE1 1 
ATOM   1520 C CE2 . TYR A 1 186 ? 16.581  6.318   9.699  1.00 12.34 ? 186 TYR A CE2 1 
ATOM   1521 C CZ  . TYR A 1 186 ? 16.566  6.673   8.372  1.00 13.06 ? 186 TYR A CZ  1 
ATOM   1522 O OH  . TYR A 1 186 ? 15.987  5.832   7.446  1.00 15.65 ? 186 TYR A OH  1 
ATOM   1523 N N   . ILE A 1 187 ? 17.697  10.476  14.117 1.00 11.67 ? 187 ILE A N   1 
ATOM   1524 C CA  . ILE A 1 187 ? 18.368  10.893  15.340 1.00 12.71 ? 187 ILE A CA  1 
ATOM   1525 C C   . ILE A 1 187 ? 18.930  9.653   16.017 1.00 11.24 ? 187 ILE A C   1 
ATOM   1526 O O   . ILE A 1 187 ? 18.304  8.588   16.021 1.00 11.77 ? 187 ILE A O   1 
ATOM   1527 C CB  . ILE A 1 187 ? 17.428  11.697  16.274 1.00 12.10 ? 187 ILE A CB  1 
ATOM   1528 C CG1 . ILE A 1 187 ? 18.132  12.121  17.571 1.00 12.04 ? 187 ILE A CG1 1 
ATOM   1529 C CG2 . ILE A 1 187 ? 16.121  10.944  16.569 1.00 11.20 ? 187 ILE A CG2 1 
ATOM   1530 C CD1 . ILE A 1 187 ? 17.348  13.192  18.362 1.00 13.68 ? 187 ILE A CD1 1 
ATOM   1531 N N   . ARG A 1 188 ? 20.136  9.781   16.553 1.00 12.95 ? 188 ARG A N   1 
ATOM   1532 C CA  . ARG A 1 188 ? 20.701  8.772   17.433 1.00 11.97 ? 188 ARG A CA  1 
ATOM   1533 C C   . ARG A 1 188 ? 20.513  9.253   18.862 1.00 13.05 ? 188 ARG A C   1 
ATOM   1534 O O   . ARG A 1 188 ? 21.000  10.324  19.227 1.00 14.86 ? 188 ARG A O   1 
ATOM   1535 C CB  . ARG A 1 188 ? 22.177  8.529   17.105 1.00 13.13 ? 188 ARG A CB  1 
ATOM   1536 C CG  . ARG A 1 188 ? 22.376  7.864   15.733 1.00 12.75 ? 188 ARG A CG  1 
ATOM   1537 C CD  . ARG A 1 188 ? 23.841  7.697   15.424 1.00 14.11 ? 188 ARG A CD  1 
ATOM   1538 N NE  . ARG A 1 188 ? 24.423  9.002   15.161 1.00 13.64 ? 188 ARG A NE  1 
ATOM   1539 C CZ  . ARG A 1 188 ? 25.670  9.327   15.470 1.00 18.43 ? 188 ARG A CZ  1 
ATOM   1540 N NH1 . ARG A 1 188 ? 26.487  8.456   16.040 1.00 20.98 ? 188 ARG A NH1 1 
ATOM   1541 N NH2 . ARG A 1 188 ? 26.091  10.565  15.246 1.00 16.77 ? 188 ARG A NH2 1 
ATOM   1542 N N   . ILE A 1 189 ? 19.790  8.481   19.656 1.00 12.86 ? 189 ILE A N   1 
ATOM   1543 C CA  . ILE A 1 189 ? 19.451  8.873   21.018 1.00 14.89 ? 189 ILE A CA  1 
ATOM   1544 C C   . ILE A 1 189 ? 20.292  8.051   21.983 1.00 15.27 ? 189 ILE A C   1 
ATOM   1545 O O   . ILE A 1 189 ? 20.356  6.820   21.872 1.00 14.66 ? 189 ILE A O   1 
ATOM   1546 C CB  . ILE A 1 189 ? 17.951  8.697   21.290 1.00 13.88 ? 189 ILE A CB  1 
ATOM   1547 C CG1 . ILE A 1 189 ? 17.165  9.659   20.406 1.00 16.08 ? 189 ILE A CG1 1 
ATOM   1548 C CG2 . ILE A 1 189 ? 17.650  8.997   22.770 1.00 16.34 ? 189 ILE A CG2 1 
ATOM   1549 C CD1 . ILE A 1 189 ? 15.706  9.581   20.601 1.00 21.09 ? 189 ILE A CD1 1 
ATOM   1550 N N   . LYS A 1 190 ? 20.925  8.735   22.935 1.00 14.55 ? 190 LYS A N   1 
ATOM   1551 C CA  . LYS A 1 190 ? 21.800  8.080   23.904 1.00 15.31 ? 190 LYS A CA  1 
ATOM   1552 C C   . LYS A 1 190 ? 21.069  6.958   24.635 1.00 13.45 ? 190 LYS A C   1 
ATOM   1553 O O   . LYS A 1 190 ? 19.897  7.090   24.986 1.00 16.17 ? 190 LYS A O   1 
ATOM   1554 C CB  . LYS A 1 190 ? 22.301  9.125   24.898 1.00 18.23 ? 190 LYS A CB  1 
ATOM   1555 C CG  . LYS A 1 190 ? 23.051  8.549   26.082 1.00 23.12 ? 190 LYS A CG  1 
ATOM   1556 C CD  . LYS A 1 190 ? 24.374  8.019   25.655 1.00 20.62 ? 190 LYS A CD  1 
ATOM   1557 C CE  . LYS A 1 190 ? 25.356  7.918   26.825 1.00 26.43 ? 190 LYS A CE  1 
ATOM   1558 N NZ  . LYS A 1 190 ? 25.721  9.237   27.386 1.00 33.45 ? 190 LYS A NZ  1 
ATOM   1559 N N   . ARG A 1 191 ? 21.761  5.841   24.858 1.00 15.81 ? 191 ARG A N   1 
ATOM   1560 C CA  . ARG A 1 191 ? 21.235  4.754   25.673 1.00 14.41 ? 191 ARG A CA  1 
ATOM   1561 C C   . ARG A 1 191 ? 22.277  4.404   26.733 1.00 15.97 ? 191 ARG A C   1 
ATOM   1562 O O   . ARG A 1 191 ? 23.394  4.933   26.745 1.00 18.16 ? 191 ARG A O   1 
ATOM   1563 C CB  . ARG A 1 191 ? 20.880  3.523   24.825 1.00 13.81 ? 191 ARG A CB  1 
ATOM   1564 C CG  . ARG A 1 191 ? 22.076  2.745   24.259 1.00 13.71 ? 191 ARG A CG  1 
ATOM   1565 C CD  . ARG A 1 191 ? 21.592  1.443   23.585 1.00 14.28 ? 191 ARG A CD  1 
ATOM   1566 N NE  . ARG A 1 191 ? 22.676  0.529   23.235 1.00 13.90 ? 191 ARG A NE  1 
ATOM   1567 C CZ  . ARG A 1 191 ? 23.225  -0.352  24.064 1.00 14.26 ? 191 ARG A CZ  1 
ATOM   1568 N NH1 . ARG A 1 191 ? 22.905  -0.391  25.341 1.00 14.38 ? 191 ARG A NH1 1 
ATOM   1569 N NH2 . ARG A 1 191 ? 24.130  -1.206  23.602 1.00 14.28 ? 191 ARG A NH2 1 
ATOM   1570 N N   . GLY A 1 192 ? 21.908  3.466   27.600 1.00 15.57 ? 192 GLY A N   1 
ATOM   1571 C CA  . GLY A 1 192 ? 22.799  3.019   28.655 1.00 16.02 ? 192 GLY A CA  1 
ATOM   1572 C C   . GLY A 1 192 ? 22.962  3.986   29.805 1.00 20.30 ? 192 GLY A C   1 
ATOM   1573 O O   . GLY A 1 192 ? 23.963  3.901   30.521 1.00 21.12 ? 192 GLY A O   1 
ATOM   1574 N N   . THR A 1 193 ? 22.009  4.892   30.021 1.00 19.30 ? 193 THR A N   1 
ATOM   1575 C CA  . THR A 1 193 ? 22.120  5.883   31.086 1.00 18.39 ? 193 THR A CA  1 
ATOM   1576 C C   . THR A 1 193 ? 21.608  5.395   32.439 1.00 19.68 ? 193 THR A C   1 
ATOM   1577 O O   . THR A 1 193 ? 21.800  6.095   33.438 1.00 25.55 ? 193 THR A O   1 
