data_7H6A
# 
_entry.id   7H6A 
# 
_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   7H6A         pdb_00007h6a 10.2210/pdb7h6a/pdb 
WWPDB D_1001407077 ?            ?                   
# 
_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                        7H6A 
_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 'C28S, F135K' ? ? 
2 non-polymer syn 'ZINC ION'                                                                                          65.409    1 
?         ?             ? ? 
3 non-polymer syn '3-[2-(dimethylamino)-2-oxoethyl]-5-fluoro-1-[(naphthalen-1-yl)methyl]-1H-indole-2-carboxylic acid' 404.434   1 
?         ?             ? ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                                                                78.133    2 
?         ?             ? ? 
5 water       nat water                                                                                               18.015    
369 ?         ?             ? ? 
# 
_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 '3-[2-(dimethylamino)-2-oxoethyl]-5-fluoro-1-[(naphthalen-1-yl)methyl]-1H-indole-2-carboxylic acid' A1AO8 
4 'DIMETHYL SULFOXIDE'                                                                                DMS   
5 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 
A1AO8 non-polymer         . '3-[2-(dimethylamino)-2-oxoethyl]-5-fluoro-1-[(naphthalen-1-yl)methyl]-1H-indole-2-carboxylic acid' ? 
'C24 H21 F N2 O3' 404.434 
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 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE'                                                                                ? 
'C2 H6 O S'       78.133  
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 111 124 124 PRO PRO A . n 
A 1 112 SER 112 125 125 SER SER A . n 
A 1 113 GLN 113 126 126 GLN GLN A . n 
A 1 114 LYS 114 127 127 LYS LYS A . n 
A 1 115 ASN 115 128 128 ASN ASN A . n 
A 1 116 PHE 116 129 129 PHE PHE 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        A1AO8 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1AO8 
_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 A1AO8 1   302 1001 A1AO8 LIG A . 
D 4 DMS   1   303 1    DMS   DMS A . 
E 4 DMS   1   304 2    DMS   DMS A . 
F 5 HOH   1   401 376  HOH   HOH A . 
F 5 HOH   2   402 139  HOH   HOH A . 
F 5 HOH   3   403 235  HOH   HOH A . 
F 5 HOH   4   404 251  HOH   HOH A . 
F 5 HOH   5   405 179  HOH   HOH A . 
F 5 HOH   6   406 207  HOH   HOH A . 
F 5 HOH   7   407 47   HOH   HOH A . 
F 5 HOH   8   408 234  HOH   HOH A . 
F 5 HOH   9   409 121  HOH   HOH A . 
F 5 HOH   10  410 112  HOH   HOH A . 
F 5 HOH   11  411 247  HOH   HOH A . 
F 5 HOH   12  412 283  HOH   HOH A . 
F 5 HOH   13  413 224  HOH   HOH A . 
F 5 HOH   14  414 211  HOH   HOH A . 
F 5 HOH   15  415 231  HOH   HOH A . 
F 5 HOH   16  416 221  HOH   HOH A . 
F 5 HOH   17  417 129  HOH   HOH A . 
F 5 HOH   18  418 271  HOH   HOH A . 
F 5 HOH   19  419 163  HOH   HOH A . 
F 5 HOH   20  420 36   HOH   HOH A . 
F 5 HOH   21  421 145  HOH   HOH A . 
F 5 HOH   22  422 80   HOH   HOH A . 
F 5 HOH   23  423 184  HOH   HOH A . 
F 5 HOH   24  424 151  HOH   HOH A . 
F 5 HOH   25  425 337  HOH   HOH A . 
F 5 HOH   26  426 168  HOH   HOH A . 
F 5 HOH   27  427 188  HOH   HOH A . 
F 5 HOH   28  428 183  HOH   HOH A . 
F 5 HOH   29  429 123  HOH   HOH A . 
F 5 HOH   30  430 241  HOH   HOH A . 
F 5 HOH   31  431 33   HOH   HOH A . 
F 5 HOH   32  432 208  HOH   HOH A . 
F 5 HOH   33  433 34   HOH   HOH A . 
F 5 HOH   34  434 164  HOH   HOH A . 
F 5 HOH   35  435 70   HOH   HOH A . 
F 5 HOH   36  436 170  HOH   HOH A . 
F 5 HOH   37  437 143  HOH   HOH A . 
F 5 HOH   38  438 180  HOH   HOH A . 
F 5 HOH   39  439 54   HOH   HOH A . 
F 5 HOH   40  440 157  HOH   HOH A . 
F 5 HOH   41  441 67   HOH   HOH A . 
F 5 HOH   42  442 154  HOH   HOH A . 
F 5 HOH   43  443 127  HOH   HOH A . 
F 5 HOH   44  444 82   HOH   HOH A . 
F 5 HOH   45  445 104  HOH   HOH A . 
F 5 HOH   46  446 286  HOH   HOH A . 
F 5 HOH   47  447 6    HOH   HOH A . 
F 5 HOH   48  448 14   HOH   HOH A . 
F 5 HOH   49  449 22   HOH   HOH A . 
F 5 HOH   50  450 135  HOH   HOH A . 
F 5 HOH   51  451 59   HOH   HOH A . 
F 5 HOH   52  452 105  HOH   HOH A . 
F 5 HOH   53  453 197  HOH   HOH A . 
F 5 HOH   54  454 20   HOH   HOH A . 
F 5 HOH   55  455 49   HOH   HOH A . 
F 5 HOH   56  456 272  HOH   HOH A . 
F 5 HOH   57  457 11   HOH   HOH A . 
F 5 HOH   58  458 172  HOH   HOH A . 
F 5 HOH   59  459 178  HOH   HOH A . 
F 5 HOH   60  460 16   HOH   HOH A . 
F 5 HOH   61  461 65   HOH   HOH A . 
F 5 HOH   62  462 320  HOH   HOH A . 
F 5 HOH   63  463 144  HOH   HOH A . 
F 5 HOH   64  464 29   HOH   HOH A . 
F 5 HOH   65  465 93   HOH   HOH A . 
F 5 HOH   66  466 289  HOH   HOH A . 
F 5 HOH   67  467 125  HOH   HOH A . 
F 5 HOH   68  468 110  HOH   HOH A . 
F 5 HOH   69  469 10   HOH   HOH A . 
F 5 HOH   70  470 26   HOH   HOH A . 
F 5 HOH   71  471 109  HOH   HOH A . 
F 5 HOH   72  472 88   HOH   HOH A . 
F 5 HOH   73  473 137  HOH   HOH A . 
F 5 HOH   74  474 261  HOH   HOH A . 
F 5 HOH   75  475 367  HOH   HOH A . 
F 5 HOH   76  476 226  HOH   HOH A . 
F 5 HOH   77  477 295  HOH   HOH A . 
F 5 HOH   78  478 156  HOH   HOH A . 
F 5 HOH   79  479 140  HOH   HOH A . 
F 5 HOH   80  480 195  HOH   HOH A . 
F 5 HOH   81  481 122  HOH   HOH A . 
F 5 HOH   82  482 238  HOH   HOH A . 
F 5 HOH   83  483 246  HOH   HOH A . 
F 5 HOH   84  484 17   HOH   HOH A . 
F 5 HOH   85  485 358  HOH   HOH A . 
F 5 HOH   86  486 19   HOH   HOH A . 
F 5 HOH   87  487 182  HOH   HOH A . 
F 5 HOH   88  488 332  HOH   HOH A . 
F 5 HOH   89  489 106  HOH   HOH A . 
F 5 HOH   90  490 28   HOH   HOH A . 
F 5 HOH   91  491 282  HOH   HOH A . 
F 5 HOH   92  492 364  HOH   HOH A . 
F 5 HOH   93  493 92   HOH   HOH A . 
F 5 HOH   94  494 55   HOH   HOH A . 
F 5 HOH   95  495 152  HOH   HOH A . 
F 5 HOH   96  496 292  HOH   HOH A . 
F 5 HOH   97  497 98   HOH   HOH A . 
F 5 HOH   98  498 298  HOH   HOH A . 
F 5 HOH   99  499 69   HOH   HOH A . 
F 5 HOH   100 500 153  HOH   HOH A . 
F 5 HOH   101 501 237  HOH   HOH A . 
F 5 HOH   102 502 64   HOH   HOH A . 
F 5 HOH   103 503 171  HOH   HOH A . 
F 5 HOH   104 504 7    HOH   HOH A . 
F 5 HOH   105 505 83   HOH   HOH A . 
F 5 HOH   106 506 102  HOH   HOH A . 
F 5 HOH   107 507 35   HOH   HOH A . 
F 5 HOH   108 508 100  HOH   HOH A . 
F 5 HOH   109 509 111  HOH   HOH A . 
F 5 HOH   110 510 12   HOH   HOH A . 
F 5 HOH   111 511 225  HOH   HOH A . 
F 5 HOH   112 512 97   HOH   HOH A . 
F 5 HOH   113 513 253  HOH   HOH A . 
F 5 HOH   114 514 39   HOH   HOH A . 
F 5 HOH   115 515 40   HOH   HOH A . 
F 5 HOH   116 516 46   HOH   HOH A . 
F 5 HOH   117 517 303  HOH   HOH A . 
F 5 HOH   118 518 333  HOH   HOH A . 
F 5 HOH   119 519 177  HOH   HOH A . 
F 5 HOH   120 520 278  HOH   HOH A . 
F 5 HOH   121 521 95   HOH   HOH A . 
F 5 HOH   122 522 8    HOH   HOH A . 
F 5 HOH   123 523 18   HOH   HOH A . 
F 5 HOH   124 524 5    HOH   HOH A . 
F 5 HOH   125 525 74   HOH   HOH A . 
F 5 HOH   126 526 85   HOH   HOH A . 
F 5 HOH   127 527 68   HOH   HOH A . 
F 5 HOH   128 528 52   HOH   HOH A . 
F 5 HOH   129 529 58   HOH   HOH A . 
F 5 HOH   130 530 354  HOH   HOH A . 
F 5 HOH   131 531 160  HOH   HOH A . 
F 5 HOH   132 532 162  HOH   HOH A . 
F 5 HOH   133 533 9    HOH   HOH A . 
F 5 HOH   134 534 13   HOH   HOH A . 
F 5 HOH   135 535 174  HOH   HOH A . 
F 5 HOH   136 536 43   HOH   HOH A . 
F 5 HOH   137 537 3    HOH   HOH A . 
F 5 HOH   138 538 236  HOH   HOH A . 
F 5 HOH   139 539 4    HOH   HOH A . 
F 5 HOH   140 540 30   HOH   HOH A . 
F 5 HOH   141 541 76   HOH   HOH A . 
F 5 HOH   142 542 191  HOH   HOH A . 
F 5 HOH   143 543 339  HOH   HOH A . 
F 5 HOH   144 544 173  HOH   HOH A . 
F 5 HOH   145 545 23   HOH   HOH A . 
F 5 HOH   146 546 209  HOH   HOH A . 
F 5 HOH   147 547 1    HOH   HOH A . 
F 5 HOH   148 548 42   HOH   HOH A . 
F 5 HOH   149 549 273  HOH   HOH A . 
F 5 HOH   150 550 189  HOH   HOH A . 
F 5 HOH   151 551 27   HOH   HOH A . 
F 5 HOH   152 552 266  HOH   HOH A . 
F 5 HOH   153 553 31   HOH   HOH A . 
F 5 HOH   154 554 15   HOH   HOH A . 
F 5 HOH   155 555 262  HOH   HOH A . 
F 5 HOH   156 556 78   HOH   HOH A . 
F 5 HOH   157 557 96   HOH   HOH A . 
F 5 HOH   158 558 239  HOH   HOH A . 
F 5 HOH   159 559 60   HOH   HOH A . 
F 5 HOH   160 560 132  HOH   HOH A . 
F 5 HOH   161 561 2    HOH   HOH A . 
F 5 HOH   162 562 32   HOH   HOH A . 
F 5 HOH   163 563 242  HOH   HOH A . 
F 5 HOH   164 564 190  HOH   HOH A . 
F 5 HOH   165 565 133  HOH   HOH A . 
F 5 HOH   166 566 51   HOH   HOH A . 
F 5 HOH   167 567 205  HOH   HOH A . 
F 5 HOH   168 568 187  HOH   HOH A . 
F 5 HOH   169 569 277  HOH   HOH A . 
F 5 HOH   170 570 25   HOH   HOH A . 
F 5 HOH   171 571 362  HOH   HOH A . 
F 5 HOH   172 572 138  HOH   HOH A . 
F 5 HOH   173 573 158  HOH   HOH A . 
F 5 HOH   174 574 50   HOH   HOH A . 
F 5 HOH   175 575 166  HOH   HOH A . 
F 5 HOH   176 576 233  HOH   HOH A . 
F 5 HOH   177 577 368  HOH   HOH A . 
F 5 HOH   178 578 307  HOH   HOH A . 
F 5 HOH   179 579 287  HOH   HOH A . 
F 5 HOH   180 580 128  HOH   HOH A . 
F 5 HOH   181 581 41   HOH   HOH A . 
F 5 HOH   182 582 90   HOH   HOH A . 
F 5 HOH   183 583 297  HOH   HOH A . 
F 5 HOH   184 584 72   HOH   HOH A . 
F 5 HOH   185 585 48   HOH   HOH A . 
F 5 HOH   186 586 202  HOH   HOH A . 
F 5 HOH   187 587 291  HOH   HOH A . 
F 5 HOH   188 588 194  HOH   HOH A . 
F 5 HOH   189 589 254  HOH   HOH A . 
F 5 HOH   190 590 115  HOH   HOH A . 
F 5 HOH   191 591 63   HOH   HOH A . 
F 5 HOH   192 592 120  HOH   HOH A . 
F 5 HOH   193 593 107  HOH   HOH A . 
F 5 HOH   194 594 230  HOH   HOH A . 
F 5 HOH   195 595 181  HOH   HOH A . 
F 5 HOH   196 596 71   HOH   HOH A . 
F 5 HOH   197 597 259  HOH   HOH A . 
F 5 HOH   198 598 200  HOH   HOH A . 
F 5 HOH   199 599 126  HOH   HOH A . 
F 5 HOH   200 600 94   HOH   HOH A . 
F 5 HOH   201 601 79   HOH   HOH A . 
F 5 HOH   202 602 24   HOH   HOH A . 
F 5 HOH   203 603 255  HOH   HOH A . 
F 5 HOH   204 604 250  HOH   HOH A . 
F 5 HOH   205 605 134  HOH   HOH A . 
F 5 HOH   206 606 45   HOH   HOH A . 
F 5 HOH   207 607 305  HOH   HOH A . 
F 5 HOH   208 608 249  HOH   HOH A . 
F 5 HOH   209 609 73   HOH   HOH A . 
F 5 HOH   210 610 84   HOH   HOH A . 
F 5 HOH   211 611 323  HOH   HOH A . 
F 5 HOH   212 612 131  HOH   HOH A . 
F 5 HOH   213 613 61   HOH   HOH A . 
F 5 HOH   214 614 220  HOH   HOH A . 
F 5 HOH   215 615 311  HOH   HOH A . 
F 5 HOH   216 616 206  HOH   HOH A . 
F 5 HOH   217 617 334  HOH   HOH A . 
F 5 HOH   218 618 114  HOH   HOH A . 
F 5 HOH   219 619 203  HOH   HOH A . 
F 5 HOH   220 620 227  HOH   HOH A . 
F 5 HOH   221 621 119  HOH   HOH A . 
F 5 HOH   222 622 44   HOH   HOH A . 
F 5 HOH   223 623 56   HOH   HOH A . 
F 5 HOH   224 624 103  HOH   HOH A . 
F 5 HOH   225 625 232  HOH   HOH A . 
F 5 HOH   226 626 214  HOH   HOH A . 
F 5 HOH   227 627 215  HOH   HOH A . 
F 5 HOH   228 628 155  HOH   HOH A . 
F 5 HOH   229 629 77   HOH   HOH A . 
F 5 HOH   230 630 223  HOH   HOH A . 
F 5 HOH   231 631 258  HOH   HOH A . 
F 5 HOH   232 632 357  HOH   HOH A . 
F 5 HOH   233 633 294  HOH   HOH A . 
F 5 HOH   234 634 81   HOH   HOH A . 
F 5 HOH   235 635 199  HOH   HOH A . 
F 5 HOH   236 636 167  HOH   HOH A . 
F 5 HOH   237 637 57   HOH   HOH A . 
F 5 HOH   238 638 37   HOH   HOH A . 
F 5 HOH   239 639 351  HOH   HOH A . 
F 5 HOH   240 640 396  HOH   HOH A . 
F 5 HOH   241 641 329  HOH   HOH A . 
F 5 HOH   242 642 306  HOH   HOH A . 
F 5 HOH   243 643 269  HOH   HOH A . 
F 5 HOH   244 644 363  HOH   HOH A . 
F 5 HOH   245 645 340  HOH   HOH A . 
F 5 HOH   246 646 270  HOH   HOH A . 
F 5 HOH   247 647 213  HOH   HOH A . 
F 5 HOH   248 648 185  HOH   HOH A . 
F 5 HOH   249 649 198  HOH   HOH A . 
F 5 HOH   250 650 21   HOH   HOH A . 
F 5 HOH   251 651 267  HOH   HOH A . 
F 5 HOH   252 652 150  HOH   HOH A . 
F 5 HOH   253 653 265  HOH   HOH A . 
F 5 HOH   254 654 377  HOH   HOH A . 
F 5 HOH   255 655 330  HOH   HOH A . 
F 5 HOH   256 656 299  HOH   HOH A . 
F 5 HOH   257 657 315  HOH   HOH A . 
F 5 HOH   258 658 336  HOH   HOH A . 
F 5 HOH   259 659 344  HOH   HOH A . 
F 5 HOH   260 660 318  HOH   HOH A . 
F 5 HOH   261 661 196  HOH   HOH A . 
F 5 HOH   262 662 116  HOH   HOH A . 
F 5 HOH   263 663 204  HOH   HOH A . 
F 5 HOH   264 664 361  HOH   HOH A . 
F 5 HOH   265 665 325  HOH   HOH A . 
F 5 HOH   266 666 159  HOH   HOH A . 
F 5 HOH   267 667 302  HOH   HOH A . 
F 5 HOH   268 668 397  HOH   HOH A . 
F 5 HOH   269 669 108  HOH   HOH A . 
F 5 HOH   270 670 411  HOH   HOH A . 
F 5 HOH   271 671 380  HOH   HOH A . 
F 5 HOH   272 672 141  HOH   HOH A . 
F 5 HOH   273 673 308  HOH   HOH A . 
F 5 HOH   274 674 353  HOH   HOH A . 
F 5 HOH   275 675 369  HOH   HOH A . 
F 5 HOH   276 676 99   HOH   HOH A . 
F 5 HOH   277 677 296  HOH   HOH A . 
F 5 HOH   278 678 228  HOH   HOH A . 
F 5 HOH   279 679 301  HOH   HOH A . 
F 5 HOH   280 680 343  HOH   HOH A . 
F 5 HOH   281 681 400  HOH   HOH A . 
F 5 HOH   282 682 217  HOH   HOH A . 
F 5 HOH   283 683 62   HOH   HOH A . 
F 5 HOH   284 684 285  HOH   HOH A . 
F 5 HOH   285 685 342  HOH   HOH A . 
F 5 HOH   286 686 310  HOH   HOH A . 
F 5 HOH   287 687 216  HOH   HOH A . 
F 5 HOH   288 688 385  HOH   HOH A . 
F 5 HOH   289 689 165  HOH   HOH A . 
F 5 HOH   290 690 66   HOH   HOH A . 
F 5 HOH   291 691 326  HOH   HOH A . 
F 5 HOH   292 692 256  HOH   HOH A . 
F 5 HOH   293 693 53   HOH   HOH A . 
F 5 HOH   294 694 279  HOH   HOH A . 
F 5 HOH   295 695 38   HOH   HOH A . 
F 5 HOH   296 696 349  HOH   HOH A . 
F 5 HOH   297 697 192  HOH   HOH A . 
F 5 HOH   298 698 257  HOH   HOH A . 
F 5 HOH   299 699 322  HOH   HOH A . 
F 5 HOH   300 700 117  HOH   HOH A . 
F 5 HOH   301 701 268  HOH   HOH A . 
F 5 HOH   302 702 87   HOH   HOH A . 
F 5 HOH   303 703 75   HOH   HOH A . 
F 5 HOH   304 704 264  HOH   HOH A . 
F 5 HOH   305 705 348  HOH   HOH A . 
F 5 HOH   306 706 193  HOH   HOH A . 
F 5 HOH   307 707 252  HOH   HOH A . 
F 5 HOH   308 708 304  HOH   HOH A . 
F 5 HOH   309 709 218  HOH   HOH A . 
F 5 HOH   310 710 169  HOH   HOH A . 
F 5 HOH   311 711 130  HOH   HOH A . 
F 5 HOH   312 712 201  HOH   HOH A . 
F 5 HOH   313 713 260  HOH   HOH A . 
F 5 HOH   314 714 146  HOH   HOH A . 
F 5 HOH   315 715 370  HOH   HOH A . 
F 5 HOH   316 716 101  HOH   HOH A . 
F 5 HOH   317 717 341  HOH   HOH A . 
F 5 HOH   318 718 356  HOH   HOH A . 
F 5 HOH   319 719 360  HOH   HOH A . 
F 5 HOH   320 720 313  HOH   HOH A . 
F 5 HOH   321 721 136  HOH   HOH A . 
F 5 HOH   322 722 113  HOH   HOH A . 
F 5 HOH   323 723 316  HOH   HOH A . 
F 5 HOH   324 724 335  HOH   HOH A . 
F 5 HOH   325 725 281  HOH   HOH A . 
F 5 HOH   326 726 240  HOH   HOH A . 
F 5 HOH   327 727 244  HOH   HOH A . 
F 5 HOH   328 728 243  HOH   HOH A . 
F 5 HOH   329 729 328  HOH   HOH A . 
F 5 HOH   330 730 222  HOH   HOH A . 
F 5 HOH   331 731 161  HOH   HOH A . 
F 5 HOH   332 732 312  HOH   HOH A . 
F 5 HOH   333 733 89   HOH   HOH A . 
F 5 HOH   334 734 280  HOH   HOH A . 
F 5 HOH   335 735 263  HOH   HOH A . 
F 5 HOH   336 736 314  HOH   HOH A . 
F 5 HOH   337 737 317  HOH   HOH A . 
F 5 HOH   338 738 219  HOH   HOH A . 
F 5 HOH   339 739 392  HOH   HOH A . 
F 5 HOH   340 740 319  HOH   HOH A . 
F 5 HOH   341 741 275  HOH   HOH A . 
F 5 HOH   342 742 147  HOH   HOH A . 
F 5 HOH   343 743 288  HOH   HOH A . 
F 5 HOH   344 744 149  HOH   HOH A . 
F 5 HOH   345 745 359  HOH   HOH A . 
F 5 HOH   346 746 229  HOH   HOH A . 
F 5 HOH   347 747 86   HOH   HOH A . 
F 5 HOH   348 748 212  HOH   HOH A . 
F 5 HOH   349 749 338  HOH   HOH A . 
F 5 HOH   350 750 118  HOH   HOH A . 
F 5 HOH   351 751 248  HOH   HOH A . 
F 5 HOH   352 752 175  HOH   HOH A . 
F 5 HOH   353 753 148  HOH   HOH A . 
F 5 HOH   354 754 409  HOH   HOH A . 
F 5 HOH   355 755 290  HOH   HOH A . 
F 5 HOH   356 756 91   HOH   HOH A . 
F 5 HOH   357 757 383  HOH   HOH A . 
F 5 HOH   358 758 186  HOH   HOH A . 
F 5 HOH   359 759 142  HOH   HOH A . 
F 5 HOH   360 760 276  HOH   HOH A . 
F 5 HOH   361 761 274  HOH   HOH A . 
F 5 HOH   362 762 210  HOH   HOH A . 
F 5 HOH   363 763 124  HOH   HOH A . 
F 5 HOH   364 764 176  HOH   HOH A . 
F 5 HOH   365 765 293  HOH   HOH A . 
F 5 HOH   366 766 284  HOH   HOH A . 
F 5 HOH   367 767 345  HOH   HOH A . 
F 5 HOH   368 768 245  HOH   HOH A . 
F 5 HOH   369 769 321  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           7H6A 
_cell.length_a           74.200 
_cell.length_b           74.200 
_cell.length_c           49.370 
_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                         7H6A 
_symmetry.space_group_name_H-M             'P 43' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                78 
# 
_exptl.entry_id          7H6A 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.71 
_exptl_crystal.density_percent_sol   54.69 
_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   2006-01-25 
_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                     7H6A 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             19.00 
_reflns.d_resolution_high            1.68 
_reflns.number_obs                   30530 
_reflns.percent_possible_obs         99.3 
_reflns.pdbx_Rmerge_I_obs            0.044 
_reflns.pdbx_netI_over_sigmaI        19.04 
_reflns.pdbx_Rrim_I_all              0.053 
_reflns.pdbx_number_measured_all     97857 
_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 1.68 1.78  14552 4827 0.213 99.4  5.34  0.256 ? ? ? ? 
1 2 1.78 1.9   14393 4588 0.101 99.8  10.10 0.121 ? ? ? ? 
1 3 1.90 2.05  13488 4265 0.064 100.0 15.57 0.076 ? ? ? ? 
1 4 2.05 2.24  12683 3952 0.05  99.9  19.93 0.059 ? ? ? ? 
1 5 2.24 2.5   11746 3631 0.042 99.9  23.36 0.05  ? ? ? ? 
1 6 2.50 2.88  10636 3239 0.039 100.0 25.85 0.047 ? ? ? ? 
1 7 2.88 3.51  9048  2739 0.034 99.9  30.33 0.04  ? ? ? ? 
1 8 3.51 4.89  7133  2105 0.031 97.5  34.58 0.036 ? ? ? ? 
1 9 4.89 19.00 4178  1184 0.033 90.3  33.52 0.039 ? ? ? ? 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 7H6A 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     28984 
_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                             19.00 
_refine.ls_d_res_high                            1.68 
_refine.ls_percent_reflns_obs                    99.25 
_refine.ls_R_factor_obs                          0.14287 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.14121 
_refine.ls_R_factor_R_free                       0.17403 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.1 
_refine.ls_number_reflns_R_free                  1544 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.967 
_refine.correlation_coeff_Fo_to_Fc_free          0.948 
_refine.B_iso_mean                               11.645 
_refine.aniso_B[1][1]                            -0.03 
_refine.aniso_B[2][2]                            -0.03 
_refine.aniso_B[3][3]                            0.06 
_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                       0.081 
_refine.pdbx_overall_ESU_R_Free                  0.083 
_refine.overall_SU_ML                            0.050 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             1.493 
_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        1759 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         39 
_refine_hist.number_atoms_solvent             369 
_refine_hist.number_atoms_total               2167 
_refine_hist.d_res_high                       1.68 
_refine_hist.d_res_low                        19.00 
# 
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             0.007  0.012  ? 1916 'X-RAY DIFFRACTION' ? 
r_bond_other_d               0.001  0.016  ? 1823 'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.552  1.823  ? 2606 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            0.733  1.779  ? 4200 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       6.805  5.000  ? 240  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       6.406  5.000  ? 15   'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       10.660 10.000 ? 319  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.081  0.200  ? 280  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.009  0.020  ? 2289 'X-RAY DIFFRACTION' ? 
r_gen_planes_other           0.004  0.020  ? 457  '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                  0.947  1.125  ? 942  'X-RAY DIFFRACTION' ? 
r_mcbond_other               0.946  1.124  ? 942  'X-RAY DIFFRACTION' ? 
r_mcangle_it                 1.471  2.021  ? 1188 'X-RAY DIFFRACTION' ? 
r_mcangle_other              1.474  2.023  ? 1189 'X-RAY DIFFRACTION' ? 
r_scbond_it                  1.387  1.306  ? 974  'X-RAY DIFFRACTION' ? 
r_scbond_other               1.386  1.309  ? 975  'X-RAY DIFFRACTION' ? 
r_scangle_it                 ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_other              2.200  2.324  ? 1419 'X-RAY DIFFRACTION' ? 
r_long_range_B_refined       4.581  16.75  ? 2185 'X-RAY DIFFRACTION' ? 
r_long_range_B_other         3.942  11.77  ? 2061 '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                       1.680 
_refine_ls_shell.d_res_low                        1.723 
_refine_ls_shell.number_reflns_R_work             2126 
_refine_ls_shell.R_factor_R_work                  0.232 
_refine_ls_shell.percent_reflns_obs               99.32 
_refine_ls_shell.R_factor_R_free                  0.236 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             80 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
# 
_struct.entry_id                  7H6A 
_struct.title                     
;THE 1.68 A CRYSTAL STRUCTURE OF HUMAN CHYMASE IN COMPLEX WITH 3-[2-(dimethylamino)-2-oxoethyl]-5-fluoro-1-(naphthalen-1-ylmethyl)indole-2-carboxylic acid (2-carboxy indole)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7H6A 
_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 ? 
E N N 4 ? 
F N N 5 ? 
# 
_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              7H6A 
_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 7H6A SER A 7   ? UNP P23946 CYS 28  'engineered mutation' 22  1 
1 7H6A 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,E,F 
# 
_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 ILE A 212 ? ASN A 226 ? ILE A 231 ASN A 245 1 ? 15 
# 
_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 ? ? ? ? ? ? ? 2.032 ? ? 
disulf2 disulf ? ? A CYS 123 SG  ? ? ? 1_555 A CYS 188 SG ? ? A CYS 136 A CYS 201 1_555 ? ? ? ? ? ? ? 2.019 ? ? 
disulf3 disulf ? ? A CYS 154 SG  ? ? ? 1_555 A CYS 167 SG ? ? A CYS 168 A CYS 182 1_555 ? ? ? ? ? ? ? 2.061 ? ? 
metalc1 metalc ? ? A HIS 10  NE2 ? ? ? 1_555 B ZN  .   ZN ? ? A HIS 25  A ZN  301 1_555 ? ? ? ? ? ? ? 2.062 ? ? 
metalc2 metalc ? ? A GLU 64  OE2 ? ? ? 1_555 B ZN  .   ZN ? ? A GLU 77  A ZN  301 1_555 ? ? ? ? ? ? ? 1.951 ? ? 
metalc3 metalc ? ? A GLU 71  OE2 ? ? ? 1_555 B ZN  .   ZN ? ? A GLU 84  A ZN  301 2_455 ? ? ? ? ? ? ? 2.017 ? ? 
metalc4 metalc ? ? A LYS 96  NZ  ? ? ? 1_555 B ZN  .   ZN ? ? A LYS 109 A ZN  301 2_455 ? ? ? ? ? ? ? 2.088 ? ? 
# 
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 OE2 ? A GLU 64 ? A GLU 77  ? 1_555 122.8 ? 
2 NE2 ? A HIS 10 ? A HIS 25 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 OE2 ? A GLU 71 ? A GLU 84  ? 1_555 71.4  ? 
3 OE2 ? A GLU 64 ? A GLU 77 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 OE2 ? A GLU 71 ? A GLU 84  ? 1_555 51.6  ? 
4 NE2 ? A HIS 10 ? A HIS 25 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 NZ  ? A LYS 96 ? A LYS 109 ? 1_555 72.9  ? 
5 OE2 ? A GLU 64 ? A GLU 77 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 NZ  ? A LYS 96 ? A LYS 109 ? 1_555 51.2  ? 
6 OE2 ? A GLU 71 ? A GLU 84 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 NZ  ? A LYS 96 ? A LYS 109 ? 1_555 6.8   ? 
