data_7H6E
# 
_entry.id   7H6E 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   7H6E         pdb_00007h6e 10.2210/pdb7h6e/pdb 
WWPDB D_1001407081 ?            ?                   
# 
_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       2025-03-05 
_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.entry_id                        7H6E 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2024-04-19 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.name_last          Rudolph 
_pdbx_contact_author.name_first         Markus 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.email              markus.rudolph@roche.com 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0447-1101 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Banner, D.W.'  1 
'Benz, J.M.'    2 
'Schlatter, D.' 3 
'Hilpert, H.'   4 
# 
_citation.id                        primary 
_citation.title                     'Crystal structures of human Chymase and Cathepsin G' 
_citation.journal_abbrev            'To be published' 
_citation.year                      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_DOI      ? 
_citation.journal_volume            ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.journal_id_ASTM           ? 
_citation.country                   ? 
_citation.journal_id_ISSN           ? 
_citation.journal_id_CSD            0353 
_citation.book_publisher            ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Markus, R.'    1 0000-0003-0447-1101 
primary 'Tosstorff, A.' 2 0000-0002-4969-3667 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man Chymase                                                                                           25032.910 1   
3.4.21.39 NO ? ? 
2 non-polymer syn 'ZINC ION'                                                                                        65.409    1   
?         ?  ? ? 
3 non-polymer syn '5-fluoro-N-[2-(methanesulfonyl)-4-(pyridin-4-yl)phenyl]-3-methyl-1-benzothiophene-2-sulfonamide' 476.564   1   
?         ?  ? ? 
4 water       nat water                                                                                             18.015    199 
?         ?  ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Alpha-chymase,Mast cell protease I' 
# 
_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       
;IIGGTESKPHSRPYMAYLEIVTSNGPSKFCGGFLIRRNFVLTAAHCAGRSITVTLGAHNITEEEDTWQKLEVIKQFRHPK
YNTSTLHHDIMLLKLKEKASLTLAVGTLPFPSQKNFVPPGRMCRVAGWGRTGVLKPGSDTLQEVKLRLMDPQACSHFRDF
DHNLQLCVGNPRKTKSAFKGDSGGPLLCAGVAQGIVSYGRSDAKPPAVFTRISHYRPWINQILQAN
;
_entity_poly.pdbx_seq_one_letter_code_can   
;IIGGTESKPHSRPYMAYLEIVTSNGPSKFCGGFLIRRNFVLTAAHCAGRSITVTLGAHNITEEEDTWQKLEVIKQFRHPK
YNTSTLHHDIMLLKLKEKASLTLAVGTLPFPSQKNFVPPGRMCRVAGWGRTGVLKPGSDTLQEVKLRLMDPQACSHFRDF
DHNLQLCVGNPRKTKSAFKGDSGGPLLCAGVAQGIVSYGRSDAKPPAVFTRISHYRPWINQILQAN
;
_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 'ZINC ION'                                                                                        ZN    
3 '5-fluoro-N-[2-(methanesulfonyl)-4-(pyridin-4-yl)phenyl]-3-methyl-1-benzothiophene-2-sulfonamide' A1AOP 
4 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   ILE n 
1 3   GLY n 
1 4   GLY n 
1 5   THR n 
1 6   GLU n 
1 7   SER n 
1 8   LYS n 
1 9   PRO n 
1 10  HIS n 
1 11  SER n 
1 12  ARG n 
1 13  PRO n 
1 14  TYR n 
1 15  MET n 
1 16  ALA n 
1 17  TYR n 
1 18  LEU n 
1 19  GLU n 
1 20  ILE n 
1 21  VAL n 
1 22  THR n 
1 23  SER n 
1 24  ASN n 
1 25  GLY n 
1 26  PRO n 
1 27  SER n 
1 28  LYS n 
1 29  PHE n 
1 30  CYS n 
1 31  GLY n 
1 32  GLY n 
1 33  PHE n 
1 34  LEU n 
1 35  ILE n 
1 36  ARG n 
1 37  ARG n 
1 38  ASN n 
1 39  PHE n 
1 40  VAL n 
1 41  LEU n 
1 42  THR n 
1 43  ALA n 
1 44  ALA n 
1 45  HIS n 
1 46  CYS n 
1 47  ALA n 
1 48  GLY n 
1 49  ARG n 
1 50  SER n 
1 51  ILE n 
1 52  THR n 
1 53  VAL n 
1 54  THR n 
1 55  LEU n 
1 56  GLY n 
1 57  ALA n 
1 58  HIS n 
1 59  ASN n 
1 60  ILE n 
1 61  THR n 
1 62  GLU n 
1 63  GLU n 
1 64  GLU n 
1 65  ASP n 
1 66  THR n 
1 67  TRP n 
1 68  GLN n 
1 69  LYS n 
1 70  LEU n 
1 71  GLU n 
1 72  VAL n 
1 73  ILE n 
1 74  LYS n 
1 75  GLN n 
1 76  PHE n 
1 77  ARG n 
1 78  HIS n 
1 79  PRO n 
1 80  LYS n 
1 81  TYR n 
1 82  ASN n 
1 83  THR n 
1 84  SER n 
1 85  THR n 
1 86  LEU n 
1 87  HIS n 
1 88  HIS n 
1 89  ASP n 
1 90  ILE n 
1 91  MET n 
1 92  LEU n 
1 93  LEU n 
1 94  LYS n 
1 95  LEU n 
1 96  LYS n 
1 97  GLU n 
1 98  LYS n 
1 99  ALA n 
1 100 SER n 
1 101 LEU n 
1 102 THR n 
1 103 LEU n 
1 104 ALA n 
1 105 VAL n 
1 106 GLY n 
1 107 THR n 
1 108 LEU n 
1 109 PRO n 
1 110 PHE n 
1 111 PRO n 
1 112 SER n 
1 113 GLN n 
1 114 LYS n 
1 115 ASN n 
1 116 PHE n 
1 117 VAL n 
1 118 PRO n 
1 119 PRO n 
1 120 GLY n 
1 121 ARG n 
1 122 MET n 
1 123 CYS n 
1 124 ARG n 
1 125 VAL n 
1 126 ALA n 
1 127 GLY n 
1 128 TRP n 
1 129 GLY n 
1 130 ARG n 
1 131 THR n 
1 132 GLY n 
1 133 VAL n 
1 134 LEU n 
1 135 LYS n 
1 136 PRO n 
1 137 GLY n 
1 138 SER n 
1 139 ASP n 
1 140 THR n 
1 141 LEU n 
1 142 GLN n 
1 143 GLU n 
1 144 VAL n 
1 145 LYS n 
1 146 LEU n 
1 147 ARG n 
1 148 LEU n 
1 149 MET n 
1 150 ASP n 
1 151 PRO n 
1 152 GLN n 
1 153 ALA n 
1 154 CYS n 
1 155 SER n 
1 156 HIS n 
1 157 PHE n 
1 158 ARG n 
1 159 ASP n 
1 160 PHE n 
1 161 ASP n 
1 162 HIS n 
1 163 ASN n 
1 164 LEU n 
1 165 GLN n 
1 166 LEU n 
1 167 CYS n 
1 168 VAL n 
1 169 GLY n 
1 170 ASN n 
1 171 PRO n 
1 172 ARG n 
1 173 LYS n 
1 174 THR n 
1 175 LYS n 
1 176 SER n 
1 177 ALA n 
1 178 PHE n 
1 179 LYS n 
1 180 GLY n 
1 181 ASP n 
1 182 SER n 
1 183 GLY n 
1 184 GLY n 
1 185 PRO n 
1 186 LEU n 
1 187 LEU n 
1 188 CYS n 
1 189 ALA n 
1 190 GLY n 
1 191 VAL n 
1 192 ALA n 
1 193 GLN n 
1 194 GLY n 
1 195 ILE n 
1 196 VAL n 
1 197 SER n 
1 198 TYR n 
1 199 GLY n 
1 200 ARG n 
1 201 SER n 
1 202 ASP n 
1 203 ALA n 
1 204 LYS n 
1 205 PRO n 
1 206 PRO n 
1 207 ALA n 
1 208 VAL n 
1 209 PHE n 
1 210 THR n 
1 211 ARG n 
1 212 ILE n 
1 213 SER n 
1 214 HIS n 
1 215 TYR n 
1 216 ARG n 
1 217 PRO n 
1 218 TRP n 
1 219 ILE n 
1 220 ASN n 
1 221 GLN n 
1 222 ILE n 
1 223 LEU n 
1 224 GLN n 
1 225 ALA n 
1 226 ASN n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   226 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'CMA1, CYH, CYM' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
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 
A1AOP non-polymer         . '5-fluoro-N-[2-(methanesulfonyl)-4-(pyridin-4-yl)phenyl]-3-methyl-1-benzothiophene-2-sulfonamide' ? 
'C21 H17 F N2 O4 S3' 476.564 
ALA   'L-peptide linking' y ALANINE                                                                                           ? 
'C3 H7 N O2'         89.093  
ARG   'L-peptide linking' y ARGININE                                                                                          ? 
'C6 H15 N4 O2 1'     175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                                                        ? 
'C4 H8 N2 O3'        132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                                                   ? 
'C4 H7 N O4'         133.103 
CYS   'L-peptide linking' y CYSTEINE                                                                                          ? 
'C3 H7 N O2 S'       121.158 
GLN   'L-peptide linking' y GLUTAMINE                                                                                         ? 
'C5 H10 N2 O3'       146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                                                   ? 
'C5 H9 N O4'         147.129 
GLY   'peptide linking'   y GLYCINE                                                                                           ? 
'C2 H5 N O2'         75.067  
HIS   'L-peptide linking' y HISTIDINE                                                                                         ? 
'C6 H10 N3 O2 1'     156.162 
HOH   non-polymer         . WATER                                                                                             ? 
'H2 O'               18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                                        ? 
'C6 H13 N O2'        131.173 
LEU   'L-peptide linking' y LEUCINE                                                                                           ? 
'C6 H13 N O2'        131.173 
LYS   'L-peptide linking' y LYSINE                                                                                            ? 
'C6 H15 N2 O2 1'     147.195 
MET   'L-peptide linking' y METHIONINE                                                                                        ? 
'C5 H11 N O2 S'      149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                                                     ? 
'C9 H11 N O2'        165.189 
PRO   'L-peptide linking' y PROLINE                                                                                           ? 
'C5 H9 N O2'         115.130 
SER   'L-peptide linking' y SERINE                                                                                            ? 
'C3 H7 N O3'         105.093 
THR   'L-peptide linking' y THREONINE                                                                                         ? 
'C4 H9 N O3'         119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                                                        ? 
'C11 H12 N2 O2'      204.225 
TYR   'L-peptide linking' y TYROSINE                                                                                          ? 
'C9 H11 N O3'        181.189 
VAL   'L-peptide linking' y VALINE                                                                                            ? 
'C5 H11 N O2'        117.146 
ZN    non-polymer         . 'ZINC ION'                                                                                        ? 
'Zn 2'               65.409  
# 
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   16  16  ILE ILE A . n 
A 1 2   ILE 2   17  17  ILE ILE A . n 
A 1 3   GLY 3   18  18  GLY GLY A . n 
A 1 4   GLY 4   19  19  GLY GLY A . n 
A 1 5   THR 5   20  20  THR THR A . n 
A 1 6   GLU 6   21  21  GLU GLU A . n 
A 1 7   SER 7   22  22  SER SER A . n 
A 1 8   LYS 8   23  23  LYS LYS A . n 
A 1 9   PRO 9   24  24  PRO PRO A . n 
A 1 10  HIS 10  25  25  HIS HIS A . n 
A 1 11  SER 11  26  26  SER SER A . n 
A 1 12  ARG 12  27  27  ARG ARG A . n 
A 1 13  PRO 13  28  28  PRO PRO A . n 
A 1 14  TYR 14  29  29  TYR TYR A . n 
A 1 15  MET 15  30  30  MET MET A . n 
A 1 16  ALA 16  31  31  ALA ALA A . n 
A 1 17  TYR 17  32  32  TYR TYR A . n 
A 1 18  LEU 18  33  33  LEU LEU A . n 
A 1 19  GLU 19  34  34  GLU GLU A . n 
A 1 20  ILE 20  35  35  ILE ILE A . n 
A 1 21  VAL 21  36  36  VAL VAL A . n 
A 1 22  THR 22  36  36  THR THR A A n 
A 1 23  SER 23  36  36  SER SER A B n 
A 1 24  ASN 24  37  37  ASN ASN A . n 
A 1 25  GLY 25  37  37  GLY GLY A A n 
A 1 26  PRO 26  38  38  PRO PRO A . n 
A 1 27  SER 27  39  39  SER SER A . n 
A 1 28  LYS 28  40  40  LYS LYS A . n 
A 1 29  PHE 29  41  41  PHE PHE A . n 
A 1 30  CYS 30  42  42  CYS CYS A . n 
A 1 31  GLY 31  43  43  GLY GLY A . n 
A 1 32  GLY 32  44  44  GLY GLY A . n 
A 1 33  PHE 33  45  45  PHE PHE A . n 
A 1 34  LEU 34  46  46  LEU LEU A . n 
A 1 35  ILE 35  47  47  ILE ILE A . n 
A 1 36  ARG 36  48  48  ARG ARG A . n 
A 1 37  ARG 37  49  49  ARG ARG A . n 
A 1 38  ASN 38  50  50  ASN ASN A . n 
A 1 39  PHE 39  51  51  PHE PHE A . n 
A 1 40  VAL 40  52  52  VAL VAL A . n 
A 1 41  LEU 41  53  53  LEU LEU A . n 
A 1 42  THR 42  54  54  THR THR A . n 
A 1 43  ALA 43  55  55  ALA ALA A . n 
A 1 44  ALA 44  56  56  ALA ALA A . n 
A 1 45  HIS 45  57  57  HIS HIS A . n 
A 1 46  CYS 46  58  58  CYS CYS A . n 
A 1 47  ALA 47  59  59  ALA ALA A . n 
A 1 48  GLY 48  60  60  GLY GLY A . n 
A 1 49  ARG 49  61  61  ARG ARG A . n 
A 1 50  SER 50  63  63  SER SER A . n 
A 1 51  ILE 51  64  64  ILE ILE A . n 
A 1 52  THR 52  65  65  THR THR A . n 
A 1 53  VAL 53  66  66  VAL VAL A . n 
A 1 54  THR 54  67  67  THR THR A . n 
A 1 55  LEU 55  68  68  LEU LEU A . n 
A 1 56  GLY 56  69  69  GLY GLY A . n 
A 1 57  ALA 57  70  70  ALA ALA A . n 
A 1 58  HIS 58  71  71  HIS HIS A . n 
A 1 59  ASN 59  72  72  ASN ASN A . n 
A 1 60  ILE 60  73  73  ILE ILE A . n 
A 1 61  THR 61  74  74  THR THR A . n 
A 1 62  GLU 62  75  75  GLU GLU A . n 
A 1 63  GLU 63  76  76  GLU GLU A . n 
A 1 64  GLU 64  77  77  GLU GLU A . n 
A 1 65  ASP 65  78  78  ASP ASP A . n 
A 1 66  THR 66  79  79  THR THR A . n 
A 1 67  TRP 67  80  80  TRP TRP A . n 
A 1 68  GLN 68  81  81  GLN GLN A . n 
A 1 69  LYS 69  82  82  LYS LYS A . n 
A 1 70  LEU 70  83  83  LEU LEU A . n 
A 1 71  GLU 71  84  84  GLU GLU A . n 
A 1 72  VAL 72  85  85  VAL VAL A . n 
A 1 73  ILE 73  86  86  ILE ILE A . n 
A 1 74  LYS 74  87  87  LYS LYS A . n 
A 1 75  GLN 75  88  88  GLN GLN A . n 
A 1 76  PHE 76  89  89  PHE PHE A . n 
A 1 77  ARG 77  90  90  ARG ARG A . n 
A 1 78  HIS 78  91  91  HIS HIS A . n 
A 1 79  PRO 79  92  92  PRO PRO A . n 
A 1 80  LYS 80  93  93  LYS LYS A . n 
A 1 81  TYR 81  94  94  TYR TYR A . n 
A 1 82  ASN 82  95  95  ASN ASN A . n 
A 1 83  THR 83  96  96  THR THR A . n 
A 1 84  SER 84  97  97  SER SER A . n 
A 1 85  THR 85  98  98  THR THR A . n 
A 1 86  LEU 86  99  99  LEU LEU A . n 
A 1 87  HIS 87  100 100 HIS HIS A . n 
A 1 88  HIS 88  101 101 HIS HIS A . n 
A 1 89  ASP 89  102 102 ASP ASP A . n 
A 1 90  ILE 90  103 103 ILE ILE A . n 
A 1 91  MET 91  104 104 MET MET A . n 
A 1 92  LEU 92  105 105 LEU LEU A . n 
A 1 93  LEU 93  106 106 LEU LEU A . n 
A 1 94  LYS 94  107 107 LYS LYS A . n 
A 1 95  LEU 95  108 108 LEU LEU A . n 
A 1 96  LYS 96  109 109 LYS LYS A . n 
A 1 97  GLU 97  110 110 GLU GLU A . n 
A 1 98  LYS 98  111 111 LYS LYS A . n 
A 1 99  ALA 99  112 112 ALA ALA A . n 
A 1 100 SER 100 113 113 SER SER A . n 
A 1 101 LEU 101 114 114 LEU LEU A . n 
A 1 102 THR 102 115 115 THR THR A . n 
A 1 103 LEU 103 116 116 LEU LEU A . n 
A 1 104 ALA 104 117 117 ALA ALA A . n 
A 1 105 VAL 105 118 118 VAL VAL A . n 
A 1 106 GLY 106 119 119 GLY GLY A . n 
A 1 107 THR 107 120 120 THR THR A . n 
A 1 108 LEU 108 121 121 LEU LEU A . n 
A 1 109 PRO 109 122 122 PRO PRO A . n 
A 1 110 PHE 110 123 123 PHE PHE A . n 
A 1 111 PRO 111 124 ?   ?   ?   A . n 
A 1 112 SER 112 125 ?   ?   ?   A . n 
A 1 113 GLN 113 126 ?   ?   ?   A . n 
A 1 114 LYS 114 127 ?   ?   ?   A . n 
A 1 115 ASN 115 128 ?   ?   ?   A . n 
A 1 116 PHE 116 129 ?   ?   ?   A . n 
A 1 117 VAL 117 130 130 VAL VAL A . n 
A 1 118 PRO 118 131 131 PRO PRO A . n 
A 1 119 PRO 119 132 132 PRO PRO A . n 
A 1 120 GLY 120 133 133 GLY GLY A . n 
A 1 121 ARG 121 134 134 ARG ARG A . n 
A 1 122 MET 122 135 135 MET MET A . n 
A 1 123 CYS 123 136 136 CYS CYS A . n 
A 1 124 ARG 124 137 137 ARG ARG A . n 
A 1 125 VAL 125 138 138 VAL VAL A . n 
A 1 126 ALA 126 139 139 ALA ALA A . n 
A 1 127 GLY 127 140 140 GLY GLY A . n 
A 1 128 TRP 128 141 141 TRP TRP A . n 
A 1 129 GLY 129 142 142 GLY GLY A . n 
A 1 130 ARG 130 143 143 ARG ARG A . n 
A 1 131 THR 131 144 144 THR THR A . n 
A 1 132 GLY 132 145 145 GLY GLY A . n 
A 1 133 VAL 133 146 146 VAL VAL A . n 
A 1 134 LEU 134 147 147 LEU LEU A . n 
A 1 135 LYS 135 148 148 LYS LYS A . n 
A 1 136 PRO 136 150 150 PRO PRO A . n 
A 1 137 GLY 137 151 151 GLY GLY A . n 
A 1 138 SER 138 152 152 SER SER A . n 
A 1 139 ASP 139 153 153 ASP ASP A . n 
A 1 140 THR 140 154 154 THR THR A . n 
A 1 141 LEU 141 155 155 LEU LEU A . n 
A 1 142 GLN 142 156 156 GLN GLN A . n 
A 1 143 GLU 143 157 157 GLU GLU A . n 
A 1 144 VAL 144 158 158 VAL VAL A . n 
A 1 145 LYS 145 159 159 LYS LYS A . n 
A 1 146 LEU 146 160 160 LEU LEU A . n 
A 1 147 ARG 147 161 161 ARG ARG A . n 
A 1 148 LEU 148 162 162 LEU LEU A . n 
A 1 149 MET 149 163 163 MET MET A . n 
A 1 150 ASP 150 164 164 ASP ASP A . n 
A 1 151 PRO 151 165 165 PRO PRO A . n 
A 1 152 GLN 152 166 166 GLN GLN A . n 
A 1 153 ALA 153 167 167 ALA ALA A . n 
A 1 154 CYS 154 168 168 CYS CYS A . n 
A 1 155 SER 155 169 169 SER SER A . n 
A 1 156 HIS 156 172 172 HIS HIS A . n 
A 1 157 PHE 157 173 173 PHE PHE A . n 
A 1 158 ARG 158 174 174 ARG ARG A . n 
A 1 159 ASP 159 175 175 ASP ASP A . n 
A 1 160 PHE 160 176 176 PHE PHE A . n 
A 1 161 ASP 161 177 177 ASP ASP A . n 
A 1 162 HIS 162 178 178 HIS HIS A . n 
A 1 163 ASN 163 178 178 ASN ASN A A n 
A 1 164 LEU 164 179 179 LEU LEU A . n 
A 1 165 GLN 165 180 180 GLN GLN A . n 
A 1 166 LEU 166 181 181 LEU LEU A . n 
A 1 167 CYS 167 182 182 CYS CYS A . n 
A 1 168 VAL 168 183 183 VAL VAL A . n 
A 1 169 GLY 169 184 184 GLY GLY A . n 
A 1 170 ASN 170 185 185 ASN ASN A . n 
A 1 171 PRO 171 186 186 PRO PRO A . n 
A 1 172 ARG 172 186 186 ARG ARG A A n 
A 1 173 LYS 173 186 186 LYS LYS A B n 
A 1 174 THR 174 187 187 THR THR A . n 
A 1 175 LYS 175 188 188 LYS LYS A . n 
A 1 176 SER 176 189 189 SER SER A . n 
A 1 177 ALA 177 190 190 ALA ALA A . n 
A 1 178 PHE 178 191 191 PHE PHE A . n 
A 1 179 LYS 179 192 192 LYS LYS A . n 
A 1 180 GLY 180 193 193 GLY GLY A . n 
A 1 181 ASP 181 194 194 ASP ASP A . n 
A 1 182 SER 182 195 195 SER SER A . n 
A 1 183 GLY 183 196 196 GLY GLY A . n 
A 1 184 GLY 184 197 197 GLY GLY A . n 
A 1 185 PRO 185 198 198 PRO PRO A . n 
A 1 186 LEU 186 199 199 LEU LEU A . n 
A 1 187 LEU 187 200 200 LEU LEU A . n 
A 1 188 CYS 188 201 201 CYS CYS A . n 
A 1 189 ALA 189 202 202 ALA ALA A . n 
A 1 190 GLY 190 207 207 GLY GLY A . n 
A 1 191 VAL 191 208 208 VAL VAL A . n 
A 1 192 ALA 192 209 209 ALA ALA A . n 
A 1 193 GLN 193 210 210 GLN GLN A . n 
A 1 194 GLY 194 211 211 GLY GLY A . n 
A 1 195 ILE 195 212 212 ILE ILE A . n 
A 1 196 VAL 196 213 213 VAL VAL A . n 
A 1 197 SER 197 214 214 SER SER A . n 
A 1 198 TYR 198 215 215 TYR TYR A . n 
A 1 199 GLY 199 216 216 GLY GLY A . n 
A 1 200 ARG 200 217 217 ARG ARG A . n 
A 1 201 SER 201 218 218 SER SER A . n 
A 1 202 ASP 202 219 219 ASP ASP A . n 
A 1 203 ALA 203 220 220 ALA ALA A . n 
A 1 204 LYS 204 221 221 LYS LYS A . n 
A 1 205 PRO 205 224 224 PRO PRO A . n 
A 1 206 PRO 206 225 225 PRO PRO A . n 
A 1 207 ALA 207 226 226 ALA ALA A . n 
A 1 208 VAL 208 227 227 VAL VAL A . n 
A 1 209 PHE 209 228 228 PHE PHE A . n 
A 1 210 THR 210 229 229 THR THR A . n 
A 1 211 ARG 211 230 230 ARG ARG A . n 
A 1 212 ILE 212 231 231 ILE ILE A . n 
A 1 213 SER 213 232 232 SER SER A . n 
A 1 214 HIS 214 233 233 HIS HIS A . n 
A 1 215 TYR 215 234 234 TYR TYR A . n 
A 1 216 ARG 216 235 235 ARG ARG A . n 
A 1 217 PRO 217 236 236 PRO PRO A . n 
A 1 218 TRP 218 237 237 TRP TRP A . n 
A 1 219 ILE 219 238 238 ILE ILE A . n 
A 1 220 ASN 220 239 239 ASN ASN A . n 
A 1 221 GLN 221 240 240 GLN GLN A . n 
A 1 222 ILE 222 241 241 ILE ILE A . n 
A 1 223 LEU 223 242 242 LEU LEU A . n 
A 1 224 GLN 224 243 243 GLN GLN A . n 
A 1 225 ALA 225 244 244 ALA ALA A . n 
A 1 226 ASN 226 245 245 ASN ASN A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1AOP 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1AOP 
_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 ZN    1   301 1000 ZN    ZN  A . 
C 3 A1AOP 1   302 1    A1AOP 125 A . 
D 4 HOH   1   401 613  HOH   HOH A . 
D 4 HOH   2   402 509  HOH   HOH A . 
D 4 HOH   3   403 234  HOH   HOH A . 
D 4 HOH   4   404 534  HOH   HOH A . 
D 4 HOH   5   405 524  HOH   HOH A . 
D 4 HOH   6   406 11   HOH   HOH A . 
D 4 HOH   7   407 78   HOH   HOH A . 
D 4 HOH   8   408 512  HOH   HOH A . 
D 4 HOH   9   409 19   HOH   HOH A . 
D 4 HOH   10  410 605  HOH   HOH A . 
D 4 HOH   11  411 275  HOH   HOH A . 
D 4 HOH   12  412 126  HOH   HOH A . 
D 4 HOH   13  413 403  HOH   HOH A . 
D 4 HOH   14  414 67   HOH   HOH A . 
D 4 HOH   15  415 503  HOH   HOH A . 
D 4 HOH   16  416 315  HOH   HOH A . 
D 4 HOH   17  417 212  HOH   HOH A . 
D 4 HOH   18  418 201  HOH   HOH A . 
D 4 HOH   19  419 737  HOH   HOH A . 
D 4 HOH   20  420 145  HOH   HOH A . 
D 4 HOH   21  421 343  HOH   HOH A . 
D 4 HOH   22  422 36   HOH   HOH A . 
D 4 HOH   23  423 52   HOH   HOH A . 
D 4 HOH   24  424 1    HOH   HOH A . 
D 4 HOH   25  425 23   HOH   HOH A . 
D 4 HOH   26  426 58   HOH   HOH A . 
D 4 HOH   27  427 21   HOH   HOH A . 
D 4 HOH   28  428 189  HOH   HOH A . 
D 4 HOH   29  429 160  HOH   HOH A . 
D 4 HOH   30  430 101  HOH   HOH A . 
D 4 HOH   31  431 407  HOH   HOH A . 
D 4 HOH   32  432 70   HOH   HOH A . 
D 4 HOH   33  433 222  HOH   HOH A . 
D 4 HOH   34  434 536  HOH   HOH A . 
D 4 HOH   35  435 41   HOH   HOH A . 
D 4 HOH   36  436 143  HOH   HOH A . 
D 4 HOH   37  437 404  HOH   HOH A . 
D 4 HOH   38  438 45   HOH   HOH A . 
D 4 HOH   39  439 15   HOH   HOH A . 
D 4 HOH   40  440 4    HOH   HOH A . 
D 4 HOH   41  441 108  HOH   HOH A . 
D 4 HOH   42  442 408  HOH   HOH A . 
D 4 HOH   43  443 106  HOH   HOH A . 
D 4 HOH   44  444 185  HOH   HOH A . 
D 4 HOH   45  445 119  HOH   HOH A . 
D 4 HOH   46  446 167  HOH   HOH A . 
D 4 HOH   47  447 400  HOH   HOH A . 
D 4 HOH   48  448 2    HOH   HOH A . 
D 4 HOH   49  449 30   HOH   HOH A . 
D 4 HOH   50  450 9    HOH   HOH A . 
D 4 HOH   51  451 186  HOH   HOH A . 
D 4 HOH   52  452 267  HOH   HOH A . 
D 4 HOH   53  453 383  HOH   HOH A . 
D 4 HOH   54  454 164  HOH   HOH A . 
D 4 HOH   55  455 630  HOH   HOH A . 
D 4 HOH   56  456 286  HOH   HOH A . 
D 4 HOH   57  457 34   HOH   HOH A . 
D 4 HOH   58  458 138  HOH   HOH A . 
D 4 HOH   59  459 39   HOH   HOH A . 
D 4 HOH   60  460 131  HOH   HOH A . 
D 4 HOH   61  461 68   HOH   HOH A . 
D 4 HOH   62  462 94   HOH   HOH A . 
D 4 HOH   63  463 8    HOH   HOH A . 
D 4 HOH   64  464 17   HOH   HOH A . 
D 4 HOH   65  465 27   HOH   HOH A . 
D 4 HOH   66  466 281  HOH   HOH A . 
D 4 HOH   67  467 502  HOH   HOH A . 
D 4 HOH   68  468 25   HOH   HOH A . 
D 4 HOH   69  469 99   HOH   HOH A . 
D 4 HOH   70  470 16   HOH   HOH A . 
D 4 HOH   71  471 542  HOH   HOH A . 
D 4 HOH   72  472 20   HOH   HOH A . 
D 4 HOH   73  473 734  HOH   HOH A . 
D 4 HOH   74  474 255  HOH   HOH A . 
D 4 HOH   75  475 305  HOH   HOH A . 
D 4 HOH   76  476 10   HOH   HOH A . 
D 4 HOH   77  477 48   HOH   HOH A . 
D 4 HOH   78  478 5    HOH   HOH A . 
D 4 HOH   79  479 33   HOH   HOH A . 
D 4 HOH   80  480 59   HOH   HOH A . 
D 4 HOH   81  481 342  HOH   HOH A . 
D 4 HOH   82  482 733  HOH   HOH A . 
D 4 HOH   83  483 91   HOH   HOH A . 
D 4 HOH   84  484 204  HOH   HOH A . 
D 4 HOH   85  485 147  HOH   HOH A . 
D 4 HOH   86  486 242  HOH   HOH A . 
D 4 HOH   87  487 735  HOH   HOH A . 
D 4 HOH   88  488 175  HOH   HOH A . 
D 4 HOH   89  489 66   HOH   HOH A . 
D 4 HOH   90  490 389  HOH   HOH A . 
D 4 HOH   91  491 49   HOH   HOH A . 
D 4 HOH   92  492 700  HOH   HOH A . 
D 4 HOH   93  493 24   HOH   HOH A . 
D 4 HOH   94  494 518  HOH   HOH A . 
D 4 HOH   95  495 38   HOH   HOH A . 
D 4 HOH   96  496 47   HOH   HOH A . 
D 4 HOH   97  497 519  HOH   HOH A . 
D 4 HOH   98  498 152  HOH   HOH A . 
D 4 HOH   99  499 13   HOH   HOH A . 
D 4 HOH   100 500 82   HOH   HOH A . 
D 4 HOH   101 501 7    HOH   HOH A . 
D 4 HOH   102 502 12   HOH   HOH A . 
D 4 HOH   103 503 604  HOH   HOH A . 
D 4 HOH   104 504 105  HOH   HOH A . 
D 4 HOH   105 505 97   HOH   HOH A . 
D 4 HOH   106 506 401  HOH   HOH A . 
D 4 HOH   107 507 168  HOH   HOH A . 
D 4 HOH   108 508 51   HOH   HOH A . 
D 4 HOH   109 509 226  HOH   HOH A . 
D 4 HOH   110 510 414  HOH   HOH A . 
D 4 HOH   111 511 274  HOH   HOH A . 
D 4 HOH   112 512 181  HOH   HOH A . 
D 4 HOH   113 513 409  HOH   HOH A . 
D 4 HOH   114 514 158  HOH   HOH A . 
D 4 HOH   115 515 102  HOH   HOH A . 
D 4 HOH   116 516 291  HOH   HOH A . 
D 4 HOH   117 517 81   HOH   HOH A . 
D 4 HOH   118 518 412  HOH   HOH A . 
D 4 HOH   119 519 90   HOH   HOH A . 
D 4 HOH   120 520 42   HOH   HOH A . 
D 4 HOH   121 521 28   HOH   HOH A . 
D 4 HOH   122 522 732  HOH   HOH A . 
D 4 HOH   123 523 148  HOH   HOH A . 
D 4 HOH   124 524 88   HOH   HOH A . 
D 4 HOH   125 525 196  HOH   HOH A . 
D 4 HOH   126 526 662  HOH   HOH A . 
D 4 HOH   127 527 292  HOH   HOH A . 
D 4 HOH   128 528 71   HOH   HOH A . 
D 4 HOH   129 529 63   HOH   HOH A . 
D 4 HOH   130 530 411  HOH   HOH A . 
D 4 HOH   131 531 132  HOH   HOH A . 
D 4 HOH   132 532 123  HOH   HOH A . 
D 4 HOH   133 533 190  HOH   HOH A . 
D 4 HOH   134 534 233  HOH   HOH A . 
D 4 HOH   135 535 609  HOH   HOH A . 
D 4 HOH   136 536 120  HOH   HOH A . 
D 4 HOH   137 537 157  HOH   HOH A . 
D 4 HOH   138 538 79   HOH   HOH A . 
D 4 HOH   139 539 61   HOH   HOH A . 
D 4 HOH   140 540 149  HOH   HOH A . 
D 4 HOH   141 541 351  HOH   HOH A . 
D 4 HOH   142 542 632  HOH   HOH A . 
D 4 HOH   143 543 501  HOH   HOH A . 
D 4 HOH   144 544 156  HOH   HOH A . 
D 4 HOH   145 545 670  HOH   HOH A . 
D 4 HOH   146 546 32   HOH   HOH A . 
D 4 HOH   147 547 29   HOH   HOH A . 
D 4 HOH   148 548 114  HOH   HOH A . 
D 4 HOH   149 549 372  HOH   HOH A . 
D 4 HOH   150 550 603  HOH   HOH A . 
D 4 HOH   151 551 56   HOH   HOH A . 
D 4 HOH   152 552 87   HOH   HOH A . 
D 4 HOH   153 553 624  HOH   HOH A . 
D 4 HOH   154 554 6    HOH   HOH A . 
D 4 HOH   155 555 397  HOH   HOH A . 
D 4 HOH   156 556 171  HOH   HOH A . 
D 4 HOH   157 557 134  HOH   HOH A . 
D 4 HOH   158 558 60   HOH   HOH A . 
D 4 HOH   159 559 615  HOH   HOH A . 
D 4 HOH   160 560 127  HOH   HOH A . 
D 4 HOH   161 561 184  HOH   HOH A . 
D 4 HOH   162 562 65   HOH   HOH A . 
D 4 HOH   163 563 161  HOH   HOH A . 
D 4 HOH   164 564 736  HOH   HOH A . 
D 4 HOH   165 565 511  HOH   HOH A . 
D 4 HOH   166 566 271  HOH   HOH A . 
D 4 HOH   167 567 612  HOH   HOH A . 
D 4 HOH   168 568 336  HOH   HOH A . 
D 4 HOH   169 569 627  HOH   HOH A . 
D 4 HOH   170 570 244  HOH   HOH A . 
D 4 HOH   171 571 685  HOH   HOH A . 
D 4 HOH   172 572 142  HOH   HOH A . 
D 4 HOH   173 573 705  HOH   HOH A . 
D 4 HOH   174 574 325  HOH   HOH A . 
D 4 HOH   175 575 618  HOH   HOH A . 
D 4 HOH   176 576 650  HOH   HOH A . 
D 4 HOH   177 577 205  HOH   HOH A . 
D 4 HOH   178 578 413  HOH   HOH A . 
D 4 HOH   179 579 689  HOH   HOH A . 
D 4 HOH   180 580 261  HOH   HOH A . 
D 4 HOH   181 581 309  HOH   HOH A . 
D 4 HOH   182 582 686  HOH   HOH A . 
D 4 HOH   183 583 725  HOH   HOH A . 
D 4 HOH   184 584 221  HOH   HOH A . 
D 4 HOH   185 585 606  HOH   HOH A . 
D 4 HOH   186 586 188  HOH   HOH A . 
D 4 HOH   187 587 277  HOH   HOH A . 
D 4 HOH   188 588 265  HOH   HOH A . 
D 4 HOH   189 589 674  HOH   HOH A . 
D 4 HOH   190 590 116  HOH   HOH A . 
D 4 HOH   191 591 18   HOH   HOH A . 
D 4 HOH   192 592 675  HOH   HOH A . 
D 4 HOH   193 593 672  HOH   HOH A . 
D 4 HOH   194 594 121  HOH   HOH A . 
D 4 HOH   195 595 159  HOH   HOH A . 
D 4 HOH   196 596 124  HOH   HOH A . 
D 4 HOH   197 597 540  HOH   HOH A . 
D 4 HOH   198 598 154  HOH   HOH A . 
D 4 HOH   199 599 608  HOH   HOH A . 
# 
loop_
_software.classification 
_software.name 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
refinement       REFMAC 5.8.0425 ? 1 
'data scaling'   XSCALE .        ? 2 
'data reduction' XDS    .        ? 3 
phasing          PHASER .        ? 4 
# 
_cell.entry_id           7H6E 
_cell.length_a           59.080 
_cell.length_b           59.140 
_cell.length_c           72.490 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        90.00 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7H6E 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
# 
_exptl.entry_id          7H6E 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.60 
_exptl_crystal.density_percent_sol   52.74 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          MICROBATCH 
_exptl_crystal_grow.pH              8.5 
_exptl_crystal_grow.temp            293 
_exptl_crystal_grow.pdbx_details    
;Sample of human Chymase in 50 mM MES/NaOH pH 5.5, 150mM NaCl, 1mM TCEP, 10% Glycerol) at a concentration of 11mg/ml to 14mg/ml.Add [2-[(4-methylpyridin-2-yl)amino]-2-oxoethyl] 2-methylquinoline-4-carboxylate at 10x molar ratio. The compound helps to obtain crystals but is not visible in the structures. Add 0.5 mM ZnCl2. Add inhibitor, incubate for 16h on ice. Crystallize using microbatch setups with Al's oil (Hampton Research), with total drop size 1ul with 50% protein sample, using crystallization reagent of 0.1M Tris/HCl pH 8.5, 0.2M NaCl, 25% PEG 3350.
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp_details    ? 
# 
_diffrn.id                     1 
_diffrn.crystal_id             1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.type                   'MAR scanner 345 mm plate' 
_diffrn_detector.detector               'IMAGE PLATE' 
_diffrn_detector.pdbx_collection_date   2006-02-08 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_scattering_type             x-ray 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    ? 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.5418 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.pdbx_wavelength_list        1.5418 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      'ROTATING ANODE' 
_diffrn_source.type                        'BRUKER AXS MICROSTAR' 
_diffrn_source.pdbx_synchrotron_site       ? 
_diffrn_source.pdbx_synchrotron_beamline   ? 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7H6E 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             19.03 
_reflns.d_resolution_high            2.0 
_reflns.number_obs                   15954 
_reflns.percent_possible_obs         89.9 
_reflns.pdbx_Rmerge_I_obs            0.06 
_reflns.pdbx_netI_over_sigmaI        16.70 
_reflns.pdbx_Rrim_I_all              0.07 
_reflns.pdbx_number_measured_all     59477 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.number_all                   ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              ? 
# 
loop_
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_ordinal 
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_unique_obs 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.percent_possible_obs 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_redundancy 
1 1 2.00 2.12  9750 2596 0.259 92.5 5.30  0.302 ? ? ? ? 
1 2 2.12 2.26  6657 1765 0.203 69.6 6.54  0.236 ? ? ? ? 
1 3 2.26 2.44  7705 2041 0.135 82.4 9.58  0.158 ? ? ? ? 
1 4 2.44 2.67  8306 2202 0.11  95.2 11.60 0.129 ? ? ? ? 
1 5 2.67 2.98  7543 2003 0.076 96.0 15.68 0.088 ? ? ? ? 
1 6 2.98 3.43  6707 1795 0.047 96.8 23.02 0.055 ? ? ? ? 
1 7 3.43 4.16  5577 1515 0.036 96.7 28.89 0.042 ? ? ? ? 
1 8 4.16 5.76  4559 1254 0.026 97.9 38.66 0.03  ? ? ? ? 
1 9 5.76 19.03 2673 783  0.025 95.1 39.72 0.03  ? ? ? ? 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 7H6E 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     15163 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             19.03 
_refine.ls_d_res_high                            2.00 
_refine.ls_percent_reflns_obs                    89.95 
_refine.ls_R_factor_obs                          0.18840 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.18478 
_refine.ls_R_factor_R_free                       0.26071 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_number_reflns_R_free                  799 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.947 
_refine.correlation_coeff_Fo_to_Fc_free          0.892 
_refine.B_iso_mean                               22.755 
_refine.aniso_B[1][1]                            2.07 
_refine.aniso_B[2][2]                            -0.32 
_refine.aniso_B[3][3]                            -1.75 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][3]                            0.00 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       0.205 
_refine.pdbx_overall_ESU_R_Free                  0.199 
_refine.overall_SU_ML                            0.132 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             4.924 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        1709 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         32 
_refine_hist.number_atoms_solvent             199 
_refine_hist.number_atoms_total               1940 
_refine_hist.d_res_high                       2.00 
_refine_hist.d_res_low                        19.03 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
r_bond_refined_d             0.011  0.012  ? 1837 'X-RAY DIFFRACTION' ? 
r_bond_other_d               0.001  0.016  ? 1738 'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.787  1.680  ? 2496 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            0.571  1.571  ? 4011 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       7.986  5.000  ? 227  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       30.831 20.610 ? 82   'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       14.084 14.920 ? 312  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       19.556 15.000 ? 14   'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.082  0.200  ? 235  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.011  0.020  ? 2077 'X-RAY DIFFRACTION' ? 
r_gen_planes_other           0.001  0.020  ? 419  'X-RAY DIFFRACTION' ? 
r_nbd_refined                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbd_other                  ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_refined              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_other                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined        ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_other          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_refined          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_other            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_other         ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined     ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_other       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_refined ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_other   ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcbond_it                  2.887  2.339  ? 903  'X-RAY DIFFRACTION' ? 
r_mcbond_other               2.888  2.337  ? 902  'X-RAY DIFFRACTION' ? 
r_mcangle_it                 4.234  4.177  ? 1131 'X-RAY DIFFRACTION' ? 
r_mcangle_other              4.232  4.178  ? 1132 'X-RAY DIFFRACTION' ? 
r_scbond_it                  2.894  2.614  ? 934  'X-RAY DIFFRACTION' ? 
r_scbond_other               2.882  2.622  ? 900  'X-RAY DIFFRACTION' ? 
r_scangle_it                 ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_other              4.409  4.718  ? 1313 'X-RAY DIFFRACTION' ? 
r_long_range_B_refined       6.541  25.00  ? 2141 'X-RAY DIFFRACTION' ? 
r_long_range_B_other         6.416  22.68  ? 2034 'X-RAY DIFFRACTION' ? 
r_rigid_bond_restr           ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_sphericity_free            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_sphericity_bonded          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.d_res_high                       2.000 
_refine_ls_shell.d_res_low                        2.051 
_refine_ls_shell.number_reflns_R_work             1129 
_refine_ls_shell.R_factor_R_work                  0.316 
_refine_ls_shell.percent_reflns_obs               91.88 
_refine_ls_shell.R_factor_R_free                  0.388 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             47 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
# 
_struct.entry_id                  7H6E 
_struct.title                     
;THE 2.0 A CRYSTAL STRUCTURE OF HUMAN CHYMASE IN COMPLEX WITH 5-fluoro-3-methyl-N-(2-methylsulfonyl-4-pyridin-4-ylphenyl)-1-benzothiophene-2-sulfonamide
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7H6E 
_struct_keywords.pdbx_keywords   HYDROLASE 
_struct_keywords.text            'HUMAN CHYMASE, SERINE PROTEINASE, 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 ? 
D N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CMA1_HUMAN 
_struct_ref.pdbx_db_accession          P23946 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;IIGGTECKPHSRPYMAYLEIVTSNGPSKFCGGFLIRRNFVLTAAHCAGRSITVTLGAHNITEEEDTWQKLEVIKQFRHPK
YNTSTLHHDIMLLKLKEKASLTLAVGTLPFPSQFNFVPPGRMCRVAGWGRTGVLKPGSDTLQEVKLRLMDPQACSHFRDF
DHNLQLCVGNPRKTKSAFKGDSGGPLLCAGVAQGIVSYGRSDAKPPAVFTRISHYRPWINQILQAN
;
_struct_ref.pdbx_align_begin           22 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              7H6E 
_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                 226 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P23946 
_struct_ref_seq.db_align_beg                  22 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  247 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       16 
_struct_ref_seq.pdbx_auth_seq_align_end       245 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 7H6E SER A 7   ? UNP P23946 CYS 28  'engineered mutation' 22  1 
1 7H6E LYS A 114 ? UNP P23946 PHE 135 'engineered mutation' 127 2 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_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,D 
# 
_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 ALA A 43  ? ALA A 47  ? ALA A 55  ALA A 59  5 ? 5  
HELX_P HELX_P2 AA2 ASP A 150 ? SER A 155 ? ASP A 164 SER A 169 5 ? 6  
HELX_P HELX_P3 AA3 TYR A 215 ? ASN A 226 ? TYR A 234 ASN A 245 1 ? 12 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1 disulf ? ? A CYS 30  SG  ? ? ? 1_555 A CYS 46  SG ? ? A CYS 42  A CYS 58  1_555 ? ? ? ? ? ? ? 2.012 ? ? 
disulf2 disulf ? ? A CYS 123 SG  ? ? ? 1_555 A CYS 188 SG ? ? A CYS 136 A CYS 201 1_555 ? ? ? ? ? ? ? 2.068 ? ? 
disulf3 disulf ? ? A CYS 154 SG  ? ? ? 1_555 A CYS 167 SG ? ? A CYS 168 A CYS 182 1_555 ? ? ? ? ? ? ? 2.040 ? ? 
metalc1 metalc ? ? A HIS 10  NE2 ? ? ? 1_555 B ZN  .   ZN ? ? A HIS 25  A ZN  301 1_555 ? ? ? ? ? ? ? 2.044 ? ? 
metalc2 metalc ? ? A GLU 64  OE1 ? ? ? 1_555 B ZN  .   ZN ? ? A GLU 77  A ZN  301 1_555 ? ? ? ? ? ? ? 2.661 ? ? 
metalc3 metalc ? ? A GLU 64  OE2 ? ? ? 1_555 B ZN  .   ZN ? ? A GLU 77  A ZN  301 1_555 ? ? ? ? ? ? ? 1.985 ? ? 
metalc4 metalc ? ? A ASP 150 OD1 ? ? ? 1_555 B ZN  .   ZN ? ? A ASP 164 A ZN  301 2_454 ? ? ? ? ? ? ? 2.051 ? ? 
metalc5 metalc ? ? B ZN  .   ZN  ? ? ? 1_555 D HOH .   O  ? ? A ZN  301 A HOH 516 2_455 ? ? ? ? ? ? ? 2.139 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
metalc ? ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  NE2 ? A HIS 10  ? A HIS 25  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 OE1 ? A GLU 64  ? A GLU 77  ? 1_555 89.0  ? 
2  NE2 ? A HIS 10  ? A HIS 25  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 OE2 ? A GLU 64  ? A GLU 77  ? 1_555 119.4 ? 
3  OE1 ? A GLU 64  ? A GLU 77  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 OE2 ? A GLU 64  ? A GLU 77  ? 1_555 52.4  ? 
4  NE2 ? A HIS 10  ? A HIS 25  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 OD1 ? A ASP 150 ? A ASP 164 ? 1_555 47.7  ? 
5  OE1 ? A GLU 64  ? A GLU 77  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 OD1 ? A ASP 150 ? A ASP 164 ? 1_555 87.9  ? 
6  OE2 ? A GLU 64  ? A GLU 77  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 OD1 ? A ASP 150 ? A ASP 164 ? 1_555 140.2 ? 
7  NE2 ? A HIS 10  ? A HIS 25  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 O   ? D HOH .   ? A HOH 516 ? 2_455 114.1 ? 