ATOM   1578 C CB  . THR A 1 193 ? 21.385  7.183   30.702 1.00 18.00 ? 193 THR A CB  1 
ATOM   1579 O OG1 . THR A 1 193 ? 19.964  7.002   30.810 1.00 20.50 ? 193 THR A OG1 1 
ATOM   1580 C CG2 . THR A 1 193 ? 21.745  7.618   29.281 1.00 18.87 ? 193 THR A CG2 1 
ATOM   1581 N N   . GLY A 1 194 ? 20.980  4.223   32.509 1.00 19.76 ? 194 GLY A N   1 
ATOM   1582 C CA  . GLY A 1 194 ? 20.455  3.723   33.766 1.00 25.92 ? 194 GLY A CA  1 
ATOM   1583 C C   . GLY A 1 194 ? 19.089  4.249   34.134 1.00 29.30 ? 194 GLY A C   1 
ATOM   1584 O O   . GLY A 1 194 ? 18.502  3.779   35.118 1.00 34.08 ? 194 GLY A O   1 
ATOM   1585 N N   . ASN A 1 195 ? 18.569  5.205   33.375 1.00 25.11 ? 195 ASN A N   1 
ATOM   1586 C CA  . ASN A 1 195 ? 17.232  5.745   33.557 1.00 28.05 ? 195 ASN A CA  1 
ATOM   1587 C C   . ASN A 1 195 ? 16.215  4.816   32.899 1.00 30.18 ? 195 ASN A C   1 
ATOM   1588 O O   . ASN A 1 195 ? 16.216  4.651   31.672 1.00 29.11 ? 195 ASN A O   1 
ATOM   1589 C CB  . ASN A 1 195 ? 17.174  7.141   32.951 1.00 29.26 ? 195 ASN A CB  1 
ATOM   1590 C CG  . ASN A 1 195 ? 15.795  7.737   32.998 1.00 32.72 ? 195 ASN A CG  1 
ATOM   1591 O OD1 . ASN A 1 195 ? 14.913  7.254   33.716 1.00 37.60 ? 195 ASN A OD1 1 
ATOM   1592 N ND2 . ASN A 1 195 ? 15.580  8.768   32.189 1.00 32.93 ? 195 ASN A ND2 1 
ATOM   1593 N N   . SER A 1 196 ? 15.349  4.215   33.716 1.00 24.12 ? 196 SER A N   1 
ATOM   1594 C CA  . SER A 1 196 ? 14.408  3.213   33.229 1.00 25.77 ? 196 SER A CA  1 
ATOM   1595 C C   . SER A 1 196 ? 13.401  3.771   32.229 1.00 19.47 ? 196 SER A C   1 
ATOM   1596 O O   . SER A 1 196 ? 12.878  3.004   31.414 1.00 21.07 ? 196 SER A O   1 
ATOM   1597 C CB  . SER A 1 196 ? 13.673  2.583   34.409 1.00 31.65 ? 196 SER A CB  1 
ATOM   1598 O OG  . SER A 1 196 ? 13.200  3.580   35.294 1.00 44.06 ? 196 SER A OG  1 
ATOM   1599 N N   . TYR A 1 197 ? 13.116  5.079   32.273 1.00 19.27 ? 197 TYR A N   1 
ATOM   1600 C CA  . TYR A 1 197 ? 12.245  5.689   31.270 1.00 18.98 ? 197 TYR A CA  1 
ATOM   1601 C C   . TYR A 1 197 ? 12.881  5.706   29.890 1.00 20.01 ? 197 TYR A C   1 
ATOM   1602 O O   . TYR A 1 197 ? 12.161  5.772   28.888 1.00 16.29 ? 197 TYR A O   1 
ATOM   1603 C CB  . TYR A 1 197 ? 11.909  7.133   31.655 1.00 20.75 ? 197 TYR A CB  1 
ATOM   1604 C CG  . TYR A 1 197 ? 11.017  7.258   32.856 1.00 24.11 ? 197 TYR A CG  1 
ATOM   1605 C CD1 . TYR A 1 197 ? 9.671   6.935   32.778 1.00 25.87 ? 197 TYR A CD1 1 
ATOM   1606 C CD2 . TYR A 1 197 ? 11.520  7.695   34.076 1.00 28.43 ? 197 TYR A CD2 1 
ATOM   1607 C CE1 . TYR A 1 197 ? 8.843   7.035   33.883 1.00 34.39 ? 197 TYR A CE1 1 
ATOM   1608 C CE2 . TYR A 1 197 ? 10.699  7.802   35.189 1.00 32.82 ? 197 TYR A CE2 1 
ATOM   1609 C CZ  . TYR A 1 197 ? 9.361   7.473   35.080 1.00 36.04 ? 197 TYR A CZ  1 
ATOM   1610 O OH  . TYR A 1 197 ? 8.530   7.576   36.168 1.00 42.92 ? 197 TYR A OH  1 
ATOM   1611 N N   . GLY A 1 198 ? 14.202  5.671   29.822 1.00 16.13 ? 198 GLY A N   1 
ATOM   1612 C CA  . GLY A 1 198 ? 14.930  5.971   28.609 1.00 17.60 ? 198 GLY A CA  1 
ATOM   1613 C C   . GLY A 1 198 ? 15.097  7.468   28.425 1.00 14.77 ? 198 GLY A C   1 
ATOM   1614 O O   . GLY A 1 198 ? 14.357  8.281   28.974 1.00 18.47 ? 198 GLY A O   1 
ATOM   1615 N N   . VAL A 1 199 ? 16.121  7.840   27.659 1.00 14.66 ? 199 VAL A N   1 
ATOM   1616 C CA  . VAL A 1 199 ? 16.290  9.245   27.321 1.00 12.84 ? 199 VAL A CA  1 
ATOM   1617 C C   . VAL A 1 199 ? 15.067  9.727   26.548 1.00 16.71 ? 199 VAL A C   1 
ATOM   1618 O O   . VAL A 1 199 ? 14.606  9.071   25.604 1.00 14.49 ? 199 VAL A O   1 
ATOM   1619 C CB  . VAL A 1 199 ? 17.602  9.442   26.545 1.00 13.36 ? 199 VAL A CB  1 
ATOM   1620 C CG1 . VAL A 1 199 ? 17.743  10.871  26.015 1.00 19.44 ? 199 VAL A CG1 1 
ATOM   1621 C CG2 . VAL A 1 199 ? 18.807  9.072   27.445 1.00 17.11 ? 199 VAL A CG2 1 
ATOM   1622 N N   . CYS A 1 200 ? 14.509  10.859  26.980 1.00 15.11 ? 200 CYS A N   1 
ATOM   1623 C CA  . CYS A 1 200 ? 13.265  11.419  26.441 1.00 15.99 ? 200 CYS A CA  1 
ATOM   1624 C C   . CYS A 1 200 ? 12.109  10.432  26.527 1.00 17.56 ? 200 CYS A C   1 
ATOM   1625 O O   . CYS A 1 200 ? 11.170  10.495  25.733 1.00 13.68 ? 200 CYS A O   1 
ATOM   1626 C CB  . CYS A 1 200 ? 13.426  11.919  25.001 1.00 21.26 ? 200 CYS A CB  1 
ATOM   1627 S SG  . CYS A 1 200 ? 14.841  13.003  24.693 1.00 19.82 ? 200 CYS A SG  1 
ATOM   1628 N N   . GLY A 1 201 ? 12.159  9.515   27.491 1.00 15.00 ? 201 GLY A N   1 
ATOM   1629 C CA  . GLY A 1 201 ? 11.077  8.566   27.675 1.00 17.30 ? 201 GLY A CA  1 
ATOM   1630 C C   . GLY A 1 201 ? 10.999  7.463   26.645 1.00 14.40 ? 201 GLY A C   1 
ATOM   1631 O O   . GLY A 1 201 ? 9.942   6.853   26.484 1.00 14.14 ? 201 GLY A O   1 
ATOM   1632 N N   . LEU A 1 202 ? 12.115  7.161   25.978 1.00 13.93 ? 202 LEU A N   1 
ATOM   1633 C CA  . LEU A 1 202 ? 12.146  6.278   24.820 1.00 13.57 ? 202 LEU A CA  1 
ATOM   1634 C C   . LEU A 1 202 ? 11.658  4.858   25.099 1.00 14.20 ? 202 LEU A C   1 