# 
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       1.14 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
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 
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 ? ARG A 147 ? GLN A 156 ARG A 161 
AA1 3 MET A 122 ? GLY A 127 ? MET A 135 GLY A 140 
AA1 4 PRO A 185 ? CYS A 188 ? PRO A 198 CYS A 201 
AA1 5 VAL A 191 ? TYR A 198 ? VAL A 208 TYR A 215 
AA1 6 ALA A 207 ? ARG A 211 ? ALA A 226 ARG A 230 
AA1 7 GLN A 165 ? VAL A 168 ? GLN A 180 VAL A 183 
AA2 1 MET A 15  ? THR A 22  A MET A 30  THR A 36  
AA2 2 GLY A 25  A ARG A 36  ? GLY A 37  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  ? THR A 22  A MET A 30  THR 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 O LEU A 146 ? O LEU A 160 N CYS A 123 ? N CYS A 136 
AA1 3 4 N ARG A 124 ? N ARG A 137 O LEU A 187 ? O LEU A 200 
AA1 4 5 N LEU A 186 ? N LEU A 199 O GLN A 193 ? O GLN A 210 
AA1 5 6 N TYR A 198 ? N TYR A 215 O VAL A 208 ? O VAL A 227 
AA1 6 7 O ALA A 207 ? O ALA A 226 N VAL A 168 ? N VAL A 183 
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 LEU A 70  ? O LEU A 83  N VAL A 53  ? N VAL A 66  
AA2 6 7 O SER A 50  ? O SER A 63  N VAL A 21  ? N VAL A 36  
# 
_pdbx_entry_details.entry_id                   7H6A 
_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 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   O 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   HOH 
_pdbx_validate_close_contact.auth_seq_id_1    649 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    724 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.00 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     567 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    A 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     652 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   2_455 
_pdbx_validate_symm_contact.dist              2.09 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 C  A LYS 148 ? ? N A PRO 150 ? ? CD A PRO 150 ? ? 106.91 128.40 -21.49 2.10 Y 
2 1 CA A PRO 150 ? ? N A PRO 150 ? ? CD A PRO 150 ? ? 101.01 111.70 -10.69 1.40 N 
# 
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 HIS A 71  ? ? -122.19 -74.12 
2 1 PRO A 150 ? ? -49.26  162.28 
# 
_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                       769 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   6.07 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1AO8 N1   N  Y N 1   
A1AO8 C4   C  Y N 2   
A1AO8 C5   C  Y N 3   
A1AO8 C6   C  N N 4   
A1AO8 C7   C  N N 5   
A1AO8 C8   C  N N 6   
A1AO8 C10  C  Y N 7   
A1AO8 C13  C  Y N 8   
A1AO8 C17  C  Y N 9   
A1AO8 C20  C  Y N 10  
A1AO8 C22  C  Y N 11  
A1AO8 C24  C  N N 12  
A1AO8 C26  C  Y N 13  
A1AO8 C28  C  Y N 14  
A1AO8 C2   C  Y N 15  
A1AO8 C3   C  Y N 16  
A1AO8 C9   C  N N 17  
A1AO8 C11  C  Y N 18  
A1AO8 C12  C  Y N 19  
A1AO8 N14  N  N N 20  
A1AO8 O15  O  N N 21  
A1AO8 O16  O  N N 22  
A1AO8 C18  C  Y N 23  
A1AO8 O19  O  N N 24  
A1AO8 F21  F  N N 25  
A1AO8 C23  C  Y N 26  
A1AO8 C25  C  N N 27  
A1AO8 C27  C  Y N 28  
A1AO8 C29  C  Y N 29  
A1AO8 C30  C  Y N 30  
A1AO8 H32  H  N N 31  
A1AO8 H31  H  N N 32  
A1AO8 H33  H  N N 33  
A1AO8 H34  H  N N 34  
A1AO8 H38  H  N N 35  
A1AO8 H39  H  N N 36  
A1AO8 H42  H  N N 37  
A1AO8 H41  H  N N 38  
A1AO8 H43  H  N N 39  
A1AO8 H47  H  N N 40  
A1AO8 H49  H  N N 41  
A1AO8 H35  H  N N 42  
A1AO8 H36  H  N N 43  
A1AO8 H37  H  N N 44  
A1AO8 H40  H  N N 45  
A1AO8 H45  H  N N 46  
A1AO8 H46  H  N N 47  
A1AO8 H44  H  N N 48  
A1AO8 H48  H  N N 49  
A1AO8 H50  H  N N 50  
A1AO8 H51  H  N N 51  
ALA   N    N  N N 52  
ALA   CA   C  N S 53  
ALA   C    C  N N 54  
ALA   O    O  N N 55  
ALA   CB   C  N N 56  
ALA   OXT  O  N N 57  
ALA   H    H  N N 58  
ALA   H2   H  N N 59  
ALA   HA   H  N N 60  
ALA   HB1  H  N N 61  
ALA   HB2  H  N N 62  
ALA   HB3  H  N N 63  
ALA   HXT  H  N N 64  
ARG   N    N  N N 65  
ARG   CA   C  N S 66  
ARG   C    C  N N 67  
ARG   O    O  N N 68  
ARG   CB   C  N N 69  
ARG   CG   C  N N 70  
ARG   CD   C  N N 71  
ARG   NE   N  N N 72  
ARG   CZ   C  N N 73  
ARG   NH1  N  N N 74  
ARG   NH2  N  N N 75  
ARG   OXT  O  N N 76  
ARG   H    H  N N 77  
ARG   H2   H  N N 78  
ARG   HA   H  N N 79  
ARG   HB2  H  N N 80  
ARG   HB3  H  N N 81  
ARG   HG2  H  N N 82  
ARG   HG3  H  N N 83  
ARG   HD2  H  N N 84  
ARG   HD3  H  N N 85  
ARG   HE   H  N N 86  
ARG   HH11 H  N N 87  
ARG   HH12 H  N N 88  
ARG   HH21 H  N N 89  
ARG   HH22 H  N N 90  
ARG   HXT  H  N N 91  
ASN   N    N  N N 92  
ASN   CA   C  N S 93  
ASN   C    C  N N 94  
ASN   O    O  N N 95  
ASN   CB   C  N N 96  
ASN   CG   C  N N 97  
ASN   OD1  O  N N 98  
ASN   ND2  N  N N 99  
ASN   OXT  O  N N 100 
ASN   H    H  N N 101 
ASN   H2   H  N N 102 
ASN   HA   H  N N 103 
ASN   HB2  H  N N 104 
ASN   HB3  H  N N 105 
ASN   HD21 H  N N 106 
ASN   HD22 H  N N 107 
ASN   HXT  H  N N 108 
ASP   N    N  N N 109 
ASP   CA   C  N S 110 
ASP   C    C  N N 111 
ASP   O    O  N N 112 
ASP   CB   C  N N 113 
ASP   CG   C  N N 114 
ASP   OD1  O  N N 115 
ASP   OD2  O  N N 116 
ASP   OXT  O  N N 117 
ASP   H    H  N N 118 
ASP   H2   H  N N 119 
ASP   HA   H  N N 120 
ASP   HB2  H  N N 121 
ASP   HB3  H  N N 122 
ASP   HD2  H  N N 123 
ASP   HXT  H  N N 124 
CYS   N    N  N N 125 
CYS   CA   C  N R 126 
CYS   C    C  N N 127 
CYS   O    O  N N 128 
CYS   CB   C  N N 129 
CYS   SG   S  N N 130 
CYS   OXT  O  N N 131 
CYS   H    H  N N 132 
CYS   H2   H  N N 133 
CYS   HA   H  N N 134 
CYS   HB2  H  N N 135 
CYS   HB3  H  N N 136 
CYS   HG   H  N N 137 
CYS   HXT  H  N N 138 
DMS   S    S  N N 139 
DMS   O    O  N N 140 
DMS   C1   C  N N 141 
DMS   C2   C  N N 142 
DMS   H11  H  N N 143 
DMS   H12  H  N N 144 
DMS   H13  H  N N 145 
DMS   H21  H  N N 146 
DMS   H22  H  N N 147 
DMS   H23  H  N N 148 
GLN   N    N  N N 149 
GLN   CA   C  N S 150 
GLN   C    C  N N 151 
GLN   O    O  N N 152 
GLN   CB   C  N N 153 
GLN   CG   C  N N 154 
GLN   CD   C  N N 155 
GLN   OE1  O  N N 156 
GLN   NE2  N  N N 157 
GLN   OXT  O  N N 158 
GLN   H    H  N N 159 
GLN   H2   H  N N 160 
GLN   HA   H  N N 161 
GLN   HB2  H  N N 162 
GLN   HB3  H  N N 163 
GLN   HG2  H  N N 164 
GLN   HG3  H  N N 165 
GLN   HE21 H  N N 166 
GLN   HE22 H  N N 167 
GLN   HXT  H  N N 168 
GLU   N    N  N N 169 
GLU   CA   C  N S 170 
GLU   C    C  N N 171 
GLU   O    O  N N 172 
GLU   CB   C  N N 173 
GLU   CG   C  N N 174 
GLU   CD   C  N N 175 
GLU   OE1  O  N N 176 
GLU   OE2  O  N N 177 
GLU   OXT  O  N N 178 
GLU   H    H  N N 179 
GLU   H2   H  N N 180 
GLU   HA   H  N N 181 
GLU   HB2  H  N N 182 
GLU   HB3  H  N N 183 
GLU   HG2  H  N N 184 
GLU   HG3  H  N N 185 
GLU   HE2  H  N N 186 
GLU   HXT  H  N N 187 
GLY   N    N  N N 188 
GLY   CA   C  N N 189 
GLY   C    C  N N 190 
GLY   O    O  N N 191 
GLY   OXT  O  N N 192 
GLY   H    H  N N 193 
GLY   H2   H  N N 194 
GLY   HA2  H  N N 195 
GLY   HA3  H  N N 196 
GLY   HXT  H  N N 197 
HIS   N    N  N N 198 
HIS   CA   C  N S 199 
HIS   C    C  N N 200 
HIS   O    O  N N 201 
HIS   CB   C  N N 202 
HIS   CG   C  Y N 203 
HIS   ND1  N  Y N 204 
HIS   CD2  C  Y N 205 
HIS   CE1  C  Y N 206 
HIS   NE2  N  Y N 207 
HIS   OXT  O  N N 208 
HIS   H    H  N N 209 
HIS   H2   H  N N 210 
HIS   HA   H  N N 211 
HIS   HB2  H  N N 212 
HIS   HB3  H  N N 213 
HIS   HD1  H  N N 214 
HIS   HD2  H  N N 215 
HIS   HE1  H  N N 216 
HIS   HE2  H  N N 217 
HIS   HXT  H  N N 218 
HOH   O    O  N N 219 
HOH   H1   H  N N 220 
HOH   H2   H  N N 221 
ILE   N    N  N N 222 
ILE   CA   C  N S 223 
ILE   C    C  N N 224 
ILE   O    O  N N 225 
ILE   CB   C  N S 226 
ILE   CG1  C  N N 227 
ILE   CG2  C  N N 228 
ILE   CD1  C  N N 229 
ILE   OXT  O  N N 230 
ILE   H    H  N N 231 
ILE   H2   H  N N 232 
ILE   HA   H  N N 233 
ILE   HB   H  N N 234 
ILE   HG12 H  N N 235 
ILE   HG13 H  N N 236 
ILE   HG21 H  N N 237 
ILE   HG22 H  N N 238 
ILE   HG23 H  N N 239 
ILE   HD11 H  N N 240 
ILE   HD12 H  N N 241 
ILE   HD13 H  N N 242 
ILE   HXT  H  N N 243 
LEU   N    N  N N 244 
LEU   CA   C  N S 245 
LEU   C    C  N N 246 
LEU   O    O  N N 247 
LEU   CB   C  N N 248 
LEU   CG   C  N N 249 
LEU   CD1  C  N N 250 
LEU   CD2  C  N N 251 
LEU   OXT  O  N N 252 
LEU   H    H  N N 253 
LEU   H2   H  N N 254 
LEU   HA   H  N N 255 
LEU   HB2  H  N N 256 
LEU   HB3  H  N N 257 
LEU   HG   H  N N 258 
LEU   HD11 H  N N 259 
LEU   HD12 H  N N 260 
LEU   HD13 H  N N 261 
LEU   HD21 H  N N 262 
LEU   HD22 H  N N 263 
LEU   HD23 H  N N 264 
LEU   HXT  H  N N 265 
LYS   N    N  N N 266 
LYS   CA   C  N S 267 
LYS   C    C  N N 268 
LYS   O    O  N N 269 
LYS   CB   C  N N 270 
LYS   CG   C  N N 271 
LYS   CD   C  N N 272 
LYS   CE   C  N N 273 
LYS   NZ   N  N N 274 
LYS   OXT  O  N N 275 
LYS   H    H  N N 276 
LYS   H2   H  N N 277 
LYS   HA   H  N N 278 
LYS   HB2  H  N N 279 
LYS   HB3  H  N N 280 
LYS   HG2  H  N N 281 
LYS   HG3  H  N N 282 
LYS   HD2  H  N N 283 
LYS   HD3  H  N N 284 
LYS   HE2  H  N N 285 
LYS   HE3  H  N N 286 
LYS   HZ1  H  N N 287 
LYS   HZ2  H  N N 288 
LYS   HZ3  H  N N 289 
LYS   HXT  H  N N 290 
MET   N    N  N N 291 
MET   CA   C  N S 292 
MET   C    C  N N 293 
MET   O    O  N N 294 
MET   CB   C  N N 295 
MET   CG   C  N N 296 
MET   SD   S  N N 297 
MET   CE   C  N N 298 
MET   OXT  O  N N 299 
MET   H    H  N N 300 
MET   H2   H  N N 301 
MET   HA   H  N N 302 
MET   HB2  H  N N 303 
MET   HB3  H  N N 304 
MET   HG2  H  N N 305 
MET   HG3  H  N N 306 
MET   HE1  H  N N 307 
MET   HE2  H  N N 308 
MET   HE3  H  N N 309 
MET   HXT  H  N N 310 
PHE   N    N  N N 311 
PHE   CA   C  N S 312 
PHE   C    C  N N 313 
PHE   O    O  N N 314 
PHE   CB   C  N N 315 
PHE   CG   C  Y N 316 
PHE   CD1  C  Y N 317 
PHE   CD2  C  Y N 318 
PHE   CE1  C  Y N 319 
PHE   CE2  C  Y N 320 
PHE   CZ   C  Y N 321 
PHE   OXT  O  N N 322 
PHE   H    H  N N 323 
PHE   H2   H  N N 324 
PHE   HA   H  N N 325 
PHE   HB2  H  N N 326 
PHE   HB3  H  N N 327 
PHE   HD1  H  N N 328 
PHE   HD2  H  N N 329 
PHE   HE1  H  N N 330 
PHE   HE2  H  N N 331 
PHE   HZ   H  N N 332 
PHE   HXT  H  N N 333 
PRO   N    N  N N 334 
PRO   CA   C  N S 335 
PRO   C    C  N N 336 
PRO   O    O  N N 337 
PRO   CB   C  N N 338 
PRO   CG   C  N N 339 
PRO   CD   C  N N 340 
PRO   OXT  O  N N 341 
PRO   H    H  N N 342 
PRO   HA   H  N N 343 
PRO   HB2  H  N N 344 
PRO   HB3  H  N N 345 
PRO   HG2  H  N N 346 
PRO   HG3  H  N N 347 
PRO   HD2  H  N N 348 
PRO   HD3  H  N N 349 
PRO   HXT  H  N N 350 
SER   N    N  N N 351 
SER   CA   C  N S 352 
SER   C    C  N N 353 
SER   O    O  N N 354 
SER   CB   C  N N 355 
SER   OG   O  N N 356 
SER   OXT  O  N N 357 
SER   H    H  N N 358 
SER   H2   H  N N 359 
SER   HA   H  N N 360 
SER   HB2  H  N N 361 
SER   HB3  H  N N 362 
SER   HG   H  N N 363 
SER   HXT  H  N N 364 
THR   N    N  N N 365 
THR   CA   C  N S 366 
THR   C    C  N N 367 
THR   O    O  N N 368 
THR   CB   C  N R 369 
THR   OG1  O  N N 370 
THR   CG2  C  N N 371 
THR   OXT  O  N N 372 
THR   H    H  N N 373 
THR   H2   H  N N 374 
THR   HA   H  N N 375 
THR   HB   H  N N 376 
THR   HG1  H  N N 377 
THR   HG21 H  N N 378 
THR   HG22 H  N N 379 
THR   HG23 H  N N 380 
THR   HXT  H  N N 381 
TRP   N    N  N N 382 
TRP   CA   C  N S 383 
TRP   C    C  N N 384 
TRP   O    O  N N 385 
TRP   CB   C  N N 386 
TRP   CG   C  Y N 387 
TRP   CD1  C  Y N 388 
TRP   CD2  C  Y N 389 
TRP   NE1  N  Y N 390 
TRP   CE2  C  Y N 391 
TRP   CE3  C  Y N 392 
TRP   CZ2  C  Y N 393 
TRP   CZ3  C  Y N 394 
TRP   CH2  C  Y N 395 
TRP   OXT  O  N N 396 
TRP   H    H  N N 397 
TRP   H2   H  N N 398 
TRP   HA   H  N N 399 
TRP   HB2  H  N N 400 
TRP   HB3  H  N N 401 
TRP   HD1  H  N N 402 
TRP   HE1  H  N N 403 
TRP   HE3  H  N N 404 
TRP   HZ2  H  N N 405 
TRP   HZ3  H  N N 406 
TRP   HH2  H  N N 407 
TRP   HXT  H  N N 408 
TYR   N    N  N N 409 
TYR   CA   C  N S 410 
TYR   C    C  N N 411 
TYR   O    O  N N 412 
TYR   CB   C  N N 413 
TYR   CG   C  Y N 414 
TYR   CD1  C  Y N 415 
TYR   CD2  C  Y N 416 
TYR   CE1  C  Y N 417 
TYR   CE2  C  Y N 418 
TYR   CZ   C  Y N 419 
TYR   OH   O  N N 420 
TYR   OXT  O  N N 421 
TYR   H    H  N N 422 
TYR   H2   H  N N 423 
TYR   HA   H  N N 424 
TYR   HB2  H  N N 425 
TYR   HB3  H  N N 426 
TYR   HD1  H  N N 427 
TYR   HD2  H  N N 428 
TYR   HE1  H  N N 429 
TYR   HE2  H  N N 430 
TYR   HH   H  N N 431 
TYR   HXT  H  N N 432 
VAL   N    N  N N 433 
VAL   CA   C  N S 434 
VAL   C    C  N N 435 
VAL   O    O  N N 436 
VAL   CB   C  N N 437 
VAL   CG1  C  N N 438 
VAL   CG2  C  N N 439 
VAL   OXT  O  N N 440 
VAL   H    H  N N 441 
VAL   H2   H  N N 442 
VAL   HA   H  N N 443 
VAL   HB   H  N N 444 
VAL   HG11 H  N N 445 
VAL   HG12 H  N N 446 
VAL   HG13 H  N N 447 
VAL   HG21 H  N N 448 
VAL   HG22 H  N N 449 
VAL   HG23 H  N N 450 
VAL   HXT  H  N N 451 
ZN    ZN   ZN N N 452 
# 
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 
A1AO8 N1  C6   sing N N 1   
A1AO8 N1  C5   sing Y N 2   
A1AO8 N1  C3   sing Y N 3   
A1AO8 C2  C3   doub Y N 4   
A1AO8 C2  C4   sing Y N 5   
A1AO8 C2  C7   sing N N 6   
A1AO8 C3  C9   sing N N 7   
A1AO8 C4  C12  doub Y N 8   
A1AO8 C4  C5   sing Y N 9   
A1AO8 C5  C11  doub Y N 10  
A1AO8 C6  C10  sing N N 11  
A1AO8 C7  C8   sing N N 12  
A1AO8 C8  N14  sing N N 13  
A1AO8 C8  O15  doub N N 14  
A1AO8 C9  O19  sing N N 15  
A1AO8 C9  O16  doub N N 16  
A1AO8 C10 C13  doub Y N 17  
A1AO8 C10 C22  sing Y N 18  
A1AO8 C11 C20  sing Y N 19  
A1AO8 C12 C17  sing Y N 20  
A1AO8 C13 C18  sing Y N 21  
A1AO8 C13 C26  sing Y N 22  
A1AO8 N14 C24  sing N N 23  
A1AO8 N14 C25  sing N N 24  
A1AO8 C17 C20  doub Y N 25  
A1AO8 C17 F21  sing N N 26  
A1AO8 C18 C28  sing Y N 27  
A1AO8 C18 C27  doub Y N 28  
A1AO8 C22 C23  doub Y N 29  
A1AO8 C23 C27  sing Y N 30  
A1AO8 C26 C29  doub Y N 31  
A1AO8 C28 C30  doub Y N 32  
A1AO8 C29 C30  sing Y N 33  
A1AO8 C6  H32  sing N N 34  
A1AO8 C6  H31  sing N N 35  
A1AO8 C7  H33  sing N N 36  
A1AO8 C7  H34  sing N N 37  
A1AO8 C20 H38  sing N N 38  
A1AO8 C22 H39  sing N N 39  
A1AO8 C24 H42  sing N N 40  
A1AO8 C24 H41  sing N N 41  
A1AO8 C24 H43  sing N N 42  
A1AO8 C26 H47  sing N N 43  
A1AO8 C28 H49  sing N N 44  
A1AO8 C11 H35  sing N N 45  
A1AO8 C12 H36  sing N N 46  
A1AO8 O19 H37  sing N N 47  
A1AO8 C23 H40  sing N N 48  
A1AO8 C25 H45  sing N N 49  
A1AO8 C25 H46  sing N N 50  
A1AO8 C25 H44  sing N N 51  
A1AO8 C27 H48  sing N N 52  
A1AO8 C29 H50  sing N N 53  
A1AO8 C30 H51  sing N N 54  
ALA   N   CA   sing N N 55  
ALA   N   H    sing N N 56  
ALA   N   H2   sing N N 57  
ALA   CA  C    sing N N 58  
ALA   CA  CB   sing N N 59  
ALA   CA  HA   sing N N 60  
ALA   C   O    doub N N 61  
ALA   C   OXT  sing N N 62  
ALA   CB  HB1  sing N N 63  
ALA   CB  HB2  sing N N 64  
ALA   CB  HB3  sing N N 65  
ALA   OXT HXT  sing N N 66  
ARG   N   CA   sing N N 67  
ARG   N   H    sing N N 68  
ARG   N   H2   sing N N 69  
ARG   CA  C    sing N N 70  
ARG   CA  CB   sing N N 71  
ARG   CA  HA   sing N N 72  
ARG   C   O    doub N N 73  
ARG   C   OXT  sing N N 74  
ARG   CB  CG   sing N N 75  
ARG   CB  HB2  sing N N 76  
ARG   CB  HB3  sing N N 77  
ARG   CG  CD   sing N N 78  
ARG   CG  HG2  sing N N 79  
ARG   CG  HG3  sing N N 80  
ARG   CD  NE   sing N N 81  
ARG   CD  HD2  sing N N 82  
ARG   CD  HD3  sing N N 83  
ARG   NE  CZ   sing N N 84  
ARG   NE  HE   sing N N 85  
ARG   CZ  NH1  sing N N 86  
ARG   CZ  NH2  doub N N 87  
ARG   NH1 HH11 sing N N 88  
ARG   NH1 HH12 sing N N 89  
ARG   NH2 HH21 sing N N 90  
ARG   NH2 HH22 sing N N 91  
ARG   OXT HXT  sing N N 92  
ASN   N   CA   sing N N 93  
ASN   N   H    sing N N 94  
ASN   N   H2   sing N N 95  
ASN   CA  C    sing N N 96  
ASN   CA  CB   sing N N 97  
ASN   CA  HA   sing N N 98  
ASN   C   O    doub N N 99  
ASN   C   OXT  sing N N 100 
ASN   CB  CG   sing N N 101 
ASN   CB  HB2  sing N N 102 
ASN   CB  HB3  sing N N 103 
ASN   CG  OD1  doub N N 104 
ASN   CG  ND2  sing N N 105 
ASN   ND2 HD21 sing N N 106 
ASN   ND2 HD22 sing N N 107 
ASN   OXT HXT  sing N N 108 
ASP   N   CA   sing N N 109 
ASP   N   H    sing N N 110 
ASP   N   H2   sing N N 111 
ASP   CA  C    sing N N 112 
ASP   CA  CB   sing N N 113 
ASP   CA  HA   sing N N 114 
ASP   C   O    doub N N 115 
ASP   C   OXT  sing N N 116 
ASP   CB  CG   sing N N 117 
ASP   CB  HB2  sing N N 118 
ASP   CB  HB3  sing N N 119 
ASP   CG  OD1  doub N N 120 
ASP   CG  OD2  sing N N 121 
ASP   OD2 HD2  sing N N 122 
ASP   OXT HXT  sing N N 123 
CYS   N   CA   sing N N 124 
CYS   N   H    sing N N 125 
CYS   N   H2   sing N N 126 
CYS   CA  C    sing N N 127 
CYS   CA  CB   sing N N 128 
CYS   CA  HA   sing N N 129 
CYS   C   O    doub N N 130 
CYS   C   OXT  sing N N 131 
CYS   CB  SG   sing N N 132 
CYS   CB  HB2  sing N N 133 
CYS   CB  HB3  sing N N 134 
CYS   SG  HG   sing N N 135 
CYS   OXT HXT  sing N N 136 
DMS   S   O    doub N N 137 
DMS   S   C1   sing N N 138 
DMS   S   C2   sing N N 139 
DMS   C1  H11  sing N N 140 
DMS   C1  H12  sing N N 141 
DMS   C1  H13  sing N N 142 
DMS   C2  H21  sing N N 143 
DMS   C2  H22  sing N N 144 
DMS   C2  H23  sing N N 145 
GLN   N   CA   sing N N 146 
GLN   N   H    sing N N 147 
GLN   N   H2   sing N N 148 
GLN   CA  C    sing N N 149 
GLN   CA  CB   sing N N 150 
GLN   CA  HA   sing N N 151 
GLN   C   O    doub N N 152 
GLN   C   OXT  sing N N 153 
GLN   CB  CG   sing N N 154 
GLN   CB  HB2  sing N N 155 
GLN   CB  HB3  sing N N 156 
GLN   CG  CD   sing N N 157 
GLN   CG  HG2  sing N N 158 
GLN   CG  HG3  sing N N 159 
GLN   CD  OE1  doub N N 160 
GLN   CD  NE2  sing N N 161 
GLN   NE2 HE21 sing N N 162 
GLN   NE2 HE22 sing N N 163 
GLN   OXT HXT  sing N N 164 
GLU   N   CA   sing N N 165 
GLU   N   H    sing N N 166 
GLU   N   H2   sing N N 167 
GLU   CA  C    sing N N 168 
GLU   CA  CB   sing N N 169 
GLU   CA  HA   sing N N 170 
GLU   C   O    doub N N 171 
GLU   C   OXT  sing N N 172 
GLU   CB  CG   sing N N 173 
GLU   CB  HB2  sing N N 174 
GLU   CB  HB3  sing N N 175 
GLU   CG  CD   sing N N 176 
GLU   CG  HG2  sing N N 177 
GLU   CG  HG3  sing N N 178 
GLU   CD  OE1  doub N N 179 
GLU   CD  OE2  sing N N 180 
GLU   OE2 HE2  sing N N 181 
GLU   OXT HXT  sing N N 182 
GLY   N   CA   sing N N 183 
GLY   N   H    sing N N 184 
GLY   N   H2   sing N N 185 
GLY   CA  C    sing N N 186 
GLY   CA  HA2  sing N N 187 
GLY   CA  HA3  sing N N 188 
GLY   C   O    doub N N 189 
GLY   C   OXT  sing N N 190 
GLY   OXT HXT  sing N N 191 
HIS   N   CA   sing N N 192 
HIS   N   H    sing N N 193 
HIS   N   H2   sing N N 194 
HIS   CA  C    sing N N 195 
HIS   CA  CB   sing N N 196 
HIS   CA  HA   sing N N 197 
HIS   C   O    doub N N 198 
HIS   C   OXT  sing N N 199 
HIS   CB  CG   sing N N 200 
HIS   CB  HB2  sing N N 201 
HIS   CB  HB3  sing N N 202 
HIS   CG  ND1  sing Y N 203 
HIS   CG  CD2  doub Y N 204 
HIS   ND1 CE1  doub Y N 205 
HIS   ND1 HD1  sing N N 206 
HIS   CD2 NE2  sing Y N 207 
HIS   CD2 HD2  sing N N 208 
HIS   CE1 NE2  sing Y N 209 
HIS   CE1 HE1  sing N N 210 
HIS   NE2 HE2  sing N N 211 
HIS   OXT HXT  sing N N 212 
HOH   O   H1   sing N N 213 
HOH   O   H2   sing N N 214 
ILE   N   CA   sing N N 215 
ILE   N   H    sing N N 216 
ILE   N   H2   sing N N 217 
ILE   CA  C    sing N N 218 
ILE   CA  CB   sing N N 219 
ILE   CA  HA   sing N N 220 
ILE   C   O    doub N N 221 
ILE   C   OXT  sing N N 222 
ILE   CB  CG1  sing N N 223 
ILE   CB  CG2  sing N N 224 
ILE   CB  HB   sing N N 225 
ILE   CG1 CD1  sing N N 226 
ILE   CG1 HG12 sing N N 227 
ILE   CG1 HG13 sing N N 228 
ILE   CG2 HG21 sing N N 229 
ILE   CG2 HG22 sing N N 230 
ILE   CG2 HG23 sing N N 231 
ILE   CD1 HD11 sing N N 232 
ILE   CD1 HD12 sing N N 233 
ILE   CD1 HD13 sing N N 234 
ILE   OXT HXT  sing N N 235 
LEU   N   CA   sing N N 236 
LEU   N   H    sing N N 237 
LEU   N   H2   sing N N 238 
LEU   CA  C    sing N N 239 
LEU   CA  CB   sing N N 240 
LEU   CA  HA   sing N N 241 
LEU   C   O    doub N N 242 
LEU   C   OXT  sing N N 243 
LEU   CB  CG   sing N N 244 
LEU   CB  HB2  sing N N 245 
LEU   CB  HB3  sing N N 246 
LEU   CG  CD1  sing N N 247 
LEU   CG  CD2  sing N N 248 
LEU   CG  HG   sing N N 249 
LEU   CD1 HD11 sing N N 250 
LEU   CD1 HD12 sing N N 251 
LEU   CD1 HD13 sing N N 252 
LEU   CD2 HD21 sing N N 253 
LEU   CD2 HD22 sing N N 254 
LEU   CD2 HD23 sing N N 255 
LEU   OXT HXT  sing N N 256 
LYS   N   CA   sing N N 257 
LYS   N   H    sing N N 258 
LYS   N   H2   sing N N 259 
LYS   CA  C    sing N N 260 
LYS   CA  CB   sing N N 261 
LYS   CA  HA   sing N N 262 
LYS   C   O    doub N N 263 
LYS   C   OXT  sing N N 264 
LYS   CB  CG   sing N N 265 
LYS   CB  HB2  sing N N 266 
LYS   CB  HB3  sing N N 267 
LYS   CG  CD   sing N N 268 
LYS   CG  HG2  sing N N 269 
LYS   CG  HG3  sing N N 270 
LYS   CD  CE   sing N N 271 
LYS   CD  HD2  sing N N 272 
LYS   CD  HD3  sing N N 273 
LYS   CE  NZ   sing N N 274 
LYS   CE  HE2  sing N N 275 
LYS   CE  HE3  sing N N 276 
LYS   NZ  HZ1  sing N N 277 
LYS   NZ  HZ2  sing N N 278 
LYS   NZ  HZ3  sing N N 279 
LYS   OXT HXT  sing N N 280 
MET   N   CA   sing N N 281 
MET   N   H    sing N N 282 
MET   N   H2   sing N N 283 
MET   CA  C    sing N N 284 
MET   CA  CB   sing N N 285 
MET   CA  HA   sing N N 286 
MET   C   O    doub N N 287 
MET   C   OXT  sing N N 288 
MET   CB  CG   sing N N 289 
MET   CB  HB2  sing N N 290 
MET   CB  HB3  sing N N 291 
MET   CG  SD   sing N N 292 
MET   CG  HG2  sing N N 293 
MET   CG  HG3  sing N N 294 
MET   SD  CE   sing N N 295 
MET   CE  HE1  sing N N 296 
MET   CE  HE2  sing N N 297 
MET   CE  HE3  sing N N 298 
MET   OXT HXT  sing N N 299 
PHE   N   CA   sing N N 300 
PHE   N   H    sing N N 301 
PHE   N   H2   sing N N 302 
PHE   CA  C    sing N N 303 
PHE   CA  CB   sing N N 304 
PHE   CA  HA   sing N N 305 
PHE   C   O    doub N N 306 
PHE   C   OXT  sing N N 307 
PHE   CB  CG   sing N N 308 
PHE   CB  HB2  sing N N 309 
PHE   CB  HB3  sing N N 310 
PHE   CG  CD1  doub Y N 311 
PHE   CG  CD2  sing Y N 312 
PHE   CD1 CE1  sing Y N 313 
PHE   CD1 HD1  sing N N 314 
PHE   CD2 CE2  doub Y N 315 
PHE   CD2 HD2  sing N N 316 
PHE   CE1 CZ   doub Y N 317 
PHE   CE1 HE1  sing N N 318 
PHE   CE2 CZ   sing Y N 319 
PHE   CE2 HE2  sing N N 320 
PHE   CZ  HZ   sing N N 321 
PHE   OXT HXT  sing N N 322 
PRO   N   CA   sing N N 323 
PRO   N   CD   sing N N 324 
PRO   N   H    sing N N 325 
PRO   CA  C    sing N N 326 
PRO   CA  CB   sing N N 327 
PRO   CA  HA   sing N N 328 
PRO   C   O    doub N N 329 
PRO   C   OXT  sing N N 330 
PRO   CB  CG   sing N N 331 
PRO   CB  HB2  sing N N 332 
PRO   CB  HB3  sing N N 333 
PRO   CG  CD   sing N N 334 
PRO   CG  HG2  sing N N 335 
PRO   CG  HG3  sing N N 336 
PRO   CD  HD2  sing N N 337 
PRO   CD  HD3  sing N N 338 
PRO   OXT HXT  sing N N 339 
SER   N   CA   sing N N 340 
SER   N   H    sing N N 341 
SER   N   H2   sing N N 342 
SER   CA  C    sing N N 343 
SER   CA  CB   sing N N 344 
SER   CA  HA   sing N N 345 
SER   C   O    doub N N 346 
SER   C   OXT  sing N N 347 
SER   CB  OG   sing N N 348 
SER   CB  HB2  sing N N 349 
SER   CB  HB3  sing N N 350 
SER   OG  HG   sing N N 351 
SER   OXT HXT  sing N N 352 
THR   N   CA   sing N N 353 
THR   N   H    sing N N 354 
THR   N   H2   sing N N 355 
THR   CA  C    sing N N 356 
THR   CA  CB   sing N N 357 
THR   CA  HA   sing N N 358 
THR   C   O    doub N N 359 
THR   C   OXT  sing N N 360 
THR   CB  OG1  sing N N 361 
THR   CB  CG2  sing N N 362 
THR   CB  HB   sing N N 363 
THR   OG1 HG1  sing N N 364 
THR   CG2 HG21 sing N N 365 
THR   CG2 HG22 sing N N 366 
THR   CG2 HG23 sing N N 367 
THR   OXT HXT  sing N N 368 
TRP   N   CA   sing N N 369 
TRP   N   H    sing N N 370 
TRP   N   H2   sing N N 371 
TRP   CA  C    sing N N 372 
TRP   CA  CB   sing N N 373 
TRP   CA  HA   sing N N 374 
TRP   C   O    doub N N 375 
TRP   C   OXT  sing N N 376 
TRP   CB  CG   sing N N 377 
TRP   CB  HB2  sing N N 378 
TRP   CB  HB3  sing N N 379 
TRP   CG  CD1  doub Y N 380 
TRP   CG  CD2  sing Y N 381 
TRP   CD1 NE1  sing Y N 382 
TRP   CD1 HD1  sing N N 383 
TRP   CD2 CE2  doub Y N 384 
TRP   CD2 CE3  sing Y N 385 
TRP   NE1 CE2  sing Y N 386 
TRP   NE1 HE1  sing N N 387 
TRP   CE2 CZ2  sing Y N 388 
TRP   CE3 CZ3  doub Y N 389 
TRP   CE3 HE3  sing N N 390 
TRP   CZ2 CH2  doub Y N 391 
TRP   CZ2 HZ2  sing N N 392 
TRP   CZ3 CH2  sing Y N 393 
TRP   CZ3 HZ3  sing N N 394 
TRP   CH2 HH2  sing N N 395 
TRP   OXT HXT  sing N N 396 
TYR   N   CA   sing N N 397 
TYR   N   H    sing N N 398 
TYR   N   H2   sing N N 399 
TYR   CA  C    sing N N 400 
TYR   CA  CB   sing N N 401 
TYR   CA  HA   sing N N 402 
TYR   C   O    doub N N 403 
TYR   C   OXT  sing N N 404 
TYR   CB  CG   sing N N 405 
TYR   CB  HB2  sing N N 406 
TYR   CB  HB3  sing N N 407 
TYR   CG  CD1  doub Y N 408 
TYR   CG  CD2  sing Y N 409 
TYR   CD1 CE1  sing Y N 410 
TYR   CD1 HD1  sing N N 411 
TYR   CD2 CE2  doub Y N 412 
TYR   CD2 HD2  sing N N 413 
TYR   CE1 CZ   doub Y N 414 
TYR   CE1 HE1  sing N N 415 
TYR   CE2 CZ   sing Y N 416 
TYR   CE2 HE2  sing N N 417 
TYR   CZ  OH   sing N N 418 
TYR   OH  HH   sing N N 419 
TYR   OXT HXT  sing N N 420 
VAL   N   CA   sing N N 421 
VAL   N   H    sing N N 422 
VAL   N   H2   sing N N 423 
VAL   CA  C    sing N N 424 
VAL   CA  CB   sing N N 425 
VAL   CA  HA   sing N N 426 
VAL   C   O    doub N N 427 
VAL   C   OXT  sing N N 428 
VAL   CB  CG1  sing N N 429 
VAL   CB  CG2  sing N N 430 
VAL   CB  HB   sing N N 431 
VAL   CG1 HG11 sing N N 432 
VAL   CG1 HG12 sing N N 433 
VAL   CG1 HG13 sing N N 434 
VAL   CG2 HG21 sing N N 435 
VAL   CG2 HG22 sing N N 436 
VAL   CG2 HG23 sing N N 437 
VAL   OXT HXT  sing N N 438 
# 
_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                    7H6A 
_atom_sites.fract_transf_matrix[1][1]   0.013477 
_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]   0.013477 
_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]   0.020255 
_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   ? -29.840 21.135  -4.944  1.00 8.75  ? 16  ILE   A N   1 
ATOM   2    C  CA  . ILE   A 1 1   ? -28.900 21.497  -6.049  1.00 8.67  ? 16  ILE   A CA  1 
ATOM   3    C  C   . ILE   A 1 1   ? -29.362 22.831  -6.627  1.00 9.44  ? 16  ILE   A C   1 
ATOM   4    O  O   . ILE   A 1 1   ? -30.496 22.938  -7.096  1.00 9.08  ? 16  ILE   A O   1 
ATOM   5    C  CB  . ILE   A 1 1   ? -28.848 20.402  -7.143  1.00 8.83  ? 16  ILE   A CB  1 
ATOM   6    C  CG1 . ILE   A 1 1   ? -28.396 19.039  -6.635  1.00 8.50  ? 16  ILE   A CG1 1 
ATOM   7    C  CG2 . ILE   A 1 1   ? -27.989 20.826  -8.321  1.00 9.30  ? 16  ILE   A CG2 1 
ATOM   8    C  CD1 . ILE   A 1 1   ? -26.956 18.956  -6.156  1.00 8.39  ? 16  ILE   A CD1 1 
ATOM   9    N  N   . ILE   A 1 2   ? -28.468 23.834  -6.617  1.00 9.94  ? 17  ILE   A N   1 
ATOM   10   C  CA  . ILE   A 1 2   ? -28.744 25.133  -7.215  1.00 10.38 ? 17  ILE   A CA  1 
ATOM   11   C  C   . ILE   A 1 2   ? -28.064 25.198  -8.582  1.00 10.20 ? 17  ILE   A C   1 
ATOM   12   O  O   . ILE   A 1 2   ? -26.876 24.909  -8.722  1.00 10.18 ? 17  ILE   A O   1 
ATOM   13   C  CB  . ILE   A 1 2   ? -28.273 26.291  -6.316  1.00 10.47 ? 17  ILE   A CB  1 
ATOM   14   C  CG1 . ILE   A 1 2   ? -28.936 26.229  -4.954  1.00 11.54 ? 17  ILE   A CG1 1 
ATOM   15   C  CG2 . ILE   A 1 2   ? -28.510 27.640  -7.015  1.00 10.58 ? 17  ILE   A CG2 1 
ATOM   16   C  CD1 . ILE   A 1 2   ? -28.404 27.238  -3.962  1.00 12.01 ? 17  ILE   A CD1 1 
ATOM   17   N  N   . GLY   A 1 3   ? -28.831 25.603  -9.611  1.00 12.02 ? 18  GLY   A N   1 
ATOM   18   C  CA  . GLY   A 1 3   ? -28.240 25.931  -10.899 1.00 12.80 ? 18  GLY   A CA  1 
ATOM   19   C  C   . GLY   A 1 3   ? -27.898 24.703  -11.741 1.00 12.84 ? 18  GLY   A C   1 
ATOM   20   O  O   . GLY   A 1 3   ? -27.077 24.771  -12.648 1.00 13.44 ? 18  GLY   A O   1 