8  OE1 ? A GLU 64  ? A GLU 77  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 O   ? D HOH .   ? A HOH 516 ? 2_455 88.3  ? 
9  OE2 ? A GLU 64  ? A GLU 77  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 O   ? D HOH .   ? A HOH 516 ? 2_455 109.6 ? 
10 OD1 ? A ASP 150 ? A ASP 164 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 O   ? D HOH .   ? A HOH 516 ? 2_455 66.3  ? 
# 
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 CYS A 30  ? CYS A 46  ? CYS A 42  ? 1_555 CYS A 58  ? 1_555 SG SG . . . None 'Disulfide bridge' 
2 CYS A 123 ? CYS A 188 ? CYS A 136 ? 1_555 CYS A 201 ? 1_555 SG SG . . . None 'Disulfide bridge' 
3 CYS A 154 ? CYS A 167 ? CYS A 168 ? 1_555 CYS A 182 ? 1_555 SG SG . . . None 'Disulfide bridge' 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          PRO 
_struct_mon_prot_cis.label_seq_id           205 
_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           PRO 
_struct_mon_prot_cis.auth_seq_id            224 
_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    206 
_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     225 
_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       1.49 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA1 7 8 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? 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 THR A 5   ? GLU A 6   ? THR A 20  GLU A 21  
AA1 2 GLN A 142 ? MET A 149 ? GLN A 156 MET A 163 
AA1 3 GLN A 165 ? VAL A 168 ? GLN A 180 VAL A 183 
AA1 4 ALA A 207 ? ARG A 211 ? ALA A 226 ARG A 230 
AA1 5 VAL A 191 ? TYR A 198 ? VAL A 208 TYR A 215 
AA1 6 PRO A 185 ? CYS A 188 ? PRO A 198 CYS A 201 
AA1 7 MET A 122 ? GLY A 127 ? MET A 135 GLY A 140 
AA1 8 GLN A 142 ? MET A 149 ? GLN A 156 MET A 163 
AA2 1 MET A 15  ? VAL A 21  ? MET A 30  VAL A 36  
AA2 2 SER A 27  ? ARG A 36  ? SER A 39  ARG A 48  
AA2 3 PHE A 39  ? THR A 42  ? PHE A 51  THR A 54  
AA2 4 MET A 91  ? LEU A 95  ? MET A 104 LEU A 108 
AA2 5 GLN A 68  ? ARG A 77  ? GLN A 81  ARG A 90  
AA2 6 SER A 50  ? LEU A 55  ? SER A 63  LEU A 68  
AA2 7 MET A 15  ? VAL A 21  ? MET A 30  VAL A 36  
# 
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 THR A 5   ? N THR A 20  O GLU A 143 ? O GLU A 157 
AA1 2 3 N MET A 149 ? N MET A 163 O CYS A 167 ? O CYS A 182 
AA1 3 4 N VAL A 168 ? N VAL A 183 O ALA A 207 ? O ALA A 226 
AA1 4 5 O VAL A 208 ? O VAL A 227 N TYR A 198 ? N TYR A 215 
AA1 5 6 O GLN A 193 ? O GLN A 210 N LEU A 186 ? N LEU A 199 
AA1 6 7 O LEU A 187 ? O LEU A 200 N ARG A 124 ? N ARG A 137 
AA1 7 8 N CYS A 123 ? N CYS A 136 O LEU A 146 ? O LEU A 160 
AA2 1 2 N ILE A 20  ? N ILE A 35  O LYS A 28  ? O LYS A 40  
AA2 2 3 N PHE A 33  ? N PHE A 45  O LEU A 41  ? O LEU A 53  
AA2 3 4 N VAL A 40  ? N VAL A 52  O LEU A 93  ? O LEU A 106 
AA2 4 5 O LEU A 92  ? O LEU A 105 N PHE A 76  ? N PHE A 89  
AA2 5 6 O GLN A 68  ? O GLN A 81  N LEU A 55  ? N LEU A 68  
AA2 6 7 O THR A 54  ? O THR A 67  N TYR A 17  ? N TYR A 32  
# 
_pdbx_entry_details.entry_id                   7H6E 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 OE1 A GLU 76  ? ? O A HOH 401 ? ? 2.05 
2 1 O   A LEU 121 ? ? O A HOH 402 ? ? 2.08 
3 1 N   A LEU 147 ? ? O A HOH 403 ? ? 2.08 
4 1 NH1 A ARG 143 ? ? O A HOH 404 ? ? 2.11 
5 1 O   A ARG 174 ? ? O A HOH 405 ? ? 2.15 
6 1 O   A HOH 517 ? ? O A HOH 562 ? ? 2.19 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 37  ? ? -99.10  -67.02 
2 1 HIS A 71  ? ? -124.67 -63.08 
3 1 SER A 214 ? ? -117.87 -70.56 
# 
_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                       599 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   6.65 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A PRO 124 ? A PRO 111 
2 1 Y 1 A SER 125 ? A SER 112 
3 1 Y 1 A GLN 126 ? A GLN 113 
4 1 Y 1 A LYS 127 ? A LYS 114 
5 1 Y 1 A ASN 128 ? A ASN 115 
6 1 Y 1 A PHE 129 ? A PHE 116 
# 
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 
A1AOP C2   C  Y N 1   
A1AOP C4   C  Y N 2   
A1AOP C5   C  Y N 3   
A1AOP F27  F  N N 4   
A1AOP C23  C  Y N 5   
A1AOP C26  C  Y N 6   
A1AOP C19  C  Y N 7   
A1AOP C10  C  Y N 8   
A1AOP S3   S  Y N 9   
A1AOP C17  C  Y N 10  
A1AOP C8   C  Y N 11  
A1AOP C25  C  N N 12  
A1AOP S1   S  N N 13  
A1AOP O12  O  N N 14  
A1AOP O13  O  N N 15  
A1AOP N7   N  N N 16  
A1AOP C9   C  Y N 17  
A1AOP C18  C  Y N 18  
A1AOP C21  C  Y N 19  
A1AOP C14  C  Y N 20  
A1AOP C22  C  Y N 21  
A1AOP C30  C  Y N 22  
A1AOP C28  C  Y N 23  
A1AOP C31  C  Y N 24  
A1AOP C29  C  Y N 25  
A1AOP N20  N  Y N 26  
A1AOP C11  C  Y N 27  
A1AOP S6   S  N N 28  
A1AOP O15  O  N N 29  
A1AOP O16  O  N N 30  
A1AOP C24  C  N N 31  
A1AOP H1   H  N N 32  
A1AOP H2   H  N N 33  
A1AOP H3   H  N N 34  
A1AOP H4   H  N N 35  
A1AOP H5   H  N N 36  
A1AOP H6   H  N N 37  
A1AOP H7   H  N N 38  
A1AOP H8   H  N N 39  
A1AOP H9   H  N N 40  
A1AOP H10  H  N N 41  
A1AOP H11  H  N N 42  
A1AOP H12  H  N N 43  
A1AOP H13  H  N N 44  
A1AOP H14  H  N N 45  
A1AOP H15  H  N N 46  
A1AOP H16  H  N N 47  
A1AOP H17  H  N N 48  
ALA   N    N  N N 49  
ALA   CA   C  N S 50  
ALA   C    C  N N 51  
ALA   O    O  N N 52  
ALA   CB   C  N N 53  
ALA   OXT  O  N N 54  
ALA   H    H  N N 55  
ALA   H2   H  N N 56  
ALA   HA   H  N N 57  
ALA   HB1  H  N N 58  
ALA   HB2  H  N N 59  
ALA   HB3  H  N N 60  
ALA   HXT  H  N N 61  
ARG   N    N  N N 62  
ARG   CA   C  N S 63  
ARG   C    C  N N 64  
ARG   O    O  N N 65  
ARG   CB   C  N N 66  
ARG   CG   C  N N 67  
ARG   CD   C  N N 68  
ARG   NE   N  N N 69  
ARG   CZ   C  N N 70  
ARG   NH1  N  N N 71  
ARG   NH2  N  N N 72  
ARG   OXT  O  N N 73  
ARG   H    H  N N 74  
ARG   H2   H  N N 75  
ARG   HA   H  N N 76  
ARG   HB2  H  N N 77  
ARG   HB3  H  N N 78  
ARG   HG2  H  N N 79  
ARG   HG3  H  N N 80  
ARG   HD2  H  N N 81  
ARG   HD3  H  N N 82  
ARG   HE   H  N N 83  
ARG   HH11 H  N N 84  
ARG   HH12 H  N N 85  
ARG   HH21 H  N N 86  
ARG   HH22 H  N N 87  
ARG   HXT  H  N N 88  
ASN   N    N  N N 89  
ASN   CA   C  N S 90  
ASN   C    C  N N 91  
ASN   O    O  N N 92  
ASN   CB   C  N N 93  
ASN   CG   C  N N 94  
ASN   OD1  O  N N 95  
ASN   ND2  N  N N 96  
ASN   OXT  O  N N 97  
ASN   H    H  N N 98  
ASN   H2   H  N N 99  
ASN   HA   H  N N 100 
ASN   HB2  H  N N 101 
ASN   HB3  H  N N 102 
ASN   HD21 H  N N 103 
ASN   HD22 H  N N 104 
ASN   HXT  H  N N 105 
ASP   N    N  N N 106 
ASP   CA   C  N S 107 
ASP   C    C  N N 108 
ASP   O    O  N N 109 
ASP   CB   C  N N 110 
ASP   CG   C  N N 111 
ASP   OD1  O  N N 112 
ASP   OD2  O  N N 113 
ASP   OXT  O  N N 114 
ASP   H    H  N N 115 
ASP   H2   H  N N 116 
ASP   HA   H  N N 117 
ASP   HB2  H  N N 118 
ASP   HB3  H  N N 119 
ASP   HD2  H  N N 120 
ASP   HXT  H  N N 121 
CYS   N    N  N N 122 
CYS   CA   C  N R 123 
CYS   C    C  N N 124 
CYS   O    O  N N 125 
CYS   CB   C  N N 126 
CYS   SG   S  N N 127 
CYS   OXT  O  N N 128 
CYS   H    H  N N 129 
CYS   H2   H  N N 130 
CYS   HA   H  N N 131 
CYS   HB2  H  N N 132 
CYS   HB3  H  N N 133 
CYS   HG   H  N N 134 
CYS   HXT  H  N N 135 
GLN   N    N  N N 136 
GLN   CA   C  N S 137 
GLN   C    C  N N 138 
GLN   O    O  N N 139 
GLN   CB   C  N N 140 
GLN   CG   C  N N 141 
GLN   CD   C  N N 142 
GLN   OE1  O  N N 143 
GLN   NE2  N  N N 144 
GLN   OXT  O  N N 145 
GLN   H    H  N N 146 
GLN   H2   H  N N 147 
GLN   HA   H  N N 148 
GLN   HB2  H  N N 149 
GLN   HB3  H  N N 150 
GLN   HG2  H  N N 151 
GLN   HG3  H  N N 152 
GLN   HE21 H  N N 153 
GLN   HE22 H  N N 154 
GLN   HXT  H  N N 155 
GLU   N    N  N N 156 
GLU   CA   C  N S 157 
GLU   C    C  N N 158 
GLU   O    O  N N 159 
GLU   CB   C  N N 160 
GLU   CG   C  N N 161 
GLU   CD   C  N N 162 
GLU   OE1  O  N N 163 
GLU   OE2  O  N N 164 
GLU   OXT  O  N N 165 
GLU   H    H  N N 166 
GLU   H2   H  N N 167 
GLU   HA   H  N N 168 
GLU   HB2  H  N N 169 
GLU   HB3  H  N N 170 
GLU   HG2  H  N N 171 
GLU   HG3  H  N N 172 
GLU   HE2  H  N N 173 
GLU   HXT  H  N N 174 
GLY   N    N  N N 175 
GLY   CA   C  N N 176 
GLY   C    C  N N 177 
GLY   O    O  N N 178 
GLY   OXT  O  N N 179 
GLY   H    H  N N 180 
GLY   H2   H  N N 181 
GLY   HA2  H  N N 182 
GLY   HA3  H  N N 183 
GLY   HXT  H  N N 184 
HIS   N    N  N N 185 
HIS   CA   C  N S 186 
HIS   C    C  N N 187 
HIS   O    O  N N 188 
HIS   CB   C  N N 189 
HIS   CG   C  Y N 190 
HIS   ND1  N  Y N 191 
HIS   CD2  C  Y N 192 
HIS   CE1  C  Y N 193 
HIS   NE2  N  Y N 194 
HIS   OXT  O  N N 195 
HIS   H    H  N N 196 
HIS   H2   H  N N 197 
HIS   HA   H  N N 198 
HIS   HB2  H  N N 199 
HIS   HB3  H  N N 200 
HIS   HD1  H  N N 201 
HIS   HD2  H  N N 202 
HIS   HE1  H  N N 203 
HIS   HE2  H  N N 204 
HIS   HXT  H  N N 205 
HOH   O    O  N N 206 
HOH   H1   H  N N 207 
HOH   H2   H  N N 208 
ILE   N    N  N N 209 
ILE   CA   C  N S 210 
ILE   C    C  N N 211 
ILE   O    O  N N 212 
ILE   CB   C  N S 213 
ILE   CG1  C  N N 214 
ILE   CG2  C  N N 215 
ILE   CD1  C  N N 216 
ILE   OXT  O  N N 217 
ILE   H    H  N N 218 
ILE   H2   H  N N 219 
ILE   HA   H  N N 220 
ILE   HB   H  N N 221 
ILE   HG12 H  N N 222 
ILE   HG13 H  N N 223 
ILE   HG21 H  N N 224 
ILE   HG22 H  N N 225 
ILE   HG23 H  N N 226 
ILE   HD11 H  N N 227 
ILE   HD12 H  N N 228 
ILE   HD13 H  N N 229 
ILE   HXT  H  N N 230 
LEU   N    N  N N 231 
LEU   CA   C  N S 232 
LEU   C    C  N N 233 
LEU   O    O  N N 234 
LEU   CB   C  N N 235 
LEU   CG   C  N N 236 
LEU   CD1  C  N N 237 
LEU   CD2  C  N N 238 
LEU   OXT  O  N N 239 
LEU   H    H  N N 240 
LEU   H2   H  N N 241 
LEU   HA   H  N N 242 
LEU   HB2  H  N N 243 
LEU   HB3  H  N N 244 
LEU   HG   H  N N 245 
LEU   HD11 H  N N 246 
LEU   HD12 H  N N 247 
LEU   HD13 H  N N 248 
LEU   HD21 H  N N 249 
LEU   HD22 H  N N 250 
LEU   HD23 H  N N 251 
LEU   HXT  H  N N 252 
LYS   N    N  N N 253 
LYS   CA   C  N S 254 
LYS   C    C  N N 255 
LYS   O    O  N N 256 
LYS   CB   C  N N 257 
LYS   CG   C  N N 258 
LYS   CD   C  N N 259 
LYS   CE   C  N N 260 
LYS   NZ   N  N N 261 
LYS   OXT  O  N N 262 
LYS   H    H  N N 263 
LYS   H2   H  N N 264 
LYS   HA   H  N N 265 
LYS   HB2  H  N N 266 
LYS   HB3  H  N N 267 
LYS   HG2  H  N N 268 
LYS   HG3  H  N N 269 
LYS   HD2  H  N N 270 
LYS   HD3  H  N N 271 
LYS   HE2  H  N N 272 
LYS   HE3  H  N N 273 
LYS   HZ1  H  N N 274 
LYS   HZ2  H  N N 275 
LYS   HZ3  H  N N 276 
LYS   HXT  H  N N 277 
MET   N    N  N N 278 
MET   CA   C  N S 279 
MET   C    C  N N 280 
MET   O    O  N N 281 
MET   CB   C  N N 282 
MET   CG   C  N N 283 
MET   SD   S  N N 284 
MET   CE   C  N N 285 
MET   OXT  O  N N 286 
MET   H    H  N N 287 
MET   H2   H  N N 288 
MET   HA   H  N N 289 
MET   HB2  H  N N 290 
MET   HB3  H  N N 291 
MET   HG2  H  N N 292 
MET   HG3  H  N N 293 
MET   HE1  H  N N 294 
MET   HE2  H  N N 295 
MET   HE3  H  N N 296 
MET   HXT  H  N N 297 
PHE   N    N  N N 298 
PHE   CA   C  N S 299 
PHE   C    C  N N 300 
PHE   O    O  N N 301 
PHE   CB   C  N N 302 
PHE   CG   C  Y N 303 
PHE   CD1  C  Y N 304 
PHE   CD2  C  Y N 305 
PHE   CE1  C  Y N 306 
PHE   CE2  C  Y N 307 
PHE   CZ   C  Y N 308 
PHE   OXT  O  N N 309 
PHE   H    H  N N 310 
PHE   H2   H  N N 311 
PHE   HA   H  N N 312 
PHE   HB2  H  N N 313 
PHE   HB3  H  N N 314 
PHE   HD1  H  N N 315 
PHE   HD2  H  N N 316 
PHE   HE1  H  N N 317 
PHE   HE2  H  N N 318 
PHE   HZ   H  N N 319 
PHE   HXT  H  N N 320 
PRO   N    N  N N 321 
PRO   CA   C  N S 322 
PRO   C    C  N N 323 
PRO   O    O  N N 324 
PRO   CB   C  N N 325 
PRO   CG   C  N N 326 
PRO   CD   C  N N 327 
PRO   OXT  O  N N 328 
PRO   H    H  N N 329 
PRO   HA   H  N N 330 
PRO   HB2  H  N N 331 
PRO   HB3  H  N N 332 
PRO   HG2  H  N N 333 
PRO   HG3  H  N N 334 
PRO   HD2  H  N N 335 
PRO   HD3  H  N N 336 
PRO   HXT  H  N N 337 
SER   N    N  N N 338 
SER   CA   C  N S 339 
SER   C    C  N N 340 
SER   O    O  N N 341 
SER   CB   C  N N 342 
SER   OG   O  N N 343 
SER   OXT  O  N N 344 
SER   H    H  N N 345 
SER   H2   H  N N 346 
SER   HA   H  N N 347 
SER   HB2  H  N N 348 
SER   HB3  H  N N 349 
SER   HG   H  N N 350 
SER   HXT  H  N N 351 
THR   N    N  N N 352 
THR   CA   C  N S 353 
THR   C    C  N N 354 
THR   O    O  N N 355 
THR   CB   C  N R 356 
THR   OG1  O  N N 357 
THR   CG2  C  N N 358 
THR   OXT  O  N N 359 
THR   H    H  N N 360 
THR   H2   H  N N 361 
THR   HA   H  N N 362 
THR   HB   H  N N 363 
THR   HG1  H  N N 364 
THR   HG21 H  N N 365 
THR   HG22 H  N N 366 
THR   HG23 H  N N 367 
THR   HXT  H  N N 368 
TRP   N    N  N N 369 
TRP   CA   C  N S 370 
TRP   C    C  N N 371 
TRP   O    O  N N 372 
TRP   CB   C  N N 373 
TRP   CG   C  Y N 374 
TRP   CD1  C  Y N 375 
TRP   CD2  C  Y N 376 
TRP   NE1  N  Y N 377 
TRP   CE2  C  Y N 378 
TRP   CE3  C  Y N 379 
TRP   CZ2  C  Y N 380 
TRP   CZ3  C  Y N 381 
TRP   CH2  C  Y N 382 
TRP   OXT  O  N N 383 
TRP   H    H  N N 384 
TRP   H2   H  N N 385 
TRP   HA   H  N N 386 
TRP   HB2  H  N N 387 
TRP   HB3  H  N N 388 
TRP   HD1  H  N N 389 
TRP   HE1  H  N N 390 
TRP   HE3  H  N N 391 
TRP   HZ2  H  N N 392 
TRP   HZ3  H  N N 393 
TRP   HH2  H  N N 394 
TRP   HXT  H  N N 395 
TYR   N    N  N N 396 
TYR   CA   C  N S 397 
TYR   C    C  N N 398 
TYR   O    O  N N 399 
TYR   CB   C  N N 400 
TYR   CG   C  Y N 401 
TYR   CD1  C  Y N 402 
TYR   CD2  C  Y N 403 
TYR   CE1  C  Y N 404 
TYR   CE2  C  Y N 405 
TYR   CZ   C  Y N 406 
TYR   OH   O  N N 407 
TYR   OXT  O  N N 408 
TYR   H    H  N N 409 
TYR   H2   H  N N 410 
TYR   HA   H  N N 411 
TYR   HB2  H  N N 412 
TYR   HB3  H  N N 413 
TYR   HD1  H  N N 414 
TYR   HD2  H  N N 415 
TYR   HE1  H  N N 416 
TYR   HE2  H  N N 417 
TYR   HH   H  N N 418 
TYR   HXT  H  N N 419 
VAL   N    N  N N 420 
VAL   CA   C  N S 421 
VAL   C    C  N N 422 
VAL   O    O  N N 423 
VAL   CB   C  N N 424 
VAL   CG1  C  N N 425 
VAL   CG2  C  N N 426 
VAL   OXT  O  N N 427 
VAL   H    H  N N 428 
VAL   H2   H  N N 429 
VAL   HA   H  N N 430 
VAL   HB   H  N N 431 
VAL   HG11 H  N N 432 
VAL   HG12 H  N N 433 
VAL   HG13 H  N N 434 
VAL   HG21 H  N N 435 
VAL   HG22 H  N N 436 
VAL   HG23 H  N N 437 
VAL   HXT  H  N N 438 
ZN    ZN   ZN N N 439 
# 
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 
A1AOP N20 C28  doub Y N 1   
A1AOP N20 C29  sing Y N 2   
A1AOP C28 C30  sing Y N 3   
A1AOP C29 C31  doub Y N 4   
A1AOP C30 C22  doub Y N 5   
A1AOP C31 C22  sing Y N 6   
A1AOP C22 C14  sing N N 7   
A1AOP C14 C11  doub Y N 8   
A1AOP C14 C21  sing Y N 9   
A1AOP C11 C4   sing Y N 10  
A1AOP C21 C18  doub Y N 11  
A1AOP O15 S6   doub N N 12  
A1AOP C4  S6   sing N N 13  
A1AOP C4  C9   doub Y N 14  
A1AOP C18 C9   sing Y N 15  
A1AOP S6  C24  sing N N 16  
A1AOP S6  O16  doub N N 17  
A1AOP C9  N7   sing N N 18  
A1AOP N7  S1   sing N N 19  
A1AOP C26 C19  doub Y N 20  
A1AOP C26 C23  sing Y N 21  
A1AOP C19 C10  sing Y N 22  
A1AOP F27 C23  sing N N 23  
A1AOP C23 C17  doub Y N 24  
A1AOP C10 S3   sing Y N 25  
A1AOP C10 C8   doub Y N 26  
A1AOP C17 C8   sing Y N 27  
A1AOP S3  C2   sing Y N 28  
A1AOP C8  C5   sing Y N 29  
A1AOP C2  C5   doub Y N 30  
A1AOP C2  S1   sing N N 31  
A1AOP C5  C25  sing N N 32  
A1AOP O12 S1   doub N N 33  
A1AOP S1  O13  doub N N 34  
A1AOP C26 H1   sing N N 35  
A1AOP C19 H2   sing N N 36  
A1AOP C17 H3   sing N N 37  
A1AOP C25 H4   sing N N 38  
A1AOP C25 H5   sing N N 39  
A1AOP C25 H6   sing N N 40  
A1AOP N7  H7   sing N N 41  
A1AOP C18 H8   sing N N 42  
A1AOP C21 H9   sing N N 43  
A1AOP C30 H10  sing N N 44  
A1AOP C28 H11  sing N N 45  
A1AOP C31 H12  sing N N 46  
A1AOP C29 H13  sing N N 47  
A1AOP C11 H14  sing N N 48  
A1AOP C24 H15  sing N N 49  
A1AOP C24 H16  sing N N 50  
A1AOP C24 H17  sing N N 51  
ALA   N   CA   sing N N 52  
ALA   N   H    sing N N 53  
ALA   N   H2   sing N N 54  
ALA   CA  C    sing N N 55  
ALA   CA  CB   sing N N 56  
ALA   CA  HA   sing N N 57  
ALA   C   O    doub N N 58  
ALA   C   OXT  sing N N 59  
ALA   CB  HB1  sing N N 60  
ALA   CB  HB2  sing N N 61  
ALA   CB  HB3  sing N N 62  
ALA   OXT HXT  sing N N 63  
ARG   N   CA   sing N N 64  
ARG   N   H    sing N N 65  
ARG   N   H2   sing N N 66  
ARG   CA  C    sing N N 67  
ARG   CA  CB   sing N N 68  
ARG   CA  HA   sing N N 69  
ARG   C   O    doub N N 70  
ARG   C   OXT  sing N N 71  
ARG   CB  CG   sing N N 72  
ARG   CB  HB2  sing N N 73  
ARG   CB  HB3  sing N N 74  
ARG   CG  CD   sing N N 75  
ARG   CG  HG2  sing N N 76  
ARG   CG  HG3  sing N N 77  
ARG   CD  NE   sing N N 78  
ARG   CD  HD2  sing N N 79  
ARG   CD  HD3  sing N N 80  
ARG   NE  CZ   sing N N 81  
ARG   NE  HE   sing N N 82  
ARG   CZ  NH1  sing N N 83  
ARG   CZ  NH2  doub N N 84  
ARG   NH1 HH11 sing N N 85  
ARG   NH1 HH12 sing N N 86  
ARG   NH2 HH21 sing N N 87  
ARG   NH2 HH22 sing N N 88  
ARG   OXT HXT  sing N N 89  
ASN   N   CA   sing N N 90  
ASN   N   H    sing N N 91  
ASN   N   H2   sing N N 92  
ASN   CA  C    sing N N 93  
ASN   CA  CB   sing N N 94  
ASN   CA  HA   sing N N 95  
ASN   C   O    doub N N 96  
ASN   C   OXT  sing N N 97  
ASN   CB  CG   sing N N 98  
ASN   CB  HB2  sing N N 99  
ASN   CB  HB3  sing N N 100 
ASN   CG  OD1  doub N N 101 
ASN   CG  ND2  sing N N 102 
ASN   ND2 HD21 sing N N 103 
ASN   ND2 HD22 sing N N 104 
ASN   OXT HXT  sing N N 105 
ASP   N   CA   sing N N 106 
ASP   N   H    sing N N 107 
ASP   N   H2   sing N N 108 
ASP   CA  C    sing N N 109 
ASP   CA  CB   sing N N 110 
ASP   CA  HA   sing N N 111 
ASP   C   O    doub N N 112 
ASP   C   OXT  sing N N 113 
ASP   CB  CG   sing N N 114 
ASP   CB  HB2  sing N N 115 
ASP   CB  HB3  sing N N 116 
ASP   CG  OD1  doub N N 117 
ASP   CG  OD2  sing N N 118 
ASP   OD2 HD2  sing N N 119 
ASP   OXT HXT  sing N N 120 
CYS   N   CA   sing N N 121 
CYS   N   H    sing N N 122 
CYS   N   H2   sing N N 123 
CYS   CA  C    sing N N 124 
CYS   CA  CB   sing N N 125 
CYS   CA  HA   sing N N 126 
CYS   C   O    doub N N 127 
CYS   C   OXT  sing N N 128 
CYS   CB  SG   sing N N 129 
CYS   CB  HB2  sing N N 130 
CYS   CB  HB3  sing N N 131 
CYS   SG  HG   sing N N 132 
CYS   OXT HXT  sing N N 133 
GLN   N   CA   sing N N 134 
GLN   N   H    sing N N 135 
GLN   N   H2   sing N N 136 
GLN   CA  C    sing N N 137 
GLN   CA  CB   sing N N 138 
GLN   CA  HA   sing N N 139 
GLN   C   O    doub N N 140 
GLN   C   OXT  sing N N 141 
GLN   CB  CG   sing N N 142 
GLN   CB  HB2  sing N N 143 
GLN   CB  HB3  sing N N 144 
GLN   CG  CD   sing N N 145 
GLN   CG  HG2  sing N N 146 
GLN   CG  HG3  sing N N 147 
GLN   CD  OE1  doub N N 148 
GLN   CD  NE2  sing N N 149 
GLN   NE2 HE21 sing N N 150 
GLN   NE2 HE22 sing N N 151 
GLN   OXT HXT  sing N N 152 
GLU   N   CA   sing N N 153 
GLU   N   H    sing N N 154 
GLU   N   H2   sing N N 155 
GLU   CA  C    sing N N 156 
GLU   CA  CB   sing N N 157 
GLU   CA  HA   sing N N 158 
GLU   C   O    doub N N 159 
GLU   C   OXT  sing N N 160 
GLU   CB  CG   sing N N 161 
GLU   CB  HB2  sing N N 162 
GLU   CB  HB3  sing N N 163 
GLU   CG  CD   sing N N 164 
GLU   CG  HG2  sing N N 165 
GLU   CG  HG3  sing N N 166 
GLU   CD  OE1  doub N N 167 
GLU   CD  OE2  sing N N 168 
GLU   OE2 HE2  sing N N 169 
GLU   OXT HXT  sing N N 170 
GLY   N   CA   sing N N 171 
GLY   N   H    sing N N 172 
GLY   N   H2   sing N N 173 
GLY   CA  C    sing N N 174 
GLY   CA  HA2  sing N N 175 
GLY   CA  HA3  sing N N 176 
GLY   C   O    doub N N 177 
GLY   C   OXT  sing N N 178 
GLY   OXT HXT  sing N N 179 
HIS   N   CA   sing N N 180 
HIS   N   H    sing N N 181 
HIS   N   H2   sing N N 182 
HIS   CA  C    sing N N 183 
HIS   CA  CB   sing N N 184 
HIS   CA  HA   sing N N 185 
HIS   C   O    doub N N 186 
HIS   C   OXT  sing N N 187 
HIS   CB  CG   sing N N 188 
HIS   CB  HB2  sing N N 189 
HIS   CB  HB3  sing N N 190 
HIS   CG  ND1  sing Y N 191 
HIS   CG  CD2  doub Y N 192 
HIS   ND1 CE1  doub Y N 193 
HIS   ND1 HD1  sing N N 194 
HIS   CD2 NE2  sing Y N 195 
HIS   CD2 HD2  sing N N 196 
HIS   CE1 NE2  sing Y N 197 
HIS   CE1 HE1  sing N N 198 
HIS   NE2 HE2  sing N N 199 
HIS   OXT HXT  sing N N 200 
HOH   O   H1   sing N N 201 
HOH   O   H2   sing N N 202 
ILE   N   CA   sing N N 203 
ILE   N   H    sing N N 204 
ILE   N   H2   sing N N 205 
ILE   CA  C    sing N N 206 
ILE   CA  CB   sing N N 207 
ILE   CA  HA   sing N N 208 
ILE   C   O    doub N N 209 
ILE   C   OXT  sing N N 210 
ILE   CB  CG1  sing N N 211 
ILE   CB  CG2  sing N N 212 
ILE   CB  HB   sing N N 213 
ILE   CG1 CD1  sing N N 214 
ILE   CG1 HG12 sing N N 215 
ILE   CG1 HG13 sing N N 216 
ILE   CG2 HG21 sing N N 217 
ILE   CG2 HG22 sing N N 218 
ILE   CG2 HG23 sing N N 219 
ILE   CD1 HD11 sing N N 220 
ILE   CD1 HD12 sing N N 221 
ILE   CD1 HD13 sing N N 222 
ILE   OXT HXT  sing N N 223 
LEU   N   CA   sing N N 224 
LEU   N   H    sing N N 225 
LEU   N   H2   sing N N 226 
LEU   CA  C    sing N N 227 
LEU   CA  CB   sing N N 228 
LEU   CA  HA   sing N N 229 
LEU   C   O    doub N N 230 
LEU   C   OXT  sing N N 231 
LEU   CB  CG   sing N N 232 
LEU   CB  HB2  sing N N 233 
LEU   CB  HB3  sing N N 234 
LEU   CG  CD1  sing N N 235 
LEU   CG  CD2  sing N N 236 
LEU   CG  HG   sing N N 237 
LEU   CD1 HD11 sing N N 238 
LEU   CD1 HD12 sing N N 239 
LEU   CD1 HD13 sing N N 240 
LEU   CD2 HD21 sing N N 241 
LEU   CD2 HD22 sing N N 242 
LEU   CD2 HD23 sing N N 243 
LEU   OXT HXT  sing N N 244 
LYS   N   CA   sing N N 245 
LYS   N   H    sing N N 246 
LYS   N   H2   sing N N 247 
LYS   CA  C    sing N N 248 
LYS   CA  CB   sing N N 249 
LYS   CA  HA   sing N N 250 
LYS   C   O    doub N N 251 
LYS   C   OXT  sing N N 252 
LYS   CB  CG   sing N N 253 
LYS   CB  HB2  sing N N 254 
LYS   CB  HB3  sing N N 255 
LYS   CG  CD   sing N N 256 
LYS   CG  HG2  sing N N 257 
LYS   CG  HG3  sing N N 258 
LYS   CD  CE   sing N N 259 
LYS   CD  HD2  sing N N 260 
LYS   CD  HD3  sing N N 261 
LYS   CE  NZ   sing N N 262 
LYS   CE  HE2  sing N N 263 
LYS   CE  HE3  sing N N 264 
LYS   NZ  HZ1  sing N N 265 
LYS   NZ  HZ2  sing N N 266 
LYS   NZ  HZ3  sing N N 267 
LYS   OXT HXT  sing N N 268 
MET   N   CA   sing N N 269 
MET   N   H    sing N N 270 
MET   N   H2   sing N N 271 
MET   CA  C    sing N N 272 
MET   CA  CB   sing N N 273 
MET   CA  HA   sing N N 274 
MET   C   O    doub N N 275 
MET   C   OXT  sing N N 276 
MET   CB  CG   sing N N 277 
MET   CB  HB2  sing N N 278 
MET   CB  HB3  sing N N 279 
MET   CG  SD   sing N N 280 
MET   CG  HG2  sing N N 281 
MET   CG  HG3  sing N N 282 
MET   SD  CE   sing N N 283 
MET   CE  HE1  sing N N 284 
MET   CE  HE2  sing N N 285 
MET   CE  HE3  sing N N 286 
MET   OXT HXT  sing N N 287 
PHE   N   CA   sing N N 288 
PHE   N   H    sing N N 289 
PHE   N   H2   sing N N 290 
PHE   CA  C    sing N N 291 
PHE   CA  CB   sing N N 292 
PHE   CA  HA   sing N N 293 
PHE   C   O    doub N N 294 
PHE   C   OXT  sing N N 295 
PHE   CB  CG   sing N N 296 
PHE   CB  HB2  sing N N 297 
PHE   CB  HB3  sing N N 298 
PHE   CG  CD1  doub Y N 299 
PHE   CG  CD2  sing Y N 300 
PHE   CD1 CE1  sing Y N 301 
PHE   CD1 HD1  sing N N 302 
PHE   CD2 CE2  doub Y N 303 
PHE   CD2 HD2  sing N N 304 
PHE   CE1 CZ   doub Y N 305 
PHE   CE1 HE1  sing N N 306 
PHE   CE2 CZ   sing Y N 307 
PHE   CE2 HE2  sing N N 308 
PHE   CZ  HZ   sing N N 309 
PHE   OXT HXT  sing N N 310 
PRO   N   CA   sing N N 311 
PRO   N   CD   sing N N 312 
PRO   N   H    sing N N 313 
PRO   CA  C    sing N N 314 
PRO   CA  CB   sing N N 315 
PRO   CA  HA   sing N N 316 
PRO   C   O    doub N N 317 
PRO   C   OXT  sing N N 318 
PRO   CB  CG   sing N N 319 
PRO   CB  HB2  sing N N 320 
PRO   CB  HB3  sing N N 321 
PRO   CG  CD   sing N N 322 
PRO   CG  HG2  sing N N 323 
PRO   CG  HG3  sing N N 324 
PRO   CD  HD2  sing N N 325 
PRO   CD  HD3  sing N N 326 
PRO   OXT HXT  sing N N 327 
SER   N   CA   sing N N 328 
SER   N   H    sing N N 329 
SER   N   H2   sing N N 330 
SER   CA  C    sing N N 331 
SER   CA  CB   sing N N 332 
SER   CA  HA   sing N N 333 
SER   C   O    doub N N 334 
SER   C   OXT  sing N N 335 
SER   CB  OG   sing N N 336 
SER   CB  HB2  sing N N 337 
SER   CB  HB3  sing N N 338 
SER   OG  HG   sing N N 339 
SER   OXT HXT  sing N N 340 
THR   N   CA   sing N N 341 
THR   N   H    sing N N 342 
THR   N   H2   sing N N 343 
THR   CA  C    sing N N 344 
THR   CA  CB   sing N N 345 
THR   CA  HA   sing N N 346 
THR   C   O    doub N N 347 
THR   C   OXT  sing N N 348 
THR   CB  OG1  sing N N 349 
THR   CB  CG2  sing N N 350 
THR   CB  HB   sing N N 351 
THR   OG1 HG1  sing N N 352 
THR   CG2 HG21 sing N N 353 
THR   CG2 HG22 sing N N 354 
THR   CG2 HG23 sing N N 355 
THR   OXT HXT  sing N N 356 
TRP   N   CA   sing N N 357 
TRP   N   H    sing N N 358 
TRP   N   H2   sing N N 359 
TRP   CA  C    sing N N 360 
TRP   CA  CB   sing N N 361 
TRP   CA  HA   sing N N 362 
TRP   C   O    doub N N 363 
TRP   C   OXT  sing N N 364 
TRP   CB  CG   sing N N 365 
TRP   CB  HB2  sing N N 366 
TRP   CB  HB3  sing N N 367 
TRP   CG  CD1  doub Y N 368 
TRP   CG  CD2  sing Y N 369 
TRP   CD1 NE1  sing Y N 370 
TRP   CD1 HD1  sing N N 371 
TRP   CD2 CE2  doub Y N 372 
TRP   CD2 CE3  sing Y N 373 
TRP   NE1 CE2  sing Y N 374 
TRP   NE1 HE1  sing N N 375 
TRP   CE2 CZ2  sing Y N 376 
TRP   CE3 CZ3  doub Y N 377 
TRP   CE3 HE3  sing N N 378 
TRP   CZ2 CH2  doub Y N 379 
TRP   CZ2 HZ2  sing N N 380 
TRP   CZ3 CH2  sing Y N 381 
TRP   CZ3 HZ3  sing N N 382 
TRP   CH2 HH2  sing N N 383 
TRP   OXT HXT  sing N N 384 
TYR   N   CA   sing N N 385 
TYR   N   H    sing N N 386 
TYR   N   H2   sing N N 387 
TYR   CA  C    sing N N 388 
TYR   CA  CB   sing N N 389 
TYR   CA  HA   sing N N 390 
TYR   C   O    doub N N 391 
TYR   C   OXT  sing N N 392 
TYR   CB  CG   sing N N 393 
TYR   CB  HB2  sing N N 394 
TYR   CB  HB3  sing N N 395 
TYR   CG  CD1  doub Y N 396 
TYR   CG  CD2  sing Y N 397 
TYR   CD1 CE1  sing Y N 398 
TYR   CD1 HD1  sing N N 399 
TYR   CD2 CE2  doub Y N 400 
TYR   CD2 HD2  sing N N 401 
TYR   CE1 CZ   doub Y N 402 
TYR   CE1 HE1  sing N N 403 
TYR   CE2 CZ   sing Y N 404 
TYR   CE2 HE2  sing N N 405 
TYR   CZ  OH   sing N N 406 
TYR   OH  HH   sing N N 407 
TYR   OXT HXT  sing N N 408 
VAL   N   CA   sing N N 409 
VAL   N   H    sing N N 410 
VAL   N   H2   sing N N 411 
VAL   CA  C    sing N N 412 
VAL   CA  CB   sing N N 413 
VAL   CA  HA   sing N N 414 
VAL   C   O    doub N N 415 
VAL   C   OXT  sing N N 416 
VAL   CB  CG1  sing N N 417 
VAL   CB  CG2  sing N N 418 
VAL   CB  HB   sing N N 419 
VAL   CG1 HG11 sing N N 420 
VAL   CG1 HG12 sing N N 421 
VAL   CG1 HG13 sing N N 422 
VAL   CG2 HG21 sing N N 423 
VAL   CG2 HG22 sing N N 424 
VAL   CG2 HG23 sing N N 425 
VAL   OXT HXT  sing N N 426 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                Switzerland 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_deposit_group.group_id            G_1002292 
_pdbx_deposit_group.group_description   'A set of chymase crystal structures for D3R plus two CatG off-target structures' 
_pdbx_deposit_group.group_title         'A set of chymase crystal structures for D3R plus two CatG off-target structures' 
_pdbx_deposit_group.group_type          undefined 
# 
_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      Other 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          'apo structure' 
# 
_atom_sites.entry_id                    7H6E 
_atom_sites.fract_transf_matrix[1][1]   0.016926 
_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]   0.016909 
_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]   0.013795 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
F  
N  
O  
S  
ZN 
# 
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   ? -8.635  8.125   11.417  1.00 15.14 ? 16  ILE   A N   1 
ATOM   2    C  CA  . ILE   A 1 1   ? -10.052 7.990   10.992  1.00 14.15 ? 16  ILE   A CA  1 
ATOM   3    C  C   . ILE   A 1 1   ? -10.849 9.176   11.558  1.00 15.52 ? 16  ILE   A C   1 
ATOM   4    O  O   . ILE   A 1 1   ? -10.810 9.372   12.779  1.00 15.60 ? 16  ILE   A O   1 
ATOM   5    C  CB  . ILE   A 1 1   ? -10.570 6.642   11.488  1.00 13.92 ? 16  ILE   A CB  1 
ATOM   6    C  CG1 . ILE   A 1 1   ? -9.717  5.461   11.022  1.00 15.70 ? 16  ILE   A CG1 1 
ATOM   7    C  CG2 . ILE   A 1 1   ? -12.032 6.465   11.084  1.00 14.71 ? 16  ILE   A CG2 1 
ATOM   8    C  CD1 . ILE   A 1 1   ? -9.987  5.014   9.600   1.00 14.00 ? 16  ILE   A CD1 1 
ATOM   9    N  N   . ILE   A 1 2   ? -11.541 9.931   10.674  1.00 15.16 ? 17  ILE   A N   1 
ATOM   10   C  CA  . ILE   A 1 2   ? -12.367 11.074  11.020  1.00 16.20 ? 17  ILE   A CA  1 
ATOM   11   C  C   . ILE   A 1 2   ? -13.822 10.643  10.918  1.00 17.28 ? 17  ILE   A C   1 
ATOM   12   O  O   . ILE   A 1 2   ? -14.184 9.945   9.969   1.00 15.65 ? 17  ILE   A O   1 
ATOM   13   C  CB  . ILE   A 1 2   ? -12.053 12.236  10.064  1.00 19.37 ? 17  ILE   A CB  1 
ATOM   14   C  CG1 . ILE   A 1 2   ? -10.579 12.592  10.160  1.00 17.60 ? 17  ILE   A CG1 1 
ATOM   15   C  CG2 . ILE   A 1 2   ? -12.953 13.461  10.288  1.00 20.16 ? 17  ILE   A CG2 1 
ATOM   16   C  CD1 . ILE   A 1 2   ? -10.168 13.585  9.135   1.00 19.74 ? 17  ILE   A CD1 1 
ATOM   17   N  N   . GLY   A 1 3   ? -14.623 10.978  11.943  1.00 19.10 ? 18  GLY   A N   1 
ATOM   18   C  CA  . GLY   A 1 3   ? -16.054 10.706  11.960  1.00 17.24 ? 18  GLY   A CA  1 
ATOM   19   C  C   . GLY   A 1 3   ? -16.388 9.246   12.181  1.00 20.42 ? 18  GLY   A C   1 
ATOM   20   O  O   . GLY   A 1 3   ? -17.529 8.840   11.939  1.00 18.88 ? 18  GLY   A O   1 
ATOM   21   N  N   . GLY   A 1 4   ? -15.420 8.477   12.700  1.00 19.03 ? 19  GLY   A N   1 
ATOM   22   C  CA  . GLY   A 1 4   ? -15.584 7.047   12.872  1.00 20.63 ? 19  GLY   A CA  1 
ATOM   23   C  C   . GLY   A 1 4   ? -16.111 6.651   14.253  1.00 23.18 ? 19  GLY   A C   1 
ATOM   24   O  O   . GLY   A 1 4   ? -16.569 7.485   15.018  1.00 24.86 ? 19  GLY   A O   1 
ATOM   25   N  N   . THR   A 1 5   ? -16.020 5.366   14.559  1.00 21.85 ? 20  THR   A N   1 
ATOM   26   C  CA  . THR   A 1 5   ? -16.396 4.803   15.845  1.00 24.92 ? 20  THR   A CA  1 
ATOM   27   C  C   . THR   A 1 5   ? -15.226 3.931   16.303  1.00 22.87 ? 20  THR   A C   1 
ATOM   28   O  O   . THR   A 1 5   ? -14.590 3.298   15.476  1.00 21.95 ? 20  THR   A O   1 
ATOM   29   C  CB  . THR   A 1 5   ? -17.655 3.908   15.780  1.00 29.67 ? 20  THR   A CB  1 
ATOM   30   O  OG1 . THR   A 1 5   ? -17.538 2.983   14.693  1.00 34.69 ? 20  THR   A OG1 1 
ATOM   31   C  CG2 . THR   A 1 5   ? -18.963 4.656   15.583  1.00 30.45 ? 20  THR   A CG2 1 