ATOM   1635 O O   . LEU A 1 202 ? 11.293  4.153   24.152 1.00 14.48 ? 202 LEU A O   1 
ATOM   1636 C CB  . LEU A 1 202 ? 13.576  6.257   24.274 1.00 14.48 ? 202 LEU A CB  1 
ATOM   1637 C CG  . LEU A 1 202 ? 13.856  5.516   22.971 1.00 14.78 ? 202 LEU A CG  1 
ATOM   1638 C CD1 . LEU A 1 202 ? 12.957  6.059   21.866 1.00 14.90 ? 202 LEU A CD1 1 
ATOM   1639 C CD2 . LEU A 1 202 ? 15.315  5.638   22.585 1.00 14.97 ? 202 LEU A CD2 1 
ATOM   1640 N N   . TYR A 1 203 ? 11.621  4.406   26.359 1.00 15.22 ? 203 TYR A N   1 
ATOM   1641 C CA  . TYR A 1 203 ? 11.211  3.036   26.648 1.00 15.49 ? 203 TYR A CA  1 
ATOM   1642 C C   . TYR A 1 203 ? 9.767   2.945   27.130 1.00 15.28 ? 203 TYR A C   1 
ATOM   1643 O O   . TYR A 1 203 ? 9.350   1.902   27.646 1.00 18.93 ? 203 TYR A O   1 
ATOM   1644 C CB  . TYR A 1 203 ? 12.152  2.392   27.670 1.00 17.46 ? 203 TYR A CB  1 
ATOM   1645 C CG  . TYR A 1 203 ? 13.621  2.556   27.341 1.00 16.08 ? 203 TYR A CG  1 
ATOM   1646 C CD1 . TYR A 1 203 ? 14.050  2.657   26.022 1.00 17.26 ? 203 TYR A CD1 1 
ATOM   1647 C CD2 . TYR A 1 203 ? 14.587  2.575   28.347 1.00 15.18 ? 203 TYR A CD2 1 
ATOM   1648 C CE1 . TYR A 1 203 ? 15.376  2.812   25.716 1.00 17.70 ? 203 TYR A CE1 1 
ATOM   1649 C CE2 . TYR A 1 203 ? 15.931  2.710   28.040 1.00 17.10 ? 203 TYR A CE2 1 
ATOM   1650 C CZ  . TYR A 1 203 ? 16.312  2.833   26.728 1.00 18.62 ? 203 TYR A CZ  1 
ATOM   1651 O OH  . TYR A 1 203 ? 17.638  2.987   26.402 1.00 16.78 ? 203 TYR A OH  1 
ATOM   1652 N N   . THR A 1 204 ? 8.984   4.002   26.934 1.00 16.95 ? 204 THR A N   1 
ATOM   1653 C CA  . THR A 1 204 ? 7.659   4.059   27.540 1.00 14.76 ? 204 THR A CA  1 
ATOM   1654 C C   . THR A 1 204 ? 6.668   3.099   26.874 1.00 17.06 ? 204 THR A C   1 
ATOM   1655 O O   . THR A 1 204 ? 5.906   2.419   27.573 1.00 19.44 ? 204 THR A O   1 
ATOM   1656 C CB  . THR A 1 204 ? 7.142   5.494   27.502 1.00 15.79 ? 204 THR A CB  1 
ATOM   1657 O OG1 . THR A 1 204 ? 7.989   6.313   28.320 1.00 15.67 ? 204 THR A OG1 1 
ATOM   1658 C CG2 . THR A 1 204 ? 5.706   5.567   28.035 1.00 16.45 ? 204 THR A CG2 1 
ATOM   1659 N N   . SER A 1 205 ? 6.637   3.039   25.534 1.00 15.30 ? 205 SER A N   1 
ATOM   1660 C CA  . SER A 1 205 ? 5.569   2.308   24.840 1.00 16.02 ? 205 SER A CA  1 
ATOM   1661 C C   . SER A 1 205 ? 6.059   1.880   23.449 1.00 14.87 ? 205 SER A C   1 
ATOM   1662 O O   . SER A 1 205 ? 6.111   2.710   22.535 1.00 17.67 ? 205 SER A O   1 
ATOM   1663 C CB  . SER A 1 205 ? 4.327   3.177   24.747 1.00 17.61 ? 205 SER A CB  1 
ATOM   1664 O OG  . SER A 1 205 ? 3.207   2.451   24.246 1.00 19.59 ? 205 SER A OG  1 
ATOM   1665 N N   . SER A 1 206 ? 6.369   0.590   23.286 1.00 14.76 ? 206 SER A N   1 
ATOM   1666 C CA  . SER A 1 206 ? 7.000   0.087   22.068 1.00 14.05 ? 206 SER A CA  1 
ATOM   1667 C C   . SER A 1 206 ? 6.266   -1.135  21.539 1.00 16.56 ? 206 SER A C   1 
ATOM   1668 O O   . SER A 1 206 ? 6.008   -2.078  22.290 1.00 15.60 ? 206 SER A O   1 
ATOM   1669 C CB  . SER A 1 206 ? 8.473   -0.264  22.313 1.00 16.48 ? 206 SER A CB  1 
ATOM   1670 O OG  . SER A 1 206 ? 9.169   0.854   22.852 1.00 14.62 ? 206 SER A OG  1 
ATOM   1671 N N   . PHE A 1 207 ? 5.972   -1.135  20.235 1.00 14.39 ? 207 PHE A N   1 
ATOM   1672 C CA  . PHE A 1 207 ? 5.180   -2.177  19.597 1.00 15.21 ? 207 PHE A CA  1 
ATOM   1673 C C   . PHE A 1 207 ? 5.805   -2.561  18.269 1.00 15.37 ? 207 PHE A C   1 
ATOM   1674 O O   . PHE A 1 207 ? 6.456   -1.742  17.609 1.00 14.94 ? 207 PHE A O   1 
ATOM   1675 C CB  . PHE A 1 207 ? 3.739   -1.713  19.340 1.00 16.09 ? 207 PHE A CB  1 
ATOM   1676 C CG  . PHE A 1 207 ? 2.930   -1.544  20.586 1.00 16.95 ? 207 PHE A CG  1 
ATOM   1677 C CD1 . PHE A 1 207 ? 2.902   -0.330  21.253 1.00 19.82 ? 207 PHE A CD1 1 
ATOM   1678 C CD2 . PHE A 1 207 ? 2.174   -2.596  21.083 1.00 20.98 ? 207 PHE A CD2 1 
ATOM   1679 C CE1 . PHE A 1 207 ? 2.153   -0.171  22.407 1.00 21.43 ? 207 PHE A CE1 1 
ATOM   1680 C CE2 . PHE A 1 207 ? 1.419   -2.441  22.232 1.00 16.29 ? 207 PHE A CE2 1 
ATOM   1681 C CZ  . PHE A 1 207 ? 1.401   -1.229  22.895 1.00 18.52 ? 207 PHE A CZ  1 
ATOM   1682 N N   . TYR A 1 208 ? 5.573   -3.802  17.851 1.00 18.32 ? 208 TYR A N   1 
ATOM   1683 C CA  . TYR A 1 208 ? 6.057   -4.251  16.553 1.00 15.14 ? 208 TYR A CA  1 
ATOM   1684 C C   . TYR A 1 208 ? 5.078   -5.246  15.945 1.00 15.48 ? 208 TYR A C   1 
ATOM   1685 O O   . TYR A 1 208 ? 4.388   -5.965  16.677 1.00 17.36 ? 208 TYR A O   1 
ATOM   1686 C CB  . TYR A 1 208 ? 7.462   -4.875  16.657 1.00 16.69 ? 208 TYR A CB  1 
ATOM   1687 C CG  . TYR A 1 208 ? 7.579   -6.035  17.617 1.00 16.11 ? 208 TYR A CG  1 
ATOM   1688 C CD1 . TYR A 1 208 ? 7.890   -5.819  18.951 1.00 20.52 ? 208 TYR A CD1 1 
ATOM   1689 C CD2 . TYR A 1 208 ? 7.410   -7.348  17.185 1.00 19.26 ? 208 TYR A CD2 1 
ATOM   1690 C CE1 . TYR A 1 208 ? 8.010   -6.873  19.845 1.00 21.79 ? 208 TYR A CE1 1 
ATOM   1691 C CE2 . TYR A 1 208 ? 7.524   -8.414  18.077 1.00 24.07 ? 208 TYR A CE2 1 
ATOM   1692 C CZ  . TYR A 1 208 ? 7.826   -8.163  19.403 1.00 26.24 ? 208 TYR A CZ  1 