ATOM   21   N  N   . GLY   A 1 4   ? -28.558 23.576  -11.462 1.00 12.59 ? 19  GLY   A N   1 
ATOM   22   C  CA  . GLY   A 1 4   ? -28.254 22.329  -12.131 1.00 12.35 ? 19  GLY   A CA  1 
ATOM   23   C  C   . GLY   A 1 4   ? -29.345 21.965  -13.134 1.00 12.30 ? 19  GLY   A C   1 
ATOM   24   O  O   . GLY   A 1 4   ? -30.137 22.818  -13.556 1.00 13.32 ? 19  GLY   A O   1 
ATOM   25   N  N   . THR   A 1 5   ? -29.366 20.685  -13.485 1.00 11.86 ? 20  THR   A N   1 
ATOM   26   C  CA  . THR   A 1 5   ? -30.305 20.129  -14.453 1.00 12.52 ? 20  THR   A CA  1 
ATOM   27   C  C   . THR   A 1 5   ? -31.015 18.948  -13.794 1.00 13.29 ? 20  THR   A C   1 
ATOM   28   O  O   . THR   A 1 5   ? -30.443 18.295  -12.917 1.00 13.23 ? 20  THR   A O   1 
ATOM   29   C  CB  . THR   A 1 5   ? -29.532 19.681  -15.693 1.00 13.09 ? 20  THR   A CB  1 
ATOM   30   O  OG1 . THR   A 1 5   ? -28.510 18.785  -15.265 1.00 13.80 ? 20  THR   A OG1 1 
ATOM   31   C  CG2 . THR   A 1 5   ? -28.848 20.820  -16.432 1.00 15.08 ? 20  THR   A CG2 1 
ATOM   32   N  N   . GLU   A 1 6   ? -32.216 18.605  -14.281 1.00 12.17 ? 21  GLU   A N   1 
ATOM   33   C  CA  . GLU   A 1 6   ? -32.839 17.335  -13.901 1.00 12.60 ? 21  GLU   A CA  1 
ATOM   34   C  C   . GLU   A 1 6   ? -31.998 16.163  -14.426 1.00 11.65 ? 21  GLU   A C   1 
ATOM   35   O  O   . GLU   A 1 6   ? -31.658 16.104  -15.614 1.00 12.46 ? 21  GLU   A O   1 
ATOM   36   C  CB  . GLU   A 1 6   ? -34.284 17.252  -14.423 1.00 13.87 ? 21  GLU   A CB  1 
ATOM   37   C  CG  . GLU   A 1 6   ? -35.064 16.037  -13.920 1.00 14.81 ? 21  GLU   A CG  1 
ATOM   38   C  CD  . GLU   A 1 6   ? -36.507 15.950  -14.376 1.00 18.35 ? 21  GLU   A CD  1 
ATOM   39   O  OE1 . GLU   A 1 6   ? -36.992 16.966  -14.972 1.00 19.03 ? 21  GLU   A OE1 1 
ATOM   40   O  OE2 . GLU   A 1 6   ? -37.132 14.871  -14.172 1.00 15.88 ? 21  GLU   A OE2 1 
ATOM   41   N  N   . SER   A 1 7   ? -31.656 15.204  -13.539 1.00 10.62 ? 22  SER   A N   1 
ATOM   42   C  CA  . SER   A 1 7   ? -30.971 13.985  -13.939 1.00 10.13 ? 22  SER   A CA  1 
ATOM   43   C  C   . SER   A 1 7   ? -31.841 13.187  -14.917 1.00 10.13 ? 22  SER   A C   1 
ATOM   44   O  O   . SER   A 1 7   ? -33.060 13.156  -14.771 1.00 9.70  ? 22  SER   A O   1 
ATOM   45   C  CB  . SER   A 1 7   ? -30.623 13.144  -12.724 1.00 9.78  ? 22  SER   A CB  1 
ATOM   46   O  OG  . SER   A 1 7   ? -29.710 13.813  -11.845 1.00 9.95  ? 22  SER   A OG  1 
ATOM   47   N  N   . LYS   A 1 8   ? -31.204 12.510  -15.883 1.00 10.67 ? 23  LYS   A N   1 
ATOM   48   C  CA  . LYS   A 1 8   ? -31.923 11.502  -16.648 1.00 11.94 ? 23  LYS   A CA  1 
ATOM   49   C  C   . LYS   A 1 8   ? -32.430 10.444  -15.667 1.00 11.16 ? 23  LYS   A C   1 
ATOM   50   O  O   . LYS   A 1 8   ? -31.661 9.939   -14.839 1.00 11.28 ? 23  LYS   A O   1 
ATOM   51   C  CB  . LYS   A 1 8   ? -31.045 10.865  -17.722 1.00 12.13 ? 23  LYS   A CB  1 
ATOM   52   C  CG  . LYS   A 1 8   ? -31.664 9.718   -18.521 1.00 13.82 ? 23  LYS   A CG  1 
ATOM   53   C  CD  . LYS   A 1 8   ? -30.668 9.088   -19.483 0.50 14.01 ? 23  LYS   A CD  1 
ATOM   54   C  CE  . LYS   A 1 8   ? -31.306 7.893   -20.133 0.50 15.07 ? 23  LYS   A CE  1 
ATOM   55   N  NZ  . LYS   A 1 8   ? -30.515 7.460   -21.276 0.50 16.10 ? 23  LYS   A NZ  1 
ATOM   56   N  N   . PRO   A 1 9   ? -33.733 10.105  -15.657 1.00 10.85 ? 24  PRO   A N   1 
ATOM   57   C  CA  . PRO   A 1 9   ? -34.248 9.228   -14.599 1.00 9.99  ? 24  PRO   A CA  1 
ATOM   58   C  C   . PRO   A 1 9   ? -33.494 7.901   -14.518 1.00 9.59  ? 24  PRO   A C   1 
ATOM   59   O  O   . PRO   A 1 9   ? -33.258 7.251   -15.540 1.00 10.23 ? 24  PRO   A O   1 
ATOM   60   C  CB  . PRO   A 1 9   ? -35.715 9.096   -14.988 1.00 11.21 ? 24  PRO   A CB  1 
ATOM   61   C  CG  . PRO   A 1 9   ? -36.018 10.400  -15.713 1.00 10.78 ? 24  PRO   A CG  1 
ATOM   62   C  CD  . PRO   A 1 9   ? -34.797 10.610  -16.548 1.00 10.84 ? 24  PRO   A CD  1 
ATOM   63   N  N   . HIS   A 1 10  ? -33.046 7.554   -13.299 1.00 8.82  ? 25  HIS   A N   1 
ATOM   64   C  CA  . HIS   A 1 10  ? -32.397 6.288   -12.984 1.00 8.93  ? 25  HIS   A CA  1 
ATOM   65   C  C   . HIS   A 1 10  ? -30.984 6.188   -13.565 1.00 8.76  ? 25  HIS   A C   1 
ATOM   66   O  O   . HIS   A 1 10  ? -30.382 5.114   -13.519 1.00 8.19  ? 25  HIS   A O   1 
ATOM   67   C  CB  . HIS   A 1 10  ? -33.261 5.086   -13.401 1.00 9.19  ? 25  HIS   A CB  1 
ATOM   68   C  CG  . HIS   A 1 10  ? -34.676 5.176   -12.954 1.00 9.13  ? 25  HIS   A CG  1 
ATOM   69   N  ND1 . HIS   A 1 10  ? -35.033 5.247   -11.626 1.00 8.22  ? 25  HIS   A ND1 1 
ATOM   70   C  CD2 . HIS   A 1 10  ? -35.832 5.216   -13.648 1.00 9.72  ? 25  HIS   A CD2 1 
ATOM   71   C  CE1 . HIS   A 1 10  ? -36.356 5.353   -11.529 1.00 9.69  ? 25  HIS   A CE1 1 
ATOM   72   N  NE2 . HIS   A 1 10  ? -36.855 5.324   -12.733 1.00 9.83  ? 25  HIS   A NE2 1 
ATOM   73   N  N   . SER   A 1 11  ? -30.415 7.314   -14.035 1.00 8.93  ? 26  SER   A N   1 
ATOM   74   C  CA  . SER   A 1 11  ? -29.075 7.339   -14.598 1.00 9.21  ? 26  SER   A CA  1 
ATOM   75   C  C   . SER   A 1 11  ? -27.962 7.296   -13.553 1.00 9.42  ? 26  SER   A C   1 
ATOM   76   O  O   . SER   A 1 11  ? -26.814 7.072   -13.934 1.00 8.85  ? 26  SER   A O   1 
ATOM   77   C  CB  . SER   A 1 11  ? -28.861 8.560   -15.490 1.00 9.47  ? 26  SER   A CB  1 
ATOM   78   O  OG  . SER   A 1 11  ? -28.962 9.773   -14.754 1.00 10.23 ? 26  SER   A OG  1 
ATOM   79   N  N   . ARG   A 1 12  ? -28.289 7.504   -12.265 1.00 8.65  ? 27  ARG   A N   1 
ATOM   80   C  CA  . ARG   A 1 12  ? -27.349 7.365   -11.161 1.00 9.20  ? 27  ARG   A CA  1 
ATOM   81   C  C   . ARG   A 1 12  ? -27.879 6.313   -10.186 1.00 8.52  ? 27  ARG   A C   1 
ATOM   82   O  O   . ARG   A 1 12  ? -28.415 6.637   -9.113  1.00 7.58  ? 27  ARG   A O   1 
ATOM   83   C  CB  . ARG   A 1 12  ? -27.157 8.739   -10.517 1.00 10.09 ? 27  ARG   A CB  1 
ATOM   84   C  CG  . ARG   A 1 12  ? -26.541 9.758   -11.478 1.00 11.90 ? 27  ARG   A CG  1 
ATOM   85   C  CD  . ARG   A 1 12  ? -26.212 11.047  -10.718 1.00 13.79 ? 27  ARG   A CD  1 
ATOM   86   N  NE  . ARG   A 1 12  ? -25.567 12.028  -11.613 1.00 15.31 ? 27  ARG   A NE  1 
ATOM   87   C  CZ  . ARG   A 1 12  ? -24.298 12.005  -11.979 1.00 15.68 ? 27  ARG   A CZ  1 
ATOM   88   N  NH1 . ARG   A 1 12  ? -23.465 11.185  -11.377 1.00 16.32 ? 27  ARG   A NH1 1 
ATOM   89   N  NH2 . ARG   A 1 12  ? -23.840 12.850  -12.909 1.00 16.48 ? 27  ARG   A NH2 1 
ATOM   90   N  N   . PRO   A 1 13  ? -27.805 5.015   -10.556 1.00 8.28  ? 28  PRO   A N   1 
ATOM   91   C  CA  . PRO   A 1 13  ? -28.558 3.984   -9.828  1.00 7.80  ? 28  PRO   A CA  1 
ATOM   92   C  C   . PRO   A 1 13  ? -28.113 3.643   -8.406  1.00 7.24  ? 28  PRO   A C   1 
ATOM   93   O  O   . PRO   A 1 13  ? -28.844 2.967   -7.684  1.00 7.20  ? 28  PRO   A O   1 
ATOM   94   C  CB  . PRO   A 1 13  ? -28.444 2.772   -10.768 1.00 8.51  ? 28  PRO   A CB  1 
ATOM   95   C  CG  . PRO   A 1 13  ? -27.211 3.017   -11.592 1.00 8.98  ? 28  PRO   A CG  1 
ATOM   96   C  CD  . PRO   A 1 13  ? -27.112 4.489   -11.751 1.00 9.06  ? 28  PRO   A CD  1 
ATOM   97   N  N   . TYR   A 1 14  ? -26.971 4.192   -7.991  1.00 7.15  ? 29  TYR   A N   1 
ATOM   98   C  CA  . TYR   A 1 14  ? -26.437 4.087   -6.635  1.00 7.19  ? 29  TYR   A CA  1 
ATOM   99   C  C   . TYR   A 1 14  ? -27.024 5.155   -5.695  1.00 7.04  ? 29  TYR   A C   1 
ATOM   100  O  O   . TYR   A 1 14  ? -26.764 5.092   -4.497  1.00 6.96  ? 29  TYR   A O   1 
ATOM   101  C  CB  . TYR   A 1 14  ? -24.905 4.251   -6.678  1.00 7.12  ? 29  TYR   A CB  1 
ATOM   102  C  CG  . TYR   A 1 14  ? -24.467 5.416   -7.561  1.00 7.66  ? 29  TYR   A CG  1 
ATOM   103  C  CD1 . TYR   A 1 14  ? -24.502 6.732   -7.090  1.00 8.21  ? 29  TYR   A CD1 1 
ATOM   104  C  CD2 . TYR   A 1 14  ? -24.074 5.220   -8.883  1.00 7.78  ? 29  TYR   A CD2 1 
ATOM   105  C  CE1 . TYR   A 1 14  ? -24.187 7.810   -7.913  1.00 8.55  ? 29  TYR   A CE1 1 
ATOM   106  C  CE2 . TYR   A 1 14  ? -23.753 6.295   -9.703  1.00 8.23  ? 29  TYR   A CE2 1 
ATOM   107  C  CZ  . TYR   A 1 14  ? -23.761 7.585   -9.208  1.00 8.57  ? 29  TYR   A CZ  1 
ATOM   108  O  OH  . TYR   A 1 14  ? -23.485 8.628   -10.079 1.00 9.98  ? 29  TYR   A OH  1 
ATOM   109  N  N   . MET   A 1 15  ? -27.804 6.136   -6.199  1.00 6.65  ? 30  MET   A N   1 
ATOM   110  C  CA  . MET   A 1 15  ? -28.274 7.232   -5.350  1.00 6.72  ? 30  MET   A CA  1 
ATOM   111  C  C   . MET   A 1 15  ? -29.311 6.761   -4.324  1.00 6.80  ? 30  MET   A C   1 
ATOM   112  O  O   . MET   A 1 15  ? -30.207 5.976   -4.649  1.00 7.13  ? 30  MET   A O   1 
ATOM   113  C  CB  . MET   A 1 15  ? -28.865 8.386   -6.170  1.00 6.88  ? 30  MET   A CB  1 
ATOM   114  C  CG  . MET   A 1 15  ? -27.815 9.193   -6.923  1.00 7.41  ? 30  MET   A CG  1 
ATOM   115  S  SD  . MET   A 1 15  ? -26.664 10.053  -5.822  1.00 7.97  ? 30  MET   A SD  1 
ATOM   116  C  CE  . MET   A 1 15  ? -27.739 10.991  -4.726  1.00 7.77  ? 30  MET   A CE  1 
ATOM   117  N  N   . ALA   A 1 16  ? -29.150 7.242   -3.087  1.00 6.65  ? 31  ALA   A N   1 
ATOM   118  C  CA  . ALA   A 1 16  ? -30.005 6.875   -1.972  1.00 6.75  ? 31  ALA   A CA  1 
ATOM   119  C  C   . ALA   A 1 16  ? -30.673 8.135   -1.432  1.00 7.07  ? 31  ALA   A C   1 
ATOM   120  O  O   . ALA   A 1 16  ? -30.015 9.157   -1.241  1.00 7.00  ? 31  ALA   A O   1 
ATOM   121  C  CB  . ALA   A 1 16  ? -29.212 6.171   -0.882  1.00 6.55  ? 31  ALA   A CB  1 
ATOM   122  N  N   . TYR   A 1 17  ? -31.977 8.028   -1.150  1.00 6.71  ? 32  TYR   A N   1 
ATOM   123  C  CA  . TYR   A 1 17  ? -32.753 9.074   -0.494  1.00 7.31  ? 32  TYR   A CA  1 
ATOM   124  C  C   . TYR   A 1 17  ? -33.034 8.637   0.944   1.00 7.45  ? 32  TYR   A C   1 
ATOM   125  O  O   . TYR   A 1 17  ? -33.624 7.571   1.170   1.00 7.34  ? 32  TYR   A O   1 
ATOM   126  C  CB  . TYR   A 1 17  ? -34.057 9.272   -1.273  1.00 8.12  ? 32  TYR   A CB  1 
ATOM   127  C  CG  . TYR   A 1 17  ? -34.996 10.341  -0.735  1.00 9.44  ? 32  TYR   A CG  1 
ATOM   128  C  CD1 . TYR   A 1 17  ? -34.885 11.664  -1.138  1.00 10.52 ? 32  TYR   A CD1 1 
ATOM   129  C  CD2 . TYR   A 1 17  ? -35.997 10.021  0.176   1.00 10.91 ? 32  TYR   A CD2 1 
ATOM   130  C  CE1 . TYR   A 1 17  ? -35.744 12.643  -0.662  1.00 11.26 ? 32  TYR   A CE1 1 
ATOM   131  C  CE2 . TYR   A 1 17  ? -36.872 10.984  0.647   1.00 12.19 ? 32  TYR   A CE2 1 
ATOM   132  C  CZ  . TYR   A 1 17  ? -36.748 12.298  0.219   1.00 12.55 ? 32  TYR   A CZ  1 
ATOM   133  O  OH  . TYR   A 1 17  ? -37.640 13.254  0.652   1.00 14.92 ? 32  TYR   A OH  1 
ATOM   134  N  N   . LEU   A 1 18  ? -32.578 9.441   1.918   1.00 7.15  ? 33  LEU   A N   1 
ATOM   135  C  CA  . LEU   A 1 18  ? -32.639 9.104   3.332   1.00 7.80  ? 33  LEU   A CA  1 
ATOM   136  C  C   . LEU   A 1 18  ? -33.669 9.980   4.047   1.00 8.39  ? 33  LEU   A C   1 
ATOM   137  O  O   . LEU   A 1 18  ? -33.575 11.208  3.955   1.00 7.68  ? 33  LEU   A O   1 
ATOM   138  C  CB  . LEU   A 1 18  ? -31.268 9.353   3.952   1.00 8.54  ? 33  LEU   A CB  1 
ATOM   139  C  CG  . LEU   A 1 18  ? -30.186 8.282   3.764   1.00 9.89  ? 33  LEU   A CG  1 
ATOM   140  C  CD1 . LEU   A 1 18  ? -29.994 7.846   2.357   1.00 11.16 ? 33  LEU   A CD1 1 
ATOM   141  C  CD2 . LEU   A 1 18  ? -28.879 8.797   4.377   1.00 9.40  ? 33  LEU   A CD2 1 
ATOM   142  N  N   . GLU   A 1 19  ? -34.570 9.332   4.803   1.00 9.70  ? 34  GLU   A N   1 
ATOM   143  C  CA  . GLU   A 1 19  ? -35.468 10.021  5.725   1.00 10.66 ? 34  GLU   A CA  1 
ATOM   144  C  C   . GLU   A 1 19  ? -34.969 9.762   7.142   1.00 10.57 ? 34  GLU   A C   1 
ATOM   145  O  O   . GLU   A 1 19  ? -34.833 8.601   7.528   1.00 9.65  ? 34  GLU   A O   1 
ATOM   146  C  CB  . GLU   A 1 19  ? -36.873 9.464   5.497   1.00 12.89 ? 34  GLU   A CB  1 
ATOM   147  C  CG  . GLU   A 1 19  ? -37.997 10.104  6.305   1.00 16.76 ? 34  GLU   A CG  1 
ATOM   148  C  CD  . GLU   A 1 19  ? -39.309 9.679   5.610   1.00 20.14 ? 34  GLU   A CD  1 
ATOM   149  O  OE1 . GLU   A 1 19  ? -39.678 8.530   5.820   1.00 24.83 ? 34  GLU   A OE1 1 
ATOM   150  O  OE2 . GLU   A 1 19  ? -39.843 10.385  4.748   0.50 22.53 ? 34  GLU   A OE2 1 
ATOM   151  N  N   . ILE   A 1 20  ? -34.691 10.838  7.886   1.00 10.75 ? 35  ILE   A N   1 
ATOM   152  C  CA  . ILE   A 1 20  ? -34.005 10.755  9.163   1.00 11.37 ? 35  ILE   A CA  1 
ATOM   153  C  C   . ILE   A 1 20  ? -34.955 11.173  10.280  1.00 11.83 ? 35  ILE   A C   1 
ATOM   154  O  O   . ILE   A 1 20  ? -35.452 12.300  10.292  1.00 10.39 ? 35  ILE   A O   1 
ATOM   155  C  CB  . ILE   A 1 20  ? -32.758 11.639  9.176   1.00 12.91 ? 35  ILE   A CB  1 
ATOM   156  C  CG1 . ILE   A 1 20  ? -31.860 11.281  7.981   1.00 14.73 ? 35  ILE   A CG1 1 
ATOM   157  C  CG2 . ILE   A 1 20  ? -32.008 11.531  10.511  1.00 14.36 ? 35  ILE   A CG2 1 
ATOM   158  C  CD1 . ILE   A 1 20  ? -31.188 12.481  7.430   1.00 14.98 ? 35  ILE   A CD1 1 
ATOM   159  N  N   . VAL   A 1 21  ? -35.153 10.250  11.214  1.00 12.44 ? 36  VAL   A N   1 
ATOM   160  C  CA  . VAL   A 1 21  ? -36.088 10.452  12.299  1.00 16.60 ? 36  VAL   A CA  1 
ATOM   161  C  C   . VAL   A 1 21  ? -35.335 10.781  13.581  1.00 16.67 ? 36  VAL   A C   1 
ATOM   162  O  O   . VAL   A 1 21  ? -34.324 10.156  13.909  1.00 13.52 ? 36  VAL   A O   1 
ATOM   163  C  CB  . VAL   A 1 21  ? -36.918 9.160   12.424  1.00 19.89 ? 36  VAL   A CB  1 
ATOM   164  C  CG1 . VAL   A 1 21  ? -37.862 9.208   13.608  1.00 22.57 ? 36  VAL   A CG1 1 
ATOM   165  C  CG2 . VAL   A 1 21  ? -37.687 8.880   11.135  1.00 22.63 ? 36  VAL   A CG2 1 
ATOM   166  N  N   . THR   A 1 22  A -35.883 11.759  14.308  1.00 18.28 ? 36  THR   A N   1 
ATOM   167  C  CA  . THR   A 1 22  A -35.444 12.123  15.648  1.00 23.32 ? 36  THR   A CA  1 
ATOM   168  C  C   . THR   A 1 22  A -36.672 12.174  16.558  1.00 24.48 ? 36  THR   A C   1 
ATOM   169  O  O   . THR   A 1 22  A -37.804 12.247  16.076  1.00 25.64 ? 36  THR   A O   1 
ATOM   170  C  CB  . THR   A 1 22  A -34.714 13.463  15.583  1.00 26.26 ? 36  THR   A CB  1 
ATOM   171  O  OG1 . THR   A 1 22  A -35.593 14.372  14.916  1.00 25.77 ? 36  THR   A OG1 1 
ATOM   172  C  CG2 . THR   A 1 22  A -33.401 13.334  14.836  1.00 25.46 ? 36  THR   A CG2 1 
ATOM   173  N  N   . SER   A 1 23  B -36.447 12.137  17.879  1.00 26.46 ? 36  SER   A N   1 
ATOM   174  C  CA  . SER   A 1 23  B -37.532 11.932  18.828  1.00 26.30 ? 36  SER   A CA  1 
ATOM   175  C  C   . SER   A 1 23  B -38.401 13.179  18.998  1.00 26.18 ? 36  SER   A C   1 
ATOM   176  O  O   . SER   A 1 23  B -39.574 13.006  19.359  1.00 23.12 ? 36  SER   A O   1 
ATOM   177  C  CB  . SER   A 1 23  B -37.018 11.499  20.180  1.00 29.81 ? 36  SER   A CB  1 
ATOM   178  O  OG  . SER   A 1 23  B -36.465 12.600  20.892  0.50 29.29 ? 36  SER   A OG  1 
ATOM   179  N  N   . ASN   A 1 24  ? -37.821 14.371  18.720  1.00 24.12 ? 37  ASN   A N   1 
ATOM   180  C  CA  . ASN   A 1 24  ? -38.345 15.685  19.101  1.00 25.57 ? 37  ASN   A CA  1 
ATOM   181  C  C   . ASN   A 1 24  ? -38.432 16.695  17.936  1.00 22.28 ? 37  ASN   A C   1 
ATOM   182  O  O   . ASN   A 1 24  ? -38.391 17.921  18.117  1.00 22.88 ? 37  ASN   A O   1 
ATOM   183  C  CB  . ASN   A 1 24  ? -37.438 16.321  20.146  1.00 28.72 ? 37  ASN   A CB  1 
ATOM   184  C  CG  . ASN   A 1 24  ? -36.110 16.716  19.541  1.00 34.03 ? 37  ASN   A CG  1 
ATOM   185  O  OD1 . ASN   A 1 24  ? -35.740 16.191  18.482  1.00 37.72 ? 37  ASN   A OD1 1 
ATOM   186  N  ND2 . ASN   A 1 24  ? -35.370 17.594  20.204  0.10 32.72 ? 37  ASN   A ND2 1 
ATOM   187  N  N   . GLY   A 1 25  A -38.509 16.207  16.701  1.00 17.14 ? 37  GLY   A N   1 
ATOM   188  C  CA  . GLY   A 1 25  A -38.855 17.056  15.586  1.00 13.56 ? 37  GLY   A CA  1 
ATOM   189  C  C   . GLY   A 1 25  A -39.338 16.180  14.444  1.00 11.80 ? 37  GLY   A C   1 
ATOM   190  O  O   . GLY   A 1 25  A -39.227 14.965  14.528  1.00 11.48 ? 37  GLY   A O   1 
ATOM   191  N  N   . PRO   A 1 26  ? -39.904 16.763  13.370  1.00 10.74 ? 38  PRO   A N   1 
ATOM   192  C  CA  . PRO   A 1 26  ? -40.300 15.979  12.194  1.00 10.63 ? 38  PRO   A CA  1 
ATOM   193  C  C   . PRO   A 1 26  ? -39.098 15.463  11.409  1.00 10.32 ? 38  PRO   A C   1 
ATOM   194  O  O   . PRO   A 1 26  ? -37.957 15.833  11.697  1.00 10.78 ? 38  PRO   A O   1 
ATOM   195  C  CB  . PRO   A 1 26  ? -41.156 16.973  11.392  1.00 10.66 ? 38  PRO   A CB  1 
ATOM   196  C  CG  . PRO   A 1 26  ? -40.568 18.322  11.765  1.00 11.52 ? 38  PRO   A CG  1 
ATOM   197  C  CD  . PRO   A 1 26  ? -40.175 18.200  13.221  1.00 10.85 ? 38  PRO   A CD  1 
ATOM   198  N  N   . SER   A 1 27  ? -39.380 14.608  10.421  1.00 10.13 ? 39  SER   A N   1 
ATOM   199  C  CA  . SER   A 1 27  ? -38.372 14.034  9.530   1.00 10.95 ? 39  SER   A CA  1 
ATOM   200  C  C   . SER   A 1 27  ? -37.477 15.103  8.907   1.00 10.56 ? 39  SER   A C   1 
ATOM   201  O  O   . SER   A 1 27  ? -37.943 16.151  8.449   1.00 10.10 ? 39  SER   A O   1 
ATOM   202  C  CB  . SER   A 1 27  ? -39.056 13.212  8.432   1.00 12.54 ? 39  SER   A CB  1 
ATOM   203  O  OG  . SER   A 1 27  ? -39.643 12.046  8.994   1.00 14.83 ? 39  SER   A OG  1 
ATOM   204  N  N   . LYS   A 1 28  ? -36.187 14.765  8.776   1.00 10.96 ? 40  LYS   A N   1 
ATOM   205  C  CA  . LYS   A 1 28  ? -35.245 15.519  7.955   1.00 11.66 ? 40  LYS   A CA  1 
ATOM   206  C  C   . LYS   A 1 28  ? -34.762 14.589  6.837   1.00 10.39 ? 40  LYS   A C   1 
ATOM   207  O  O   . LYS   A 1 28  ? -35.039 13.386  6.879   1.00 9.55  ? 40  LYS   A O   1 
ATOM   208  C  CB  . LYS   A 1 28  ? -34.041 15.975  8.783   1.00 13.92 ? 40  LYS   A CB  1 
ATOM   209  C  CG  . LYS   A 1 28  ? -34.336 16.992  9.872   1.00 17.11 ? 40  LYS   A CG  1 
ATOM   210  C  CD  . LYS   A 1 28  ? -33.056 17.568  10.477  1.00 21.68 ? 40  LYS   A CD  1 
ATOM   211  C  CE  . LYS   A 1 28  ? -33.341 18.761  11.342  1.00 27.52 ? 40  LYS   A CE  1 
ATOM   212  N  NZ  . LYS   A 1 28  ? -33.948 18.320  12.596  1.00 30.90 ? 40  LYS   A NZ  1 
ATOM   213  N  N   . PHE   A 1 29  ? -34.085 15.151  5.822   1.00 10.00 ? 41  PHE   A N   1 
ATOM   214  C  CA  . PHE   A 1 29  ? -33.733 14.341  4.659   1.00 10.86 ? 41  PHE   A CA  1 
ATOM   215  C  C   . PHE   A 1 29  ? -32.285 14.596  4.257   1.00 9.36  ? 41  PHE   A C   1 
ATOM   216  O  O   . PHE   A 1 29  ? -31.791 15.705  4.404   1.00 9.64  ? 41  PHE   A O   1 
ATOM   217  C  CB  . PHE   A 1 29  ? -34.684 14.597  3.480   1.00 13.28 ? 41  PHE   A CB  1 
ATOM   218  C  CG  . PHE   A 1 29  ? -36.142 14.363  3.859   1.00 15.50 ? 41  PHE   A CG  1 
ATOM   219  C  CD1 . PHE   A 1 29  ? -36.778 13.146  3.605   1.00 17.88 ? 41  PHE   A CD1 1 
ATOM   220  C  CD2 . PHE   A 1 29  ? -36.843 15.337  4.560   1.00 17.69 ? 41  PHE   A CD2 1 
ATOM   221  C  CE1 . PHE   A 1 29  ? -38.100 12.941  3.995   1.00 18.51 ? 41  PHE   A CE1 1 
ATOM   222  C  CE2 . PHE   A 1 29  ? -38.153 15.118  4.979   1.00 17.26 ? 41  PHE   A CE2 1 
ATOM   223  C  CZ  . PHE   A 1 29  ? -38.786 13.930  4.667   1.00 18.81 ? 41  PHE   A CZ  1 
ATOM   224  N  N   . CYS   A 1 30  ? -31.658 13.537  3.721   1.00 8.21  ? 42  CYS   A N   1 
ATOM   225  C  CA  . CYS   A 1 30  ? -30.304 13.574  3.190   1.00 7.52  ? 42  CYS   A CA  1 
ATOM   226  C  C   . CYS   A 1 30  ? -30.226 12.713  1.930   1.00 6.93  ? 42  CYS   A C   1 
ATOM   227  O  O   . CYS   A 1 30  ? -31.112 11.916  1.627   1.00 7.42  ? 42  CYS   A O   1 
ATOM   228  C  CB  . CYS   A 1 30  ? -29.290 13.043  4.203   1.00 7.51  ? 42  CYS   A CB  1 
ATOM   229  S  SG  . CYS   A 1 30  ? -28.970 14.163  5.596   1.00 8.18  ? 42  CYS   A SG  1 
ATOM   230  N  N   . GLY   A 1 31  ? -29.129 12.875  1.196   1.00 7.01  ? 43  GLY   A N   1 
ATOM   231  C  CA  . GLY   A 1 31  ? -28.738 11.904  0.200   1.00 6.64  ? 43  GLY   A CA  1 
ATOM   232  C  C   . GLY   A 1 31  ? -27.731 10.912  0.779   1.00 6.73  ? 43  GLY   A C   1 
ATOM   233  O  O   . GLY   A 1 31  ? -27.274 11.031  1.920   1.00 6.82  ? 43  GLY   A O   1 
ATOM   234  N  N   . GLY   A 1 32  ? -27.307 9.996   -0.093  1.00 6.49  ? 44  GLY   A N   1 
ATOM   235  C  CA  . GLY   A 1 32  ? -26.326 8.970   0.210   1.00 6.50  ? 44  GLY   A CA  1 
ATOM   236  C  C   . GLY   A 1 32  ? -26.078 8.156   -1.060  1.00 6.54  ? 44  GLY   A C   1 
ATOM   237  O  O   . GLY   A 1 32  ? -26.667 8.431   -2.106  1.00 6.45  ? 44  GLY   A O   1 
ATOM   238  N  N   . PHE   A 1 33  ? -25.204 7.163   -0.987  1.00 6.87  ? 45  PHE   A N   1 
ATOM   239  C  CA  . PHE   A 1 33  ? -24.979 6.305   -2.139  1.00 7.40  ? 45  PHE   A CA  1 
ATOM   240  C  C   . PHE   A 1 33  ? -24.669 4.877   -1.696  1.00 7.17  ? 45  PHE   A C   1 
ATOM   241  O  O   . PHE   A 1 33  ? -23.923 4.634   -0.752  1.00 7.15  ? 45  PHE   A O   1 
ATOM   242  C  CB  . PHE   A 1 33  ? -23.918 6.866   -3.108  1.00 7.93  ? 45  PHE   A CB  1 
ATOM   243  C  CG  . PHE   A 1 33  ? -22.599 7.366   -2.513  1.00 9.64  ? 45  PHE   A CG  1 
ATOM   244  C  CD1 . PHE   A 1 33  ? -22.560 8.460   -1.664  1.00 11.28 ? 45  PHE   A CD1 1 
ATOM   245  C  CD2 . PHE   A 1 33  ? -21.400 6.773   -2.853  1.00 10.69 ? 45  PHE   A CD2 1 
ATOM   246  C  CE1 . PHE   A 1 33  ? -21.359 8.901   -1.116  1.00 12.61 ? 45  PHE   A CE1 1 
ATOM   247  C  CE2 . PHE   A 1 33  ? -20.191 7.233   -2.326  1.00 10.77 ? 45  PHE   A CE2 1 
ATOM   248  C  CZ  . PHE   A 1 33  ? -20.175 8.292   -1.467  1.00 11.00 ? 45  PHE   A CZ  1 
ATOM   249  N  N   . LEU   A 1 34  ? -25.140 3.931   -2.507  1.00 6.52  ? 46  LEU   A N   1 
ATOM   250  C  CA  . LEU   A 1 34  ? -24.993 2.507   -2.247  1.00 6.98  ? 46  LEU   A CA  1 
ATOM   251  C  C   . LEU   A 1 34  ? -23.608 2.044   -2.685  1.00 7.27  ? 46  LEU   A C   1 
ATOM   252  O  O   . LEU   A 1 34  ? -23.338 2.029   -3.885  1.00 7.97  ? 46  LEU   A O   1 
ATOM   253  C  CB  . LEU   A 1 34  ? -26.069 1.756   -3.043  1.00 7.09  ? 46  LEU   A CB  1 
ATOM   254  C  CG  . LEU   A 1 34  ? -26.254 0.278   -2.669  1.00 7.43  ? 46  LEU   A CG  1 
ATOM   255  C  CD1 . LEU   A 1 34  ? -26.950 0.141   -1.321  1.00 7.68  ? 46  LEU   A CD1 1 
ATOM   256  C  CD2 . LEU   A 1 34  ? -27.064 -0.374  -3.765  1.00 7.51  ? 46  LEU   A CD2 1 
ATOM   257  N  N   . ILE   A 1 35  ? -22.760 1.614   -1.741  1.00 7.97  ? 47  ILE   A N   1 
ATOM   258  C  CA  . ILE   A 1 35  ? -21.411 1.163   -2.087  1.00 8.86  ? 47  ILE   A CA  1 
ATOM   259  C  C   . ILE   A 1 35  ? -21.265 -0.355  -1.998  1.00 9.23  ? 47  ILE   A C   1 
ATOM   260  O  O   . ILE   A 1 35  ? -20.316 -0.899  -2.560  1.00 9.50  ? 47  ILE   A O   1 
ATOM   261  C  CB  . ILE   A 1 35  ? -20.319 1.903   -1.281  1.00 9.71  ? 47  ILE   A CB  1 
ATOM   262  C  CG1 . ILE   A 1 35  ? -20.392 1.624   0.219   1.00 10.17 ? 47  ILE   A CG1 1 
ATOM   263  C  CG2 . ILE   A 1 35  ? -20.380 3.400   -1.600  1.00 10.44 ? 47  ILE   A CG2 1 
ATOM   264  C  CD1 . ILE   A 1 35  ? -19.085 1.901   0.954   1.00 10.94 ? 47  ILE   A CD1 1 
ATOM   265  N  N   . ARG   A 1 36  ? -22.163 -1.027  -1.255  1.00 9.17  ? 48  ARG   A N   1 
ATOM   266  C  CA  . ARG   A 1 36  ? -22.331 -2.468  -1.286  1.00 9.59  ? 48  ARG   A CA  1 
ATOM   267  C  C   . ARG   A 1 36  ? -23.824 -2.752  -1.277  1.00 9.33  ? 48  ARG   A C   1 
ATOM   268  O  O   . ARG   A 1 36  ? -24.597 -1.868  -0.916  1.00 8.32  ? 48  ARG   A O   1 
ATOM   269  C  CB  . ARG   A 1 36  ? -21.791 -3.150  -0.029  1.00 11.00 ? 48  ARG   A CB  1 
ATOM   270  C  CG  . ARG   A 1 36  ? -20.291 -3.016  0.110   1.00 12.98 ? 48  ARG   A CG  1 
ATOM   271  C  CD  . ARG   A 1 36  ? -19.543 -3.887  -0.876  1.00 14.09 ? 48  ARG   A CD  1 
ATOM   272  N  NE  . ARG   A 1 36  ? -18.105 -3.881  -0.595  0.50 13.24 ? 48  ARG   A NE  1 
ATOM   273  C  CZ  . ARG   A 1 36  ? -17.239 -2.956  -0.962  0.50 13.42 ? 48  ARG   A CZ  1 
ATOM   274  N  NH1 . ARG   A 1 36  ? -17.632 -1.878  -1.620  0.50 13.35 ? 48  ARG   A NH1 1 
ATOM   275  N  NH2 . ARG   A 1 36  ? -15.971 -3.114  -0.631  0.50 13.76 ? 48  ARG   A NH2 1 
ATOM   276  N  N   . ARG   A 1 37  ? -24.256 -3.980  -1.607  1.00 9.06  ? 49  ARG   A N   1 
ATOM   277  C  CA  . ARG   A 1 37  ? -25.698 -4.218  -1.638  1.00 8.69  ? 49  ARG   A CA  1 
ATOM   278  C  C   . ARG   A 1 37  ? -26.364 -3.943  -0.278  1.00 8.89  ? 49  ARG   A C   1 
ATOM   279  O  O   . ARG   A 1 37  ? -27.570 -3.692  -0.245  1.00 8.45  ? 49  ARG   A O   1 
ATOM   280  C  CB  . ARG   A 1 37  ? -26.088 -5.593  -2.186  1.00 9.21  ? 49  ARG   A CB  1 
ATOM   281  C  CG  . ARG   A 1 37  ? -25.777 -5.769  -3.669  1.00 9.01  ? 49  ARG   A CG  1 
ATOM   282  C  CD  . ARG   A 1 37  ? -25.981 -7.188  -4.189  1.00 9.23  ? 49  ARG   A CD  1 
ATOM   283  N  NE  . ARG   A 1 37  ? -27.395 -7.583  -4.138  1.00 8.85  ? 49  ARG   A NE  1 
ATOM   284  C  CZ  . ARG   A 1 37  ? -27.873 -8.753  -4.554  1.00 9.42  ? 49  ARG   A CZ  1 
ATOM   285  N  NH1 . ARG   A 1 37  ? -27.038 -9.665  -5.022  1.00 9.09  ? 49  ARG   A NH1 1 
ATOM   286  N  NH2 . ARG   A 1 37  ? -29.172 -9.009  -4.525  1.00 9.55  ? 49  ARG   A NH2 1 
ATOM   287  N  N   . ASN   A 1 38  ? -25.614 -3.983  0.838   1.00 8.67  ? 50  ASN   A N   1 
ATOM   288  C  CA  . ASN   A 1 38  ? -26.211 -3.679  2.142   1.00 8.96  ? 50  ASN   A CA  1 
ATOM   289  C  C   . ASN   A 1 38  ? -25.492 -2.531  2.856   1.00 8.19  ? 50  ASN   A C   1 
ATOM   290  O  O   . ASN   A 1 38  ? -25.577 -2.440  4.080   1.00 8.08  ? 50  ASN   A O   1 
ATOM   291  C  CB  . ASN   A 1 38  ? -26.321 -4.914  3.040   1.00 9.43  ? 50  ASN   A CB  1 
ATOM   292  C  CG  . ASN   A 1 38  ? -24.984 -5.509  3.387   1.00 11.15 ? 50  ASN   A CG  1 
ATOM   293  O  OD1 . ASN   A 1 38  ? -23.957 -5.202  2.769   1.00 11.80 ? 50  ASN   A OD1 1 
ATOM   294  N  ND2 . ASN   A 1 38  ? -24.973 -6.380  4.388   1.00 12.29 ? 50  ASN   A ND2 1 
ATOM   295  N  N   . PHE   A 1 39  ? -24.796 -1.637  2.130   1.00 8.09  ? 51  PHE   A N   1 
ATOM   296  C  CA  . PHE   A 1 39  ? -24.190 -0.483  2.793   1.00 7.97  ? 51  PHE   A CA  1 
ATOM   297  C  C   . PHE   A 1 39  ? -24.351 0.787   1.953   1.00 7.65  ? 51  PHE   A C   1 
ATOM   298  O  O   . PHE   A 1 39  ? -24.050 0.814   0.766   1.00 7.30  ? 51  PHE   A O   1 
ATOM   299  C  CB  . PHE   A 1 39  ? -22.701 -0.624  3.120   1.00 8.67  ? 51  PHE   A CB  1 
ATOM   300  C  CG  . PHE   A 1 39  ? -22.382 -1.326  4.423   1.00 9.97  ? 51  PHE   A CG  1 
ATOM   301  C  CD1 . PHE   A 1 39  ? -22.317 -0.599  5.608   1.00 11.30 ? 51  PHE   A CD1 1 
ATOM   302  C  CD2 . PHE   A 1 39  ? -22.167 -2.696  4.461   1.00 11.97 ? 51  PHE   A CD2 1 
ATOM   303  C  CE1 . PHE   A 1 39  ? -21.976 -1.237  6.784   1.00 12.40 ? 51  PHE   A CE1 1 
ATOM   304  C  CE2 . PHE   A 1 39  ? -21.846 -3.318  5.657   1.00 12.71 ? 51  PHE   A CE2 1 
ATOM   305  C  CZ  . PHE   A 1 39  ? -21.770 -2.577  6.802   1.00 11.33 ? 51  PHE   A CZ  1 
ATOM   306  N  N   . VAL   A 1 40  ? -24.784 1.859   2.635   1.00 7.14  ? 52  VAL   A N   1 
ATOM   307  C  CA  . VAL   A 1 40  ? -24.910 3.197   2.094   1.00 7.02  ? 52  VAL   A CA  1 
ATOM   308  C  C   . VAL   A 1 40  ? -23.935 4.122   2.819   1.00 6.76  ? 52  VAL   A C   1 
ATOM   309  O  O   . VAL   A 1 40  ? -23.851 4.100   4.039   1.00 6.90  ? 52  VAL   A O   1 
ATOM   310  C  CB  . VAL   A 1 40  ? -26.360 3.692   2.256   1.00 6.99  ? 52  VAL   A CB  1 
ATOM   311  C  CG1 . VAL   A 1 40  ? -26.500 5.187   2.005   1.00 7.16  ? 52  VAL   A CG1 1 
ATOM   312  C  CG2 . VAL   A 1 40  ? -27.329 2.904   1.376   1.00 7.19  ? 52  VAL   A CG2 1 
ATOM   313  N  N   . LEU   A 1 41  ? -23.199 4.925   2.047   1.00 6.72  ? 53  LEU   A N   1 
ATOM   314  C  CA  . LEU   A 1 41  ? -22.308 5.932   2.590   1.00 6.85  ? 53  LEU   A CA  1 
ATOM   315  C  C   . LEU   A 1 41  ? -23.011 7.293   2.544   1.00 6.58  ? 53  LEU   A C   1 
ATOM   316  O  O   . LEU   A 1 41  ? -23.709 7.616   1.573   1.00 6.97  ? 53  LEU   A O   1 
ATOM   317  C  CB  . LEU   A 1 41  ? -21.036 5.871   1.738   1.00 7.63  ? 53  LEU   A CB  1 