ATOM   32   N  N   . GLU   A 1 6   ? -14.965 3.895   17.612  1.00 26.33 ? 21  GLU   A N   1 
ATOM   33   C  CA  . GLU   A 1 6   ? -14.018 2.978   18.223  1.00 22.45 ? 21  GLU   A CA  1 
ATOM   34   C  C   . GLU   A 1 6   ? -14.463 1.575   17.836  1.00 21.34 ? 21  GLU   A C   1 
ATOM   35   O  O   . GLU   A 1 6   ? -15.621 1.280   18.011  1.00 18.20 ? 21  GLU   A O   1 
ATOM   36   C  CB  . GLU   A 1 6   ? -14.048 3.072   19.737  1.00 21.63 ? 21  GLU   A CB  1 
ATOM   37   C  CG  . GLU   A 1 6   ? -12.986 2.184   20.381  1.00 21.92 ? 21  GLU   A CG  1 
ATOM   38   C  CD  . GLU   A 1 6   ? -12.833 2.268   21.896  1.00 22.27 ? 21  GLU   A CD  1 
ATOM   39   O  OE1 . GLU   A 1 6   ? -13.327 3.255   22.510  1.00 23.99 ? 21  GLU   A OE1 1 
ATOM   40   O  OE2 . GLU   A 1 6   ? -12.114 1.408   22.439  1.00 18.61 ? 21  GLU   A OE2 1 
ATOM   41   N  N   . SER   A 1 7   ? -13.584 0.803   17.191  1.00 16.38 ? 22  SER   A N   1 
ATOM   42   C  CA  . SER   A 1 7   ? -13.853 -0.586  16.861  1.00 18.15 ? 22  SER   A CA  1 
ATOM   43   C  C   . SER   A 1 7   ? -14.170 -1.364  18.155  1.00 17.11 ? 22  SER   A C   1 
ATOM   44   O  O   . SER   A 1 7   ? -13.680 -1.061  19.243  1.00 15.91 ? 22  SER   A O   1 
ATOM   45   C  CB  . SER   A 1 7   ? -12.627 -1.222  16.139  1.00 16.89 ? 22  SER   A CB  1 
ATOM   46   O  OG  . SER   A 1 7   ? -12.292 -0.564  14.919  1.00 15.96 ? 22  SER   A OG  1 
ATOM   47   N  N   . LYS   A 1 8   ? -14.984 -2.393  18.017  1.00 18.98 ? 23  LYS   A N   1 
ATOM   48   C  CA  . LYS   A 1 8   ? -15.134 -3.414  19.031  1.00 19.65 ? 23  LYS   A CA  1 
ATOM   49   C  C   . LYS   A 1 8   ? -13.785 -4.088  19.134  1.00 15.59 ? 23  LYS   A C   1 
ATOM   50   O  O   . LYS   A 1 8   ? -13.272 -4.459  18.099  1.00 14.88 ? 23  LYS   A O   1 
ATOM   51   C  CB  . LYS   A 1 8   ? -16.204 -4.433  18.635  1.00 21.83 ? 23  LYS   A CB  1 
ATOM   52   C  CG  . LYS   A 1 8   ? -16.395 -5.542  19.649  1.00 22.68 ? 23  LYS   A CG  1 
ATOM   53   C  CD  . LYS   A 1 8   ? -17.214 -6.768  19.200  1.00 22.43 ? 23  LYS   A CD  1 
ATOM   54   C  CE  . LYS   A 1 8   ? -17.101 -7.823  20.287  1.00 23.79 ? 23  LYS   A CE  1 
ATOM   55   N  NZ  . LYS   A 1 8   ? -17.427 -9.194  19.857  1.00 27.14 ? 23  LYS   A NZ  1 
ATOM   56   N  N   . PRO   A 1 9   ? -13.168 -4.124  20.331  1.00 16.16 ? 24  PRO   A N   1 
ATOM   57   C  CA  . PRO   A 1 9   ? -11.827 -4.664  20.480  1.00 14.93 ? 24  PRO   A CA  1 
ATOM   58   C  C   . PRO   A 1 9   ? -11.686 -5.987  19.751  1.00 13.61 ? 24  PRO   A C   1 
ATOM   59   O  O   . PRO   A 1 9   ? -12.537 -6.846  19.909  1.00 12.65 ? 24  PRO   A O   1 
ATOM   60   C  CB  . PRO   A 1 9   ? -11.689 -4.806  21.997  1.00 16.38 ? 24  PRO   A CB  1 
ATOM   61   C  CG  . PRO   A 1 9   ? -12.579 -3.741  22.549  1.00 16.48 ? 24  PRO   A CG  1 
ATOM   62   C  CD  . PRO   A 1 9   ? -13.759 -3.717  21.629  1.00 15.69 ? 24  PRO   A CD  1 
ATOM   63   N  N   . HIS   A 1 10  ? -10.634 -6.125  18.930  1.00 14.23 ? 25  HIS   A N   1 
ATOM   64   C  CA  . HIS   A 1 10  ? -10.237 -7.375  18.264  1.00 15.62 ? 25  HIS   A CA  1 
ATOM   65   C  C   . HIS   A 1 10  ? -11.237 -7.868  17.235  1.00 16.37 ? 25  HIS   A C   1 
ATOM   66   O  O   . HIS   A 1 10  ? -11.142 -9.032  16.779  1.00 19.19 ? 25  HIS   A O   1 
ATOM   67   C  CB  . HIS   A 1 10  ? -9.855  -8.495  19.252  1.00 16.62 ? 25  HIS   A CB  1 
ATOM   68   C  CG  . HIS   A 1 10  ? -9.034  -7.973  20.374  1.00 15.25 ? 25  HIS   A CG  1 
ATOM   69   N  ND1 . HIS   A 1 10  ? -7.823  -7.361  20.161  1.00 16.26 ? 25  HIS   A ND1 1 
ATOM   70   C  CD2 . HIS   A 1 10  ? -9.301  -7.847  21.684  1.00 16.22 ? 25  HIS   A CD2 1 
ATOM   71   C  CE1 . HIS   A 1 10  ? -7.326  -6.941  21.320  1.00 15.25 ? 25  HIS   A CE1 1 
ATOM   72   N  NE2 . HIS   A 1 10  ? -8.232  -7.198  22.279  1.00 18.13 ? 25  HIS   A NE2 1 
ATOM   73   N  N   . SER   A 1 11  ? -12.186 -7.000  16.852  1.00 14.93 ? 26  SER   A N   1 
ATOM   74   C  CA  . SER   A 1 11  ? -13.148 -7.401  15.834  1.00 16.22 ? 26  SER   A CA  1 
ATOM   75   C  C   . SER   A 1 11  ? -12.578 -7.281  14.423  1.00 17.41 ? 26  SER   A C   1 
ATOM   76   O  O   . SER   A 1 11  ? -13.270 -7.662  13.518  1.00 15.98 ? 26  SER   A O   1 
ATOM   77   C  CB  . SER   A 1 11  ? -14.390 -6.582  15.924  1.00 16.26 ? 26  SER   A CB  1 
ATOM   78   O  OG  . SER   A 1 11  ? -14.096 -5.222  15.758  1.00 18.11 ? 26  SER   A OG  1 
ATOM   79   N  N   . ARG   A 1 12  ? -11.381 -6.692  14.225  1.00 16.66 ? 27  ARG   A N   1 
ATOM   80   C  CA  . ARG   A 1 12  ? -10.818 -6.604  12.892  1.00 17.88 ? 27  ARG   A CA  1 
ATOM   81   C  C   . ARG   A 1 12  ? -9.441  -7.245  12.955  1.00 16.69 ? 27  ARG   A C   1 
ATOM   82   O  O   . ARG   A 1 12  ? -8.448  -6.536  12.966  1.00 16.89 ? 27  ARG   A O   1 
ATOM   83   C  CB  . ARG   A 1 12  ? -10.738 -5.149  12.418  1.00 19.85 ? 27  ARG   A CB  1 
ATOM   84   C  CG  . ARG   A 1 12  ? -12.008 -4.327  12.562  1.00 22.21 ? 27  ARG   A CG  1 
ATOM   85   C  CD  . ARG   A 1 12  ? -13.121 -4.819  11.710  1.00 25.65 ? 27  ARG   A CD  1 
ATOM   86   N  NE  . ARG   A 1 12  ? -14.401 -4.171  11.994  1.00 29.59 ? 27  ARG   A NE  1 
ATOM   87   C  CZ  . ARG   A 1 12  ? -15.580 -4.676  11.616  1.00 31.39 ? 27  ARG   A CZ  1 
ATOM   88   N  NH1 . ARG   A 1 12  ? -15.622 -5.808  10.932  1.00 32.79 ? 27  ARG   A NH1 1 
ATOM   89   N  NH2 . ARG   A 1 12  ? -16.707 -4.062  11.917  1.00 30.44 ? 27  ARG   A NH2 1 
ATOM   90   N  N   . PRO   A 1 13  ? -9.380  -8.569  13.172  1.00 18.36 ? 28  PRO   A N   1 
ATOM   91   C  CA  . PRO   A 1 13  ? -8.174  -9.232  13.681  1.00 18.79 ? 28  PRO   A CA  1 
ATOM   92   C  C   . PRO   A 1 13  ? -7.006  -9.325  12.689  1.00 16.10 ? 28  PRO   A C   1 
ATOM   93   O  O   . PRO   A 1 13  ? -5.906  -9.755  13.047  1.00 14.85 ? 28  PRO   A O   1 
ATOM   94   C  CB  . PRO   A 1 13  ? -8.726  -10.594 14.166  1.00 19.46 ? 28  PRO   A CB  1 
ATOM   95   C  CG  . PRO   A 1 13  ? -9.901  -10.845 13.266  1.00 20.00 ? 28  PRO   A CG  1 
ATOM   96   C  CD  . PRO   A 1 13  ? -10.528 -9.484  13.046  1.00 21.16 ? 28  PRO   A CD  1 
ATOM   97   N  N   . TYR   A 1 14  ? -7.267  -8.874  11.461  1.00 14.41 ? 29  TYR   A N   1 
ATOM   98   C  CA  . TYR   A 1 14  ? -6.275  -8.717  10.392  1.00 15.29 ? 29  TYR   A CA  1 
ATOM   99   C  C   . TYR   A 1 14  ? -5.502  -7.407  10.529  1.00 15.01 ? 29  TYR   A C   1 
ATOM   100  O  O   . TYR   A 1 14  ? -4.427  -7.249  9.918   1.00 14.21 ? 29  TYR   A O   1 
ATOM   101  C  CB  . TYR   A 1 14  ? -6.970  -8.789  9.025   1.00 15.25 ? 29  TYR   A CB  1 
ATOM   102  C  CG  . TYR   A 1 14  ? -8.267  -7.991  8.967   1.00 15.39 ? 29  TYR   A CG  1 
ATOM   103  C  CD1 . TYR   A 1 14  ? -8.242  -6.613  8.803   1.00 17.36 ? 29  TYR   A CD1 1 
ATOM   104  C  CD2 . TYR   A 1 14  ? -9.521  -8.620  9.063   1.00 16.42 ? 29  TYR   A CD2 1 
ATOM   105  C  CE1 . TYR   A 1 14  ? -9.418  -5.861  8.771   1.00 19.14 ? 29  TYR   A CE1 1 
ATOM   106  C  CE2 . TYR   A 1 14  ? -10.698 -7.884  8.986   1.00 16.90 ? 29  TYR   A CE2 1 
ATOM   107  C  CZ  . TYR   A 1 14  ? -10.651 -6.499  8.871   1.00 18.50 ? 29  TYR   A CZ  1 
ATOM   108  O  OH  . TYR   A 1 14  ? -11.767 -5.722  8.829   1.00 19.32 ? 29  TYR   A OH  1 
ATOM   109  N  N   . MET   A 1 15  ? -6.000  -6.473  11.361  1.00 14.06 ? 30  MET   A N   1 
ATOM   110  C  CA  . MET   A 1 15  ? -5.374  -5.155  11.407  1.00 13.85 ? 30  MET   A CA  1 
ATOM   111  C  C   . MET   A 1 15  ? -3.991  -5.230  12.027  1.00 13.33 ? 30  MET   A C   1 
ATOM   112  O  O   . MET   A 1 15  ? -3.826  -5.893  13.037  1.00 11.32 ? 30  MET   A O   1 
ATOM   113  C  CB  . MET   A 1 15  ? -6.178  -4.146  12.211  1.00 15.50 ? 30  MET   A CB  1 
ATOM   114  C  CG  . MET   A 1 15  ? -7.373  -3.624  11.480  1.00 14.94 ? 30  MET   A CG  1 
ATOM   115  S  SD  . MET   A 1 15  ? -7.047  -2.912  9.867   1.00 15.54 ? 30  MET   A SD  1 
ATOM   116  C  CE  . MET   A 1 15  ? -5.928  -1.537  10.206  1.00 17.17 ? 30  MET   A CE  1 
ATOM   117  N  N   . ALA   A 1 16  ? -3.054  -4.504  11.392  1.00 15.04 ? 31  ALA   A N   1 
ATOM   118  C  CA  . ALA   A 1 16  ? -1.656  -4.427  11.807  1.00 16.34 ? 31  ALA   A CA  1 
ATOM   119  C  C   . ALA   A 1 16  ? -1.306  -2.964  12.047  1.00 16.62 ? 31  ALA   A C   1 
ATOM   120  O  O   . ALA   A 1 16  ? -1.715  -2.089  11.277  1.00 14.68 ? 31  ALA   A O   1 
ATOM   121  C  CB  . ALA   A 1 16  ? -0.738  -5.005  10.737  1.00 15.84 ? 31  ALA   A CB  1 
ATOM   122  N  N   . TYR   A 1 17  ? -0.468  -2.750  13.067  1.00 13.91 ? 32  TYR   A N   1 
ATOM   123  C  CA  . TYR   A 1 17  ? -0.017  -1.450  13.473  1.00 14.48 ? 32  TYR   A CA  1 
ATOM   124  C  C   . TYR   A 1 17  ? 1.478   -1.489  13.259  1.00 14.72 ? 32  TYR   A C   1 
ATOM   125  O  O   . TYR   A 1 17  ? 2.117   -2.411  13.774  1.00 13.68 ? 32  TYR   A O   1 
ATOM   126  C  CB  . TYR   A 1 17  ? -0.441  -1.149  14.912  1.00 14.50 ? 32  TYR   A CB  1 
ATOM   127  C  CG  . TYR   A 1 17  ? 0.125   0.149   15.457  1.00 17.32 ? 32  TYR   A CG  1 
ATOM   128  C  CD1 . TYR   A 1 17  ? -0.509  1.353   15.199  1.00 19.87 ? 32  TYR   A CD1 1 
ATOM   129  C  CD2 . TYR   A 1 17  ? 1.243   0.179   16.258  1.00 22.16 ? 32  TYR   A CD2 1 
ATOM   130  C  CE1 . TYR   A 1 17  ? -0.020  2.560   15.665  1.00 21.92 ? 32  TYR   A CE1 1 
ATOM   131  C  CE2 . TYR   A 1 17  ? 1.760   1.378   16.740  1.00 27.33 ? 32  TYR   A CE2 1 
ATOM   132  C  CZ  . TYR   A 1 17  ? 1.120   2.570   16.439  1.00 23.59 ? 32  TYR   A CZ  1 
ATOM   133  O  OH  . TYR   A 1 17  ? 1.537   3.750   16.935  1.00 22.93 ? 32  TYR   A OH  1 
ATOM   134  N  N   . LEU   A 1 18  ? 1.936   -0.575  12.401  1.00 13.81 ? 33  LEU   A N   1 
ATOM   135  C  CA  . LEU   A 1 18  ? 3.274   -0.556  11.857  1.00 15.39 ? 33  LEU   A CA  1 
ATOM   136  C  C   . LEU   A 1 18  ? 4.037   0.593   12.516  1.00 15.79 ? 33  LEU   A C   1 
ATOM   137  O  O   . LEU   A 1 18  ? 3.582   1.733   12.543  1.00 14.23 ? 33  LEU   A O   1 
ATOM   138  C  CB  . LEU   A 1 18  ? 3.237   -0.350  10.341  1.00 16.61 ? 33  LEU   A CB  1 
ATOM   139  C  CG  . LEU   A 1 18  ? 2.958   -1.580  9.464   1.00 19.32 ? 33  LEU   A CG  1 
ATOM   140  C  CD1 . LEU   A 1 18  ? 1.702   -2.326  9.852   1.00 17.40 ? 33  LEU   A CD1 1 
ATOM   141  C  CD2 . LEU   A 1 18  ? 2.882   -1.226  7.984   1.00 20.66 ? 33  LEU   A CD2 1 
ATOM   142  N  N   A GLU   A 1 19  ? 5.188   0.230   13.089  0.50 18.49 ? 34  GLU   A N   1 
ATOM   143  N  N   B GLU   A 1 19  ? 5.156   0.261   13.156  0.50 17.73 ? 34  GLU   A N   1 
ATOM   144  C  CA  A GLU   A 1 19  ? 6.113   1.172   13.684  0.50 20.32 ? 34  GLU   A CA  1 
ATOM   145  C  CA  B GLU   A 1 19  ? 6.034   1.300   13.645  0.50 18.83 ? 34  GLU   A CA  1 
ATOM   146  C  C   A GLU   A 1 19  ? 7.336   1.220   12.774  0.50 20.33 ? 34  GLU   A C   1 
ATOM   147  C  C   B GLU   A 1 19  ? 7.293   1.244   12.790  0.50 19.54 ? 34  GLU   A C   1 
ATOM   148  O  O   A GLU   A 1 19  ? 8.076   0.240   12.679  0.50 21.29 ? 34  GLU   A O   1 
ATOM   149  O  O   B GLU   A 1 19  ? 7.995   0.235   12.744  0.50 20.69 ? 34  GLU   A O   1 
ATOM   150  C  CB  A GLU   A 1 19  ? 6.476   0.752   15.109  0.50 22.06 ? 34  GLU   A CB  1 
ATOM   151  C  CB  B GLU   A 1 19  ? 6.295   1.209   15.146  0.50 18.90 ? 34  GLU   A CB  1 
ATOM   152  C  CG  A GLU   A 1 19  ? 5.353   0.935   16.114  0.50 22.86 ? 34  GLU   A CG  1 
ATOM   153  C  CG  B GLU   A 1 19  ? 7.263   2.276   15.625  0.50 18.22 ? 34  GLU   A CG  1 
ATOM   154  C  CD  A GLU   A 1 19  ? 5.707   0.450   17.517  0.50 21.96 ? 34  GLU   A CD  1 
ATOM   155  C  CD  B GLU   A 1 19  ? 7.573   2.245   17.105  0.50 18.92 ? 34  GLU   A CD  1 
ATOM   156  O  OE1 A GLU   A 1 19  ? 5.796   -0.759  17.696  0.50 18.58 ? 34  GLU   A OE1 1 
ATOM   157  O  OE1 B GLU   A 1 19  ? 7.264   1.228   17.745  0.50 19.71 ? 34  GLU   A OE1 1 
ATOM   158  O  OE2 A GLU   A 1 19  ? 5.942   1.303   18.413  0.50 21.98 ? 34  GLU   A OE2 1 
ATOM   159  O  OE2 B GLU   A 1 19  ? 8.122   3.251   17.621  0.50 20.15 ? 34  GLU   A OE2 1 
ATOM   160  N  N   . ILE   A 1 20  ? 7.522   2.354   12.089  1.00 21.31 ? 35  ILE   A N   1 
ATOM   161  C  CA  . ILE   A 1 20  ? 8.522   2.449   11.030  1.00 21.65 ? 35  ILE   A CA  1 
ATOM   162  C  C   . ILE   A 1 20  ? 9.611   3.397   11.491  1.00 23.71 ? 35  ILE   A C   1 
ATOM   163  O  O   . ILE   A 1 20  ? 9.339   4.548   11.806  1.00 23.81 ? 35  ILE   A O   1 
ATOM   164  C  CB  . ILE   A 1 20  ? 7.871   2.951   9.726   1.00 24.85 ? 35  ILE   A CB  1 
ATOM   165  C  CG1 . ILE   A 1 20  ? 6.709   2.047   9.305   1.00 23.21 ? 35  ILE   A CG1 1 
ATOM   166  C  CG2 . ILE   A 1 20  ? 8.920   3.104   8.615   1.00 24.47 ? 35  ILE   A CG2 1 
ATOM   167  C  CD1 . ILE   A 1 20  ? 5.483   2.779   8.935   1.00 24.61 ? 35  ILE   A CD1 1 
ATOM   168  N  N   . VAL   A 1 21  ? 10.830  2.869   11.517  1.00 28.72 ? 36  VAL   A N   1 
ATOM   169  C  CA  . VAL   A 1 21  ? 11.999  3.687   11.701  1.00 35.98 ? 36  VAL   A CA  1 
ATOM   170  C  C   . VAL   A 1 21  ? 12.402  4.220   10.336  1.00 39.31 ? 36  VAL   A C   1 
ATOM   171  O  O   . VAL   A 1 21  ? 12.977  3.466   9.545   1.00 40.19 ? 36  VAL   A O   1 
ATOM   172  C  CB  . VAL   A 1 21  ? 13.147  2.878   12.330  1.00 43.85 ? 36  VAL   A CB  1 
ATOM   173  C  CG1 . VAL   A 1 21  ? 14.401  3.740   12.476  1.00 45.60 ? 36  VAL   A CG1 1 
ATOM   174  C  CG2 . VAL   A 1 21  ? 12.731  2.259   13.662  1.00 41.46 ? 36  VAL   A CG2 1 
ATOM   175  N  N   . THR   A 1 22  A 12.131  5.519   10.097  1.00 42.27 ? 36  THR   A N   1 
ATOM   176  C  CA  . THR   A 1 22  A 12.345  6.170   8.800   1.00 44.48 ? 36  THR   A CA  1 
ATOM   177  C  C   . THR   A 1 22  A 13.832  6.143   8.423   1.00 44.12 ? 36  THR   A C   1 
ATOM   178  O  O   . THR   A 1 22  A 14.692  6.260   9.294   1.00 48.39 ? 36  THR   A O   1 
ATOM   179  C  CB  . THR   A 1 22  A 11.852  7.625   8.803   1.00 41.70 ? 36  THR   A CB  1 
ATOM   180  O  OG1 . THR   A 1 22  A 12.540  8.356   9.832   1.00 36.63 ? 36  THR   A OG1 1 
ATOM   181  C  CG2 . THR   A 1 22  A 10.354  7.723   8.989   1.00 40.39 ? 36  THR   A CG2 1 
ATOM   182  N  N   . SER   A 1 23  B 14.115  5.986   7.121   1.00 54.09 ? 36  SER   A N   1 
ATOM   183  C  CA  . SER   A 1 23  B 15.438  5.587   6.641   1.00 63.11 ? 36  SER   A CA  1 
ATOM   184  C  C   . SER   A 1 23  B 16.493  6.638   6.995   1.00 59.96 ? 36  SER   A C   1 
ATOM   185  O  O   . SER   A 1 23  B 17.693  6.337   7.026   1.00 56.60 ? 36  SER   A O   1 
ATOM   186  C  CB  . SER   A 1 23  B 15.439  5.278   5.150   1.00 61.24 ? 36  SER   A CB  1 
ATOM   187  O  OG  . SER   A 1 23  B 16.525  4.418   4.805   0.50 54.73 ? 36  SER   A OG  1 
ATOM   188  N  N   . ASN   A 1 24  ? 16.006  7.850   7.283   1.00 54.86 ? 37  ASN   A N   1 
ATOM   189  C  CA  . ASN   A 1 24  ? 16.816  8.981   7.688   1.00 58.61 ? 37  ASN   A CA  1 
ATOM   190  C  C   . ASN   A 1 24  ? 16.799  9.167   9.205   1.00 51.13 ? 37  ASN   A C   1 
ATOM   191  O  O   . ASN   A 1 24  ? 17.855  8.969   9.800   1.00 49.86 ? 37  ASN   A O   1 
ATOM   192  C  CB  . ASN   A 1 24  ? 16.391  10.231  6.910   1.00 63.82 ? 37  ASN   A CB  1 
ATOM   193  C  CG  . ASN   A 1 24  ? 16.793  10.130  5.454   1.00 56.02 ? 37  ASN   A CG  1 
ATOM   194  O  OD1 . ASN   A 1 24  ? 17.778  9.448   5.132   1.00 44.90 ? 37  ASN   A OD1 1 
ATOM   195  N  ND2 . ASN   A 1 24  ? 16.058  10.797  4.578   0.10 53.21 ? 37  ASN   A ND2 1 
ATOM   196  N  N   . GLY   A 1 25  A 15.646  9.535   9.813   1.00 55.15 ? 37  GLY   A N   1 
ATOM   197  C  CA  . GLY   A 1 25  A 15.597  9.913   11.228  1.00 54.46 ? 37  GLY   A CA  1 
ATOM   198  C  C   . GLY   A 1 25  A 14.474  9.284   12.079  1.00 58.39 ? 37  GLY   A C   1 
ATOM   199  O  O   . GLY   A 1 25  A 14.628  8.184   12.628  1.00 52.78 ? 37  GLY   A O   1 
ATOM   200  N  N   . PRO   A 1 26  ? 13.359  10.016  12.350  1.00 54.08 ? 38  PRO   A N   1 
ATOM   201  C  CA  . PRO   A 1 26  ? 12.414  9.625   13.402  1.00 58.36 ? 38  PRO   A CA  1 
ATOM   202  C  C   . PRO   A 1 26  ? 11.545  8.399   13.068  1.00 51.32 ? 38  PRO   A C   1 
ATOM   203  O  O   . PRO   A 1 26  ? 11.777  7.721   12.063  1.00 42.63 ? 38  PRO   A O   1 
ATOM   204  C  CB  . PRO   A 1 26  ? 11.592  10.899  13.608  0.10 55.68 ? 38  PRO   A CB  1 
ATOM   205  C  CG  . PRO   A 1 26  ? 11.616  11.546  12.234  0.10 55.57 ? 38  PRO   A CG  1 
ATOM   206  C  CD  . PRO   A 1 26  ? 12.978  11.270  11.679  0.10 55.29 ? 38  PRO   A CD  1 
ATOM   207  N  N   . SER   A 1 27  ? 10.573  8.104   13.951  1.00 41.76 ? 39  SER   A N   1 
ATOM   208  C  CA  . SER   A 1 27  ? 9.637   6.998   13.791  1.00 43.38 ? 39  SER   A CA  1 
ATOM   209  C  C   . SER   A 1 27  ? 8.303   7.491   13.229  1.00 35.56 ? 39  SER   A C   1 
ATOM   210  O  O   . SER   A 1 27  ? 7.787   8.532   13.609  1.00 32.87 ? 39  SER   A O   1 
ATOM   211  C  CB  . SER   A 1 27  ? 9.398   6.248   15.095  1.00 46.82 ? 39  SER   A CB  1 
ATOM   212  O  OG  . SER   A 1 27  ? 10.095  5.003   15.115  1.00 49.43 ? 39  SER   A OG  1 
ATOM   213  N  N   . LYS   A 1 28  ? 7.719   6.705   12.333  1.00 28.87 ? 40  LYS   A N   1 
ATOM   214  C  CA  . LYS   A 1 28  ? 6.351   6.957   11.935  1.00 30.72 ? 40  LYS   A CA  1 
ATOM   215  C  C   . LYS   A 1 28  ? 5.555   5.648   12.030  1.00 26.69 ? 40  LYS   A C   1 
ATOM   216  O  O   . LYS   A 1 28  ? 6.144   4.569   12.253  1.00 23.19 ? 40  LYS   A O   1 
ATOM   217  C  CB  . LYS   A 1 28  ? 6.313   7.585   10.538  1.00 28.32 ? 40  LYS   A CB  1 
ATOM   218  C  CG  . LYS   A 1 28  ? 6.589   6.633   9.403   1.00 29.73 ? 40  LYS   A CG  1 
ATOM   219  C  CD  . LYS   A 1 28  ? 6.233   7.183   8.053   1.00 35.47 ? 40  LYS   A CD  1 
ATOM   220  C  CE  . LYS   A 1 28  ? 6.728   6.286   6.941   1.00 36.05 ? 40  LYS   A CE  1 
ATOM   221  N  NZ  . LYS   A 1 28  ? 6.820   7.046   5.687   1.00 37.98 ? 40  LYS   A NZ  1 
ATOM   222  N  N   . PHE   A 1 29  ? 4.246   5.810   11.776  1.00 21.22 ? 41  PHE   A N   1 
ATOM   223  C  CA  . PHE   A 1 29  ? 3.201   4.834   12.028  1.00 24.25 ? 41  PHE   A CA  1 
ATOM   224  C  C   . PHE   A 1 29  ? 2.255   4.809   10.827  1.00 18.62 ? 41  PHE   A C   1 
ATOM   225  O  O   . PHE   A 1 29  ? 1.901   5.867   10.303  1.00 14.15 ? 41  PHE   A O   1 
ATOM   226  C  CB  . PHE   A 1 29  ? 2.384   5.134   13.304  1.00 28.44 ? 41  PHE   A CB  1 
ATOM   227  C  CG  . PHE   A 1 29  ? 3.282   5.424   14.485  1.00 40.16 ? 41  PHE   A CG  1 
ATOM   228  C  CD1 . PHE   A 1 29  ? 3.910   4.390   15.178  1.00 45.72 ? 41  PHE   A CD1 1 
ATOM   229  C  CD2 . PHE   A 1 29  ? 3.593   6.737   14.837  1.00 40.93 ? 41  PHE   A CD2 1 
ATOM   230  C  CE1 . PHE   A 1 29  ? 4.802   4.669   16.211  1.00 50.03 ? 41  PHE   A CE1 1 
ATOM   231  C  CE2 . PHE   A 1 29  ? 4.498   7.011   15.853  1.00 39.86 ? 41  PHE   A CE2 1 
ATOM   232  C  CZ  . PHE   A 1 29  ? 5.113   5.978   16.523  1.00 45.26 ? 41  PHE   A CZ  1 
ATOM   233  N  N   . CYS   A 1 30  ? 1.918   3.561   10.446  1.00 16.40 ? 42  CYS   A N   1 
ATOM   234  C  CA  . CYS   A 1 30  ? 0.959   3.228   9.415   1.00 16.47 ? 42  CYS   A CA  1 
ATOM   235  C  C   . CYS   A 1 30  ? 0.022   2.101   9.897   1.00 13.57 ? 42  CYS   A C   1 
ATOM   236  O  O   . CYS   A 1 30  ? 0.206   1.422   10.889  1.00 13.66 ? 42  CYS   A O   1 
ATOM   237  C  CB  . CYS   A 1 30  ? 1.708   2.805   8.154   1.00 15.64 ? 42  CYS   A CB  1 
ATOM   238  S  SG  . CYS   A 1 30  ? 2.388   4.159   7.133   1.00 19.36 ? 42  CYS   A SG  1 
ATOM   239  N  N   . GLY   A 1 31  ? -0.986  1.850   9.107   1.00 13.23 ? 43  GLY   A N   1 
ATOM   240  C  CA  . GLY   A 1 31  ? -1.772  0.654   9.236   1.00 14.68 ? 43  GLY   A CA  1 
ATOM   241  C  C   . GLY   A 1 31  ? -1.224  -0.340  8.220   1.00 15.38 ? 43  GLY   A C   1 
ATOM   242  O  O   . GLY   A 1 31  ? -0.232  -0.058  7.509   1.00 16.55 ? 43  GLY   A O   1 
ATOM   243  N  N   . GLY   A 1 32  ? -1.951  -1.445  8.126   1.00 14.54 ? 44  GLY   A N   1 
ATOM   244  C  CA  . GLY   A 1 32  ? -1.588  -2.603  7.337   1.00 15.76 ? 44  GLY   A CA  1 
ATOM   245  C  C   . GLY   A 1 32  ? -2.550  -3.725  7.700   1.00 16.58 ? 44  GLY   A C   1 
ATOM   246  O  O   . GLY   A 1 32  ? -3.353  -3.568  8.622   1.00 14.31 ? 44  GLY   A O   1 
ATOM   247  N  N   . PHE   A 1 33  ? -2.462  -4.830  6.964   1.00 18.37 ? 45  PHE   A N   1 
ATOM   248  C  CA  . PHE   A 1 33  ? -3.247  -6.006  7.277   1.00 17.98 ? 45  PHE   A CA  1 
ATOM   249  C  C   . PHE   A 1 33  ? -2.511  -7.289  6.947   1.00 16.02 ? 45  PHE   A C   1 
ATOM   250  O  O   . PHE   A 1 33  ? -1.825  -7.382  5.942   1.00 14.37 ? 45  PHE   A O   1 
ATOM   251  C  CB  . PHE   A 1 33  ? -4.603  -5.967  6.611   1.00 19.34 ? 45  PHE   A CB  1 
ATOM   252  C  CG  . PHE   A 1 33  ? -4.619  -5.577  5.172   1.00 20.66 ? 45  PHE   A CG  1 
ATOM   253  C  CD1 . PHE   A 1 33  ? -4.314  -4.277  4.783   1.00 21.40 ? 45  PHE   A CD1 1 
ATOM   254  C  CD2 . PHE   A 1 33  ? -5.020  -6.499  4.223   1.00 21.24 ? 45  PHE   A CD2 1 
ATOM   255  C  CE1 . PHE   A 1 33  ? -4.398  -3.912  3.441   1.00 21.95 ? 45  PHE   A CE1 1 
ATOM   256  C  CE2 . PHE   A 1 33  ? -5.053  -6.151  2.888   1.00 22.65 ? 45  PHE   A CE2 1 
ATOM   257  C  CZ  . PHE   A 1 33  ? -4.764  -4.855  2.500   1.00 21.29 ? 45  PHE   A CZ  1 
ATOM   258  N  N   . LEU   A 1 34  ? -2.745  -8.288  7.819   1.00 15.66 ? 46  LEU   A N   1 
ATOM   259  C  CA  . LEU   A 1 34  ? -2.163  -9.603  7.659   1.00 15.23 ? 46  LEU   A CA  1 
ATOM   260  C  C   . LEU   A 1 34  ? -2.996  -10.368 6.599   1.00 16.85 ? 46  LEU   A C   1 
ATOM   261  O  O   . LEU   A 1 34  ? -4.177  -10.583 6.823   1.00 15.18 ? 46  LEU   A O   1 
ATOM   262  C  CB  . LEU   A 1 34  ? -2.172  -10.311 9.026   1.00 15.35 ? 46  LEU   A CB  1 
ATOM   263  C  CG  . LEU   A 1 34  ? -1.333  -11.574 9.148   1.00 16.73 ? 46  LEU   A CG  1 
ATOM   264  C  CD1 . LEU   A 1 34  ? 0.117   -11.194 9.268   1.00 16.82 ? 46  LEU   A CD1 1 
ATOM   265  C  CD2 . LEU   A 1 34  ? -1.756  -12.445 10.324  1.00 18.91 ? 46  LEU   A CD2 1 
ATOM   266  N  N   . ILE   A 1 35  ? -2.322  -10.878 5.555   1.00 16.10 ? 47  ILE   A N   1 
ATOM   267  C  CA  . ILE   A 1 35  ? -2.921  -11.639 4.448   1.00 20.60 ? 47  ILE   A CA  1 
ATOM   268  C  C   . ILE   A 1 35  ? -2.379  -13.063 4.390   1.00 20.13 ? 47  ILE   A C   1 
ATOM   269  O  O   . ILE   A 1 35  ? -3.013  -13.869 3.757   1.00 19.76 ? 47  ILE   A O   1 
ATOM   270  C  CB  . ILE   A 1 35  ? -2.637  -10.976 3.086   1.00 22.05 ? 47  ILE   A CB  1 
ATOM   271  C  CG1 . ILE   A 1 35  ? -1.132  -10.745 2.878   1.00 22.84 ? 47  ILE   A CG1 1 
ATOM   272  C  CG2 . ILE   A 1 35  ? -3.444  -9.691  3.039   1.00 27.36 ? 47  ILE   A CG2 1 
ATOM   273  C  CD1 . ILE   A 1 35  ? -0.706  -10.539 1.468   1.00 26.95 ? 47  ILE   A CD1 1 
ATOM   274  N  N   . ARG   A 1 36  ? -1.252  -13.344 5.044   1.00 22.86 ? 48  ARG   A N   1 
ATOM   275  C  CA  . ARG   A 1 36  ? -0.787  -14.695 5.329   1.00 22.80 ? 48  ARG   A CA  1 
ATOM   276  C  C   . ARG   A 1 36  ? -0.087  -14.691 6.691   1.00 21.01 ? 48  ARG   A C   1 
ATOM   277  O  O   . ARG   A 1 36  ? 0.220   -13.611 7.224   1.00 18.70 ? 48  ARG   A O   1 
ATOM   278  C  CB  . ARG   A 1 36  ? 0.193   -15.153 4.239   1.00 27.84 ? 48  ARG   A CB  1 
ATOM   279  C  CG  . ARG   A 1 36  ? -0.119  -16.535 3.664   1.00 31.18 ? 48  ARG   A CG  1 
ATOM   280  C  CD  . ARG   A 1 36  ? 0.906   -17.011 2.658   1.00 36.95 ? 48  ARG   A CD  1 
ATOM   281  N  NE  . ARG   A 1 36  ? 2.280   -16.828 3.150   1.00 40.13 ? 48  ARG   A NE  1 
ATOM   282  C  CZ  . ARG   A 1 36  ? 3.379   -16.837 2.398   1.00 42.96 ? 48  ARG   A CZ  1 
ATOM   283  N  NH1 . ARG   A 1 36  ? 3.297   -17.052 1.092   1.00 42.71 ? 48  ARG   A NH1 1 
ATOM   284  N  NH2 . ARG   A 1 36  ? 4.554   -16.610 2.964   1.00 41.92 ? 48  ARG   A NH2 1 
ATOM   285  N  N   . ARG   A 1 37  ? 0.215   -15.877 7.237   1.00 17.36 ? 49  ARG   A N   1 
ATOM   286  C  CA  . ARG   A 1 37  ? 0.753   -15.906 8.582   1.00 19.88 ? 49  ARG   A CA  1 
ATOM   287  C  C   . ARG   A 1 37  ? 1.957   -14.991 8.648   1.00 17.95 ? 49  ARG   A C   1 
ATOM   288  O  O   . ARG   A 1 37  ? 2.057   -14.242 9.590   1.00 19.06 ? 49  ARG   A O   1 
ATOM   289  C  CB  . ARG   A 1 37  ? 1.046   -17.327 9.067   1.00 23.73 ? 49  ARG   A CB  1 
ATOM   290  C  CG  . ARG   A 1 37  ? -0.237  -18.091 9.408   1.00 21.79 ? 49  ARG   A CG  1 
ATOM   291  C  CD  . ARG   A 1 37  ? -0.028  -19.526 9.914   1.00 21.60 ? 49  ARG   A CD  1 
ATOM   292  N  NE  . ARG   A 1 37  ? 0.648   -19.476 11.200  1.00 20.98 ? 49  ARG   A NE  1 
ATOM   293  C  CZ  . ARG   A 1 37  ? 1.525   -20.396 11.644  1.00 22.03 ? 49  ARG   A CZ  1 
ATOM   294  N  NH1 . ARG   A 1 37  ? 1.819   -21.470 10.940  1.00 19.94 ? 49  ARG   A NH1 1 
ATOM   295  N  NH2 . ARG   A 1 37  ? 2.107   -20.239 12.812  1.00 19.22 ? 49  ARG   A NH2 1 
ATOM   296  N  N   . ASN   A 1 38  ? 2.786   -14.942 7.616   1.00 19.34 ? 50  ASN   A N   1 
ATOM   297  C  CA  . ASN   A 1 38  ? 3.974   -14.094 7.686   1.00 21.14 ? 50  ASN   A CA  1 
ATOM   298  C  C   . ASN   A 1 38  ? 4.029   -12.999 6.622   1.00 20.80 ? 50  ASN   A C   1 
ATOM   299  O  O   . ASN   A 1 38  ? 5.099   -12.458 6.340   1.00 20.41 ? 50  ASN   A O   1 
ATOM   300  C  CB  . ASN   A 1 38  ? 5.236   -14.909 7.552   1.00 19.13 ? 50  ASN   A CB  1 
ATOM   301  C  CG  . ASN   A 1 38  ? 5.395   -15.675 6.258   1.00 18.03 ? 50  ASN   A CG  1 
ATOM   302  O  OD1 . ASN   A 1 38  ? 4.473   -15.902 5.478   1.00 19.49 ? 50  ASN   A OD1 1 
ATOM   303  N  ND2 . ASN   A 1 38  ? 6.597   -16.183 6.084   1.00 18.64 ? 50  ASN   A ND2 1 
ATOM   304  N  N   . PHE   A 1 39  ? 2.865   -12.534 6.170   1.00 18.47 ? 51  PHE   A N   1 
ATOM   305  C  CA  . PHE   A 1 39  ? 2.847   -11.371 5.290   1.00 19.10 ? 51  PHE   A CA  1 
ATOM   306  C  C   . PHE   A 1 39  ? 1.792   -10.325 5.650   1.00 18.73 ? 51  PHE   A C   1 
ATOM   307  O  O   . PHE   A 1 39  ? 0.618   -10.632 5.928   1.00 18.80 ? 51  PHE   A O   1 
ATOM   308  C  CB  . PHE   A 1 39  ? 2.681   -11.833 3.852   1.00 21.93 ? 51  PHE   A CB  1 
ATOM   309  C  CG  . PHE   A 1 39  ? 3.989   -12.060 3.129   1.00 22.52 ? 51  PHE   A CG  1 
ATOM   310  C  CD1 . PHE   A 1 39  ? 4.651   -10.992 2.542   1.00 23.52 ? 51  PHE   A CD1 1 
ATOM   311  C  CD2 . PHE   A 1 39  ? 4.499   -13.338 2.948   1.00 23.91 ? 51  PHE   A CD2 1 
ATOM   312  C  CE1 . PHE   A 1 39  ? 5.829   -11.184 1.841   1.00 25.02 ? 51  PHE   A CE1 1 
ATOM   313  C  CE2 . PHE   A 1 39  ? 5.706   -13.529 2.278   1.00 23.79 ? 51  PHE   A CE2 1 
ATOM   314  C  CZ  . PHE   A 1 39  ? 6.370   -12.453 1.738   1.00 23.87 ? 51  PHE   A CZ  1 
ATOM   315  N  N   . VAL   A 1 40  ? 2.244   -9.072  5.586   1.00 16.74 ? 52  VAL   A N   1 
ATOM   316  C  CA  . VAL   A 1 40  ? 1.415   -7.894  5.792   1.00 17.83 ? 52  VAL   A CA  1 
ATOM   317  C  C   . VAL   A 1 40  ? 1.373   -7.040  4.523   1.00 17.37 ? 52  VAL   A C   1 
ATOM   318  O  O   . VAL   A 1 40  ? 2.390   -6.794  3.858   1.00 16.85 ? 52  VAL   A O   1 
ATOM   319  C  CB  . VAL   A 1 40  ? 1.908   -7.066  6.999   1.00 18.83 ? 52  VAL   A CB  1 
ATOM   320  C  CG1 . VAL   A 1 40  ? 1.173   -5.736  7.117   1.00 20.16 ? 52  VAL   A CG1 1 
ATOM   321  C  CG2 . VAL   A 1 40  ? 1.784   -7.862  8.293   1.00 19.02 ? 52  VAL   A CG2 1 
ATOM   322  N  N   A LEU   A 1 41  ? 0.180   -6.555  4.195   0.50 16.31 ? 53  LEU   A N   1 
ATOM   323  N  N   B LEU   A 1 41  ? 0.159   -6.609  4.159   0.50 17.57 ? 53  LEU   A N   1 
ATOM   324  C  CA  A LEU   A 1 41  ? 0.053   -5.685  3.044   0.50 15.62 ? 53  LEU   A CA  1 
ATOM   325  C  CA  B LEU   A 1 41  ? -0.017  -5.662  3.071   0.50 17.85 ? 53  LEU   A CA  1 
ATOM   326  C  C   A LEU   A 1 41  ? -0.192  -4.262  3.547   0.50 15.63 ? 53  LEU   A C   1 
ATOM   327  C  C   B LEU   A 1 41  ? -0.074  -4.256  3.669   0.50 16.77 ? 53  LEU   A C   1 
ATOM   328  O  O   A LEU   A 1 41  ? -1.061  -4.063  4.384   0.50 15.10 ? 53  LEU   A O   1 
ATOM   329  O  O   B LEU   A 1 41  ? -0.672  -4.047  4.711   0.50 16.67 ? 53  LEU   A O   1 
ATOM   330  C  CB  A LEU   A 1 41  ? -1.097  -6.199  2.184   0.50 15.69 ? 53  LEU   A CB  1 
ATOM   331  C  CB  B LEU   A 1 41  ? -1.311  -5.974  2.317   0.50 19.94 ? 53  LEU   A CB  1 
ATOM   332  C  CG  A LEU   A 1 41  ? -1.288  -5.458  0.869   0.50 14.69 ? 53  LEU   A CG  1 
ATOM   333  C  CG  B LEU   A 1 41  ? -1.148  -6.527  0.905   0.50 20.16 ? 53  LEU   A CG  1 
ATOM   334  C  CD1 A LEU   A 1 41  ? -0.046  -5.615  0.005   0.50 15.80 ? 53  LEU   A CD1 1 
ATOM   335  C  CD1 B LEU   A 1 41  ? -2.486  -6.587  0.189   0.50 20.85 ? 53  LEU   A CD1 1 
ATOM   336  C  CD2 A LEU   A 1 41  ? -2.517  -5.953  0.130   0.50 15.39 ? 53  LEU   A CD2 1 
ATOM   337  C  CD2 B LEU   A 1 41  ? -0.140  -5.709  0.118   0.50 21.34 ? 53  LEU   A CD2 1 
ATOM   338  N  N   . THR   A 1 42  ? 0.554   -3.293  3.015   1.00 14.97 ? 54  THR   A N   1 
ATOM   339  C  CA  . THR   A 1 42  ? 0.459   -1.900  3.441   1.00 15.50 ? 54  THR   A CA  1 
ATOM   340  C  C   . THR   A 1 42  ? 0.735   -0.964  2.253   1.00 15.07 ? 54  THR   A C   1 
ATOM   341  O  O   . THR   A 1 42  ? 0.875   -1.405  1.099   1.00 15.58 ? 54  THR   A O   1 
ATOM   342  C  CB  . THR   A 1 42  ? 1.507   -1.677  4.535   1.00 15.08 ? 54  THR   A CB  1 
ATOM   343  O  OG1 . THR   A 1 42  ? 1.356   -0.386  5.096   1.00 15.22 ? 54  THR   A OG1 1 
ATOM   344  C  CG2 . THR   A 1 42  ? 2.917   -1.823  4.002   1.00 15.62 ? 54  THR   A CG2 1 
ATOM   345  N  N   . ALA   A 1 43  ? 0.883   0.332   2.537   1.00 15.41 ? 55  ALA   A N   1 
ATOM   346  C  CA  . ALA   A 1 43  ? 1.252   1.281   1.486   1.00 17.10 ? 55  ALA   A CA  1 
ATOM   347  C  C   . ALA   A 1 43  ? 2.766   1.320   1.296   1.00 17.61 ? 55  ALA   A C   1 
ATOM   348  O  O   . ALA   A 1 43  ? 3.458   1.375   2.277   1.00 15.85 ? 55  ALA   A O   1 
ATOM   349  C  CB  . ALA   A 1 43  ? 0.758   2.669   1.820   1.00 15.93 ? 55  ALA   A CB  1 
ATOM   350  N  N   . ALA   A 1 44  ? 3.236   1.523   0.060   1.00 19.05 ? 56  ALA   A N   1 
ATOM   351  C  CA  . ALA   A 1 44  ? 4.638   1.753   -0.242  1.00 22.58 ? 56  ALA   A CA  1 
ATOM   352  C  C   . ALA   A 1 44  ? 5.181   2.996   0.470   1.00 22.71 ? 56  ALA   A C   1 
ATOM   353  O  O   . ALA   A 1 44  ? 6.285   2.942   0.947   1.00 22.54 ? 56  ALA   A O   1 
ATOM   354  C  CB  . ALA   A 1 44  ? 4.880   1.857   -1.738  1.00 25.54 ? 56  ALA   A CB  1 
ATOM   355  N  N   . HIS   A 1 45  ? 4.418   4.081   0.635   1.00 23.47 ? 57  HIS   A N   1 
ATOM   356  C  CA  . HIS   A 1 45  ? 4.959   5.230   1.347   1.00 21.59 ? 57  HIS   A CA  1 
ATOM   357  C  C   . HIS   A 1 45  ? 5.283   4.982   2.826   1.00 25.73 ? 57  HIS   A C   1 