ATOM   1693 O OH  . TYR A 1 208 ? 7.945   -9.202  20.304 1.00 26.98 ? 208 TYR A OH  1 
ATOM   1694 N N   . PRO A 1 209 ? 4.991   -5.302  14.619 1.00 13.63 ? 209 PRO A N   1 
ATOM   1695 C CA  . PRO A 1 209 ? 4.115   -6.276  13.962 1.00 13.93 ? 209 PRO A CA  1 
ATOM   1696 C C   . PRO A 1 209 ? 4.704   -7.678  13.917 1.00 19.26 ? 209 PRO A C   1 
ATOM   1697 O O   . PRO A 1 209 ? 5.920   -7.882  13.897 1.00 18.75 ? 209 PRO A O   1 
ATOM   1698 C CB  . PRO A 1 209 ? 3.962   -5.708  12.545 1.00 14.38 ? 209 PRO A CB  1 
ATOM   1699 C CG  . PRO A 1 209 ? 5.241   -4.932  12.321 1.00 16.30 ? 209 PRO A CG  1 
ATOM   1700 C CD  . PRO A 1 209 ? 5.698   -4.433  13.658 1.00 13.76 ? 209 PRO A CD  1 
ATOM   1701 N N   . VAL A 1 210 ? 3.805   -8.654  13.884 1.00 19.82 ? 210 VAL A N   1 
ATOM   1702 C CA  . VAL A 1 210 ? 4.162   -10.057 13.720 1.00 21.57 ? 210 VAL A CA  1 
ATOM   1703 C C   . VAL A 1 210 ? 3.672   -10.513 12.359 1.00 21.19 ? 210 VAL A C   1 
ATOM   1704 O O   . VAL A 1 210 ? 2.531   -10.225 11.983 1.00 21.85 ? 210 VAL A O   1 
ATOM   1705 C CB  . VAL A 1 210 ? 3.553   -10.923 14.832 1.00 23.06 ? 210 VAL A CB  1 
ATOM   1706 C CG1 . VAL A 1 210 ? 3.878   -12.399 14.592 1.00 27.57 ? 210 VAL A CG1 1 
ATOM   1707 C CG2 . VAL A 1 210 ? 4.076   -10.473 16.155 1.00 24.82 ? 210 VAL A CG2 1 
ATOM   1708 N N   . LYS A 1 211 ? 4.526   -11.208 11.621 1.00 22.00 ? 211 LYS A N   1 
ATOM   1709 C CA  . LYS A 1 211 ? 4.141   -11.784 10.342 1.00 25.21 ? 211 LYS A CA  1 
ATOM   1710 C C   . LYS A 1 211 ? 4.773   -13.156 10.193 1.00 30.38 ? 211 LYS A C   1 
ATOM   1711 O O   . LYS A 1 211 ? 5.994   -13.299 10.298 1.00 28.86 ? 211 LYS A O   1 
ATOM   1712 C CB  . LYS A 1 211 ? 4.546   -10.899 9.161  1.00 29.42 ? 211 LYS A CB  1 
ATOM   1713 C CG  . LYS A 1 211 ? 4.220   -11.556 7.830  1.00 31.44 ? 211 LYS A CG  1 
ATOM   1714 C CD  . LYS A 1 211 ? 3.922   -10.549 6.752  1.00 37.27 ? 211 LYS A CD  1 
ATOM   1715 C CE  . LYS A 1 211 ? 3.573   -11.241 5.440  1.00 33.48 ? 211 LYS A CE  1 
ATOM   1716 N NZ  . LYS A 1 211 ? 2.142   -11.652 5.399  1.00 37.01 ? 211 LYS A NZ  1 
ATOM   1717 N N   . ASN A 1 212 ? 3.939   -14.150 9.922  1.00 31.82 ? 212 ASN A N   1 
ATOM   1718 C CA  . ASN A 1 212 ? 4.391   -15.527 9.804  1.00 38.68 ? 212 ASN A CA  1 
ATOM   1719 C C   . ASN A 1 212 ? 5.075   -15.774 8.468  1.00 42.56 ? 212 ASN A C   1 
ATOM   1720 O O   . ASN A 1 212 ? 5.919   -16.656 8.361  1.00 46.11 ? 212 ASN A O   1 
ATOM   1721 C CB  . ASN A 1 212 ? 3.211   -16.475 9.976  1.00 42.26 ? 212 ASN A CB  1 
ATOM   1722 C CG  . ASN A 1 212 ? 2.695   -16.490 11.394 1.00 44.82 ? 212 ASN A CG  1 
ATOM   1723 O OD1 . ASN A 1 212 ? 3.432   -16.183 12.334 1.00 52.83 ? 212 ASN A OD1 1 
ATOM   1724 N ND2 . ASN A 1 212 ? 1.420   -16.834 11.560 1.00 55.11 ? 212 ASN A ND2 1 
ATOM   1725 O OXT . ASN A 1 212 ? 4.804   -15.100 7.472  1.00 42.24 ? 212 ASN A OXT 1 
HETATM 1726 C C1  . E64 B 2 .   ? 2.786   13.544  16.188 0.82 27.67 ? 301 E64 A C1  1 
HETATM 1727 O O1  . E64 B 2 .   ? 2.190   13.564  15.116 0.82 22.22 ? 301 E64 A O1  1 
HETATM 1728 O O2  . E64 B 2 .   ? 3.812   14.246  16.447 0.82 28.70 ? 301 E64 A O2  1 
HETATM 1729 C C2  . E64 B 2 .   ? 2.290   12.635  17.319 0.82 28.37 ? 301 E64 A C2  1 
HETATM 1730 C C3  . E64 B 2 .   ? 0.813   12.815  17.661 0.82 26.39 ? 301 E64 A C3  1 
HETATM 1731 O O3  . E64 B 2 .   ? 0.629   14.078  18.260 0.82 24.86 ? 301 E64 A O3  1 
HETATM 1732 C C4  . E64 B 2 .   ? 0.284   11.624  18.484 0.82 23.02 ? 301 E64 A C4  1 
HETATM 1733 O O4  . E64 B 2 .   ? -0.209  10.670  17.912 0.82 19.80 ? 301 E64 A O4  1 
HETATM 1734 N N1  . E64 B 2 .   ? 0.396   11.663  19.822 0.82 30.27 ? 301 E64 A N1  1 
HETATM 1735 C C6  . E64 B 2 .   ? -0.068  10.567  20.665 0.82 20.97 ? 301 E64 A C6  1 
HETATM 1736 C C7  . E64 B 2 .   ? 0.966   10.228  21.732 0.82 29.02 ? 301 E64 A C7  1 
HETATM 1737 C C8  . E64 B 2 .   ? 2.213   9.475   21.264 0.82 21.57 ? 301 E64 A C8  1 
HETATM 1738 C C9  . E64 B 2 .   ? 3.080   9.224   22.497 0.82 19.05 ? 301 E64 A C9  1 
HETATM 1739 C C10 . E64 B 2 .   ? 1.853   8.160   20.582 0.82 26.47 ? 301 E64 A C10 1 
HETATM 1740 C C11 . E64 B 2 .   ? -1.377  10.956  21.363 0.82 31.19 ? 301 E64 A C11 1 
HETATM 1741 O O5  . E64 B 2 .   ? -1.507  12.047  21.897 0.82 36.55 ? 301 E64 A O5  1 
HETATM 1742 N N2  . E64 B 2 .   ? -2.335  10.021  21.357 0.82 30.56 ? 301 E64 A N2  1 
HETATM 1743 C C12 . E64 B 2 .   ? -3.630  10.197  21.972 0.82 30.52 ? 301 E64 A C12 1 
HETATM 1744 C C13 . E64 B 2 .   ? -4.666  10.757  21.007 0.82 25.19 ? 301 E64 A C13 1 
HETATM 1745 C C14 . E64 B 2 .   ? -4.966  12.238  21.191 0.82 32.73 ? 301 E64 A C14 1 
HETATM 1746 C C15 . E64 B 2 .   ? -5.798  12.533  22.442 0.82 40.96 ? 301 E64 A C15 1 
HETATM 1747 N N3  . E64 B 2 .   ? -7.249  12.468  22.300 0.82 42.44 ? 301 E64 A N3  1 
HETATM 1748 C C16 . E64 B 2 .   ? -8.010  13.154  21.438 0.82 35.50 ? 301 E64 A C16 1 
HETATM 1749 N N4  . E64 B 2 .   ? -9.325  13.026  21.396 0.82 30.21 ? 301 E64 A N4  1 