ATOM   318  C  CG  . LEU   A 1 41  ? -19.857 6.734   2.182   1.00 8.26  ? 53  LEU   A CG  1 
ATOM   319  C  CD1 . LEU   A 1 41  ? -19.431 6.376   3.577   1.00 8.67  ? 53  LEU   A CD1 1 
ATOM   320  C  CD2 . LEU   A 1 41  ? -18.702 6.599   1.211   1.00 8.95  ? 53  LEU   A CD2 1 
ATOM   321  N  N   . THR   A 1 42  ? -22.836 8.094   3.596   1.00 6.38  ? 54  THR   A N   1 
ATOM   322  C  CA  . THR   A 1 42  ? -23.484 9.392   3.735   1.00 6.20  ? 54  THR   A CA  1 
ATOM   323  C  C   . THR   A 1 42  ? -22.685 10.227  4.744   1.00 6.23  ? 54  THR   A C   1 
ATOM   324  O  O   . THR   A 1 42  ? -21.546 9.873   5.059   1.00 6.48  ? 54  THR   A O   1 
ATOM   325  C  CB  . THR   A 1 42  ? -24.956 9.223   4.142   1.00 6.14  ? 54  THR   A CB  1 
ATOM   326  O  OG1 . THR   A 1 42  ? -25.653 10.465  4.061   1.00 6.20  ? 54  THR   A OG1 1 
ATOM   327  C  CG2 . THR   A 1 42  ? -25.111 8.602   5.509   1.00 6.35  ? 54  THR   A CG2 1 
ATOM   328  N  N   . ALA   A 1 43  ? -23.259 11.362  5.181   1.00 6.22  ? 55  ALA   A N   1 
ATOM   329  C  CA  . ALA   A 1 43  ? -22.633 12.272  6.137   1.00 6.26  ? 55  ALA   A CA  1 
ATOM   330  C  C   . ALA   A 1 43  ? -23.032 11.903  7.565   1.00 6.94  ? 55  ALA   A C   1 
ATOM   331  O  O   . ALA   A 1 43  ? -24.193 11.576  7.818   1.00 6.41  ? 55  ALA   A O   1 
ATOM   332  C  CB  . ALA   A 1 43  ? -23.051 13.716  5.829   1.00 6.38  ? 55  ALA   A CB  1 
ATOM   333  N  N   . ALA   A 1 44  ? -22.082 12.014  8.514   1.00 6.37  ? 56  ALA   A N   1 
ATOM   334  C  CA  . ALA   A 1 44  ? -22.360 11.770  9.928   1.00 7.00  ? 56  ALA   A CA  1 
ATOM   335  C  C   . ALA   A 1 44  ? -23.436 12.687  10.518  1.00 7.16  ? 56  ALA   A C   1 
ATOM   336  O  O   . ALA   A 1 44  ? -24.133 12.288  11.454  1.00 7.58  ? 56  ALA   A O   1 
ATOM   337  C  CB  . ALA   A 1 44  ? -21.078 11.898  10.732  1.00 6.96  ? 56  ALA   A CB  1 
ATOM   338  N  N   . HIS   A 1 45  ? -23.545 13.924  10.030  1.00 6.85  ? 57  HIS   A N   1 
ATOM   339  C  CA  . HIS   A 1 45  ? -24.567 14.852  10.503  1.00 7.51  ? 57  HIS   A CA  1 
ATOM   340  C  C   . HIS   A 1 45  ? -25.978 14.410  10.092  1.00 7.67  ? 57  HIS   A C   1 
ATOM   341  O  O   . HIS   A 1 45  ? -26.952 14.997  10.584  1.00 7.61  ? 57  HIS   A O   1 
ATOM   342  C  CB  . HIS   A 1 45  ? -24.262 16.299  10.103  1.00 7.98  ? 57  HIS   A CB  1 
ATOM   343  C  CG  . HIS   A 1 45  ? -24.600 16.659  8.691   1.00 7.77  ? 57  HIS   A CG  1 
ATOM   344  N  ND1 . HIS   A 1 45  ? -23.616 16.805  7.724   1.00 7.95  ? 57  HIS   A ND1 1 
ATOM   345  C  CD2 . HIS   A 1 45  ? -25.768 16.954  8.086   1.00 8.23  ? 57  HIS   A CD2 1 
ATOM   346  C  CE1 . HIS   A 1 45  ? -24.190 17.133  6.568   1.00 8.51  ? 57  HIS   A CE1 1 
ATOM   347  N  NE2 . HIS   A 1 45  ? -25.500 17.250  6.755   1.00 8.19  ? 57  HIS   A NE2 1 
ATOM   348  N  N   . CYS   A 1 46  ? -26.091 13.357  9.256   1.00 7.29  ? 58  CYS   A N   1 
ATOM   349  C  CA  . CYS   A 1 46  ? -27.384 12.773  8.891   1.00 7.60  ? 58  CYS   A CA  1 
ATOM   350  C  C   . CYS   A 1 46  ? -27.806 11.634  9.845   1.00 7.84  ? 58  CYS   A C   1 
ATOM   351  O  O   . CYS   A 1 46  ? -28.811 10.956  9.591   1.00 8.41  ? 58  CYS   A O   1 
ATOM   352  C  CB  . CYS   A 1 46  ? -27.405 12.293  7.435   1.00 7.53  ? 58  CYS   A CB  1 
ATOM   353  S  SG  . CYS   A 1 46  ? -27.112 13.617  6.213   1.00 8.27  ? 58  CYS   A SG  1 
ATOM   354  N  N   . ALA   A 1 47  ? -27.076 11.413  10.944  1.00 7.93  ? 59  ALA   A N   1 
ATOM   355  C  CA  . ALA   A 1 47  ? -27.437 10.374  11.906  1.00 8.28  ? 59  ALA   A CA  1 
ATOM   356  C  C   . ALA   A 1 47  ? -28.732 10.743  12.618  1.00 8.65  ? 59  ALA   A C   1 
ATOM   357  O  O   . ALA   A 1 47  ? -29.053 11.923  12.774  1.00 9.08  ? 59  ALA   A O   1 
ATOM   358  C  CB  . ALA   A 1 47  ? -26.322 10.193  12.916  1.00 8.51  ? 59  ALA   A CB  1 
ATOM   359  N  N   . GLY   A 1 48  ? -29.488 9.724   13.050  1.00 8.95  ? 60  GLY   A N   1 
ATOM   360  C  CA  . GLY   A 1 48  ? -30.698 9.986   13.798  1.00 9.56  ? 60  GLY   A CA  1 
ATOM   361  C  C   . GLY   A 1 48  ? -31.076 8.772   14.640  1.00 9.14  ? 60  GLY   A C   1 
ATOM   362  O  O   . GLY   A 1 48  ? -30.297 7.832   14.778  1.00 9.46  ? 60  GLY   A O   1 
ATOM   363  N  N   . ARG   A 1 49  ? -32.263 8.828   15.233  1.00 9.11  ? 61  ARG   A N   1 
ATOM   364  C  CA  . ARG   A 1 49  ? -32.731 7.690   16.012  1.00 9.37  ? 61  ARG   A CA  1 
ATOM   365  C  C   . ARG   A 1 49  ? -32.991 6.508   15.086  1.00 9.61  ? 61  ARG   A C   1 
ATOM   366  O  O   . ARG   A 1 49  ? -32.766 5.371   15.474  1.00 10.18 ? 61  ARG   A O   1 
ATOM   367  C  CB  . ARG   A 1 49  ? -33.985 8.076   16.783  1.00 9.37  ? 61  ARG   A CB  1 
ATOM   368  C  CG  . ARG   A 1 49  ? -34.561 6.959   17.632  1.00 9.96  ? 61  ARG   A CG  1 
ATOM   369  C  CD  . ARG   A 1 49  ? -33.595 6.403   18.643  1.00 10.57 ? 61  ARG   A CD  1 
ATOM   370  N  NE  . ARG   A 1 49  ? -34.231 5.304   19.393  1.00 10.69 ? 61  ARG   A NE  1 
ATOM   371  C  CZ  . ARG   A 1 49  ? -34.387 4.063   18.918  1.00 12.00 ? 61  ARG   A CZ  1 
ATOM   372  N  NH1 . ARG   A 1 49  ? -33.874 3.706   17.737  1.00 11.75 ? 61  ARG   A NH1 1 
ATOM   373  N  NH2 . ARG   A 1 49  ? -34.988 3.152   19.682  1.00 12.00 ? 61  ARG   A NH2 1 
ATOM   374  N  N   . SER   A 1 50  ? -33.569 6.782   13.919  1.00 9.66  ? 63  SER   A N   1 
ATOM   375  C  CA  . SER   A 1 50  ? -33.788 5.752   12.922  1.00 10.67 ? 63  SER   A CA  1 
ATOM   376  C  C   . SER   A 1 50  ? -33.746 6.398   11.535  1.00 10.12 ? 63  SER   A C   1 
ATOM   377  O  O   . SER   A 1 50  ? -33.948 7.607   11.408  1.00 10.44 ? 63  SER   A O   1 
ATOM   378  C  CB  . SER   A 1 50  ? -35.063 4.982   13.157  1.00 12.23 ? 63  SER   A CB  1 
ATOM   379  O  OG  . SER   A 1 50  ? -36.190 5.832   13.162  1.00 13.68 ? 63  SER   A OG  1 
ATOM   380  N  N   . ILE   A 1 51  ? -33.390 5.594   10.524  1.00 9.32  ? 64  ILE   A N   1 
ATOM   381  C  CA  . ILE   A 1 51  ? -33.280 6.090   9.157   1.00 8.54  ? 64  ILE   A CA  1 
ATOM   382  C  C   . ILE   A 1 51  ? -33.940 5.086   8.212   1.00 8.14  ? 64  ILE   A C   1 
ATOM   383  O  O   . ILE   A 1 51  ? -33.778 3.884   8.395   1.00 8.52  ? 64  ILE   A O   1 
ATOM   384  C  CB  . ILE   A 1 51  ? -31.809 6.315   8.761   1.00 8.42  ? 64  ILE   A CB  1 
ATOM   385  C  CG1 . ILE   A 1 51  ? -31.132 7.386   9.666   1.00 8.59  ? 64  ILE   A CG1 1 
ATOM   386  C  CG2 . ILE   A 1 51  ? -31.682 6.682   7.279   1.00 8.25  ? 64  ILE   A CG2 1 
ATOM   387  C  CD1 . ILE   A 1 51  ? -29.632 7.529   9.436   1.00 8.94  ? 64  ILE   A CD1 1 
ATOM   388  N  N   A THR   A 1 52  ? -34.660 5.606   7.215   0.50 8.77  ? 65  THR   A N   1 
ATOM   389  N  N   B THR   A 1 52  ? -34.642 5.589   7.190   0.50 8.63  ? 65  THR   A N   1 
ATOM   390  C  CA  A THR   A 1 52  ? -35.131 4.811   6.091   0.50 9.27  ? 65  THR   A CA  1 
ATOM   391  C  CA  B THR   A 1 52  ? -35.103 4.759   6.084   0.50 9.02  ? 65  THR   A CA  1 
ATOM   392  C  C   A THR   A 1 52  ? -34.369 5.215   4.819   0.50 8.76  ? 65  THR   A C   1 
ATOM   393  C  C   B THR   A 1 52  ? -34.475 5.214   4.764   0.50 8.62  ? 65  THR   A C   1 
ATOM   394  O  O   A THR   A 1 52  ? -34.010 6.384   4.640   0.50 8.44  ? 65  THR   A O   1 
ATOM   395  O  O   B THR   A 1 52  ? -34.380 6.402   4.471   0.50 8.44  ? 65  THR   A O   1 
ATOM   396  C  CB  A THR   A 1 52  ? -36.636 4.986   5.903   0.50 10.39 ? 65  THR   A CB  1 
ATOM   397  C  CB  B THR   A 1 52  ? -36.622 4.773   5.971   0.50 9.79  ? 65  THR   A CB  1 
ATOM   398  O  OG1 A THR   A 1 52  ? -37.334 4.794   7.131   0.50 10.97 ? 65  THR   A OG1 1 
ATOM   399  O  OG1 B THR   A 1 52  ? -36.968 6.122   5.651   0.50 10.98 ? 65  THR   A OG1 1 
ATOM   400  C  CG2 A THR   A 1 52  ? -37.168 3.974   4.910   0.50 11.21 ? 65  THR   A CG2 1 
ATOM   401  C  CG2 B THR   A 1 52  ? -37.256 4.179   7.216   0.50 9.74  ? 65  THR   A CG2 1 
ATOM   402  N  N   . VAL   A 1 53  ? -34.103 4.226   3.958   1.00 8.42  ? 66  VAL   A N   1 
ATOM   403  C  CA  . VAL   A 1 53  ? -33.425 4.411   2.691   1.00 8.22  ? 66  VAL   A CA  1 
ATOM   404  C  C   . VAL   A 1 53  ? -34.379 4.048   1.560   1.00 8.25  ? 66  VAL   A C   1 
ATOM   405  O  O   . VAL   A 1 53  ? -34.985 2.970   1.582   1.00 8.95  ? 66  VAL   A O   1 
ATOM   406  C  CB  . VAL   A 1 53  ? -32.153 3.548   2.645   1.00 8.83  ? 66  VAL   A CB  1 
ATOM   407  C  CG1 . VAL   A 1 53  ? -31.589 3.456   1.236   1.00 9.29  ? 66  VAL   A CG1 1 
ATOM   408  C  CG2 . VAL   A 1 53  ? -31.113 4.072   3.624   1.00 8.96  ? 66  VAL   A CG2 1 
ATOM   409  N  N   . THR   A 1 54  ? -34.468 4.924   0.552   1.00 7.07  ? 67  THR   A N   1 
ATOM   410  C  CA  . THR   A 1 54  ? -35.197 4.600   -0.679  1.00 7.33  ? 67  THR   A CA  1 
ATOM   411  C  C   . THR   A 1 54  ? -34.193 4.611   -1.833  1.00 7.11  ? 67  THR   A C   1 
ATOM   412  O  O   . THR   A 1 54  ? -33.608 5.657   -2.133  1.00 6.90  ? 67  THR   A O   1 
ATOM   413  C  CB  . THR   A 1 54  ? -36.328 5.583   -0.984  1.00 7.61  ? 67  THR   A CB  1 
ATOM   414  O  OG1 . THR   A 1 54  ? -37.229 5.633   0.123   1.00 7.82  ? 67  THR   A OG1 1 
ATOM   415  C  CG2 . THR   A 1 54  ? -37.122 5.167   -2.217  1.00 7.83  ? 67  THR   A CG2 1 
ATOM   416  N  N   . LEU   A 1 55  ? -34.033 3.434   -2.464  1.00 7.36  ? 68  LEU   A N   1 
ATOM   417  C  CA  . LEU   A 1 55  ? -33.255 3.258   -3.681  1.00 7.56  ? 68  LEU   A CA  1 
ATOM   418  C  C   . LEU   A 1 55  ? -34.189 3.244   -4.889  1.00 7.44  ? 68  LEU   A C   1 
ATOM   419  O  O   . LEU   A 1 55  ? -35.383 2.962   -4.755  1.00 7.29  ? 68  LEU   A O   1 
ATOM   420  C  CB  . LEU   A 1 55  ? -32.527 1.922   -3.580  1.00 8.33  ? 68  LEU   A CB  1 
ATOM   421  C  CG  . LEU   A 1 55  ? -31.608 1.742   -2.374  1.00 8.61  ? 68  LEU   A CG  1 
ATOM   422  C  CD1 . LEU   A 1 55  ? -30.933 0.380   -2.390  1.00 9.25  ? 68  LEU   A CD1 1 
ATOM   423  C  CD2 . LEU   A 1 55  ? -30.560 2.818   -2.295  1.00 9.31  ? 68  LEU   A CD2 1 
ATOM   424  N  N   . GLY   A 1 56  ? -33.630 3.563   -6.059  1.00 7.15  ? 69  GLY   A N   1 
ATOM   425  C  CA  . GLY   A 1 56  ? -34.387 3.450   -7.301  1.00 7.30  ? 69  GLY   A CA  1 
ATOM   426  C  C   . GLY   A 1 56  ? -35.282 4.648   -7.611  1.00 7.56  ? 69  GLY   A C   1 
ATOM   427  O  O   . GLY   A 1 56  ? -36.111 4.546   -8.524  1.00 8.30  ? 69  GLY   A O   1 
ATOM   428  N  N   . ALA   A 1 57  ? -35.112 5.780   -6.908  1.00 7.68  ? 70  ALA   A N   1 
ATOM   429  C  CA  . ALA   A 1 57  ? -36.015 6.907   -7.093  1.00 7.89  ? 70  ALA   A CA  1 
ATOM   430  C  C   . ALA   A 1 57  ? -35.524 7.892   -8.143  1.00 8.33  ? 70  ALA   A C   1 
ATOM   431  O  O   . ALA   A 1 57  ? -34.321 8.069   -8.372  1.00 7.58  ? 70  ALA   A O   1 
ATOM   432  C  CB  . ALA   A 1 57  ? -36.321 7.619   -5.767  1.00 8.19  ? 70  ALA   A CB  1 
ATOM   433  N  N   . HIS   A 1 58  ? -36.505 8.552   -8.774  1.00 8.54  ? 71  HIS   A N   1 
ATOM   434  C  CA  . HIS   A 1 58  ? -36.272 9.767   -9.537  1.00 9.51  ? 71  HIS   A CA  1 
ATOM   435  C  C   . HIS   A 1 58  ? -37.137 10.901  -8.971  1.00 9.23  ? 71  HIS   A C   1 
ATOM   436  O  O   . HIS   A 1 58  ? -36.628 11.799  -8.311  1.00 8.86  ? 71  HIS   A O   1 
ATOM   437  C  CB  . HIS   A 1 58  ? -36.430 9.537   -11.043 1.00 9.63  ? 71  HIS   A CB  1 
ATOM   438  C  CG  . HIS   A 1 58  ? -36.126 10.791  -11.774 1.00 9.90  ? 71  HIS   A CG  1 
ATOM   439  N  ND1 . HIS   A 1 58  ? -34.864 11.349  -11.697 1.00 9.33  ? 71  HIS   A ND1 1 
ATOM   440  C  CD2 . HIS   A 1 58  ? -36.903 11.675  -12.447 1.00 10.25 ? 71  HIS   A CD2 1 
ATOM   441  C  CE1 . HIS   A 1 58  ? -34.861 12.496  -12.361 1.00 9.76  ? 71  HIS   A CE1 1 
ATOM   442  N  NE2 . HIS   A 1 58  ? -36.088 12.736  -12.808 1.00 10.44 ? 71  HIS   A NE2 1 
ATOM   443  N  N   . ASN   A 1 59  ? -38.448 10.855  -9.242  1.00 9.66  ? 72  ASN   A N   1 
ATOM   444  C  CA  . ASN   A 1 59  ? -39.407 11.714  -8.584  1.00 10.24 ? 72  ASN   A CA  1 
ATOM   445  C  C   . ASN   A 1 59  ? -39.821 11.053  -7.278  1.00 11.10 ? 72  ASN   A C   1 
ATOM   446  O  O   . ASN   A 1 59  ? -40.555 10.065  -7.271  1.00 10.83 ? 72  ASN   A O   1 
ATOM   447  C  CB  . ASN   A 1 59  ? -40.631 11.989  -9.460  1.00 11.44 ? 72  ASN   A CB  1 
ATOM   448  C  CG  . ASN   A 1 59  ? -41.481 13.091  -8.866  1.00 12.11 ? 72  ASN   A CG  1 
ATOM   449  O  OD1 . ASN   A 1 59  ? -41.722 13.128  -7.658  1.00 12.08 ? 72  ASN   A OD1 1 
ATOM   450  N  ND2 . ASN   A 1 59  ? -41.935 14.028  -9.682  1.00 14.88 ? 72  ASN   A ND2 1 
ATOM   451  N  N   . ILE   A 1 60  ? -39.355 11.603  -6.151  1.00 11.01 ? 73  ILE   A N   1 
ATOM   452  C  CA  . ILE   A 1 60  ? -39.564 11.005  -4.848  1.00 11.50 ? 73  ILE   A CA  1 
ATOM   453  C  C   . ILE   A 1 60  ? -41.017 11.133  -4.363  1.00 12.53 ? 73  ILE   A C   1 
ATOM   454  O  O   . ILE   A 1 60  ? -41.315 10.575  -3.308  1.00 12.12 ? 73  ILE   A O   1 
ATOM   455  C  CB  . ILE   A 1 60  ? -38.543 11.599  -3.843  1.00 11.99 ? 73  ILE   A CB  1 
ATOM   456  C  CG1 . ILE   A 1 60  ? -38.437 10.775  -2.560  0.50 11.72 ? 73  ILE   A CG1 1 
ATOM   457  C  CG2 . ILE   A 1 60  ? -38.820 13.081  -3.561  1.00 12.64 ? 73  ILE   A CG2 1 
ATOM   458  C  CD1 . ILE   A 1 60  ? -37.944 9.350   -2.765  0.50 11.83 ? 73  ILE   A CD1 1 
ATOM   459  N  N   . THR   A 1 61  ? -41.903 11.824  -5.117  1.00 13.21 ? 74  THR   A N   1 
ATOM   460  C  CA  . THR   A 1 61  ? -43.305 11.970  -4.734  1.00 14.62 ? 74  THR   A CA  1 
ATOM   461  C  C   . THR   A 1 61  ? -44.177 10.911  -5.420  1.00 15.17 ? 74  THR   A C   1 
ATOM   462  O  O   . THR   A 1 61  ? -45.359 10.801  -5.093  1.00 15.14 ? 74  THR   A O   1 
ATOM   463  C  CB  . THR   A 1 61  ? -43.847 13.376  -5.036  1.00 15.35 ? 74  THR   A CB  1 
ATOM   464  O  OG1 . THR   A 1 61  ? -43.988 13.578  -6.443  1.00 13.99 ? 74  THR   A OG1 1 
ATOM   465  C  CG2 . THR   A 1 61  ? -42.993 14.466  -4.411  1.00 16.38 ? 74  THR   A CG2 1 
ATOM   466  N  N   . GLU   A 1 62  ? -43.618 10.154  -6.368  1.00 14.38 ? 75  GLU   A N   1 
ATOM   467  C  CA  . GLU   A 1 62  ? -44.416 9.207   -7.145  1.00 14.96 ? 75  GLU   A CA  1 
ATOM   468  C  C   . GLU   A 1 62  ? -43.829 7.797   -7.040  1.00 12.72 ? 75  GLU   A C   1 
ATOM   469  O  O   . GLU   A 1 62  ? -42.814 7.523   -7.673  1.00 12.32 ? 75  GLU   A O   1 
ATOM   470  C  CB  . GLU   A 1 62  ? -44.471 9.655   -8.601  1.00 18.49 ? 75  GLU   A CB  1 
ATOM   471  C  CG  . GLU   A 1 62  ? -45.507 8.908   -9.445  0.50 19.69 ? 75  GLU   A CG  1 
ATOM   472  C  CD  . GLU   A 1 62  ? -45.413 8.999   -10.967 0.50 22.11 ? 75  GLU   A CD  1 
ATOM   473  O  OE1 . GLU   A 1 62  ? -46.488 8.747   -11.570 0.50 22.07 ? 75  GLU   A OE1 1 
ATOM   474  O  OE2 . GLU   A 1 62  ? -44.328 9.224   -11.573 0.50 20.65 ? 75  GLU   A OE2 1 
ATOM   475  N  N   . GLU   A 1 63  ? -44.490 6.946   -6.244  1.00 13.60 ? 76  GLU   A N   1 
ATOM   476  C  CA  . GLU   A 1 63  ? -44.083 5.567   -6.036  1.00 14.68 ? 76  GLU   A CA  1 
ATOM   477  C  C   . GLU   A 1 63  ? -44.072 4.858   -7.393  1.00 12.93 ? 76  GLU   A C   1 
ATOM   478  O  O   . GLU   A 1 63  ? -44.970 5.062   -8.211  1.00 12.49 ? 76  GLU   A O   1 
ATOM   479  C  CB  . GLU   A 1 63  ? -45.026 4.881   -5.039  1.00 18.67 ? 76  GLU   A CB  1 
ATOM   480  C  CG  . GLU   A 1 63  ? -44.616 3.443   -4.726  1.00 22.93 ? 76  GLU   A CG  1 
ATOM   481  C  CD  . GLU   A 1 63  ? -45.218 2.772   -3.497  1.00 31.13 ? 76  GLU   A CD  1 
ATOM   482  O  OE1 . GLU   A 1 63  ? -46.327 3.188   -3.120  1.00 34.48 ? 76  GLU   A OE1 1 
ATOM   483  O  OE2 . GLU   A 1 63  ? -44.564 1.873   -2.899  1.00 37.29 ? 76  GLU   A OE2 1 
ATOM   484  N  N   . GLU   A 1 64  ? -43.069 4.005   -7.609  1.00 10.88 ? 77  GLU   A N   1 
ATOM   485  C  CA  . GLU   A 1 64  ? -42.979 3.225   -8.840  1.00 10.18 ? 77  GLU   A CA  1 
ATOM   486  C  C   . GLU   A 1 64  ? -42.277 1.908   -8.554  1.00 8.74  ? 77  GLU   A C   1 
ATOM   487  O  O   . GLU   A 1 64  ? -41.687 1.737   -7.495  1.00 8.19  ? 77  GLU   A O   1 
ATOM   488  C  CB  . GLU   A 1 64  ? -42.276 3.985   -9.948  1.00 11.05 ? 77  GLU   A CB  1 
ATOM   489  C  CG  . GLU   A 1 64  ? -40.935 4.588   -9.537  1.00 12.03 ? 77  GLU   A CG  1 
ATOM   490  C  CD  . GLU   A 1 64  ? -40.127 5.169   -10.687 1.00 11.97 ? 77  GLU   A CD  1 
ATOM   491  O  OE1 . GLU   A 1 64  ? -39.331 6.093   -10.420 1.00 10.73 ? 77  GLU   A OE1 1 
ATOM   492  O  OE2 . GLU   A 1 64  ? -40.185 4.624   -11.819 1.00 12.13 ? 77  GLU   A OE2 1 
ATOM   493  N  N   . ASP   A 1 65  ? -42.299 0.978   -9.523  1.00 7.98  ? 78  ASP   A N   1 
ATOM   494  C  CA  . ASP   A 1 65  ? -41.775 -0.357  -9.303  1.00 7.79  ? 78  ASP   A CA  1 
ATOM   495  C  C   . ASP   A 1 65  ? -40.269 -0.358  -9.023  1.00 7.39  ? 78  ASP   A C   1 
ATOM   496  O  O   . ASP   A 1 65  ? -39.803 -1.262  -8.329  1.00 7.53  ? 78  ASP   A O   1 
ATOM   497  C  CB  . ASP   A 1 65  ? -42.111 -1.288  -10.462 1.00 7.75  ? 78  ASP   A CB  1 
ATOM   498  C  CG  . ASP   A 1 65  ? -43.515 -1.869  -10.440 1.00 8.08  ? 78  ASP   A CG  1 
ATOM   499  O  OD1 . ASP   A 1 65  ? -43.832 -2.610  -11.387 1.00 8.35  ? 78  ASP   A OD1 1 
ATOM   500  O  OD2 . ASP   A 1 65  ? -44.294 -1.577  -9.489  1.00 8.72  ? 78  ASP   A OD2 1 
ATOM   501  N  N   . THR   A 1 66  ? -39.517 0.631   -9.528  1.00 6.84  ? 79  THR   A N   1 
ATOM   502  C  CA  . THR   A 1 66  ? -38.082 0.707   -9.275  1.00 7.25  ? 79  THR   A CA  1 
ATOM   503  C  C   . THR   A 1 66  ? -37.783 0.981   -7.795  1.00 7.17  ? 79  THR   A C   1 
ATOM   504  O  O   . THR   A 1 66  ? -36.642 0.735   -7.377  1.00 6.94  ? 79  THR   A O   1 
ATOM   505  C  CB  . THR   A 1 66  ? -37.399 1.807   -10.104 1.00 7.38  ? 79  THR   A CB  1 
ATOM   506  O  OG1 . THR   A 1 66  ? -38.005 3.076   -9.833  1.00 7.63  ? 79  THR   A OG1 1 
ATOM   507  C  CG2 . THR   A 1 66  ? -37.443 1.571   -11.606 1.00 7.65  ? 79  THR   A CG2 1 
ATOM   508  N  N   . TRP   A 1 67  ? -38.743 1.542   -7.024  1.00 7.62  ? 80  TRP   A N   1 
ATOM   509  C  CA  . TRP   A 1 67  ? -38.439 1.844   -5.624  1.00 7.55  ? 80  TRP   A CA  1 
ATOM   510  C  C   . TRP   A 1 67  ? -38.096 0.579   -4.847  1.00 7.33  ? 80  TRP   A C   1 
ATOM   511  O  O   . TRP   A 1 67  ? -38.781 -0.435  -4.972  1.00 7.75  ? 80  TRP   A O   1 
ATOM   512  C  CB  . TRP   A 1 67  ? -39.594 2.556   -4.918  1.00 7.95  ? 80  TRP   A CB  1 
ATOM   513  C  CG  . TRP   A 1 67  ? -39.757 4.008   -5.265  1.00 8.39  ? 80  TRP   A CG  1 
ATOM   514  C  CD1 . TRP   A 1 67  ? -39.218 4.720   -6.292  1.00 8.68  ? 80  TRP   A CD1 1 
ATOM   515  C  CD2 . TRP   A 1 67  ? -40.607 4.920   -4.541  1.00 9.43  ? 80  TRP   A CD2 1 
ATOM   516  N  NE1 . TRP   A 1 67  ? -39.643 6.025   -6.238  1.00 9.07  ? 80  TRP   A NE1 1 
ATOM   517  C  CE2 . TRP   A 1 67  ? -40.502 6.167   -5.183  1.00 9.20  ? 80  TRP   A CE2 1 
ATOM   518  C  CE3 . TRP   A 1 67  ? -41.440 4.779   -3.428  1.00 11.02 ? 80  TRP   A CE3 1 
ATOM   519  C  CZ2 . TRP   A 1 67  ? -41.220 7.275   -4.742  1.00 10.94 ? 80  TRP   A CZ2 1 
ATOM   520  C  CZ3 . TRP   A 1 67  ? -42.167 5.873   -3.003  1.00 11.74 ? 80  TRP   A CZ3 1 
ATOM   521  C  CH2 . TRP   A 1 67  ? -42.064 7.089   -3.673  1.00 11.02 ? 80  TRP   A CH2 1 
ATOM   522  N  N   . GLN   A 1 68  ? -37.068 0.677   -4.003  1.00 7.50  ? 81  GLN   A N   1 
ATOM   523  C  CA  . GLN   A 1 68  ? -36.815 -0.266  -2.931  1.00 7.76  ? 81  GLN   A CA  1 
ATOM   524  C  C   . GLN   A 1 68  ? -36.679 0.535   -1.637  1.00 8.79  ? 81  GLN   A C   1 
ATOM   525  O  O   . GLN   A 1 68  ? -35.741 1.303   -1.483  1.00 8.65  ? 81  GLN   A O   1 
ATOM   526  C  CB  . GLN   A 1 68  ? -35.572 -1.135  -3.172  1.00 8.15  ? 81  GLN   A CB  1 
ATOM   527  C  CG  . GLN   A 1 68  ? -35.620 -1.962  -4.451  1.00 8.16  ? 81  GLN   A CG  1 
ATOM   528  C  CD  . GLN   A 1 68  ? -34.325 -2.710  -4.654  1.00 7.93  ? 81  GLN   A CD  1 
ATOM   529  O  OE1 . GLN   A 1 68  ? -33.797 -3.296  -3.698  1.00 8.49  ? 81  GLN   A OE1 1 
ATOM   530  N  NE2 . GLN   A 1 68  ? -33.775 -2.621  -5.867  1.00 8.28  ? 81  GLN   A NE2 1 
ATOM   531  N  N   . LYS   A 1 69  ? -37.657 0.366   -0.727  1.00 9.37  ? 82  LYS   A N   1 
ATOM   532  C  CA  . LYS   A 1 69  ? -37.631 1.025   0.567   1.00 10.32 ? 82  LYS   A CA  1 
ATOM   533  C  C   . LYS   A 1 69  ? -36.994 0.046   1.545   1.00 11.12 ? 82  LYS   A C   1 
ATOM   534  O  O   . LYS   A 1 69  ? -37.507 -1.067  1.731   1.00 12.50 ? 82  LYS   A O   1 
ATOM   535  C  CB  . LYS   A 1 69  ? -39.054 1.353   1.032   1.00 11.34 ? 82  LYS   A CB  1 
ATOM   536  C  CG  . LYS   A 1 69  ? -39.827 2.365   0.214   1.00 12.84 ? 82  LYS   A CG  1 
ATOM   537  C  CD  . LYS   A 1 69  ? -41.179 2.727   0.822   0.50 12.61 ? 82  LYS   A CD  1 
ATOM   538  C  CE  . LYS   A 1 69  ? -41.892 3.818   0.093   0.10 12.69 ? 82  LYS   A CE  1 
ATOM   539  N  NZ  . LYS   A 1 69  ? -43.134 4.170   0.784   0.10 12.88 ? 82  LYS   A NZ  1 
ATOM   540  N  N   . LEU   A 1 70  ? -35.842 0.413   2.098   1.00 10.47 ? 83  LEU   A N   1 
ATOM   541  C  CA  . LEU   A 1 70  ? -35.033 -0.520  2.856   1.00 10.80 ? 83  LEU   A CA  1 
ATOM   542  C  C   . LEU   A 1 70  ? -34.771 -0.016  4.272   1.00 10.55 ? 83  LEU   A C   1 
ATOM   543  O  O   . LEU   A 1 70  ? -34.489 1.154   4.483   1.00 10.42 ? 83  LEU   A O   1 
ATOM   544  C  CB  . LEU   A 1 70  ? -33.738 -0.757  2.090   1.00 12.85 ? 83  LEU   A CB  1 
ATOM   545  C  CG  . LEU   A 1 70  ? -33.968 -1.399  0.716   1.00 15.04 ? 83  LEU   A CG  1 
ATOM   546  C  CD1 . LEU   A 1 70  ? -32.675 -1.400  -0.070  1.00 17.01 ? 83  LEU   A CD1 1 
ATOM   547  C  CD2 . LEU   A 1 70  ? -34.529 -2.796  0.900   1.00 17.80 ? 83  LEU   A CD2 1 
ATOM   548  N  N   . GLU   A 1 71  ? -34.885 -0.939  5.231   1.00 9.86  ? 84  GLU   A N   1 
ATOM   549  C  CA  . GLU   A 1 71  ? -34.625 -0.688  6.638   1.00 9.33  ? 84  GLU   A CA  1 
ATOM   550  C  C   . GLU   A 1 71  ? -33.124 -0.627  6.897   1.00 8.94  ? 84  GLU   A C   1 
ATOM   551  O  O   . GLU   A 1 71  ? -32.353 -1.393  6.317   1.00 8.77  ? 84  GLU   A O   1 
ATOM   552  C  CB  . GLU   A 1 71  ? -35.271 -1.839  7.423   1.00 10.65 ? 84  GLU   A CB  1 
ATOM   553  C  CG  . GLU   A 1 71  ? -34.961 -1.871  8.913   1.00 11.54 ? 84  GLU   A CG  1 
ATOM   554  C  CD  . GLU   A 1 71  ? -35.480 -3.135  9.578   1.00 12.69 ? 84  GLU   A CD  1 
ATOM   555  O  OE1 . GLU   A 1 71  ? -36.398 -3.825  9.045   1.00 16.44 ? 84  GLU   A OE1 1 
ATOM   556  O  OE2 . GLU   A 1 71  ? -34.806 -3.514  10.541  1.00 10.91 ? 84  GLU   A OE2 1 
ATOM   557  N  N   . VAL   A 1 72  ? -32.727 0.312   7.761   1.00 8.75  ? 85  VAL   A N   1 
ATOM   558  C  CA  . VAL   A 1 72  ? -31.368 0.394   8.288   1.00 8.54  ? 85  VAL   A CA  1 
ATOM   559  C  C   . VAL   A 1 72  ? -31.301 -0.338  9.630   1.00 8.90  ? 85  VAL   A C   1 
ATOM   560  O  O   . VAL   A 1 72  ? -32.086 -0.026  10.530  1.00 9.76  ? 85  VAL   A O   1 
ATOM   561  C  CB  . VAL   A 1 72  ? -30.965 1.869   8.460   1.00 8.50  ? 85  VAL   A CB  1 
ATOM   562  C  CG1 . VAL   A 1 72  ? -29.630 1.971   9.187   1.00 8.52  ? 85  VAL   A CG1 1 
ATOM   563  C  CG2 . VAL   A 1 72  ? -30.917 2.601   7.117   1.00 8.36  ? 85  VAL   A CG2 1 
ATOM   564  N  N   A ILE   A 1 73  ? -30.351 -1.268  9.808   0.50 9.07  ? 86  ILE   A N   1 
ATOM   565  N  N   B ILE   A 1 73  ? -30.384 -1.314  9.733   0.50 8.65  ? 86  ILE   A N   1 
ATOM   566  C  CA  A ILE   A 1 73  ? -30.242 -1.970  11.087  0.50 9.02  ? 86  ILE   A CA  1 
ATOM   567  C  CA  B ILE   A 1 73  ? -30.196 -2.058  10.973  0.50 8.42  ? 86  ILE   A CA  1 
ATOM   568  C  C   A ILE   A 1 73  ? -29.222 -1.348  12.030  0.50 8.62  ? 86  ILE   A C   1 
ATOM   569  C  C   B ILE   A 1 73  ? -29.327 -1.272  11.962  0.50 8.34  ? 86  ILE   A C   1 
ATOM   570  O  O   A ILE   A 1 73  ? -29.282 -1.567  13.238  0.50 8.36  ? 86  ILE   A O   1 
ATOM   571  O  O   B ILE   A 1 73  ? -29.685 -1.194  13.135  0.50 8.46  ? 86  ILE   A O   1 
ATOM   572  C  CB  A ILE   A 1 73  ? -29.928 -3.460  10.906  0.50 9.71  ? 86  ILE   A CB  1 
ATOM   573  C  CB  B ILE   A 1 73  ? -29.667 -3.487  10.710  0.50 8.44  ? 86  ILE   A CB  1 
ATOM   574  C  CG1 A ILE   A 1 73  ? -28.727 -3.740  10.020  0.50 9.69  ? 86  ILE   A CG1 1 
ATOM   575  C  CG1 B ILE   A 1 73  ? -29.822 -4.341  11.966  0.50 8.71  ? 86  ILE   A CG1 1 
ATOM   576  C  CG2 A ILE   A 1 73  ? -31.176 -4.153  10.399  0.50 10.15 ? 86  ILE   A CG2 1 
ATOM   577  C  CG2 B ILE   A 1 73  ? -28.235 -3.510  10.182  0.50 8.23  ? 86  ILE   A CG2 1 
ATOM   578  C  CD1 A ILE   A 1 73  ? -28.442 -5.222  9.857   0.50 10.25 ? 86  ILE   A CD1 1 
ATOM   579  C  CD1 B ILE   A 1 73  ? -29.175 -5.707  11.888  0.50 8.69  ? 86  ILE   A CD1 1 
ATOM   580  N  N   . LYS   A 1 74  ? -28.226 -0.656  11.490  1.00 8.42  ? 87  LYS   A N   1 
ATOM   581  C  CA  . LYS   A 1 74  ? -27.214 -0.036  12.338  1.00 8.56  ? 87  LYS   A CA  1 
ATOM   582  C  C   . LYS   A 1 74  ? -26.546 1.117   11.590  1.00 8.76  ? 87  LYS   A C   1 
ATOM   583  O  O   . LYS   A 1 74  ? -26.364 1.038   10.367  1.00 7.87  ? 87  LYS   A O   1 
ATOM   584  C  CB  . LYS   A 1 74  ? -26.155 -1.080  12.720  1.00 9.65  ? 87  LYS   A CB  1 
ATOM   585  C  CG  . LYS   A 1 74  ? -25.127 -0.681  13.781  0.50 10.22 ? 87  LYS   A CG  1 
ATOM   586  C  CD  . LYS   A 1 74  ? -24.376 -1.888  14.337  0.50 11.19 ? 87  LYS   A CD  1 
ATOM   587  C  CE  . LYS   A 1 74  ? -23.280 -1.541  15.302  0.50 12.42 ? 87  LYS   A CE  1 
ATOM   588  N  NZ  . LYS   A 1 74  ? -23.838 -0.777  16.415  0.50 14.01 ? 87  LYS   A NZ  1 
ATOM   589  N  N   . GLN   A 1 75  ? -26.204 2.160   12.369  1.00 9.05  ? 88  GLN   A N   1 
ATOM   590  C  CA  . GLN   A 1 75  ? -25.503 3.351   11.906  1.00 8.88  ? 88  GLN   A CA  1 
ATOM   591  C  C   . GLN   A 1 75  ? -24.080 3.333   12.452  1.00 9.49  ? 88  GLN   A C   1 
ATOM   592  O  O   . GLN   A 1 75  ? -23.865 3.102   13.644  1.00 10.49 ? 88  GLN   A O   1 
ATOM   593  C  CB  . GLN   A 1 75  ? -26.221 4.610   12.383  1.00 8.80  ? 88  GLN   A CB  1 
ATOM   594  C  CG  . GLN   A 1 75  ? -27.670 4.727   11.929  1.00 8.59  ? 88  GLN   A CG  1 
ATOM   595  C  CD  . GLN   A 1 75  ? -28.416 5.815   12.660  1.00 8.98  ? 88  GLN   A CD  1 
ATOM   596  O  OE1 . GLN   A 1 75  ? -28.009 6.987   12.660  1.00 8.75  ? 88  GLN   A OE1 1 
ATOM   597  N  NE2 . GLN   A 1 75  ? -29.518 5.454   13.308  1.00 8.96  ? 88  GLN   A NE2 1 
ATOM   598  N  N   . PHE   A 1 76  ? -23.100 3.551   11.563  1.00 8.91  ? 89  PHE   A N   1 
ATOM   599  C  CA  . PHE   A 1 76  ? -21.695 3.607   11.927  1.00 9.67  ? 89  PHE   A CA  1 
ATOM   600  C  C   . PHE   A 1 76  ? -21.171 5.014   11.653  1.00 10.02 ? 89  PHE   A C   1 
ATOM   601  O  O   . PHE   A 1 76  ? -20.634 5.265   10.582  1.00 9.18  ? 89  PHE   A O   1 
ATOM   602  C  CB  . PHE   A 1 76  ? -20.863 2.585   11.139  1.00 10.24 ? 89  PHE   A CB  1 
ATOM   603  C  CG  . PHE   A 1 76  ? -21.215 1.123   11.383  1.00 10.61 ? 89  PHE   A CG  1 
ATOM   604  C  CD1 . PHE   A 1 76  ? -22.208 0.495   10.643  1.00 11.69 ? 89  PHE   A CD1 1 
ATOM   605  C  CD2 . PHE   A 1 76  ? -20.563 0.376   12.354  1.00 11.70 ? 89  PHE   A CD2 1 
ATOM   606  C  CE1 . PHE   A 1 76  ? -22.513 -0.831  10.844  1.00 12.92 ? 89  PHE   A CE1 1 
ATOM   607  C  CE2 . PHE   A 1 76  ? -20.879 -0.970  12.562  1.00 12.59 ? 89  PHE   A CE2 1 
ATOM   608  C  CZ  . PHE   A 1 76  ? -21.862 -1.568  11.815  1.00 12.78 ? 89  PHE   A CZ  1 
ATOM   609  N  N   . ARG   A 1 77  ? -21.289 5.907   12.643  1.00 10.78 ? 90  ARG   A N   1 
ATOM   610  C  CA  . ARG   A 1 77  ? -20.793 7.273   12.526  1.00 12.47 ? 90  ARG   A CA  1 
ATOM   611  C  C   . ARG   A 1 77  ? -19.290 7.251   12.788  1.00 12.01 ? 90  ARG   A C   1 
ATOM   612  O  O   . ARG   A 1 77  ? -18.826 6.461   13.614  1.00 12.09 ? 90  ARG   A O   1 
ATOM   613  C  CB  . ARG   A 1 77  ? -21.639 8.124   13.483  1.00 14.40 ? 90  ARG   A CB  1 
ATOM   614  C  CG  . ARG   A 1 77  ? -21.543 9.624   13.256  1.00 17.17 ? 90  ARG   A CG  1 
ATOM   615  C  CD  . ARG   A 1 77  ? -22.437 10.483  14.160  1.00 20.23 ? 90  ARG   A CD  1 