ATOM   358  O  O   . HIS   A 1 45  ? 5.831   5.869   3.476   1.00 19.02 ? 57  HIS   A O   1 
ATOM   359  C  CB  . HIS   A 1 45  ? 4.040   6.431   1.172   1.00 20.14 ? 57  HIS   A CB  1 
ATOM   360  C  CG  . HIS   A 1 45  ? 2.782   6.440   1.959   1.00 19.51 ? 57  HIS   A CG  1 
ATOM   361  N  ND1 . HIS   A 1 45  ? 1.558   6.098   1.371   1.00 17.21 ? 57  HIS   A ND1 1 
ATOM   362  C  CD2 . HIS   A 1 45  ? 2.513   6.899   3.196   1.00 19.14 ? 57  HIS   A CD2 1 
ATOM   363  C  CE1 . HIS   A 1 45  ? 0.606   6.274   2.257   1.00 19.60 ? 57  HIS   A CE1 1 
ATOM   364  N  NE2 . HIS   A 1 45  ? 1.156   6.736   3.392   1.00 19.46 ? 57  HIS   A NE2 1 
ATOM   365  N  N   . CYS   A 1 46  ? 4.889   3.830   3.382   1.00 22.11 ? 58  CYS   A N   1 
ATOM   366  C  CA  . CYS   A 1 46  ? 5.205   3.521   4.752   1.00 22.21 ? 58  CYS   A CA  1 
ATOM   367  C  C   . CYS   A 1 46  ? 6.549   2.808   4.859   1.00 24.20 ? 58  CYS   A C   1 
ATOM   368  O  O   . CYS   A 1 46  ? 6.828   2.270   5.901   1.00 23.04 ? 58  CYS   A O   1 
ATOM   369  C  CB  . CYS   A 1 46  ? 4.148   2.596   5.339   1.00 21.84 ? 58  CYS   A CB  1 
ATOM   370  S  SG  . CYS   A 1 46  ? 2.489   3.318   5.308   1.00 18.66 ? 58  CYS   A SG  1 
ATOM   371  N  N   . ALA   A 1 47  ? 7.343   2.707   3.795   1.00 23.46 ? 59  ALA   A N   1 
ATOM   372  C  CA  . ALA   A 1 47  ? 8.596   1.987   3.935   1.00 24.14 ? 59  ALA   A CA  1 
ATOM   373  C  C   . ALA   A 1 47  ? 9.542   2.810   4.803   1.00 24.42 ? 59  ALA   A C   1 
ATOM   374  O  O   . ALA   A 1 47  ? 9.247   3.954   5.128   1.00 26.41 ? 59  ALA   A O   1 
ATOM   375  C  CB  . ALA   A 1 47  ? 9.187   1.622   2.596   1.00 25.44 ? 59  ALA   A CB  1 
ATOM   376  N  N   . GLY   A 1 48  ? 10.670  2.200   5.193   1.00 23.07 ? 60  GLY   A N   1 
ATOM   377  C  CA  . GLY   A 1 48  ? 11.564  2.772   6.179   1.00 21.83 ? 60  GLY   A CA  1 
ATOM   378  C  C   . GLY   A 1 48  ? 12.791  1.889   6.357   1.00 21.45 ? 60  GLY   A C   1 
ATOM   379  O  O   . GLY   A 1 48  ? 12.992  0.919   5.632   1.00 24.50 ? 60  GLY   A O   1 
ATOM   380  N  N   . ARG   A 1 49  ? 13.634  2.244   7.309   1.00 28.41 ? 61  ARG   A N   1 
ATOM   381  C  CA  . ARG   A 1 49  ? 14.854  1.484   7.543   1.00 31.21 ? 61  ARG   A CA  1 
ATOM   382  C  C   . ARG   A 1 49  ? 14.442  0.119   8.070   1.00 28.92 ? 61  ARG   A C   1 
ATOM   383  O  O   . ARG   A 1 49  ? 14.949  -0.922  7.642   1.00 29.56 ? 61  ARG   A O   1 
ATOM   384  C  CB  . ARG   A 1 49  ? 15.775  2.224   8.524   1.00 36.50 ? 61  ARG   A CB  1 
ATOM   385  C  CG  . ARG   A 1 49  ? 17.136  1.574   8.720   1.00 36.00 ? 61  ARG   A CG  1 
ATOM   386  C  CD  . ARG   A 1 49  ? 18.070  2.476   9.499   0.50 37.53 ? 61  ARG   A CD  1 
ATOM   387  N  NE  . ARG   A 1 49  ? 18.567  3.548   8.644   0.50 39.81 ? 61  ARG   A NE  1 
ATOM   388  C  CZ  . ARG   A 1 49  ? 19.374  3.370   7.605   0.50 39.92 ? 61  ARG   A CZ  1 
ATOM   389  N  NH1 . ARG   A 1 49  ? 19.808  2.168   7.272   0.50 41.92 ? 61  ARG   A NH1 1 
ATOM   390  N  NH2 . ARG   A 1 49  ? 19.766  4.409   6.901   0.50 44.44 ? 61  ARG   A NH2 1 
ATOM   391  N  N   . SER   A 1 50  ? 13.473  0.149   8.978   1.00 23.01 ? 63  SER   A N   1 
ATOM   392  C  CA  . SER   A 1 50  ? 13.054  -1.068  9.621   1.00 23.95 ? 63  SER   A CA  1 
ATOM   393  C  C   . SER   A 1 50  ? 11.648  -0.844  10.137  1.00 21.23 ? 63  SER   A C   1 
ATOM   394  O  O   . SER   A 1 50  ? 11.274  0.296   10.382  1.00 24.29 ? 63  SER   A O   1 
ATOM   395  C  CB  . SER   A 1 50  ? 14.003  -1.444  10.742  1.00 22.35 ? 63  SER   A CB  1 
ATOM   396  O  OG  . SER   A 1 50  ? 13.885  -0.473  11.779  1.00 24.35 ? 63  SER   A OG  1 
ATOM   397  N  N   . ILE   A 1 51  ? 10.916  -1.945  10.298  1.00 22.48 ? 64  ILE   A N   1 
ATOM   398  C  CA  . ILE   A 1 51  ? 9.500   -1.874  10.623  1.00 23.55 ? 64  ILE   A CA  1 
ATOM   399  C  C   . ILE   A 1 51  ? 9.213   -2.957  11.627  1.00 20.68 ? 64  ILE   A C   1 
ATOM   400  O  O   . ILE   A 1 51  ? 9.720   -4.068  11.480  1.00 16.66 ? 64  ILE   A O   1 
ATOM   401  C  CB  . ILE   A 1 51  ? 8.620   -2.033  9.377   1.00 22.23 ? 64  ILE   A CB  1 
ATOM   402  C  CG1 . ILE   A 1 51  ? 8.989   -0.975  8.348   1.00 23.41 ? 64  ILE   A CG1 1 
ATOM   403  C  CG2 . ILE   A 1 51  ? 7.125   -1.985  9.723   1.00 20.44 ? 64  ILE   A CG2 1 
ATOM   404  C  CD1 . ILE   A 1 51  ? 8.266   -1.108  7.014   1.00 23.01 ? 64  ILE   A CD1 1 
ATOM   405  N  N   . THR   A 1 52  ? 8.344   -2.599  12.575  1.00 23.09 ? 65  THR   A N   1 
ATOM   406  C  CA  . THR   A 1 52  ? 7.755   -3.563  13.495  1.00 23.08 ? 65  THR   A CA  1 
ATOM   407  C  C   . THR   A 1 52  ? 6.256   -3.607  13.281  1.00 23.22 ? 65  THR   A C   1 
ATOM   408  O  O   . THR   A 1 52  ? 5.631   -2.574  13.071  1.00 24.25 ? 65  THR   A O   1 
ATOM   409  C  CB  . THR   A 1 52  ? 8.035   -3.153  14.947  1.00 28.15 ? 65  THR   A CB  1 
ATOM   410  O  OG1 . THR   A 1 52  ? 9.441   -3.035  15.109  1.00 27.74 ? 65  THR   A OG1 1 
ATOM   411  C  CG2 . THR   A 1 52  ? 7.557   -4.145  15.993  1.00 31.08 ? 65  THR   A CG2 1 
ATOM   412  N  N   . VAL   A 1 53  ? 5.684   -4.806  13.371  1.00 18.86 ? 66  VAL   A N   1 
ATOM   413  C  CA  . VAL   A 1 53  ? 4.257   -4.959  13.236  1.00 16.97 ? 66  VAL   A CA  1 
ATOM   414  C  C   . VAL   A 1 53  ? 3.683   -5.444  14.559  1.00 14.72 ? 66  VAL   A C   1 
ATOM   415  O  O   . VAL   A 1 53  ? 4.186   -6.433  15.124  1.00 15.51 ? 66  VAL   A O   1 
ATOM   416  C  CB  . VAL   A 1 53  ? 3.935   -5.954  12.120  1.00 17.88 ? 66  VAL   A CB  1 
ATOM   417  C  CG1 . VAL   A 1 53  ? 2.502   -6.324  12.085  1.00 17.84 ? 66  VAL   A CG1 1 
ATOM   418  C  CG2 . VAL   A 1 53  ? 4.364   -5.421  10.794  1.00 20.85 ? 66  VAL   A CG2 1 
ATOM   419  N  N   . THR   A 1 54  ? 2.613   -4.788  15.022  1.00 12.26 ? 67  THR   A N   1 
ATOM   420  C  CA  . THR   A 1 54  ? 1.876   -5.252  16.164  1.00 12.19 ? 67  THR   A CA  1 
ATOM   421  C  C   . THR   A 1 54  ? 0.511   -5.742  15.670  1.00 13.61 ? 67  THR   A C   1 
ATOM   422  O  O   . THR   A 1 54  ? -0.283  -4.975  15.096  1.00 14.69 ? 67  THR   A O   1 
ATOM   423  C  CB  . THR   A 1 54  ? 1.724   -4.144  17.207  1.00 12.82 ? 67  THR   A CB  1 
ATOM   424  O  OG1 . THR   A 1 54  ? 3.025   -3.767  17.585  1.00 14.38 ? 67  THR   A OG1 1 
ATOM   425  C  CG2 . THR   A 1 54  ? 0.983   -4.609  18.444  1.00 11.70 ? 67  THR   A CG2 1 
ATOM   426  N  N   . LEU   A 1 55  ? 0.287   -7.029  15.836  1.00 12.61 ? 68  LEU   A N   1 
ATOM   427  C  CA  . LEU   A 1 55  ? -0.981  -7.691  15.633  1.00 13.79 ? 68  LEU   A CA  1 
ATOM   428  C  C   . LEU   A 1 55  ? -1.730  -7.921  16.960  1.00 14.44 ? 68  LEU   A C   1 
ATOM   429  O  O   . LEU   A 1 55  ? -1.134  -8.005  18.016  1.00 13.12 ? 68  LEU   A O   1 
ATOM   430  C  CB  . LEU   A 1 55  ? -0.686  -9.030  14.955  1.00 13.87 ? 68  LEU   A CB  1 
ATOM   431  C  CG  . LEU   A 1 55  ? 0.140   -8.951  13.681  1.00 15.06 ? 68  LEU   A CG  1 
ATOM   432  C  CD1 . LEU   A 1 55  ? 0.653   -10.321 13.318  1.00 14.16 ? 68  LEU   A CD1 1 
ATOM   433  C  CD2 . LEU   A 1 55  ? -0.626  -8.277  12.536  1.00 14.86 ? 68  LEU   A CD2 1 
ATOM   434  N  N   . GLY   A 1 56  ? -3.042  -8.090  16.876  1.00 15.04 ? 69  GLY   A N   1 
ATOM   435  C  CA  . GLY   A 1 56  ? -3.873  -8.388  18.042  1.00 15.05 ? 69  GLY   A CA  1 
ATOM   436  C  C   . GLY   A 1 56  ? -4.181  -7.132  18.860  1.00 15.85 ? 69  GLY   A C   1 
ATOM   437  O  O   . GLY   A 1 56  ? -4.689  -7.210  19.982  1.00 16.97 ? 69  GLY   A O   1 
ATOM   438  N  N   . ALA   A 1 57  ? -3.813  -5.945  18.372  1.00 14.30 ? 70  ALA   A N   1 
ATOM   439  C  CA  . ALA   A 1 57  ? -3.941  -4.779  19.240  1.00 13.19 ? 70  ALA   A CA  1 
ATOM   440  C  C   . ALA   A 1 57  ? -5.320  -4.130  19.100  1.00 13.83 ? 70  ALA   A C   1 
ATOM   441  O  O   . ALA   A 1 57  ? -5.980  -4.273  18.075  1.00 14.03 ? 70  ALA   A O   1 
ATOM   442  C  CB  . ALA   A 1 57  ? -2.847  -3.783  18.929  1.00 13.05 ? 70  ALA   A CB  1 
ATOM   443  N  N   . HIS   A 1 58  ? -5.721  -3.389  20.139  1.00 13.03 ? 71  HIS   A N   1 
ATOM   444  C  CA  . HIS   A 1 58  ? -6.855  -2.478  20.071  1.00 13.98 ? 71  HIS   A CA  1 
ATOM   445  C  C   . HIS   A 1 58  ? -6.381  -1.103  20.487  1.00 14.77 ? 71  HIS   A C   1 
ATOM   446  O  O   . HIS   A 1 58  ? -6.417  -0.155  19.708  1.00 15.09 ? 71  HIS   A O   1 
ATOM   447  C  CB  . HIS   A 1 58  ? -8.005  -2.979  20.928  1.00 13.45 ? 71  HIS   A CB  1 
ATOM   448  C  CG  . HIS   A 1 58  ? -9.170  -2.076  20.858  1.00 16.61 ? 71  HIS   A CG  1 
ATOM   449  N  ND1 . HIS   A 1 58  ? -9.749  -1.775  19.667  1.00 15.87 ? 71  HIS   A ND1 1 
ATOM   450  C  CD2 . HIS   A 1 58  ? -9.825  -1.351  21.823  1.00 16.85 ? 71  HIS   A CD2 1 
ATOM   451  C  CE1 . HIS   A 1 58  ? -10.751 -0.940  19.892  1.00 18.53 ? 71  HIS   A CE1 1 
ATOM   452  N  NE2 . HIS   A 1 58  ? -10.811 -0.641  21.203  1.00 15.92 ? 71  HIS   A NE2 1 
ATOM   453  N  N   . ASN   A 1 59  ? -5.943  -1.018  21.746  1.00 15.95 ? 72  ASN   A N   1 
ATOM   454  C  CA  . ASN   A 1 59  ? -5.391  0.224   22.264  1.00 16.40 ? 72  ASN   A CA  1 
ATOM   455  C  C   . ASN   A 1 59  ? -3.907  0.037   22.205  1.00 14.80 ? 72  ASN   A C   1 
ATOM   456  O  O   . ASN   A 1 59  ? -3.393  -0.853  22.910  1.00 16.85 ? 72  ASN   A O   1 
ATOM   457  C  CB  . ASN   A 1 59  ? -5.788  0.548   23.690  1.00 17.22 ? 72  ASN   A CB  1 
ATOM   458  C  CG  . ASN   A 1 59  ? -5.209  1.864   24.161  1.00 17.99 ? 72  ASN   A CG  1 
ATOM   459  O  OD1 . ASN   A 1 59  ? -4.060  2.193   23.846  1.00 17.06 ? 72  ASN   A OD1 1 
ATOM   460  N  ND2 . ASN   A 1 59  ? -6.050  2.621   24.856  1.00 15.42 ? 72  ASN   A ND2 1 
ATOM   461  N  N   A ILE   A 1 60  ? -3.234  0.842   21.372  0.50 14.85 ? 73  ILE   A N   1 
ATOM   462  N  N   B ILE   A 1 60  ? -3.234  0.838   21.368  0.50 15.26 ? 73  ILE   A N   1 
ATOM   463  C  CA  A ILE   A 1 60  ? -1.851  0.538   21.053  0.50 15.55 ? 73  ILE   A CA  1 
ATOM   464  C  CA  B ILE   A 1 60  ? -1.847  0.558   21.036  0.50 16.33 ? 73  ILE   A CA  1 
ATOM   465  C  C   A ILE   A 1 60  ? -0.900  1.013   22.150  0.50 16.95 ? 73  ILE   A C   1 
ATOM   466  C  C   B ILE   A 1 60  ? -0.921  0.923   22.198  0.50 17.30 ? 73  ILE   A C   1 
ATOM   467  O  O   A ILE   A 1 60  ? 0.299   0.778   22.066  0.50 18.35 ? 73  ILE   A O   1 
ATOM   468  O  O   B ILE   A 1 60  ? 0.232   0.506   22.228  0.50 18.25 ? 73  ILE   A O   1 
ATOM   469  C  CB  A ILE   A 1 60  ? -1.461  1.072   19.656  0.50 15.97 ? 73  ILE   A CB  1 
ATOM   470  C  CB  B ILE   A 1 60  ? -1.458  1.264   19.718  0.50 17.62 ? 73  ILE   A CB  1 
ATOM   471  C  CG1 A ILE   A 1 60  ? -1.847  2.533   19.434  0.50 16.46 ? 73  ILE   A CG1 1 
ATOM   472  C  CG1 B ILE   A 1 60  ? -0.297  0.585   18.978  0.50 18.38 ? 73  ILE   A CG1 1 
ATOM   473  C  CG2 A ILE   A 1 60  ? -2.023  0.178   18.575  0.50 14.14 ? 73  ILE   A CG2 1 
ATOM   474  C  CG2 B ILE   A 1 60  ? -1.142  2.726   19.973  0.50 16.56 ? 73  ILE   A CG2 1 
ATOM   475  C  CD1 A ILE   A 1 60  ? -0.913  3.508   20.081  0.50 16.91 ? 73  ILE   A CD1 1 
ATOM   476  C  CD1 B ILE   A 1 60  ? -0.234  -0.935  19.068  0.50 17.56 ? 73  ILE   A CD1 1 
ATOM   477  N  N   . THR   A 1 61  ? -1.405  1.654   23.205  1.00 18.92 ? 74  THR   A N   1 
ATOM   478  C  CA  . THR   A 1 61  ? -0.573  1.899   24.388  1.00 18.30 ? 74  THR   A CA  1 
ATOM   479  C  C   . THR   A 1 61  ? -0.793  0.830   25.456  1.00 19.18 ? 74  THR   A C   1 
ATOM   480  O  O   . THR   A 1 61  ? -0.219  0.929   26.516  1.00 22.34 ? 74  THR   A O   1 
ATOM   481  C  CB  . THR   A 1 61  ? -0.871  3.232   25.051  1.00 17.73 ? 74  THR   A CB  1 
ATOM   482  O  OG1 . THR   A 1 61  ? -2.213  3.234   25.537  1.00 14.41 ? 74  THR   A OG1 1 
ATOM   483  C  CG2 . THR   A 1 61  ? -0.658  4.380   24.099  1.00 20.24 ? 74  THR   A CG2 1 
ATOM   484  N  N   . GLU   A 1 62  ? -1.586  -0.200  25.175  1.00 17.69 ? 75  GLU   A N   1 
ATOM   485  C  CA  . GLU   A 1 62  ? -1.907  -1.219  26.165  1.00 19.98 ? 75  GLU   A CA  1 
ATOM   486  C  C   . GLU   A 1 62  ? -1.549  -2.610  25.638  1.00 15.53 ? 75  GLU   A C   1 
ATOM   487  O  O   . GLU   A 1 62  ? -2.214  -3.211  24.797  1.00 14.18 ? 75  GLU   A O   1 
ATOM   488  C  CB  . GLU   A 1 62  ? -3.391  -1.119  26.523  1.00 20.89 ? 75  GLU   A CB  1 
ATOM   489  C  CG  . GLU   A 1 62  ? -3.773  -2.116  27.603  1.00 24.83 ? 75  GLU   A CG  1 
ATOM   490  C  CD  . GLU   A 1 62  ? -5.245  -2.414  27.731  1.00 29.39 ? 75  GLU   A CD  1 
ATOM   491  O  OE1 . GLU   A 1 62  ? -5.752  -2.120  28.817  1.00 33.91 ? 75  GLU   A OE1 1 
ATOM   492  O  OE2 . GLU   A 1 62  ? -5.889  -2.965  26.730  1.00 30.45 ? 75  GLU   A OE2 1 
ATOM   493  N  N   . GLU   A 1 63  ? -0.491  -3.175  26.166  1.00 17.11 ? 76  GLU   A N   1 
ATOM   494  C  CA  . GLU   A 1 63  ? -0.125  -4.520  25.785  1.00 19.16 ? 76  GLU   A CA  1 
ATOM   495  C  C   . GLU   A 1 63  ? -1.138  -5.451  26.400  1.00 18.19 ? 76  GLU   A C   1 
ATOM   496  O  O   . GLU   A 1 63  ? -1.594  -5.169  27.477  1.00 19.48 ? 76  GLU   A O   1 
ATOM   497  C  CB  . GLU   A 1 63  ? 1.243   -4.915  26.279  1.00 23.33 ? 76  GLU   A CB  1 
ATOM   498  C  CG  . GLU   A 1 63  ? 2.295   -3.981  25.755  1.00 28.48 ? 76  GLU   A CG  1 
ATOM   499  C  CD  . GLU   A 1 63  ? 3.706   -4.509  25.960  1.00 26.68 ? 76  GLU   A CD  1 
ATOM   500  O  OE1 . GLU   A 1 63  ? 3.847   -5.512  26.701  1.00 25.23 ? 76  GLU   A OE1 1 
ATOM   501  O  OE2 . GLU   A 1 63  ? 4.644   -3.897  25.375  1.00 28.61 ? 76  GLU   A OE2 1 
ATOM   502  N  N   . GLU   A 1 64  ? -1.537  -6.448  25.620  1.00 17.64 ? 77  GLU   A N   1 
ATOM   503  C  CA  . GLU   A 1 64  ? -2.474  -7.448  26.015  1.00 18.03 ? 77  GLU   A CA  1 
ATOM   504  C  C   . GLU   A 1 64  ? -1.886  -8.784  25.635  1.00 19.25 ? 77  GLU   A C   1 
ATOM   505  O  O   . GLU   A 1 64  ? -0.945  -8.875  24.857  1.00 16.78 ? 77  GLU   A O   1 
ATOM   506  C  CB  . GLU   A 1 64  ? -3.818  -7.275  25.313  1.00 19.81 ? 77  GLU   A CB  1 
ATOM   507  C  CG  . GLU   A 1 64  ? -4.449  -5.913  25.481  1.00 17.83 ? 77  GLU   A CG  1 
ATOM   508  C  CD  . GLU   A 1 64  ? -5.774  -5.906  24.776  1.00 17.51 ? 77  GLU   A CD  1 
ATOM   509  O  OE1 . GLU   A 1 64  ? -5.909  -5.296  23.714  1.00 17.02 ? 77  GLU   A OE1 1 
ATOM   510  O  OE2 . GLU   A 1 64  ? -6.664  -6.508  25.307  1.00 16.00 ? 77  GLU   A OE2 1 
ATOM   511  N  N   . ASP   A 1 65  ? -2.510  -9.804  26.208  1.00 18.90 ? 78  ASP   A N   1 
ATOM   512  C  CA  . ASP   A 1 65  ? -2.241  -11.175 25.890  1.00 23.15 ? 78  ASP   A CA  1 
ATOM   513  C  C   . ASP   A 1 65  ? -2.507  -11.509 24.420  1.00 21.77 ? 78  ASP   A C   1 
ATOM   514  O  O   . ASP   A 1 65  ? -1.942  -12.483 23.926  1.00 20.97 ? 78  ASP   A O   1 
ATOM   515  C  CB  . ASP   A 1 65  ? -3.137  -12.053 26.771  1.00 26.83 ? 78  ASP   A CB  1 
ATOM   516  C  CG  . ASP   A 1 65  ? -2.571  -13.453 26.784  1.00 31.67 ? 78  ASP   A CG  1 
ATOM   517  O  OD1 . ASP   A 1 65  ? -1.344  -13.586 27.062  1.00 36.00 ? 78  ASP   A OD1 1 
ATOM   518  O  OD2 . ASP   A 1 65  ? -3.326  -14.376 26.437  1.00 39.70 ? 78  ASP   A OD2 1 
ATOM   519  N  N   . THR   A 1 66  ? -3.425  -10.774 23.766  1.00 18.32 ? 79  THR   A N   1 
ATOM   520  C  CA  . THR   A 1 66  ? -3.646  -10.907 22.333  1.00 16.44 ? 79  THR   A CA  1 
ATOM   521  C  C   . THR   A 1 66  ? -2.492  -10.462 21.437  1.00 14.64 ? 79  THR   A C   1 
ATOM   522  O  O   . THR   A 1 66  ? -2.437  -10.768 20.243  1.00 14.21 ? 79  THR   A O   1 
ATOM   523  C  CB  . THR   A 1 66  ? -4.862  -10.088 21.908  1.00 15.32 ? 79  THR   A CB  1 
ATOM   524  O  OG1 . THR   A 1 66  ? -4.626  -8.731  22.266  1.00 14.98 ? 79  THR   A OG1 1 
ATOM   525  C  CG2 . THR   A 1 66  ? -6.137  -10.586 22.564  1.00 16.54 ? 79  THR   A CG2 1 
ATOM   526  N  N   . TRP   A 1 67  ? -1.606  -9.627  21.931  1.00 15.99 ? 80  TRP   A N   1 
ATOM   527  C  CA  . TRP   A 1 67  ? -0.650  -9.018  21.019  1.00 14.10 ? 80  TRP   A CA  1 
ATOM   528  C  C   . TRP   A 1 67  ? 0.282   -10.066 20.444  1.00 17.21 ? 80  TRP   A C   1 
ATOM   529  O  O   . TRP   A 1 67  ? 0.676   -11.011 21.124  1.00 18.79 ? 80  TRP   A O   1 
ATOM   530  C  CB  . TRP   A 1 67  ? 0.199   -7.974  21.718  1.00 15.59 ? 80  TRP   A CB  1 
ATOM   531  C  CG  . TRP   A 1 67  ? -0.480  -6.675  21.960  1.00 15.95 ? 80  TRP   A CG  1 
ATOM   532  C  CD1 . TRP   A 1 67  ? -1.825  -6.406  22.049  1.00 15.42 ? 80  TRP   A CD1 1 
ATOM   533  C  CD2 . TRP   A 1 67  ? 0.214   -5.440  21.992  1.00 16.21 ? 80  TRP   A CD2 1 
ATOM   534  N  NE1 . TRP   A 1 67  ? -2.002  -5.063  22.239  1.00 16.03 ? 80  TRP   A NE1 1 
ATOM   535  C  CE2 . TRP   A 1 67  ? -0.766  -4.444  22.183  1.00 16.45 ? 80  TRP   A CE2 1 
ATOM   536  C  CE3 . TRP   A 1 67  ? 1.577   -5.092  21.947  1.00 16.76 ? 80  TRP   A CE3 1 
ATOM   537  C  CZ2 . TRP   A 1 67  ? -0.410  -3.109  22.372  1.00 14.38 ? 80  TRP   A CZ2 1 
ATOM   538  C  CZ3 . TRP   A 1 67  ? 1.905   -3.756  22.046  1.00 16.62 ? 80  TRP   A CZ3 1 
ATOM   539  C  CH2 . TRP   A 1 67  ? 0.911   -2.781  22.232  1.00 15.89 ? 80  TRP   A CH2 1 
ATOM   540  N  N   . GLN   A 1 68  ? 0.729   -9.794  19.221  1.00 18.28 ? 81  GLN   A N   1 
ATOM   541  C  CA  . GLN   A 1 68  ? 1.866   -10.479 18.630  1.00 17.13 ? 81  GLN   A CA  1 
ATOM   542  C  C   . GLN   A 1 68  ? 2.630   -9.394  17.886  1.00 18.77 ? 81  GLN   A C   1 
ATOM   543  O  O   . GLN   A 1 68  ? 2.064   -8.720  17.037  1.00 18.94 ? 81  GLN   A O   1 
ATOM   544  C  CB  . GLN   A 1 68  ? 1.417   -11.637 17.744  1.00 16.30 ? 81  GLN   A CB  1 
ATOM   545  C  CG  . GLN   A 1 68  ? 0.852   -12.825 18.483  1.00 16.81 ? 81  GLN   A CG  1 
ATOM   546  C  CD  . GLN   A 1 68  ? 0.316   -13.837 17.501  1.00 17.67 ? 81  GLN   A CD  1 
ATOM   547  O  OE1 . GLN   A 1 68  ? 1.038   -14.325 16.647  1.00 17.40 ? 81  GLN   A OE1 1 
ATOM   548  N  NE2 . GLN   A 1 68  ? -0.984  -14.061 17.527  1.00 18.64 ? 81  GLN   A NE2 1 
ATOM   549  N  N   . LYS   A 1 69  ? 3.842   -9.141  18.344  1.00 18.62 ? 82  LYS   A N   1 
ATOM   550  C  CA  . LYS   A 1 69  ? 4.643   -8.039  17.870  1.00 21.81 ? 82  LYS   A CA  1 
ATOM   551  C  C   . LYS   A 1 69  ? 5.893   -8.644  17.228  1.00 20.54 ? 82  LYS   A C   1 
ATOM   552  O  O   . LYS   A 1 69  ? 6.615   -9.396  17.863  1.00 24.66 ? 82  LYS   A O   1 
ATOM   553  C  CB  . LYS   A 1 69  ? 4.919   -7.091  19.045  1.00 24.47 ? 82  LYS   A CB  1 
ATOM   554  C  CG  . LYS   A 1 69  ? 5.603   -5.795  18.640  1.00 27.55 ? 82  LYS   A CG  1 
ATOM   555  C  CD  . LYS   A 1 69  ? 5.933   -4.911  19.817  1.00 30.41 ? 82  LYS   A CD  1 
ATOM   556  C  CE  . LYS   A 1 69  ? 6.398   -3.536  19.400  1.00 34.45 ? 82  LYS   A CE  1 
ATOM   557  N  NZ  . LYS   A 1 69  ? 6.091   -2.508  20.431  1.00 35.55 ? 82  LYS   A NZ  1 
ATOM   558  N  N   . LEU   A 1 70  ? 6.076   -8.347  15.943  1.00 17.91 ? 83  LEU   A N   1 
ATOM   559  C  CA  . LEU   A 1 70  ? 6.918   -9.075  15.011  1.00 20.14 ? 83  LEU   A CA  1 
ATOM   560  C  C   . LEU   A 1 70  ? 7.721   -8.062  14.203  1.00 21.81 ? 83  LEU   A C   1 
ATOM   561  O  O   . LEU   A 1 70  ? 7.137   -7.145  13.610  1.00 18.48 ? 83  LEU   A O   1 
ATOM   562  C  CB  . LEU   A 1 70  ? 6.005   -9.919  14.096  1.00 18.73 ? 83  LEU   A CB  1 
ATOM   563  C  CG  . LEU   A 1 70  ? 5.442   -11.190 14.747  1.00 24.22 ? 83  LEU   A CG  1 
ATOM   564  C  CD1 . LEU   A 1 70  ? 4.693   -12.078 13.775  1.00 24.18 ? 83  LEU   A CD1 1 
ATOM   565  C  CD2 . LEU   A 1 70  ? 6.571   -12.031 15.340  1.00 30.09 ? 83  LEU   A CD2 1 
ATOM   566  N  N   . GLU   A 1 71  ? 9.007   -8.353  14.059  1.00 22.36 ? 84  GLU   A N   1 
ATOM   567  C  CA  . GLU   A 1 71  ? 9.901   -7.580  13.202  1.00 30.98 ? 84  GLU   A CA  1 
ATOM   568  C  C   . GLU   A 1 71  ? 9.685   -7.876  11.717  1.00 28.24 ? 84  GLU   A C   1 
ATOM   569  O  O   . GLU   A 1 71  ? 9.489   -9.017  11.296  1.00 26.06 ? 84  GLU   A O   1 
ATOM   570  C  CB  . GLU   A 1 71  ? 11.376  -7.863  13.523  1.00 29.06 ? 84  GLU   A CB  1 
ATOM   571  C  CG  . GLU   A 1 71  ? 11.834  -7.309  14.872  1.00 36.77 ? 84  GLU   A CG  1 
ATOM   572  C  CD  . GLU   A 1 71  ? 11.151  -6.038  15.380  1.00 41.85 ? 84  GLU   A CD  1 
ATOM   573  O  OE1 . GLU   A 1 71  ? 11.057  -5.047  14.601  1.00 41.22 ? 84  GLU   A OE1 1 
ATOM   574  O  OE2 . GLU   A 1 71  ? 10.679  -6.039  16.564  1.00 45.17 ? 84  GLU   A OE2 1 
ATOM   575  N  N   . VAL   A 1 72  ? 9.854   -6.853  10.886  1.00 25.02 ? 85  VAL   A N   1 
ATOM   576  C  CA  . VAL   A 1 72  ? 9.827   -7.120  9.468   1.00 25.53 ? 85  VAL   A CA  1 
ATOM   577  C  C   . VAL   A 1 72  ? 11.220  -7.516  8.999   1.00 24.65 ? 85  VAL   A C   1 
ATOM   578  O  O   . VAL   A 1 72  ? 12.181  -6.790  9.250   1.00 24.78 ? 85  VAL   A O   1 
ATOM   579  C  CB  . VAL   A 1 72  ? 9.244   -5.908  8.728   1.00 24.32 ? 85  VAL   A CB  1 
ATOM   580  C  CG1 . VAL   A 1 72  ? 9.662   -5.852  7.269   1.00 21.42 ? 85  VAL   A CG1 1 
ATOM   581  C  CG2 . VAL   A 1 72  ? 7.732   -5.942  8.888   1.00 22.33 ? 85  VAL   A CG2 1 
ATOM   582  N  N   . ILE   A 1 73  ? 11.313  -8.624  8.255   1.00 24.84 ? 86  ILE   A N   1 
ATOM   583  C  CA  . ILE   A 1 73  ? 12.626  -9.029  7.775   1.00 29.14 ? 86  ILE   A CA  1 
ATOM   584  C  C   . ILE   A 1 73  ? 12.849  -8.651  6.322   1.00 29.96 ? 86  ILE   A C   1 
ATOM   585  O  O   . ILE   A 1 73  ? 14.018  -8.619  5.969   1.00 33.52 ? 86  ILE   A O   1 
ATOM   586  C  CB  . ILE   A 1 73  ? 12.994  -10.510 8.005   1.00 29.43 ? 86  ILE   A CB  1 
ATOM   587  C  CG1 . ILE   A 1 73  ? 12.103  -11.488 7.241   1.00 36.06 ? 86  ILE   A CG1 1 
ATOM   588  C  CG2 . ILE   A 1 73  ? 13.032  -10.801 9.479   1.00 35.25 ? 86  ILE   A CG2 1 
ATOM   589  C  CD1 . ILE   A 1 73  ? 12.674  -12.897 7.146   1.00 33.82 ? 86  ILE   A CD1 1 
ATOM   590  N  N   . LYS   A 1 74  ? 11.789  -8.400  5.522   1.00 32.21 ? 87  LYS   A N   1 
ATOM   591  C  CA  . LYS   A 1 74  ? 11.957  -7.945  4.148   1.00 35.53 ? 87  LYS   A CA  1 
ATOM   592  C  C   . LYS   A 1 74  ? 10.778  -7.098  3.658   1.00 30.49 ? 87  LYS   A C   1 
ATOM   593  O  O   . LYS   A 1 74  ? 9.631   -7.489  3.831   1.00 23.80 ? 87  LYS   A O   1 
ATOM   594  C  CB  . LYS   A 1 74  ? 12.098  -9.158  3.219   1.00 37.69 ? 87  LYS   A CB  1 
ATOM   595  C  CG  . LYS   A 1 74  ? 12.453  -8.786  1.791   1.00 46.78 ? 87  LYS   A CG  1 
ATOM   596  C  CD  . LYS   A 1 74  ? 13.509  -9.682  1.154   1.00 52.78 ? 87  LYS   A CD  1 
ATOM   597  C  CE  . LYS   A 1 74  ? 13.673  -9.433  -0.342  1.00 60.69 ? 87  LYS   A CE  1 
ATOM   598  N  NZ  . LYS   A 1 74  ? 13.407  -8.017  -0.721  1.00 61.57 ? 87  LYS   A NZ  1 
ATOM   599  N  N   . GLN   A 1 75  ? 11.079  -5.964  2.998   1.00 26.44 ? 88  GLN   A N   1 
ATOM   600  C  CA  . GLN   A 1 75  ? 10.070  -5.067  2.444   1.00 26.13 ? 88  GLN   A CA  1 
ATOM   601  C  C   . GLN   A 1 75  ? 10.018  -5.242  0.934   1.00 26.38 ? 88  GLN   A C   1 
ATOM   602  O  O   . GLN   A 1 75  ? 11.002  -4.991  0.235   1.00 27.24 ? 88  GLN   A O   1 
ATOM   603  C  CB  . GLN   A 1 75  ? 10.361  -3.594  2.765   1.00 26.08 ? 88  GLN   A CB  1 
ATOM   604  C  CG  . GLN   A 1 75  ? 10.469  -3.277  4.250   1.00 28.36 ? 88  GLN   A CG  1 
ATOM   605  C  CD  . GLN   A 1 75  ? 11.113  -1.955  4.586   1.00 28.25 ? 88  GLN   A CD  1 
ATOM   606  O  OE1 . GLN   A 1 75  ? 10.732  -0.908  4.079   1.00 28.93 ? 88  GLN   A OE1 1 
ATOM   607  N  NE2 . GLN   A 1 75  ? 12.049  -1.960  5.520   1.00 33.07 ? 88  GLN   A NE2 1 
ATOM   608  N  N   . PHE   A 1 76  ? 8.854   -5.620  0.424   1.00 23.63 ? 89  PHE   A N   1 
ATOM   609  C  CA  . PHE   A 1 76  ? 8.671   -5.703  -1.015  1.00 27.49 ? 89  PHE   A CA  1 
ATOM   610  C  C   . PHE   A 1 76  ? 7.827   -4.544  -1.525  1.00 25.77 ? 89  PHE   A C   1 
ATOM   611  O  O   . PHE   A 1 76  ? 6.620   -4.641  -1.607  1.00 24.08 ? 89  PHE   A O   1 
ATOM   612  C  CB  . PHE   A 1 76  ? 7.982   -6.999  -1.417  1.00 27.60 ? 89  PHE   A CB  1 
ATOM   613  C  CG  . PHE   A 1 76  ? 8.744   -8.231  -1.037  1.00 31.64 ? 89  PHE   A CG  1 
ATOM   614  C  CD1 . PHE   A 1 76  ? 8.566   -8.819  0.207   1.00 28.45 ? 89  PHE   A CD1 1 
ATOM   615  C  CD2 . PHE   A 1 76  ? 9.615   -8.823  -1.951  1.00 34.16 ? 89  PHE   A CD2 1 
ATOM   616  C  CE1 . PHE   A 1 76  ? 9.249   -9.980  0.535   1.00 29.01 ? 89  PHE   A CE1 1 
ATOM   617  C  CE2 . PHE   A 1 76  ? 10.292  -9.987  -1.623  1.00 29.67 ? 89  PHE   A CE2 1 
ATOM   618  C  CZ  . PHE   A 1 76  ? 10.101  -10.562 -0.378  1.00 30.15 ? 89  PHE   A CZ  1 
ATOM   619  N  N   . ARG   A 1 77  ? 8.486   -3.432  -1.783  1.00 27.12 ? 90  ARG   A N   1 
ATOM   620  C  CA  . ARG   A 1 77  ? 7.835   -2.276  -2.346  1.00 29.18 ? 90  ARG   A CA  1 
ATOM   621  C  C   . ARG   A 1 77  ? 7.533   -2.545  -3.811  1.00 28.19 ? 90  ARG   A C   1 
ATOM   622  O  O   . ARG   A 1 77  ? 8.254   -3.295  -4.473  1.00 27.83 ? 90  ARG   A O   1 
ATOM   623  C  CB  . ARG   A 1 77  ? 8.713   -1.050  -2.146  1.00 30.89 ? 90  ARG   A CB  1 
ATOM   624  C  CG  . ARG   A 1 77  ? 7.916   0.230   -2.051  1.00 33.07 ? 90  ARG   A CG  1 
ATOM   625  C  CD  . ARG   A 1 77  ? 8.747   1.366   -1.502  1.00 35.48 ? 90  ARG   A CD  1 
ATOM   626  N  NE  . ARG   A 1 77  ? 10.015  1.459   -2.181  1.00 40.78 ? 90  ARG   A NE  1 
ATOM   627  C  CZ  . ARG   A 1 77  ? 10.787  2.533   -2.231  1.00 41.45 ? 90  ARG   A CZ  1 
ATOM   628  N  NH1 . ARG   A 1 77  ? 10.418  3.657   -1.644  1.00 42.09 ? 90  ARG   A NH1 1 
ATOM   629  N  NH2 . ARG   A 1 77  ? 11.934  2.475   -2.882  1.00 44.74 ? 90  ARG   A NH2 1 
ATOM   630  N  N   . HIS   A 1 78  ? 6.391   -2.024  -4.282  1.00 24.99 ? 91  HIS   A N   1 
ATOM   631  C  CA  . HIS   A 1 78  ? 6.056   -2.165  -5.677  1.00 25.79 ? 91  HIS   A CA  1 
ATOM   632  C  C   . HIS   A 1 78  ? 7.165   -1.556  -6.527  1.00 26.23 ? 91  HIS   A C   1 
ATOM   633  O  O   . HIS   A 1 78  ? 7.579   -0.422  -6.290  1.00 24.70 ? 91  HIS   A O   1 
ATOM   634  C  CB  . HIS   A 1 78  ? 4.712   -1.565  -6.053  1.00 27.09 ? 91  HIS   A CB  1 
ATOM   635  C  CG  . HIS   A 1 78  ? 4.274   -2.165  -7.337  1.00 26.92 ? 91  HIS   A CG  1 
ATOM   636  N  ND1 . HIS   A 1 78  ? 4.757   -1.683  -8.526  1.00 28.93 ? 91  HIS   A ND1 1 
ATOM   637  C  CD2 . HIS   A 1 78  ? 3.604   -3.304  -7.613  1.00 25.67 ? 91  HIS   A CD2 1 
ATOM   638  C  CE1 . HIS   A 1 78  ? 4.300   -2.452  -9.490  1.00 28.33 ? 91  HIS   A CE1 1 
ATOM   639  N  NE2 . HIS   A 1 78  ? 3.579   -3.441  -8.957  1.00 28.46 ? 91  HIS   A NE2 1 
ATOM   640  N  N   . PRO   A 1 79  ? 7.725   -2.299  -7.511  1.00 27.05 ? 92  PRO   A N   1 
ATOM   641  C  CA  . PRO   A 1 79  ? 8.912   -1.820  -8.236  1.00 28.03 ? 92  PRO   A CA  1 
ATOM   642  C  C   . PRO   A 1 79  ? 8.685   -0.558  -9.101  1.00 28.69 ? 92  PRO   A C   1 
ATOM   643  O  O   . PRO   A 1 79  ? 9.598   0.181   -9.408  1.00 32.93 ? 92  PRO   A O   1 
ATOM   644  C  CB  . PRO   A 1 79  ? 9.334   -3.052  -9.018  1.00 30.35 ? 92  PRO   A CB  1 
ATOM   645  C  CG  . PRO   A 1 79  ? 7.997   -3.747  -9.275  1.00 31.28 ? 92  PRO   A CG  1 
ATOM   646  C  CD  . PRO   A 1 79  ? 7.242   -3.606  -7.974  1.00 27.32 ? 92  PRO   A CD  1 
ATOM   647  N  N   . LYS   A 1 80  ? 7.444   -0.234  -9.395  1.00 33.47 ? 93  LYS   A N   1 
ATOM   648  C  CA  . LYS   A 1 80  ? 7.055   0.928   -10.170 1.00 31.58 ? 93  LYS   A CA  1 
ATOM   649  C  C   . LYS   A 1 80  ? 6.464   2.004   -9.272  1.00 34.20 ? 93  LYS   A C   1 
ATOM   650  O  O   . LYS   A 1 80  ? 5.795   2.920   -9.754  1.00 26.71 ? 93  LYS   A O   1 
ATOM   651  C  CB  . LYS   A 1 80  ? 5.935   0.488   -11.117 1.00 39.68 ? 93  LYS   A CB  1 
ATOM   652  C  CG  . LYS   A 1 80  ? 6.366   -0.503  -12.191 1.00 52.74 ? 93  LYS   A CG  1 
ATOM   653  C  CD  . LYS   A 1 80  ? 5.209   -1.108  -12.979 1.00 58.54 ? 93  LYS   A CD  1 
ATOM   654  C  CE  . LYS   A 1 80  ? 5.398   -2.593  -13.247 1.00 63.25 ? 93  LYS   A CE  1 
ATOM   655  N  NZ  . LYS   A 1 80  ? 4.576   -3.072  -14.386 1.00 65.33 ? 93  LYS   A NZ  1 
ATOM   656  N  N   . TYR   A 1 81  ? 6.622   1.843   -7.949  1.00 32.17 ? 94  TYR   A N   1 
ATOM   657  C  CA  . TYR   A 1 81  ? 6.185   2.868   -7.024  1.00 27.62 ? 94  TYR   A CA  1 
ATOM   658  C  C   . TYR   A 1 81  ? 6.860   4.185   -7.411  1.00 27.56 ? 94  TYR   A C   1 
ATOM   659  O  O   . TYR   A 1 81  ? 8.022   4.186   -7.769  1.00 30.08 ? 94  TYR   A O   1 
ATOM   660  C  CB  . TYR   A 1 81  ? 6.572   2.492   -5.584  1.00 23.97 ? 94  TYR   A CB  1 
ATOM   661  C  CG  . TYR   A 1 81  ? 6.229   3.560   -4.563  1.00 21.71 ? 94  TYR   A CG  1 
ATOM   662  C  CD1 . TYR   A 1 81  ? 4.961   4.097   -4.521  1.00 23.02 ? 94  TYR   A CD1 1 
ATOM   663  C  CD2 . TYR   A 1 81  ? 7.181   4.100   -3.707  1.00 24.39 ? 94  TYR   A CD2 1 
ATOM   664  C  CE1 . TYR   A 1 81  ? 4.613   5.082   -3.615  1.00 23.55 ? 94  TYR   A CE1 1 
ATOM   665  C  CE2 . TYR   A 1 81  ? 6.841   5.065   -2.766  1.00 25.20 ? 94  TYR   A CE2 1 
ATOM   666  C  CZ  . TYR   A 1 81  ? 5.550   5.563   -2.731  1.00 24.75 ? 94  TYR   A CZ  1 
ATOM   667  O  OH  . TYR   A 1 81  ? 5.152   6.563   -1.893  1.00 24.20 ? 94  TYR   A OH  1 
ATOM   668  N  N   . ASN   A 1 82  ? 6.132   5.293   -7.243  1.00 31.22 ? 95  ASN   A N   1 
ATOM   669  C  CA  . ASN   A 1 82  ? 6.540   6.639   -7.592  1.00 25.50 ? 95  ASN   A CA  1 
ATOM   670  C  C   . ASN   A 1 82  ? 6.237   7.548   -6.419  1.00 28.71 ? 95  ASN   A C   1 
ATOM   671  O  O   . ASN   A 1 82  ? 5.055   7.748   -6.108  1.00 33.27 ? 95  ASN   A O   1 
ATOM   672  C  CB  . ASN   A 1 82  ? 5.751   7.070   -8.818  1.00 31.35 ? 95  ASN   A CB  1 
ATOM   673  C  CG  . ASN   A 1 82  ? 6.165   8.416   -9.361  1.00 29.52 ? 95  ASN   A CG  1 
ATOM   674  O  OD1 . ASN   A 1 82  ? 6.449   9.344   -8.609  1.00 34.96 ? 95  ASN   A OD1 1 
ATOM   675  N  ND2 . ASN   A 1 82  ? 6.199   8.500   -10.671 1.00 29.32 ? 95  ASN   A ND2 1 
ATOM   676  N  N   . THR   A 1 83  ? 7.299   8.111   -5.813  1.00 27.12 ? 96  THR   A N   1 
ATOM   677  C  CA  . THR   A 1 83  ? 7.229   8.819   -4.555  1.00 27.69 ? 96  THR   A CA  1 
ATOM   678  C  C   . THR   A 1 83  ? 6.516   10.146  -4.775  1.00 39.30 ? 96  THR   A C   1 
ATOM   679  O  O   . THR   A 1 83  ? 6.081   10.747  -3.802  1.00 41.06 ? 96  THR   A O   1 
ATOM   680  C  CB  . THR   A 1 83  ? 8.615   9.061   -3.960  0.50 26.70 ? 96  THR   A CB  1 
ATOM   681  O  OG1 . THR   A 1 83  ? 9.377   9.517   -5.079  0.50 25.15 ? 96  THR   A OG1 1 
ATOM   682  C  CG2 . THR   A 1 83  ? 9.227   7.814   -3.356  0.50 26.34 ? 96  THR   A CG2 1 