HETATM 1750 N N5  . E64 B 2 .   ? -7.447  14.000  20.574 0.82 39.68 ? 301 E64 A N5  1 
HETATM 1751 O O   . HOH C 3 .   ? 30.248  6.836   20.088 1.00 33.58 ? 401 HOH A O   1 
HETATM 1752 O O   . HOH C 3 .   ? -8.697  -2.901  13.325 1.00 31.28 ? 402 HOH A O   1 
HETATM 1753 O O   . HOH C 3 .   ? 3.236   7.467   -6.780 1.00 28.91 ? 403 HOH A O   1 
HETATM 1754 O O   . HOH C 3 .   ? -5.481  -0.661  6.578  1.00 34.02 ? 404 HOH A O   1 
HETATM 1755 O O   . HOH C 3 .   ? -10.227 0.601   22.043 1.00 34.74 ? 405 HOH A O   1 
HETATM 1756 O O   . HOH C 3 .   ? -0.906  20.535  6.757  1.00 40.05 ? 406 HOH A O   1 
HETATM 1757 O O   . HOH C 3 .   ? 6.780   -1.066  25.693 1.00 21.87 ? 407 HOH A O   1 
HETATM 1758 O O   . HOH C 3 .   ? -1.205  1.879   -7.052 1.00 36.62 ? 408 HOH A O   1 
HETATM 1759 O O   . HOH C 3 .   ? 5.863   6.832   31.802 1.00 37.82 ? 409 HOH A O   1 
HETATM 1760 O O   . HOH C 3 .   ? -10.979 16.153  5.601  1.00 26.63 ? 410 HOH A O   1 
HETATM 1761 O O   . HOH C 3 .   ? 3.133   -5.953  -0.541 1.00 25.96 ? 411 HOH A O   1 
HETATM 1762 O O   . HOH C 3 .   ? 11.384  -1.319  26.935 1.00 18.43 ? 412 HOH A O   1 
HETATM 1763 O O   . HOH C 3 .   ? 5.455   16.307  25.882 1.00 23.91 ? 413 HOH A O   1 
HETATM 1764 O O   . HOH C 3 .   ? 23.071  16.202  5.023  1.00 25.86 ? 414 HOH A O   1 
HETATM 1765 O O   . HOH C 3 .   ? 18.806  23.309  14.453 1.00 33.18 ? 415 HOH A O   1 
HETATM 1766 O O   . HOH C 3 .   ? 0.925   12.700  -1.625 1.00 30.15 ? 416 HOH A O   1 
HETATM 1767 O O   . HOH C 3 .   ? 17.650  19.967  12.327 1.00 27.34 ? 417 HOH A O   1 
HETATM 1768 O O   . HOH C 3 .   ? 15.714  6.266   4.873  1.00 19.04 ? 418 HOH A O   1 
HETATM 1769 O O   . HOH C 3 .   ? -9.765  13.947  14.742 1.00 27.60 ? 419 HOH A O   1 
HETATM 1770 O O   . HOH C 3 .   ? -7.329  -1.484  15.233 1.00 28.36 ? 420 HOH A O   1 
HETATM 1771 O O   . HOH C 3 .   ? -10.037 5.777   21.008 1.00 25.31 ? 421 HOH A O   1 
HETATM 1772 O O   . HOH C 3 .   ? 7.949   -10.297 14.748 1.00 34.45 ? 422 HOH A O   1 
HETATM 1773 O O   . HOH C 3 .   ? 6.226   6.158   7.503  1.00 12.86 ? 423 HOH A O   1 
HETATM 1774 O O   . HOH C 3 .   ? 26.758  -0.316  25.564 1.00 22.80 ? 424 HOH A O   1 
HETATM 1775 O O   . HOH C 3 .   ? 5.169   16.079  15.072 1.00 21.85 ? 425 HOH A O   1 
HETATM 1776 O O   . HOH C 3 .   ? 0.525   -5.731  12.647 1.00 18.56 ? 426 HOH A O   1 
HETATM 1777 O O   . HOH C 3 .   ? 16.438  15.095  0.693  1.00 12.37 ? 427 HOH A O   1 
HETATM 1778 O O   . HOH C 3 .   ? 25.684  -2.240  21.318 1.00 17.96 ? 428 HOH A O   1 
HETATM 1779 O O   . HOH C 3 .   ? 19.692  -7.710  13.067 1.00 31.53 ? 429 HOH A O   1 
HETATM 1780 O O   . HOH C 3 .   ? -4.827  -8.784  -1.161 1.00 33.01 ? 430 HOH A O   1 
HETATM 1781 O O   . HOH C 3 .   ? 24.630  2.521   11.587 1.00 19.37 ? 431 HOH A O   1 
HETATM 1782 O O   . HOH C 3 .   ? 21.917  8.777   11.945 1.00 21.30 ? 432 HOH A O   1 
HETATM 1783 O O   . HOH C 3 .   ? 23.288  2.045   13.933 1.00 17.25 ? 433 HOH A O   1 
HETATM 1784 O O   . HOH C 3 .   ? 14.419  20.624  25.695 1.00 24.42 ? 434 HOH A O   1 
HETATM 1785 O O   . HOH C 3 .   ? 20.050  19.288  7.984  1.00 28.12 ? 435 HOH A O   1 
HETATM 1786 O O   . HOH C 3 .   ? 8.712   3.674   23.529 1.00 15.09 ? 436 HOH A O   1 
HETATM 1787 O O   . HOH C 3 .   ? 10.759  2.407   6.345  1.00 13.46 ? 437 HOH A O   1 
HETATM 1788 O O   . HOH C 3 .   ? 17.906  10.000  4.792  1.00 21.37 ? 438 HOH A O   1 
HETATM 1789 O O   . HOH C 3 .   ? 7.215   9.078   13.057 1.00 15.04 ? 439 HOH A O   1 
HETATM 1790 O O   . HOH C 3 .   ? 23.719  16.265  10.604 1.00 32.39 ? 440 HOH A O   1 
HETATM 1791 O O   . HOH C 3 .   ? 23.656  -6.179  12.709 1.00 22.17 ? 441 HOH A O   1 
HETATM 1792 O O   . HOH C 3 .   ? 17.163  -6.058  30.045 1.00 34.86 ? 442 HOH A O   1 
HETATM 1793 O O   . HOH C 3 .   ? 7.247   8.098   30.247 1.00 25.57 ? 443 HOH A O   1 
HETATM 1794 O O   . HOH C 3 .   ? 19.091  9.522   31.392 1.00 21.69 ? 444 HOH A O   1 
HETATM 1795 O O   . HOH C 3 .   ? 26.015  14.262  12.614 1.00 28.49 ? 445 HOH A O   1 
HETATM 1796 O O   . HOH C 3 .   ? -2.592  -7.893  -3.241 1.00 39.35 ? 446 HOH A O   1 
HETATM 1797 O O   . HOH C 3 .   ? 2.718   11.722  27.837 1.00 29.66 ? 447 HOH A O   1 
HETATM 1798 O O   . HOH C 3 .   ? 11.476  0.184   7.822  1.00 13.89 ? 448 HOH A O   1 
HETATM 1799 O O   . HOH C 3 .   ? 1.487   1.335   26.066 1.00 32.02 ? 449 HOH A O   1 
HETATM 1800 O O   . HOH C 3 .   ? -2.040  18.933  13.892 1.00 35.14 ? 450 HOH A O   1 
HETATM 1801 O O   . HOH C 3 .   ? 14.949  -10.668 11.715 1.00 28.24 ? 451 HOH A O   1 
HETATM 1802 O O   . HOH C 3 .   ? 24.735  -12.530 20.217 1.00 22.97 ? 452 HOH A O   1 
HETATM 1803 O O   . HOH C 3 .   ? 24.671  4.165   33.161 1.00 32.37 ? 453 HOH A O   1 
HETATM 1804 O O   . HOH C 3 .   ? 6.282   5.396   3.590  1.00 16.76 ? 454 HOH A O   1 
HETATM 1805 O O   . HOH C 3 .   ? 17.858  5.869   26.369 1.00 16.82 ? 455 HOH A O   1 
HETATM 1806 O O   . HOH C 3 .   ? 8.478   5.272   6.043  1.00 14.43 ? 456 HOH A O   1 
HETATM 1807 O O   . HOH C 3 .   ? 3.831   16.416  4.391  1.00 22.67 ? 457 HOH A O   1 