ATOM   616  N  NE  . ARG   A 1 77  ? -22.097 10.273  15.573  1.00 23.30 ? 90  ARG   A NE  1 
ATOM   617  C  CZ  . ARG   A 1 77  ? -22.638 10.906  16.596  1.00 28.98 ? 90  ARG   A CZ  1 
ATOM   618  N  NH1 . ARG   A 1 77  ? -23.407 11.973  16.410  1.00 28.55 ? 90  ARG   A NH1 1 
ATOM   619  N  NH2 . ARG   A 1 77  ? -22.392 10.463  17.820  1.00 32.14 ? 90  ARG   A NH2 1 
ATOM   620  N  N   . HIS   A 1 78  ? -18.511 8.057   12.050  1.00 11.73 ? 91  HIS   A N   1 
ATOM   621  C  CA  . HIS   A 1 78  ? -17.075 8.110   12.264  1.00 12.39 ? 91  HIS   A CA  1 
ATOM   622  C  C   . HIS   A 1 78  ? -16.820 8.429   13.741  1.00 12.29 ? 91  HIS   A C   1 
ATOM   623  O  O   . HIS   A 1 78  ? -17.442 9.341   14.299  1.00 11.57 ? 91  HIS   A O   1 
ATOM   624  C  CB  . HIS   A 1 78  ? -16.388 9.163   11.384  1.00 13.10 ? 91  HIS   A CB  1 
ATOM   625  C  CG  . HIS   A 1 78  ? -14.920 8.959   11.314  1.00 14.01 ? 91  HIS   A CG  1 
ATOM   626  N  ND1 . HIS   A 1 78  ? -14.068 9.252   12.368  1.00 13.76 ? 91  HIS   A ND1 1 
ATOM   627  C  CD2 . HIS   A 1 78  ? -14.158 8.391   10.354  1.00 15.08 ? 91  HIS   A CD2 1 
ATOM   628  C  CE1 . HIS   A 1 78  ? -12.839 8.940   12.016  1.00 15.13 ? 91  HIS   A CE1 1 
ATOM   629  N  NE2 . HIS   A 1 78  ? -12.856 8.392   10.803  1.00 15.81 ? 91  HIS   A NE2 1 
ATOM   630  N  N   . PRO   A 1 79  ? -15.952 7.644   14.419  1.00 13.34 ? 92  PRO   A N   1 
ATOM   631  C  CA  . PRO   A 1 79  ? -15.765 7.796   15.866  1.00 14.37 ? 92  PRO   A CA  1 
ATOM   632  C  C   . PRO   A 1 79  ? -15.165 9.136   16.283  1.00 14.73 ? 92  PRO   A C   1 
ATOM   633  O  O   . PRO   A 1 79  ? -15.337 9.532   17.433  1.00 16.09 ? 92  PRO   A O   1 
ATOM   634  C  CB  . PRO   A 1 79  ? -14.852 6.620   16.246  1.00 14.20 ? 92  PRO   A CB  1 
ATOM   635  C  CG  . PRO   A 1 79  ? -14.221 6.160   14.970  1.00 15.46 ? 92  PRO   A CG  1 
ATOM   636  C  CD  . PRO   A 1 79  ? -15.201 6.511   13.862  1.00 14.74 ? 92  PRO   A CD  1 
ATOM   637  N  N   . LYS   A 1 80  ? -14.539 9.866   15.344  1.00 13.70 ? 93  LYS   A N   1 
ATOM   638  C  CA  . LYS   A 1 80  ? -13.946 11.167  15.652  1.00 15.09 ? 93  LYS   A CA  1 
ATOM   639  C  C   . LYS   A 1 80  ? -14.780 12.342  15.122  1.00 13.41 ? 93  LYS   A C   1 
ATOM   640  O  O   . LYS   A 1 80  ? -14.372 13.498  15.260  1.00 12.65 ? 93  LYS   A O   1 
ATOM   641  C  CB  . LYS   A 1 80  ? -12.502 11.178  15.132  1.00 16.58 ? 93  LYS   A CB  1 
ATOM   642  C  CG  . LYS   A 1 80  ? -11.562 10.202  15.838  1.00 18.68 ? 93  LYS   A CG  1 
ATOM   643  C  CD  . LYS   A 1 80  ? -10.085 10.350  15.492  0.10 18.06 ? 93  LYS   A CD  1 
ATOM   644  C  CE  . LYS   A 1 80  ? -9.235  9.500   16.385  0.10 18.02 ? 93  LYS   A CE  1 
ATOM   645  N  NZ  . LYS   A 1 80  ? -7.804  9.678   16.138  0.10 17.98 ? 93  LYS   A NZ  1 
ATOM   646  N  N   . TYR   A 1 81  ? -16.011 12.066  14.628  1.00 12.10 ? 94  TYR   A N   1 
ATOM   647  C  CA  . TYR   A 1 81  ? -16.917 13.108  14.178  1.00 11.62 ? 94  TYR   A CA  1 
ATOM   648  C  C   . TYR   A 1 81  ? -17.116 14.144  15.286  1.00 13.33 ? 94  TYR   A C   1 
ATOM   649  O  O   . TYR   A 1 81  ? -17.423 13.795  16.428  1.00 15.01 ? 94  TYR   A O   1 
ATOM   650  C  CB  . TYR   A 1 81  ? -18.260 12.527  13.731  1.00 11.41 ? 94  TYR   A CB  1 
ATOM   651  C  CG  . TYR   A 1 81  ? -19.289 13.593  13.399  1.00 10.94 ? 94  TYR   A CG  1 
ATOM   652  C  CD1 . TYR   A 1 81  ? -19.070 14.515  12.383  1.00 11.03 ? 94  TYR   A CD1 1 
ATOM   653  C  CD2 . TYR   A 1 81  ? -20.490 13.685  14.093  1.00 11.77 ? 94  TYR   A CD2 1 
ATOM   654  C  CE1 . TYR   A 1 81  ? -20.004 15.497  12.094  1.00 10.67 ? 94  TYR   A CE1 1 
ATOM   655  C  CE2 . TYR   A 1 81  ? -21.429 14.665  13.810  1.00 11.70 ? 94  TYR   A CE2 1 
ATOM   656  C  CZ  . TYR   A 1 81  ? -21.198 15.552  12.782  1.00 11.74 ? 94  TYR   A CZ  1 
ATOM   657  O  OH  . TYR   A 1 81  ? -22.084 16.533  12.475  1.00 12.56 ? 94  TYR   A OH  1 
ATOM   658  N  N   . ASN   A 1 82  ? -16.964 15.421  14.921  1.00 13.05 ? 95  ASN   A N   1 
ATOM   659  C  CA  . ASN   A 1 82  ? -17.028 16.538  15.843  1.00 14.62 ? 95  ASN   A CA  1 
ATOM   660  C  C   . ASN   A 1 82  ? -18.169 17.468  15.426  1.00 14.93 ? 95  ASN   A C   1 
ATOM   661  O  O   . ASN   A 1 82  ? -18.125 18.060  14.351  1.00 15.28 ? 95  ASN   A O   1 
ATOM   662  C  CB  . ASN   A 1 82  ? -15.657 17.209  15.901  1.00 15.24 ? 95  ASN   A CB  1 
ATOM   663  C  CG  . ASN   A 1 82  ? -15.584 18.330  16.919  1.00 16.17 ? 95  ASN   A CG  1 
ATOM   664  O  OD1 . ASN   A 1 82  ? -16.397 19.249  16.911  1.00 15.71 ? 95  ASN   A OD1 1 
ATOM   665  N  ND2 . ASN   A 1 82  ? -14.581 18.296  17.779  1.00 20.20 ? 95  ASN   A ND2 1 
ATOM   666  N  N   . THR   A 1 83  ? -19.170 17.657  16.292  1.00 15.45 ? 96  THR   A N   1 
ATOM   667  C  CA  . THR   A 1 83  ? -20.341 18.446  15.924  1.00 17.18 ? 96  THR   A CA  1 
ATOM   668  C  C   . THR   A 1 83  ? -20.040 19.946  15.875  1.00 18.24 ? 96  THR   A C   1 
ATOM   669  O  O   . THR   A 1 83  ? -20.855 20.691  15.343  1.00 21.75 ? 96  THR   A O   1 
ATOM   670  C  CB  . THR   A 1 83  ? -21.510 18.173  16.871  1.00 19.25 ? 96  THR   A CB  1 
ATOM   671  O  OG1 . THR   A 1 83  ? -21.084 18.486  18.197  1.00 19.96 ? 96  THR   A OG1 1 
ATOM   672  C  CG2 . THR   A 1 83  ? -21.953 16.725  16.841  1.00 19.09 ? 96  THR   A CG2 1 
ATOM   673  N  N   . SER   A 1 84  ? -18.926 20.400  16.472  1.00 17.26 ? 97  SER   A N   1 
ATOM   674  C  CA  . SER   A 1 84  ? -18.522 21.801  16.445  1.00 18.25 ? 97  SER   A CA  1 
ATOM   675  C  C   . SER   A 1 84  ? -17.764 22.158  15.166  1.00 15.86 ? 97  SER   A C   1 
ATOM   676  O  O   . SER   A 1 84  ? -18.118 23.147  14.520  1.00 18.82 ? 97  SER   A O   1 
ATOM   677  C  CB  . SER   A 1 84  ? -17.682 22.174  17.646  1.00 19.89 ? 97  SER   A CB  1 
ATOM   678  O  OG  . SER   A 1 84  ? -18.486 22.115  18.811  1.00 24.99 ? 97  SER   A OG  1 
ATOM   679  N  N   . THR   A 1 85  ? -16.722 21.382  14.843  1.00 13.70 ? 98  THR   A N   1 
ATOM   680  C  CA  . THR   A 1 85  ? -15.846 21.660  13.703  1.00 12.54 ? 98  THR   A CA  1 
ATOM   681  C  C   . THR   A 1 85  ? -16.413 21.045  12.422  1.00 11.79 ? 98  THR   A C   1 
ATOM   682  O  O   . THR   A 1 85  ? -16.040 21.470  11.323  1.00 11.06 ? 98  THR   A O   1 
ATOM   683  C  CB  . THR   A 1 85  ? -14.433 21.119  13.907  1.00 13.28 ? 98  THR   A CB  1 
ATOM   684  O  OG1 . THR   A 1 85  ? -14.505 19.701  14.103  1.00 12.40 ? 98  THR   A OG1 1 
ATOM   685  C  CG2 . THR   A 1 85  ? -13.718 21.789  15.070  1.00 13.63 ? 98  THR   A CG2 1 
ATOM   686  N  N   . LEU   A 1 86  ? -17.238 20.006  12.593  1.00 11.72 ? 99  LEU   A N   1 
ATOM   687  C  CA  . LEU   A 1 86  ? -17.725 19.130  11.530  1.00 11.17 ? 99  LEU   A CA  1 
ATOM   688  C  C   . LEU   A 1 86  ? -16.595 18.347  10.855  1.00 11.31 ? 99  LEU   A C   1 
ATOM   689  O  O   . LEU   A 1 86  ? -16.812 17.758  9.806   1.00 10.03 ? 99  LEU   A O   1 
ATOM   690  C  CB  . LEU   A 1 86  ? -18.603 19.879  10.519  1.00 11.68 ? 99  LEU   A CB  1 
ATOM   691  C  CG  . LEU   A 1 86  ? -19.834 20.598  11.079  1.00 13.27 ? 99  LEU   A CG  1 
ATOM   692  C  CD1 . LEU   A 1 86  ? -20.552 21.391  9.996   1.00 13.70 ? 99  LEU   A CD1 1 
ATOM   693  C  CD2 . LEU   A 1 86  ? -20.799 19.630  11.713  1.00 13.75 ? 99  LEU   A CD2 1 
ATOM   694  N  N   . HIS   A 1 87  ? -15.432 18.178  11.501  1.00 10.55 ? 100 HIS   A N   1 
ATOM   695  C  CA  . HIS   A 1 87  ? -14.438 17.252  10.991  1.00 10.79 ? 100 HIS   A CA  1 
ATOM   696  C  C   . HIS   A 1 87  ? -14.961 15.817  11.023  1.00 9.80  ? 100 HIS   A C   1 
ATOM   697  O  O   . HIS   A 1 87  ? -15.725 15.456  11.926  1.00 9.99  ? 100 HIS   A O   1 
ATOM   698  C  CB  . HIS   A 1 87  ? -13.121 17.327  11.768  1.00 11.05 ? 100 HIS   A CB  1 
ATOM   699  C  CG  . HIS   A 1 87  ? -12.391 18.606  11.543  1.00 12.78 ? 100 HIS   A CG  1 
ATOM   700  N  ND1 . HIS   A 1 87  ? -11.206 18.887  12.201  1.00 14.24 ? 100 HIS   A ND1 1 
ATOM   701  C  CD2 . HIS   A 1 87  ? -12.592 19.632  10.705  1.00 13.49 ? 100 HIS   A CD2 1 
ATOM   702  C  CE1 . HIS   A 1 87  ? -10.753 20.075  11.788  1.00 15.38 ? 100 HIS   A CE1 1 
ATOM   703  N  NE2 . HIS   A 1 87  ? -11.558 20.545  10.882  1.00 12.88 ? 100 HIS   A NE2 1 
ATOM   704  N  N   . HIS   A 1 88  ? -14.561 15.043  10.004  1.00 9.65  ? 101 HIS   A N   1 
ATOM   705  C  CA  . HIS   A 1 88  ? -14.859 13.616  9.914   1.00 9.51  ? 101 HIS   A CA  1 
ATOM   706  C  C   . HIS   A 1 88  ? -16.358 13.380  9.737   1.00 9.09  ? 101 HIS   A C   1 
ATOM   707  O  O   . HIS   A 1 88  ? -16.927 12.482  10.348  1.00 9.05  ? 101 HIS   A O   1 
ATOM   708  C  CB  . HIS   A 1 88  ? -14.285 12.843  11.108  1.00 9.99  ? 101 HIS   A CB  1 
ATOM   709  C  CG  . HIS   A 1 88  ? -12.907 13.275  11.432  1.00 10.90 ? 101 HIS   A CG  1 
ATOM   710  N  ND1 . HIS   A 1 88  ? -12.550 13.800  12.656  1.00 13.62 ? 101 HIS   A ND1 1 
ATOM   711  C  CD2 . HIS   A 1 88  ? -11.819 13.317  10.670  1.00 11.01 ? 101 HIS   A CD2 1 
ATOM   712  C  CE1 . HIS   A 1 88  ? -11.268 14.139  12.608  1.00 11.89 ? 101 HIS   A CE1 1 
ATOM   713  N  NE2 . HIS   A 1 88  ? -10.817 13.869  11.424  1.00 14.76 ? 101 HIS   A NE2 1 
ATOM   714  N  N   . ASP   A 1 89  ? -16.974 14.166  8.852   1.00 8.47  ? 102 ASP   A N   1 
ATOM   715  C  CA  . ASP   A 1 89  ? -18.404 14.111  8.601   1.00 8.32  ? 102 ASP   A CA  1 
ATOM   716  C  C   . ASP   A 1 89  ? -18.709 12.977  7.620   1.00 8.09  ? 102 ASP   A C   1 
ATOM   717  O  O   . ASP   A 1 89  ? -18.937 13.207  6.439   1.00 8.37  ? 102 ASP   A O   1 
ATOM   718  C  CB  . ASP   A 1 89  ? -18.950 15.456  8.136   1.00 8.32  ? 102 ASP   A CB  1 
ATOM   719  C  CG  . ASP   A 1 89  ? -20.466 15.562  8.103   1.00 7.93  ? 102 ASP   A CG  1 
ATOM   720  O  OD1 . ASP   A 1 89  ? -21.133 14.631  8.651   1.00 8.76  ? 102 ASP   A OD1 1 
ATOM   721  O  OD2 . ASP   A 1 89  ? -20.964 16.583  7.585   1.00 8.32  ? 102 ASP   A OD2 1 
ATOM   722  N  N   . ILE   A 1 90  ? -18.734 11.742  8.133   1.00 7.36  ? 103 ILE   A N   1 
ATOM   723  C  CA  . ILE   A 1 90  ? -18.873 10.554  7.308   1.00 7.78  ? 103 ILE   A CA  1 
ATOM   724  C  C   . ILE   A 1 90  ? -19.517 9.462   8.155   1.00 8.13  ? 103 ILE   A C   1 
ATOM   725  O  O   . ILE   A 1 90  ? -19.218 9.350   9.343   1.00 8.57  ? 103 ILE   A O   1 
ATOM   726  C  CB  . ILE   A 1 90  ? -17.531 10.140  6.658   1.00 8.20  ? 103 ILE   A CB  1 
ATOM   727  C  CG1 . ILE   A 1 90  ? -17.728 9.031   5.615   1.00 8.32  ? 103 ILE   A CG1 1 
ATOM   728  C  CG2 . ILE   A 1 90  ? -16.465 9.783   7.702   1.00 8.65  ? 103 ILE   A CG2 1 
ATOM   729  C  CD1 . ILE   A 1 90  ? -16.512 8.755   4.747   1.00 8.64  ? 103 ILE   A CD1 1 
ATOM   730  N  N   . MET   A 1 91  ? -20.409 8.678   7.526   1.00 8.09  ? 104 MET   A N   1 
ATOM   731  C  CA  . MET   A 1 91  ? -21.146 7.610   8.181   1.00 8.09  ? 104 MET   A CA  1 
ATOM   732  C  C   . MET   A 1 91  ? -21.515 6.516   7.180   1.00 8.35  ? 104 MET   A C   1 
ATOM   733  O  O   . MET   A 1 91  ? -21.834 6.795   6.012   1.00 8.47  ? 104 MET   A O   1 
ATOM   734  C  CB  . MET   A 1 91  ? -22.411 8.151   8.863   1.00 8.60  ? 104 MET   A CB  1 
ATOM   735  C  CG  . MET   A 1 91  ? -23.366 7.113   9.455   1.00 8.26  ? 104 MET   A CG  1 
ATOM   736  S  SD  . MET   A 1 91  ? -24.726 7.847   10.402  1.00 8.89  ? 104 MET   A SD  1 
ATOM   737  C  CE  . MET   A 1 91  ? -25.607 8.800   9.170   1.00 8.27  ? 104 MET   A CE  1 
ATOM   738  N  N   . LEU   A 1 92  ? -21.455 5.261   7.679   1.00 7.83  ? 105 LEU   A N   1 
ATOM   739  C  CA  . LEU   A 1 92  ? -21.938 4.109   6.937   1.00 7.99  ? 105 LEU   A CA  1 
ATOM   740  C  C   . LEU   A 1 92  ? -23.235 3.600   7.561   1.00 7.74  ? 105 LEU   A C   1 
ATOM   741  O  O   . LEU   A 1 92  ? -23.349 3.533   8.788   1.00 8.29  ? 105 LEU   A O   1 
ATOM   742  C  CB  . LEU   A 1 92  ? -20.869 3.022   6.917   1.00 8.66  ? 105 LEU   A CB  1 
ATOM   743  C  CG  . LEU   A 1 92  ? -19.772 3.208   5.871   1.00 8.76  ? 105 LEU   A CG  1 
ATOM   744  C  CD1 . LEU   A 1 92  ? -18.589 2.338   6.265   1.00 9.39  ? 105 LEU   A CD1 1 
ATOM   745  C  CD2 . LEU   A 1 92  ? -20.235 2.888   4.436   1.00 8.52  ? 105 LEU   A CD2 1 
ATOM   746  N  N   . LEU   A 1 93  ? -24.188 3.241   6.698   1.00 7.75  ? 106 LEU   A N   1 
ATOM   747  C  CA  . LEU   A 1 93  ? -25.461 2.654   7.099   1.00 8.02  ? 106 LEU   A CA  1 
ATOM   748  C  C   . LEU   A 1 93  ? -25.509 1.221   6.616   1.00 8.22  ? 106 LEU   A C   1 
ATOM   749  O  O   . LEU   A 1 93  ? -25.432 0.986   5.418   1.00 8.24  ? 106 LEU   A O   1 
ATOM   750  C  CB  . LEU   A 1 93  ? -26.663 3.396   6.530   1.00 7.61  ? 106 LEU   A CB  1 
ATOM   751  C  CG  . LEU   A 1 93  ? -26.719 4.900   6.797   1.00 7.95  ? 106 LEU   A CG  1 
ATOM   752  C  CD1 . LEU   A 1 93  ? -27.887 5.491   6.014   1.00 8.27  ? 106 LEU   A CD1 1 
ATOM   753  C  CD2 . LEU   A 1 93  ? -26.803 5.186   8.275   1.00 8.10  ? 106 LEU   A CD2 1 
ATOM   754  N  N   . LYS   A 1 94  ? -25.706 0.277   7.546   1.00 8.53  ? 107 LYS   A N   1 
ATOM   755  C  CA  . LYS   A 1 94  ? -25.889 -1.109  7.155   1.00 8.87  ? 107 LYS   A CA  1 
ATOM   756  C  C   . LYS   A 1 94  ? -27.380 -1.358  7.012   1.00 8.50  ? 107 LYS   A C   1 
ATOM   757  O  O   . LYS   A 1 94  ? -28.163 -1.065  7.928   1.00 8.09  ? 107 LYS   A O   1 
ATOM   758  C  CB  . LYS   A 1 94  ? -25.276 -2.069  8.174   1.00 10.04 ? 107 LYS   A CB  1 
ATOM   759  C  CG  . LYS   A 1 94  ? -25.330 -3.522  7.757   1.00 11.26 ? 107 LYS   A CG  1 
ATOM   760  C  CD  . LYS   A 1 94  ? -24.651 -4.454  8.750   1.00 13.04 ? 107 LYS   A CD  1 
ATOM   761  C  CE  . LYS   A 1 94  ? -24.682 -5.850  8.239   1.00 14.35 ? 107 LYS   A CE  1 
ATOM   762  N  NZ  . LYS   A 1 94  ? -23.887 -6.728  9.107   1.00 15.88 ? 107 LYS   A NZ  1 
ATOM   763  N  N   . LEU   A 1 95  ? -27.750 -1.909  5.857   1.00 8.15  ? 108 LEU   A N   1 
ATOM   764  C  CA  . LEU   A 1 95  ? -29.136 -2.249  5.570   1.00 8.68  ? 108 LEU   A CA  1 
ATOM   765  C  C   . LEU   A 1 95  ? -29.456 -3.641  6.115   1.00 9.18  ? 108 LEU   A C   1 
ATOM   766  O  O   . LEU   A 1 95  ? -28.598 -4.539  6.163   1.00 9.15  ? 108 LEU   A O   1 
ATOM   767  C  CB  . LEU   A 1 95  ? -29.434 -2.171  4.080   1.00 9.00  ? 108 LEU   A CB  1 
ATOM   768  C  CG  . LEU   A 1 95  ? -28.934 -0.912  3.364   1.00 9.55  ? 108 LEU   A CG  1 
ATOM   769  C  CD1 . LEU   A 1 95  ? -29.253 -0.938  1.874   1.00 10.04 ? 108 LEU   A CD1 1 
ATOM   770  C  CD2 . LEU   A 1 95  ? -29.514 0.368   3.997   1.00 10.22 ? 108 LEU   A CD2 1 
ATOM   771  N  N   . LYS   A 1 96  ? -30.728 -3.804  6.483   1.00 9.95  ? 109 LYS   A N   1 
ATOM   772  C  CA  . LYS   A 1 96  ? -31.225 -5.039  7.065   1.00 11.53 ? 109 LYS   A CA  1 
ATOM   773  C  C   . LYS   A 1 96  ? -31.067 -6.199  6.088   1.00 11.57 ? 109 LYS   A C   1 
ATOM   774  O  O   . LYS   A 1 96  ? -30.706 -7.302  6.524   1.00 13.01 ? 109 LYS   A O   1 
ATOM   775  C  CB  . LYS   A 1 96  ? -32.705 -4.929  7.442   1.00 12.84 ? 109 LYS   A CB  1 
ATOM   776  C  CG  . LYS   A 1 96  ? -33.277 -6.125  8.214   1.00 13.84 ? 109 LYS   A CG  1 
ATOM   777  C  CD  . LYS   A 1 96  ? -32.777 -6.189  9.645   1.00 15.65 ? 109 LYS   A CD  1 
ATOM   778  C  CE  . LYS   A 1 96  ? -33.357 -7.283  10.510  1.00 16.03 ? 109 LYS   A CE  1 
ATOM   779  N  NZ  . LYS   A 1 96  ? -34.767 -7.060  10.807  1.00 14.21 ? 109 LYS   A NZ  1 
ATOM   780  N  N   . GLU   A 1 97  ? -31.351 -5.953  4.803   1.00 11.22 ? 110 GLU   A N   1 
ATOM   781  C  CA  . GLU   A 1 97  ? -31.147 -6.951  3.763   1.00 12.67 ? 110 GLU   A CA  1 
ATOM   782  C  C   . GLU   A 1 97  ? -30.347 -6.343  2.612   1.00 11.44 ? 110 GLU   A C   1 
ATOM   783  O  O   . GLU   A 1 97  ? -30.171 -5.136  2.519   1.00 11.85 ? 110 GLU   A O   1 
ATOM   784  C  CB  . GLU   A 1 97  ? -32.473 -7.526  3.283   1.00 15.65 ? 110 GLU   A CB  1 
ATOM   785  C  CG  . GLU   A 1 97  ? -33.200 -8.381  4.331   1.00 18.85 ? 110 GLU   A CG  1 
ATOM   786  C  CD  . GLU   A 1 97  ? -32.413 -9.488  5.023   0.50 18.52 ? 110 GLU   A CD  1 
ATOM   787  O  OE1 . GLU   A 1 97  ? -32.748 -9.726  6.208   0.50 20.58 ? 110 GLU   A OE1 1 
ATOM   788  O  OE2 . GLU   A 1 97  ? -31.469 -10.084 4.441   0.50 19.04 ? 110 GLU   A OE2 1 
ATOM   789  N  N   . LYS   A 1 98  ? -29.828 -7.199  1.739   1.00 10.41 ? 111 LYS   A N   1 
ATOM   790  C  CA  . LYS   A 1 98  ? -29.116 -6.709  0.572   1.00 10.33 ? 111 LYS   A CA  1 
ATOM   791  C  C   . LYS   A 1 98  ? -30.174 -6.216  -0.404  1.00 10.44 ? 111 LYS   A C   1 
ATOM   792  O  O   . LYS   A 1 98  ? -31.186 -6.906  -0.603  1.00 11.04 ? 111 LYS   A O   1 
ATOM   793  C  CB  . LYS   A 1 98  ? -28.195 -7.814  0.005   1.00 10.81 ? 111 LYS   A CB  1 
ATOM   794  C  CG  . LYS   A 1 98  ? -26.848 -7.979  0.765   1.00 11.36 ? 111 LYS   A CG  1 
ATOM   795  C  CD  . LYS   A 1 98  ? -25.866 -9.074  0.349   0.50 10.70 ? 111 LYS   A CD  1 
ATOM   796  C  CE  . LYS   A 1 98  ? -24.585 -9.095  1.161   0.50 10.93 ? 111 LYS   A CE  1 
ATOM   797  N  NZ  . LYS   A 1 98  ? -23.526 -9.961  0.612   0.50 10.48 ? 111 LYS   A NZ  1 
ATOM   798  N  N   . ALA   A 1 99  ? -29.915 -5.063  -1.037  1.00 9.50  ? 112 ALA   A N   1 
ATOM   799  C  CA  . ALA   A 1 99  ? -30.767 -4.548  -2.098  1.00 9.46  ? 112 ALA   A CA  1 
ATOM   800  C  C   . ALA   A 1 99  ? -30.789 -5.503  -3.290  1.00 9.92  ? 112 ALA   A C   1 
ATOM   801  O  O   . ALA   A 1 99  ? -29.825 -6.234  -3.542  1.00 9.88  ? 112 ALA   A O   1 
ATOM   802  C  CB  . ALA   A 1 99  ? -30.290 -3.189  -2.566  1.00 9.97  ? 112 ALA   A CB  1 
ATOM   803  N  N   . SER   A 1 100 ? -31.870 -5.436  -4.056  1.00 9.83  ? 113 SER   A N   1 
ATOM   804  C  CA  . SER   A 1 100 ? -31.941 -6.124  -5.336  1.00 9.65  ? 113 SER   A CA  1 
ATOM   805  C  C   . SER   A 1 100 ? -31.220 -5.301  -6.391  1.00 8.98  ? 113 SER   A C   1 
ATOM   806  O  O   . SER   A 1 100 ? -31.339 -4.079  -6.433  1.00 8.75  ? 113 SER   A O   1 
ATOM   807  C  CB  . SER   A 1 100 ? -33.351 -6.383  -5.783  1.00 10.49 ? 113 SER   A CB  1 
ATOM   808  O  OG  . SER   A 1 100 ? -34.032 -7.249  -4.886  1.00 11.10 ? 113 SER   A OG  1 
ATOM   809  N  N   . LEU   A 1 101 ? -30.477 -5.994  -7.264  1.00 8.50  ? 114 LEU   A N   1 
ATOM   810  C  CA  . LEU   A 1 101 ? -29.861 -5.357  -8.411  1.00 8.77  ? 114 LEU   A CA  1 
ATOM   811  C  C   . LEU   A 1 101 ? -30.859 -5.301  -9.564  1.00 8.78  ? 114 LEU   A C   1 
ATOM   812  O  O   . LEU   A 1 101 ? -31.446 -6.322  -9.930  1.00 9.75  ? 114 LEU   A O   1 
ATOM   813  C  CB  . LEU   A 1 101 ? -28.582 -6.084  -8.829  1.00 9.16  ? 114 LEU   A CB  1 
ATOM   814  C  CG  . LEU   A 1 101 ? -27.506 -6.246  -7.757  1.00 9.60  ? 114 LEU   A CG  1 
ATOM   815  C  CD1 . LEU   A 1 101 ? -26.307 -6.985  -8.320  1.00 10.03 ? 114 LEU   A CD1 1 
ATOM   816  C  CD2 . LEU   A 1 101 ? -27.094 -4.897  -7.210  1.00 10.60 ? 114 LEU   A CD2 1 
ATOM   817  N  N   . THR   A 1 102 ? -31.075 -4.079  -10.088 1.00 8.04  ? 115 THR   A N   1 
ATOM   818  C  CA  . THR   A 1 102 ? -31.956 -3.802  -11.219 1.00 8.51  ? 115 THR   A CA  1 
ATOM   819  C  C   . THR   A 1 102 ? -31.273 -2.784  -12.120 1.00 8.95  ? 115 THR   A C   1 
ATOM   820  O  O   . THR   A 1 102 ? -30.228 -2.256  -11.778 1.00 8.82  ? 115 THR   A O   1 
ATOM   821  C  CB  . THR   A 1 102 ? -33.320 -3.259  -10.780 1.00 8.73  ? 115 THR   A CB  1 
ATOM   822  O  OG1 . THR   A 1 102 ? -33.147 -1.979  -10.171 1.00 8.14  ? 115 THR   A OG1 1 
ATOM   823  C  CG2 . THR   A 1 102 ? -34.028 -4.196  -9.829  1.00 9.00  ? 115 THR   A CG2 1 
ATOM   824  N  N   . LEU   A 1 103 ? -31.914 -2.412  -13.232 1.00 9.53  ? 116 LEU   A N   1 
ATOM   825  C  CA  . LEU   A 1 103 ? -31.363 -1.343  -14.057 1.00 9.90  ? 116 LEU   A CA  1 
ATOM   826  C  C   . LEU   A 1 103 ? -31.271 -0.058  -13.231 1.00 9.67  ? 116 LEU   A C   1 
ATOM   827  O  O   . LEU   A 1 103 ? -30.304 0.688   -13.365 1.00 10.97 ? 116 LEU   A O   1 
ATOM   828  C  CB  . LEU   A 1 103 ? -32.210 -1.126  -15.307 1.00 11.17 ? 116 LEU   A CB  1 
ATOM   829  C  CG  . LEU   A 1 103 ? -31.728 -0.026  -16.257 1.00 12.15 ? 116 LEU   A CG  1 
ATOM   830  C  CD1 . LEU   A 1 103 ? -30.305 -0.253  -16.739 1.00 12.85 ? 116 LEU   A CD1 1 
ATOM   831  C  CD2 . LEU   A 1 103 ? -32.666 0.039   -17.451 1.00 13.63 ? 116 LEU   A CD2 1 
ATOM   832  N  N   . ALA   A 1 104 ? -32.255 0.169   -12.353 1.00 8.90  ? 117 ALA   A N   1 
ATOM   833  C  CA  . ALA   A 1 104 ? -32.380 1.413   -11.600 1.00 8.48  ? 117 ALA   A CA  1 
ATOM   834  C  C   . ALA   A 1 104 ? -31.629 1.401   -10.261 1.00 7.90  ? 117 ALA   A C   1 
ATOM   835  O  O   . ALA   A 1 104 ? -31.511 2.450   -9.633  1.00 8.02  ? 117 ALA   A O   1 
ATOM   836  C  CB  . ALA   A 1 104 ? -33.842 1.720   -11.374 1.00 8.80  ? 117 ALA   A CB  1 
ATOM   837  N  N   . VAL   A 1 105 ? -31.114 0.246   -9.833  1.00 7.57  ? 118 VAL   A N   1 
ATOM   838  C  CA  . VAL   A 1 105 ? -30.451 0.124   -8.530  1.00 7.61  ? 118 VAL   A CA  1 
ATOM   839  C  C   . VAL   A 1 105 ? -29.189 -0.721  -8.670  1.00 7.62  ? 118 VAL   A C   1 
ATOM   840  O  O   . VAL   A 1 105 ? -29.254 -1.889  -9.053  1.00 8.33  ? 118 VAL   A O   1 
ATOM   841  C  CB  . VAL   A 1 105 ? -31.367 -0.462  -7.437  1.00 7.60  ? 118 VAL   A CB  1 
ATOM   842  C  CG1 . VAL   A 1 105 ? -30.602 -0.703  -6.130  1.00 7.68  ? 118 VAL   A CG1 1 
ATOM   843  C  CG2 . VAL   A 1 105 ? -32.556 0.445   -7.163  1.00 7.49  ? 118 VAL   A CG2 1 
ATOM   844  N  N   . GLY   A 1 106 ? -28.047 -0.117  -8.327  1.00 7.75  ? 119 GLY   A N   1 
ATOM   845  C  CA  . GLY   A 1 106 ? -26.765 -0.784  -8.408  1.00 7.43  ? 119 GLY   A CA  1 
ATOM   846  C  C   . GLY   A 1 106 ? -25.762 -0.095  -7.495  1.00 7.42  ? 119 GLY   A C   1 
ATOM   847  O  O   . GLY   A 1 106 ? -26.009 1.027   -7.029  1.00 7.61  ? 119 GLY   A O   1 
ATOM   848  N  N   . THR   A 1 107 ? -24.652 -0.785  -7.221  1.00 7.90  ? 120 THR   A N   1 
ATOM   849  C  CA  . THR   A 1 107 ? -23.629 -0.264  -6.322  1.00 8.80  ? 120 THR   A CA  1 
ATOM   850  C  C   . THR   A 1 107 ? -22.611 0.571   -7.091  1.00 9.78  ? 120 THR   A C   1 
ATOM   851  O  O   . THR   A 1 107 ? -22.436 0.421   -8.312  1.00 9.92  ? 120 THR   A O   1 
ATOM   852  C  CB  . THR   A 1 107 ? -22.923 -1.385  -5.548  1.00 9.58  ? 120 THR   A CB  1 
ATOM   853  O  OG1 . THR   A 1 107 ? -22.121 -2.143  -6.469  1.00 10.55 ? 120 THR   A OG1 1 
ATOM   854  C  CG2 . THR   A 1 107 ? -23.912 -2.266  -4.813  1.00 10.09 ? 120 THR   A CG2 1 
ATOM   855  N  N   . LEU   A 1 108 ? -21.916 1.428   -6.333  1.00 10.57 ? 121 LEU   A N   1 
ATOM   856  C  CA  . LEU   A 1 108 ? -20.776 2.190   -6.799  1.00 11.30 ? 121 LEU   A CA  1 
ATOM   857  C  C   . LEU   A 1 108 ? -19.591 1.858   -5.899  1.00 13.01 ? 121 LEU   A C   1 
ATOM   858  O  O   . LEU   A 1 108 ? -19.329 2.590   -4.957  1.00 12.78 ? 121 LEU   A O   1 
ATOM   859  C  CB  . LEU   A 1 108 ? -21.110 3.681   -6.746  1.00 11.92 ? 121 LEU   A CB  1 
ATOM   860  C  CG  . LEU   A 1 108 ? -20.079 4.620   -7.391  1.00 13.01 ? 121 LEU   A CG  1 
ATOM   861  C  CD1 . LEU   A 1 108 ? -20.113 4.503   -8.890  1.00 13.54 ? 121 LEU   A CD1 1 
ATOM   862  C  CD2 . LEU   A 1 108 ? -20.273 6.044   -6.981  1.00 12.82 ? 121 LEU   A CD2 1 
ATOM   863  N  N   . PRO   A 1 109 ? -18.890 0.723   -6.088  1.00 15.60 ? 122 PRO   A N   1 
ATOM   864  C  CA  . PRO   A 1 109 ? -17.735 0.386   -5.254  1.00 16.66 ? 122 PRO   A CA  1 
ATOM   865  C  C   . PRO   A 1 109 ? -16.557 1.285   -5.620  1.00 16.33 ? 122 PRO   A C   1 
ATOM   866  O  O   . PRO   A 1 109 ? -16.502 1.848   -6.714  1.00 16.24 ? 122 PRO   A O   1 
ATOM   867  C  CB  . PRO   A 1 109 ? -17.500 -1.100  -5.602  1.00 18.17 ? 122 PRO   A CB  1 
ATOM   868  C  CG  . PRO   A 1 109 ? -17.904 -1.158  -7.047  1.00 17.96 ? 122 PRO   A CG  1 
ATOM   869  C  CD  . PRO   A 1 109 ? -19.174 -0.309  -7.098  1.00 17.71 ? 122 PRO   A CD  1 
ATOM   870  N  N   . PHE   A 1 110 ? -15.648 1.464   -4.658  1.00 16.94 ? 123 PHE   A N   1 
ATOM   871  C  CA  . PHE   A 1 110 ? -14.453 2.249   -4.905  1.00 18.23 ? 123 PHE   A CA  1 
ATOM   872  C  C   . PHE   A 1 110 ? -13.491 1.446   -5.782  1.00 18.94 ? 123 PHE   A C   1 
ATOM   873  O  O   . PHE   A 1 110 ? -13.395 0.228   -5.645  1.00 20.24 ? 123 PHE   A O   1 
ATOM   874  C  CB  . PHE   A 1 110 ? -13.780 2.636   -3.587  1.00 17.79 ? 123 PHE   A CB  1 
ATOM   875  C  CG  . PHE   A 1 110 ? -14.586 3.648   -2.786  1.00 16.11 ? 123 PHE   A CG  1 
ATOM   876  C  CD1 . PHE   A 1 110 ? -15.304 3.264   -1.662  1.00 17.19 ? 123 PHE   A CD1 1 
ATOM   877  C  CD2 . PHE   A 1 110 ? -14.669 4.970   -3.210  1.00 15.64 ? 123 PHE   A CD2 1 
ATOM   878  C  CE1 . PHE   A 1 110 ? -16.069 4.194   -0.956  1.00 16.63 ? 123 PHE   A CE1 1 
ATOM   879  C  CE2 . PHE   A 1 110 ? -15.456 5.891   -2.516  1.00 16.02 ? 123 PHE   A CE2 1 
ATOM   880  C  CZ  . PHE   A 1 110 ? -16.150 5.502   -1.395  1.00 15.87 ? 123 PHE   A CZ  1 
ATOM   881  N  N   . PRO   A 1 111 ? -12.704 2.113   -6.651  1.00 21.95 ? 124 PRO   A N   1 
ATOM   882  C  CA  . PRO   A 1 111 ? -11.568 1.456   -7.304  1.00 22.94 ? 124 PRO   A CA  1 
ATOM   883  C  C   . PRO   A 1 111 ? -10.451 1.264   -6.279  1.00 23.59 ? 124 PRO   A C   1 
ATOM   884  O  O   . PRO   A 1 111 ? -10.487 1.842   -5.200  1.00 23.05 ? 124 PRO   A O   1 
ATOM   885  C  CB  . PRO   A 1 111 ? -11.199 2.445   -8.413  1.00 23.10 ? 124 PRO   A CB  1 
ATOM   886  C  CG  . PRO   A 1 111 ? -11.549 3.799   -7.816  1.00 23.60 ? 124 PRO   A CG  1 
ATOM   887  C  CD  . PRO   A 1 111 ? -12.826 3.534   -7.016  1.00 21.33 ? 124 PRO   A CD  1 
ATOM   888  N  N   A SER   A 1 112 ? -9.442  0.458   -6.624  0.50 23.19 ? 125 SER   A N   1 
ATOM   889  N  N   B SER   A 1 112 ? -9.450  0.456   -6.641  0.50 23.76 ? 125 SER   A N   1 
ATOM   890  C  CA  A SER   A 1 112 ? -8.353  0.181   -5.699  0.50 23.29 ? 125 SER   A CA  1 
ATOM   891  C  CA  B SER   A 1 112 ? -8.332  0.172   -5.756  0.50 24.29 ? 125 SER   A CA  1 
ATOM   892  C  C   A SER   A 1 112 ? -7.573  1.454   -5.362  0.50 23.24 ? 125 SER   A C   1 
ATOM   893  C  C   B SER   A 1 112 ? -7.602  1.458   -5.367  0.50 23.68 ? 125 SER   A C   1 
ATOM   894  O  O   A SER   A 1 112 ? -7.168  1.624   -4.211  0.50 25.74 ? 125 SER   A O   1 
ATOM   895  O  O   B SER   A 1 112 ? -7.274  1.644   -4.195  0.50 26.08 ? 125 SER   A O   1 
ATOM   896  C  CB  A SER   A 1 112 ? -7.449  -0.907  -6.234  0.50 23.90 ? 125 SER   A CB  1 
ATOM   897  C  CB  B SER   A 1 112 ? -7.396  -0.822  -6.402  0.50 25.56 ? 125 SER   A CB  1 
ATOM   898  O  OG  A SER   A 1 112 ? -7.071  -0.641  -7.577  0.50 23.80 ? 125 SER   A OG  1 
ATOM   899  O  OG  B SER   A 1 112 ? -8.131  -1.902  -6.962  0.50 26.99 ? 125 SER   A OG  1 
ATOM   900  N  N   . GLN   A 1 113 ? -7.364  2.333   -6.356  1.00 22.68 ? 126 GLN   A N   1 
ATOM   901  C  CA  . GLN   A 1 113 ? -6.581  3.555   -6.172  1.00 23.85 ? 126 GLN   A CA  1 
ATOM   902  C  C   . GLN   A 1 113 ? -7.305  4.518   -5.225  1.00 24.37 ? 126 GLN   A C   1 
ATOM   903  O  O   . GLN   A 1 113 ? -8.537  4.603   -5.254  1.00 22.29 ? 126 GLN   A O   1 
ATOM   904  C  CB  . GLN   A 1 113 ? -6.203  4.230   -7.500  1.00 23.72 ? 126 GLN   A CB  1 
ATOM   905  C  CG  . GLN   A 1 113 ? -7.360  4.632   -8.415  0.50 23.23 ? 126 GLN   A CG  1 
ATOM   906  C  CD  . GLN   A 1 113 ? -7.943  6.014   -8.190  0.10 22.29 ? 126 GLN   A CD  1 
ATOM   907  O  OE1 . GLN   A 1 113 ? -8.906  6.416   -8.856  0.50 22.05 ? 126 GLN   A OE1 1 
ATOM   908  N  NE2 . GLN   A 1 113 ? -7.376  6.770   -7.261  0.50 21.41 ? 126 GLN   A NE2 1 
ATOM   909  N  N   . LYS   A 1 114 ? -6.525  5.200   -4.365  1.00 22.77 ? 127 LYS   A N   1 
ATOM   910  C  CA  . LYS   A 1 114 ? -7.055  6.176   -3.418  1.00 23.38 ? 127 LYS   A CA  1 
ATOM   911  C  C   . LYS   A 1 114 ? -6.205  7.446   -3.450  1.00 22.30 ? 127 LYS   A C   1 
ATOM   912  O  O   . LYS   A 1 114 ? -5.951  8.048   -2.415  1.00 21.43 ? 127 LYS   A O   1 
ATOM   913  C  CB  . LYS   A 1 114 ? -7.115  5.624   -1.990  1.00 24.58 ? 127 LYS   A CB  1 