ATOM   683  N  N   . SER   A 1 84  ? 6.402   10.595  -6.039  1.00 40.02 ? 97  SER   A N   1 
ATOM   684  C  CA  . SER   A 1 84  ? 5.809   11.893  -6.316  1.00 42.56 ? 97  SER   A CA  1 
ATOM   685  C  C   . SER   A 1 84  ? 4.325   11.702  -6.615  1.00 38.11 ? 97  SER   A C   1 
ATOM   686  O  O   . SER   A 1 84  ? 3.519   12.334  -5.945  1.00 33.49 ? 97  SER   A O   1 
ATOM   687  C  CB  . SER   A 1 84  ? 6.557   12.709  -7.413  1.00 35.38 ? 97  SER   A CB  1 
ATOM   688  O  OG  . SER   A 1 84  ? 7.849   13.080  -6.965  0.10 35.07 ? 97  SER   A OG  1 
ATOM   689  N  N   . THR   A 1 85  ? 3.970   10.838  -7.588  1.00 38.50 ? 98  THR   A N   1 
ATOM   690  C  CA  . THR   A 1 85  ? 2.566   10.638  -7.987  1.00 31.94 ? 98  THR   A CA  1 
ATOM   691  C  C   . THR   A 1 85  ? 1.757   9.662   -7.113  1.00 32.55 ? 98  THR   A C   1 
ATOM   692  O  O   . THR   A 1 85  ? 0.540   9.592   -7.242  1.00 27.78 ? 98  THR   A O   1 
ATOM   693  C  CB  . THR   A 1 85  ? 2.486   10.134  -9.426  1.00 31.61 ? 98  THR   A CB  1 
ATOM   694  O  OG1 . THR   A 1 85  ? 3.228   8.930   -9.536  1.00 26.01 ? 98  THR   A OG1 1 
ATOM   695  C  CG2 . THR   A 1 85  ? 3.045   11.134  -10.418 1.00 32.57 ? 98  THR   A CG2 1 
ATOM   696  N  N   . LEU   A 1 86  ? 2.456   8.921   -6.237  1.00 32.83 ? 99  LEU   A N   1 
ATOM   697  C  CA  . LEU   A 1 86  ? 1.971   7.770   -5.487  1.00 33.79 ? 99  LEU   A CA  1 
ATOM   698  C  C   . LEU   A 1 86  ? 1.247   6.741   -6.363  1.00 27.17 ? 99  LEU   A C   1 
ATOM   699  O  O   . LEU   A 1 86  ? 0.475   5.964   -5.841  1.00 27.32 ? 99  LEU   A O   1 
ATOM   700  C  CB  . LEU   A 1 86  ? 1.107   8.230   -4.302  1.00 34.33 ? 99  LEU   A CB  1 
ATOM   701  C  CG  . LEU   A 1 86  ? 1.842   8.937   -3.154  1.00 35.53 ? 99  LEU   A CG  1 
ATOM   702  C  CD1 . LEU   A 1 86  ? 1.261   8.544   -1.818  1.00 38.42 ? 99  LEU   A CD1 1 
ATOM   703  C  CD2 . LEU   A 1 86  ? 3.331   8.665   -3.134  1.00 33.38 ? 99  LEU   A CD2 1 
ATOM   704  N  N   . HIS   A 1 87  ? 1.621   6.585   -7.631  1.00 27.01 ? 100 HIS   A N   1 
ATOM   705  C  CA  . HIS   A 1 87  ? 1.212   5.397   -8.383  1.00 27.64 ? 100 HIS   A CA  1 
ATOM   706  C  C   . HIS   A 1 87  ? 1.827   4.143   -7.756  1.00 22.25 ? 100 HIS   A C   1 
ATOM   707  O  O   . HIS   A 1 87  ? 2.966   4.181   -7.307  1.00 28.68 ? 100 HIS   A O   1 
ATOM   708  C  CB  . HIS   A 1 87  ? 1.545   5.557   -9.878  1.00 25.40 ? 100 HIS   A CB  1 
ATOM   709  C  CG  . HIS   A 1 87  ? 0.547   6.397   -10.605 1.00 27.12 ? 100 HIS   A CG  1 
ATOM   710  N  ND1 . HIS   A 1 87  ? 0.665   6.677   -11.946 1.00 28.44 ? 100 HIS   A ND1 1 
ATOM   711  C  CD2 . HIS   A 1 87  ? -0.560  7.047   -10.175 1.00 28.91 ? 100 HIS   A CD2 1 
ATOM   712  C  CE1 . HIS   A 1 87  ? -0.335  7.461   -12.318 1.00 33.47 ? 100 HIS   A CE1 1 
ATOM   713  N  NE2 . HIS   A 1 87  ? -1.105  7.712   -11.252 1.00 33.95 ? 100 HIS   A NE2 1 
ATOM   714  N  N   . HIS   A 1 88  ? 1.077   3.046   -7.741  1.00 21.86 ? 101 HIS   A N   1 
ATOM   715  C  CA  . HIS   A 1 88  ? 1.546   1.751   -7.239  1.00 24.21 ? 101 HIS   A CA  1 
ATOM   716  C  C   . HIS   A 1 88  ? 1.888   1.843   -5.737  1.00 22.27 ? 101 HIS   A C   1 
ATOM   717  O  O   . HIS   A 1 88  ? 2.849   1.249   -5.252  1.00 23.83 ? 101 HIS   A O   1 
ATOM   718  C  CB  . HIS   A 1 88  ? 2.666   1.194   -8.169  1.00 26.18 ? 101 HIS   A CB  1 
ATOM   719  C  CG  . HIS   A 1 88  ? 2.331   1.349   -9.629  1.00 26.55 ? 101 HIS   A CG  1 
ATOM   720  N  ND1 . HIS   A 1 88  ? 3.122   2.077   -10.530 1.00 27.86 ? 101 HIS   A ND1 1 
ATOM   721  C  CD2 . HIS   A 1 88  ? 1.226   1.019   -10.323 1.00 22.99 ? 101 HIS   A CD2 1 
ATOM   722  C  CE1 . HIS   A 1 88  ? 2.563   2.064   -11.711 1.00 24.36 ? 101 HIS   A CE1 1 
ATOM   723  N  NE2 . HIS   A 1 88  ? 1.424   1.427   -11.606 1.00 27.97 ? 101 HIS   A NE2 1 
ATOM   724  N  N   . ASP   A 1 89  ? 1.046   2.531   -4.960  1.00 20.80 ? 102 ASP   A N   1 
ATOM   725  C  CA  . ASP   A 1 89  ? 1.339   2.715   -3.543  1.00 23.10 ? 102 ASP   A CA  1 
ATOM   726  C  C   . ASP   A 1 89  ? 0.985   1.440   -2.764  1.00 22.20 ? 102 ASP   A C   1 
ATOM   727  O  O   . ASP   A 1 89  ? -0.009  1.403   -2.031  1.00 22.04 ? 102 ASP   A O   1 
ATOM   728  C  CB  . ASP   A 1 89  ? 0.630   3.944   -2.955  1.00 19.59 ? 102 ASP   A CB  1 
ATOM   729  C  CG  . ASP   A 1 89  ? 1.180   4.371   -1.591  1.00 20.12 ? 102 ASP   A CG  1 
ATOM   730  O  OD1 . ASP   A 1 89  ? 2.177   3.833   -1.157  1.00 19.98 ? 102 ASP   A OD1 1 
ATOM   731  O  OD2 . ASP   A 1 89  ? 0.607   5.252   -0.989  1.00 23.70 ? 102 ASP   A OD2 1 
ATOM   732  N  N   . ILE   A 1 90  ? 1.820   0.412   -2.910  1.00 21.07 ? 103 ILE   A N   1 
ATOM   733  C  CA  . ILE   A 1 90  ? 1.555   -0.873  -2.297  1.00 19.49 ? 103 ILE   A CA  1 
ATOM   734  C  C   . ILE   A 1 90  ? 2.885   -1.531  -1.934  1.00 22.88 ? 103 ILE   A C   1 
ATOM   735  O  O   . ILE   A 1 90  ? 3.891   -1.402  -2.655  1.00 22.83 ? 103 ILE   A O   1 
ATOM   736  C  CB  . ILE   A 1 90  ? 0.664   -1.724  -3.222  1.00 18.36 ? 103 ILE   A CB  1 
ATOM   737  C  CG1 . ILE   A 1 90  ? 0.095   -2.941  -2.503  1.00 18.15 ? 103 ILE   A CG1 1 
ATOM   738  C  CG2 . ILE   A 1 90  ? 1.349   -2.158  -4.512  1.00 18.54 ? 103 ILE   A CG2 1 
ATOM   739  C  CD1 . ILE   A 1 90  ? -0.864  -3.739  -3.312  1.00 18.54 ? 103 ILE   A CD1 1 
ATOM   740  N  N   . MET   A 1 91  ? 2.889   -2.216  -0.793  1.00 19.54 ? 104 MET   A N   1 
ATOM   741  C  CA  . MET   A 1 91  ? 4.096   -2.854  -0.302  1.00 19.23 ? 104 MET   A CA  1 
ATOM   742  C  C   . MET   A 1 91  ? 3.693   -4.083  0.501   1.00 17.99 ? 104 MET   A C   1 
ATOM   743  O  O   . MET   A 1 91  ? 2.672   -4.102  1.210   1.00 15.86 ? 104 MET   A O   1 
ATOM   744  C  CB  . MET   A 1 91  ? 4.981   -1.903  0.517   1.00 19.11 ? 104 MET   A CB  1 
ATOM   745  C  CG  . MET   A 1 91  ? 6.138   -2.611  1.217   1.00 19.24 ? 104 MET   A CG  1 
ATOM   746  S  SD  . MET   A 1 91  ? 7.217   -1.478  1.977   1.00 19.49 ? 104 MET   A SD  1 
ATOM   747  C  CE  . MET   A 1 91  ? 6.077   -0.544  3.013   1.00 20.47 ? 104 MET   A CE  1 
ATOM   748  N  N   . LEU   A 1 92  ? 4.427   -5.158  0.274   1.00 17.64 ? 105 LEU   A N   1 
ATOM   749  C  CA  . LEU   A 1 92  ? 4.285   -6.358  1.092   1.00 19.23 ? 105 LEU   A CA  1 
ATOM   750  C  C   . LEU   A 1 92  ? 5.401   -6.397  2.110   1.00 20.32 ? 105 LEU   A C   1 
ATOM   751  O  O   . LEU   A 1 92  ? 6.532   -6.057  1.780   1.00 19.74 ? 105 LEU   A O   1 
ATOM   752  C  CB  . LEU   A 1 92  ? 4.349   -7.603  0.228   1.00 20.13 ? 105 LEU   A CB  1 
ATOM   753  C  CG  . LEU   A 1 92  ? 3.020   -8.009  -0.389  1.00 19.25 ? 105 LEU   A CG  1 
ATOM   754  C  CD1 . LEU   A 1 92  ? 3.273   -8.916  -1.534  1.00 21.22 ? 105 LEU   A CD1 1 
ATOM   755  C  CD2 . LEU   A 1 92  ? 2.092   -8.660  0.613   1.00 18.44 ? 105 LEU   A CD2 1 
ATOM   756  N  N   . LEU   A 1 93  ? 5.076   -6.811  3.348   1.00 21.82 ? 106 LEU   A N   1 
ATOM   757  C  CA  . LEU   A 1 93  ? 6.103   -6.992  4.377   1.00 20.51 ? 106 LEU   A CA  1 
ATOM   758  C  C   . LEU   A 1 93  ? 6.131   -8.453  4.778   1.00 20.70 ? 106 LEU   A C   1 
ATOM   759  O  O   . LEU   A 1 93  ? 5.101   -8.989  5.178   1.00 20.73 ? 106 LEU   A O   1 
ATOM   760  C  CB  . LEU   A 1 93  ? 5.783   -6.135  5.596   1.00 21.38 ? 106 LEU   A CB  1 
ATOM   761  C  CG  . LEU   A 1 93  ? 5.550   -4.654  5.316   1.00 18.92 ? 106 LEU   A CG  1 
ATOM   762  C  CD1 . LEU   A 1 93  ? 5.008   -3.966  6.540   1.00 17.63 ? 106 LEU   A CD1 1 
ATOM   763  C  CD2 . LEU   A 1 93  ? 6.811   -3.963  4.816   1.00 18.79 ? 106 LEU   A CD2 1 
ATOM   764  N  N   . LYS   A 1 94  ? 7.322   -9.070  4.685   1.00 19.45 ? 107 LYS   A N   1 
ATOM   765  C  CA  . LYS   A 1 94  ? 7.554   -10.384 5.225   1.00 20.96 ? 107 LYS   A CA  1 
ATOM   766  C  C   . LYS   A 1 94  ? 7.945   -10.300 6.705   1.00 21.93 ? 107 LYS   A C   1 
ATOM   767  O  O   . LYS   A 1 94  ? 8.925   -9.620  7.069   1.00 21.99 ? 107 LYS   A O   1 
ATOM   768  C  CB  . LYS   A 1 94  ? 8.703   -11.075 4.470   1.00 24.61 ? 107 LYS   A CB  1 
ATOM   769  C  CG  . LYS   A 1 94  ? 8.848   -12.563 4.810   1.00 24.20 ? 107 LYS   A CG  1 
ATOM   770  C  CD  . LYS   A 1 94  ? 9.786   -13.394 3.953   1.00 25.38 ? 107 LYS   A CD  1 
ATOM   771  C  CE  . LYS   A 1 94  ? 9.646   -14.866 4.308   1.00 27.10 ? 107 LYS   A CE  1 
ATOM   772  N  NZ  . LYS   A 1 94  ? 10.238  -15.727 3.256   1.00 30.94 ? 107 LYS   A NZ  1 
ATOM   773  N  N   . LEU   A 1 95  ? 7.264   -11.095 7.545   1.00 20.26 ? 108 LEU   A N   1 
ATOM   774  C  CA  . LEU   A 1 95  ? 7.548   -11.095 8.978   1.00 21.13 ? 108 LEU   A CA  1 
ATOM   775  C  C   . LEU   A 1 95  ? 8.591   -12.158 9.346   1.00 23.98 ? 108 LEU   A C   1 
ATOM   776  O  O   . LEU   A 1 95  ? 8.710   -13.199 8.710   1.00 24.16 ? 108 LEU   A O   1 
ATOM   777  C  CB  . LEU   A 1 95  ? 6.262   -11.359 9.773   1.00 22.31 ? 108 LEU   A CB  1 
ATOM   778  C  CG  . LEU   A 1 95  ? 5.073   -10.460 9.432   1.00 24.86 ? 108 LEU   A CG  1 
ATOM   779  C  CD1 . LEU   A 1 95  ? 3.869   -10.790 10.344  1.00 23.84 ? 108 LEU   A CD1 1 
ATOM   780  C  CD2 . LEU   A 1 95  ? 5.449   -8.980  9.506   1.00 24.73 ? 108 LEU   A CD2 1 
ATOM   781  N  N   . LYS   A 1 96  ? 9.250   -11.950 10.479  1.00 28.02 ? 109 LYS   A N   1 
ATOM   782  C  CA  . LYS   A 1 96  ? 10.391  -12.759 10.844  1.00 31.07 ? 109 LYS   A CA  1 
ATOM   783  C  C   . LYS   A 1 96  ? 9.919   -14.156 11.180  1.00 30.35 ? 109 LYS   A C   1 
ATOM   784  O  O   . LYS   A 1 96  ? 10.615  -15.113 10.929  1.00 38.35 ? 109 LYS   A O   1 
ATOM   785  C  CB  . LYS   A 1 96  ? 11.177  -12.179 12.020  1.00 35.11 ? 109 LYS   A CB  1 
ATOM   786  C  CG  . LYS   A 1 96  ? 12.346  -13.059 12.451  1.00 40.36 ? 109 LYS   A CG  1 
ATOM   787  C  CD  . LYS   A 1 96  ? 13.440  -12.324 13.154  1.00 43.16 ? 109 LYS   A CD  1 
ATOM   788  C  CE  . LYS   A 1 96  ? 14.121  -13.201 14.171  1.00 48.79 ? 109 LYS   A CE  1 
ATOM   789  N  NZ  . LYS   A 1 96  ? 15.294  -12.480 14.724  1.00 58.44 ? 109 LYS   A NZ  1 
ATOM   790  N  N   . GLU   A 1 97  ? 8.738   -14.278 11.743  1.00 35.34 ? 110 GLU   A N   1 
ATOM   791  C  CA  . GLU   A 1 97  ? 8.121   -15.587 11.836  1.00 38.25 ? 110 GLU   A CA  1 
ATOM   792  C  C   . GLU   A 1 97  ? 6.640   -15.440 11.562  1.00 29.07 ? 110 GLU   A C   1 
ATOM   793  O  O   . GLU   A 1 97  ? 6.153   -14.317 11.410  1.00 28.25 ? 110 GLU   A O   1 
ATOM   794  C  CB  . GLU   A 1 97  ? 8.375   -16.239 13.192  1.00 45.53 ? 110 GLU   A CB  1 
ATOM   795  C  CG  . GLU   A 1 97  ? 8.123   -15.346 14.374  1.00 46.61 ? 110 GLU   A CG  1 
ATOM   796  C  CD  . GLU   A 1 97  ? 9.249   -15.551 15.355  1.00 56.00 ? 110 GLU   A CD  1 
ATOM   797  O  OE1 . GLU   A 1 97  ? 10.013  -16.525 15.120  1.00 59.99 ? 110 GLU   A OE1 1 
ATOM   798  O  OE2 . GLU   A 1 97  ? 9.414   -14.711 16.282  1.00 63.37 ? 110 GLU   A OE2 1 
ATOM   799  N  N   . LYS   A 1 98  ? 5.970   -16.594 11.555  1.00 24.97 ? 111 LYS   A N   1 
ATOM   800  C  CA  . LYS   A 1 98  ? 4.554   -16.679 11.279  1.00 24.13 ? 111 LYS   A CA  1 
ATOM   801  C  C   . LYS   A 1 98  ? 3.770   -16.306 12.527  1.00 25.78 ? 111 LYS   A C   1 
ATOM   802  O  O   . LYS   A 1 98  ? 4.049   -16.790 13.616  1.00 25.34 ? 111 LYS   A O   1 
ATOM   803  C  CB  . LYS   A 1 98  ? 4.201   -18.084 10.821  1.00 23.46 ? 111 LYS   A CB  1 
ATOM   804  C  CG  . LYS   A 1 98  ? 4.787   -18.426 9.466   1.00 26.48 ? 111 LYS   A CG  1 
ATOM   805  C  CD  . LYS   A 1 98  ? 4.572   -19.845 8.988   1.00 31.81 ? 111 LYS   A CD  1 
ATOM   806  C  CE  . LYS   A 1 98  ? 4.987   -20.002 7.534   1.00 38.28 ? 111 LYS   A CE  1 
ATOM   807  N  NZ  . LYS   A 1 98  ? 4.224   -21.088 6.858   1.00 46.04 ? 111 LYS   A NZ  1 
ATOM   808  N  N   . ALA   A 1 99  ? 2.775   -15.455 12.337  1.00 22.02 ? 112 ALA   A N   1 
ATOM   809  C  CA  . ALA   A 1 99  ? 1.837   -15.132 13.393  1.00 25.38 ? 112 ALA   A CA  1 
ATOM   810  C  C   . ALA   A 1 99  ? 1.061   -16.389 13.766  1.00 28.52 ? 112 ALA   A C   1 
ATOM   811  O  O   . ALA   A 1 99  ? 0.766   -17.185 12.872  1.00 32.38 ? 112 ALA   A O   1 
ATOM   812  C  CB  . ALA   A 1 99  ? 0.887   -14.074 12.919  1.00 27.33 ? 112 ALA   A CB  1 
ATOM   813  N  N   . SER   A 1 100 ? 0.738   -16.544 15.064  1.00 26.46 ? 113 SER   A N   1 
ATOM   814  C  CA  . SER   A 1 100 ? -0.180  -17.577 15.530  1.00 24.76 ? 113 SER   A CA  1 
ATOM   815  C  C   . SER   A 1 100 ? -1.612  -17.107 15.268  1.00 24.84 ? 113 SER   A C   1 
ATOM   816  O  O   . SER   A 1 100 ? -2.010  -16.036 15.714  1.00 23.25 ? 113 SER   A O   1 
ATOM   817  C  CB  . SER   A 1 100 ? 0.000   -17.877 17.003  1.00 25.47 ? 113 SER   A CB  1 
ATOM   818  O  OG  . SER   A 1 100 ? 1.338   -18.221 17.347  1.00 25.57 ? 113 SER   A OG  1 
ATOM   819  N  N   . LEU   A 1 101 ? -2.407  -17.885 14.544  1.00 26.17 ? 114 LEU   A N   1 
ATOM   820  C  CA  . LEU   A 1 101 ? -3.807  -17.513 14.355  1.00 28.21 ? 114 LEU   A CA  1 
ATOM   821  C  C   . LEU   A 1 101 ? -4.567  -17.725 15.658  1.00 30.29 ? 114 LEU   A C   1 
ATOM   822  O  O   . LEU   A 1 101 ? -4.456  -18.793 16.242  1.00 32.75 ? 114 LEU   A O   1 
ATOM   823  C  CB  . LEU   A 1 101 ? -4.432  -18.359 13.249  1.00 28.51 ? 114 LEU   A CB  1 
ATOM   824  C  CG  . LEU   A 1 101 ? -3.697  -18.316 11.909  1.00 32.14 ? 114 LEU   A CG  1 
ATOM   825  C  CD1 . LEU   A 1 101 ? -4.429  -19.167 10.863  1.00 32.53 ? 114 LEU   A CD1 1 
ATOM   826  C  CD2 . LEU   A 1 101 ? -3.477  -16.878 11.430  1.00 30.89 ? 114 LEU   A CD2 1 
ATOM   827  N  N   . THR   A 1 102 ? -5.274  -16.682 16.114  1.00 28.19 ? 115 THR   A N   1 
ATOM   828  C  CA  . THR   A 1 102 ? -6.023  -16.660 17.357  1.00 21.60 ? 115 THR   A CA  1 
ATOM   829  C  C   . THR   A 1 102 ? -7.298  -15.924 17.040  1.00 19.72 ? 115 THR   A C   1 
ATOM   830  O  O   . THR   A 1 102 ? -7.399  -15.340 15.985  1.00 21.08 ? 115 THR   A O   1 
ATOM   831  C  CB  . THR   A 1 102 ? -5.308  -15.900 18.476  1.00 23.52 ? 115 THR   A CB  1 
ATOM   832  O  OG1 . THR   A 1 102 ? -5.182  -14.533 18.070  1.00 18.60 ? 115 THR   A OG1 1 
ATOM   833  C  CG2 . THR   A 1 102 ? -3.949  -16.506 18.816  1.00 26.08 ? 115 THR   A CG2 1 
ATOM   834  N  N   . LEU   A 1 103 ? -8.222  -15.848 17.977  1.00 21.61 ? 116 LEU   A N   1 
ATOM   835  C  CA  . LEU   A 1 103 ? -9.410  -15.054 17.754  1.00 22.36 ? 116 LEU   A CA  1 
ATOM   836  C  C   . LEU   A 1 103 ? -9.026  -13.619 17.366  1.00 21.54 ? 116 LEU   A C   1 
ATOM   837  O  O   . LEU   A 1 103 ? -9.740  -12.997 16.581  1.00 18.98 ? 116 LEU   A O   1 
ATOM   838  C  CB  . LEU   A 1 103 ? -10.260 -15.088 19.031  1.00 24.38 ? 116 LEU   A CB  1 
ATOM   839  C  CG  . LEU   A 1 103 ? -11.580 -14.301 18.992  1.00 28.03 ? 116 LEU   A CG  1 
ATOM   840  C  CD1 . LEU   A 1 103 ? -12.473 -14.830 17.879  1.00 29.38 ? 116 LEU   A CD1 1 
ATOM   841  C  CD2 . LEU   A 1 103 ? -12.316 -14.359 20.341  1.00 32.42 ? 116 LEU   A CD2 1 
ATOM   842  N  N   . ALA   A 1 104 ? -7.955  -13.083 17.987  1.00 18.92 ? 117 ALA   A N   1 
ATOM   843  C  CA  . ALA   A 1 104 ? -7.598  -11.684 17.887  1.00 19.50 ? 117 ALA   A CA  1 
ATOM   844  C  C   . ALA   A 1 104 ? -6.681  -11.391 16.698  1.00 18.21 ? 117 ALA   A C   1 
ATOM   845  O  O   . ALA   A 1 104 ? -6.525  -10.224 16.366  1.00 18.41 ? 117 ALA   A O   1 
ATOM   846  C  CB  . ALA   A 1 104 ? -6.959  -11.205 19.185  1.00 19.02 ? 117 ALA   A CB  1 
ATOM   847  N  N   . VAL   A 1 105 ? -6.055  -12.439 16.143  1.00 18.52 ? 118 VAL   A N   1 
ATOM   848  C  CA  . VAL   A 1 105 ? -5.073  -12.354 15.076  1.00 17.16 ? 118 VAL   A CA  1 
ATOM   849  C  C   . VAL   A 1 105 ? -5.460  -13.370 14.023  1.00 17.13 ? 118 VAL   A C   1 
ATOM   850  O  O   . VAL   A 1 105 ? -5.354  -14.567 14.273  1.00 18.23 ? 118 VAL   A O   1 
ATOM   851  C  CB  . VAL   A 1 105 ? -3.648  -12.659 15.573  1.00 15.82 ? 118 VAL   A CB  1 
ATOM   852  C  CG1 . VAL   A 1 105 ? -2.694  -12.672 14.411  1.00 15.55 ? 118 VAL   A CG1 1 
ATOM   853  C  CG2 . VAL   A 1 105 ? -3.246  -11.645 16.628  1.00 15.96 ? 118 VAL   A CG2 1 
ATOM   854  N  N   . GLY   A 1 106 ? -5.935  -12.860 12.890  1.00 20.62 ? 119 GLY   A N   1 
ATOM   855  C  CA  . GLY   A 1 106 ? -6.313  -13.660 11.743  1.00 21.02 ? 119 GLY   A CA  1 
ATOM   856  C  C   . GLY   A 1 106 ? -5.864  -13.006 10.455  1.00 21.66 ? 119 GLY   A C   1 
ATOM   857  O  O   . GLY   A 1 106 ? -5.564  -11.805 10.451  1.00 24.91 ? 119 GLY   A O   1 
ATOM   858  N  N   . THR   A 1 107 ? -5.832  -13.804 9.379   1.00 22.80 ? 120 THR   A N   1 
ATOM   859  C  CA  . THR   A 1 107 ? -5.545  -13.291 8.059   1.00 22.98 ? 120 THR   A CA  1 
ATOM   860  C  C   . THR   A 1 107 ? -6.816  -12.782 7.381   1.00 22.21 ? 120 THR   A C   1 
ATOM   861  O  O   . THR   A 1 107 ? -7.903  -13.170 7.743   1.00 21.13 ? 120 THR   A O   1 
ATOM   862  C  CB  . THR   A 1 107 ? -4.870  -14.331 7.193   1.00 22.50 ? 120 THR   A CB  1 
ATOM   863  O  OG1 . THR   A 1 107 ? -5.937  -15.227 6.909   1.00 24.33 ? 120 THR   A OG1 1 
ATOM   864  C  CG2 . THR   A 1 107 ? -3.687  -14.962 7.874   1.00 25.03 ? 120 THR   A CG2 1 
ATOM   865  N  N   . LEU   A 1 108 ? -6.662  -11.857 6.430   1.00 22.51 ? 121 LEU   A N   1 
ATOM   866  C  CA  . LEU   A 1 108 ? -7.791  -11.298 5.684   1.00 28.54 ? 121 LEU   A CA  1 
ATOM   867  C  C   . LEU   A 1 108 ? -7.824  -11.901 4.274   1.00 28.22 ? 121 LEU   A C   1 
ATOM   868  O  O   . LEU   A 1 108 ? -6.869  -11.740 3.503   1.00 25.14 ? 121 LEU   A O   1 
ATOM   869  C  CB  . LEU   A 1 108 ? -7.708  -9.766  5.607   1.00 26.93 ? 121 LEU   A CB  1 
ATOM   870  C  CG  . LEU   A 1 108 ? -8.859  -9.087  4.820   1.00 32.26 ? 121 LEU   A CG  1 
ATOM   871  C  CD1 . LEU   A 1 108 ? -10.224 -9.365  5.449   1.00 35.72 ? 121 LEU   A CD1 1 
ATOM   872  C  CD2 . LEU   A 1 108 ? -8.668  -7.577  4.698   1.00 31.05 ? 121 LEU   A CD2 1 
ATOM   873  N  N   . PRO   A 1 109 ? -8.935  -12.583 3.900   1.00 41.19 ? 122 PRO   A N   1 
ATOM   874  C  CA  . PRO   A 1 109 ? -9.200  -13.014 2.515   1.00 44.84 ? 122 PRO   A CA  1 
ATOM   875  C  C   . PRO   A 1 109 ? -9.308  -11.961 1.393   1.00 49.21 ? 122 PRO   A C   1 
ATOM   876  O  O   . PRO   A 1 109 ? -9.570  -10.759 1.591   1.00 40.00 ? 122 PRO   A O   1 
ATOM   877  C  CB  . PRO   A 1 109 ? -10.565 -13.710 2.618   1.00 39.70 ? 122 PRO   A CB  1 
ATOM   878  C  CG  . PRO   A 1 109 ? -10.700 -14.116 4.063   1.00 39.20 ? 122 PRO   A CG  1 
ATOM   879  C  CD  . PRO   A 1 109 ? -9.967  -13.065 4.842   1.00 44.27 ? 122 PRO   A CD  1 
ATOM   880  N  N   . PHE   A 1 110 ? -9.186  -12.499 0.166   1.00 65.43 ? 123 PHE   A N   1 
ATOM   881  C  CA  . PHE   A 1 110 ? -9.429  -11.801 -1.088  1.00 60.14 ? 123 PHE   A CA  1 
ATOM   882  C  C   . PHE   A 1 110 ? -10.731 -12.305 -1.730  1.00 65.33 ? 123 PHE   A C   1 
ATOM   883  O  O   . PHE   A 1 110 ? -11.091 -11.735 -2.788  1.00 61.21 ? 123 PHE   A O   1 
ATOM   884  C  CB  . PHE   A 1 110 ? -8.252  -12.033 -2.032  1.00 52.24 ? 123 PHE   A CB  1 
ATOM   885  C  CG  . PHE   A 1 110 ? -7.002  -11.243 -1.720  1.00 53.31 ? 123 PHE   A CG  1 
ATOM   886  C  CD1 . PHE   A 1 110 ? -5.757  -11.851 -1.770  1.00 58.78 ? 123 PHE   A CD1 1 
ATOM   887  C  CD2 . PHE   A 1 110 ? -7.060  -9.888  -1.435  1.00 48.14 ? 123 PHE   A CD2 1 
ATOM   888  C  CE1 . PHE   A 1 110 ? -4.601  -11.131 -1.528  1.00 57.24 ? 123 PHE   A CE1 1 
ATOM   889  C  CE2 . PHE   A 1 110 ? -5.905  -9.172  -1.192  1.00 56.16 ? 123 PHE   A CE2 1 
ATOM   890  C  CZ  . PHE   A 1 110 ? -4.678  -9.791  -1.234  1.00 58.82 ? 123 PHE   A CZ  1 
ATOM   891  N  N   . VAL   A 1 117 ? -13.857 -9.262  -9.646  0.50 52.26 ? 130 VAL   A N   1 
ATOM   892  C  CA  . VAL   A 1 117 ? -14.975 -9.365  -8.663  0.50 60.79 ? 130 VAL   A CA  1 
ATOM   893  C  C   . VAL   A 1 117 ? -15.291 -7.966  -8.113  1.00 74.20 ? 130 VAL   A C   1 
ATOM   894  O  O   . VAL   A 1 117 ? -14.707 -7.531  -7.119  1.00 69.95 ? 130 VAL   A O   1 
ATOM   895  C  CB  . VAL   A 1 117 ? -14.607 -10.400 -7.583  0.50 56.29 ? 130 VAL   A CB  1 
ATOM   896  C  CG1 . VAL   A 1 117 ? -15.699 -10.552 -6.538  0.50 53.05 ? 130 VAL   A CG1 1 
ATOM   897  C  CG2 . VAL   A 1 117 ? -14.263 -11.747 -8.214  0.50 50.24 ? 130 VAL   A CG2 1 
ATOM   898  N  N   . PRO   A 1 118 ? -16.258 -7.230  -8.728  1.00 86.48 ? 131 PRO   A N   1 
ATOM   899  C  CA  . PRO   A 1 118 ? -16.287 -5.765  -8.686  1.00 89.66 ? 131 PRO   A CA  1 
ATOM   900  C  C   . PRO   A 1 118 ? -17.084 -5.149  -7.525  1.00 89.87 ? 131 PRO   A C   1 
ATOM   901  O  O   . PRO   A 1 118 ? -18.213 -5.554  -7.251  1.00 94.46 ? 131 PRO   A O   1 
ATOM   902  C  CB  . PRO   A 1 118 ? -16.899 -5.416  -10.046 1.00 85.71 ? 131 PRO   A CB  1 
ATOM   903  C  CG  . PRO   A 1 118 ? -17.852 -6.578  -10.315 1.00 87.59 ? 131 PRO   A CG  1 
ATOM   904  C  CD  . PRO   A 1 118 ? -17.386 -7.772  -9.508  1.00 86.15 ? 131 PRO   A CD  1 
ATOM   905  N  N   . PRO   A 1 119 ? -16.563 -4.093  -6.848  1.00 73.57 ? 132 PRO   A N   1 
ATOM   906  C  CA  . PRO   A 1 119 ? -17.070 -3.698  -5.534  1.00 66.44 ? 132 PRO   A CA  1 
ATOM   907  C  C   . PRO   A 1 119 ? -18.416 -2.973  -5.563  1.00 56.45 ? 132 PRO   A C   1 
ATOM   908  O  O   . PRO   A 1 119 ? -18.731 -2.335  -6.565  1.00 57.78 ? 132 PRO   A O   1 
ATOM   909  C  CB  . PRO   A 1 119 ? -15.973 -2.763  -5.008  1.00 72.46 ? 132 PRO   A CB  1 
ATOM   910  C  CG  . PRO   A 1 119 ? -14.884 -2.658  -6.088  1.00 72.28 ? 132 PRO   A CG  1 
ATOM   911  C  CD  . PRO   A 1 119 ? -15.481 -3.215  -7.338  1.00 73.60 ? 132 PRO   A CD  1 
ATOM   912  N  N   . GLY   A 1 120 ? -19.168 -3.032  -4.447  1.00 45.01 ? 133 GLY   A N   1 
ATOM   913  C  CA  . GLY   A 1 120 ? -20.365 -2.220  -4.230  1.00 41.76 ? 133 GLY   A CA  1 
ATOM   914  C  C   . GLY   A 1 120 ? -20.008 -0.844  -3.654  1.00 32.99 ? 133 GLY   A C   1 
ATOM   915  O  O   . GLY   A 1 120 ? -18.830 -0.481  -3.686  1.00 40.48 ? 133 GLY   A O   1 
ATOM   916  N  N   . ARG   A 1 121 ? -20.979 -0.130  -3.053  1.00 29.17 ? 134 ARG   A N   1 
ATOM   917  C  CA  . ARG   A 1 121 ? -20.825 1.281   -2.677  1.00 30.70 ? 134 ARG   A CA  1 
ATOM   918  C  C   . ARG   A 1 121 ? -20.370 1.482   -1.225  1.00 33.06 ? 134 ARG   A C   1 
ATOM   919  O  O   . ARG   A 1 121 ? -19.637 2.425   -0.919  1.00 40.72 ? 134 ARG   A O   1 
ATOM   920  C  CB  . ARG   A 1 121 ? -22.102 2.098   -2.962  1.00 29.36 ? 134 ARG   A CB  1 
ATOM   921  C  CG  . ARG   A 1 121 ? -22.323 2.388   -4.449  1.00 30.18 ? 134 ARG   A CG  1 
ATOM   922  C  CD  . ARG   A 1 121 ? -21.284 3.304   -5.125  1.00 28.21 ? 134 ARG   A CD  1 
ATOM   923  N  NE  . ARG   A 1 121 ? -21.573 3.516   -6.538  1.00 26.13 ? 134 ARG   A NE  1 
ATOM   924  C  CZ  . ARG   A 1 121 ? -20.959 4.377   -7.337  1.00 24.61 ? 134 ARG   A CZ  1 
ATOM   925  N  NH1 . ARG   A 1 121 ? -19.951 5.102   -6.912  1.00 21.56 ? 134 ARG   A NH1 1 
ATOM   926  N  NH2 . ARG   A 1 121 ? -21.329 4.499   -8.599  1.00 25.65 ? 134 ARG   A NH2 1 
ATOM   927  N  N   . MET   A 1 122 ? -20.830 0.669   -0.282  1.00 36.33 ? 135 MET   A N   1 
ATOM   928  C  CA  . MET   A 1 122 ? -20.568 1.031   1.101   1.00 37.15 ? 135 MET   A CA  1 
ATOM   929  C  C   . MET   A 1 122 ? -19.422 0.161   1.622   1.00 33.04 ? 135 MET   A C   1 
ATOM   930  O  O   . MET   A 1 122 ? -19.431 -1.052  1.499   1.00 30.29 ? 135 MET   A O   1 
ATOM   931  C  CB  . MET   A 1 122 ? -21.852 0.953   1.927   1.00 43.37 ? 135 MET   A CB  1 
ATOM   932  C  CG  . MET   A 1 122 ? -22.891 2.059   1.533   1.00 52.63 ? 135 MET   A CG  1 
ATOM   933  S  SD  . MET   A 1 122 ? -22.338 3.867   1.473   1.00 58.37 ? 135 MET   A SD  1 
ATOM   934  C  CE  . MET   A 1 122 ? -21.567 4.071   3.087   1.00 50.04 ? 135 MET   A CE  1 
ATOM   935  N  N   . CYS   A 1 123 ? -18.357 0.831   2.060   1.00 28.93 ? 136 CYS   A N   1 
ATOM   936  C  CA  . CYS   A 1 123 ? -17.098 0.175   2.365   1.00 28.46 ? 136 CYS   A CA  1 
ATOM   937  C  C   . CYS   A 1 123 ? -16.686 0.641   3.759   1.00 22.47 ? 136 CYS   A C   1 
ATOM   938  O  O   . CYS   A 1 123 ? -17.384 1.411   4.360   1.00 19.10 ? 136 CYS   A O   1 
ATOM   939  C  CB  . CYS   A 1 123 ? -16.030 0.491   1.316   1.00 27.33 ? 136 CYS   A CB  1 
ATOM   940  S  SG  . CYS   A 1 123 ? -16.446 -0.092  -0.355  1.00 25.68 ? 136 CYS   A SG  1 
ATOM   941  N  N   . ARG   A 1 124 ? -15.653 0.049   4.329   1.00 21.65 ? 137 ARG   A N   1 
ATOM   942  C  CA  . ARG   A 1 124 ? -15.292 0.327   5.701   1.00 20.29 ? 137 ARG   A CA  1 
ATOM   943  C  C   . ARG   A 1 124 ? -13.772 0.292   5.764   1.00 17.28 ? 137 ARG   A C   1 
ATOM   944  O  O   . ARG   A 1 124 ? -13.153 -0.571  5.106   1.00 12.70 ? 137 ARG   A O   1 
ATOM   945  C  CB  . ARG   A 1 124 ? -15.972 -0.697  6.625   1.00 23.20 ? 137 ARG   A CB  1 
ATOM   946  C  CG  . ARG   A 1 124 ? -15.351 -0.790  8.014   1.00 31.22 ? 137 ARG   A CG  1 
ATOM   947  C  CD  . ARG   A 1 124 ? -15.948 -1.815  8.991   1.00 33.79 ? 137 ARG   A CD  1 
ATOM   948  N  NE  . ARG   A 1 124 ? -17.322 -1.413  9.215   0.50 32.66 ? 137 ARG   A NE  1 
ATOM   949  C  CZ  . ARG   A 1 124 ? -18.373 -2.186  9.106   0.50 28.51 ? 137 ARG   A CZ  1 
ATOM   950  N  NH1 . ARG   A 1 124 ? -18.243 -3.476  8.846   0.50 27.44 ? 137 ARG   A NH1 1 
ATOM   951  N  NH2 . ARG   A 1 124 ? -19.557 -1.648  9.313   0.50 29.72 ? 137 ARG   A NH2 1 
ATOM   952  N  N   . VAL   A 1 125 ? -13.221 1.283   6.487   1.00 16.38 ? 138 VAL   A N   1 
ATOM   953  C  CA  . VAL   A 1 125 ? -11.798 1.329   6.765   1.00 16.56 ? 138 VAL   A CA  1 
ATOM   954  C  C   . VAL   A 1 125 ? -11.569 1.583   8.252   1.00 15.62 ? 138 VAL   A C   1 
ATOM   955  O  O   . VAL   A 1 125 ? -12.370 2.228   8.902   1.00 14.94 ? 138 VAL   A O   1 
ATOM   956  C  CB  . VAL   A 1 125 ? -11.072 2.342   5.854   1.00 17.29 ? 138 VAL   A CB  1 
ATOM   957  C  CG1 . VAL   A 1 125 ? -11.603 3.733   5.984   1.00 17.65 ? 138 VAL   A CG1 1 
ATOM   958  C  CG2 . VAL   A 1 125 ? -9.563  2.336   6.048   1.00 18.67 ? 138 VAL   A CG2 1 
ATOM   959  N  N   . ALA   A 1 126 ? -10.449 1.050   8.775   1.00 15.12 ? 139 ALA   A N   1 
ATOM   960  C  CA  . ALA   A 1 126 ? -10.091 1.122   10.166  1.00 13.40 ? 139 ALA   A CA  1 
ATOM   961  C  C   . ALA   A 1 126 ? -8.622  1.534   10.306  1.00 13.33 ? 139 ALA   A C   1 
ATOM   962  O  O   . ALA   A 1 126 ? -7.832  1.403   9.378   1.00 13.57 ? 139 ALA   A O   1 
ATOM   963  C  CB  . ALA   A 1 126 ? -10.363 -0.208  10.808  1.00 14.15 ? 139 ALA   A CB  1 
ATOM   964  N  N   . GLY   A 1 127 ? -8.303  2.195   11.405  1.00 11.52 ? 140 GLY   A N   1 
ATOM   965  C  CA  . GLY   A 1 127 ? -6.930  2.573   11.647  1.00 11.90 ? 140 GLY   A CA  1 
ATOM   966  C  C   . GLY   A 1 127 ? -6.762  3.375   12.926  1.00 11.73 ? 140 GLY   A C   1 
ATOM   967  O  O   . GLY   A 1 127 ? -7.739  3.676   13.613  1.00 11.21 ? 140 GLY   A O   1 
ATOM   968  N  N   . TRP   A 1 128 ? -5.495  3.661   13.238  1.00 12.95 ? 141 TRP   A N   1 
ATOM   969  C  CA  . TRP   A 1 128 ? -5.178  4.387   14.471  1.00 13.59 ? 141 TRP   A CA  1 
ATOM   970  C  C   . TRP   A 1 128 ? -4.722  5.814   14.170  1.00 14.46 ? 141 TRP   A C   1 
ATOM   971  O  O   . TRP   A 1 128 ? -4.011  6.444   14.969  1.00 14.91 ? 141 TRP   A O   1 
ATOM   972  C  CB  . TRP   A 1 128 ? -4.101  3.624   15.230  1.00 13.38 ? 141 TRP   A CB  1 
ATOM   973  C  CG  . TRP   A 1 128 ? -4.491  2.297   15.790  1.00 13.00 ? 141 TRP   A CG  1 
ATOM   974  C  CD1 . TRP   A 1 128 ? -4.901  2.041   17.052  1.00 14.37 ? 141 TRP   A CD1 1 
ATOM   975  C  CD2 . TRP   A 1 128 ? -4.348  1.019   15.156  1.00 13.99 ? 141 TRP   A CD2 1 
ATOM   976  N  NE1 . TRP   A 1 128 ? -5.078  0.704   17.234  1.00 16.23 ? 141 TRP   A NE1 1 
ATOM   977  C  CE2 . TRP   A 1 128 ? -4.722  0.050   16.093  1.00 15.30 ? 141 TRP   A CE2 1 
ATOM   978  C  CE3 . TRP   A 1 128 ? -3.940  0.602   13.894  1.00 12.89 ? 141 TRP   A CE3 1 
ATOM   979  C  CZ2 . TRP   A 1 128 ? -4.710  -1.310  15.802  1.00 16.24 ? 141 TRP   A CZ2 1 
ATOM   980  C  CZ3 . TRP   A 1 128 ? -3.984  -0.727  13.591  1.00 14.87 ? 141 TRP   A CZ3 1 
ATOM   981  C  CH2 . TRP   A 1 128 ? -4.344  -1.681  14.534  1.00 14.01 ? 141 TRP   A CH2 1 
ATOM   982  N  N   . GLY   A 1 129 ? -5.130  6.325   13.003  1.00 14.36 ? 142 GLY   A N   1 
ATOM   983  C  CA  . GLY   A 1 129 ? -4.645  7.611   12.537  1.00 13.27 ? 142 GLY   A CA  1 
ATOM   984  C  C   . GLY   A 1 129 ? -5.390  8.716   13.252  1.00 14.05 ? 142 GLY   A C   1 
ATOM   985  O  O   . GLY   A 1 129 ? -6.186  8.483   14.178  1.00 15.25 ? 142 GLY   A O   1 
ATOM   986  N  N   . ARG   A 1 130 ? -5.138  9.909   12.771  1.00 14.05 ? 143 ARG   A N   1 
ATOM   987  C  CA  . ARG   A 1 130 ? -5.668  11.123  13.333  1.00 16.16 ? 143 ARG   A CA  1 
ATOM   988  C  C   . ARG   A 1 130 ? -7.173  11.179  13.153  1.00 15.67 ? 143 ARG   A C   1 
ATOM   989  O  O   . ARG   A 1 130 ? -7.716  10.599  12.215  1.00 16.55 ? 143 ARG   A O   1 
ATOM   990  C  CB  . ARG   A 1 130 ? -5.100  12.345  12.625  1.00 18.05 ? 143 ARG   A CB  1 
ATOM   991  C  CG  . ARG   A 1 130 ? -3.604  12.507  12.792  1.00 22.33 ? 143 ARG   A CG  1 
ATOM   992  C  CD  . ARG   A 1 130 ? -3.131  13.924  12.437  1.00 24.23 ? 143 ARG   A CD  1 
ATOM   993  N  NE  . ARG   A 1 130 ? -1.764  13.789  12.004  1.00 27.25 ? 143 ARG   A NE  1 
ATOM   994  C  CZ  . ARG   A 1 130 ? -0.844  14.739  11.995  1.00 36.12 ? 143 ARG   A CZ  1 
ATOM   995  N  NH1 . ARG   A 1 130 ? -1.086  15.926  12.521  1.00 28.80 ? 143 ARG   A NH1 1 
ATOM   996  N  NH2 . ARG   A 1 130 ? 0.350   14.457  11.466  1.00 43.56 ? 143 ARG   A NH2 1 
ATOM   997  N  N   . THR   A 1 131 ? -7.814  11.854  14.094  1.00 15.66 ? 144 THR   A N   1 
ATOM   998  C  CA  . THR   A 1 131 ? -9.255  11.853  14.162  1.00 18.33 ? 144 THR   A CA  1 
ATOM   999  C  C   . THR   A 1 131 ? -9.816  13.167  13.652  1.00 18.17 ? 144 THR   A C   1 
ATOM   1000 O  O   . THR   A 1 131 ? -11.012 13.370  13.740  1.00 19.23 ? 144 THR   A O   1 
ATOM   1001 C  CB  . THR   A 1 131 ? -9.718  11.551  15.575  1.00 21.09 ? 144 THR   A CB  1 
ATOM   1002 O  OG1 . THR   A 1 131 ? -9.126  12.568  16.386  1.00 18.21 ? 144 THR   A OG1 1 
ATOM   1003 C  CG2 . THR   A 1 131 ? -9.308  10.152  15.988  1.00 23.59 ? 144 THR   A CG2 1 
ATOM   1004 N  N   . GLY   A 1 132 ? -8.958  13.982  13.038  1.00 20.86 ? 145 GLY   A N   1 
ATOM   1005 C  CA  . GLY   A 1 132 ? -9.357  15.299  12.577  1.00 21.86 ? 145 GLY   A CA  1 
ATOM   1006 C  C   . GLY   A 1 132 ? -8.107  15.997  12.083  1.00 21.77 ? 145 GLY   A C   1 
ATOM   1007 O  O   . GLY   A 1 132 ? -7.005  15.483  12.330  1.00 17.25 ? 145 GLY   A O   1 