HETATM 1808 O O   . HOH C 3 .   ? 19.427  20.796  19.984 1.00 25.66 ? 458 HOH A O   1 
HETATM 1809 O O   . HOH C 3 .   ? 14.291  18.194  24.065 1.00 17.15 ? 459 HOH A O   1 
HETATM 1810 O O   . HOH C 3 .   ? 9.885   7.945   -1.200 1.00 21.84 ? 460 HOH A O   1 
HETATM 1811 O O   . HOH C 3 .   ? 20.734  -0.872  1.867  1.00 32.88 ? 461 HOH A O   1 
HETATM 1812 O O   . HOH C 3 .   ? 11.755  16.902  24.350 1.00 15.68 ? 462 HOH A O   1 
HETATM 1813 O O   . HOH C 3 .   ? -0.447  18.182  7.246  1.00 25.55 ? 463 HOH A O   1 
HETATM 1814 O O   . HOH C 3 .   ? -9.055  0.422   14.949 1.00 30.44 ? 464 HOH A O   1 
HETATM 1815 O O   . HOH C 3 .   ? 9.611   0.034   25.463 1.00 16.14 ? 465 HOH A O   1 
HETATM 1816 O O   . HOH C 3 .   ? 10.232  8.993   7.926  1.00 12.94 ? 466 HOH A O   1 
HETATM 1817 O O   . HOH C 3 .   ? -4.791  16.052  -0.891 1.00 22.32 ? 467 HOH A O   1 
HETATM 1818 O O   . HOH C 3 .   ? -11.833 1.185   9.326  1.00 32.33 ? 468 HOH A O   1 
HETATM 1819 O O   . HOH C 3 .   ? 9.171   -4.443  11.889 1.00 15.56 ? 469 HOH A O   1 
HETATM 1820 O O   . HOH C 3 .   ? -1.603  15.629  17.683 1.00 28.35 ? 470 HOH A O   1 
HETATM 1821 O O   . HOH C 3 .   ? 27.256  10.945  25.805 1.00 35.62 ? 471 HOH A O   1 
HETATM 1822 O O   . HOH C 3 .   ? 5.623   11.367  32.099 1.00 34.38 ? 472 HOH A O   1 
HETATM 1823 O O   . HOH C 3 .   ? 4.127   2.393   29.743 1.00 30.64 ? 473 HOH A O   1 
HETATM 1824 O O   . HOH C 3 .   ? 26.424  12.425  23.355 1.00 28.24 ? 474 HOH A O   1 
HETATM 1825 O O   . HOH C 3 .   ? 2.565   3.415   21.683 1.00 20.91 ? 475 HOH A O   1 
HETATM 1826 O O   . HOH C 3 .   ? 8.412   -3.851  2.459  1.00 17.24 ? 476 HOH A O   1 
HETATM 1827 O O   . HOH C 3 .   ? 15.673  -3.222  -0.477 1.00 28.47 ? 477 HOH A O   1 
HETATM 1828 O O   . HOH C 3 .   ? -10.616 8.914   13.716 1.00 23.68 ? 478 HOH A O   1 
HETATM 1829 O O   . HOH C 3 .   ? -4.917  9.107   24.997 1.00 40.17 ? 479 HOH A O   1 
HETATM 1830 O O   . HOH C 3 .   ? 11.820  -7.894  23.547 1.00 24.29 ? 480 HOH A O   1 
HETATM 1831 O O   . HOH C 3 .   ? -7.569  7.905   12.856 1.00 15.39 ? 481 HOH A O   1 
HETATM 1832 O O   . HOH C 3 .   ? 5.320   5.025   -3.187 1.00 24.99 ? 482 HOH A O   1 
HETATM 1833 O O   . HOH C 3 .   ? 6.255   7.970   -1.496 1.00 23.30 ? 483 HOH A O   1 
HETATM 1834 O O   . HOH C 3 .   ? 7.693   -8.554  23.179 1.00 29.29 ? 484 HOH A O   1 
HETATM 1835 O O   . HOH C 3 .   ? 4.710   2.760   20.072 1.00 16.67 ? 485 HOH A O   1 
HETATM 1836 O O   . HOH C 3 .   ? 14.935  -9.935  3.199  1.00 35.68 ? 486 HOH A O   1 
HETATM 1837 O O   . HOH C 3 .   ? 23.399  3.219   7.156  1.00 26.06 ? 487 HOH A O   1 
HETATM 1838 O O   . HOH C 3 .   ? -13.702 6.594   14.979 1.00 31.55 ? 488 HOH A O   1 
HETATM 1839 O O   . HOH C 3 .   ? -11.547 7.812   17.748 1.00 24.81 ? 489 HOH A O   1 
HETATM 1840 O O   . HOH C 3 .   ? -11.747 6.045   11.076 1.00 23.93 ? 490 HOH A O   1 
HETATM 1841 O O   . HOH C 3 .   ? 2.158   -14.131 6.801  1.00 40.45 ? 491 HOH A O   1 
HETATM 1842 O O   . HOH C 3 .   ? -17.041 14.864  6.755  1.00 34.72 ? 492 HOH A O   1 
HETATM 1843 O O   . HOH C 3 .   ? 0.660   15.784  1.197  1.00 33.00 ? 493 HOH A O   1 
HETATM 1844 O O   A HOH C 3 .   ? -14.419 8.396   -1.614 0.55 22.03 ? 494 HOH A O   1 
HETATM 1845 O O   B HOH C 3 .   ? -14.636 8.800   0.423  0.45 21.28 ? 494 HOH A O   1 
HETATM 1846 O O   . HOH C 3 .   ? -4.306  17.760  1.216  1.00 26.21 ? 495 HOH A O   1 
HETATM 1847 O O   . HOH C 3 .   ? 13.427  -5.019  -2.165 1.00 32.28 ? 496 HOH A O   1 
HETATM 1848 O O   . HOH C 3 .   ? 21.484  9.193   9.362  1.00 16.84 ? 497 HOH A O   1 
HETATM 1849 O O   A HOH C 3 .   ? 19.744  16.613  7.411  0.47 12.16 ? 498 HOH A O   1 
HETATM 1850 O O   B HOH C 3 .   ? 21.530  16.897  6.670  0.22 8.17  ? 498 HOH A O   1 
HETATM 1851 O O   C HOH C 3 .   ? 22.764  15.730  8.107  0.31 10.98 ? 498 HOH A O   1 
HETATM 1852 O O   . HOH C 3 .   ? 19.235  5.115   28.770 1.00 17.93 ? 499 HOH A O   1 
HETATM 1853 O O   . HOH C 3 .   ? 8.721   5.491   -3.829 1.00 32.72 ? 500 HOH A O   1 
HETATM 1854 O O   . HOH C 3 .   ? 22.207  16.321  23.321 1.00 22.75 ? 501 HOH A O   1 
HETATM 1855 O O   . HOH C 3 .   ? 13.339  -13.061 11.561 1.00 39.89 ? 502 HOH A O   1 
HETATM 1856 O O   . HOH C 3 .   ? 6.491   -8.202  -0.686 1.00 33.31 ? 503 HOH A O   1 
HETATM 1857 O O   . HOH C 3 .   ? 15.477  4.047   1.354  1.00 28.37 ? 504 HOH A O   1 
HETATM 1858 O O   . HOH C 3 .   ? -8.086  5.707   -5.673 1.00 15.35 ? 505 HOH A O   1 
HETATM 1859 O O   . HOH C 3 .   ? -13.434 1.859   2.853  1.00 29.97 ? 506 HOH A O   1 
HETATM 1860 O O   . HOH C 3 .   ? 15.132  12.131  29.499 1.00 20.19 ? 507 HOH A O   1 
HETATM 1861 O O   . HOH C 3 .   ? 19.847  2.218   30.564 1.00 23.94 ? 508 HOH A O   1 
HETATM 1862 O O   . HOH C 3 .   ? 16.457  -0.560  31.279 1.00 26.27 ? 509 HOH A O   1 
HETATM 1863 O O   . HOH C 3 .   ? 17.080  0.413   3.472  1.00 18.61 ? 510 HOH A O   1 
HETATM 1864 O O   . HOH C 3 .   ? 22.353  19.118  17.523 1.00 23.64 ? 511 HOH A O   1 
HETATM 1865 O O   . HOH C 3 .   ? 1.058   13.983  21.440 1.00 31.91 ? 512 HOH A O   1 