ATOM   914  C  CG  . LYS   A 1 114 ? -5.835  4.965   -1.469  1.00 24.66 ? 127 LYS   A CG  1 
ATOM   915  C  CD  . LYS   A 1 114 ? -5.989  4.321   -0.097  0.50 25.38 ? 127 LYS   A CD  1 
ATOM   916  C  CE  . LYS   A 1 114 ? -4.739  3.595   0.294   0.50 26.52 ? 127 LYS   A CE  1 
ATOM   917  N  NZ  . LYS   A 1 114 ? -4.857  2.965   1.610   0.50 26.18 ? 127 LYS   A NZ  1 
ATOM   918  N  N   . ASN   A 1 115 ? -5.842  7.872   -4.659  1.00 21.41 ? 128 ASN   A N   1 
ATOM   919  C  CA  . ASN   A 1 115 ? -4.973  9.014   -4.876  1.00 23.85 ? 128 ASN   A CA  1 
ATOM   920  C  C   . ASN   A 1 115 ? -5.659  10.305  -4.419  1.00 20.71 ? 128 ASN   A C   1 
ATOM   921  O  O   . ASN   A 1 115 ? -6.860  10.490  -4.614  1.00 20.12 ? 128 ASN   A O   1 
ATOM   922  C  CB  . ASN   A 1 115 ? -4.565  9.108   -6.343  1.00 26.91 ? 128 ASN   A CB  1 
ATOM   923  C  CG  . ASN   A 1 115 ? -3.887  7.840   -6.831  1.00 31.01 ? 128 ASN   A CG  1 
ATOM   924  O  OD1 . ASN   A 1 115 ? -4.294  7.248   -7.840  1.00 37.34 ? 128 ASN   A OD1 1 
ATOM   925  N  ND2 . ASN   A 1 115 ? -2.864  7.398   -6.121  1.00 30.68 ? 128 ASN   A ND2 1 
ATOM   926  N  N   . PHE   A 1 116 ? -4.856  11.229  -3.891  1.00 19.60 ? 129 PHE   A N   1 
ATOM   927  C  CA  . PHE   A 1 116 ? -5.342  12.537  -3.466  1.00 17.70 ? 129 PHE   A CA  1 
ATOM   928  C  C   . PHE   A 1 116 ? -5.705  13.351  -4.706  1.00 17.43 ? 129 PHE   A C   1 
ATOM   929  O  O   . PHE   A 1 116 ? -4.924  13.428  -5.664  1.00 17.17 ? 129 PHE   A O   1 
ATOM   930  C  CB  . PHE   A 1 116 ? -4.240  13.145  -2.592  1.00 17.77 ? 129 PHE   A CB  1 
ATOM   931  C  CG  . PHE   A 1 116 ? -4.569  14.465  -1.906  1.00 16.67 ? 129 PHE   A CG  1 
ATOM   932  C  CD1 . PHE   A 1 116 ? -4.927  14.498  -0.571  1.00 16.14 ? 129 PHE   A CD1 1 
ATOM   933  C  CD2 . PHE   A 1 116 ? -4.495  15.669  -2.603  1.00 17.16 ? 129 PHE   A CD2 1 
ATOM   934  C  CE1 . PHE   A 1 116 ? -5.222  15.696  0.059   1.00 17.01 ? 129 PHE   A CE1 1 
ATOM   935  C  CE2 . PHE   A 1 116 ? -4.800  16.873  -1.972  1.00 16.98 ? 129 PHE   A CE2 1 
ATOM   936  C  CZ  . PHE   A 1 116 ? -5.147  16.884  -0.637  1.00 15.79 ? 129 PHE   A CZ  1 
ATOM   937  N  N   . VAL   A 1 117 ? -6.913  13.926  -4.710  1.00 15.18 ? 130 VAL   A N   1 
ATOM   938  C  CA  . VAL   A 1 117 ? -7.413  14.691  -5.834  1.00 16.03 ? 130 VAL   A CA  1 
ATOM   939  C  C   . VAL   A 1 117 ? -7.083  16.165  -5.619  1.00 16.95 ? 130 VAL   A C   1 
ATOM   940  O  O   . VAL   A 1 117 ? -7.636  16.836  -4.732  1.00 16.34 ? 130 VAL   A O   1 
ATOM   941  C  CB  . VAL   A 1 117 ? -8.924  14.507  -6.061  1.00 17.08 ? 130 VAL   A CB  1 
ATOM   942  C  CG1 . VAL   A 1 117 ? -9.375  15.248  -7.316  1.00 16.98 ? 130 VAL   A CG1 1 
ATOM   943  C  CG2 . VAL   A 1 117 ? -9.297  13.031  -6.101  1.00 16.73 ? 130 VAL   A CG2 1 
ATOM   944  N  N   . PRO   A 1 118 ? -6.229  16.747  -6.487  1.00 17.49 ? 131 PRO   A N   1 
ATOM   945  C  CA  . PRO   A 1 118 ? -5.852  18.143  -6.361  1.00 17.27 ? 131 PRO   A CA  1 
ATOM   946  C  C   . PRO   A 1 118 ? -6.921  19.063  -6.921  1.00 16.97 ? 131 PRO   A C   1 
ATOM   947  O  O   . PRO   A 1 118 ? -7.804  18.640  -7.663  1.00 15.93 ? 131 PRO   A O   1 
ATOM   948  C  CB  . PRO   A 1 118 ? -4.553  18.196  -7.205  1.00 18.56 ? 131 PRO   A CB  1 
ATOM   949  C  CG  . PRO   A 1 118 ? -4.847  17.254  -8.346  1.00 19.53 ? 131 PRO   A CG  1 
ATOM   950  C  CD  . PRO   A 1 118 ? -5.618  16.115  -7.684  1.00 17.41 ? 131 PRO   A CD  1 
ATOM   951  N  N   . PRO   A 1 119 ? -6.849  20.371  -6.602  1.00 16.11 ? 132 PRO   A N   1 
ATOM   952  C  CA  . PRO   A 1 119 ? -7.715  21.358  -7.229  1.00 16.41 ? 132 PRO   A CA  1 
ATOM   953  C  C   . PRO   A 1 119 ? -7.572  21.403  -8.750  1.00 16.68 ? 132 PRO   A C   1 
ATOM   954  O  O   . PRO   A 1 119 ? -6.499  21.092  -9.270  1.00 17.74 ? 132 PRO   A O   1 
ATOM   955  C  CB  . PRO   A 1 119 ? -7.259  22.686  -6.604  1.00 16.85 ? 132 PRO   A CB  1 
ATOM   956  C  CG  . PRO   A 1 119 ? -6.569  22.290  -5.315  1.00 16.86 ? 132 PRO   A CG  1 
ATOM   957  C  CD  . PRO   A 1 119 ? -5.952  20.936  -5.577  1.00 17.40 ? 132 PRO   A CD  1 
ATOM   958  N  N   . GLY   A 1 120 ? -8.661  21.781  -9.420  1.00 16.86 ? 133 GLY   A N   1 
ATOM   959  C  CA  . GLY   A 1 120 ? -8.626  22.243  -10.801 1.00 16.80 ? 133 GLY   A CA  1 
ATOM   960  C  C   . GLY   A 1 120 ? -9.706  21.635  -11.698 1.00 17.81 ? 133 GLY   A C   1 
ATOM   961  O  O   . GLY   A 1 120 ? -10.183 22.296  -12.621 1.00 19.29 ? 133 GLY   A O   1 
ATOM   962  N  N   . ARG   A 1 121 ? -10.070 20.371  -11.469 1.00 17.08 ? 134 ARG   A N   1 
ATOM   963  C  CA  . ARG   A 1 121 ? -10.970 19.674  -12.382 1.00 16.85 ? 134 ARG   A CA  1 
ATOM   964  C  C   . ARG   A 1 121 ? -12.440 19.996  -12.088 1.00 18.89 ? 134 ARG   A C   1 
ATOM   965  O  O   . ARG   A 1 121 ? -12.763 20.657  -11.095 1.00 17.27 ? 134 ARG   A O   1 
ATOM   966  C  CB  . ARG   A 1 121 ? -10.670 18.175  -12.320 1.00 16.92 ? 134 ARG   A CB  1 
ATOM   967  C  CG  . ARG   A 1 121 ? -11.095 17.438  -11.057 1.00 17.20 ? 134 ARG   A CG  1 
ATOM   968  C  CD  . ARG   A 1 121 ? -11.259 15.937  -11.259 0.50 15.11 ? 134 ARG   A CD  1 
ATOM   969  N  NE  . ARG   A 1 121 ? -12.312 15.695  -12.253 0.50 14.21 ? 134 ARG   A NE  1 
ATOM   970  C  CZ  . ARG   A 1 121 ? -12.169 14.956  -13.339 0.50 13.17 ? 134 ARG   A CZ  1 
ATOM   971  N  NH1 . ARG   A 1 121 ? -11.129 14.152  -13.458 0.50 13.22 ? 134 ARG   A NH1 1 
ATOM   972  N  NH2 . ARG   A 1 121 ? -13.083 15.003  -14.281 0.50 12.94 ? 134 ARG   A NH2 1 
ATOM   973  N  N   . MET   A 1 122 ? -13.318 19.519  -12.992 1.00 16.27 ? 135 MET   A N   1 
ATOM   974  C  CA  . MET   A 1 122 ? -14.760 19.558  -12.818 1.00 15.91 ? 135 MET   A CA  1 
ATOM   975  C  C   . MET   A 1 122 ? -15.238 18.185  -12.343 1.00 14.42 ? 135 MET   A C   1 
ATOM   976  O  O   . MET   A 1 122 ? -14.720 17.157  -12.772 1.00 13.40 ? 135 MET   A O   1 
ATOM   977  C  CB  . MET   A 1 122 ? -15.483 19.910  -14.119 1.00 17.35 ? 135 MET   A CB  1 
ATOM   978  C  CG  . MET   A 1 122 ? -15.051 21.221  -14.751 1.00 19.68 ? 135 MET   A CG  1 
ATOM   979  S  SD  . MET   A 1 122 ? -15.401 22.682  -13.755 1.00 22.46 ? 135 MET   A SD  1 
ATOM   980  C  CE  . MET   A 1 122 ? -17.182 22.859  -13.708 1.00 21.05 ? 135 MET   A CE  1 
ATOM   981  N  N   . CYS   A 1 123 ? -16.217 18.209  -11.434 1.00 12.50 ? 136 CYS   A N   1 
ATOM   982  C  CA  . CYS   A 1 123 ? -16.854 17.017  -10.882 1.00 12.09 ? 136 CYS   A CA  1 
ATOM   983  C  C   . CYS   A 1 123 ? -18.360 17.266  -10.874 1.00 11.96 ? 136 CYS   A C   1 
ATOM   984  O  O   . CYS   A 1 123 ? -18.794 18.391  -11.088 1.00 11.92 ? 136 CYS   A O   1 
ATOM   985  C  CB  . CYS   A 1 123 ? -16.317 16.672  -9.490  1.00 11.85 ? 136 CYS   A CB  1 
ATOM   986  S  SG  . CYS   A 1 123 ? -14.509 16.492  -9.385  1.00 11.88 ? 136 CYS   A SG  1 
ATOM   987  N  N   . ARG   A 1 124 ? -19.170 16.228  -10.610 1.00 10.97 ? 137 ARG   A N   1 
ATOM   988  C  CA  . ARG   A 1 124 ? -20.619 16.365  -10.629 1.00 11.45 ? 137 ARG   A CA  1 
ATOM   989  C  C   . ARG   A 1 124 ? -21.203 15.852  -9.313  1.00 9.83  ? 137 ARG   A C   1 
ATOM   990  O  O   . ARG   A 1 124 ? -20.736 14.852  -8.792  1.00 10.66 ? 137 ARG   A O   1 
ATOM   991  C  CB  . ARG   A 1 124 ? -21.251 15.578  -11.783 1.00 13.28 ? 137 ARG   A CB  1 
ATOM   992  C  CG  . ARG   A 1 124 ? -20.727 16.013  -13.153 1.00 15.66 ? 137 ARG   A CG  1 
ATOM   993  C  CD  . ARG   A 1 124 ? -21.235 15.121  -14.284 1.00 17.18 ? 137 ARG   A CD  1 
ATOM   994  N  NE  . ARG   A 1 124 ? -20.585 15.423  -15.571 0.50 16.42 ? 137 ARG   A NE  1 
ATOM   995  C  CZ  . ARG   A 1 124 ? -21.022 16.274  -16.483 0.50 16.83 ? 137 ARG   A CZ  1 
ATOM   996  N  NH1 . ARG   A 1 124 ? -22.110 17.001  -16.281 0.50 15.65 ? 137 ARG   A NH1 1 
ATOM   997  N  NH2 . ARG   A 1 124 ? -20.346 16.414  -17.611 0.50 18.03 ? 137 ARG   A NH2 1 
ATOM   998  N  N   . VAL   A 1 125 ? -22.211 16.562  -8.792  1.00 8.65  ? 138 VAL   A N   1 
ATOM   999  C  CA  . VAL   A 1 125 ? -22.930 16.175  -7.579  1.00 8.47  ? 138 VAL   A CA  1 
ATOM   1000 C  C   . VAL   A 1 125 ? -24.430 16.130  -7.880  1.00 7.97  ? 138 VAL   A C   1 
ATOM   1001 O  O   . VAL   A 1 125 ? -24.925 16.920  -8.687  1.00 8.09  ? 138 VAL   A O   1 
ATOM   1002 C  CB  . VAL   A 1 125 ? -22.614 17.141  -6.417  1.00 9.18  ? 138 VAL   A CB  1 
ATOM   1003 C  CG1 . VAL   A 1 125 ? -22.954 18.595  -6.752  1.00 10.26 ? 138 VAL   A CG1 1 
ATOM   1004 C  CG2 . VAL   A 1 125 ? -23.317 16.691  -5.136  1.00 9.17  ? 138 VAL   A CG2 1 
ATOM   1005 N  N   . ALA   A 1 126 ? -25.151 15.181  -7.251  1.00 8.18  ? 139 ALA   A N   1 
ATOM   1006 C  CA  . ALA   A 1 126 ? -26.586 15.022  -7.447  1.00 7.73  ? 139 ALA   A CA  1 
ATOM   1007 C  C   . ALA   A 1 126 ? -27.321 15.022  -6.103  1.00 7.84  ? 139 ALA   A C   1 
ATOM   1008 O  O   . ALA   A 1 126 ? -26.756 14.640  -5.077  1.00 8.46  ? 139 ALA   A O   1 
ATOM   1009 C  CB  . ALA   A 1 126 ? -26.862 13.737  -8.226  1.00 8.11  ? 139 ALA   A CB  1 
ATOM   1010 N  N   . GLY   A 1 127 ? -28.581 15.423  -6.122  1.00 7.99  ? 140 GLY   A N   1 
ATOM   1011 C  CA  . GLY   A 1 127 ? -29.399 15.418  -4.913  1.00 8.43  ? 140 GLY   A CA  1 
ATOM   1012 C  C   . GLY   A 1 127 ? -30.822 15.913  -5.149  1.00 8.47  ? 140 GLY   A C   1 
ATOM   1013 O  O   . GLY   A 1 127 ? -31.142 16.461  -6.212  1.00 8.37  ? 140 GLY   A O   1 
ATOM   1014 N  N   . TRP   A 1 128 ? -31.645 15.744  -4.108  1.00 8.22  ? 141 TRP   A N   1 
ATOM   1015 C  CA  . TRP   A 1 128 ? -33.036 16.178  -4.077  1.00 8.59  ? 141 TRP   A CA  1 
ATOM   1016 C  C   . TRP   A 1 128 ? -33.196 17.436  -3.220  1.00 9.43  ? 141 TRP   A C   1 
ATOM   1017 O  O   . TRP   A 1 128 ? -34.300 17.753  -2.781  1.00 10.10 ? 141 TRP   A O   1 
ATOM   1018 C  CB  . TRP   A 1 128 ? -33.909 15.037  -3.528  1.00 8.26  ? 141 TRP   A CB  1 
ATOM   1019 C  CG  . TRP   A 1 128 ? -34.068 13.838  -4.435  1.00 7.78  ? 141 TRP   A CG  1 
ATOM   1020 C  CD1 . TRP   A 1 128 ? -35.052 13.693  -5.372  1.00 8.33  ? 141 TRP   A CD1 1 
ATOM   1021 C  CD2 . TRP   A 1 128 ? -33.306 12.610  -4.472  1.00 7.59  ? 141 TRP   A CD2 1 
ATOM   1022 N  NE1 . TRP   A 1 128 ? -34.965 12.481  -5.990  1.00 8.08  ? 141 TRP   A NE1 1 
ATOM   1023 C  CE2 . TRP   A 1 128 ? -33.897 11.793  -5.470  1.00 7.83  ? 141 TRP   A CE2 1 
ATOM   1024 C  CE3 . TRP   A 1 128 ? -32.203 12.119  -3.763  1.00 7.50  ? 141 TRP   A CE3 1 
ATOM   1025 C  CZ2 . TRP   A 1 128 ? -33.410 10.519  -5.772  1.00 7.84  ? 141 TRP   A CZ2 1 
ATOM   1026 C  CZ3 . TRP   A 1 128 ? -31.729 10.856  -4.057  1.00 7.39  ? 141 TRP   A CZ3 1 
ATOM   1027 C  CH2 . TRP   A 1 128 ? -32.306 10.084  -5.072  1.00 7.80  ? 141 TRP   A CH2 1 
ATOM   1028 N  N   . GLY   A 1 129 ? -32.090 18.134  -2.946  1.00 9.42  ? 142 GLY   A N   1 
ATOM   1029 C  CA  . GLY   A 1 129 ? -32.146 19.286  -2.053  1.00 9.28  ? 142 GLY   A CA  1 
ATOM   1030 C  C   . GLY   A 1 129 ? -32.773 20.532  -2.683  1.00 10.01 ? 142 GLY   A C   1 
ATOM   1031 O  O   . GLY   A 1 129 ? -33.259 20.541  -3.813  1.00 10.01 ? 142 GLY   A O   1 
ATOM   1032 N  N   . ARG   A 1 130 ? -32.779 21.606  -1.888  1.00 10.64 ? 143 ARG   A N   1 
ATOM   1033 C  CA  . ARG   A 1 130 ? -33.337 22.880  -2.297  1.00 11.69 ? 143 ARG   A CA  1 
ATOM   1034 C  C   . ARG   A 1 130 ? -32.607 23.422  -3.518  1.00 11.49 ? 143 ARG   A C   1 
ATOM   1035 O  O   . ARG   A 1 130 ? -31.396 23.227  -3.661  1.00 10.90 ? 143 ARG   A O   1 
ATOM   1036 C  CB  . ARG   A 1 130 ? -33.235 23.904  -1.168  1.00 12.43 ? 143 ARG   A CB  1 
ATOM   1037 C  CG  . ARG   A 1 130 ? -33.919 23.508  0.132   1.00 14.58 ? 143 ARG   A CG  1 
ATOM   1038 C  CD  . ARG   A 1 130 ? -33.904 24.643  1.144   1.00 15.86 ? 143 ARG   A CD  1 
ATOM   1039 N  NE  . ARG   A 1 130 ? -34.591 24.273  2.387   1.00 19.32 ? 143 ARG   A NE  1 
ATOM   1040 C  CZ  . ARG   A 1 130 ? -35.878 24.530  2.649   0.50 20.96 ? 143 ARG   A CZ  1 
ATOM   1041 N  NH1 . ARG   A 1 130 ? -36.681 25.003  1.712   0.50 20.76 ? 143 ARG   A NH1 1 
ATOM   1042 N  NH2 . ARG   A 1 130 ? -36.383 24.257  3.837   0.50 21.93 ? 143 ARG   A NH2 1 
ATOM   1043 N  N   . THR   A 1 131 ? -33.377 24.113  -4.373  1.00 11.91 ? 144 THR   A N   1 
ATOM   1044 C  CA  . THR   A 1 131 ? -32.893 24.679  -5.625  1.00 12.87 ? 144 THR   A CA  1 
ATOM   1045 C  C   . THR   A 1 131 ? -32.666 26.180  -5.473  1.00 13.08 ? 144 THR   A C   1 
ATOM   1046 O  O   . THR   A 1 131 ? -32.392 26.870  -6.444  1.00 14.96 ? 144 THR   A O   1 
ATOM   1047 C  CB  . THR   A 1 131 ? -33.867 24.373  -6.767  1.00 14.08 ? 144 THR   A CB  1 
ATOM   1048 O  OG1 . THR   A 1 131 ? -35.152 24.944  -6.504  1.00 14.95 ? 144 THR   A OG1 1 
ATOM   1049 C  CG2 . THR   A 1 131 ? -34.014 22.880  -6.965  1.00 14.52 ? 144 THR   A CG2 1 
ATOM   1050 N  N   . GLY   A 1 132 ? -32.742 26.669  -4.236  1.00 14.65 ? 145 GLY   A N   1 
ATOM   1051 C  CA  . GLY   A 1 132 ? -32.418 28.052  -3.904  1.00 14.95 ? 145 GLY   A CA  1 
ATOM   1052 C  C   . GLY   A 1 132 ? -32.708 28.296  -2.426  1.00 15.25 ? 145 GLY   A C   1 
ATOM   1053 O  O   . GLY   A 1 132 ? -33.266 27.423  -1.768  1.00 15.36 ? 145 GLY   A O   1 
ATOM   1054 N  N   . VAL   A 1 133 ? -32.297 29.459  -1.902  1.00 14.42 ? 146 VAL   A N   1 
ATOM   1055 C  CA  . VAL   A 1 133 ? -32.452 29.760  -0.484  1.00 16.10 ? 146 VAL   A CA  1 
ATOM   1056 C  C   . VAL   A 1 133 ? -33.927 29.684  -0.085  1.00 18.01 ? 146 VAL   A C   1 
ATOM   1057 O  O   . VAL   A 1 133 ? -34.258 29.167  0.974   1.00 19.63 ? 146 VAL   A O   1 
ATOM   1058 C  CB  . VAL   A 1 133 ? -31.833 31.125  -0.123  1.00 17.00 ? 146 VAL   A CB  1 
ATOM   1059 C  CG1 . VAL   A 1 133 ? -32.219 31.582  1.284   1.00 16.94 ? 146 VAL   A CG1 1 
ATOM   1060 C  CG2 . VAL   A 1 133 ? -30.304 31.066  -0.227  1.00 17.32 ? 146 VAL   A CG2 1 
ATOM   1061 N  N   . LEU   A 1 134 ? -34.818 30.244  -0.893  1.00 20.00 ? 147 LEU   A N   1 
ATOM   1062 C  CA  . LEU   A 1 134 ? -36.206 30.292  -0.457  1.00 23.01 ? 147 LEU   A CA  1 
ATOM   1063 C  C   . LEU   A 1 134 ? -37.032 29.179  -1.103  1.00 24.58 ? 147 LEU   A C   1 
ATOM   1064 O  O   . LEU   A 1 134 ? -38.257 29.222  -1.029  1.00 26.62 ? 147 LEU   A O   1 
ATOM   1065 C  CB  . LEU   A 1 134 ? -36.753 31.687  -0.767  1.00 27.93 ? 147 LEU   A CB  1 
ATOM   1066 C  CG  . LEU   A 1 134 ? -36.073 32.839  -0.017  1.00 30.34 ? 147 LEU   A CG  1 
ATOM   1067 C  CD1 . LEU   A 1 134 ? -36.654 34.198  -0.418  1.00 31.86 ? 147 LEU   A CD1 1 
ATOM   1068 C  CD2 . LEU   A 1 134 ? -36.175 32.629  1.493   1.00 31.66 ? 147 LEU   A CD2 1 
ATOM   1069 N  N   . LYS   A 1 135 ? -36.374 28.169  -1.695  1.00 21.18 ? 148 LYS   A N   1 
ATOM   1070 C  CA  . LYS   A 1 135 ? -37.074 27.171  -2.493  1.00 22.29 ? 148 LYS   A CA  1 
ATOM   1071 C  C   . LYS   A 1 135 ? -37.091 25.839  -1.743  1.00 20.28 ? 148 LYS   A C   1 
ATOM   1072 O  O   . LYS   A 1 135 ? -36.128 25.498  -1.062  1.00 19.58 ? 148 LYS   A O   1 
ATOM   1073 C  CB  . LYS   A 1 135 ? -36.443 27.085  -3.888  1.00 24.36 ? 148 LYS   A CB  1 
ATOM   1074 C  CG  . LYS   A 1 135 ? -36.358 28.421  -4.632  1.00 28.99 ? 148 LYS   A CG  1 
ATOM   1075 C  CD  . LYS   A 1 135 ? -36.529 28.280  -6.143  1.00 32.02 ? 148 LYS   A CD  1 
ATOM   1076 C  CE  . LYS   A 1 135 ? -36.002 29.407  -6.979  0.50 31.26 ? 148 LYS   A CE  1 
ATOM   1077 N  NZ  . LYS   A 1 135 ? -36.831 30.605  -6.857  0.50 32.25 ? 148 LYS   A NZ  1 
ATOM   1078 N  N   . PRO   A 1 136 ? -38.261 25.204  -1.623  1.00 22.68 ? 150 PRO   A N   1 
ATOM   1079 C  CA  . PRO   A 1 136 ? -38.260 23.799  -1.244  1.00 20.22 ? 150 PRO   A CA  1 
ATOM   1080 C  C   . PRO   A 1 136 ? -37.352 22.794  -1.975  1.00 16.30 ? 150 PRO   A C   1 
ATOM   1081 O  O   . PRO   A 1 136 ? -36.850 23.033  -3.076  1.00 16.29 ? 150 PRO   A O   1 
ATOM   1082 C  CB  . PRO   A 1 136 ? -39.756 23.499  -1.475  1.00 22.53 ? 150 PRO   A CB  1 
ATOM   1083 C  CG  . PRO   A 1 136 ? -39.986 24.091  -2.823  1.00 23.38 ? 150 PRO   A CG  1 
ATOM   1084 C  CD  . PRO   A 1 136 ? -38.842 25.132  -2.955  1.00 23.54 ? 150 PRO   A CD  1 
ATOM   1085 N  N   . GLY   A 1 137 ? -37.161 21.652  -1.317  1.00 15.86 ? 151 GLY   A N   1 
ATOM   1086 C  CA  . GLY   A 1 137 ? -36.483 20.509  -1.911  1.00 14.54 ? 151 GLY   A CA  1 
ATOM   1087 C  C   . GLY   A 1 137 ? -37.123 20.099  -3.233  1.00 15.05 ? 151 GLY   A C   1 
ATOM   1088 O  O   . GLY   A 1 137 ? -38.341 20.192  -3.395  1.00 18.26 ? 151 GLY   A O   1 
ATOM   1089 N  N   . SER   A 1 138 ? -36.291 19.662  -4.190  1.00 13.66 ? 152 SER   A N   1 
ATOM   1090 C  CA  . SER   A 1 138 ? -36.712 19.214  -5.499  1.00 12.88 ? 152 SER   A CA  1 
ATOM   1091 C  C   . SER   A 1 138 ? -37.442 17.873  -5.386  1.00 13.24 ? 152 SER   A C   1 
ATOM   1092 O  O   . SER   A 1 138 ? -36.985 16.963  -4.701  1.00 13.27 ? 152 SER   A O   1 
ATOM   1093 C  CB  . SER   A 1 138 ? -35.523 19.116  -6.433  1.00 12.61 ? 152 SER   A CB  1 
ATOM   1094 O  OG  . SER   A 1 138 ? -35.886 18.705  -7.740  1.00 11.82 ? 152 SER   A OG  1 
ATOM   1095 N  N   . ASP   A 1 139 ? -38.557 17.734  -6.109  1.00 12.27 ? 153 ASP   A N   1 
ATOM   1096 C  CA  . ASP   A 1 139 ? -39.222 16.441  -6.182  1.00 12.32 ? 153 ASP   A CA  1 
ATOM   1097 C  C   . ASP   A 1 139 ? -38.434 15.455  -7.064  1.00 11.83 ? 153 ASP   A C   1 
ATOM   1098 O  O   . ASP   A 1 139 ? -38.511 14.242  -6.817  1.00 11.56 ? 153 ASP   A O   1 
ATOM   1099 C  CB  . ASP   A 1 139 ? -40.629 16.575  -6.743  1.00 14.31 ? 153 ASP   A CB  1 
ATOM   1100 C  CG  . ASP   A 1 139 ? -41.672 17.281  -5.882  1.00 15.48 ? 153 ASP   A CG  1 
ATOM   1101 O  OD1 . ASP   A 1 139 ? -41.459 17.462  -4.644  1.00 17.09 ? 153 ASP   A OD1 1 
ATOM   1102 O  OD2 . ASP   A 1 139 ? -42.732 17.605  -6.470  1.00 17.41 ? 153 ASP   A OD2 1 
ATOM   1103 N  N   . THR   A 1 140 ? -37.668 15.968  -8.044  1.00 10.80 ? 154 THR   A N   1 
ATOM   1104 C  CA  . THR   A 1 140 ? -36.862 15.148  -8.955  1.00 11.42 ? 154 THR   A CA  1 
ATOM   1105 C  C   . THR   A 1 140 ? -35.380 15.226  -8.592  1.00 10.80 ? 154 THR   A C   1 
ATOM   1106 O  O   . THR   A 1 140 ? -34.913 16.274  -8.148  1.00 10.63 ? 154 THR   A O   1 
ATOM   1107 C  CB  . THR   A 1 140 ? -37.041 15.568  -10.411 1.00 13.33 ? 154 THR   A CB  1 
ATOM   1108 O  OG1 . THR   A 1 140 ? -36.723 16.959  -10.516 1.00 13.03 ? 154 THR   A OG1 1 
ATOM   1109 C  CG2 . THR   A 1 140 ? -38.452 15.279  -10.908 1.00 14.30 ? 154 THR   A CG2 1 
ATOM   1110 N  N   . LEU   A 1 141 ? -34.635 14.148  -8.855  1.00 9.51  ? 155 LEU   A N   1 
ATOM   1111 C  CA  . LEU   A 1 141 ? -33.188 14.183  -8.711  1.00 9.35  ? 155 LEU   A CA  1 
ATOM   1112 C  C   . LEU   A 1 141 ? -32.591 15.206  -9.680  1.00 9.58  ? 155 LEU   A C   1 
ATOM   1113 O  O   . LEU   A 1 141 ? -32.874 15.200  -10.894 1.00 9.58  ? 155 LEU   A O   1 
ATOM   1114 C  CB  . LEU   A 1 141 ? -32.600 12.788  -8.936  1.00 9.02  ? 155 LEU   A CB  1 
ATOM   1115 C  CG  . LEU   A 1 141 ? -31.086 12.650  -8.768  1.00 8.88  ? 155 LEU   A CG  1 
ATOM   1116 C  CD1 . LEU   A 1 141 ? -30.643 12.847  -7.330  1.00 9.20  ? 155 LEU   A CD1 1 
ATOM   1117 C  CD2 . LEU   A 1 141 ? -30.575 11.314  -9.263  1.00 9.13  ? 155 LEU   A CD2 1 
ATOM   1118 N  N   . GLN   A 1 142 ? -31.731 16.085  -9.131  1.00 9.43  ? 156 GLN   A N   1 
ATOM   1119 C  CA  . GLN   A 1 142 ? -31.043 17.135  -9.873  1.00 9.39  ? 156 GLN   A CA  1 
ATOM   1120 C  C   . GLN   A 1 142 ? -29.529 16.891  -9.800  1.00 9.59  ? 156 GLN   A C   1 
ATOM   1121 O  O   . GLN   A 1 142 ? -29.047 16.195  -8.894  1.00 8.48  ? 156 GLN   A O   1 
ATOM   1122 C  CB  . GLN   A 1 142 ? -31.347 18.520  -9.285  1.00 9.89  ? 156 GLN   A CB  1 
ATOM   1123 C  CG  . GLN   A 1 142 ? -32.819 18.923  -9.237  1.00 10.60 ? 156 GLN   A CG  1 
ATOM   1124 C  CD  . GLN   A 1 142 ? -33.282 19.535  -10.537 1.00 12.44 ? 156 GLN   A CD  1 
ATOM   1125 O  OE1 . GLN   A 1 142 ? -32.656 20.467  -11.069 1.00 13.68 ? 156 GLN   A OE1 1 
ATOM   1126 N  NE2 . GLN   A 1 142 ? -34.371 18.993  -11.063 1.00 12.89 ? 156 GLN   A NE2 1 
ATOM   1127 N  N   . GLU   A 1 143 ? -28.773 17.481  -10.746 1.00 9.29  ? 157 GLU   A N   1 
ATOM   1128 C  CA  . GLU   A 1 143 ? -27.324 17.366  -10.734 1.00 9.56  ? 157 GLU   A CA  1 
ATOM   1129 C  C   . GLU   A 1 143 ? -26.680 18.613  -11.342 1.00 9.73  ? 157 GLU   A C   1 
ATOM   1130 O  O   . GLU   A 1 143 ? -27.323 19.347  -12.086 1.00 9.54  ? 157 GLU   A O   1 
ATOM   1131 C  CB  . GLU   A 1 143 ? -26.833 16.107  -11.435 1.00 10.39 ? 157 GLU   A CB  1 
ATOM   1132 C  CG  . GLU   A 1 143 ? -27.263 16.012  -12.900 1.00 10.95 ? 157 GLU   A CG  1 
ATOM   1133 C  CD  . GLU   A 1 143 ? -26.722 14.730  -13.499 1.00 12.59 ? 157 GLU   A CD  1 
ATOM   1134 O  OE1 . GLU   A 1 143 ? -25.670 14.774  -14.203 1.00 13.77 ? 157 GLU   A OE1 1 
ATOM   1135 O  OE2 . GLU   A 1 143 ? -27.330 13.659  -13.206 1.00 11.98 ? 157 GLU   A OE2 1 
ATOM   1136 N  N   . VAL   A 1 144 ? -25.432 18.861  -10.942 1.00 9.49  ? 158 VAL   A N   1 
ATOM   1137 C  CA  . VAL   A 1 144 ? -24.698 20.049  -11.367 1.00 9.74  ? 158 VAL   A CA  1 
ATOM   1138 C  C   . VAL   A 1 144 ? -23.202 19.728  -11.439 1.00 10.32 ? 158 VAL   A C   1 
ATOM   1139 O  O   . VAL   A 1 144 ? -22.693 18.942  -10.623 1.00 9.80  ? 158 VAL   A O   1 
ATOM   1140 C  CB  . VAL   A 1 144 ? -25.005 21.224  -10.417 1.00 10.68 ? 158 VAL   A CB  1 
ATOM   1141 C  CG1 . VAL   A 1 144 ? -24.418 21.014  -9.013  1.00 10.31 ? 158 VAL   A CG1 1 
ATOM   1142 C  CG2 . VAL   A 1 144 ? -24.543 22.551  -11.020 1.00 11.09 ? 158 VAL   A CG2 1 
ATOM   1143 N  N   . LYS   A 1 145 ? -22.515 20.331  -12.441 1.00 10.57 ? 159 LYS   A N   1 
ATOM   1144 C  CA  . LYS   A 1 145 ? -21.078 20.221  -12.610 1.00 11.44 ? 159 LYS   A CA  1 
ATOM   1145 C  C   . LYS   A 1 145 ? -20.425 21.420  -11.923 1.00 11.61 ? 159 LYS   A C   1 
ATOM   1146 O  O   . LYS   A 1 145 ? -20.849 22.549  -12.172 1.00 12.67 ? 159 LYS   A O   1 
ATOM   1147 C  CB  . LYS   A 1 145 ? -20.686 20.159  -14.093 1.00 14.10 ? 159 LYS   A CB  1 
ATOM   1148 C  CG  . LYS   A 1 145 ? -19.234 19.856  -14.362 0.50 14.72 ? 159 LYS   A CG  1 
ATOM   1149 C  CD  . LYS   A 1 145 ? -18.912 19.449  -15.795 0.50 16.80 ? 159 LYS   A CD  1 
ATOM   1150 C  CE  . LYS   A 1 145 ? -18.877 20.631  -16.681 0.50 17.80 ? 159 LYS   A CE  1 
ATOM   1151 N  NZ  . LYS   A 1 145 ? -18.082 20.319  -17.866 0.50 19.90 ? 159 LYS   A NZ  1 
ATOM   1152 N  N   . LEU   A 1 146 ? -19.431 21.138  -11.063 1.00 11.86 ? 160 LEU   A N   1 
ATOM   1153 C  CA  . LEU   A 1 146 ? -18.801 22.106  -10.164 1.00 12.03 ? 160 LEU   A CA  1 
ATOM   1154 C  C   . LEU   A 1 146 ? -17.274 22.003  -10.221 1.00 11.91 ? 160 LEU   A C   1 
ATOM   1155 O  O   . LEU   A 1 146 ? -16.717 20.924  -10.397 1.00 12.39 ? 160 LEU   A O   1 
ATOM   1156 C  CB  . LEU   A 1 146 ? -19.241 21.873  -8.718  1.00 12.11 ? 160 LEU   A CB  1 
ATOM   1157 C  CG  . LEU   A 1 146 ? -20.731 22.050  -8.418  1.00 12.64 ? 160 LEU   A CG  1 
ATOM   1158 C  CD1 . LEU   A 1 146 ? -21.038 21.667  -6.956  1.00 12.65 ? 160 LEU   A CD1 1 
ATOM   1159 C  CD2 . LEU   A 1 146 ? -21.258 23.425  -8.753  1.00 12.97 ? 160 LEU   A CD2 1 
ATOM   1160 N  N   A ARG   A 1 147 ? -16.616 23.150  -10.040 0.50 11.80 ? 161 ARG   A N   1 
ATOM   1161 N  N   B ARG   A 1 147 ? -16.584 23.126  -9.974  0.50 11.77 ? 161 ARG   A N   1 
ATOM   1162 C  CA  A ARG   A 1 147 ? -15.169 23.232  -10.073 0.50 12.25 ? 161 ARG   A CA  1 
ATOM   1163 C  CA  B ARG   A 1 147 ? -15.129 23.172  -10.007 0.50 12.24 ? 161 ARG   A CA  1 
ATOM   1164 C  C   A ARG   A 1 147 ? -14.595 22.943  -8.691  0.50 11.31 ? 161 ARG   A C   1 
ATOM   1165 C  C   B ARG   A 1 147 ? -14.529 22.795  -8.651  0.50 12.07 ? 161 ARG   A C   1 
ATOM   1166 O  O   A ARG   A 1 147 ? -15.002 23.580  -7.713  0.50 10.25 ? 161 ARG   A O   1 
ATOM   1167 O  O   B ARG   A 1 147 ? -15.019 23.205  -7.597  0.50 11.59 ? 161 ARG   A O   1 
ATOM   1168 C  CB  A ARG   A 1 147 ? -14.775 24.640  -10.521 0.50 14.15 ? 161 ARG   A CB  1 
ATOM   1169 C  CB  B ARG   A 1 147 ? -14.638 24.568  -10.407 0.50 13.27 ? 161 ARG   A CB  1 
ATOM   1170 C  CG  A ARG   A 1 147 ? -13.271 24.838  -10.652 0.50 15.90 ? 161 ARG   A CG  1 
ATOM   1171 C  CG  B ARG   A 1 147 ? -13.125 24.756  -10.461 0.50 13.98 ? 161 ARG   A CG  1 
ATOM   1172 C  CD  A ARG   A 1 147 ? -12.938 26.188  -11.260 0.50 17.71 ? 161 ARG   A CD  1 
ATOM   1173 C  CD  B ARG   A 1 147 ? -12.455 24.255  -11.752 0.50 14.83 ? 161 ARG   A CD  1 
ATOM   1174 N  NE  A ARG   A 1 147 ? -11.586 26.223  -11.830 0.50 19.87 ? 161 ARG   A NE  1 
ATOM   1175 N  NE  B ARG   A 1 147 ? -12.905 24.965  -12.957 0.50 15.01 ? 161 ARG   A NE  1 
ATOM   1176 C  CZ  A ARG   A 1 147 ? -10.534 26.841  -11.308 0.50 21.66 ? 161 ARG   A CZ  1 
ATOM   1177 C  CZ  B ARG   A 1 147 ? -12.716 24.519  -14.207 0.50 15.64 ? 161 ARG   A CZ  1 
ATOM   1178 N  NH1 A ARG   A 1 147 ? -10.589 27.348  -10.090 0.50 22.66 ? 161 ARG   A NH1 1 
ATOM   1179 N  NH1 B ARG   A 1 147 ? -12.052 23.400  -14.442 0.50 15.67 ? 161 ARG   A NH1 1 
ATOM   1180 N  NH2 A ARG   A 1 147 ? -9.403  26.893  -11.989 0.50 21.90 ? 161 ARG   A NH2 1 
ATOM   1181 N  NH2 B ARG   A 1 147 ? -13.215 25.192  -15.227 0.50 16.53 ? 161 ARG   A NH2 1 
ATOM   1182 N  N   A LEU   A 1 148 ? -13.635 22.010  -8.629  0.50 10.52 ? 162 LEU   A N   1 
ATOM   1183 N  N   B LEU   A 1 148 ? -13.409 22.071  -8.692  0.50 12.11 ? 162 LEU   A N   1 
ATOM   1184 C  CA  A LEU   A 1 148 ? -12.800 21.865  -7.446  0.50 10.40 ? 162 LEU   A CA  1 
ATOM   1185 C  CA  B LEU   A 1 148 ? -12.639 21.789  -7.493  0.50 12.40 ? 162 LEU   A CA  1 
ATOM   1186 C  C   A LEU   A 1 148 ? -11.889 23.087  -7.367  0.50 10.65 ? 162 LEU   A C   1 
ATOM   1187 C  C   B LEU   A 1 148 ? -11.652 22.930  -7.239  0.50 11.84 ? 162 LEU   A C   1 
ATOM   1188 O  O   A LEU   A 1 148 ? -11.157 23.400  -8.315  0.50 9.36  ? 162 LEU   A O   1 
ATOM   1189 O  O   B LEU   A 1 148 ? -10.655 23.061  -7.955  0.50 10.34 ? 162 LEU   A O   1 
ATOM   1190 C  CB  A LEU   A 1 148 ? -11.953 20.597  -7.384  0.50 10.47 ? 162 LEU   A CB  1 
ATOM   1191 C  CB  B LEU   A 1 148 ? -11.938 20.455  -7.720  0.50 14.15 ? 162 LEU   A CB  1 
ATOM   1192 C  CG  A LEU   A 1 148 ? -12.684 19.263  -7.587  0.50 10.08 ? 162 LEU   A CG  1 
ATOM   1193 C  CG  B LEU   A 1 148 ? -11.688 19.591  -6.483  0.50 14.70 ? 162 LEU   A CG  1 
ATOM   1194 C  CD1 A LEU   A 1 148 ? -11.742 18.098  -7.459  0.50 10.19 ? 162 LEU   A CD1 1 
ATOM   1195 C  CD1 B LEU   A 1 148 ? -13.003 19.296  -5.766  0.50 14.76 ? 162 LEU   A CD1 1 
ATOM   1196 C  CD2 A LEU   A 1 148 ? -13.812 19.101  -6.581  0.50 10.08 ? 162 LEU   A CD2 1 
ATOM   1197 C  CD2 B LEU   A 1 148 ? -11.019 18.263  -6.829  0.50 15.30 ? 162 LEU   A CD2 1 
ATOM   1198 N  N   . MET   A 1 149 ? -11.927 23.738  -6.201  1.00 10.35 ? 163 MET   A N   1 
ATOM   1199 C  CA  . MET   A 1 149 ? -11.210 24.981  -5.973  1.00 10.45 ? 163 MET   A CA  1 
ATOM   1200 C  C   . MET   A 1 149 ? -9.956  24.736  -5.135  1.00 10.16 ? 163 MET   A C   1 
ATOM   1201 O  O   . MET   A 1 149 ? -9.836  23.782  -4.353  1.00 9.96  ? 163 MET   A O   1 
ATOM   1202 C  CB  . MET   A 1 149 ? -12.120 25.981  -5.243  1.00 10.15 ? 163 MET   A CB  1 
ATOM   1203 C  CG  . MET   A 1 149 ? -13.459 26.232  -5.921  1.00 11.29 ? 163 MET   A CG  1 
ATOM   1204 S  SD  . MET   A 1 149 ? -13.218 27.034  -7.520  1.00 14.21 ? 163 MET   A SD  1 
ATOM   1205 C  CE  . MET   A 1 149 ? -12.368 28.539  -7.035  1.00 14.63 ? 163 MET   A CE  1 
ATOM   1206 N  N   . ASP   A 1 150 ? -8.992  25.648  -5.274  1.00 10.74 ? 164 ASP   A N   1 
ATOM   1207 C  CA  . ASP   A 1 150 ? -7.862  25.670  -4.370  1.00 11.42 ? 164 ASP   A CA  1 
ATOM   1208 C  C   . ASP   A 1 150 ? -8.370  25.861  -2.943  1.00 10.42 ? 164 ASP   A C   1 
ATOM   1209 O  O   . ASP   A 1 150 ? -9.369  26.539  -2.751  1.00 10.17 ? 164 ASP   A O   1 
ATOM   1210 C  CB  . ASP   A 1 150 ? -6.905  26.791  -4.744  1.00 13.87 ? 164 ASP   A CB  1 
ATOM   1211 C  CG  . ASP   A 1 150 ? -6.172  26.586  -6.057  1.00 16.97 ? 164 ASP   A CG  1 