ATOM   1008 N  N   . VAL   A 1 133 ? -8.272  17.122  11.369  1.00 22.56 ? 146 VAL   A N   1 
ATOM   1009 C  CA  . VAL   A 1 133 ? -7.116  17.697  10.674  1.00 25.92 ? 146 VAL   A CA  1 
ATOM   1010 C  C   . VAL   A 1 133 ? -5.856  17.793  11.548  1.00 27.62 ? 146 VAL   A C   1 
ATOM   1011 O  O   . VAL   A 1 133 ? -4.712  17.402  11.112  1.00 28.26 ? 146 VAL   A O   1 
ATOM   1012 C  CB  . VAL   A 1 133 ? -7.392  19.114  10.141  1.00 32.98 ? 146 VAL   A CB  1 
ATOM   1013 C  CG1 . VAL   A 1 133 ? -6.154  19.647  9.412   1.00 35.06 ? 146 VAL   A CG1 1 
ATOM   1014 C  CG2 . VAL   A 1 133 ? -8.633  19.176  9.272   1.00 39.26 ? 146 VAL   A CG2 1 
ATOM   1015 N  N   . LEU   A 1 134 ? -6.053  18.507  12.669  1.00 19.14 ? 147 LEU   A N   1 
ATOM   1016 C  CA  . LEU   A 1 134 ? -4.961  18.873  13.597  1.00 20.03 ? 147 LEU   A CA  1 
ATOM   1017 C  C   . LEU   A 1 134 ? -5.090  18.096  14.920  1.00 18.15 ? 147 LEU   A C   1 
ATOM   1018 O  O   . LEU   A 1 134 ? -4.633  18.556  15.959  1.00 16.96 ? 147 LEU   A O   1 
ATOM   1019 C  CB  . LEU   A 1 134 ? -5.011  20.381  13.900  1.00 18.80 ? 147 LEU   A CB  1 
ATOM   1020 C  CG  . LEU   A 1 134 ? -4.942  21.311  12.685  1.00 17.61 ? 147 LEU   A CG  1 
ATOM   1021 C  CD1 . LEU   A 1 134 ? -5.228  22.733  13.067  1.00 17.94 ? 147 LEU   A CD1 1 
ATOM   1022 C  CD2 . LEU   A 1 134 ? -3.603  21.199  12.008  1.00 16.98 ? 147 LEU   A CD2 1 
ATOM   1023 N  N   A LYS   A 1 135 ? -5.696  16.905  14.854  0.50 17.18 ? 148 LYS   A N   1 
ATOM   1024 N  N   B LYS   A 1 135 ? -5.789  16.955  14.862  0.50 18.00 ? 148 LYS   A N   1 
ATOM   1025 C  CA  A LYS   A 1 135 ? -5.968  16.086  16.026  0.50 17.10 ? 148 LYS   A CA  1 
ATOM   1026 C  CA  B LYS   A 1 135 ? -6.069  16.131  16.024  0.50 18.41 ? 148 LYS   A CA  1 
ATOM   1027 C  C   A LYS   A 1 135 ? -4.854  15.048  16.191  0.50 18.23 ? 148 LYS   A C   1 
ATOM   1028 C  C   B LYS   A 1 135 ? -4.964  15.085  16.167  0.50 18.39 ? 148 LYS   A C   1 
ATOM   1029 O  O   A LYS   A 1 135 ? -4.171  14.683  15.242  0.50 17.62 ? 148 LYS   A O   1 
ATOM   1030 O  O   B LYS   A 1 135 ? -4.231  14.767  15.236  0.50 17.33 ? 148 LYS   A O   1 
ATOM   1031 C  CB  A LYS   A 1 135 ? -7.323  15.385  15.907  0.50 15.67 ? 148 LYS   A CB  1 
ATOM   1032 C  CB  B LYS   A 1 135 ? -7.430  15.443  15.907  0.50 18.68 ? 148 LYS   A CB  1 
ATOM   1033 C  CG  A LYS   A 1 135 ? -8.545  16.277  15.940  0.50 15.09 ? 148 LYS   A CG  1 
ATOM   1034 C  CG  B LYS   A 1 135 ? -8.623  16.360  15.743  0.50 20.16 ? 148 LYS   A CG  1 
ATOM   1035 C  CD  A LYS   A 1 135 ? -8.753  16.977  17.261  0.50 15.36 ? 148 LYS   A CD  1 
ATOM   1036 C  CD  B LYS   A 1 135 ? -9.037  17.034  17.022  0.50 22.75 ? 148 LYS   A CD  1 
ATOM   1037 C  CE  A LYS   A 1 135 ? -10.061 17.737  17.303  0.50 14.55 ? 148 LYS   A CE  1 
ATOM   1038 C  CE  B LYS   A 1 135 ? -10.189 18.001  16.850  0.50 23.54 ? 148 LYS   A CE  1 
ATOM   1039 N  NZ  A LYS   A 1 135 ? -11.121 16.891  17.879  0.50 14.12 ? 148 LYS   A NZ  1 
ATOM   1040 N  NZ  B LYS   A 1 135 ? -10.384 18.776  18.095  0.50 27.58 ? 148 LYS   A NZ  1 
ATOM   1041 N  N   . PRO   A 1 136 ? -4.650  14.530  17.416  1.00 20.87 ? 150 PRO   A N   1 
ATOM   1042 C  CA  . PRO   A 1 136 ? -3.781  13.382  17.621  1.00 22.09 ? 150 PRO   A CA  1 
ATOM   1043 C  C   . PRO   A 1 136 ? -4.255  12.109  16.900  1.00 19.85 ? 150 PRO   A C   1 
ATOM   1044 O  O   . PRO   A 1 136 ? -5.443  11.969  16.550  1.00 17.17 ? 150 PRO   A O   1 
ATOM   1045 C  CB  . PRO   A 1 136 ? -3.843  13.168  19.130  1.00 22.63 ? 150 PRO   A CB  1 
ATOM   1046 C  CG  . PRO   A 1 136 ? -4.958  14.018  19.666  1.00 23.73 ? 150 PRO   A CG  1 
ATOM   1047 C  CD  . PRO   A 1 136 ? -5.323  15.012  18.640  1.00 24.17 ? 150 PRO   A CD  1 
ATOM   1048 N  N   . GLY   A 1 137 ? -3.311  11.181  16.723  1.00 17.60 ? 151 GLY   A N   1 
ATOM   1049 C  CA  . GLY   A 1 137 ? -3.621  9.782   16.442  1.00 19.64 ? 151 GLY   A CA  1 
ATOM   1050 C  C   . GLY   A 1 137 ? -4.616  9.187   17.449  1.00 17.54 ? 151 GLY   A C   1 
ATOM   1051 O  O   . GLY   A 1 137 ? -4.900  9.757   18.501  1.00 21.84 ? 151 GLY   A O   1 
ATOM   1052 N  N   . SER   A 1 138 ? -5.329  8.138   17.066  1.00 16.88 ? 152 SER   A N   1 
ATOM   1053 C  CA  . SER   A 1 138 ? -6.170  7.451   18.031  1.00 17.02 ? 152 SER   A CA  1 
ATOM   1054 C  C   . SER   A 1 138 ? -5.336  6.371   18.737  1.00 17.95 ? 152 SER   A C   1 
ATOM   1055 O  O   . SER   A 1 138 ? -4.603  5.595   18.093  1.00 16.15 ? 152 SER   A O   1 
ATOM   1056 C  CB  . SER   A 1 138 ? -7.372  6.856   17.395  1.00 18.12 ? 152 SER   A CB  1 
ATOM   1057 O  OG  . SER   A 1 138 ? -8.241  6.360   18.382  1.00 16.00 ? 152 SER   A OG  1 
ATOM   1058 N  N   . ASP   A 1 139 ? -5.405  6.349   20.064  1.00 14.86 ? 153 ASP   A N   1 
ATOM   1059 C  CA  . ASP   A 1 139 ? -4.866  5.214   20.787  1.00 17.83 ? 153 ASP   A CA  1 
ATOM   1060 C  C   . ASP   A 1 139 ? -5.661  3.945   20.425  1.00 17.94 ? 153 ASP   A C   1 
ATOM   1061 O  O   . ASP   A 1 139 ? -5.088  2.863   20.392  1.00 13.40 ? 153 ASP   A O   1 
ATOM   1062 C  CB  . ASP   A 1 139 ? -4.860  5.470   22.291  1.00 19.22 ? 153 ASP   A CB  1 
ATOM   1063 C  CG  . ASP   A 1 139 ? -3.754  6.382   22.810  1.00 20.47 ? 153 ASP   A CG  1 
ATOM   1064 O  OD1 . ASP   A 1 139 ? -2.960  6.804   22.005  1.00 20.76 ? 153 ASP   A OD1 1 
ATOM   1065 O  OD2 . ASP   A 1 139 ? -3.750  6.670   24.048  1.00 21.88 ? 153 ASP   A OD2 1 
ATOM   1066 N  N   . THR   A 1 140 ? -6.988  4.077   20.238  1.00 17.65 ? 154 THR   A N   1 
ATOM   1067 C  CA  . THR   A 1 140 ? -7.830  2.928   19.958  1.00 17.18 ? 154 THR   A CA  1 
ATOM   1068 C  C   . THR   A 1 140 ? -8.081  2.822   18.469  1.00 16.43 ? 154 THR   A C   1 
ATOM   1069 O  O   . THR   A 1 140 ? -8.053  3.799   17.741  1.00 17.14 ? 154 THR   A O   1 
ATOM   1070 C  CB  . THR   A 1 140 ? -9.146  2.993   20.735  1.00 16.17 ? 154 THR   A CB  1 
ATOM   1071 O  OG1 . THR   A 1 140 ? -9.783  4.216   20.372  1.00 15.46 ? 154 THR   A OG1 1 
ATOM   1072 C  CG2 . THR   A 1 140 ? -8.901  2.920   22.231  1.00 16.85 ? 154 THR   A CG2 1 
ATOM   1073 N  N   . LEU   A 1 141 ? -8.330  1.602   18.013  1.00 16.92 ? 155 LEU   A N   1 
ATOM   1074 C  CA  . LEU   A 1 141 ? -8.703  1.399   16.624  1.00 14.91 ? 155 LEU   A CA  1 
ATOM   1075 C  C   . LEU   A 1 141 ? -10.072 1.985   16.367  1.00 15.34 ? 155 LEU   A C   1 
ATOM   1076 O  O   . LEU   A 1 141 ? -11.033 1.666   17.080  1.00 16.12 ? 155 LEU   A O   1 
ATOM   1077 C  CB  . LEU   A 1 141 ? -8.702  -0.089  16.338  1.00 14.50 ? 155 LEU   A CB  1 
ATOM   1078 C  CG  . LEU   A 1 141 ? -8.931  -0.500  14.882  1.00 13.28 ? 155 LEU   A CG  1 
ATOM   1079 C  CD1 . LEU   A 1 141 ? -7.755  -0.134  13.972  1.00 12.25 ? 155 LEU   A CD1 1 
ATOM   1080 C  CD2 . LEU   A 1 141 ? -9.078  -2.004  14.862  1.00 12.66 ? 155 LEU   A CD2 1 
ATOM   1081 N  N   . GLN   A 1 142 ? -10.113 2.856   15.363  1.00 15.01 ? 156 GLN   A N   1 
ATOM   1082 C  CA  . GLN   A 1 142 ? -11.335 3.471   14.899  1.00 16.37 ? 156 GLN   A CA  1 
ATOM   1083 C  C   . GLN   A 1 142 ? -11.717 2.841   13.555  1.00 17.97 ? 156 GLN   A C   1 
ATOM   1084 O  O   . GLN   A 1 142 ? -10.894 2.294   12.831  1.00 15.80 ? 156 GLN   A O   1 
ATOM   1085 C  CB  . GLN   A 1 142 ? -11.105 4.958   14.701  1.00 15.85 ? 156 GLN   A CB  1 
ATOM   1086 C  CG  . GLN   A 1 142 ? -10.633 5.696   15.928  1.00 16.04 ? 156 GLN   A CG  1 
ATOM   1087 C  CD  . GLN   A 1 142 ? -11.718 6.038   16.909  1.00 17.06 ? 156 GLN   A CD  1 
ATOM   1088 O  OE1 . GLN   A 1 142 ? -12.790 6.511   16.555  1.00 19.25 ? 156 GLN   A OE1 1 
ATOM   1089 N  NE2 . GLN   A 1 142 ? -11.441 5.771   18.171  1.00 20.70 ? 156 GLN   A NE2 1 
ATOM   1090 N  N   . GLU   A 1 143 ? -12.986 2.928   13.200  1.00 18.41 ? 157 GLU   A N   1 
ATOM   1091 C  CA  . GLU   A 1 143 ? -13.413 2.468   11.887  1.00 19.54 ? 157 GLU   A CA  1 
ATOM   1092 C  C   . GLU   A 1 143 ? -14.506 3.424   11.398  1.00 20.03 ? 157 GLU   A C   1 
ATOM   1093 O  O   . GLU   A 1 143 ? -15.122 4.105   12.196  1.00 17.34 ? 157 GLU   A O   1 
ATOM   1094 C  CB  . GLU   A 1 143 ? -13.836 1.002   11.881  1.00 18.87 ? 157 GLU   A CB  1 
ATOM   1095 C  CG  . GLU   A 1 143 ? -14.983 0.653   12.840  1.00 20.52 ? 157 GLU   A CG  1 
ATOM   1096 C  CD  . GLU   A 1 143 ? -15.182 -0.852  13.025  1.00 23.07 ? 157 GLU   A CD  1 
ATOM   1097 O  OE1 . GLU   A 1 143 ? -16.250 -1.296  12.685  1.00 26.40 ? 157 GLU   A OE1 1 
ATOM   1098 O  OE2 . GLU   A 1 143 ? -14.247 -1.603  13.446  1.00 21.03 ? 157 GLU   A OE2 1 
ATOM   1099 N  N   . VAL   A 1 144 ? -14.691 3.490   10.081  1.00 18.46 ? 158 VAL   A N   1 
ATOM   1100 C  CA  . VAL   A 1 144 ? -15.726 4.315   9.502   1.00 19.88 ? 158 VAL   A CA  1 
ATOM   1101 C  C   . VAL   A 1 144 ? -16.233 3.676   8.206   1.00 22.62 ? 158 VAL   A C   1 
ATOM   1102 O  O   . VAL   A 1 144 ? -15.491 3.021   7.461   1.00 20.40 ? 158 VAL   A O   1 
ATOM   1103 C  CB  . VAL   A 1 144 ? -15.199 5.747   9.295   1.00 17.01 ? 158 VAL   A CB  1 
ATOM   1104 C  CG1 . VAL   A 1 144 ? -14.123 5.849   8.234   1.00 16.97 ? 158 VAL   A CG1 1 
ATOM   1105 C  CG2 . VAL   A 1 144 ? -16.337 6.691   9.006   1.00 17.84 ? 158 VAL   A CG2 1 
ATOM   1106 N  N   . LYS   A 1 145 ? -17.519 3.896   7.932   1.00 23.64 ? 159 LYS   A N   1 
ATOM   1107 C  CA  . LYS   A 1 145 ? -18.116 3.451   6.686   1.00 23.17 ? 159 LYS   A CA  1 
ATOM   1108 C  C   . LYS   A 1 145 ? -18.003 4.592   5.682   1.00 22.85 ? 159 LYS   A C   1 
ATOM   1109 O  O   . LYS   A 1 145 ? -18.451 5.685   6.010   1.00 23.00 ? 159 LYS   A O   1 
ATOM   1110 C  CB  . LYS   A 1 145 ? -19.586 3.104   6.951   1.00 24.66 ? 159 LYS   A CB  1 
ATOM   1111 C  CG  . LYS   A 1 145 ? -19.838 1.930   7.895   1.00 27.20 ? 159 LYS   A CG  1 
ATOM   1112 C  CD  . LYS   A 1 145 ? -21.291 1.816   8.383   0.50 25.19 ? 159 LYS   A CD  1 
ATOM   1113 C  CE  . LYS   A 1 145 ? -21.503 0.676   9.356   0.10 24.38 ? 159 LYS   A CE  1 
ATOM   1114 N  NZ  . LYS   A 1 145 ? -22.944 0.454   9.618   0.10 23.82 ? 159 LYS   A NZ  1 
ATOM   1115 N  N   . LEU   A 1 146 ? -17.440 4.336   4.489   1.00 21.71 ? 160 LEU   A N   1 
ATOM   1116 C  CA  . LEU   A 1 146 ? -17.269 5.330   3.437   1.00 21.35 ? 160 LEU   A CA  1 
ATOM   1117 C  C   . LEU   A 1 146 ? -17.910 4.832   2.138   1.00 22.90 ? 160 LEU   A C   1 
ATOM   1118 O  O   . LEU   A 1 146 ? -17.999 3.636   1.911   1.00 20.17 ? 160 LEU   A O   1 
ATOM   1119 C  CB  . LEU   A 1 146 ? -15.782 5.594   3.210   1.00 20.59 ? 160 LEU   A CB  1 
ATOM   1120 C  CG  . LEU   A 1 146 ? -14.994 5.997   4.445   1.00 18.60 ? 160 LEU   A CG  1 
ATOM   1121 C  CD1 . LEU   A 1 146 ? -13.505 6.023   4.135   1.00 18.66 ? 160 LEU   A CD1 1 
ATOM   1122 C  CD2 . LEU   A 1 146 ? -15.519 7.318   5.011   1.00 19.23 ? 160 LEU   A CD2 1 
ATOM   1123 N  N   . ARG   A 1 147 ? -18.375 5.770   1.299   1.00 25.05 ? 161 ARG   A N   1 
ATOM   1124 C  CA  . ARG   A 1 147 ? -18.953 5.415   0.009   1.00 25.17 ? 161 ARG   A CA  1 
ATOM   1125 C  C   . ARG   A 1 147 ? -17.863 5.393   -1.059  1.00 20.23 ? 161 ARG   A C   1 
ATOM   1126 O  O   . ARG   A 1 147 ? -17.095 6.335   -1.183  1.00 17.60 ? 161 ARG   A O   1 
ATOM   1127 C  CB  . ARG   A 1 147 ? -20.035 6.412   -0.392  1.00 24.28 ? 161 ARG   A CB  1 
ATOM   1128 C  CG  . ARG   A 1 147 ? -20.570 6.200   -1.795  1.00 25.83 ? 161 ARG   A CG  1 
ATOM   1129 C  CD  . ARG   A 1 147 ? -21.668 7.226   -2.099  1.00 27.94 ? 161 ARG   A CD  1 
ATOM   1130 N  NE  . ARG   A 1 147 ? -22.496 6.797   -3.203  1.00 29.79 ? 161 ARG   A NE  1 
ATOM   1131 C  CZ  . ARG   A 1 147 ? -22.272 7.067   -4.467  1.00 28.15 ? 161 ARG   A CZ  1 
ATOM   1132 N  NH1 . ARG   A 1 147 ? -21.216 7.779   -4.810  1.00 33.33 ? 161 ARG   A NH1 1 
ATOM   1133 N  NH2 . ARG   A 1 147 ? -23.080 6.582   -5.388  1.00 27.36 ? 161 ARG   A NH2 1 
ATOM   1134 N  N   . LEU   A 1 148 ? -17.788 4.298   -1.821  1.00 19.46 ? 162 LEU   A N   1 
ATOM   1135 C  CA  . LEU   A 1 148 ? -16.947 4.300   -3.005  1.00 21.23 ? 162 LEU   A CA  1 
ATOM   1136 C  C   . LEU   A 1 148 ? -17.521 5.230   -4.081  1.00 19.05 ? 162 LEU   A C   1 
ATOM   1137 O  O   . LEU   A 1 148 ? -18.704 5.172   -4.369  1.00 25.32 ? 162 LEU   A O   1 
ATOM   1138 C  CB  . LEU   A 1 148 ? -16.879 2.868   -3.487  1.00 28.21 ? 162 LEU   A CB  1 
ATOM   1139 C  CG  . LEU   A 1 148 ? -15.911 2.661   -4.627  1.00 30.61 ? 162 LEU   A CG  1 
ATOM   1140 C  CD1 . LEU   A 1 148 ? -14.493 2.684   -4.096  1.00 36.24 ? 162 LEU   A CD1 1 
ATOM   1141 C  CD2 . LEU   A 1 148 ? -16.243 1.369   -5.328  1.00 31.78 ? 162 LEU   A CD2 1 
ATOM   1142 N  N   . MET   A 1 149 ? -16.742 6.185   -4.571  1.00 16.98 ? 163 MET   A N   1 
ATOM   1143 C  CA  . MET   A 1 149 ? -17.232 7.182   -5.511  1.00 20.40 ? 163 MET   A CA  1 
ATOM   1144 C  C   . MET   A 1 149 ? -16.789 6.842   -6.922  1.00 18.22 ? 163 MET   A C   1 
ATOM   1145 O  O   . MET   A 1 149 ? -15.801 6.134   -7.108  1.00 16.51 ? 163 MET   A O   1 
ATOM   1146 C  CB  . MET   A 1 149 ? -16.702 8.602   -5.223  1.00 20.09 ? 163 MET   A CB  1 
ATOM   1147 C  CG  . MET   A 1 149 ? -16.864 9.101   -3.818  1.00 19.24 ? 163 MET   A CG  1 
ATOM   1148 S  SD  . MET   A 1 149 ? -18.496 9.152   -3.161  1.00 22.25 ? 163 MET   A SD  1 
ATOM   1149 C  CE  . MET   A 1 149 ? -19.236 10.378  -4.247  1.00 21.45 ? 163 MET   A CE  1 
ATOM   1150 N  N   . ASP   A 1 150 ? -17.512 7.397   -7.908  1.00 18.02 ? 164 ASP   A N   1 
ATOM   1151 C  CA  . ASP   A 1 150 ? -17.012 7.362   -9.265  1.00 17.51 ? 164 ASP   A CA  1 
ATOM   1152 C  C   . ASP   A 1 150 ? -15.651 8.032   -9.364  1.00 17.19 ? 164 ASP   A C   1 
ATOM   1153 O  O   . ASP   A 1 150 ? -15.297 8.919   -8.591  1.00 17.56 ? 164 ASP   A O   1 
ATOM   1154 C  CB  . ASP   A 1 150 ? -17.922 8.045   -10.263 1.00 18.85 ? 164 ASP   A CB  1 
ATOM   1155 C  CG  . ASP   A 1 150 ? -19.213 7.295   -10.524 1.00 19.68 ? 164 ASP   A CG  1 
ATOM   1156 O  OD1 . ASP   A 1 150 ? -20.037 7.842   -11.264 1.00 21.32 ? 164 ASP   A OD1 1 
ATOM   1157 O  OD2 . ASP   A 1 150 ? -19.410 6.243   -9.898  1.00 18.32 ? 164 ASP   A OD2 1 
ATOM   1158 N  N   . PRO   A 1 151 ? -14.827 7.649   -10.351 1.00 16.38 ? 165 PRO   A N   1 
ATOM   1159 C  CA  . PRO   A 1 151 ? -13.493 8.231   -10.479 1.00 18.04 ? 165 PRO   A CA  1 
ATOM   1160 C  C   . PRO   A 1 151 ? -13.486 9.721   -10.796 1.00 20.89 ? 165 PRO   A C   1 
ATOM   1161 O  O   . PRO   A 1 151 ? -12.536 10.423  -10.488 1.00 21.23 ? 165 PRO   A O   1 
ATOM   1162 C  CB  . PRO   A 1 151 ? -12.827 7.400   -11.541 1.00 15.55 ? 165 PRO   A CB  1 
ATOM   1163 C  CG  . PRO   A 1 151 ? -14.010 6.814   -12.286 1.00 16.28 ? 165 PRO   A CG  1 
ATOM   1164 C  CD  . PRO   A 1 151 ? -15.016 6.496   -11.234 1.00 16.59 ? 165 PRO   A CD  1 
ATOM   1165 N  N   . GLN   A 1 152 ? -14.557 10.212  -11.409 1.00 19.44 ? 166 GLN   A N   1 
ATOM   1166 C  CA  . GLN   A 1 152 ? -14.691 11.644  -11.634 1.00 20.09 ? 166 GLN   A CA  1 
ATOM   1167 C  C   . GLN   A 1 152 ? -14.566 12.497  -10.353 1.00 20.06 ? 166 GLN   A C   1 
ATOM   1168 O  O   . GLN   A 1 152 ? -14.131 13.632  -10.417 1.00 20.29 ? 166 GLN   A O   1 
ATOM   1169 C  CB  . GLN   A 1 152 ? -16.048 11.900  -12.275 1.00 18.42 ? 166 GLN   A CB  1 
ATOM   1170 C  CG  . GLN   A 1 152 ? -16.098 11.415  -13.697 1.00 19.70 ? 166 GLN   A CG  1 
ATOM   1171 C  CD  . GLN   A 1 152 ? -16.449 9.959   -13.881 1.00 20.76 ? 166 GLN   A CD  1 
ATOM   1172 O  OE1 . GLN   A 1 152 ? -16.945 9.271   -12.995 1.00 23.31 ? 166 GLN   A OE1 1 
ATOM   1173 N  NE2 . GLN   A 1 152 ? -16.166 9.464   -15.063 1.00 21.29 ? 166 GLN   A NE2 1 
ATOM   1174 N  N   . ALA   A 1 153 ? -15.080 11.996  -9.231  1.00 21.64 ? 167 ALA   A N   1 
ATOM   1175 C  CA  . ALA   A 1 153 ? -15.139 12.655  -7.941  1.00 20.48 ? 167 ALA   A CA  1 
ATOM   1176 C  C   . ALA   A 1 153 ? -13.727 12.901  -7.444  1.00 19.81 ? 167 ALA   A C   1 
ATOM   1177 O  O   . ALA   A 1 153 ? -13.562 13.703  -6.534  1.00 18.57 ? 167 ALA   A O   1 
ATOM   1178 C  CB  . ALA   A 1 153 ? -15.882 11.786  -6.927  1.00 21.51 ? 167 ALA   A CB  1 
ATOM   1179 N  N   . CYS   A 1 154 ? -12.753 12.165  -7.996  1.00 18.62 ? 168 CYS   A N   1 
ATOM   1180 C  CA  . CYS   A 1 154 ? -11.363 12.400  -7.686  1.00 17.25 ? 168 CYS   A CA  1 
ATOM   1181 C  C   . CYS   A 1 154 ? -10.620 13.119  -8.806  1.00 19.90 ? 168 CYS   A C   1 
ATOM   1182 O  O   . CYS   A 1 154 ? -9.382  13.134  -8.763  1.00 17.51 ? 168 CYS   A O   1 
ATOM   1183 C  CB  . CYS   A 1 154 ? -10.641 11.090  -7.411  1.00 19.39 ? 168 CYS   A CB  1 
ATOM   1184 S  SG  . CYS   A 1 154 ? -10.944 10.480  -5.751  1.00 18.56 ? 168 CYS   A SG  1 
ATOM   1185 N  N   . SER   A 1 155 ? -11.328 13.733  -9.775  1.00 19.60 ? 169 SER   A N   1 
ATOM   1186 C  CA  . SER   A 1 155 ? -10.640 14.354  -10.924 1.00 25.62 ? 169 SER   A CA  1 
ATOM   1187 C  C   . SER   A 1 155 ? -9.701  15.483  -10.500 1.00 23.34 ? 169 SER   A C   1 
ATOM   1188 O  O   . SER   A 1 155 ? -8.785  15.854  -11.212 1.00 22.87 ? 169 SER   A O   1 
ATOM   1189 C  CB  . SER   A 1 155 ? -11.634 14.876  -11.977 1.00 23.44 ? 169 SER   A CB  1 
ATOM   1190 O  OG  . SER   A 1 155 ? -12.437 15.870  -11.406 1.00 25.62 ? 169 SER   A OG  1 
ATOM   1191 N  N   . HIS   A 1 156 ? -9.928  16.031  -9.321  1.00 28.03 ? 172 HIS   A N   1 
ATOM   1192 C  CA  . HIS   A 1 156 ? -9.114  17.123  -8.817  1.00 28.30 ? 172 HIS   A CA  1 
ATOM   1193 C  C   . HIS   A 1 156 ? -7.735  16.668  -8.350  1.00 28.92 ? 172 HIS   A C   1 
ATOM   1194 O  O   . HIS   A 1 156 ? -6.907  17.506  -8.120  1.00 30.52 ? 172 HIS   A O   1 
ATOM   1195 C  CB  . HIS   A 1 156 ? -9.907  17.846  -7.732  1.00 28.62 ? 172 HIS   A CB  1 
ATOM   1196 C  CG  . HIS   A 1 156 ? -10.231 17.016  -6.528  1.00 30.74 ? 172 HIS   A CG  1 
ATOM   1197 N  ND1 . HIS   A 1 156 ? -11.174 15.996  -6.565  1.00 30.10 ? 172 HIS   A ND1 1 
ATOM   1198 C  CD2 . HIS   A 1 156 ? -9.762  17.076  -5.247  1.00 29.20 ? 172 HIS   A CD2 1 
ATOM   1199 C  CE1 . HIS   A 1 156 ? -11.283 15.468  -5.357  1.00 29.45 ? 172 HIS   A CE1 1 
ATOM   1200 N  NE2 . HIS   A 1 156 ? -10.421 16.115  -4.526  1.00 31.10 ? 172 HIS   A NE2 1 
ATOM   1201 N  N   . PHE   A 1 157 ? -7.487  15.366  -8.185  1.00 32.21 ? 173 PHE   A N   1 
ATOM   1202 C  CA  . PHE   A 1 157 ? -6.153  14.823  -7.918  1.00 29.94 ? 173 PHE   A CA  1 
ATOM   1203 C  C   . PHE   A 1 157 ? -5.466  14.550  -9.254  1.00 31.06 ? 173 PHE   A C   1 
ATOM   1204 O  O   . PHE   A 1 157 ? -5.873  13.646  -9.973  1.00 26.60 ? 173 PHE   A O   1 
ATOM   1205 C  CB  . PHE   A 1 157 ? -6.255  13.511  -7.128  1.00 29.15 ? 173 PHE   A CB  1 
ATOM   1206 C  CG  . PHE   A 1 157 ? -6.776  13.665  -5.720  1.00 26.96 ? 173 PHE   A CG  1 
ATOM   1207 C  CD1 . PHE   A 1 157 ? -5.989  14.253  -4.737  1.00 24.76 ? 173 PHE   A CD1 1 
ATOM   1208 C  CD2 . PHE   A 1 157 ? -8.037  13.224  -5.371  1.00 25.37 ? 173 PHE   A CD2 1 
ATOM   1209 C  CE1 . PHE   A 1 157 ? -6.471  14.414  -3.451  1.00 23.69 ? 173 PHE   A CE1 1 
ATOM   1210 C  CE2 . PHE   A 1 157 ? -8.506  13.365  -4.075  1.00 27.61 ? 173 PHE   A CE2 1 
ATOM   1211 C  CZ  . PHE   A 1 157 ? -7.737  13.998  -3.126  1.00 26.91 ? 173 PHE   A CZ  1 
ATOM   1212 N  N   . ARG   A 1 158 ? -4.462  15.353  -9.617  1.00 30.47 ? 174 ARG   A N   1 
ATOM   1213 C  CA  . ARG   A 1 158 ? -4.048  15.397  -11.009 1.00 36.56 ? 174 ARG   A CA  1 
ATOM   1214 C  C   . ARG   A 1 158 ? -3.559  14.018  -11.469 1.00 36.45 ? 174 ARG   A C   1 
ATOM   1215 O  O   . ARG   A 1 158 ? -3.894  13.601  -12.586 1.00 27.32 ? 174 ARG   A O   1 
ATOM   1216 C  CB  . ARG   A 1 158 ? -3.017  16.501  -11.296 1.00 39.19 ? 174 ARG   A CB  1 
ATOM   1217 C  CG  . ARG   A 1 158 ? -1.837  16.581  -10.329 1.00 47.16 ? 174 ARG   A CG  1 
ATOM   1218 C  CD  . ARG   A 1 158 ? -0.571  17.247  -10.884 0.50 44.05 ? 174 ARG   A CD  1 
ATOM   1219 N  NE  . ARG   A 1 158 ? -0.142  16.676  -12.152 0.50 40.25 ? 174 ARG   A NE  1 
ATOM   1220 C  CZ  . ARG   A 1 158 ? 0.801   17.178  -12.942 0.50 47.29 ? 174 ARG   A CZ  1 
ATOM   1221 N  NH1 . ARG   A 1 158 ? 1.457   18.280  -12.604 0.50 47.51 ? 174 ARG   A NH1 1 
ATOM   1222 N  NH2 . ARG   A 1 158 ? 1.074   16.572  -14.084 0.50 42.76 ? 174 ARG   A NH2 1 
ATOM   1223 N  N   . ASP   A 1 159 ? -2.843  13.297  -10.581 1.00 32.99 ? 175 ASP   A N   1 
ATOM   1224 C  CA  . ASP   A 1 159 ? -2.255  12.004  -10.898 1.00 29.59 ? 175 ASP   A CA  1 
ATOM   1225 C  C   . ASP   A 1 159 ? -3.171  10.816  -10.559 1.00 26.96 ? 175 ASP   A C   1 
ATOM   1226 O  O   . ASP   A 1 159 ? -2.693  9.677   -10.513 1.00 23.32 ? 175 ASP   A O   1 
ATOM   1227 C  CB  . ASP   A 1 159 ? -0.918  11.886  -10.180 1.00 30.99 ? 175 ASP   A CB  1 
ATOM   1228 C  CG  . ASP   A 1 159 ? 0.103   12.854  -10.724 1.00 33.98 ? 175 ASP   A CG  1 
ATOM   1229 O  OD1 . ASP   A 1 159 ? 0.254   12.865  -11.947 1.00 36.18 ? 175 ASP   A OD1 1 
ATOM   1230 O  OD2 . ASP   A 1 159 ? 0.722   13.583  -9.919  1.00 37.91 ? 175 ASP   A OD2 1 
ATOM   1231 N  N   . PHE   A 1 160 ? -4.481  11.037  -10.360 1.00 25.48 ? 176 PHE   A N   1 
ATOM   1232 C  CA  . PHE   A 1 160 ? -5.398  9.924   -10.119 1.00 27.62 ? 176 PHE   A CA  1 
ATOM   1233 C  C   . PHE   A 1 160 ? -5.557  9.068   -11.374 1.00 28.04 ? 176 PHE   A C   1 
ATOM   1234 O  O   . PHE   A 1 160 ? -5.458  9.579   -12.469 1.00 34.46 ? 176 PHE   A O   1 
ATOM   1235 C  CB  . PHE   A 1 160 ? -6.799  10.409  -9.702  1.00 27.46 ? 176 PHE   A CB  1 
ATOM   1236 C  CG  . PHE   A 1 160 ? -7.748  9.323   -9.281  1.00 23.29 ? 176 PHE   A CG  1 
ATOM   1237 C  CD1 . PHE   A 1 160 ? -8.635  8.757   -10.162 1.00 24.12 ? 176 PHE   A CD1 1 
ATOM   1238 C  CD2 . PHE   A 1 160 ? -7.677  8.773   -8.013  1.00 26.63 ? 176 PHE   A CD2 1 
ATOM   1239 C  CE1 . PHE   A 1 160 ? -9.519  7.759   -9.762  1.00 21.44 ? 176 PHE   A CE1 1 
ATOM   1240 C  CE2 . PHE   A 1 160 ? -8.566  7.794   -7.609  1.00 21.91 ? 176 PHE   A CE2 1 
ATOM   1241 C  CZ  . PHE   A 1 160 ? -9.481  7.286   -8.491  1.00 21.70 ? 176 PHE   A CZ  1 
ATOM   1242 N  N   . ASP   A 1 161 ? -5.872  7.779   -11.199 1.00 26.13 ? 177 ASP   A N   1 
ATOM   1243 C  CA  . ASP   A 1 161 ? -5.987  6.833   -12.285 1.00 21.89 ? 177 ASP   A CA  1 
ATOM   1244 C  C   . ASP   A 1 161 ? -6.879  5.687   -11.850 1.00 22.53 ? 177 ASP   A C   1 
ATOM   1245 O  O   . ASP   A 1 161 ? -6.467  4.863   -11.024 1.00 20.34 ? 177 ASP   A O   1 
ATOM   1246 C  CB  . ASP   A 1 161 ? -4.628  6.288   -12.703 1.00 21.96 ? 177 ASP   A CB  1 
ATOM   1247 C  CG  . ASP   A 1 161 ? -4.672  5.320   -13.883 1.00 27.74 ? 177 ASP   A CG  1 
ATOM   1248 O  OD1 . ASP   A 1 161 ? -3.598  5.086   -14.507 1.00 29.52 ? 177 ASP   A OD1 1 
ATOM   1249 O  OD2 . ASP   A 1 161 ? -5.766  4.789   -14.184 1.00 24.85 ? 177 ASP   A OD2 1 
ATOM   1250 N  N   . HIS   A 1 162 ? -8.082  5.666   -12.452 1.00 19.55 ? 178 HIS   A N   1 
ATOM   1251 C  CA  . HIS   A 1 162 ? -9.170  4.770   -12.127 1.00 20.04 ? 178 HIS   A CA  1 
ATOM   1252 C  C   . HIS   A 1 162 ? -8.742  3.306   -12.170 1.00 21.63 ? 178 HIS   A C   1 
ATOM   1253 O  O   . HIS   A 1 162 ? -9.377  2.457   -11.541 1.00 20.63 ? 178 HIS   A O   1 
ATOM   1254 C  CB  . HIS   A 1 162 ? -10.334 4.989   -13.094 1.00 19.95 ? 178 HIS   A CB  1 
ATOM   1255 C  CG  . HIS   A 1 162 ? -11.416 3.976   -12.983 1.00 23.09 ? 178 HIS   A CG  1 
ATOM   1256 N  ND1 . HIS   A 1 162 ? -12.336 3.971   -11.922 1.00 23.81 ? 178 HIS   A ND1 1 
ATOM   1257 C  CD2 . HIS   A 1 162 ? -11.789 2.977   -13.825 1.00 25.38 ? 178 HIS   A CD2 1 
ATOM   1258 C  CE1 . HIS   A 1 162 ? -13.197 2.968   -12.083 1.00 24.38 ? 178 HIS   A CE1 1 
ATOM   1259 N  NE2 . HIS   A 1 162 ? -12.864 2.322   -13.251 1.00 25.95 ? 178 HIS   A NE2 1 
ATOM   1260 N  N   . ASN   A 1 163 A -7.762  3.001   -13.023 1.00 24.50 ? 178 ASN   A N   1 
ATOM   1261 C  CA  . ASN   A 1 163 A -7.289  1.635   -13.162 1.00 25.55 ? 178 ASN   A CA  1 
ATOM   1262 C  C   . ASN   A 1 163 A -6.467  1.208   -11.937 1.00 24.08 ? 178 ASN   A C   1 
ATOM   1263 O  O   . ASN   A 1 163 A -6.468  0.035   -11.582 1.00 20.66 ? 178 ASN   A O   1 
ATOM   1264 C  CB  . ASN   A 1 163 A -6.402  1.442   -14.408 1.00 31.02 ? 178 ASN   A CB  1 
ATOM   1265 C  CG  . ASN   A 1 163 A -7.145  1.537   -15.729 1.00 34.46 ? 178 ASN   A CG  1 
ATOM   1266 O  OD1 . ASN   A 1 163 A -6.772  2.338   -16.580 1.00 37.12 ? 178 ASN   A OD1 1 
ATOM   1267 N  ND2 . ASN   A 1 163 A -8.200  0.755   -15.893 1.00 32.20 ? 178 ASN   A ND2 1 
ATOM   1268 N  N   . LEU   A 1 164 ? -5.663  2.134   -11.404 1.00 21.42 ? 179 LEU   A N   1 
ATOM   1269 C  CA  . LEU   A 1 164 ? -4.793  1.832   -10.299 1.00 22.27 ? 179 LEU   A CA  1 
ATOM   1270 C  C   . LEU   A 1 164 ? -5.495  2.086   -8.951  1.00 21.74 ? 179 LEU   A C   1 
ATOM   1271 O  O   . LEU   A 1 164 ? -5.014  1.632   -7.930  1.00 21.22 ? 179 LEU   A O   1 
ATOM   1272 C  CB  . LEU   A 1 164 ? -3.533  2.680   -10.468 1.00 22.58 ? 179 LEU   A CB  1 
ATOM   1273 C  CG  . LEU   A 1 164 ? -2.875  2.708   -11.847 1.00 27.66 ? 179 LEU   A CG  1 
ATOM   1274 C  CD1 . LEU   A 1 164 ? -1.660  3.623   -11.828 1.00 28.50 ? 179 LEU   A CD1 1 
ATOM   1275 C  CD2 . LEU   A 1 164 ? -2.472  1.328   -12.340 1.00 31.33 ? 179 LEU   A CD2 1 
ATOM   1276 N  N   . GLN   A 1 165 ? -6.642  2.796   -8.898  1.00 23.53 ? 180 GLN   A N   1 
ATOM   1277 C  CA  . GLN   A 1 165 ? -6.991  3.495   -7.668  1.00 20.77 ? 180 GLN   A CA  1 
ATOM   1278 C  C   . GLN   A 1 165 ? -8.494  3.586   -7.488  1.00 20.04 ? 180 GLN   A C   1 
ATOM   1279 O  O   . GLN   A 1 165 ? -9.222  3.623   -8.461  1.00 22.34 ? 180 GLN   A O   1 
ATOM   1280 C  CB  . GLN   A 1 165 ? -6.375  4.893   -7.636  1.00 22.07 ? 180 GLN   A CB  1 
ATOM   1281 C  CG  . GLN   A 1 165 ? -4.865  4.908   -7.470  1.00 23.94 ? 180 GLN   A CG  1 
ATOM   1282 C  CD  . GLN   A 1 165 ? -4.310  6.270   -7.820  1.00 22.51 ? 180 GLN   A CD  1 
ATOM   1283 O  OE1 . GLN   A 1 165 ? -4.771  6.941   -8.748  1.00 20.08 ? 180 GLN   A OE1 1 
ATOM   1284 N  NE2 . GLN   A 1 165 ? -3.261  6.659   -7.125  1.00 20.47 ? 180 GLN   A NE2 1 
ATOM   1285 N  N   . LEU   A 1 166 ? -8.906  3.545   -6.223  1.00 18.90 ? 181 LEU   A N   1 
ATOM   1286 C  CA  . LEU   A 1 166 ? -10.261 3.823   -5.794  1.00 19.83 ? 181 LEU   A CA  1 
ATOM   1287 C  C   . LEU   A 1 166 ? -10.417 5.257   -5.294  1.00 18.98 ? 181 LEU   A C   1 
ATOM   1288 O  O   . LEU   A 1 166 ? -9.522  5.808   -4.673  1.00 18.76 ? 181 LEU   A O   1 
ATOM   1289 C  CB  . LEU   A 1 166 ? -10.624 2.829   -4.698  1.00 20.95 ? 181 LEU   A CB  1 
ATOM   1290 C  CG  . LEU   A 1 166 ? -10.432 1.363   -5.074  1.00 23.07 ? 181 LEU   A CG  1 
ATOM   1291 C  CD1 . LEU   A 1 166 ? -10.669 0.439   -3.887  1.00 22.87 ? 181 LEU   A CD1 1 
ATOM   1292 C  CD2 . LEU   A 1 166 ? -11.365 0.993   -6.214  1.00 23.61 ? 181 LEU   A CD2 1 
ATOM   1293 N  N   . CYS   A 1 167 ? -11.636 5.789   -5.457  1.00 19.24 ? 182 CYS   A N   1 
ATOM   1294 C  CA  . CYS   A 1 167 ? -11.971 7.126   -5.027  1.00 20.03 ? 182 CYS   A CA  1 
ATOM   1295 C  C   . CYS   A 1 167 ? -12.988 6.949   -3.915  1.00 22.39 ? 182 CYS   A C   1 
ATOM   1296 O  O   . CYS   A 1 167 ? -14.088 6.405   -4.142  1.00 19.57 ? 182 CYS   A O   1 
ATOM   1297 C  CB  . CYS   A 1 167 ? -12.450 7.957   -6.219  1.00 20.58 ? 182 CYS   A CB  1 
ATOM   1298 S  SG  . CYS   A 1 167 ? -12.820 9.685   -5.856  1.00 18.44 ? 182 CYS   A SG  1 
ATOM   1299 N  N   . VAL   A 1 168 ? -12.600 7.381   -2.698  1.00 20.93 ? 183 VAL   A N   1 
ATOM   1300 C  CA  . VAL   A 1 168 ? -13.311 6.914   -1.520  1.00 18.54 ? 183 VAL   A CA  1 
ATOM   1301 C  C   . VAL   A 1 168 ? -13.715 8.054   -0.576  1.00 19.31 ? 183 VAL   A C   1 
ATOM   1302 O  O   . VAL   A 1 168 ? -12.874 8.788   -0.070  1.00 21.18 ? 183 VAL   A O   1 
ATOM   1303 C  CB  . VAL   A 1 168 ? -12.471 5.857   -0.778  1.00 18.51 ? 183 VAL   A CB  1 
ATOM   1304 C  CG1 . VAL   A 1 168 ? -13.287 5.153   0.287   1.00 17.54 ? 183 VAL   A CG1 1 
ATOM   1305 C  CG2 . VAL   A 1 168 ? -11.816 4.861   -1.728  1.00 19.65 ? 183 VAL   A CG2 1 
ATOM   1306 N  N   . GLY   A 1 169 ? -15.007 8.111   -0.239  1.00 19.71 ? 184 GLY   A N   1 
ATOM   1307 C  CA  . GLY   A 1 169 ? -15.539 9.094   0.705   1.00 17.37 ? 184 GLY   A CA  1 
ATOM   1308 C  C   . GLY   A 1 169 ? -16.409 10.152  0.011   1.00 19.10 ? 184 GLY   A C   1 
ATOM   1309 O  O   . GLY   A 1 169 ? -15.943 10.953  -0.803  1.00 16.20 ? 184 GLY   A O   1 
ATOM   1310 N  N   . ASN   A 1 170 ? -17.704 10.133  0.345   1.00 17.64 ? 185 ASN   A N   1 
ATOM   1311 C  CA  . ASN   A 1 170 ? -18.625 11.192  -0.008  1.00 21.32 ? 185 ASN   A CA  1 
ATOM   1312 C  C   . ASN   A 1 170 ? -18.130 12.549  0.483   1.00 26.14 ? 185 ASN   A C   1 
ATOM   1313 O  O   . ASN   A 1 170 ? -17.952 12.718  1.679   1.00 31.54 ? 185 ASN   A O   1 
ATOM   1314 C  CB  . ASN   A 1 170 ? -19.962 10.857  0.640   1.00 23.74 ? 185 ASN   A CB  1 
ATOM   1315 C  CG  . ASN   A 1 170 ? -21.123 11.760  0.259   1.00 29.96 ? 185 ASN   A CG  1 
ATOM   1316 O  OD1 . ASN   A 1 170 ? -20.981 12.940  -0.074  1.00 24.65 ? 185 ASN   A OD1 1 
ATOM   1317 N  ND2 . ASN   A 1 170 ? -22.313 11.215  0.454   1.00 32.86 ? 185 ASN   A ND2 1 
ATOM   1318 N  N   . PRO   A 1 171 ? -17.984 13.575  -0.388  1.00 25.24 ? 186 PRO   A N   1 
ATOM   1319 C  CA  . PRO   A 1 171 ? -17.435 14.854  0.031   1.00 29.09 ? 186 PRO   A CA  1 
ATOM   1320 C  C   . PRO   A 1 171 ? -18.382 15.692  0.886   1.00 26.59 ? 186 PRO   A C   1 
ATOM   1321 O  O   . PRO   A 1 171 ? -17.923 16.603  1.573   1.00 22.91 ? 186 PRO   A O   1 
ATOM   1322 C  CB  . PRO   A 1 171 ? -16.949 15.513  -1.275  1.00 25.24 ? 186 PRO   A CB  1 
ATOM   1323 C  CG  . PRO   A 1 171 ? -17.858 14.896  -2.320  1.00 25.91 ? 186 PRO   A CG  1 
ATOM   1324 C  CD  . PRO   A 1 171 ? -18.182 13.502  -1.842  1.00 26.86 ? 186 PRO   A CD  1 
ATOM   1325 N  N   . ARG   A 1 172 A -19.655 15.300  0.944   1.00 23.27 ? 186 ARG   A N   1 
ATOM   1326 C  CA  . ARG   A 1 172 A -20.639 16.034  1.727   1.00 27.94 ? 186 ARG   A CA  1 
ATOM   1327 C  C   . ARG   A 1 172 A -20.440 15.808  3.218   1.00 29.90 ? 186 ARG   A C   1 
ATOM   1328 O  O   . ARG   A 1 172 A -20.808 16.665  4.028   1.00 33.45 ? 186 ARG   A O   1 
ATOM   1329 C  CB  . ARG   A 1 172 A -22.085 15.612  1.393   1.00 26.85 ? 186 ARG   A CB  1 
ATOM   1330 C  CG  . ARG   A 1 172 A -22.562 15.909  -0.019  0.10 24.22 ? 186 ARG   A CG  1 
ATOM   1331 C  CD  . ARG   A 1 172 A -24.077 15.817  -0.044  0.10 22.81 ? 186 ARG   A CD  1 
ATOM   1332 N  NE  . ARG   A 1 172 A -24.627 15.598  -1.371  0.10 21.68 ? 186 ARG   A NE  1 