HETATM 1866 O O   . HOH C 3 .   ? 21.185  19.904  23.700 1.00 24.01 ? 513 HOH A O   1 
HETATM 1867 O O   . HOH C 3 .   ? 12.821  13.392  10.057 1.00 13.00 ? 514 HOH A O   1 
HETATM 1868 O O   . HOH C 3 .   ? 8.849   7.266   11.791 1.00 13.55 ? 515 HOH A O   1 
HETATM 1869 O O   . HOH C 3 .   ? 14.450  14.161  32.493 1.00 30.27 ? 516 HOH A O   1 
HETATM 1870 O O   . HOH C 3 .   ? 0.047   7.600   2.672  1.00 15.53 ? 517 HOH A O   1 
HETATM 1871 O O   . HOH C 3 .   ? 11.700  0.192   -2.639 1.00 38.78 ? 518 HOH A O   1 
HETATM 1872 O O   . HOH C 3 .   ? 18.152  -3.931  30.155 1.00 25.35 ? 519 HOH A O   1 
HETATM 1873 O O   A HOH C 3 .   ? 20.387  18.961  10.305 0.57 21.40 ? 520 HOH A O   1 
HETATM 1874 O O   B HOH C 3 .   ? 18.973  20.510  10.255 0.43 20.87 ? 520 HOH A O   1 
HETATM 1875 O O   . HOH C 3 .   ? 25.355  -2.415  11.314 1.00 22.91 ? 521 HOH A O   1 
HETATM 1876 O O   . HOH C 3 .   ? 13.270  10.490  30.590 1.00 30.61 ? 522 HOH A O   1 
HETATM 1877 O O   . HOH C 3 .   ? -14.298 6.977   7.379  1.00 30.57 ? 523 HOH A O   1 
HETATM 1878 O O   . HOH C 3 .   ? 7.284   -11.890 12.774 1.00 26.56 ? 524 HOH A O   1 
HETATM 1879 O O   . HOH C 3 .   ? 21.054  -13.122 20.576 1.00 32.55 ? 525 HOH A O   1 
HETATM 1880 O O   . HOH C 3 .   ? 10.906  -7.766  17.588 1.00 31.71 ? 526 HOH A O   1 
HETATM 1881 O O   . HOH C 3 .   ? -3.387  -13.659 10.912 1.00 39.97 ? 527 HOH A O   1 
HETATM 1882 O O   . HOH C 3 .   ? 22.066  -4.555  10.849 1.00 22.22 ? 528 HOH A O   1 
HETATM 1883 O O   . HOH C 3 .   ? 10.185  14.294  32.984 1.00 29.29 ? 529 HOH A O   1 
HETATM 1884 O O   . HOH C 3 .   ? 15.925  8.746   3.495  1.00 16.24 ? 530 HOH A O   1 
HETATM 1885 O O   . HOH C 3 .   ? 24.046  7.017   10.763 1.00 27.34 ? 531 HOH A O   1 
HETATM 1886 O O   . HOH C 3 .   ? 19.774  -5.971  10.774 1.00 25.02 ? 532 HOH A O   1 
HETATM 1887 O O   . HOH C 3 .   ? -9.233  -3.656  0.725  1.00 36.45 ? 533 HOH A O   1 
HETATM 1888 O O   A HOH C 3 .   ? 7.648   18.591  9.972  0.62 25.63 ? 534 HOH A O   1 
HETATM 1889 O O   B HOH C 3 .   ? 5.911   17.971  11.184 0.38 19.67 ? 534 HOH A O   1 
HETATM 1890 O O   . HOH C 3 .   ? 28.776  -7.563  17.494 1.00 25.24 ? 535 HOH A O   1 
HETATM 1891 O O   . HOH C 3 .   ? 12.055  -11.388 -2.929 1.00 37.72 ? 536 HOH A O   1 
HETATM 1892 O O   . HOH C 3 .   ? 6.575   0.800   -3.057 1.00 23.65 ? 537 HOH A O   1 
HETATM 1893 O O   . HOH C 3 .   ? 28.919  9.924   17.068 1.00 28.52 ? 538 HOH A O   1 
HETATM 1894 O O   A HOH C 3 .   ? 11.968  15.894  3.192  0.58 11.12 ? 539 HOH A O   1 
HETATM 1895 O O   B HOH C 3 .   ? 10.901  14.036  3.159  0.42 12.36 ? 539 HOH A O   1 
HETATM 1896 O O   . HOH C 3 .   ? 22.289  9.370   5.489  1.00 30.88 ? 540 HOH A O   1 
HETATM 1897 O O   . HOH C 3 .   ? -10.905 0.527   12.848 1.00 19.89 ? 541 HOH A O   1 
HETATM 1898 O O   . HOH C 3 .   ? 4.034   2.594   -3.095 1.00 19.71 ? 542 HOH A O   1 
HETATM 1899 O O   . HOH C 3 .   ? 18.408  -6.708  0.167  1.00 40.22 ? 543 HOH A O   1 
HETATM 1900 O O   . HOH C 3 .   ? -7.584  -7.881  0.132  1.00 31.12 ? 544 HOH A O   1 
HETATM 1901 O O   . HOH C 3 .   ? -8.309  14.881  12.145 1.00 20.49 ? 545 HOH A O   1 
HETATM 1902 O O   . HOH C 3 .   ? -2.019  -9.542  18.002 1.00 27.62 ? 546 HOH A O   1 
HETATM 1903 O O   . HOH C 3 .   ? -7.636  16.485  9.557  1.00 18.90 ? 547 HOH A O   1 
HETATM 1904 O O   . HOH C 3 .   ? 14.873  -8.245  31.592 1.00 37.29 ? 548 HOH A O   1 
HETATM 1905 O O   . HOH C 3 .   ? 26.597  5.673   14.384 1.00 24.86 ? 549 HOH A O   1 
HETATM 1906 O O   . HOH C 3 .   ? 28.103  12.353  19.239 1.00 25.40 ? 550 HOH A O   1 
HETATM 1907 O O   . HOH C 3 .   ? 23.547  -4.198  8.928  1.00 35.89 ? 551 HOH A O   1 
HETATM 1908 O O   . HOH C 3 .   ? 5.967   12.336  3.070  1.00 27.09 ? 552 HOH A O   1 
HETATM 1909 O O   . HOH C 3 .   ? -10.278 16.636  8.545  1.00 32.25 ? 553 HOH A O   1 
HETATM 1910 O O   . HOH C 3 .   ? 3.295   17.894  13.468 1.00 32.25 ? 554 HOH A O   1 
HETATM 1911 O O   . HOH C 3 .   ? 12.579  23.535  25.713 1.00 25.08 ? 555 HOH A O   1 
HETATM 1912 O O   . HOH C 3 .   ? 10.779  -9.413  21.533 1.00 33.93 ? 556 HOH A O   1 
HETATM 1913 O O   . HOH C 3 .   ? -2.278  -1.292  -2.979 1.00 15.06 ? 557 HOH A O   1 
HETATM 1914 O O   . HOH C 3 .   ? 17.447  1.822   31.955 1.00 28.86 ? 558 HOH A O   1 
HETATM 1915 O O   . HOH C 3 .   ? 1.907   20.539  6.435  1.00 34.30 ? 559 HOH A O   1 
HETATM 1916 O O   . HOH C 3 .   ? 21.267  21.783  17.861 1.00 32.95 ? 560 HOH A O   1 
HETATM 1917 O O   A HOH C 3 .   ? 25.604  9.652   11.817 0.72 28.17 ? 561 HOH A O   1 
HETATM 1918 O O   B HOH C 3 .   ? 27.748  9.626   12.202 0.28 22.99 ? 561 HOH A O   1 
HETATM 1919 O O   . HOH C 3 .   ? -13.106 14.076  1.688  1.00 21.95 ? 562 HOH A O   1 
HETATM 1920 O O   . HOH C 3 .   ? 2.592   9.874   -0.876 1.00 14.65 ? 563 HOH A O   1 
HETATM 1921 O O   . HOH C 3 .   ? 9.813   -7.868  25.442 1.00 22.75 ? 564 HOH A O   1 
HETATM 1922 O O   . HOH C 3 .   ? 1.687   -8.078  23.379 1.00 29.41 ? 565 HOH A O   1 