ATOM   1212 O  OD1 . ASP   A 1 150 ? -6.172  27.522  -6.862  1.00 24.53 ? 164 ASP   A OD1 1 
ATOM   1213 O  OD2 . ASP   A 1 150 ? -5.583  25.512  -6.233  1.00 20.46 ? 164 ASP   A OD2 1 
ATOM   1214 N  N   . PRO   A 1 151 ? -7.702  25.310  -1.906  1.00 10.82 ? 165 PRO   A N   1 
ATOM   1215 C  CA  . PRO   A 1 151 ? -8.229  25.362  -0.543  1.00 10.40 ? 165 PRO   A CA  1 
ATOM   1216 C  C   . PRO   A 1 151 ? -8.403  26.783  0.002   1.00 9.76  ? 165 PRO   A C   1 
ATOM   1217 O  O   . PRO   A 1 151 ? -9.256  27.009  0.853   1.00 8.79  ? 165 PRO   A O   1 
ATOM   1218 C  CB  . PRO   A 1 151 ? -7.228  24.499  0.256   1.00 10.96 ? 165 PRO   A CB  1 
ATOM   1219 C  CG  . PRO   A 1 151 ? -5.949  24.491  -0.576  1.00 10.97 ? 165 PRO   A CG  1 
ATOM   1220 C  CD  . PRO   A 1 151 ? -6.443  24.555  -2.000  1.00 11.22 ? 165 PRO   A CD  1 
ATOM   1221 N  N   . GLN   A 1 152 ? -7.619  27.759  -0.484  1.00 9.76  ? 166 GLN   A N   1 
ATOM   1222 C  CA  . GLN   A 1 152 ? -7.752  29.122  0.025   1.00 10.08 ? 166 GLN   A CA  1 
ATOM   1223 C  C   . GLN   A 1 152 ? -9.142  29.700  -0.279  1.00 8.93  ? 166 GLN   A C   1 
ATOM   1224 O  O   . GLN   A 1 152 ? -9.630  30.577  0.435   1.00 8.51  ? 166 GLN   A O   1 
ATOM   1225 C  CB  . GLN   A 1 152 ? -6.663  30.056  -0.496  1.00 11.69 ? 166 GLN   A CB  1 
ATOM   1226 C  CG  . GLN   A 1 152 ? -6.476  30.055  -1.999  1.00 13.36 ? 166 GLN   A CG  1 
ATOM   1227 C  CD  . GLN   A 1 152 ? -5.325  29.165  -2.422  1.00 15.35 ? 166 GLN   A CD  1 
ATOM   1228 O  OE1 . GLN   A 1 152 ? -5.160  28.033  -1.942  1.00 15.72 ? 166 GLN   A OE1 1 
ATOM   1229 N  NE2 . GLN   A 1 152 ? -4.478  29.710  -3.281  1.00 17.57 ? 166 GLN   A NE2 1 
ATOM   1230 N  N   . ALA   A 1 153 ? -9.844  29.139  -1.271  1.00 8.59  ? 167 ALA   A N   1 
ATOM   1231 C  CA  . ALA   A 1 153 ? -11.195 29.583  -1.578  1.00 8.29  ? 167 ALA   A CA  1 
ATOM   1232 C  C   . ALA   A 1 153 ? -12.187 29.277  -0.441  1.00 7.97  ? 167 ALA   A C   1 
ATOM   1233 O  O   . ALA   A 1 153 ? -13.278 29.871  -0.436  1.00 8.22  ? 167 ALA   A O   1 
ATOM   1234 C  CB  . ALA   A 1 153 ? -11.667 28.941  -2.877  1.00 8.31  ? 167 ALA   A CB  1 
ATOM   1235 N  N   . CYS   A 1 154 ? -11.834 28.331  0.443   1.00 7.76  ? 168 CYS   A N   1 
ATOM   1236 C  CA  . CYS   A 1 154 ? -12.680 27.912  1.562   1.00 7.32  ? 168 CYS   A CA  1 
ATOM   1237 C  C   . CYS   A 1 154 ? -12.132 28.394  2.911   1.00 7.78  ? 168 CYS   A C   1 
ATOM   1238 O  O   . CYS   A 1 154 ? -12.616 27.987  3.961   1.00 7.17  ? 168 CYS   A O   1 
ATOM   1239 C  CB  . CYS   A 1 154 ? -12.842 26.389  1.578   1.00 7.35  ? 168 CYS   A CB  1 
ATOM   1240 S  SG  . CYS   A 1 154 ? -14.082 25.769  0.408   1.00 7.38  ? 168 CYS   A SG  1 
ATOM   1241 N  N   . SER   A 1 155 ? -11.178 29.337  2.911   1.00 7.89  ? 169 SER   A N   1 
ATOM   1242 C  CA  . SER   A 1 155 ? -10.530 29.795  4.141   1.00 7.84  ? 169 SER   A CA  1 
ATOM   1243 C  C   . SER   A 1 155 ? -11.527 30.386  5.146   1.00 8.11  ? 169 SER   A C   1 
ATOM   1244 O  O   . SER   A 1 155 ? -11.347 30.254  6.360   1.00 8.02  ? 169 SER   A O   1 
ATOM   1245 C  CB  . SER   A 1 155 ? -9.448  30.798  3.809   1.00 8.18  ? 169 SER   A CB  1 
ATOM   1246 O  OG  . SER   A 1 155 ? -8.763  31.232  4.989   1.00 9.36  ? 169 SER   A OG  1 
ATOM   1247 N  N   . HIS   A 1 156 ? -12.578 31.045  4.639   1.00 7.66  ? 172 HIS   A N   1 
ATOM   1248 C  CA  . HIS   A 1 156 ? -13.571 31.701  5.481   1.00 7.39  ? 172 HIS   A CA  1 
ATOM   1249 C  C   . HIS   A 1 156 ? -14.316 30.691  6.362   1.00 7.26  ? 172 HIS   A C   1 
ATOM   1250 O  O   . HIS   A 1 156 ? -14.898 31.060  7.392   1.00 8.18  ? 172 HIS   A O   1 
ATOM   1251 C  CB  . HIS   A 1 156 ? -14.530 32.537  4.625   1.00 7.52  ? 172 HIS   A CB  1 
ATOM   1252 C  CG  . HIS   A 1 156 ? -15.237 31.798  3.546   1.00 7.45  ? 172 HIS   A CG  1 
ATOM   1253 N  ND1 . HIS   A 1 156 ? -14.587 31.366  2.408   1.00 7.50  ? 172 HIS   A ND1 1 
ATOM   1254 C  CD2 . HIS   A 1 156 ? -16.533 31.416  3.414   1.00 7.79  ? 172 HIS   A CD2 1 
ATOM   1255 C  CE1 . HIS   A 1 156 ? -15.482 30.764  1.615   1.00 7.11  ? 172 HIS   A CE1 1 
ATOM   1256 N  NE2 . HIS   A 1 156 ? -16.685 30.821  2.190   1.00 7.54  ? 172 HIS   A NE2 1 
ATOM   1257 N  N   . PHE   A 1 157 ? -14.373 29.432  5.935   1.00 6.99  ? 173 PHE   A N   1 
ATOM   1258 C  CA  . PHE   A 1 157 ? -14.813 28.365  6.829   1.00 7.23  ? 173 PHE   A CA  1 
ATOM   1259 C  C   . PHE   A 1 157 ? -13.633 28.063  7.748   1.00 7.96  ? 173 PHE   A C   1 
ATOM   1260 O  O   . PHE   A 1 157 ? -12.676 27.408  7.330   1.00 7.66  ? 173 PHE   A O   1 
ATOM   1261 C  CB  . PHE   A 1 157 ? -15.253 27.151  6.004   1.00 7.30  ? 173 PHE   A CB  1 
ATOM   1262 C  CG  . PHE   A 1 157 ? -16.394 27.388  5.020   1.00 7.46  ? 173 PHE   A CG  1 
ATOM   1263 C  CD1 . PHE   A 1 157 ? -17.673 27.697  5.451   1.00 8.03  ? 173 PHE   A CD1 1 
ATOM   1264 C  CD2 . PHE   A 1 157 ? -16.194 27.256  3.650   1.00 7.26  ? 173 PHE   A CD2 1 
ATOM   1265 C  CE1 . PHE   A 1 157 ? -18.716 27.896  4.548   1.00 8.46  ? 173 PHE   A CE1 1 
ATOM   1266 C  CE2 . PHE   A 1 157 ? -17.233 27.460  2.749   1.00 7.85  ? 173 PHE   A CE2 1 
ATOM   1267 C  CZ  . PHE   A 1 157 ? -18.497 27.765  3.193   1.00 8.00  ? 173 PHE   A CZ  1 
ATOM   1268 N  N   . ARG   A 1 158 ? -13.668 28.578  8.985   1.00 9.14  ? 174 ARG   A N   1 
ATOM   1269 C  CA  . ARG   A 1 158 ? -12.443 28.645  9.768   1.00 10.32 ? 174 ARG   A CA  1 
ATOM   1270 C  C   . ARG   A 1 158 ? -11.975 27.256  10.191  1.00 10.43 ? 174 ARG   A C   1 
ATOM   1271 O  O   . ARG   A 1 158 ? -10.783 27.083  10.457  1.00 10.59 ? 174 ARG   A O   1 
ATOM   1272 C  CB  . ARG   A 1 158 ? -12.603 29.587  10.968  1.00 11.99 ? 174 ARG   A CB  1 
ATOM   1273 C  CG  . ARG   A 1 158 ? -13.031 31.008  10.632  1.00 13.20 ? 174 ARG   A CG  1 
ATOM   1274 C  CD  . ARG   A 1 158 ? -12.213 31.688  9.562   1.00 13.30 ? 174 ARG   A CD  1 
ATOM   1275 N  NE  . ARG   A 1 158 ? -10.795 31.821  9.904   1.00 13.49 ? 174 ARG   A NE  1 
ATOM   1276 C  CZ  . ARG   A 1 158 ? -9.881  32.447  9.155   1.00 14.58 ? 174 ARG   A CZ  1 
ATOM   1277 N  NH1 . ARG   A 1 158 ? -10.228 33.092  8.050   1.00 15.46 ? 174 ARG   A NH1 1 
ATOM   1278 N  NH2 . ARG   A 1 158 ? -8.610  32.403  9.527   1.00 14.34 ? 174 ARG   A NH2 1 
ATOM   1279 N  N   . ASP   A 1 159 ? -12.893 26.268  10.218  1.00 10.06 ? 175 ASP   A N   1 
ATOM   1280 C  CA  . ASP   A 1 159 ? -12.534 24.883  10.527  1.00 10.06 ? 175 ASP   A CA  1 
ATOM   1281 C  C   . ASP   A 1 159 ? -12.327 23.996  9.295   1.00 9.30  ? 175 ASP   A C   1 
ATOM   1282 O  O   . ASP   A 1 159 ? -12.144 22.781  9.445   1.00 9.63  ? 175 ASP   A O   1 
ATOM   1283 C  CB  . ASP   A 1 159 ? -13.548 24.266  11.474  1.00 10.64 ? 175 ASP   A CB  1 
ATOM   1284 C  CG  . ASP   A 1 159 ? -13.527 24.896  12.857  1.00 12.76 ? 175 ASP   A CG  1 
ATOM   1285 O  OD1 . ASP   A 1 159 ? -12.417 25.036  13.422  1.00 13.58 ? 175 ASP   A OD1 1 
ATOM   1286 O  OD2 . ASP   A 1 159 ? -14.601 25.285  13.327  1.00 14.86 ? 175 ASP   A OD2 1 
ATOM   1287 N  N   . PHE   A 1 160 ? -12.311 24.573  8.091   1.00 8.86  ? 176 PHE   A N   1 
ATOM   1288 C  CA  . PHE   A 1 160 ? -11.971 23.819  6.892   1.00 9.37  ? 176 PHE   A CA  1 
ATOM   1289 C  C   . PHE   A 1 160 ? -10.512 23.362  6.939   1.00 9.60  ? 176 PHE   A C   1 
ATOM   1290 O  O   . PHE   A 1 160 ? -9.661  24.070  7.472   1.00 9.54  ? 176 PHE   A O   1 
ATOM   1291 C  CB  . PHE   A 1 160 ? -12.229 24.679  5.653   1.00 9.65  ? 176 PHE   A CB  1 
ATOM   1292 C  CG  . PHE   A 1 160 ? -11.699 24.101  4.360   1.00 9.82  ? 176 PHE   A CG  1 
ATOM   1293 C  CD1 . PHE   A 1 160 ? -10.446 24.462  3.872   1.00 10.56 ? 176 PHE   A CD1 1 
ATOM   1294 C  CD2 . PHE   A 1 160 ? -12.468 23.204  3.621   1.00 10.35 ? 176 PHE   A CD2 1 
ATOM   1295 C  CE1 . PHE   A 1 160 ? -9.959  23.914  2.697   1.00 10.03 ? 176 PHE   A CE1 1 
ATOM   1296 C  CE2 . PHE   A 1 160 ? -11.972 22.665  2.434   1.00 10.08 ? 176 PHE   A CE2 1 
ATOM   1297 C  CZ  . PHE   A 1 160 ? -10.725 23.014  1.986   1.00 10.09 ? 176 PHE   A CZ  1 
ATOM   1298 N  N   A ASP   A 1 161 ? -10.243 22.141  6.463   0.50 9.61  ? 177 ASP   A N   1 
ATOM   1299 N  N   B ASP   A 1 161 ? -10.236 22.182  6.363   0.50 9.70  ? 177 ASP   A N   1 
ATOM   1300 C  CA  A ASP   A 1 161 ? -8.869  21.693  6.284   0.50 10.10 ? 177 ASP   A CA  1 
ATOM   1301 C  CA  B ASP   A 1 161 ? -8.893  21.611  6.337   0.50 10.25 ? 177 ASP   A CA  1 
ATOM   1302 C  C   A ASP   A 1 161 ? -8.744  20.976  4.946   0.50 10.43 ? 177 ASP   A C   1 
ATOM   1303 C  C   B ASP   A 1 161 ? -8.682  20.881  5.007   0.50 10.50 ? 177 ASP   A C   1 
ATOM   1304 O  O   A ASP   A 1 161 ? -9.543  20.105  4.608   0.50 10.17 ? 177 ASP   A O   1 
ATOM   1305 O  O   B ASP   A 1 161 ? -9.366  19.892  4.740   0.50 9.82  ? 177 ASP   A O   1 
ATOM   1306 C  CB  A ASP   A 1 161 ? -8.354  20.815  7.416   0.50 10.53 ? 177 ASP   A CB  1 
ATOM   1307 C  CB  B ASP   A 1 161 ? -8.681  20.688  7.532   0.50 10.90 ? 177 ASP   A CB  1 
ATOM   1308 C  CG  A ASP   A 1 161 ? -6.923  20.320  7.234   0.50 11.36 ? 177 ASP   A CG  1 
ATOM   1309 C  CG  B ASP   A 1 161 ? -7.318  20.024  7.650   0.50 11.97 ? 177 ASP   A CG  1 
ATOM   1310 O  OD1 A ASP   A 1 161 ? -6.749  19.160  6.806   0.50 11.19 ? 177 ASP   A OD1 1 
ATOM   1311 O  OD1 B ASP   A 1 161 ? -6.754  19.634  6.598   0.50 11.85 ? 177 ASP   A OD1 1 
ATOM   1312 O  OD2 A ASP   A 1 161 ? -5.982  21.081  7.551   0.50 12.45 ? 177 ASP   A OD2 1 
ATOM   1313 O  OD2 B ASP   A 1 161 ? -6.836  19.880  8.802   0.50 12.57 ? 177 ASP   A OD2 1 
ATOM   1314 N  N   . HIS   A 1 162 ? -7.683  21.319  4.221   1.00 10.68 ? 178 HIS   A N   1 
ATOM   1315 C  CA  . HIS   A 1 162 ? -7.426  20.800  2.878   1.00 10.80 ? 178 HIS   A CA  1 
ATOM   1316 C  C   . HIS   A 1 162 ? -7.193  19.283  2.855   1.00 10.89 ? 178 HIS   A C   1 
ATOM   1317 O  O   . HIS   A 1 162 ? -7.526  18.618  1.872   1.00 10.33 ? 178 HIS   A O   1 
ATOM   1318 C  CB  . HIS   A 1 162 ? -6.205  21.523  2.287   1.00 10.72 ? 178 HIS   A CB  1 
ATOM   1319 C  CG  . HIS   A 1 162 ? -5.803  21.158  0.898   1.00 10.35 ? 178 HIS   A CG  1 
ATOM   1320 N  ND1 . HIS   A 1 162 ? -6.676  21.155  -0.183  1.00 11.20 ? 178 HIS   A ND1 1 
ATOM   1321 C  CD2 . HIS   A 1 162 ? -4.611  20.768  0.406   1.00 10.82 ? 178 HIS   A CD2 1 
ATOM   1322 C  CE1 . HIS   A 1 162 ? -6.027  20.779  -1.269  1.00 11.10 ? 178 HIS   A CE1 1 
ATOM   1323 N  NE2 . HIS   A 1 162 ? -4.766  20.519  -0.939  1.00 11.34 ? 178 HIS   A NE2 1 
ATOM   1324 N  N   A ASN   A 1 163 A -6.561  18.754  3.918   0.50 10.24 ? 178 ASN   A N   1 
ATOM   1325 N  N   B ASN   A 1 163 A -6.602  18.719  3.903   0.50 11.86 ? 178 ASN   A N   1 
ATOM   1326 C  CA  A ASN   A 1 163 A -6.242  17.335  4.010   0.50 9.91  ? 178 ASN   A CA  1 
ATOM   1327 C  CA  B ASN   A 1 163 A -6.271  17.308  3.846   0.50 12.85 ? 178 ASN   A CA  1 
ATOM   1328 C  C   A ASN   A 1 163 A -7.534  16.528  4.107   0.50 9.98  ? 178 ASN   A C   1 
ATOM   1329 C  C   B ASN   A 1 163 A -7.480  16.457  4.254   0.50 11.44 ? 178 ASN   A C   1 
ATOM   1330 O  O   A ASN   A 1 163 A -7.621  15.465  3.508   0.50 9.82  ? 178 ASN   A O   1 
ATOM   1331 O  O   B ASN   A 1 163 A -7.470  15.253  4.018   0.50 11.15 ? 178 ASN   A O   1 
ATOM   1332 C  CB  A ASN   A 1 163 A -5.307  16.983  5.172   0.50 9.39  ? 178 ASN   A CB  1 
ATOM   1333 C  CB  B ASN   A 1 163 A -4.942  17.045  4.546   0.50 14.84 ? 178 ASN   A CB  1 
ATOM   1334 C  CG  A ASN   A 1 163 A -4.445  15.779  4.840   0.50 9.15  ? 178 ASN   A CG  1 
ATOM   1335 C  CG  B ASN   A 1 163 A -3.861  16.727  3.535   0.50 17.72 ? 178 ASN   A CG  1 
ATOM   1336 O  OD1 A ASN   A 1 163 A -4.111  15.573  3.673   0.50 10.33 ? 178 ASN   A OD1 1 
ATOM   1337 O  OD1 B ASN   A 1 163 A -3.487  17.553  2.679   0.50 18.55 ? 178 ASN   A OD1 1 
ATOM   1338 N  ND2 A ASN   A 1 163 A -4.107  14.946  5.810   0.50 9.18  ? 178 ASN   A ND2 1 
ATOM   1339 N  ND2 B ASN   A 1 163 A -3.386  15.493  3.591   0.50 19.81 ? 178 ASN   A ND2 1 
ATOM   1340 N  N   . LEU   A 1 164 ? -8.522  17.083  4.814   1.00 10.14 ? 179 LEU   A N   1 
ATOM   1341 C  CA  . LEU   A 1 164 ? -9.724  16.357  5.206   1.00 10.89 ? 179 LEU   A CA  1 
ATOM   1342 C  C   . LEU   A 1 164 ? -10.889 16.572  4.242   1.00 9.71  ? 179 LEU   A C   1 
ATOM   1343 O  O   . LEU   A 1 164 ? -11.876 15.827  4.309   1.00 10.73 ? 179 LEU   A O   1 
ATOM   1344 C  CB  . LEU   A 1 164 ? -10.178 16.814  6.590   1.00 12.23 ? 179 LEU   A CB  1 
ATOM   1345 C  CG  . LEU   A 1 164 ? -9.211  16.628  7.763   1.00 14.29 ? 179 LEU   A CG  1 
ATOM   1346 C  CD1 . LEU   A 1 164 ? -9.873  17.048  9.070   1.00 14.79 ? 179 LEU   A CD1 1 
ATOM   1347 C  CD2 . LEU   A 1 164 ? -8.703  15.217  7.848   1.00 16.03 ? 179 LEU   A CD2 1 
ATOM   1348 N  N   . GLN   A 1 165 ? -10.874 17.665  3.477   1.00 8.91  ? 180 GLN   A N   1 
ATOM   1349 C  CA  . GLN   A 1 165 ? -12.075 18.153  2.810   1.00 8.58  ? 180 GLN   A CA  1 
ATOM   1350 C  C   . GLN   A 1 165 ? -11.710 18.715  1.443   1.00 9.30  ? 180 GLN   A C   1 
ATOM   1351 O  O   . GLN   A 1 165 ? -10.600 19.233  1.227   1.00 9.65  ? 180 GLN   A O   1 
ATOM   1352 C  CB  . GLN   A 1 165 ? -12.786 19.249  3.618   1.00 8.71  ? 180 GLN   A CB  1 
ATOM   1353 C  CG  . GLN   A 1 165 ? -13.399 18.756  4.933   1.00 8.55  ? 180 GLN   A CG  1 
ATOM   1354 C  CD  . GLN   A 1 165 ? -13.513 19.809  6.018   1.00 9.52  ? 180 GLN   A CD  1 
ATOM   1355 O  OE1 . GLN   A 1 165 ? -12.650 20.683  6.180   1.00 10.54 ? 180 GLN   A OE1 1 
ATOM   1356 N  NE2 . GLN   A 1 165 ? -14.559 19.738  6.827   1.00 9.30  ? 180 GLN   A NE2 1 
ATOM   1357 N  N   . LEU   A 1 166 ? -12.695 18.650  0.537   1.00 8.58  ? 181 LEU   A N   1 
ATOM   1358 C  CA  . LEU   A 1 166 ? -12.637 19.314  -0.752  1.00 8.82  ? 181 LEU   A CA  1 
ATOM   1359 C  C   . LEU   A 1 166 ? -13.406 20.626  -0.677  1.00 8.22  ? 181 LEU   A C   1 
ATOM   1360 O  O   . LEU   A 1 166 ? -14.420 20.740  0.032   1.00 8.43  ? 181 LEU   A O   1 
ATOM   1361 C  CB  . LEU   A 1 166 ? -13.244 18.408  -1.816  1.00 9.51  ? 181 LEU   A CB  1 
ATOM   1362 C  CG  . LEU   A 1 166 ? -12.495 17.122  -2.136  1.00 10.64 ? 181 LEU   A CG  1 
ATOM   1363 C  CD1 . LEU   A 1 166 ? -13.423 16.247  -2.982  1.00 11.18 ? 181 LEU   A CD1 1 
ATOM   1364 C  CD2 . LEU   A 1 166 ? -11.236 17.463  -2.909  1.00 11.72 ? 181 LEU   A CD2 1 
ATOM   1365 N  N   . CYS   A 1 167 ? -12.934 21.609  -1.472  1.00 7.93  ? 182 CYS   A N   1 
ATOM   1366 C  CA  . CYS   A 1 167 ? -13.534 22.924  -1.602  1.00 7.59  ? 182 CYS   A CA  1 
ATOM   1367 C  C   . CYS   A 1 167 ? -14.208 23.027  -2.970  1.00 7.71  ? 182 CYS   A C   1 
ATOM   1368 O  O   . CYS   A 1 167 ? -13.526 22.975  -3.995  1.00 7.80  ? 182 CYS   A O   1 
ATOM   1369 C  CB  . CYS   A 1 167 ? -12.458 23.994  -1.460  1.00 7.55  ? 182 CYS   A CB  1 
ATOM   1370 S  SG  . CYS   A 1 167 ? -13.079 25.689  -1.391  1.00 8.12  ? 182 CYS   A SG  1 
ATOM   1371 N  N   . VAL   A 1 168 ? -15.554 23.108  -3.000  1.00 7.06  ? 183 VAL   A N   1 
ATOM   1372 C  CA  . VAL   A 1 168 ? -16.269 22.795  -4.239  1.00 7.44  ? 183 VAL   A CA  1 
ATOM   1373 C  C   . VAL   A 1 168 ? -17.227 23.908  -4.657  1.00 7.76  ? 183 VAL   A C   1 
ATOM   1374 O  O   . VAL   A 1 168 ? -18.170 24.223  -3.939  1.00 7.36  ? 183 VAL   A O   1 
ATOM   1375 C  CB  . VAL   A 1 168 ? -17.016 21.454  -4.094  1.00 8.01  ? 183 VAL   A CB  1 
ATOM   1376 C  CG1 . VAL   A 1 168 ? -17.668 21.083  -5.415  1.00 8.51  ? 183 VAL   A CG1 1 
ATOM   1377 C  CG2 . VAL   A 1 168 ? -16.089 20.357  -3.579  1.00 8.21  ? 183 VAL   A CG2 1 
ATOM   1378 N  N   . GLY   A 1 169 ? -17.008 24.430  -5.889  1.00 7.90  ? 184 GLY   A N   1 
ATOM   1379 C  CA  . GLY   A 1 169 ? -17.883 25.436  -6.484  1.00 8.51  ? 184 GLY   A CA  1 
ATOM   1380 C  C   . GLY   A 1 169 ? -17.193 26.793  -6.647  1.00 9.43  ? 184 GLY   A C   1 
ATOM   1381 O  O   . GLY   A 1 169 ? -16.825 27.436  -5.669  1.00 8.48  ? 184 GLY   A O   1 
ATOM   1382 N  N   . ASN   A 1 170 ? -17.068 27.225  -7.909  1.00 9.93  ? 185 ASN   A N   1 
ATOM   1383 C  CA  . ASN   A 1 170 ? -16.528 28.532  -8.260  1.00 11.10 ? 185 ASN   A CA  1 
ATOM   1384 C  C   . ASN   A 1 170 ? -17.393 29.630  -7.638  1.00 10.87 ? 185 ASN   A C   1 
ATOM   1385 O  O   . ASN   A 1 170 ? -18.604 29.668  -7.847  1.00 11.11 ? 185 ASN   A O   1 
ATOM   1386 C  CB  . ASN   A 1 170 ? -16.468 28.635  -9.784  1.00 12.79 ? 185 ASN   A CB  1 
ATOM   1387 C  CG  . ASN   A 1 170 ? -15.939 29.960  -10.304 1.00 15.20 ? 185 ASN   A CG  1 
ATOM   1388 O  OD1 . ASN   A 1 170 ? -15.775 30.909  -9.545  1.00 13.91 ? 185 ASN   A OD1 1 
ATOM   1389 N  ND2 . ASN   A 1 170 ? -15.695 30.055  -11.609 1.00 17.54 ? 185 ASN   A ND2 1 
ATOM   1390 N  N   . PRO   A 1 171 ? -16.824 30.537  -6.811  1.00 11.39 ? 186 PRO   A N   1 
ATOM   1391 C  CA  . PRO   A 1 171 ? -17.629 31.570  -6.159  1.00 12.25 ? 186 PRO   A CA  1 
ATOM   1392 C  C   . PRO   A 1 171 ? -18.278 32.582  -7.110  1.00 14.26 ? 186 PRO   A C   1 
ATOM   1393 O  O   . PRO   A 1 171 ? -19.226 33.265  -6.722  1.00 15.31 ? 186 PRO   A O   1 
ATOM   1394 C  CB  . PRO   A 1 171 ? -16.649 32.220  -5.161  1.00 12.44 ? 186 PRO   A CB  1 
ATOM   1395 C  CG  . PRO   A 1 171 ? -15.294 31.976  -5.753  1.00 12.04 ? 186 PRO   A CG  1 
ATOM   1396 C  CD  . PRO   A 1 171 ? -15.402 30.588  -6.426  1.00 11.54 ? 186 PRO   A CD  1 
ATOM   1397 N  N   . ARG   A 1 172 A -17.817 32.617  -8.375  1.00 16.64 ? 186 ARG   A N   1 
ATOM   1398 C  CA  . ARG   A 1 172 A -18.374 33.509  -9.385  1.00 19.22 ? 186 ARG   A CA  1 
ATOM   1399 C  C   . ARG   A 1 172 A -19.695 33.019  -9.979  1.00 21.06 ? 186 ARG   A C   1 
ATOM   1400 O  O   . ARG   A 1 172 A -20.314 33.745  -10.757 1.00 21.54 ? 186 ARG   A O   1 
ATOM   1401 C  CB  . ARG   A 1 172 A -17.429 33.608  -10.586 1.00 22.11 ? 186 ARG   A CB  1 
ATOM   1402 C  CG  . ARG   A 1 172 A -16.131 34.343  -10.321 1.00 25.92 ? 186 ARG   A CG  1 
ATOM   1403 C  CD  . ARG   A 1 172 A -16.140 35.730  -10.915 1.00 27.57 ? 186 ARG   A CD  1 
ATOM   1404 N  NE  . ARG   A 1 172 A -16.205 35.854  -12.382 1.00 24.23 ? 186 ARG   A NE  1 
ATOM   1405 C  CZ  . ARG   A 1 172 A -16.497 37.013  -12.975 1.00 23.70 ? 186 ARG   A CZ  1 
ATOM   1406 N  NH1 . ARG   A 1 172 A -16.550 38.128  -12.266 1.00 29.53 ? 186 ARG   A NH1 1 
ATOM   1407 N  NH2 . ARG   A 1 172 A -16.738 37.090  -14.267 1.00 21.93 ? 186 ARG   A NH2 1 
ATOM   1408 N  N   . LYS   A 1 173 B -20.107 31.779  -9.671  1.00 18.56 ? 186 LYS   A N   1 
ATOM   1409 C  CA  . LYS   A 1 173 B -21.321 31.197  -10.201 1.00 18.87 ? 186 LYS   A CA  1 
ATOM   1410 C  C   . LYS   A 1 173 B -22.253 30.876  -9.037  1.00 19.21 ? 186 LYS   A C   1 
ATOM   1411 O  O   . LYS   A 1 173 B -21.788 30.833  -7.898  1.00 19.01 ? 186 LYS   A O   1 
ATOM   1412 C  CB  . LYS   A 1 173 B -21.016 29.880  -10.915 1.00 20.48 ? 186 LYS   A CB  1 
ATOM   1413 C  CG  . LYS   A 1 173 B -19.843 29.880  -11.886 1.00 24.34 ? 186 LYS   A CG  1 
ATOM   1414 C  CD  . LYS   A 1 173 B -20.175 30.580  -13.184 1.00 25.21 ? 186 LYS   A CD  1 
ATOM   1415 C  CE  . LYS   A 1 173 B -19.051 30.575  -14.188 1.00 24.89 ? 186 LYS   A CE  1 
ATOM   1416 N  NZ  . LYS   A 1 173 B -19.427 31.466  -15.291 1.00 25.06 ? 186 LYS   A NZ  1 
ATOM   1417 N  N   . THR   A 1 174 ? -23.544 30.667  -9.343  1.00 18.97 ? 187 THR   A N   1 
ATOM   1418 C  CA  . THR   A 1 174 ? -24.528 30.262  -8.339  1.00 19.47 ? 187 THR   A CA  1 
ATOM   1419 C  C   . THR   A 1 174 ? -24.525 28.746  -8.138  1.00 16.63 ? 187 THR   A C   1 
ATOM   1420 O  O   . THR   A 1 174 ? -25.028 28.247  -7.131  1.00 14.27 ? 187 THR   A O   1 
ATOM   1421 C  CB  . THR   A 1 174 ? -25.926 30.739  -8.738  1.00 22.42 ? 187 THR   A CB  1 
ATOM   1422 O  OG1 . THR   A 1 174 ? -26.325 29.975  -9.872  1.00 25.47 ? 187 THR   A OG1 1 
ATOM   1423 C  CG2 . THR   A 1 174 ? -25.975 32.227  -8.996  1.00 24.55 ? 187 THR   A CG2 1 
ATOM   1424 N  N   . LYS   A 1 175 ? -24.019 27.996  -9.116  1.00 14.98 ? 188 LYS   A N   1 
ATOM   1425 C  CA  . LYS   A 1 175 ? -24.083 26.539  -9.083  1.00 14.30 ? 188 LYS   A CA  1 
ATOM   1426 C  C   . LYS   A 1 175 ? -23.519 25.987  -7.769  1.00 12.60 ? 188 LYS   A C   1 
ATOM   1427 O  O   . LYS   A 1 175 ? -22.413 26.347  -7.363  1.00 11.63 ? 188 LYS   A O   1 
ATOM   1428 C  CB  . LYS   A 1 175 ? -23.281 25.954  -10.250 1.00 16.40 ? 188 LYS   A CB  1 
ATOM   1429 C  CG  . LYS   A 1 175 ? -23.815 26.298  -11.640 1.00 18.94 ? 188 LYS   A CG  1 
ATOM   1430 C  CD  . LYS   A 1 175 ? -23.186 25.476  -12.765 1.00 20.74 ? 188 LYS   A CD  1 
ATOM   1431 C  CE  . LYS   A 1 175 ? -21.684 25.514  -12.863 1.00 26.02 ? 188 LYS   A CE  1 
ATOM   1432 N  NZ  . LYS   A 1 175 ? -21.107 24.655  -13.914 1.00 28.29 ? 188 LYS   A NZ  1 
ATOM   1433 N  N   . SER   A 1 176 ? -24.263 25.078  -7.103  1.00 10.80 ? 189 SER   A N   1 
ATOM   1434 C  CA  . SER   A 1 176 ? -23.782 24.559  -5.822  1.00 10.20 ? 189 SER   A CA  1 
ATOM   1435 C  C   . SER   A 1 176 ? -24.629 23.390  -5.337  1.00 9.51  ? 189 SER   A C   1 
ATOM   1436 O  O   . SER   A 1 176 ? -25.826 23.337  -5.616  1.00 8.69  ? 189 SER   A O   1 
ATOM   1437 C  CB  . SER   A 1 176 ? -23.793 25.655  -4.767  1.00 10.20 ? 189 SER   A CB  1 
ATOM   1438 O  OG  . SER   A 1 176 ? -23.122 25.233  -3.584  1.00 11.12 ? 189 SER   A OG  1 
ATOM   1439 N  N   . ALA   A 1 177 ? -24.023 22.501  -4.536  1.00 8.86  ? 190 ALA   A N   1 
ATOM   1440 C  CA  . ALA   A 1 177 ? -24.815 21.697  -3.614  1.00 8.69  ? 190 ALA   A CA  1 
ATOM   1441 C  C   . ALA   A 1 177 ? -25.393 22.612  -2.536  1.00 8.66  ? 190 ALA   A C   1 
ATOM   1442 O  O   . ALA   A 1 177 ? -24.766 23.616  -2.156  1.00 9.03  ? 190 ALA   A O   1 
ATOM   1443 C  CB  . ALA   A 1 177 ? -23.958 20.619  -2.974  1.00 8.90  ? 190 ALA   A CB  1 
ATOM   1444 N  N   . PHE   A 1 178 ? -26.545 22.229  -1.982  1.00 8.58  ? 191 PHE   A N   1 
ATOM   1445 C  CA  . PHE   A 1 178 ? -27.131 23.033  -0.902  1.00 8.35  ? 191 PHE   A CA  1 
ATOM   1446 C  C   . PHE   A 1 178 ? -27.899 22.159  0.085   1.00 8.86  ? 191 PHE   A C   1 
ATOM   1447 O  O   . PHE   A 1 178 ? -27.788 20.936  0.090   1.00 8.16  ? 191 PHE   A O   1 
ATOM   1448 C  CB  . PHE   A 1 178 ? -27.928 24.161  -1.578  1.00 8.87  ? 191 PHE   A CB  1 
ATOM   1449 C  CG  . PHE   A 1 178 ? -28.422 25.276  -0.664  1.00 9.31  ? 191 PHE   A CG  1 
ATOM   1450 C  CD1 . PHE   A 1 178 ? -27.550 25.946  0.183   1.00 10.18 ? 191 PHE   A CD1 1 
ATOM   1451 C  CD2 . PHE   A 1 178 ? -29.776 25.631  -0.637  1.00 9.93  ? 191 PHE   A CD2 1 
ATOM   1452 C  CE1 . PHE   A 1 178 ? -28.007 26.922  1.051   1.00 10.20 ? 191 PHE   A CE1 1 
ATOM   1453 C  CE2 . PHE   A 1 178 ? -30.223 26.630  0.205   1.00 9.96  ? 191 PHE   A CE2 1 
ATOM   1454 C  CZ  . PHE   A 1 178 ? -29.340 27.264  1.060   1.00 10.86 ? 191 PHE   A CZ  1 
ATOM   1455 N  N   . LYS   A 1 179 ? -28.627 22.814  0.997   1.00 9.23  ? 192 LYS   A N   1 
ATOM   1456 C  CA  . LYS   A 1 179 ? -29.449 22.122  1.981   1.00 9.88  ? 192 LYS   A CA  1 
ATOM   1457 C  C   . LYS   A 1 179 ? -30.344 21.079  1.311   1.00 9.80  ? 192 LYS   A C   1 
ATOM   1458 O  O   . LYS   A 1 179 ? -30.983 21.331  0.293   1.00 10.57 ? 192 LYS   A O   1 
ATOM   1459 C  CB  . LYS   A 1 179 ? -30.281 23.155  2.746   1.00 10.98 ? 192 LYS   A CB  1 
ATOM   1460 C  CG  . LYS   A 1 179 ? -29.479 24.089  3.648   1.00 11.94 ? 192 LYS   A CG  1 
ATOM   1461 C  CD  . LYS   A 1 179 ? -30.355 25.173  4.266   1.00 14.20 ? 192 LYS   A CD  1 
ATOM   1462 C  CE  . LYS   A 1 179 ? -29.657 26.057  5.259   1.00 16.15 ? 192 LYS   A CE  1 
ATOM   1463 N  NZ  . LYS   A 1 179 ? -30.611 26.994  5.881   1.00 18.26 ? 192 LYS   A NZ  1 
ATOM   1464 N  N   . GLY   A 1 180 ? -30.344 19.886  1.907   1.00 9.56  ? 193 GLY   A N   1 
ATOM   1465 C  CA  . GLY   A 1 180 ? -31.084 18.749  1.396   1.00 9.75  ? 193 GLY   A CA  1 
ATOM   1466 C  C   . GLY   A 1 180 ? -30.227 17.857  0.500   1.00 9.59  ? 193 GLY   A C   1 
ATOM   1467 O  O   . GLY   A 1 180 ? -30.663 16.762  0.146   1.00 10.17 ? 193 GLY   A O   1 
ATOM   1468 N  N   . ASP   A 1 181 ? -29.019 18.315  0.125   1.00 8.54  ? 194 ASP   A N   1 
ATOM   1469 C  CA  . ASP   A 1 181 ? -28.105 17.523  -0.676  1.00 8.02  ? 194 ASP   A CA  1 
ATOM   1470 C  C   . ASP   A 1 181 ? -27.065 16.817  0.200   1.00 7.82  ? 194 ASP   A C   1 
ATOM   1471 O  O   . ASP   A 1 181 ? -26.251 16.069  -0.331  1.00 7.47  ? 194 ASP   A O   1 
ATOM   1472 C  CB  . ASP   A 1 181 ? -27.432 18.414  -1.714  1.00 8.24  ? 194 ASP   A CB  1 
ATOM   1473 C  CG  . ASP   A 1 181 ? -28.379 19.009  -2.749  1.00 8.65  ? 194 ASP   A CG  1 
ATOM   1474 O  OD1 . ASP   A 1 181 ? -29.308 18.263  -3.210  1.00 8.61  ? 194 ASP   A OD1 1 
ATOM   1475 O  OD2 . ASP   A 1 181 ? -28.154 20.185  -3.141  1.00 8.34  ? 194 ASP   A OD2 1 
ATOM   1476 N  N   . SER   A 1 182 ? -27.073 17.087  1.512   1.00 7.73  ? 195 SER   A N   1 
ATOM   1477 C  CA  . SER   A 1 182 ? -26.158 16.494  2.492   1.00 8.35  ? 195 SER   A CA  1 
ATOM   1478 C  C   . SER   A 1 182 ? -25.992 15.007  2.259   1.00 7.63  ? 195 SER   A C   1 
ATOM   1479 O  O   . SER   A 1 182 ? -26.982 14.323  2.070   1.00 8.18  ? 195 SER   A O   1 
ATOM   1480 C  CB  . SER   A 1 182 ? -26.666 16.639  3.952   1.00 8.88  ? 195 SER   A CB  1 
ATOM   1481 O  OG  . SER   A 1 182 ? -26.698 17.983  4.380   1.00 10.39 ? 195 SER   A OG  1 
ATOM   1482 N  N   . GLY   A 1 183 ? -24.748 14.508  2.254   1.00 7.31  ? 196 GLY   A N   1 
ATOM   1483 C  CA  . GLY   A 1 183 ? -24.492 13.073  2.208   1.00 7.36  ? 196 GLY   A CA  1 
ATOM   1484 C  C   . GLY   A 1 183 ? -24.380 12.493  0.804   1.00 7.45  ? 196 GLY   A C   1 
ATOM   1485 O  O   . GLY   A 1 183 ? -23.957 11.343  0.649   1.00 7.49  ? 196 GLY   A O   1 
ATOM   1486 N  N   . GLY   A 1 184 ? -24.752 13.277  -0.215  1.00 7.39  ? 197 GLY   A N   1 
ATOM   1487 C  CA  . GLY   A 1 184 ? -24.679 12.842  -1.596  1.00 7.31  ? 197 GLY   A CA  1 
ATOM   1488 C  C   . GLY   A 1 184 ? -23.239 12.821  -2.102  1.00 7.52  ? 197 GLY   A C   1 
ATOM   1489 O  O   . GLY   A 1 184 ? -22.384 13.577  -1.589  1.00 7.03  ? 197 GLY   A O   1 
ATOM   1490 N  N   . PRO   A 1 185 ? -22.933 11.981  -3.106  1.00 7.84  ? 198 PRO   A N   1 
ATOM   1491 C  CA  . PRO   A 1 185 ? -21.579 11.885  -3.657  1.00 8.12  ? 198 PRO   A CA  1 
ATOM   1492 C  C   . PRO   A 1 185 ? -21.204 12.975  -4.653  1.00 8.46  ? 198 PRO   A C   1 
ATOM   1493 O  O   . PRO   A 1 185 ? -22.041 13.479  -5.411  1.00 8.53  ? 198 PRO   A O   1 
ATOM   1494 C  CB  . PRO   A 1 185 ? -21.631 10.526  -4.325  1.00 8.47  ? 198 PRO   A CB  1 
ATOM   1495 C  CG  . PRO   A 1 185 ? -23.014 10.516  -4.927  1.00 8.87  ? 198 PRO   A CG  1 
ATOM   1496 C  CD  . PRO   A 1 185 ? -23.884 11.107  -3.821  1.00 8.45  ? 198 PRO   A CD  1 
ATOM   1497 N  N   . LEU   A 1 186 ? -19.929 13.346  -4.612  1.00 8.21  ? 199 LEU   A N   1 
ATOM   1498 C  CA  . LEU   A 1 186 ? -19.309 14.117  -5.684  1.00 8.46  ? 199 LEU   A CA  1 
ATOM   1499 C  C   . LEU   A 1 186 ? -18.487 13.167  -6.536  1.00 8.76  ? 199 LEU   A C   1 
ATOM   1500 O  O   . LEU   A 1 186 ? -17.552 12.557  -6.005  1.00 8.94  ? 199 LEU   A O   1 
ATOM   1501 C  CB  . LEU   A 1 186 ? -18.383 15.174  -5.074  1.00 8.39  ? 199 LEU   A CB  1 
ATOM   1502 C  CG  . LEU   A 1 186 ? -17.697 16.118  -6.075  1.00 8.43  ? 199 LEU   A CG  1 
ATOM   1503 C  CD1 . LEU   A 1 186 ? -18.690 17.106  -6.647  1.00 9.29  ? 199 LEU   A CD1 1 
ATOM   1504 C  CD2 . LEU   A 1 186 ? -16.559 16.840  -5.375  1.00 9.00  ? 199 LEU   A CD2 1 
ATOM   1505 N  N   . LEU   A 1 187 ? -18.863 13.017  -7.815  1.00 10.15 ? 200 LEU   A N   1 
ATOM   1506 C  CA  . LEU   A 1 187 ? -18.162 12.105  -8.712  1.00 11.83 ? 200 LEU   A CA  1 
ATOM   1507 C  C   . LEU   A 1 187 ? -17.238 12.901  -9.635  1.00 10.28 ? 200 LEU   A C   1 
ATOM   1508 O  O   . LEU   A 1 187 ? -17.641 13.894  -10.229 1.00 9.25  ? 200 LEU   A O   1 
ATOM   1509 C  CB  . LEU   A 1 187 ? -19.151 11.275  -9.522  1.00 13.51 ? 200 LEU   A CB  1 