ATOM   1333 C  CZ  . ARG   A 1 172 A -25.042 14.420  -1.828  0.10 20.74 ? 186 ARG   A CZ  1 
ATOM   1334 N  NH1 . ARG   A 1 172 A -24.961 13.345  -1.062  0.10 20.03 ? 186 ARG   A NH1 1 
ATOM   1335 N  NH2 . ARG   A 1 172 A -25.532 14.320  -3.050  0.10 20.33 ? 186 ARG   A NH2 1 
ATOM   1336 N  N   . LYS   A 1 173 B -19.938 14.619  3.579   1.00 30.90 ? 186 LYS   A N   1 
ATOM   1337 C  CA  . LYS   A 1 173 B -19.699 14.257  4.975   1.00 29.63 ? 186 LYS   A CA  1 
ATOM   1338 C  C   . LYS   A 1 173 B -18.221 14.442  5.316   1.00 24.86 ? 186 LYS   A C   1 
ATOM   1339 O  O   . LYS   A 1 173 B -17.421 14.578  4.420   1.00 31.06 ? 186 LYS   A O   1 
ATOM   1340 C  CB  . LYS   A 1 173 B -20.143 12.821  5.213   1.00 26.55 ? 186 LYS   A CB  1 
ATOM   1341 C  CG  . LYS   A 1 173 B -21.526 12.494  4.659   1.00 28.75 ? 186 LYS   A CG  1 
ATOM   1342 C  CD  . LYS   A 1 173 B -21.979 11.088  4.922   1.00 28.72 ? 186 LYS   A CD  1 
ATOM   1343 C  CE  . LYS   A 1 173 B -23.443 10.887  4.566   0.50 25.37 ? 186 LYS   A CE  1 
ATOM   1344 N  NZ  . LYS   A 1 173 B -23.877 9.571   5.063   0.50 25.05 ? 186 LYS   A NZ  1 
ATOM   1345 N  N   . THR   A 1 174 ? -17.878 14.474  6.608   1.00 25.63 ? 187 THR   A N   1 
ATOM   1346 C  CA  . THR   A 1 174 ? -16.486 14.552  7.054   1.00 24.34 ? 187 THR   A CA  1 
ATOM   1347 C  C   . THR   A 1 174 ? -15.794 13.197  7.269   1.00 22.40 ? 187 THR   A C   1 
ATOM   1348 O  O   . THR   A 1 174 ? -14.583 13.172  7.522   1.00 23.14 ? 187 THR   A O   1 
ATOM   1349 C  CB  . THR   A 1 174 ? -16.359 15.290  8.400   1.00 25.52 ? 187 THR   A CB  1 
ATOM   1350 O  OG1 . THR   A 1 174 ? -17.027 14.642  9.494   1.00 29.57 ? 187 THR   A OG1 1 
ATOM   1351 C  CG2 . THR   A 1 174 ? -16.838 16.715  8.279   1.00 25.44 ? 187 THR   A CG2 1 
ATOM   1352 N  N   A LYS   A 1 175 ? -16.566 12.101  7.194   0.50 21.04 ? 188 LYS   A N   1 
ATOM   1353 N  N   B LYS   A 1 175 ? -16.551 12.102  7.160   0.50 21.51 ? 188 LYS   A N   1 
ATOM   1354 C  CA  A LYS   A 1 175 ? -16.041 10.749  7.328   0.50 20.58 ? 188 LYS   A CA  1 
ATOM   1355 C  CA  B LYS   A 1 175 ? -16.013 10.767  7.353   0.50 21.47 ? 188 LYS   A CA  1 
ATOM   1356 C  C   A LYS   A 1 175 ? -14.932 10.522  6.299   0.50 19.41 ? 188 LYS   A C   1 
ATOM   1357 C  C   B LYS   A 1 175 ? -14.945 10.472  6.302   0.50 19.81 ? 188 LYS   A C   1 
ATOM   1358 O  O   A LYS   A 1 175 ? -15.156 10.755  5.111   0.50 16.86 ? 188 LYS   A O   1 
ATOM   1359 O  O   B LYS   A 1 175 ? -15.210 10.596  5.107   0.50 17.31 ? 188 LYS   A O   1 
ATOM   1360 C  CB  A LYS   A 1 175 ? -17.130 9.698   7.117   0.50 19.88 ? 188 LYS   A CB  1 
ATOM   1361 C  CB  B LYS   A 1 175 ? -17.134 9.738   7.289   0.50 21.22 ? 188 LYS   A CB  1 
ATOM   1362 C  CG  A LYS   A 1 175 ? -18.299 9.740   8.085   0.50 19.95 ? 188 LYS   A CG  1 
ATOM   1363 C  CG  B LYS   A 1 175 ? -18.151 9.867   8.404   0.50 22.00 ? 188 LYS   A CG  1 
ATOM   1364 C  CD  A LYS   A 1 175 ? -19.218 8.533   7.979   0.50 18.32 ? 188 LYS   A CD  1 
ATOM   1365 C  CD  B LYS   A 1 175 ? -19.339 8.946   8.231   0.50 21.18 ? 188 LYS   A CD  1 
ATOM   1366 C  CE  A LYS   A 1 175 ? -20.143 8.586   6.786   0.50 17.71 ? 188 LYS   A CE  1 
ATOM   1367 C  CE  B LYS   A 1 175 ? -20.331 9.106   9.360   0.50 20.20 ? 188 LYS   A CE  1 
ATOM   1368 N  NZ  A LYS   A 1 175 ? -20.820 7.293   6.564   0.50 16.55 ? 188 LYS   A NZ  1 
ATOM   1369 N  NZ  B LYS   A 1 175 ? -21.531 8.285   9.116   0.50 21.42 ? 188 LYS   A NZ  1 
ATOM   1370 N  N   . SER   A 1 176 ? -13.729 10.140  6.785   1.00 17.24 ? 189 SER   A N   1 
ATOM   1371 C  CA  . SER   A 1 176 ? -12.595 9.847   5.938   1.00 16.45 ? 189 SER   A CA  1 
ATOM   1372 C  C   . SER   A 1 176 ? -11.529 9.038   6.685   1.00 17.96 ? 189 SER   A C   1 
ATOM   1373 O  O   . SER   A 1 176 ? -11.393 9.141   7.914   1.00 22.25 ? 189 SER   A O   1 
ATOM   1374 C  CB  . SER   A 1 176 ? -12.005 11.149  5.496   1.00 18.29 ? 189 SER   A CB  1 
ATOM   1375 O  OG  . SER   A 1 176 ? -10.878 10.942  4.632   1.00 18.20 ? 189 SER   A OG  1 
ATOM   1376 N  N   . ALA   A 1 177 ? -10.696 8.313   5.940   1.00 16.66 ? 190 ALA   A N   1 
ATOM   1377 C  CA  . ALA   A 1 177 ? -9.373  7.942   6.423   1.00 15.67 ? 190 ALA   A CA  1 
ATOM   1378 C  C   . ALA   A 1 177 ? -8.554  9.210   6.435   1.00 16.05 ? 190 ALA   A C   1 
ATOM   1379 O  O   . ALA   A 1 177 ? -8.846  10.131  5.688   1.00 15.80 ? 190 ALA   A O   1 
ATOM   1380 C  CB  . ALA   A 1 177 ? -8.687  6.897   5.570   1.00 15.80 ? 190 ALA   A CB  1 
ATOM   1381 N  N   . PHE   A 1 178 ? -7.519  9.238   7.277   1.00 16.97 ? 191 PHE   A N   1 
ATOM   1382 C  CA  . PHE   A 1 178 ? -6.666  10.409  7.329   1.00 18.39 ? 191 PHE   A CA  1 
ATOM   1383 C  C   . PHE   A 1 178 ? -5.221  9.978   7.598   1.00 17.95 ? 191 PHE   A C   1 
ATOM   1384 O  O   . PHE   A 1 178 ? -4.896  8.781   7.481   1.00 15.37 ? 191 PHE   A O   1 
ATOM   1385 C  CB  . PHE   A 1 178 ? -7.224  11.436  8.316   1.00 18.69 ? 191 PHE   A CB  1 
ATOM   1386 C  CG  . PHE   A 1 178 ? -6.696  12.831  8.074   1.00 22.39 ? 191 PHE   A CG  1 
ATOM   1387 C  CD1 . PHE   A 1 178 ? -6.620  13.377  6.790   1.00 22.45 ? 191 PHE   A CD1 1 
ATOM   1388 C  CD2 . PHE   A 1 178 ? -6.297  13.636  9.140   1.00 23.71 ? 191 PHE   A CD2 1 
ATOM   1389 C  CE1 . PHE   A 1 178 ? -6.061  14.639  6.568   1.00 21.93 ? 191 PHE   A CE1 1 
ATOM   1390 C  CE2 . PHE   A 1 178 ? -5.817  14.920  8.918   1.00 25.79 ? 191 PHE   A CE2 1 
ATOM   1391 C  CZ  . PHE   A 1 178 ? -5.659  15.413  7.640   1.00 23.68 ? 191 PHE   A CZ  1 
ATOM   1392 N  N   . LYS   A 1 179 ? -4.361  10.979  7.931   1.00 19.21 ? 192 LYS   A N   1 
ATOM   1393 C  CA  . LYS   A 1 179 ? -2.979  10.742  8.322   1.00 17.66 ? 192 LYS   A CA  1 
ATOM   1394 C  C   . LYS   A 1 179 ? -2.877  9.634   9.376   1.00 16.73 ? 192 LYS   A C   1 
ATOM   1395 O  O   . LYS   A 1 179 ? -3.611  9.629   10.346  1.00 16.57 ? 192 LYS   A O   1 
ATOM   1396 C  CB  . LYS   A 1 179 ? -2.339  12.018  8.885   1.00 18.22 ? 192 LYS   A CB  1 
ATOM   1397 C  CG  . LYS   A 1 179 ? -2.217  13.121  7.855   1.00 19.92 ? 192 LYS   A CG  1 
ATOM   1398 C  CD  . LYS   A 1 179 ? -1.664  14.414  8.359   1.00 23.06 ? 192 LYS   A CD  1 
ATOM   1399 C  CE  . LYS   A 1 179 ? -2.124  15.558  7.465   1.00 30.17 ? 192 LYS   A CE  1 
ATOM   1400 N  NZ  . LYS   A 1 179 ? -1.133  16.663  7.437   1.00 35.32 ? 192 LYS   A NZ  1 
ATOM   1401 N  N   . GLY   A 1 180 ? -1.882  8.753   9.257   1.00 18.11 ? 193 GLY   A N   1 
ATOM   1402 C  CA  . GLY   A 1 180 ? -1.732  7.639   10.202  1.00 16.67 ? 193 GLY   A CA  1 
ATOM   1403 C  C   . GLY   A 1 180 ? -2.546  6.405   9.774   1.00 16.22 ? 193 GLY   A C   1 
ATOM   1404 O  O   . GLY   A 1 180 ? -2.244  5.280   10.202  1.00 15.13 ? 193 GLY   A O   1 
ATOM   1405 N  N   . ASP   A 1 181 ? -3.561  6.604   8.904   1.00 15.34 ? 194 ASP   A N   1 
ATOM   1406 C  CA  . ASP   A 1 181 ? -4.397  5.472   8.446   1.00 13.30 ? 194 ASP   A CA  1 
ATOM   1407 C  C   . ASP   A 1 181 ? -3.829  4.784   7.198   1.00 13.01 ? 194 ASP   A C   1 
ATOM   1408 O  O   . ASP   A 1 181 ? -4.261  3.694   6.804   1.00 13.36 ? 194 ASP   A O   1 
ATOM   1409 C  CB  . ASP   A 1 181 ? -5.839  5.886   8.234   1.00 13.24 ? 194 ASP   A CB  1 
ATOM   1410 C  CG  . ASP   A 1 181 ? -6.574  6.357   9.485   1.00 16.79 ? 194 ASP   A CG  1 
ATOM   1411 O  OD1 . ASP   A 1 181 ? -6.470  5.656   10.511  1.00 18.91 ? 194 ASP   A OD1 1 
ATOM   1412 O  OD2 . ASP   A 1 181 ? -7.400  7.345   9.397   1.00 16.56 ? 194 ASP   A OD2 1 
ATOM   1413 N  N   . SER   A 1 182 ? -2.755  5.355   6.631   1.00 15.91 ? 195 SER   A N   1 
ATOM   1414 C  CA  . SER   A 1 182 ? -2.029  4.782   5.511   1.00 16.67 ? 195 SER   A CA  1 
ATOM   1415 C  C   . SER   A 1 182 ? -1.838  3.291   5.671   1.00 14.47 ? 195 SER   A C   1 
ATOM   1416 O  O   . SER   A 1 182 ? -1.559  2.811   6.768   1.00 14.88 ? 195 SER   A O   1 
ATOM   1417 C  CB  . SER   A 1 182 ? -0.668  5.465   5.353   1.00 20.03 ? 195 SER   A CB  1 
ATOM   1418 O  OG  . SER   A 1 182 ? -0.859  6.843   5.120   1.00 21.76 ? 195 SER   A OG  1 
ATOM   1419 N  N   . GLY   A 1 183 ? -2.003  2.571   4.567   1.00 15.59 ? 196 GLY   A N   1 
ATOM   1420 C  CA  . GLY   A 1 183 ? -1.713  1.143   4.509   1.00 16.51 ? 196 GLY   A CA  1 
ATOM   1421 C  C   . GLY   A 1 183 ? -2.860  0.247   5.006   1.00 15.92 ? 196 GLY   A C   1 
ATOM   1422 O  O   . GLY   A 1 183 ? -2.874  -0.955  4.749   1.00 16.25 ? 196 GLY   A O   1 
ATOM   1423 N  N   . GLY   A 1 184 ? -3.807  0.812   5.743   1.00 15.65 ? 197 GLY   A N   1 
ATOM   1424 C  CA  . GLY   A 1 184 ? -4.935  0.025   6.184   1.00 16.33 ? 197 GLY   A CA  1 
ATOM   1425 C  C   . GLY   A 1 184 ? -5.843  -0.350  5.007   1.00 17.80 ? 197 GLY   A C   1 
ATOM   1426 O  O   . GLY   A 1 184 ? -5.879  0.336   3.979   1.00 17.52 ? 197 GLY   A O   1 
ATOM   1427 N  N   . PRO   A 1 185 ? -6.576  -1.474  5.146   1.00 16.33 ? 198 PRO   A N   1 
ATOM   1428 C  CA  . PRO   A 1 185 ? -7.431  -1.960  4.100   1.00 17.07 ? 198 PRO   A CA  1 
ATOM   1429 C  C   . PRO   A 1 185 ? -8.788  -1.296  4.119   1.00 16.15 ? 198 PRO   A C   1 
ATOM   1430 O  O   . PRO   A 1 185 ? -9.241  -0.906  5.170   1.00 14.99 ? 198 PRO   A O   1 
ATOM   1431 C  CB  . PRO   A 1 185 ? -7.595  -3.437  4.451   1.00 18.43 ? 198 PRO   A CB  1 
ATOM   1432 C  CG  . PRO   A 1 185 ? -7.579  -3.422  5.965   1.00 17.81 ? 198 PRO   A CG  1 
ATOM   1433 C  CD  . PRO   A 1 185 ? -6.647  -2.311  6.363   1.00 16.64 ? 198 PRO   A CD  1 
ATOM   1434 N  N   . LEU   A 1 186 ? -9.339  -1.073  2.922   1.00 17.38 ? 199 LEU   A N   1 
ATOM   1435 C  CA  . LEU   A 1 186 ? -10.750 -0.794  2.723   1.00 17.21 ? 199 LEU   A CA  1 
ATOM   1436 C  C   . LEU   A 1 186 ? -11.498 -2.092  2.369   1.00 19.47 ? 199 LEU   A C   1 
ATOM   1437 O  O   . LEU   A 1 186 ? -11.177 -2.744  1.375   1.00 18.24 ? 199 LEU   A O   1 
ATOM   1438 C  CB  . LEU   A 1 186 ? -10.875 0.206   1.562   1.00 16.62 ? 199 LEU   A CB  1 
ATOM   1439 C  CG  . LEU   A 1 186 ? -12.308 0.616   1.234   1.00 14.78 ? 199 LEU   A CG  1 
ATOM   1440 C  CD1 . LEU   A 1 186 ? -12.800 1.579   2.317   1.00 16.25 ? 199 LEU   A CD1 1 
ATOM   1441 C  CD2 . LEU   A 1 186 ? -12.358 1.289   -0.146  1.00 14.16 ? 199 LEU   A CD2 1 
ATOM   1442 N  N   . LEU   A 1 187 ? -12.517 -2.448  3.157   1.00 21.17 ? 200 LEU   A N   1 
ATOM   1443 C  CA  . LEU   A 1 187 ? -13.303 -3.621  2.865   1.00 23.82 ? 200 LEU   A CA  1 
ATOM   1444 C  C   . LEU   A 1 187 ? -14.639 -3.151  2.342   1.00 24.50 ? 200 LEU   A C   1 
ATOM   1445 O  O   . LEU   A 1 187 ? -15.210 -2.170  2.816   1.00 28.72 ? 200 LEU   A O   1 
ATOM   1446 C  CB  . LEU   A 1 187 ? -13.487 -4.521  4.104   1.00 25.57 ? 200 LEU   A CB  1 
ATOM   1447 C  CG  . LEU   A 1 187 ? -12.284 -5.370  4.468   1.00 24.10 ? 200 LEU   A CG  1 
ATOM   1448 C  CD1 . LEU   A 1 187 ? -11.229 -4.488  5.093   1.00 27.34 ? 200 LEU   A CD1 1 
ATOM   1449 C  CD2 . LEU   A 1 187 ? -12.651 -6.501  5.410   1.00 27.05 ? 200 LEU   A CD2 1 
ATOM   1450 N  N   . CYS   A 1 188 ? -15.111 -3.908  1.360   1.00 23.60 ? 201 CYS   A N   1 
ATOM   1451 C  CA  . CYS   A 1 188 ? -16.439 -3.756  0.774   1.00 25.54 ? 201 CYS   A CA  1 
ATOM   1452 C  C   . CYS   A 1 188 ? -17.045 -5.165  0.838   1.00 25.88 ? 201 CYS   A C   1 
ATOM   1453 O  O   . CYS   A 1 188 ? -16.365 -6.153  0.478   1.00 23.34 ? 201 CYS   A O   1 
ATOM   1454 C  CB  . CYS   A 1 188 ? -16.331 -3.146  -0.628  1.00 26.59 ? 201 CYS   A CB  1 
ATOM   1455 S  SG  . CYS   A 1 188 ? -15.225 -1.705  -0.784  1.00 27.67 ? 201 CYS   A SG  1 
ATOM   1456 N  N   . ALA   A 1 189 ? -18.183 -5.312  1.525   1.00 27.02 ? 202 ALA   A N   1 
ATOM   1457 C  CA  . ALA   A 1 189 ? -18.735 -6.647  1.723   1.00 30.72 ? 202 ALA   A CA  1 
ATOM   1458 C  C   . ALA   A 1 189 ? -17.670 -7.608  2.239   1.00 33.92 ? 202 ALA   A C   1 
ATOM   1459 O  O   . ALA   A 1 189 ? -17.468 -8.666  1.655   1.00 33.45 ? 202 ALA   A O   1 
ATOM   1460 C  CB  . ALA   A 1 189 ? -19.245 -7.180  0.409   1.00 31.37 ? 202 ALA   A CB  1 
ATOM   1461 N  N   . GLY   A 1 190 ? -16.953 -7.235  3.297   1.00 32.38 ? 207 GLY   A N   1 
ATOM   1462 C  CA  . GLY   A 1 190 ? -16.101 -8.208  3.955   1.00 30.12 ? 207 GLY   A CA  1 
ATOM   1463 C  C   . GLY   A 1 190 ? -14.908 -8.605  3.093   1.00 31.27 ? 207 GLY   A C   1 
ATOM   1464 O  O   . GLY   A 1 190 ? -14.046 -9.350  3.575   1.00 28.32 ? 207 GLY   A O   1 
ATOM   1465 N  N   . VAL   A 1 191 ? -14.787 -7.978  1.897   1.00 33.57 ? 208 VAL   A N   1 
ATOM   1466 C  CA  . VAL   A 1 191 ? -13.665 -8.235  1.009   1.00 30.24 ? 208 VAL   A CA  1 
ATOM   1467 C  C   . VAL   A 1 191 ? -12.804 -6.990  0.844   1.00 26.00 ? 208 VAL   A C   1 
ATOM   1468 O  O   . VAL   A 1 191 ? -13.313 -5.913  0.511   1.00 28.10 ? 208 VAL   A O   1 
ATOM   1469 C  CB  . VAL   A 1 191 ? -14.144 -8.740  -0.367  1.00 31.09 ? 208 VAL   A CB  1 
ATOM   1470 C  CG1 . VAL   A 1 191 ? -12.999 -8.848  -1.374  0.50 27.20 ? 208 VAL   A CG1 1 
ATOM   1471 C  CG2 . VAL   A 1 191 ? -14.865 -10.078 -0.218  0.50 30.29 ? 208 VAL   A CG2 1 
ATOM   1472 N  N   . ALA   A 1 192 ? -11.497 -7.230  0.924   1.00 21.74 ? 209 ALA   A N   1 
ATOM   1473 C  CA  . ALA   A 1 192 ? -10.473 -6.199  0.833   1.00 25.90 ? 209 ALA   A CA  1 
ATOM   1474 C  C   . ALA   A 1 192 ? -10.366 -5.665  -0.592  1.00 25.14 ? 209 ALA   A C   1 
ATOM   1475 O  O   . ALA   A 1 192 ? -9.985  -6.417  -1.480  1.00 28.83 ? 209 ALA   A O   1 
ATOM   1476 C  CB  . ALA   A 1 192 ? -9.151  -6.774  1.279   1.00 22.32 ? 209 ALA   A CB  1 
ATOM   1477 N  N   . GLN   A 1 193 ? -10.745 -4.402  -0.815  1.00 21.71 ? 210 GLN   A N   1 
ATOM   1478 C  CA  . GLN   A 1 193 ? -10.693 -3.809  -2.135  1.00 20.14 ? 210 GLN   A CA  1 
ATOM   1479 C  C   . GLN   A 1 193 ? -9.636  -2.704  -2.275  1.00 21.16 ? 210 GLN   A C   1 
ATOM   1480 O  O   . GLN   A 1 193 ? -9.207  -2.438  -3.392  1.00 20.39 ? 210 GLN   A O   1 
ATOM   1481 C  CB  . GLN   A 1 193 ? -12.077 -3.249  -2.474  1.00 23.03 ? 210 GLN   A CB  1 
ATOM   1482 C  CG  . GLN   A 1 193 ? -13.161 -4.303  -2.697  1.00 24.68 ? 210 GLN   A CG  1 
ATOM   1483 C  CD  . GLN   A 1 193 ? -13.042 -5.118  -3.965  0.50 20.92 ? 210 GLN   A CD  1 
ATOM   1484 O  OE1 . GLN   A 1 193 ? -13.896 -5.949  -4.285  0.50 18.04 ? 210 GLN   A OE1 1 
ATOM   1485 N  NE2 . GLN   A 1 193 ? -11.962 -4.917  -4.688  0.50 21.12 ? 210 GLN   A NE2 1 
ATOM   1486 N  N   . GLY   A 1 194 ? -9.295  -1.978  -1.201  1.00 18.10 ? 211 GLY   A N   1 
ATOM   1487 C  CA  . GLY   A 1 194 ? -8.411  -0.823  -1.324  1.00 18.96 ? 211 GLY   A CA  1 
ATOM   1488 C  C   . GLY   A 1 194 ? -7.378  -0.769  -0.200  1.00 17.43 ? 211 GLY   A C   1 
ATOM   1489 O  O   . GLY   A 1 194 ? -7.516  -1.503  0.774   1.00 23.73 ? 211 GLY   A O   1 
ATOM   1490 N  N   . ILE   A 1 195 ? -6.405  0.128   -0.336  1.00 15.59 ? 212 ILE   A N   1 
ATOM   1491 C  CA  . ILE   A 1 195 ? -5.390  0.447   0.662   1.00 16.99 ? 212 ILE   A CA  1 
ATOM   1492 C  C   . ILE   A 1 195 ? -5.316  1.966   0.768   1.00 17.02 ? 212 ILE   A C   1 
ATOM   1493 O  O   . ILE   A 1 195 ? -5.106  2.620   -0.257  1.00 17.74 ? 212 ILE   A O   1 
ATOM   1494 C  CB  . ILE   A 1 195 ? -4.007  -0.141  0.284   1.00 15.91 ? 212 ILE   A CB  1 
ATOM   1495 C  CG1 . ILE   A 1 195 ? -4.081  -1.634  -0.050  1.00 18.57 ? 212 ILE   A CG1 1 
ATOM   1496 C  CG2 . ILE   A 1 195 ? -2.990  0.132   1.375   1.00 14.37 ? 212 ILE   A CG2 1 
ATOM   1497 C  CD1 . ILE   A 1 195 ? -2.755  -2.223  -0.481  1.00 20.58 ? 212 ILE   A CD1 1 
ATOM   1498 N  N   . VAL   A 1 196 ? -5.486  2.520   1.982   1.00 15.72 ? 213 VAL   A N   1 
ATOM   1499 C  CA  . VAL   A 1 196 ? -5.423  3.963   2.170   1.00 14.31 ? 213 VAL   A CA  1 
ATOM   1500 C  C   . VAL   A 1 196 ? -4.104  4.439   1.569   1.00 15.07 ? 213 VAL   A C   1 
ATOM   1501 O  O   . VAL   A 1 196 ? -3.034  3.908   1.891   1.00 16.41 ? 213 VAL   A O   1 
ATOM   1502 C  CB  . VAL   A 1 196 ? -5.486  4.342   3.657   1.00 13.97 ? 213 VAL   A CB  1 
ATOM   1503 C  CG1 . VAL   A 1 196 ? -5.281  5.812   3.915   1.00 14.52 ? 213 VAL   A CG1 1 
ATOM   1504 C  CG2 . VAL   A 1 196 ? -6.743  3.878   4.350   1.00 14.11 ? 213 VAL   A CG2 1 
ATOM   1505 N  N   . SER   A 1 197 ? -4.167  5.437   0.701   1.00 14.73 ? 214 SER   A N   1 
ATOM   1506 C  CA  . SER   A 1 197 ? -2.953  5.991   0.092   1.00 17.06 ? 214 SER   A CA  1 
ATOM   1507 C  C   . SER   A 1 197 ? -2.789  7.460   0.476   1.00 16.27 ? 214 SER   A C   1 
ATOM   1508 O  O   . SER   A 1 197 ? -1.884  7.800   1.240   1.00 16.71 ? 214 SER   A O   1 
ATOM   1509 C  CB  . SER   A 1 197 ? -2.907  5.748   -1.413  1.00 18.94 ? 214 SER   A CB  1 
ATOM   1510 O  OG  . SER   A 1 197 ? -1.617  6.125   -1.966  1.00 18.51 ? 214 SER   A OG  1 
ATOM   1511 N  N   . TYR   A 1 198 ? -3.639  8.340   -0.053  1.00 17.05 ? 215 TYR   A N   1 
ATOM   1512 C  CA  . TYR   A 1 198 ? -3.483  9.762   0.195   1.00 20.54 ? 215 TYR   A CA  1 
ATOM   1513 C  C   . TYR   A 1 198 ? -4.790  10.511  -0.034  1.00 22.36 ? 215 TYR   A C   1 
ATOM   1514 O  O   . TYR   A 1 198 ? -5.765  9.931   -0.501  1.00 17.59 ? 215 TYR   A O   1 
ATOM   1515 C  CB  . TYR   A 1 198 ? -2.423  10.412  -0.687  1.00 22.99 ? 215 TYR   A CB  1 
ATOM   1516 C  CG  . TYR   A 1 198 ? -2.733  10.490  -2.182  1.00 24.00 ? 215 TYR   A CG  1 
ATOM   1517 C  CD1 . TYR   A 1 198 ? -2.394  9.452   -3.049  1.00 27.58 ? 215 TYR   A CD1 1 
ATOM   1518 C  CD2 . TYR   A 1 198 ? -3.223  11.650  -2.754  1.00 25.27 ? 215 TYR   A CD2 1 
ATOM   1519 C  CE1 . TYR   A 1 198 ? -2.622  9.531   -4.419  1.00 26.52 ? 215 TYR   A CE1 1 
ATOM   1520 C  CE2 . TYR   A 1 198 ? -3.456  11.740  -4.119  1.00 30.94 ? 215 TYR   A CE2 1 
ATOM   1521 C  CZ  . TYR   A 1 198 ? -3.149  10.684  -4.965  1.00 28.53 ? 215 TYR   A CZ  1 
ATOM   1522 O  OH  . TYR   A 1 198 ? -3.407  10.748  -6.317  1.00 25.56 ? 215 TYR   A OH  1 
ATOM   1523 N  N   . GLY   A 1 199 ? -4.754  11.823  0.275   1.00 20.66 ? 216 GLY   A N   1 
ATOM   1524 C  CA  . GLY   A 1 199 ? -5.908  12.676  0.056   1.00 23.69 ? 216 GLY   A CA  1 
ATOM   1525 C  C   . GLY   A 1 199 ? -5.492  14.124  0.259   1.00 21.54 ? 216 GLY   A C   1 
ATOM   1526 O  O   . GLY   A 1 199 ? -4.302  14.399  0.207   1.00 19.29 ? 216 GLY   A O   1 
ATOM   1527 N  N   . ARG   A 1 200 ? -6.472  14.976  0.590   1.00 21.79 ? 217 ARG   A N   1 
ATOM   1528 C  CA  . ARG   A 1 200 ? -6.209  16.361  0.917   1.00 22.72 ? 217 ARG   A CA  1 
ATOM   1529 C  C   . ARG   A 1 200 ? -5.765  16.501  2.368   1.00 22.27 ? 217 ARG   A C   1 
ATOM   1530 O  O   . ARG   A 1 200 ? -6.376  15.953  3.281   1.00 22.53 ? 217 ARG   A O   1 
ATOM   1531 C  CB  . ARG   A 1 200 ? -7.448  17.225  0.704   1.00 23.33 ? 217 ARG   A CB  1 
ATOM   1532 C  CG  . ARG   A 1 200 ? -7.803  17.463  -0.764  1.00 25.20 ? 217 ARG   A CG  1 
ATOM   1533 C  CD  . ARG   A 1 200 ? -9.219  17.997  -0.879  1.00 25.56 ? 217 ARG   A CD  1 
ATOM   1534 N  NE  . ARG   A 1 200 ? -9.174  19.335  -0.371  1.00 26.75 ? 217 ARG   A NE  1 
ATOM   1535 C  CZ  . ARG   A 1 200 ? -8.777  20.384  -1.087  1.00 36.36 ? 217 ARG   A CZ  1 
ATOM   1536 N  NH1 . ARG   A 1 200 ? -8.467  20.255  -2.369  1.00 35.99 ? 217 ARG   A NH1 1 
ATOM   1537 N  NH2 . ARG   A 1 200 ? -8.706  21.571  -0.518  1.00 37.80 ? 217 ARG   A NH2 1 
ATOM   1538 N  N   . SER   A 1 201 ? -4.765  17.335  2.580   1.00 22.85 ? 218 SER   A N   1 
ATOM   1539 C  CA  . SER   A 1 201 ? -4.292  17.577  3.927   1.00 24.59 ? 218 SER   A CA  1 
ATOM   1540 C  C   . SER   A 1 201 ? -5.334  18.345  4.724   1.00 24.07 ? 218 SER   A C   1 
ATOM   1541 O  O   . SER   A 1 201 ? -5.293  18.238  5.931   1.00 25.12 ? 218 SER   A O   1 
ATOM   1542 C  CB  . SER   A 1 201 ? -2.919  18.208  3.979   1.00 28.06 ? 218 SER   A CB  1 
ATOM   1543 O  OG  . SER   A 1 201 ? -2.845  19.368  3.194   1.00 33.20 ? 218 SER   A OG  1 
ATOM   1544 N  N   . ASP   A 1 202 ? -6.379  18.926  4.112   1.00 23.06 ? 219 ASP   A N   1 
ATOM   1545 C  CA  . ASP   A 1 202 ? -7.458  19.514  4.897   1.00 22.59 ? 219 ASP   A CA  1 
ATOM   1546 C  C   . ASP   A 1 202 ? -8.576  18.489  5.120   1.00 21.40 ? 219 ASP   A C   1 
ATOM   1547 O  O   . ASP   A 1 202 ? -9.675  18.792  5.608   1.00 17.83 ? 219 ASP   A O   1 
ATOM   1548 C  CB  . ASP   A 1 202 ? -7.956  20.810  4.260   1.00 25.91 ? 219 ASP   A CB  1 
ATOM   1549 C  CG  . ASP   A 1 202 ? -8.704  20.564  2.959   1.00 28.72 ? 219 ASP   A CG  1 
ATOM   1550 O  OD1 . ASP   A 1 202 ? -8.313  19.669  2.272   1.00 33.12 ? 219 ASP   A OD1 1 
ATOM   1551 O  OD2 . ASP   A 1 202 ? -9.660  21.278  2.667   1.00 32.77 ? 219 ASP   A OD2 1 
ATOM   1552 N  N   . ALA   A 1 203 ? -8.313  17.254  4.728   1.00 20.98 ? 220 ALA   A N   1 
ATOM   1553 C  CA  . ALA   A 1 203 ? -9.223  16.183  5.071   1.00 24.75 ? 220 ALA   A CA  1 
ATOM   1554 C  C   . ALA   A 1 203 ? -10.556 16.182  4.304   1.00 22.27 ? 220 ALA   A C   1 
ATOM   1555 O  O   . ALA   A 1 203 ? -11.394 15.344  4.639   1.00 21.67 ? 220 ALA   A O   1 
ATOM   1556 C  CB  . ALA   A 1 203 ? -9.463  16.218  6.556   1.00 28.91 ? 220 ALA   A CB  1 
ATOM   1557 N  N   . LYS   A 1 204 ? -10.794 17.080  3.319   1.00 23.52 ? 221 LYS   A N   1 
ATOM   1558 C  CA  . LYS   A 1 204 ? -12.052 17.050  2.550   1.00 19.61 ? 221 LYS   A CA  1 
ATOM   1559 C  C   . LYS   A 1 204 ? -12.057 15.789  1.661   1.00 17.55 ? 221 LYS   A C   1 
ATOM   1560 O  O   . LYS   A 1 204 ? -11.173 15.578  0.855   1.00 16.15 ? 221 LYS   A O   1 
ATOM   1561 C  CB  . LYS   A 1 204 ? -12.265 18.264  1.629   1.00 20.64 ? 221 LYS   A CB  1 
ATOM   1562 C  CG  . LYS   A 1 204 ? -13.649 18.382  0.955   1.00 24.21 ? 221 LYS   A CG  1 
ATOM   1563 C  CD  . LYS   A 1 204 ? -14.782 18.629  1.950   1.00 28.87 ? 221 LYS   A CD  1 
ATOM   1564 C  CE  . LYS   A 1 204 ? -16.051 19.136  1.275   1.00 32.02 ? 221 LYS   A CE  1 
ATOM   1565 N  NZ  . LYS   A 1 204 ? -17.199 19.251  2.216   1.00 29.46 ? 221 LYS   A NZ  1 
ATOM   1566 N  N   . PRO   A 1 205 ? -12.979 14.838  1.881   1.00 16.63 ? 224 PRO   A N   1 
ATOM   1567 C  CA  . PRO   A 1 205 ? -13.066 13.671  1.039   1.00 17.99 ? 224 PRO   A CA  1 
ATOM   1568 C  C   . PRO   A 1 205 ? -13.385 14.078  -0.388  1.00 22.27 ? 224 PRO   A C   1 
ATOM   1569 O  O   . PRO   A 1 205 ? -13.934 15.177  -0.563  1.00 20.21 ? 224 PRO   A O   1 
ATOM   1570 C  CB  . PRO   A 1 205 ? -14.294 12.931  1.533   1.00 15.43 ? 224 PRO   A CB  1 
ATOM   1571 C  CG  . PRO   A 1 205 ? -14.553 13.521  2.875   1.00 16.99 ? 224 PRO   A CG  1 
ATOM   1572 C  CD  . PRO   A 1 205 ? -14.077 14.927  2.839   1.00 17.08 ? 224 PRO   A CD  1 
ATOM   1573 N  N   . PRO   A 1 206 ? -13.260 13.167  -1.386  1.00 20.74 ? 225 PRO   A N   1 
ATOM   1574 C  CA  . PRO   A 1 206 ? -12.859 11.784  -1.161  1.00 20.53 ? 225 PRO   A CA  1 
ATOM   1575 C  C   . PRO   A 1 206 ? -11.346 11.660  -0.966  1.00 16.60 ? 225 PRO   A C   1 
ATOM   1576 O  O   . PRO   A 1 206 ? -10.642 12.617  -1.181  1.00 17.98 ? 225 PRO   A O   1 
ATOM   1577 C  CB  . PRO   A 1 206 ? -13.237 11.092  -2.470  1.00 20.21 ? 225 PRO   A CB  1 
ATOM   1578 C  CG  . PRO   A 1 206 ? -13.052 12.214  -3.502  1.00 22.22 ? 225 PRO   A CG  1 
ATOM   1579 C  CD  . PRO   A 1 206 ? -13.519 13.467  -2.806  1.00 22.53 ? 225 PRO   A CD  1 
ATOM   1580 N  N   . ALA   A 1 207 ? -10.859 10.487  -0.569  1.00 18.02 ? 226 ALA   A N   1 
ATOM   1581 C  CA  . ALA   A 1 207 ? -9.426  10.209  -0.649  1.00 17.88 ? 226 ALA   A CA  1 
ATOM   1582 C  C   . ALA   A 1 207 ? -9.155  9.125   -1.696  1.00 17.54 ? 226 ALA   A C   1 
ATOM   1583 O  O   . ALA   A 1 207 ? -10.086 8.536   -2.255  1.00 16.33 ? 226 ALA   A O   1 
ATOM   1584 C  CB  . ALA   A 1 207 ? -8.889  9.821   0.718   1.00 18.18 ? 226 ALA   A CB  1 
ATOM   1585 N  N   . VAL   A 1 208 ? -7.857  8.833   -1.867  1.00 15.41 ? 227 VAL   A N   1 
ATOM   1586 C  CA  . VAL   A 1 208 ? -7.323  7.941   -2.861  1.00 17.77 ? 227 VAL   A CA  1 
ATOM   1587 C  C   . VAL   A 1 208 ? -6.747  6.711   -2.145  1.00 20.32 ? 227 VAL   A C   1 
ATOM   1588 O  O   . VAL   A 1 208 ? -5.952  6.796   -1.204  1.00 17.91 ? 227 VAL   A O   1 
ATOM   1589 C  CB  . VAL   A 1 208 ? -6.242  8.691   -3.673  1.00 17.71 ? 227 VAL   A CB  1 
ATOM   1590 C  CG1 . VAL   A 1 208 ? -5.474  7.782   -4.625  1.00 15.73 ? 227 VAL   A CG1 1 
ATOM   1591 C  CG2 . VAL   A 1 208 ? -6.834  9.909   -4.400  1.00 15.96 ? 227 VAL   A CG2 1 
ATOM   1592 N  N   . PHE   A 1 209 ? -7.208  5.556   -2.599  1.00 19.37 ? 228 PHE   A N   1 
ATOM   1593 C  CA  . PHE   A 1 209 ? -6.714  4.281   -2.127  1.00 20.45 ? 228 PHE   A CA  1 
ATOM   1594 C  C   . PHE   A 1 209 ? -6.164  3.503   -3.328  1.00 18.07 ? 228 PHE   A C   1 
ATOM   1595 O  O   . PHE   A 1 209 ? -6.670  3.671   -4.452  1.00 18.96 ? 228 PHE   A O   1 
ATOM   1596 C  CB  . PHE   A 1 209 ? -7.886  3.489   -1.528  1.00 19.07 ? 228 PHE   A CB  1 
ATOM   1597 C  CG  . PHE   A 1 209 ? -8.489  3.981   -0.232  1.00 18.20 ? 228 PHE   A CG  1 
ATOM   1598 C  CD1 . PHE   A 1 209 ? -8.998  5.262   -0.101  1.00 17.89 ? 228 PHE   A CD1 1 
ATOM   1599 C  CD2 . PHE   A 1 209 ? -8.563  3.127   0.864   1.00 19.62 ? 228 PHE   A CD2 1 
ATOM   1600 C  CE1 . PHE   A 1 209 ? -9.552  5.688   1.101   1.00 20.09 ? 228 PHE   A CE1 1 
ATOM   1601 C  CE2 . PHE   A 1 209 ? -9.132  3.544   2.058   1.00 18.82 ? 228 PHE   A CE2 1 
ATOM   1602 C  CZ  . PHE   A 1 209 ? -9.654  4.816   2.169   1.00 18.57 ? 228 PHE   A CZ  1 
ATOM   1603 N  N   . THR   A 1 210 ? -5.220  2.600   -3.060  1.00 16.91 ? 229 THR   A N   1 
ATOM   1604 C  CA  . THR   A 1 210 ? -4.690  1.677   -4.039  1.00 18.11 ? 229 THR   A CA  1 
ATOM   1605 C  C   . THR   A 1 210 ? -5.753  0.637   -4.381  1.00 17.55 ? 229 THR   A C   1 
ATOM   1606 O  O   . THR   A 1 210 ? -6.376  0.098   -3.476  1.00 17.77 ? 229 THR   A O   1 
ATOM   1607 C  CB  . THR   A 1 210 ? -3.433  0.999   -3.512  1.00 18.63 ? 229 THR   A CB  1 
ATOM   1608 O  OG1 . THR   A 1 210 ? -2.532  2.029   -3.111  1.00 19.88 ? 229 THR   A OG1 1 
ATOM   1609 C  CG2 . THR   A 1 210 ? -2.749  0.109   -4.525  1.00 19.81 ? 229 THR   A CG2 1 
ATOM   1610 N  N   . ARG   A 1 211 ? -5.979  0.394   -5.684  1.00 18.26 ? 230 ARG   A N   1 
ATOM   1611 C  CA  . ARG   A 1 211 ? -6.903  -0.639  -6.138  1.00 18.65 ? 230 ARG   A CA  1 
ATOM   1612 C  C   . ARG   A 1 211 ? -6.187  -1.992  -6.097  1.00 19.22 ? 230 ARG   A C   1 
ATOM   1613 O  O   . ARG   A 1 211 ? -5.322  -2.250  -6.952  1.00 18.76 ? 230 ARG   A O   1 
ATOM   1614 C  CB  . ARG   A 1 211 ? -7.439  -0.372  -7.555  1.00 17.71 ? 230 ARG   A CB  1 
ATOM   1615 C  CG  . ARG   A 1 211 ? -8.540  -1.332  -7.998  1.00 19.63 ? 230 ARG   A CG  1 
ATOM   1616 C  CD  . ARG   A 1 211 ? -8.894  -1.222  -9.481  1.00 20.20 ? 230 ARG   A CD  1 
ATOM   1617 N  NE  . ARG   A 1 211 ? -9.595  0.024   -9.813  1.00 19.61 ? 230 ARG   A NE  1 
ATOM   1618 C  CZ  . ARG   A 1 211 ? -10.906 0.199   -9.606  1.00 24.89 ? 230 ARG   A CZ  1 
ATOM   1619 N  NH1 . ARG   A 1 211 ? -11.599 -0.766  -9.022  1.00 23.30 ? 230 ARG   A NH1 1 
ATOM   1620 N  NH2 . ARG   A 1 211 ? -11.538 1.337   -9.938  1.00 26.42 ? 230 ARG   A NH2 1 
ATOM   1621 N  N   . ILE   A 1 212 ? -6.553  -2.807  -5.091  1.00 18.25 ? 231 ILE   A N   1 
ATOM   1622 C  CA  . ILE   A 1 212 ? -5.882  -4.074  -4.812  1.00 21.11 ? 231 ILE   A CA  1 
ATOM   1623 C  C   . ILE   A 1 212 ? -5.991  -5.072  -5.979  1.00 21.30 ? 231 ILE   A C   1 
ATOM   1624 O  O   . ILE   A 1 212 ? -5.013  -5.736  -6.284  1.00 20.33 ? 231 ILE   A O   1 
ATOM   1625 C  CB  . ILE   A 1 212 ? -6.396  -4.694  -3.505  1.00 19.13 ? 231 ILE   A CB  1 
ATOM   1626 C  CG1 . ILE   A 1 212 ? -6.040  -3.882  -2.247  1.00 19.78 ? 231 ILE   A CG1 1 
ATOM   1627 C  CG2 . ILE   A 1 212 ? -5.890  -6.110  -3.390  1.00 18.55 ? 231 ILE   A CG2 1 
ATOM   1628 C  CD1 . ILE   A 1 212 ? -6.735  -4.392  -0.985  1.00 20.51 ? 231 ILE   A CD1 1 
ATOM   1629 N  N   . SER   A 1 213 ? -7.136  -5.110  -6.668  1.00 21.95 ? 232 SER   A N   1 
ATOM   1630 C  CA  . SER   A 1 213 ? -7.355  -6.052  -7.759  1.00 23.18 ? 232 SER   A CA  1 
ATOM   1631 C  C   . SER   A 1 213 ? -6.332  -5.842  -8.868  1.00 21.17 ? 232 SER   A C   1 
ATOM   1632 O  O   . SER   A 1 213 ? -5.741  -6.791  -9.357  1.00 25.33 ? 232 SER   A O   1 
ATOM   1633 C  CB  . SER   A 1 213 ? -8.729  -5.913  -8.297  1.00 21.76 ? 232 SER   A CB  1 
ATOM   1634 O  OG  . SER   A 1 213 ? -8.795  -4.634  -8.912  1.00 22.06 ? 232 SER   A OG  1 
ATOM   1635 N  N   . HIS   A 1 214 ? -5.937  -4.606  -9.125  1.00 23.40 ? 233 HIS   A N   1 
ATOM   1636 C  CA  . HIS   A 1 214 ? -4.965  -4.377  -10.181 1.00 25.21 ? 233 HIS   A CA  1 
ATOM   1637 C  C   . HIS   A 1 214 ? -3.652  -5.100  -9.879  1.00 25.94 ? 233 HIS   A C   1 
ATOM   1638 O  O   . HIS   A 1 214 ? -2.923  -5.476  -10.814 1.00 27.13 ? 233 HIS   A O   1 
ATOM   1639 C  CB  . HIS   A 1 214 ? -4.743  -2.887  -10.402 1.00 25.94 ? 233 HIS   A CB  1 
ATOM   1640 C  CG  . HIS   A 1 214 ? -3.792  -2.564  -11.494 1.00 28.98 ? 233 HIS   A CG  1 
ATOM   1641 N  ND1 . HIS   A 1 214 ? -4.161  -2.651  -12.809 1.00 33.26 ? 233 HIS   A ND1 1 
ATOM   1642 C  CD2 . HIS   A 1 214 ? -2.516  -2.132  -11.492 1.00 32.80 ? 233 HIS   A CD2 1 
ATOM   1643 C  CE1 . HIS   A 1 214 ? -3.150  -2.291  -13.565 1.00 30.86 ? 233 HIS   A CE1 1 
ATOM   1644 N  NE2 . HIS   A 1 214 ? -2.133  -1.979  -12.800 1.00 30.23 ? 233 HIS   A NE2 1 
ATOM   1645 N  N   . TYR   A 1 215 ? -3.324  -5.243  -8.580  1.00 24.99 ? 234 TYR   A N   1 
ATOM   1646 C  CA  . TYR   A 1 215 ? -1.995  -5.673  -8.159  1.00 23.29 ? 234 TYR   A CA  1 
ATOM   1647 C  C   . TYR   A 1 215 ? -1.949  -7.155  -7.795  1.00 22.17 ? 234 TYR   A C   1 
ATOM   1648 O  O   . TYR   A 1 215 ? -0.915  -7.632  -7.328  1.00 21.00 ? 234 TYR   A O   1 
ATOM   1649 C  CB  . TYR   A 1 215 ? -1.563  -4.820  -6.949  1.00 25.23 ? 234 TYR   A CB  1 
ATOM   1650 C  CG  . TYR   A 1 215 ? -1.361  -3.373  -7.377  1.00 22.21 ? 234 TYR   A CG  1 
ATOM   1651 C  CD1 . TYR   A 1 215 ? -0.205  -2.993  -8.029  1.00 20.14 ? 234 TYR   A CD1 1 
ATOM   1652 C  CD2 . TYR   A 1 215 ? -2.383  -2.443  -7.293  1.00 20.54 ? 234 TYR   A CD2 1 
ATOM   1653 C  CE1 . TYR   A 1 215 ? -0.028  -1.707  -8.495  1.00 20.02 ? 234 TYR   A CE1 1 
ATOM   1654 C  CE2 . TYR   A 1 215 ? -2.208  -1.148  -7.718  1.00 19.22 ? 234 TYR   A CE2 1 
ATOM   1655 C  CZ  . TYR   A 1 215 ? -1.038  -0.782  -8.356  1.00 19.99 ? 234 TYR   A CZ  1 
ATOM   1656 O  OH  . TYR   A 1 215 ? -0.847  0.483   -8.853  1.00 25.46 ? 234 TYR   A OH  1 
ATOM   1657 N  N   . ARG   A 1 216 ? -3.040  -7.885  -7.962  1.00 22.81 ? 235 ARG   A N   1 
ATOM   1658 C  CA  . ARG   A 1 216 ? -3.118  -9.294  -7.549  1.00 29.18 ? 235 ARG   A CA  1 