HETATM 1923 O O   . HOH C 3 .   ? 10.038  3.781   34.958 1.00 39.46 ? 566 HOH A O   1 
HETATM 1924 O O   . HOH C 3 .   ? 22.864  -0.986  29.371 1.00 27.37 ? 567 HOH A O   1 
HETATM 1925 O O   . HOH C 3 .   ? 28.123  -5.483  15.160 1.00 19.35 ? 568 HOH A O   1 
HETATM 1926 O O   . HOH C 3 .   ? 7.039   12.017  0.507  1.00 22.79 ? 569 HOH A O   1 
HETATM 1927 O O   . HOH C 3 .   ? 8.090   13.613  2.402  1.00 19.91 ? 570 HOH A O   1 
HETATM 1928 O O   . HOH C 3 .   ? -9.919  14.624  18.520 1.00 34.16 ? 571 HOH A O   1 
HETATM 1929 O O   . HOH C 3 .   ? 31.030  3.377   20.857 1.00 30.59 ? 572 HOH A O   1 
HETATM 1930 O O   . HOH C 3 .   ? 0.094   -5.982  21.747 1.00 38.09 ? 573 HOH A O   1 
HETATM 1931 O O   . HOH C 3 .   ? 8.612   19.893  14.147 1.00 42.01 ? 574 HOH A O   1 
HETATM 1932 O O   . HOH C 3 .   ? -17.752 16.725  2.727  1.00 24.43 ? 575 HOH A O   1 
HETATM 1933 O O   . HOH C 3 .   ? -12.382 11.072  1.258  1.00 28.38 ? 576 HOH A O   1 
HETATM 1934 O O   . HOH C 3 .   ? 19.755  7.725   5.493  1.00 20.62 ? 577 HOH A O   1 
HETATM 1935 O O   . HOH C 3 .   ? 4.288   10.005  29.677 1.00 30.68 ? 578 HOH A O   1 
HETATM 1936 O O   . HOH C 3 .   ? -1.286  -12.472 17.140 1.00 45.07 ? 579 HOH A O   1 
HETATM 1937 O O   . HOH C 3 .   ? 13.031  10.940  33.018 1.00 37.89 ? 580 HOH A O   1 
HETATM 1938 O O   . HOH C 3 .   ? 27.874  15.083  14.831 1.00 38.04 ? 581 HOH A O   1 
HETATM 1939 O O   . HOH C 3 .   ? 25.065  0.202   28.102 1.00 25.81 ? 582 HOH A O   1 
HETATM 1940 O O   . HOH C 3 .   ? 17.557  -7.881  27.651 1.00 34.67 ? 583 HOH A O   1 
HETATM 1941 O O   . HOH C 3 .   ? 25.284  -11.627 17.519 1.00 26.84 ? 584 HOH A O   1 
HETATM 1942 O O   . HOH C 3 .   ? 11.450  -9.747  18.775 1.00 30.16 ? 585 HOH A O   1 
HETATM 1943 O O   . HOH C 3 .   ? 23.887  13.114  8.449  1.00 21.07 ? 586 HOH A O   1 
HETATM 1944 O O   . HOH C 3 .   ? 3.951   12.745  0.574  1.00 33.87 ? 587 HOH A O   1 
HETATM 1945 O O   . HOH C 3 .   ? 27.925  8.678   24.188 1.00 33.96 ? 588 HOH A O   1 
HETATM 1946 O O   . HOH C 3 .   ? 22.371  2.325   4.401  1.00 32.73 ? 589 HOH A O   1 
HETATM 1947 O O   . HOH C 3 .   ? 17.715  4.171   3.905  1.00 26.51 ? 590 HOH A O   1 
HETATM 1948 O O   . HOH C 3 .   ? -1.839  13.119  -2.611 1.00 24.16 ? 591 HOH A O   1 
HETATM 1949 O O   . HOH C 3 .   ? 23.612  9.979   7.776  1.00 26.68 ? 592 HOH A O   1 
HETATM 1950 O O   . HOH C 3 .   ? 1.279   17.588  4.981  1.00 23.76 ? 593 HOH A O   1 
HETATM 1951 O O   . HOH C 3 .   ? 8.146   7.724   9.081  1.00 12.91 ? 594 HOH A O   1 
HETATM 1952 O O   . HOH C 3 .   ? -2.093  15.687  -1.222 1.00 23.25 ? 595 HOH A O   1 
HETATM 1953 O O   . HOH C 3 .   ? -5.478  -5.952  23.246 1.00 36.77 ? 596 HOH A O   1 
HETATM 1954 O O   . HOH C 3 .   ? 20.793  24.796  19.412 1.00 31.66 ? 597 HOH A O   1 
HETATM 1955 O O   . HOH C 3 .   ? 3.725   -8.737  0.389  1.00 32.49 ? 598 HOH A O   1 
HETATM 1956 O O   . HOH C 3 .   ? 14.979  2.627   -0.586 1.00 35.22 ? 599 HOH A O   1 
HETATM 1957 O O   . HOH C 3 .   ? 6.043   18.711  15.890 1.00 42.58 ? 600 HOH A O   1 
HETATM 1958 O O   . HOH C 3 .   ? 8.931   2.317   -3.365 1.00 38.79 ? 601 HOH A O   1 
HETATM 1959 O O   . HOH C 3 .   ? 14.420  21.409  6.873  1.00 24.08 ? 602 HOH A O   1 
HETATM 1960 O O   . HOH C 3 .   ? 23.713  9.656   2.569  1.00 36.87 ? 603 HOH A O   1 
HETATM 1961 O O   . HOH C 3 .   ? 15.416  -9.440  26.706 1.00 34.32 ? 604 HOH A O   1 
HETATM 1962 O O   . HOH C 3 .   ? -3.905  -7.651  16.523 1.00 33.63 ? 605 HOH A O   1 
HETATM 1963 O O   . HOH C 3 .   ? 11.178  6.895   -3.310 1.00 26.18 ? 606 HOH A O   1 
HETATM 1964 O O   . HOH C 3 .   ? -13.624 11.742  21.884 1.00 31.02 ? 607 HOH A O   1 
HETATM 1965 O O   . HOH C 3 .   ? -12.753 8.110   12.876 1.00 32.00 ? 608 HOH A O   1 
HETATM 1966 O O   . HOH C 3 .   ? -14.134 4.883   9.530  1.00 25.94 ? 609 HOH A O   1 
HETATM 1967 O O   . HOH C 3 .   ? 11.593  2.523   -1.153 1.00 19.88 ? 610 HOH A O   1 
HETATM 1968 O O   . HOH C 3 .   ? 2.403   16.181  25.972 1.00 30.91 ? 611 HOH A O   1 
HETATM 1969 O O   . HOH C 3 .   ? -17.692 8.884   -1.569 1.00 31.09 ? 612 HOH A O   1 
HETATM 1970 O O   . HOH C 3 .   ? 22.096  17.924  20.557 1.00 34.63 ? 613 HOH A O   1 
HETATM 1971 O O   . HOH C 3 .   ? 20.613  -11.259 16.778 1.00 27.08 ? 614 HOH A O   1 
HETATM 1972 O O   . HOH C 3 .   ? 16.295  -10.709 9.584  1.00 40.66 ? 615 HOH A O   1 
HETATM 1973 O O   . HOH C 3 .   ? -5.731  19.781  2.535  1.00 31.32 ? 616 HOH A O   1 
HETATM 1974 O O   . HOH C 3 .   ? 22.021  -8.319  13.088 1.00 28.98 ? 617 HOH A O   1 
HETATM 1975 O O   . HOH C 3 .   ? -4.855  -10.042 -3.921 1.00 38.37 ? 618 HOH A O   1 
HETATM 1976 O O   . HOH C 3 .   ? 19.183  22.812  11.189 1.00 36.50 ? 619 HOH A O   1 
HETATM 1977 O O   . HOH C 3 .   ? 27.559  3.906   33.807 1.00 38.12 ? 620 HOH A O   1 
HETATM 1978 O O   . HOH C 3 .   ? 12.466  4.818   -3.126 1.00 24.82 ? 621 HOH A O   1 
HETATM 1979 O O   . HOH C 3 .   ? -6.407  18.701  9.868  1.00 29.77 ? 622 HOH A O   1 
HETATM 1980 O O   . HOH C 3 .   ? -2.860  -12.699 -2.987 1.00 40.82 ? 623 HOH A O   1 
# 