ATOM   1659 C  C   . ARG   A 1 216 ? -2.071  -10.221 -8.162  1.00 35.23 ? 235 ARG   A C   1 
ATOM   1660 O  O   . ARG   A 1 216 ? -1.671  -11.171 -7.501  1.00 37.68 ? 235 ARG   A O   1 
ATOM   1661 C  CB  . ARG   A 1 216 ? -4.462  -9.946  -7.908  1.00 31.28 ? 235 ARG   A CB  1 
ATOM   1662 C  CG  . ARG   A 1 216 ? -5.552  -9.654  -6.887  1.00 40.03 ? 235 ARG   A CG  1 
ATOM   1663 C  CD  . ARG   A 1 216 ? -5.229  -10.098 -5.448  1.00 46.27 ? 235 ARG   A CD  1 
ATOM   1664 N  NE  . ARG   A 1 216 ? -5.281  -11.552 -5.232  1.00 47.24 ? 235 ARG   A NE  1 
ATOM   1665 C  CZ  . ARG   A 1 216 ? -6.414  -12.268 -5.117  1.00 49.43 ? 235 ARG   A CZ  1 
ATOM   1666 N  NH1 . ARG   A 1 216 ? -7.616  -11.676 -5.181  1.00 36.46 ? 235 ARG   A NH1 1 
ATOM   1667 N  NH2 . ARG   A 1 216 ? -6.321  -13.579 -4.918  1.00 48.99 ? 235 ARG   A NH2 1 
ATOM   1668 N  N   . PRO   A 1 217 ? -1.654  -10.071 -9.440  1.00 35.80 ? 236 PRO   A N   1 
ATOM   1669 C  CA  . PRO   A 1 217 ? -0.572  -10.893 -9.954  1.00 32.54 ? 236 PRO   A CA  1 
ATOM   1670 C  C   . PRO   A 1 217 ? 0.762   -10.667 -9.251  1.00 29.92 ? 236 PRO   A C   1 
ATOM   1671 O  O   . PRO   A 1 217 ? 1.527   -11.610 -9.026  1.00 31.92 ? 236 PRO   A O   1 
ATOM   1672 C  CB  . PRO   A 1 217 ? -0.541  -10.573 -11.457 1.00 32.64 ? 236 PRO   A CB  1 
ATOM   1673 C  CG  . PRO   A 1 217 ? -1.884  -9.982  -11.766 1.00 36.12 ? 236 PRO   A CG  1 
ATOM   1674 C  CD  . PRO   A 1 217 ? -2.334  -9.291  -10.490 1.00 38.07 ? 236 PRO   A CD  1 
ATOM   1675 N  N   . TRP   A 1 218 ? 1.083   -9.399  -8.997  1.00 29.21 ? 237 TRP   A N   1 
ATOM   1676 C  CA  . TRP   A 1 218 ? 2.296   -9.070  -8.267  1.00 26.74 ? 237 TRP   A CA  1 
ATOM   1677 C  C   . TRP   A 1 218 ? 2.272   -9.650  -6.844  1.00 29.20 ? 237 TRP   A C   1 
ATOM   1678 O  O   . TRP   A 1 218 ? 3.285   -10.152 -6.375  1.00 29.37 ? 237 TRP   A O   1 
ATOM   1679 C  CB  . TRP   A 1 218 ? 2.481   -7.564  -8.262  1.00 27.64 ? 237 TRP   A CB  1 
ATOM   1680 C  CG  . TRP   A 1 218 ? 3.658   -7.133  -7.440  1.00 30.54 ? 237 TRP   A CG  1 
ATOM   1681 C  CD1 . TRP   A 1 218 ? 4.963   -7.147  -7.821  1.00 31.59 ? 237 TRP   A CD1 1 
ATOM   1682 C  CD2 . TRP   A 1 218 ? 3.643   -6.570  -6.117  1.00 27.30 ? 237 TRP   A CD2 1 
ATOM   1683 N  NE1 . TRP   A 1 218 ? 5.763   -6.678  -6.811  1.00 34.57 ? 237 TRP   A NE1 1 
ATOM   1684 C  CE2 . TRP   A 1 218 ? 4.982   -6.282  -5.771  1.00 28.83 ? 237 TRP   A CE2 1 
ATOM   1685 C  CE3 . TRP   A 1 218 ? 2.640   -6.266  -5.188  1.00 31.51 ? 237 TRP   A CE3 1 
ATOM   1686 C  CZ2 . TRP   A 1 218 ? 5.341   -5.768  -4.522  1.00 32.43 ? 237 TRP   A CZ2 1 
ATOM   1687 C  CZ3 . TRP   A 1 218 ? 2.988   -5.714  -3.966  1.00 26.98 ? 237 TRP   A CZ3 1 
ATOM   1688 C  CH2 . TRP   A 1 218 ? 4.321   -5.498  -3.632  1.00 27.48 ? 237 TRP   A CH2 1 
ATOM   1689 N  N   . ILE   A 1 219 ? 1.130   -9.529  -6.130  1.00 27.59 ? 238 ILE   A N   1 
ATOM   1690 C  CA  . ILE   A 1 219 ? 1.014   -10.081 -4.795  1.00 24.69 ? 238 ILE   A CA  1 
ATOM   1691 C  C   . ILE   A 1 219 ? 1.253   -11.594 -4.855  1.00 25.19 ? 238 ILE   A C   1 
ATOM   1692 O  O   . ILE   A 1 219 ? 2.060   -12.095 -4.072  1.00 20.60 ? 238 ILE   A O   1 
ATOM   1693 C  CB  . ILE   A 1 219 ? -0.345  -9.743  -4.161  1.00 22.36 ? 238 ILE   A CB  1 
ATOM   1694 C  CG1 . ILE   A 1 219 ? -0.550  -8.249  -3.953  1.00 25.04 ? 238 ILE   A CG1 1 
ATOM   1695 C  CG2 . ILE   A 1 219 ? -0.535  -10.507 -2.864  1.00 22.28 ? 238 ILE   A CG2 1 
ATOM   1696 C  CD1 . ILE   A 1 219 ? -1.978  -7.861  -3.679  1.00 23.34 ? 238 ILE   A CD1 1 
ATOM   1697 N  N   . ASN   A 1 220 ? 0.529   -12.302 -5.759  1.00 27.84 ? 239 ASN   A N   1 
ATOM   1698 C  CA  . ASN   A 1 220 ? 0.635   -13.753 -5.941  1.00 33.18 ? 239 ASN   A CA  1 
ATOM   1699 C  C   . ASN   A 1 220 ? 2.080   -14.173 -6.226  1.00 31.53 ? 239 ASN   A C   1 
ATOM   1700 O  O   . ASN   A 1 220 ? 2.571   -15.111 -5.612  1.00 31.94 ? 239 ASN   A O   1 
ATOM   1701 C  CB  . ASN   A 1 220 ? -0.305  -14.269 -7.027  1.00 33.78 ? 239 ASN   A CB  1 
ATOM   1702 C  CG  . ASN   A 1 220 ? -1.759  -14.102 -6.626  1.00 38.39 ? 239 ASN   A CG  1 
ATOM   1703 O  OD1 . ASN   A 1 220 ? -2.058  -13.709 -5.500  1.00 42.95 ? 239 ASN   A OD1 1 
ATOM   1704 N  ND2 . ASN   A 1 220 ? -2.677  -14.364 -7.539  1.00 40.46 ? 239 ASN   A ND2 1 
ATOM   1705 N  N   . GLN   A 1 221 ? 2.755   -13.410 -7.082  1.00 29.32 ? 240 GLN   A N   1 
ATOM   1706 C  CA  . GLN   A 1 221 ? 4.147   -13.617 -7.404  1.00 35.11 ? 240 GLN   A CA  1 
ATOM   1707 C  C   . GLN   A 1 221 ? 4.995   -13.567 -6.127  1.00 37.81 ? 240 GLN   A C   1 
ATOM   1708 O  O   . GLN   A 1 221 ? 5.815   -14.452 -5.950  1.00 37.44 ? 240 GLN   A O   1 
ATOM   1709 C  CB  . GLN   A 1 221 ? 4.593   -12.610 -8.476  1.00 37.49 ? 240 GLN   A CB  1 
ATOM   1710 C  CG  . GLN   A 1 221 ? 6.084   -12.241 -8.442  1.00 40.58 ? 240 GLN   A CG  1 
ATOM   1711 C  CD  . GLN   A 1 221 ? 6.460   -11.167 -9.438  0.50 39.21 ? 240 GLN   A CD  1 
ATOM   1712 O  OE1 . GLN   A 1 221 ? 5.670   -10.751 -10.282 0.50 45.19 ? 240 GLN   A OE1 1 
ATOM   1713 N  NE2 . GLN   A 1 221 ? 7.680   -10.678 -9.329  0.50 37.47 ? 240 GLN   A NE2 1 
ATOM   1714 N  N   . ILE   A 1 222 ? 4.844   -12.527 -5.280  1.00 34.66 ? 241 ILE   A N   1 
ATOM   1715 C  CA  . ILE   A 1 222 ? 5.698   -12.364 -4.105  1.00 34.07 ? 241 ILE   A CA  1 
ATOM   1716 C  C   . ILE   A 1 222 ? 5.370   -13.490 -3.121  1.00 31.63 ? 241 ILE   A C   1 
ATOM   1717 O  O   . ILE   A 1 222 ? 6.260   -14.188 -2.648  1.00 38.46 ? 241 ILE   A O   1 
ATOM   1718 C  CB  . ILE   A 1 222 ? 5.578   -10.958 -3.450  1.00 35.50 ? 241 ILE   A CB  1 
ATOM   1719 C  CG1 . ILE   A 1 222 ? 5.857   -9.783  -4.405  1.00 29.78 ? 241 ILE   A CG1 1 
ATOM   1720 C  CG2 . ILE   A 1 222 ? 6.459   -10.879 -2.214  1.00 33.58 ? 241 ILE   A CG2 1 
ATOM   1721 C  CD1 . ILE   A 1 222 ? 7.304   -9.613  -4.810  1.00 31.92 ? 241 ILE   A CD1 1 
ATOM   1722 N  N   . LEU   A 1 223 ? 4.083   -13.744 -2.879  1.00 32.07 ? 242 LEU   A N   1 
ATOM   1723 C  CA  . LEU   A 1 223 ? 3.679   -14.800 -1.961  1.00 31.57 ? 242 LEU   A CA  1 
ATOM   1724 C  C   . LEU   A 1 223 ? 4.218   -16.159 -2.414  1.00 40.71 ? 242 LEU   A C   1 
ATOM   1725 O  O   . LEU   A 1 223 ? 4.834   -16.882 -1.612  1.00 35.71 ? 242 LEU   A O   1 
ATOM   1726 C  CB  . LEU   A 1 223 ? 2.154   -14.817 -1.823  1.00 35.14 ? 242 LEU   A CB  1 
ATOM   1727 C  CG  . LEU   A 1 223 ? 1.544   -13.622 -1.077  1.00 34.74 ? 242 LEU   A CG  1 
ATOM   1728 C  CD1 . LEU   A 1 223 ? 0.084   -13.876 -0.763  1.00 39.53 ? 242 LEU   A CD1 1 
ATOM   1729 C  CD2 . LEU   A 1 223 ? 2.310   -13.306 0.201   1.00 35.79 ? 242 LEU   A CD2 1 
ATOM   1730 N  N   . GLN   A 1 224 ? 3.999   -16.502 -3.696  1.00 41.81 ? 243 GLN   A N   1 
ATOM   1731 C  CA  . GLN   A 1 224 ? 4.359   -17.822 -4.211  1.00 41.03 ? 243 GLN   A CA  1 
ATOM   1732 C  C   . GLN   A 1 224 ? 5.862   -18.069 -4.087  1.00 38.55 ? 243 GLN   A C   1 
ATOM   1733 O  O   . GLN   A 1 224 ? 6.262   -19.220 -4.002  1.00 41.65 ? 243 GLN   A O   1 
ATOM   1734 C  CB  . GLN   A 1 224 ? 3.908   -17.995 -5.666  1.00 44.24 ? 243 GLN   A CB  1 
ATOM   1735 C  CG  . GLN   A 1 224 ? 2.810   -19.039 -5.840  0.50 39.67 ? 243 GLN   A CG  1 
ATOM   1736 C  CD  . GLN   A 1 224 ? 3.392   -20.430 -5.796  0.50 37.21 ? 243 GLN   A CD  1 
ATOM   1737 O  OE1 . GLN   A 1 224 ? 4.606   -20.612 -5.915  0.50 34.93 ? 243 GLN   A OE1 1 
ATOM   1738 N  NE2 . GLN   A 1 224 ? 2.532   -21.423 -5.634  0.50 33.30 ? 243 GLN   A NE2 1 
ATOM   1739 N  N   . ALA   A 1 225 ? 6.657   -16.988 -4.019  1.00 36.61 ? 244 ALA   A N   1 
ATOM   1740 C  CA  . ALA   A 1 225 ? 8.107   -17.024 -4.114  1.00 33.04 ? 244 ALA   A CA  1 
ATOM   1741 C  C   . ALA   A 1 225 ? 8.827   -16.617 -2.820  1.00 40.57 ? 244 ALA   A C   1 
ATOM   1742 O  O   . ALA   A 1 225 ? 10.067  -16.487 -2.821  1.00 37.57 ? 244 ALA   A O   1 
ATOM   1743 C  CB  . ALA   A 1 225 ? 8.506   -16.090 -5.215  1.00 34.11 ? 244 ALA   A CB  1 
ATOM   1744 N  N   . ASN   A 1 226 ? 8.082   -16.403 -1.723  1.00 38.36 ? 245 ASN   A N   1 
ATOM   1745 C  CA  . ASN   A 1 226 ? 8.679   -16.048 -0.443  1.00 36.72 ? 245 ASN   A CA  1 
ATOM   1746 C  C   . ASN   A 1 226 ? 7.829   -16.574 0.726   1.00 36.58 ? 245 ASN   A C   1 
ATOM   1747 O  O   . ASN   A 1 226 ? 8.260   -16.367 1.855   1.00 33.91 ? 245 ASN   A O   1 
ATOM   1748 C  CB  . ASN   A 1 226 ? 8.789   -14.535 -0.264  1.00 33.86 ? 245 ASN   A CB  1 
ATOM   1749 C  CG  . ASN   A 1 226 ? 9.572   -13.859 -1.359  1.00 40.27 ? 245 ASN   A CG  1 
ATOM   1750 O  OD1 . ASN   A 1 226 ? 10.762  -13.620 -1.208  1.00 43.33 ? 245 ASN   A OD1 1 
ATOM   1751 N  ND2 . ASN   A 1 226 ? 8.922   -13.577 -2.475  1.00 42.40 ? 245 ASN   A ND2 1 
ATOM   1752 O  OXT . ASN   A 1 226 ? 6.733   -17.102 0.473   1.00 41.29 ? 245 ASN   A OXT 1 
HETATM 1753 ZN ZN  . ZN    B 2 .   ? -8.284  -6.409  24.164  1.00 19.34 ? 301 ZN    A ZN  1 
HETATM 1754 C  C2  . A1AOP C 3 .   ? -2.438  12.539  3.847   1.00 19.67 ? 302 A1AOP A C2  1 
HETATM 1755 C  C4  . A1AOP C 3 .   ? 0.924   12.182  0.583   1.00 26.16 ? 302 A1AOP A C4  1 
HETATM 1756 C  C5  . A1AOP C 3 .   ? -2.749  11.231  3.896   1.00 18.04 ? 302 A1AOP A C5  1 
HETATM 1757 F  F27 . A1AOP C 3 .   ? -6.863  8.926   3.563   1.00 17.80 ? 302 A1AOP A F27 1 
HETATM 1758 C  C23 . A1AOP C 3 .   ? -6.189  10.043  3.552   1.00 16.86 ? 302 A1AOP A C23 1 
HETATM 1759 C  C26 . A1AOP C 3 .   ? -6.926  11.250  3.359   1.00 18.83 ? 302 A1AOP A C26 1 
HETATM 1760 C  C19 . A1AOP C 3 .   ? -6.226  12.406  3.364   1.00 17.17 ? 302 A1AOP A C19 1 
HETATM 1761 C  C10 . A1AOP C 3 .   ? -4.874  12.270  3.567   1.00 17.77 ? 302 A1AOP A C10 1 
HETATM 1762 S  S3  . A1AOP C 3 .   ? -3.767  13.614  3.648   1.00 21.73 ? 302 A1AOP A S3  1 
HETATM 1763 C  C17 . A1AOP C 3 .   ? -4.869  9.858   3.651   1.00 17.51 ? 302 A1AOP A C17 1 
HETATM 1764 C  C8  . A1AOP C 3 .   ? -4.160  11.054  3.723   1.00 18.75 ? 302 A1AOP A C8  1 
HETATM 1765 C  C25 . A1AOP C 3 .   ? -1.730  10.123  4.122   1.00 18.28 ? 302 A1AOP A C25 1 
HETATM 1766 S  S1  . A1AOP C 3 .   ? -0.858  13.260  4.033   1.00 23.79 ? 302 A1AOP A S1  1 
HETATM 1767 O  O12 . A1AOP C 3 .   ? -1.213  14.652  3.923   1.00 27.80 ? 302 A1AOP A O12 1 
HETATM 1768 O  O13 . A1AOP C 3 .   ? -0.305  12.604  5.220   1.00 22.84 ? 302 A1AOP A O13 1 
HETATM 1769 N  N7  . A1AOP C 3 .   ? 0.246   12.667  2.842   1.00 19.06 ? 302 A1AOP A N7  1 
HETATM 1770 C  C9  . A1AOP C 3 .   ? 0.076   12.889  1.463   1.00 22.82 ? 302 A1AOP A C9  1 
HETATM 1771 C  C18 . A1AOP C 3 .   ? -0.907  13.759  0.930   1.00 21.21 ? 302 A1AOP A C18 1 
HETATM 1772 C  C21 . A1AOP C 3 .   ? -1.018  13.916  -0.416  1.00 25.19 ? 302 A1AOP A C21 1 
HETATM 1773 C  C14 . A1AOP C 3 .   ? -0.146  13.199  -1.274  1.00 28.30 ? 302 A1AOP A C14 1 
HETATM 1774 C  C22 . A1AOP C 3 .   ? -0.244  13.324  -2.729  1.00 33.64 ? 302 A1AOP A C22 1 
HETATM 1775 C  C30 . A1AOP C 3 .   ? 0.243   12.218  -3.551  1.00 28.01 ? 302 A1AOP A C30 1 
HETATM 1776 C  C28 . A1AOP C 3 .   ? 0.173   12.369  -4.939  1.00 35.66 ? 302 A1AOP A C28 1 
HETATM 1777 C  C31 . A1AOP C 3 .   ? -0.821  14.518  -3.292  1.00 31.89 ? 302 A1AOP A C31 1 
HETATM 1778 C  C29 . A1AOP C 3 .   ? -0.877  14.625  -4.685  1.00 32.24 ? 302 A1AOP A C29 1 
HETATM 1779 N  N20 . A1AOP C 3 .   ? -0.385  13.558  -5.493  1.00 32.04 ? 302 A1AOP A N20 1 
HETATM 1780 C  C11 . A1AOP C 3 .   ? 0.875   12.354  -0.764  1.00 25.68 ? 302 A1AOP A C11 1 
HETATM 1781 S  S6  . A1AOP C 3 .   ? 2.110   11.143  1.214   1.00 30.50 ? 302 A1AOP A S6  1 
HETATM 1782 O  O15 . A1AOP C 3 .   ? 2.865   10.731  0.052   1.00 31.82 ? 302 A1AOP A O15 1 
HETATM 1783 O  O16 . A1AOP C 3 .   ? 2.970   11.951  2.050   1.00 28.83 ? 302 A1AOP A O16 1 
HETATM 1784 C  C24 . A1AOP C 3 .   ? 1.186   9.792   1.946   1.00 26.14 ? 302 A1AOP A C24 1 
HETATM 1785 O  O   . HOH   D 4 .   ? 2.874   -6.841  27.925  1.00 38.02 ? 401 HOH   A O   1 
HETATM 1786 O  O   . HOH   D 4 .   ? -6.139  -13.641 3.072   1.00 42.29 ? 402 HOH   A O   1 
HETATM 1787 O  O   . HOH   D 4 .   ? -7.828  19.218  13.494  1.00 23.98 ? 403 HOH   A O   1 
HETATM 1788 O  O   . HOH   D 4 .   ? -2.466  16.375  14.046  1.00 24.25 ? 404 HOH   A O   1 
HETATM 1789 O  O   . HOH   D 4 .   ? -4.578  11.851  -13.624 1.00 36.38 ? 405 HOH   A O   1 
HETATM 1790 O  O   . HOH   D 4 .   ? -1.733  9.221   -7.679  1.00 21.52 ? 406 HOH   A O   1 
HETATM 1791 O  O   . HOH   D 4 .   ? -13.657 -7.120  9.106   1.00 26.57 ? 407 HOH   A O   1 
HETATM 1792 O  O   . HOH   D 4 .   ? 5.773   -3.337  23.350  1.00 35.69 ? 408 HOH   A O   1 
HETATM 1793 O  O   . HOH   D 4 .   ? -15.120 14.974  -5.215  1.00 29.68 ? 409 HOH   A O   1 
HETATM 1794 O  O   . HOH   D 4 .   ? 19.921  8.390   5.459   1.00 39.29 ? 410 HOH   A O   1 
HETATM 1795 O  O   . HOH   D 4 .   ? 4.360   -1.740  24.324  1.00 42.41 ? 411 HOH   A O   1 
HETATM 1796 O  O   . HOH   D 4 .   ? -4.842  5.240   25.678  1.00 18.96 ? 412 HOH   A O   1 
HETATM 1797 O  O   . HOH   D 4 .   ? -2.449  6.384   17.282  1.00 22.16 ? 413 HOH   A O   1 
HETATM 1798 O  O   . HOH   D 4 .   ? 9.377   -5.459  -4.530  1.00 40.64 ? 414 HOH   A O   1 
HETATM 1799 O  O   . HOH   D 4 .   ? -11.248 1.485   24.723  1.00 22.24 ? 415 HOH   A O   1 
HETATM 1800 O  O   . HOH   D 4 .   ? 7.917   -0.552  19.289  1.00 44.92 ? 416 HOH   A O   1 
HETATM 1801 O  O   . HOH   D 4 .   ? -14.787 7.563   17.558  1.00 46.79 ? 417 HOH   A O   1 
HETATM 1802 O  O   . HOH   D 4 .   ? -9.534  -1.396  7.575   1.00 30.66 ? 418 HOH   A O   1 
HETATM 1803 O  O   . HOH   D 4 .   ? 12.415  -4.122  12.753  1.00 46.99 ? 419 HOH   A O   1 
HETATM 1804 O  O   . HOH   D 4 .   ? 12.500  -1.245  13.680  1.00 28.81 ? 420 HOH   A O   1 
HETATM 1805 O  O   . HOH   D 4 .   ? -10.709 14.033  17.627  1.00 44.71 ? 421 HOH   A O   1 
HETATM 1806 O  O   . HOH   D 4 .   ? -17.229 11.068  3.722   1.00 22.08 ? 422 HOH   A O   1 
HETATM 1807 O  O   . HOH   D 4 .   ? 8.835   -15.637 8.145   1.00 39.57 ? 423 HOH   A O   1 
HETATM 1808 O  O   . HOH   D 4 .   ? -2.724  -5.011  15.751  1.00 11.56 ? 424 HOH   A O   1 
HETATM 1809 O  O   . HOH   D 4 .   ? 4.278   -2.442  15.818  1.00 14.85 ? 425 HOH   A O   1 
HETATM 1810 O  O   . HOH   D 4 .   ? 9.902   0.229   -5.492  1.00 30.64 ? 426 HOH   A O   1 
HETATM 1811 O  O   . HOH   D 4 .   ? -1.750  5.890   -4.615  1.00 21.48 ? 427 HOH   A O   1 
HETATM 1812 O  O   . HOH   D 4 .   ? 8.842   14.967  -8.361  1.00 20.29 ? 428 HOH   A O   1 
HETATM 1813 O  O   . HOH   D 4 .   ? -19.248 6.996   12.314  1.00 26.98 ? 429 HOH   A O   1 
HETATM 1814 O  O   . HOH   D 4 .   ? 6.585   -16.162 -7.692  1.00 44.61 ? 430 HOH   A O   1 
HETATM 1815 O  O   . HOH   D 4 .   ? 12.164  -4.155  9.963   1.00 30.93 ? 431 HOH   A O   1 
HETATM 1816 O  O   . HOH   D 4 .   ? -10.156 18.806  20.654  1.00 23.37 ? 432 HOH   A O   1 
HETATM 1817 O  O   . HOH   D 4 .   ? -9.343  6.066   22.101  1.00 45.72 ? 433 HOH   A O   1 
HETATM 1818 O  O   . HOH   D 4 .   ? 17.731  10.854  2.627   1.00 39.84 ? 434 HOH   A O   1 
HETATM 1819 O  O   . HOH   D 4 .   ? -10.347 12.810  2.947   1.00 34.55 ? 435 HOH   A O   1 
HETATM 1820 O  O   . HOH   D 4 .   ? 9.931   1.664   16.705  1.00 31.61 ? 436 HOH   A O   1 
HETATM 1821 O  O   . HOH   D 4 .   ? 0.294   6.013   16.823  1.00 26.94 ? 437 HOH   A O   1 
HETATM 1822 O  O   . HOH   D 4 .   ? -11.903 -11.580 16.628  1.00 16.58 ? 438 HOH   A O   1 
HETATM 1823 O  O   . HOH   D 4 .   ? -4.357  -3.470  22.733  1.00 13.28 ? 439 HOH   A O   1 
HETATM 1824 O  O   . HOH   D 4 .   ? -4.936  -7.701  14.530  1.00 13.51 ? 440 HOH   A O   1 
HETATM 1825 O  O   . HOH   D 4 .   ? -9.983  8.025   19.373  1.00 22.23 ? 441 HOH   A O   1 
HETATM 1826 O  O   . HOH   D 4 .   ? 12.601  -4.209  6.717   1.00 38.05 ? 442 HOH   A O   1 
HETATM 1827 O  O   . HOH   D 4 .   ? -10.755 17.662  10.784  1.00 35.25 ? 443 HOH   A O   1 
HETATM 1828 O  O   . HOH   D 4 .   ? 1.098   -1.692  27.627  1.00 21.61 ? 444 HOH   A O   1 
HETATM 1829 O  O   . HOH   D 4 .   ? -13.362 12.238  14.017  1.00 21.91 ? 445 HOH   A O   1 
HETATM 1830 O  O   . HOH   D 4 .   ? -7.473  11.976  18.338  1.00 23.16 ? 446 HOH   A O   1 
HETATM 1831 O  O   . HOH   D 4 .   ? -17.224 -10.858 21.883  1.00 27.79 ? 447 HOH   A O   1 
HETATM 1832 O  O   . HOH   D 4 .   ? -5.310  2.048   8.976   1.00 10.12 ? 448 HOH   A O   1 
HETATM 1833 O  O   . HOH   D 4 .   ? -11.157 -3.119  -7.903  1.00 33.43 ? 449 HOH   A O   1 
HETATM 1834 O  O   . HOH   D 4 .   ? -7.056  -7.886  17.481  1.00 15.10 ? 450 HOH   A O   1 
HETATM 1835 O  O   . HOH   D 4 .   ? -14.079 0.577   -14.847 1.00 36.67 ? 451 HOH   A O   1 
HETATM 1836 O  O   . HOH   D 4 .   ? -0.234  -1.037  -14.405 1.00 42.78 ? 452 HOH   A O   1 
HETATM 1837 O  O   . HOH   D 4 .   ? -5.919  20.279  1.287   1.00 16.87 ? 453 HOH   A O   1 
HETATM 1838 O  O   . HOH   D 4 .   ? 2.563   0.346   20.720  1.00 27.80 ? 454 HOH   A O   1 
HETATM 1839 O  O   . HOH   D 4 .   ? -0.324  6.874   21.586  1.00 37.39 ? 455 HOH   A O   1 
HETATM 1840 O  O   . HOH   D 4 .   ? -8.649  23.732  2.963   1.00 43.82 ? 456 HOH   A O   1 
HETATM 1841 O  O   . HOH   D 4 .   ? -10.733 15.470  -1.945  1.00 20.20 ? 457 HOH   A O   1 
HETATM 1842 O  O   . HOH   D 4 .   ? -1.998  2.263   -0.456  1.00 40.89 ? 458 HOH   A O   1 
HETATM 1843 O  O   . HOH   D 4 .   ? -6.956  -2.470  24.318  1.00 15.56 ? 459 HOH   A O   1 
HETATM 1844 O  O   . HOH   D 4 .   ? 3.726   -1.753  19.410  1.00 21.16 ? 460 HOH   A O   1 
HETATM 1845 O  O   . HOH   D 4 .   ? -7.843  -4.737  -11.422 1.00 30.63 ? 461 HOH   A O   1 
HETATM 1846 O  O   . HOH   D 4 .   ? -13.299 15.430  6.828   1.00 25.75 ? 462 HOH   A O   1 
HETATM 1847 O  O   . HOH   D 4 .   ? -2.951  -13.266 19.368  1.00 13.90 ? 463 HOH   A O   1 
HETATM 1848 O  O   . HOH   D 4 .   ? -1.895  3.570   -5.240  1.00 19.63 ? 464 HOH   A O   1 
HETATM 1849 O  O   . HOH   D 4 .   ? -9.594  -4.098  -5.719  1.00 15.00 ? 465 HOH   A O   1 
HETATM 1850 O  O   . HOH   D 4 .   ? -19.516 19.423  0.814   1.00 36.97 ? 466 HOH   A O   1 
HETATM 1851 O  O   . HOH   D 4 .   ? -17.001 17.259  4.300   1.00 26.13 ? 467 HOH   A O   1 
HETATM 1852 O  O   . HOH   D 4 .   ? -11.593 4.737   -9.184  1.00 16.27 ? 468 HOH   A O   1 
HETATM 1853 O  O   . HOH   D 4 .   ? -6.378  8.227   21.776  1.00 21.86 ? 469 HOH   A O   1 
HETATM 1854 O  O   . HOH   D 4 .   ? -13.452 4.767   -7.274  1.00 13.85 ? 470 HOH   A O   1 
HETATM 1855 O  O   . HOH   D 4 .   ? -5.431  -13.723 24.835  1.00 35.03 ? 471 HOH   A O   1 
HETATM 1856 O  O   . HOH   D 4 .   ? -8.153  6.616   13.885  1.00 11.68 ? 472 HOH   A O   1 
HETATM 1857 O  O   . HOH   D 4 .   ? 2.256   8.035   8.667   1.00 28.71 ? 473 HOH   A O   1 
HETATM 1858 O  O   . HOH   D 4 .   ? -3.679  3.040   -16.336 1.00 32.82 ? 474 HOH   A O   1 
HETATM 1859 O  O   . HOH   D 4 .   ? -16.117 10.182  15.403  1.00 36.36 ? 475 HOH   A O   1 
HETATM 1860 O  O   . HOH   D 4 .   ? -1.687  2.963   -7.843  1.00 29.81 ? 476 HOH   A O   1 
HETATM 1861 O  O   . HOH   D 4 .   ? -0.911  18.664  12.155  1.00 31.20 ? 477 HOH   A O   1 
HETATM 1862 O  O   . HOH   D 4 .   ? -9.433  -5.407  15.715  1.00 11.99 ? 478 HOH   A O   1 
HETATM 1863 O  O   . HOH   D 4 .   ? -13.009 8.405   14.157  1.00 19.87 ? 479 HOH   A O   1 
HETATM 1864 O  O   . HOH   D 4 .   ? -7.480  -16.144 13.331  1.00 19.38 ? 480 HOH   A O   1 
HETATM 1865 O  O   . HOH   D 4 .   ? -16.416 14.493  12.202  1.00 45.59 ? 481 HOH   A O   1 
HETATM 1866 O  O   . HOH   D 4 .   ? -0.035  8.585   7.185   1.00 21.27 ? 482 HOH   A O   1 
HETATM 1867 O  O   . HOH   D 4 .   ? -7.100  -2.420  -12.732 1.00 38.74 ? 483 HOH   A O   1 
HETATM 1868 O  O   . HOH   D 4 .   ? -19.320 10.930  11.497  1.00 38.73 ? 484 HOH   A O   1 
HETATM 1869 O  O   . HOH   D 4 .   ? -15.573 4.909   22.465  1.00 39.49 ? 485 HOH   A O   1 
HETATM 1870 O  O   . HOH   D 4 .   ? -18.036 0.781   10.787  1.00 46.41 ? 486 HOH   A O   1 
HETATM 1871 O  O   . HOH   D 4 .   ? 1.150   10.690  6.649   1.00 40.62 ? 487 HOH   A O   1 
HETATM 1872 O  O   . HOH   D 4 .   ? -7.829  -0.488  27.875  1.00 25.80 ? 488 HOH   A O   1 
HETATM 1873 O  O   . HOH   D 4 .   ? -2.365  7.700   19.410  1.00 35.85 ? 489 HOH   A O   1 
HETATM 1874 O  O   . HOH   D 4 .   ? -2.882  13.309  -7.345  1.00 30.93 ? 490 HOH   A O   1 
HETATM 1875 O  O   . HOH   D 4 .   ? 10.313  -0.246  14.313  1.00 25.37 ? 491 HOH   A O   1 
HETATM 1876 O  O   . HOH   D 4 .   ? -6.939  18.787  -4.223  1.00 33.47 ? 492 HOH   A O   1 
HETATM 1877 O  O   . HOH   D 4 .   ? 8.604   4.469   0.355   1.00 24.94 ? 493 HOH   A O   1 
HETATM 1878 O  O   . HOH   D 4 .   ? 0.855   -18.012 0.056   1.00 42.08 ? 494 HOH   A O   1 
HETATM 1879 O  O   . HOH   D 4 .   ? -9.027  13.594  0.920   1.00 18.54 ? 495 HOH   A O   1 
HETATM 1880 O  O   . HOH   D 4 .   ? -11.477 8.791   2.882   1.00 23.09 ? 496 HOH   A O   1 
HETATM 1881 O  O   . HOH   D 4 .   ? -12.408 19.404  5.154   1.00 27.70 ? 497 HOH   A O   1 
HETATM 1882 O  O   . HOH   D 4 .   ? -3.204  -6.524  -13.436 1.00 30.69 ? 498 HOH   A O   1 
HETATM 1883 O  O   . HOH   D 4 .   ? -8.930  -3.981  18.053  1.00 16.15 ? 499 HOH   A O   1 
HETATM 1884 O  O   . HOH   D 4 .   ? -9.847  -12.201 9.600   1.00 24.50 ? 500 HOH   A O   1 
HETATM 1885 O  O   . HOH   D 4 .   ? -3.610  2.956   11.164  1.00 12.79 ? 501 HOH   A O   1 
HETATM 1886 O  O   . HOH   D 4 .   ? -6.607  -5.831  15.757  1.00 10.66 ? 502 HOH   A O   1 
HETATM 1887 O  O   . HOH   D 4 .   ? 8.021   -9.095  20.341  1.00 37.92 ? 503 HOH   A O   1 
HETATM 1888 O  O   . HOH   D 4 .   ? -18.665 3.203   12.059  1.00 32.10 ? 504 HOH   A O   1 
HETATM 1889 O  O   . HOH   D 4 .   ? 11.533  -2.720  -1.445  1.00 42.09 ? 505 HOH   A O   1 
HETATM 1890 O  O   . HOH   D 4 .   ? -10.456 10.940  -12.412 1.00 17.89 ? 506 HOH   A O   1 
HETATM 1891 O  O   . HOH   D 4 .   ? 7.644   -18.920 11.969  1.00 30.87 ? 507 HOH   A O   1 
HETATM 1892 O  O   . HOH   D 4 .   ? -20.064 8.771   -7.293  1.00 12.79 ? 508 HOH   A O   1 
HETATM 1893 O  O   . HOH   D 4 .   ? 6.396   4.757   -11.933 1.00 33.80 ? 509 HOH   A O   1 
HETATM 1894 O  O   . HOH   D 4 .   ? -20.423 10.683  -11.801 1.00 29.95 ? 510 HOH   A O   1 
HETATM 1895 O  O   . HOH   D 4 .   ? -3.848  10.146  21.195  1.00 30.62 ? 511 HOH   A O   1 
HETATM 1896 O  O   . HOH   D 4 .   ? -15.492 -9.435  17.671  1.00 28.35 ? 512 HOH   A O   1 
HETATM 1897 O  O   . HOH   D 4 .   ? 13.830  -4.973  2.818   1.00 28.53 ? 513 HOH   A O   1 
HETATM 1898 O  O   . HOH   D 4 .   ? -16.160 5.545   19.718  1.00 39.41 ? 514 HOH   A O   1 
HETATM 1899 O  O   . HOH   D 4 .   ? -8.227  -17.063 20.650  1.00 36.69 ? 515 HOH   A O   1 
HETATM 1900 O  O   . HOH   D 4 .   ? -20.425 4.440   -11.982 1.00 7.83  ? 516 HOH   A O   1 
HETATM 1901 O  O   . HOH   D 4 .   ? -22.544 8.466   1.492   1.00 26.31 ? 517 HOH   A O   1 
HETATM 1902 O  O   . HOH   D 4 .   ? -6.729  -8.001  27.860  1.00 19.62 ? 518 HOH   A O   1 
HETATM 1903 O  O   . HOH   D 4 .   ? -15.876 11.105  -17.509 1.00 23.93 ? 519 HOH   A O   1 
HETATM 1904 O  O   . HOH   D 4 .   ? -2.423  -14.458 21.762  1.00 25.22 ? 520 HOH   A O   1 
HETATM 1905 O  O   . HOH   D 4 .   ? -18.285 8.427   2.713   1.00 21.85 ? 521 HOH   A O   1 
HETATM 1906 O  O   . HOH   D 4 .   ? -18.691 -2.536  3.980   1.00 39.30 ? 522 HOH   A O   1 
HETATM 1907 O  O   . HOH   D 4 .   ? -1.696  -17.935 6.219   1.00 18.87 ? 523 HOH   A O   1 
HETATM 1908 O  O   . HOH   D 4 .   ? -9.715  -14.751 14.160  1.00 26.09 ? 524 HOH   A O   1 
HETATM 1909 O  O   . HOH   D 4 .   ? -13.583 -0.740  23.912  1.00 30.70 ? 525 HOH   A O   1 
HETATM 1910 O  O   . HOH   D 4 .   ? -3.123  16.482  -7.191  1.00 39.85 ? 526 HOH   A O   1 
HETATM 1911 O  O   . HOH   D 4 .   ? -9.908  21.327  7.188   1.00 29.10 ? 527 HOH   A O   1 
HETATM 1912 O  O   . HOH   D 4 .   ? 3.037   8.547   12.064  1.00 33.40 ? 528 HOH   A O   1 
HETATM 1913 O  O   . HOH   D 4 .   ? -9.465  -7.001  -4.395  1.00 32.39 ? 529 HOH   A O   1 
HETATM 1914 O  O   . HOH   D 4 .   ? -4.716  -9.329  28.230  1.00 19.74 ? 530 HOH   A O   1 
HETATM 1915 O  O   . HOH   D 4 .   ? -8.981  2.308   25.623  1.00 33.48 ? 531 HOH   A O   1 
HETATM 1916 O  O   . HOH   D 4 .   ? -16.916 -4.566  4.774   1.00 28.19 ? 532 HOH   A O   1 
HETATM 1917 O  O   . HOH   D 4 .   ? -16.399 -3.021  15.199  1.00 22.87 ? 533 HOH   A O   1 
HETATM 1918 O  O   . HOH   D 4 .   ? -13.179 6.404   20.600  1.00 35.48 ? 534 HOH   A O   1 
HETATM 1919 O  O   . HOH   D 4 .   ? -18.070 -11.517 17.978  1.00 42.45 ? 535 HOH   A O   1 
HETATM 1920 O  O   . HOH   D 4 .   ? 16.651  0.773   12.174  1.00 42.63 ? 536 HOH   A O   1 
HETATM 1921 O  O   . HOH   D 4 .   ? -13.930 -9.671  6.617   1.00 42.28 ? 537 HOH   A O   1 
HETATM 1922 O  O   . HOH   D 4 .   ? -7.447  -16.271 10.247  1.00 30.18 ? 538 HOH   A O   1 
HETATM 1923 O  O   . HOH   D 4 .   ? 8.813   -7.184  -7.030  1.00 31.21 ? 539 HOH   A O   1 
HETATM 1924 O  O   . HOH   D 4 .   ? 2.638   -18.342 6.046   1.00 24.74 ? 540 HOH   A O   1 
HETATM 1925 O  O   . HOH   D 4 .   ? -15.463 -9.717  14.315  1.00 40.73 ? 541 HOH   A O   1 
HETATM 1926 O  O   . HOH   D 4 .   ? -1.474  -20.811 14.054  1.00 40.04 ? 542 HOH   A O   1 
HETATM 1927 O  O   . HOH   D 4 .   ? -13.448 16.857  -8.511  1.00 25.86 ? 543 HOH   A O   1 
HETATM 1928 O  O   . HOH   D 4 .   ? 10.479  -11.952 -4.661  1.00 32.59 ? 544 HOH   A O   1 
HETATM 1929 O  O   . HOH   D 4 .   ? 0.023   11.219  11.535  1.00 33.87 ? 545 HOH   A O   1 
HETATM 1930 O  O   . HOH   D 4 .   ? -7.254  -13.972 20.959  1.00 18.83 ? 546 HOH   A O   1 
HETATM 1931 O  O   . HOH   D 4 .   ? -19.290 5.111   10.282  1.00 11.50 ? 547 HOH   A O   1 
HETATM 1932 O  O   . HOH   D 4 .   ? -15.586 -4.560  7.459   1.00 31.37 ? 548 HOH   A O   1 
HETATM 1933 O  O   . HOH   D 4 .   ? 10.607  -2.762  18.067  1.00 38.65 ? 549 HOH   A O   1 
HETATM 1934 O  O   . HOH   D 4 .   ? 13.451  10.352  2.792   1.00 36.31 ? 550 HOH   A O   1 
HETATM 1935 O  O   . HOH   D 4 .   ? -14.277 2.341   -8.627  1.00 24.01 ? 551 HOH   A O   1 
HETATM 1936 O  O   . HOH   D 4 .   ? -0.038  -6.871  -10.846 1.00 33.07 ? 552 HOH   A O   1 
HETATM 1937 O  O   . HOH   D 4 .   ? -18.463 3.284   -10.737 1.00 31.85 ? 553 HOH   A O   1 
HETATM 1938 O  O   . HOH   D 4 .   ? -9.441  8.066   -14.118 1.00 45.61 ? 554 HOH   A O   1 
HETATM 1939 O  O   . HOH   D 4 .   ? -14.915 15.311  -13.403 1.00 43.28 ? 555 HOH   A O   1 
HETATM 1940 O  O   . HOH   D 4 .   ? 0.537   -14.293 -10.575 1.00 41.85 ? 556 HOH   A O   1 
HETATM 1941 O  O   . HOH   D 4 .   ? -0.383  11.447  15.283  1.00 24.23 ? 557 HOH   A O   1 
HETATM 1942 O  O   . HOH   D 4 .   ? 1.515   -5.226  -10.817 1.00 25.06 ? 558 HOH   A O   1 
HETATM 1943 O  O   . HOH   D 4 .   ? -13.360 -9.432  10.704  1.00 31.88 ? 559 HOH   A O   1 
HETATM 1944 O  O   . HOH   D 4 .   ? -0.399  5.673   -15.245 1.00 51.56 ? 560 HOH   A O   1 
HETATM 1945 O  O   . HOH   D 4 .   ? 2.083   4.585   -14.202 1.00 40.50 ? 561 HOH   A O   1 
HETATM 1946 O  O   . HOH   D 4 .   ? -21.312 8.049   3.256   1.00 32.88 ? 562 HOH   A O   1 
HETATM 1947 O  O   . HOH   D 4 .   ? 1.645   -2.690  -12.624 1.00 42.98 ? 563 HOH   A O   1 
HETATM 1948 O  O   . HOH   D 4 .   ? -0.713  6.442   13.747  1.00 30.58 ? 564 HOH   A O   1 
HETATM 1949 O  O   . HOH   D 4 .   ? -4.278  19.173  -0.384  1.00 34.11 ? 565 HOH   A O   1 
HETATM 1950 O  O   . HOH   D 4 .   ? 3.609   -5.561  -11.970 1.00 43.41 ? 566 HOH   A O   1 
HETATM 1951 O  O   . HOH   D 4 .   ? -8.233  -18.580 14.647  1.00 41.14 ? 567 HOH   A O   1 
HETATM 1952 O  O   . HOH   D 4 .   ? -10.550 18.525  13.790  1.00 30.39 ? 568 HOH   A O   1 
HETATM 1953 O  O   . HOH   D 4 .   ? -13.076 21.358  3.836   1.00 42.63 ? 569 HOH   A O   1 
HETATM 1954 O  O   . HOH   D 4 .   ? -18.641 11.480  -9.626  1.00 34.30 ? 570 HOH   A O   1 
HETATM 1955 O  O   . HOH   D 4 .   ? -17.806 14.377  -9.162  1.00 39.97 ? 571 HOH   A O   1 
HETATM 1956 O  O   . HOH   D 4 .   ? -14.267 17.504  5.295   1.00 19.26 ? 572 HOH   A O   1 
HETATM 1957 O  O   . HOH   D 4 .   ? -0.320  -0.989  29.664  1.00 46.29 ? 573 HOH   A O   1 
HETATM 1958 O  O   . HOH   D 4 .   ? 12.652  -16.960 0.625   1.00 36.80 ? 574 HOH   A O   1 
HETATM 1959 O  O   . HOH   D 4 .   ? -9.885  -15.831 9.678   1.00 38.71 ? 575 HOH   A O   1 
HETATM 1960 O  O   . HOH   D 4 .   ? -16.301 -7.168  7.390   1.00 48.40 ? 576 HOH   A O   1 
HETATM 1961 O  O   . HOH   D 4 .   ? -13.573 10.272  16.120  1.00 31.19 ? 577 HOH   A O   1 
HETATM 1962 O  O   . HOH   D 4 .   ? -6.437  -11.150 26.204  1.00 37.88 ? 578 HOH   A O   1 
HETATM 1963 O  O   . HOH   D 4 .   ? 8.349   -6.892  20.478  1.00 40.60 ? 579 HOH   A O   1 
HETATM 1964 O  O   . HOH   D 4 .   ? -8.857  -0.572  25.383  1.00 29.07 ? 580 HOH   A O   1 
HETATM 1965 O  O   . HOH   D 4 .   ? -12.540 9.916   18.771  1.00 38.71 ? 581 HOH   A O   1 
HETATM 1966 O  O   . HOH   D 4 .   ? -4.839  -15.103 22.595  1.00 38.48 ? 582 HOH   A O   1 
HETATM 1967 O  O   . HOH   D 4 .   ? -1.538  -19.093 20.276  1.00 29.17 ? 583 HOH   A O   1 
HETATM 1968 O  O   . HOH   D 4 .   ? -15.796 -12.952 18.696  1.00 35.98 ? 584 HOH   A O   1 
HETATM 1969 O  O   . HOH   D 4 .   ? -11.957 -11.708 8.108   1.00 34.10 ? 585 HOH   A O   1 
HETATM 1970 O  O   . HOH   D 4 .   ? 7.246   -7.082  28.893  1.00 41.43 ? 586 HOH   A O   1 
HETATM 1971 O  O   . HOH   D 4 .   ? -16.371 -13.299 21.069  1.00 37.89 ? 587 HOH   A O   1 
HETATM 1972 O  O   . HOH   D 4 .   ? 2.784   3.553   24.621  1.00 44.46 ? 588 HOH   A O   1 
HETATM 1973 O  O   . HOH   D 4 .   ? -19.773 11.198  -7.760  1.00 30.19 ? 589 HOH   A O   1 
HETATM 1974 O  O   . HOH   D 4 .   ? -13.611 -12.156 14.580  1.00 27.57 ? 590 HOH   A O   1 
HETATM 1975 O  O   . HOH   D 4 .   ? 14.464  -8.266  12.815  1.00 42.71 ? 591 HOH   A O   1 
HETATM 1976 O  O   . HOH   D 4 .   ? 1.668   8.240   17.392  1.00 25.89 ? 592 HOH   A O   1 
HETATM 1977 O  O   . HOH   D 4 .   ? 3.872   10.570  14.789  1.00 32.55 ? 593 HOH   A O   1 
HETATM 1978 O  O   . HOH   D 4 .   ? -12.709 17.114  9.011   1.00 33.61 ? 594 HOH   A O   1 
HETATM 1979 O  O   . HOH   D 4 .   ? -20.089 12.837  -13.388 1.00 23.94 ? 595 HOH   A O   1 
HETATM 1980 O  O   . HOH   D 4 .   ? -10.790 -13.932 11.510  1.00 28.03 ? 596 HOH   A O   1 
HETATM 1981 O  O   . HOH   D 4 .   ? -12.221 -16.330 14.149  1.00 35.39 ? 597 HOH   A O   1 
HETATM 1982 O  O   . HOH   D 4 .   ? -13.151 -12.286 11.964  1.00 24.35 ? 598 HOH   A O   1 
HETATM 1983 O  O   . HOH   D 4 .   ? -16.134 -15.186 17.284  1.00 41.47 ? 599 HOH   A O   1 
# 