ATOM   1510 C  CG  . LEU   A 1 187 ? -19.885 10.194  -8.709  1.00 16.70 ? 200 LEU   A CG  1 
ATOM   1511 C  CD1 . LEU   A 1 187 ? -21.168 10.806  -8.199  1.00 18.93 ? 200 LEU   A CD1 1 
ATOM   1512 C  CD2 . LEU   A 1 187 ? -20.113 8.971   -9.553  1.00 18.14 ? 200 LEU   A CD2 1 
ATOM   1513 N  N   . CYS   A 1 188 ? -15.997 12.424  -9.756  1.00 11.09 ? 201 CYS   A N   1 
ATOM   1514 C  CA  . CYS   A 1 188 ? -14.996 13.023  -10.631 1.00 11.80 ? 201 CYS   A CA  1 
ATOM   1515 C  C   . CYS   A 1 188 ? -14.572 11.921  -11.609 1.00 12.37 ? 201 CYS   A C   1 
ATOM   1516 O  O   . CYS   A 1 188 ? -14.017 10.922  -11.187 1.00 12.10 ? 201 CYS   A O   1 
ATOM   1517 C  CB  . CYS   A 1 188 ? -13.801 13.534  -9.828  1.00 11.86 ? 201 CYS   A CB  1 
ATOM   1518 S  SG  . CYS   A 1 188 ? -14.191 14.710  -8.490  1.00 12.06 ? 201 CYS   A SG  1 
ATOM   1519 N  N   . ALA   A 1 189 ? -14.909 12.083  -12.897 1.00 15.57 ? 202 ALA   A N   1 
ATOM   1520 C  CA  . ALA   A 1 189 ? -14.665 11.054  -13.906 1.00 18.23 ? 202 ALA   A CA  1 
ATOM   1521 C  C   . ALA   A 1 189 ? -15.256 9.717   -13.453 1.00 19.87 ? 202 ALA   A C   1 
ATOM   1522 O  O   . ALA   A 1 189 ? -14.628 8.662   -13.557 1.00 20.56 ? 202 ALA   A O   1 
ATOM   1523 C  CB  . ALA   A 1 189 ? -13.173 10.947  -14.194 1.00 19.62 ? 202 ALA   A CB  1 
ATOM   1524 N  N   . GLY   A 1 190 ? -16.469 9.770   -12.899 1.00 18.94 ? 207 GLY   A N   1 
ATOM   1525 C  CA  . GLY   A 1 190 ? -17.215 8.562   -12.573 1.00 18.23 ? 207 GLY   A CA  1 
ATOM   1526 C  C   . GLY   A 1 190 ? -16.787 7.893   -11.272 1.00 17.28 ? 207 GLY   A C   1 
ATOM   1527 O  O   . GLY   A 1 190 ? -17.253 6.797   -10.998 1.00 17.37 ? 207 GLY   A O   1 
ATOM   1528 N  N   . VAL   A 1 191 ? -15.922 8.537   -10.472 1.00 15.15 ? 208 VAL   A N   1 
ATOM   1529 C  CA  . VAL   A 1 191 ? -15.400 7.963   -9.239  1.00 14.02 ? 208 VAL   A CA  1 
ATOM   1530 C  C   . VAL   A 1 191 ? -15.818 8.883   -8.088  1.00 11.84 ? 208 VAL   A C   1 
ATOM   1531 O  O   . VAL   A 1 191 ? -15.589 10.079  -8.182  1.00 11.62 ? 208 VAL   A O   1 
ATOM   1532 C  CB  . VAL   A 1 191 ? -13.865 7.848   -9.281  1.00 16.13 ? 208 VAL   A CB  1 
ATOM   1533 C  CG1 . VAL   A 1 191 ? -13.299 7.311   -7.971  1.00 17.18 ? 208 VAL   A CG1 1 
ATOM   1534 C  CG2 . VAL   A 1 191 ? -13.421 7.002   -10.473 1.00 18.33 ? 208 VAL   A CG2 1 
ATOM   1535 N  N   . ALA   A 1 192 ? -16.417 8.330   -7.028  1.00 11.34 ? 209 ALA   A N   1 
ATOM   1536 C  CA  . ALA   A 1 192 ? -16.811 9.145   -5.882  1.00 10.29 ? 209 ALA   A CA  1 
ATOM   1537 C  C   . ALA   A 1 192 ? -15.577 9.656   -5.144  1.00 10.23 ? 209 ALA   A C   1 
ATOM   1538 O  O   . ALA   A 1 192 ? -14.771 8.858   -4.680  1.00 10.89 ? 209 ALA   A O   1 
ATOM   1539 C  CB  . ALA   A 1 192 ? -17.733 8.382   -4.957  1.00 10.48 ? 209 ALA   A CB  1 
ATOM   1540 N  N   . GLN   A 1 193 ? -15.460 10.985  -5.005  1.00 9.70  ? 210 GLN   A N   1 
ATOM   1541 C  CA  . GLN   A 1 193 ? -14.293 11.569  -4.349  1.00 8.74  ? 210 GLN   A CA  1 
ATOM   1542 C  C   . GLN   A 1 193 ? -14.685 12.460  -3.169  1.00 8.17  ? 210 GLN   A C   1 
ATOM   1543 O  O   . GLN   A 1 193 ? -13.839 12.755  -2.316  1.00 8.22  ? 210 GLN   A O   1 
ATOM   1544 C  CB  . GLN   A 1 193 ? -13.437 12.381  -5.318  1.00 9.44  ? 210 GLN   A CB  1 
ATOM   1545 C  CG  . GLN   A 1 193 ? -12.873 11.591  -6.503  1.00 10.36 ? 210 GLN   A CG  1 
ATOM   1546 C  CD  . GLN   A 1 193 ? -11.691 10.701  -6.188  0.50 9.85  ? 210 GLN   A CD  1 
ATOM   1547 O  OE1 . GLN   A 1 193 ? -11.011 10.196  -7.094  0.50 11.12 ? 210 GLN   A OE1 1 
ATOM   1548 N  NE2 . GLN   A 1 193 ? -11.413 10.481  -4.915  1.00 10.35 ? 210 GLN   A NE2 1 
ATOM   1549 N  N   . GLY   A 1 194 ? -15.960 12.831  -3.073  1.00 8.03  ? 211 GLY   A N   1 
ATOM   1550 C  CA  . GLY   A 1 194 ? -16.421 13.710  -2.007  1.00 7.81  ? 211 GLY   A CA  1 
ATOM   1551 C  C   . GLY   A 1 194 ? -17.822 13.352  -1.505  1.00 7.43  ? 211 GLY   A C   1 
ATOM   1552 O  O   . GLY   A 1 194 ? -18.549 12.636  -2.187  1.00 7.26  ? 211 GLY   A O   1 
ATOM   1553 N  N   . ILE   A 1 195 ? -18.179 13.872  -0.313  1.00 6.77  ? 212 ILE   A N   1 
ATOM   1554 C  CA  . ILE   A 1 195 ? -19.519 13.759  0.266   1.00 6.92  ? 212 ILE   A CA  1 
ATOM   1555 C  C   . ILE   A 1 195 ? -19.976 15.169  0.645   1.00 6.72  ? 212 ILE   A C   1 
ATOM   1556 O  O   . ILE   A 1 195 ? -19.256 15.850  1.356   1.00 6.88  ? 212 ILE   A O   1 
ATOM   1557 C  CB  . ILE   A 1 195 ? -19.523 12.833  1.505   1.00 7.10  ? 212 ILE   A CB  1 
ATOM   1558 C  CG1 . ILE   A 1 195 ? -18.975 11.447  1.186   1.00 7.57  ? 212 ILE   A CG1 1 
ATOM   1559 C  CG2 . ILE   A 1 195 ? -20.916 12.745  2.126   1.00 7.64  ? 212 ILE   A CG2 1 
ATOM   1560 C  CD1 . ILE   A 1 195 ? -18.753 10.556  2.386   1.00 7.59  ? 212 ILE   A CD1 1 
ATOM   1561 N  N   . VAL   A 1 196 ? -21.169 15.604  0.215   1.00 6.71  ? 213 VAL   A N   1 
ATOM   1562 C  CA  . VAL   A 1 196 ? -21.667 16.930  0.594   1.00 6.49  ? 213 VAL   A CA  1 
ATOM   1563 C  C   . VAL   A 1 196 ? -21.719 17.059  2.125   1.00 7.11  ? 213 VAL   A C   1 
ATOM   1564 O  O   . VAL   A 1 196 ? -22.375 16.231  2.795   1.00 6.97  ? 213 VAL   A O   1 
ATOM   1565 C  CB  . VAL   A 1 196 ? -23.082 17.183  0.025   1.00 6.61  ? 213 VAL   A CB  1 
ATOM   1566 C  CG1 . VAL   A 1 196 ? -23.598 18.546  0.438   1.00 6.69  ? 213 VAL   A CG1 1 
ATOM   1567 C  CG2 . VAL   A 1 196 ? -23.186 17.022  -1.478  1.00 6.73  ? 213 VAL   A CG2 1 
ATOM   1568 N  N   . SER   A 1 197 ? -21.034 18.070  2.692   1.00 7.07  ? 214 SER   A N   1 
ATOM   1569 C  CA  . SER   A 1 197 ? -21.018 18.273  4.140   1.00 6.92  ? 214 SER   A CA  1 
ATOM   1570 C  C   . SER   A 1 197 ? -21.714 19.565  4.585   1.00 6.93  ? 214 SER   A C   1 
ATOM   1571 O  O   . SER   A 1 197 ? -22.775 19.525  5.213   1.00 7.07  ? 214 SER   A O   1 
ATOM   1572 C  CB  . SER   A 1 197 ? -19.598 18.127  4.696   1.00 7.24  ? 214 SER   A CB  1 
ATOM   1573 O  OG  . SER   A 1 197 ? -19.600 18.334  6.097   1.00 7.12  ? 214 SER   A OG  1 
ATOM   1574 N  N   . TYR   A 1 198 ? -21.177 20.742  4.272   1.00 6.58  ? 215 TYR   A N   1 
ATOM   1575 C  CA  . TYR   A 1 198 ? -21.811 21.971  4.711   1.00 7.23  ? 215 TYR   A CA  1 
ATOM   1576 C  C   . TYR   A 1 198 ? -21.383 23.148  3.845   1.00 7.19  ? 215 TYR   A C   1 
ATOM   1577 O  O   . TYR   A 1 198 ? -20.525 23.009  2.982   1.00 6.81  ? 215 TYR   A O   1 
ATOM   1578 C  CB  . TYR   A 1 198 ? -21.448 22.269  6.169   1.00 7.89  ? 215 TYR   A CB  1 
ATOM   1579 C  CG  . TYR   A 1 198 ? -19.998 22.630  6.464   1.00 7.72  ? 215 TYR   A CG  1 
ATOM   1580 C  CD1 . TYR   A 1 198 ? -19.046 21.669  6.783   1.00 7.94  ? 215 TYR   A CD1 1 
ATOM   1581 C  CD2 . TYR   A 1 198 ? -19.592 23.966  6.512   1.00 8.62  ? 215 TYR   A CD2 1 
ATOM   1582 C  CE1 . TYR   A 1 198 ? -17.726 22.008  7.075   1.00 8.00  ? 215 TYR   A CE1 1 
ATOM   1583 C  CE2 . TYR   A 1 198 ? -18.291 24.317  6.848   1.00 9.12  ? 215 TYR   A CE2 1 
ATOM   1584 C  CZ  . TYR   A 1 198 ? -17.350 23.344  7.139   1.00 8.81  ? 215 TYR   A CZ  1 
ATOM   1585 O  OH  . TYR   A 1 198 ? -16.036 23.674  7.439   1.00 8.98  ? 215 TYR   A OH  1 
ATOM   1586 N  N   . GLY   A 1 199 ? -22.002 24.303  4.108   1.00 7.50  ? 216 GLY   A N   1 
ATOM   1587 C  CA  . GLY   A 1 199 ? -21.632 25.542  3.440   1.00 7.73  ? 216 GLY   A CA  1 
ATOM   1588 C  C   . GLY   A 1 199 ? -22.385 26.703  4.078   1.00 8.31  ? 216 GLY   A C   1 
ATOM   1589 O  O   . GLY   A 1 199 ? -22.817 26.601  5.231   1.00 9.06  ? 216 GLY   A O   1 
ATOM   1590 N  N   . ARG   A 1 200 ? -22.550 27.788  3.321   1.00 8.80  ? 217 ARG   A N   1 
ATOM   1591 C  CA  . ARG   A 1 200 ? -23.179 28.997  3.812   1.00 9.54  ? 217 ARG   A CA  1 
ATOM   1592 C  C   . ARG   A 1 200 ? -24.706 28.905  3.707   1.00 10.40 ? 217 ARG   A C   1 
ATOM   1593 O  O   . ARG   A 1 200 ? -25.234 28.438  2.701   1.00 9.99  ? 217 ARG   A O   1 
ATOM   1594 C  CB  . ARG   A 1 200 ? -22.723 30.222  3.002   1.00 9.20  ? 217 ARG   A CB  1 
ATOM   1595 C  CG  . ARG   A 1 200 ? -21.322 30.683  3.371   1.00 9.49  ? 217 ARG   A CG  1 
ATOM   1596 C  CD  . ARG   A 1 200 ? -20.839 31.827  2.495   1.00 9.89  ? 217 ARG   A CD  1 
ATOM   1597 N  NE  . ARG   A 1 200 ? -21.684 33.013  2.656   1.00 10.12 ? 217 ARG   A NE  1 
ATOM   1598 C  CZ  . ARG   A 1 200 ? -21.355 34.099  3.380   1.00 12.10 ? 217 ARG   A CZ  1 
ATOM   1599 N  NH1 . ARG   A 1 200 ? -20.250 34.122  4.122   1.00 13.53 ? 217 ARG   A NH1 1 
ATOM   1600 N  NH2 . ARG   A 1 200 ? -22.118 35.176  3.335   1.00 12.51 ? 217 ARG   A NH2 1 
ATOM   1601 N  N   A SER   A 1 201 ? -25.404 29.449  4.721   0.50 11.23 ? 218 SER   A N   1 
ATOM   1602 N  N   B SER   A 1 201 ? -25.394 29.467  4.711   0.50 11.37 ? 218 SER   A N   1 
ATOM   1603 C  CA  A SER   A 1 201 ? -26.861 29.549  4.709   0.50 11.39 ? 218 SER   A CA  1 
ATOM   1604 C  CA  B SER   A 1 201 ? -26.849 29.529  4.715   0.50 11.65 ? 218 SER   A CA  1 
ATOM   1605 C  C   A SER   A 1 201 ? -27.371 30.300  3.475   0.50 11.66 ? 218 SER   A C   1 
ATOM   1606 C  C   B SER   A 1 201 ? -27.400 30.355  3.546   0.50 11.77 ? 218 SER   A C   1 
ATOM   1607 O  O   A SER   A 1 201 ? -28.426 29.973  2.930   0.50 12.36 ? 218 SER   A O   1 
ATOM   1608 O  O   B SER   A 1 201 ? -28.527 30.123  3.116   0.50 12.50 ? 218 SER   A O   1 
ATOM   1609 C  CB  A SER   A 1 201 ? -27.389 30.208  5.975   0.50 12.09 ? 218 SER   A CB  1 
ATOM   1610 C  CB  B SER   A 1 201 ? -27.349 30.052  6.044   0.50 12.53 ? 218 SER   A CB  1 
ATOM   1611 O  OG  A SER   A 1 201 ? -26.884 29.603  7.156   0.50 12.93 ? 218 SER   A OG  1 
ATOM   1612 O  OG  B SER   A 1 201 ? -26.764 31.316  6.329   0.50 13.99 ? 218 SER   A OG  1 
ATOM   1613 N  N   . ASP   A 1 202 ? -26.612 31.301  3.005   1.00 10.88 ? 219 ASP   A N   1 
ATOM   1614 C  CA  . ASP   A 1 202 ? -27.043 32.116  1.872   1.00 11.34 ? 219 ASP   A CA  1 
ATOM   1615 C  C   . ASP   A 1 202 ? -26.675 31.518  0.514   1.00 11.80 ? 219 ASP   A C   1 
ATOM   1616 O  O   . ASP   A 1 202 ? -26.901 32.144  -0.515  1.00 11.55 ? 219 ASP   A O   1 
ATOM   1617 C  CB  . ASP   A 1 202 ? -26.545 33.548  2.008   1.00 11.24 ? 219 ASP   A CB  1 
ATOM   1618 C  CG  . ASP   A 1 202 ? -25.050 33.740  1.797   1.00 11.66 ? 219 ASP   A CG  1 
ATOM   1619 O  OD1 . ASP   A 1 202 ? -24.332 32.721  1.536   1.00 10.52 ? 219 ASP   A OD1 1 
ATOM   1620 O  OD2 . ASP   A 1 202 ? -24.606 34.909  1.904   1.00 11.50 ? 219 ASP   A OD2 1 
ATOM   1621 N  N   . ALA   A 1 203 ? -26.119 30.299  0.512   1.00 11.62 ? 220 ALA   A N   1 
ATOM   1622 C  CA  . ALA   A 1 203 ? -25.875 29.502  -0.684  1.00 11.40 ? 220 ALA   A CA  1 
ATOM   1623 C  C   . ALA   A 1 203 ? -24.700 30.001  -1.532  1.00 11.65 ? 220 ALA   A C   1 
ATOM   1624 O  O   . ALA   A 1 203 ? -24.458 29.420  -2.591  1.00 12.22 ? 220 ALA   A O   1 
ATOM   1625 C  CB  . ALA   A 1 203 ? -27.131 29.373  -1.540  1.00 11.21 ? 220 ALA   A CB  1 
ATOM   1626 N  N   . LYS   A 1 204 ? -23.903 30.973  -1.064  1.00 11.14 ? 221 LYS   A N   1 
ATOM   1627 C  CA  . LYS   A 1 204 ? -22.802 31.453  -1.893  1.00 11.78 ? 221 LYS   A CA  1 
ATOM   1628 C  C   . LYS   A 1 204 ? -21.705 30.391  -1.898  1.00 10.99 ? 221 LYS   A C   1 
ATOM   1629 O  O   . LYS   A 1 204 ? -21.203 30.023  -0.833  1.00 10.95 ? 221 LYS   A O   1 
ATOM   1630 C  CB  . LYS   A 1 204 ? -22.210 32.769  -1.376  1.00 13.27 ? 221 LYS   A CB  1 
ATOM   1631 C  CG  . LYS   A 1 204 ? -23.088 34.020  -1.507  1.00 16.14 ? 221 LYS   A CG  1 
ATOM   1632 C  CD  . LYS   A 1 204 ? -22.449 35.266  -0.893  1.00 18.81 ? 221 LYS   A CD  1 
ATOM   1633 C  CE  . LYS   A 1 204 ? -23.253 36.544  -1.093  1.00 21.08 ? 221 LYS   A CE  1 
ATOM   1634 N  NZ  . LYS   A 1 204 ? -22.570 37.722  -0.555  0.10 20.24 ? 221 LYS   A NZ  1 
ATOM   1635 N  N   . PRO   A 1 205 ? -21.325 29.883  -3.075  1.00 10.00 ? 224 PRO   A N   1 
ATOM   1636 C  CA  . PRO   A 1 205 ? -20.287 28.858  -3.073  1.00 9.68  ? 224 PRO   A CA  1 
ATOM   1637 C  C   . PRO   A 1 205 ? -18.920 29.489  -2.820  1.00 8.93  ? 224 PRO   A C   1 
ATOM   1638 O  O   . PRO   A 1 205 ? -18.776 30.717  -2.924  1.00 9.44  ? 224 PRO   A O   1 
ATOM   1639 C  CB  . PRO   A 1 205 ? -20.354 28.138  -4.426  1.00 9.90  ? 224 PRO   A CB  1 
ATOM   1640 C  CG  . PRO   A 1 205 ? -21.415 28.885  -5.193  1.00 11.04 ? 224 PRO   A CG  1 
ATOM   1641 C  CD  . PRO   A 1 205 ? -21.889 30.089  -4.419  1.00 10.70 ? 224 PRO   A CD  1 
ATOM   1642 N  N   . PRO   A 1 206 ? -17.861 28.701  -2.527  1.00 8.47  ? 225 PRO   A N   1 
ATOM   1643 C  CA  . PRO   A 1 206 ? -17.889 27.230  -2.446  1.00 8.36  ? 225 PRO   A CA  1 
ATOM   1644 C  C   . PRO   A 1 206 ? -18.538 26.587  -1.218  1.00 8.47  ? 225 PRO   A C   1 
ATOM   1645 O  O   . PRO   A 1 206 ? -18.757 27.259  -0.202  1.00 8.53  ? 225 PRO   A O   1 
ATOM   1646 C  CB  . PRO   A 1 206 ? -16.378 26.870  -2.481  1.00 8.67  ? 225 PRO   A CB  1 
ATOM   1647 C  CG  . PRO   A 1 206 ? -15.727 28.047  -1.816  1.00 8.60  ? 225 PRO   A CG  1 
ATOM   1648 C  CD  . PRO   A 1 206 ? -16.507 29.234  -2.323  1.00 8.89  ? 225 PRO   A CD  1 
ATOM   1649 N  N   . ALA   A 1 207 ? -18.833 25.290  -1.343  1.00 7.99  ? 226 ALA   A N   1 
ATOM   1650 C  CA  . ALA   A 1 207 ? -19.224 24.445  -0.219  1.00 8.00  ? 226 ALA   A CA  1 
ATOM   1651 C  C   . ALA   A 1 207 ? -18.127 23.435  0.128   1.00 8.29  ? 226 ALA   A C   1 
ATOM   1652 O  O   . ALA   A 1 207 ? -17.169 23.216  -0.636  1.00 8.65  ? 226 ALA   A O   1 
ATOM   1653 C  CB  . ALA   A 1 207 ? -20.545 23.754  -0.524  1.00 8.46  ? 226 ALA   A CB  1 
ATOM   1654 N  N   . VAL   A 1 208 ? -18.276 22.814  1.303   1.00 8.07  ? 227 VAL   A N   1 
ATOM   1655 C  CA  . VAL   A 1 208 ? -17.282 21.918  1.882   1.00 7.83  ? 227 VAL   A CA  1 
ATOM   1656 C  C   . VAL   A 1 208 ? -17.782 20.483  1.781   1.00 7.91  ? 227 VAL   A C   1 
ATOM   1657 O  O   . VAL   A 1 208 ? -18.909 20.191  2.181   1.00 8.10  ? 227 VAL   A O   1 
ATOM   1658 C  CB  . VAL   A 1 208 ? -17.004 22.289  3.348   1.00 7.83  ? 227 VAL   A CB  1 
ATOM   1659 C  CG1 . VAL   A 1 208 ? -16.075 21.301  4.051   1.00 7.75  ? 227 VAL   A CG1 1 
ATOM   1660 C  CG2 . VAL   A 1 208 ? -16.487 23.715  3.470   1.00 7.70  ? 227 VAL   A CG2 1 
ATOM   1661 N  N   . PHE   A 1 209 ? -16.941 19.622  1.211   1.00 7.86  ? 228 PHE   A N   1 
ATOM   1662 C  CA  . PHE   A 1 209 ? -17.227 18.209  1.034   1.00 7.64  ? 228 PHE   A CA  1 
ATOM   1663 C  C   . PHE   A 1 209 ? -16.190 17.376  1.788   1.00 7.43  ? 228 PHE   A C   1 
ATOM   1664 O  O   . PHE   A 1 209 ? -14.998 17.689  1.782   1.00 7.55  ? 228 PHE   A O   1 
ATOM   1665 C  CB  . PHE   A 1 209 ? -17.183 17.818  -0.447  1.00 7.31  ? 228 PHE   A CB  1 
ATOM   1666 C  CG  . PHE   A 1 209 ? -18.345 18.249  -1.342  1.00 7.35  ? 228 PHE   A CG  1 
ATOM   1667 C  CD1 . PHE   A 1 209 ? -18.682 19.591  -1.485  1.00 7.55  ? 228 PHE   A CD1 1 
ATOM   1668 C  CD2 . PHE   A 1 209 ? -19.077 17.303  -2.061  1.00 7.15  ? 228 PHE   A CD2 1 
ATOM   1669 C  CE1 . PHE   A 1 209 ? -19.702 19.977  -2.329  1.00 7.54  ? 228 PHE   A CE1 1 
ATOM   1670 C  CE2 . PHE   A 1 209 ? -20.098 17.694  -2.912  1.00 7.02  ? 228 PHE   A CE2 1 
ATOM   1671 C  CZ  . PHE   A 1 209 ? -20.402 19.026  -3.046  1.00 7.10  ? 228 PHE   A CZ  1 
ATOM   1672 N  N   . THR   A 1 210 ? -16.619 16.259  2.393   1.00 7.34  ? 229 THR   A N   1 
ATOM   1673 C  CA  . THR   A 1 210 ? -15.681 15.315  2.981   1.00 7.33  ? 229 THR   A CA  1 
ATOM   1674 C  C   . THR   A 1 210 ? -14.793 14.725  1.891   1.00 7.93  ? 229 THR   A C   1 
ATOM   1675 O  O   . THR   A 1 210 ? -15.298 14.322  0.849   1.00 7.91  ? 229 THR   A O   1 
ATOM   1676 C  CB  . THR   A 1 210 ? -16.428 14.188  3.687   1.00 7.31  ? 229 THR   A CB  1 
ATOM   1677 O  OG1 . THR   A 1 210 ? -17.342 14.780  4.594   1.00 7.19  ? 229 THR   A OG1 1 
ATOM   1678 C  CG2 . THR   A 1 210 ? -15.479 13.241  4.401   1.00 8.04  ? 229 THR   A CG2 1 
ATOM   1679 N  N   . ARG   A 1 211 ? -13.474 14.676  2.114   1.00 7.87  ? 230 ARG   A N   1 
ATOM   1680 C  CA  . ARG   A 1 211 ? -12.555 14.119  1.123   1.00 8.39  ? 230 ARG   A CA  1 
ATOM   1681 C  C   . ARG   A 1 211 ? -12.438 12.606  1.321   1.00 8.86  ? 230 ARG   A C   1 
ATOM   1682 O  O   . ARG   A 1 211 ? -11.831 12.139  2.289   1.00 9.07  ? 230 ARG   A O   1 
ATOM   1683 C  CB  . ARG   A 1 211 ? -11.154 14.732  1.266   1.00 8.89  ? 230 ARG   A CB  1 
ATOM   1684 C  CG  . ARG   A 1 211 ? -10.121 14.250  0.259   1.00 9.25  ? 230 ARG   A CG  1 
ATOM   1685 C  CD  . ARG   A 1 211 ? -8.738  14.789  0.598   1.00 9.72  ? 230 ARG   A CD  1 
ATOM   1686 N  NE  . ARG   A 1 211 ? -8.554  16.228  0.337   1.00 10.25 ? 230 ARG   A NE  1 
ATOM   1687 C  CZ  . ARG   A 1 211 ? -8.351  16.807  -0.841  1.00 10.24 ? 230 ARG   A CZ  1 
ATOM   1688 N  NH1 . ARG   A 1 211 ? -8.266  16.073  -1.958  1.00 11.31 ? 230 ARG   A NH1 1 
ATOM   1689 N  NH2 . ARG   A 1 211 ? -8.188  18.128  -0.918  1.00 9.80  ? 230 ARG   A NH2 1 
ATOM   1690 N  N   . ILE   A 1 212 ? -13.060 11.823  0.434   1.00 9.03  ? 231 ILE   A N   1 
ATOM   1691 C  CA  . ILE   A 1 212 ? -13.199 10.395  0.667   1.00 9.51  ? 231 ILE   A CA  1 
ATOM   1692 C  C   . ILE   A 1 212 ? -11.836 9.689   0.793   1.00 10.41 ? 231 ILE   A C   1 
ATOM   1693 O  O   . ILE   A 1 212 ? -11.702 8.768   1.595   1.00 10.03 ? 231 ILE   A O   1 
ATOM   1694 C  CB  . ILE   A 1 212 ? -14.087 9.749   -0.409  1.00 9.87  ? 231 ILE   A CB  1 
ATOM   1695 C  CG1 . ILE   A 1 212 ? -15.539 10.247  -0.347  1.00 10.01 ? 231 ILE   A CG1 1 
ATOM   1696 C  CG2 . ILE   A 1 212 ? -14.020 8.233   -0.275  1.00 10.38 ? 231 ILE   A CG2 1 
ATOM   1697 C  CD1 . ILE   A 1 212 ? -16.432 9.662   -1.438  1.00 10.02 ? 231 ILE   A CD1 1 
ATOM   1698 N  N   . SER   A 1 213 ? -10.841 10.084  0.002   1.00 10.92 ? 232 SER   A N   1 
ATOM   1699 C  CA  . SER   A 1 213 ? -9.557  9.393   0.001   1.00 11.52 ? 232 SER   A CA  1 
ATOM   1700 C  C   . SER   A 1 213 ? -8.995  9.257   1.416   1.00 12.51 ? 232 SER   A C   1 
ATOM   1701 O  O   . SER   A 1 213 ? -8.373  8.242   1.752   1.00 12.39 ? 232 SER   A O   1 
ATOM   1702 C  CB  . SER   A 1 213 ? -8.565  10.066  -0.904  1.00 11.44 ? 232 SER   A CB  1 
ATOM   1703 O  OG  . SER   A 1 213 ? -8.188  11.366  -0.449  1.00 11.79 ? 232 SER   A OG  1 
ATOM   1704 N  N   . HIS   A 1 214 ? -9.182  10.299  2.241   1.00 12.34 ? 233 HIS   A N   1 
ATOM   1705 C  CA  . HIS   A 1 214 ? -8.670  10.309  3.607   1.00 13.61 ? 233 HIS   A CA  1 
ATOM   1706 C  C   . HIS   A 1 214 ? -9.280  9.210   4.481   1.00 13.13 ? 233 HIS   A C   1 
ATOM   1707 O  O   . HIS   A 1 214 ? -8.630  8.771   5.446   1.00 12.98 ? 233 HIS   A O   1 
ATOM   1708 C  CB  . HIS   A 1 214 ? -8.858  11.699  4.232   1.00 14.23 ? 233 HIS   A CB  1 
ATOM   1709 C  CG  . HIS   A 1 214 ? -8.156  11.884  5.542   1.00 16.10 ? 233 HIS   A CG  1 
ATOM   1710 N  ND1 . HIS   A 1 214 ? -6.802  12.147  5.625   1.00 17.17 ? 233 HIS   A ND1 1 
ATOM   1711 C  CD2 . HIS   A 1 214 ? -8.600  11.785  6.815   1.00 16.60 ? 233 HIS   A CD2 1 
ATOM   1712 C  CE1 . HIS   A 1 214 ? -6.449  12.212  6.902   1.00 17.27 ? 233 HIS   A CE1 1 
ATOM   1713 N  NE2 . HIS   A 1 214 ? -7.522  12.023  7.646   1.00 18.21 ? 233 HIS   A NE2 1 
ATOM   1714 N  N   . TYR   A 1 215 ? -10.534 8.801   4.174   1.00 11.34 ? 234 TYR   A N   1 
ATOM   1715 C  CA  . TYR   A 1 215 ? -11.331 7.897   5.003   1.00 11.49 ? 234 TYR   A CA  1 
ATOM   1716 C  C   . TYR   A 1 215 ? -11.367 6.475   4.431   1.00 11.12 ? 234 TYR   A C   1 
ATOM   1717 O  O   . TYR   A 1 215 ? -12.071 5.624   4.969   1.00 12.35 ? 234 TYR   A O   1 
ATOM   1718 C  CB  . TYR   A 1 215 ? -12.755 8.452   5.193   1.00 11.17 ? 234 TYR   A CB  1 
ATOM   1719 C  CG  . TYR   A 1 215 ? -12.663 9.790   5.920   1.00 10.57 ? 234 TYR   A CG  1 
ATOM   1720 C  CD1 . TYR   A 1 215 ? -12.467 9.828   7.297   1.00 12.02 ? 234 TYR   A CD1 1 
ATOM   1721 C  CD2 . TYR   A 1 215 ? -12.626 10.997  5.231   1.00 10.17 ? 234 TYR   A CD2 1 
ATOM   1722 C  CE1 . TYR   A 1 215 ? -12.281 11.027  7.974   1.00 11.17 ? 234 TYR   A CE1 1 
ATOM   1723 C  CE2 . TYR   A 1 215 ? -12.465 12.202  5.901   1.00 10.71 ? 234 TYR   A CE2 1 
ATOM   1724 C  CZ  . TYR   A 1 215 ? -12.271 12.218  7.274   1.00 10.96 ? 234 TYR   A CZ  1 
ATOM   1725 O  OH  . TYR   A 1 215 ? -12.071 13.418  7.920   1.00 11.08 ? 234 TYR   A OH  1 
ATOM   1726 N  N   . ARG   A 1 216 ? -10.624 6.205   3.358   1.00 11.68 ? 235 ARG   A N   1 
ATOM   1727 C  CA  . ARG   A 1 216 ? -10.697 4.887   2.731   1.00 13.50 ? 235 ARG   A CA  1 
ATOM   1728 C  C   . ARG   A 1 216 ? -10.317 3.788   3.729   1.00 14.43 ? 235 ARG   A C   1 
ATOM   1729 O  O   . ARG   A 1 216 ? -10.985 2.744   3.782   1.00 15.05 ? 235 ARG   A O   1 
ATOM   1730 C  CB  . ARG   A 1 216 ? -9.909  4.820   1.422   1.00 14.37 ? 235 ARG   A CB  1 
ATOM   1731 C  CG  . ARG   A 1 216 ? -10.500 5.571   0.233   1.00 15.03 ? 235 ARG   A CG  1 
ATOM   1732 C  CD  . ARG   A 1 216 ? -11.717 4.901   -0.350  1.00 16.06 ? 235 ARG   A CD  1 
ATOM   1733 N  NE  . ARG   A 1 216 ? -11.390 3.581   -0.900  1.00 16.10 ? 235 ARG   A NE  1 
ATOM   1734 C  CZ  . ARG   A 1 216 ? -10.750 3.335   -2.031  1.00 16.48 ? 235 ARG   A CZ  1 
ATOM   1735 N  NH1 . ARG   A 1 216 ? -10.462 4.305   -2.883  1.00 16.63 ? 235 ARG   A NH1 1 
ATOM   1736 N  NH2 . ARG   A 1 216 ? -10.476 2.076   -2.339  1.00 17.90 ? 235 ARG   A NH2 1 
ATOM   1737 N  N   . PRO   A 1 217 ? -9.262  3.942   4.572   1.00 14.66 ? 236 PRO   A N   1 
ATOM   1738 C  CA  . PRO   A 1 217 ? -8.947  2.902   5.556   1.00 15.56 ? 236 PRO   A CA  1 
ATOM   1739 C  C   . PRO   A 1 217 ? -10.088 2.603   6.524   1.00 14.31 ? 236 PRO   A C   1 
ATOM   1740 O  O   . PRO   A 1 217 ? -10.398 1.433   6.769   1.00 15.67 ? 236 PRO   A O   1 
ATOM   1741 C  CB  . PRO   A 1 217 ? -7.693  3.439   6.284   1.00 16.16 ? 236 PRO   A CB  1 
ATOM   1742 C  CG  . PRO   A 1 217 ? -7.067  4.348   5.238   1.00 16.34 ? 236 PRO   A CG  1 
ATOM   1743 C  CD  . PRO   A 1 217 ? -8.262  5.028   4.556   1.00 15.75 ? 236 PRO   A CD  1 
ATOM   1744 N  N   . TRP   A 1 218 ? -10.730 3.662   7.035   1.00 13.34 ? 237 TRP   A N   1 
ATOM   1745 C  CA  . TRP   A 1 218 ? -11.857 3.497   7.940   1.00 13.09 ? 237 TRP   A CA  1 
ATOM   1746 C  C   . TRP   A 1 218 ? -13.022 2.785   7.237   1.00 12.38 ? 237 TRP   A C   1 
ATOM   1747 O  O   . TRP   A 1 218 ? -13.594 1.843   7.786   1.00 13.04 ? 237 TRP   A O   1 
ATOM   1748 C  CB  . TRP   A 1 218 ? -12.272 4.842   8.562   1.00 13.50 ? 237 TRP   A CB  1 
ATOM   1749 C  CG  . TRP   A 1 218 ? -13.487 4.736   9.442   1.00 13.92 ? 237 TRP   A CG  1 
ATOM   1750 C  CD1 . TRP   A 1 218 ? -13.540 4.284   10.725  1.00 15.11 ? 237 TRP   A CD1 1 
ATOM   1751 C  CD2 . TRP   A 1 218 ? -14.849 5.055   9.077   1.00 13.42 ? 237 TRP   A CD2 1 
ATOM   1752 N  NE1 . TRP   A 1 218 ? -14.819 4.305   11.189  1.00 15.34 ? 237 TRP   A NE1 1 
ATOM   1753 C  CE2 . TRP   A 1 218 ? -15.649 4.750   10.196  1.00 13.92 ? 237 TRP   A CE2 1 
ATOM   1754 C  CE3 . TRP   A 1 218 ? -15.454 5.539   7.916   1.00 13.08 ? 237 TRP   A CE3 1 
ATOM   1755 C  CZ2 . TRP   A 1 218 ? -17.027 4.942   10.195  1.00 14.15 ? 237 TRP   A CZ2 1 
ATOM   1756 C  CZ3 . TRP   A 1 218 ? -16.819 5.739   7.920   1.00 13.02 ? 237 TRP   A CZ3 1 
ATOM   1757 C  CH2 . TRP   A 1 218 ? -17.590 5.417   9.035   1.00 13.29 ? 237 TRP   A CH2 1 
ATOM   1758 N  N   . ILE   A 1 219 ? -13.381 3.227   6.026   1.00 11.40 ? 238 ILE   A N   1 
ATOM   1759 C  CA  . ILE   A 1 219 ? -14.458 2.593   5.269   1.00 11.95 ? 238 ILE   A CA  1 
ATOM   1760 C  C   . ILE   A 1 219 ? -14.189 1.090   5.120   1.00 13.02 ? 238 ILE   A C   1 
ATOM   1761 O  O   . ILE   A 1 219 ? -15.050 0.252   5.403   1.00 13.08 ? 238 ILE   A O   1 
ATOM   1762 C  CB  . ILE   A 1 219 ? -14.662 3.267   3.901   1.00 11.57 ? 238 ILE   A CB  1 
ATOM   1763 C  CG1 . ILE   A 1 219 ? -15.140 4.725   4.067   1.00 12.26 ? 238 ILE   A CG1 1 
ATOM   1764 C  CG2 . ILE   A 1 219 ? -15.618 2.454   3.028   1.00 11.79 ? 238 ILE   A CG2 1 
ATOM   1765 C  CD1 . ILE   A 1 219 ? -15.077 5.547   2.799   1.00 12.88 ? 238 ILE   A CD1 1 
ATOM   1766 N  N   . ASN   A 1 220 ? -12.960 0.756   4.714   1.00 13.67 ? 239 ASN   A N   1 
ATOM   1767 C  CA  . ASN   A 1 220 ? -12.561 -0.630  4.534   1.00 14.03 ? 239 ASN   A CA  1 
ATOM   1768 C  C   . ASN   A 1 220 ? -12.727 -1.412  5.837   1.00 14.46 ? 239 ASN   A C   1 
ATOM   1769 O  O   . ASN   A 1 220 ? -13.219 -2.536  5.813   1.00 15.99 ? 239 ASN   A O   1 
ATOM   1770 C  CB  . ASN   A 1 220 ? -11.165 -0.729  3.936   1.00 14.66 ? 239 ASN   A CB  1 
ATOM   1771 C  CG  . ASN   A 1 220 ? -10.710 -2.167  3.852   0.50 13.75 ? 239 ASN   A CG  1 
ATOM   1772 O  OD1 . ASN   A 1 220 ? -9.847  -2.593  4.629   0.50 15.77 ? 239 ASN   A OD1 1 
ATOM   1773 N  ND2 . ASN   A 1 220 ? -11.317 -2.934  2.964   0.50 12.98 ? 239 ASN   A ND2 1 
ATOM   1774 N  N   . GLN   A 1 221 ? -12.313 -0.831  6.969   1.00 15.76 ? 240 GLN   A N   1 
ATOM   1775 C  CA  . GLN   A 1 221 ? -12.347 -1.497  8.271   1.00 17.78 ? 240 GLN   A CA  1 
ATOM   1776 C  C   . GLN   A 1 221 ? -13.781 -1.863  8.670   1.00 18.47 ? 240 GLN   A C   1 
ATOM   1777 O  O   . GLN   A 1 221 ? -14.052 -2.957  9.186   1.00 17.60 ? 240 GLN   A O   1 
ATOM   1778 C  CB  . GLN   A 1 221 ? -11.708 -0.547  9.291   1.00 19.55 ? 240 GLN   A CB  1 
ATOM   1779 C  CG  . GLN   A 1 221 ? -11.528 -1.123  10.691  1.00 22.50 ? 240 GLN   A CG  1 
ATOM   1780 C  CD  . GLN   A 1 221 ? -10.883 -0.153  11.658  0.10 20.99 ? 240 GLN   A CD  1 
ATOM   1781 O  OE1 . GLN   A 1 221 ? -10.716 1.038   11.371  0.10 20.30 ? 240 GLN   A OE1 1 
ATOM   1782 N  NE2 . GLN   A 1 221 ? -10.523 -0.654  12.830  0.10 20.93 ? 240 GLN   A NE2 1 
ATOM   1783 N  N   . ILE   A 1 222 ? -14.706 -0.914  8.473   1.00 14.88 ? 241 ILE   A N   1 
ATOM   1784 C  CA  . ILE   A 1 222 ? -16.111 -1.153  8.779   1.00 14.55 ? 241 ILE   A CA  1 
ATOM   1785 C  C   . ILE   A 1 222 ? -16.671 -2.244  7.863   1.00 14.71 ? 241 ILE   A C   1 
ATOM   1786 O  O   . ILE   A 1 222 ? -17.359 -3.139  8.360   1.00 16.67 ? 241 ILE   A O   1 
ATOM   1787 C  CB  . ILE   A 1 222 ? -16.942 0.144   8.669   1.00 14.67 ? 241 ILE   A CB  1 
ATOM   1788 C  CG1 . ILE   A 1 222 ? -16.491 1.211   9.679   1.00 15.53 ? 241 ILE   A CG1 1 
ATOM   1789 C  CG2 . ILE   A 1 222 ? -18.448 -0.150  8.791   1.00 14.94 ? 241 ILE   A CG2 1 
ATOM   1790 C  CD1 . ILE   A 1 222 ? -16.684 0.824   11.131  1.00 17.06 ? 241 ILE   A CD1 1 
ATOM   1791 N  N   . LEU   A 1 223 ? -16.414 -2.155  6.548   1.00 14.49 ? 242 LEU   A N   1 
ATOM   1792 C  CA  . LEU   A 1 223 ? -16.987 -3.085  5.576   1.00 15.25 ? 242 LEU   A CA  1 
ATOM   1793 C  C   . LEU   A 1 223 ? -16.478 -4.507  5.848   1.00 19.38 ? 242 LEU   A C   1 
ATOM   1794 O  O   . LEU   A 1 223 ? -17.260 -5.460  5.798   1.00 20.19 ? 242 LEU   A O   1 
ATOM   1795 C  CB  . LEU   A 1 223 ? -16.752 -2.719  4.117   1.00 15.39 ? 242 LEU   A CB  1 
ATOM   1796 C  CG  . LEU   A 1 223 ? -17.382 -1.412  3.628   1.00 16.77 ? 242 LEU   A CG  1 
ATOM   1797 C  CD1 . LEU   A 1 223 ? -17.123 -1.145  2.152   1.00 17.05 ? 242 LEU   A CD1 1 
ATOM   1798 C  CD2 . LEU   A 1 223 ? -18.851 -1.368  3.937   1.00 16.47 ? 242 LEU   A CD2 1 
ATOM   1799 N  N   . GLN   A 1 224 ? -15.188 -4.641  6.170   1.00 19.39 ? 243 GLN   A N   1 
ATOM   1800 C  CA  . GLN   A 1 224 ? -14.602 -5.964  6.378   1.00 22.70 ? 243 GLN   A CA  1 
ATOM   1801 C  C   . GLN   A 1 224 ? -15.099 -6.621  7.672   1.00 23.49 ? 243 GLN   A C   1 
ATOM   1802 O  O   . GLN   A 1 224 ? -15.143 -7.847  7.721   1.00 27.15 ? 243 GLN   A O   1 
ATOM   1803 C  CB  . GLN   A 1 224 ? -13.072 -5.920  6.305   1.00 23.54 ? 243 GLN   A CB  1 
ATOM   1804 C  CG  . GLN   A 1 224 ? -12.507 -5.528  4.944   0.50 24.85 ? 243 GLN   A CG  1 
ATOM   1805 C  CD  . GLN   A 1 224 ? -12.768 -6.543  3.853   0.50 26.92 ? 243 GLN   A CD  1 
ATOM   1806 O  OE1 . GLN   A 1 224 ? -12.389 -7.715  3.955   0.50 28.68 ? 243 GLN   A OE1 1 
ATOM   1807 N  NE2 . GLN   A 1 224 ? -13.426 -6.098  2.790   0.50 26.63 ? 243 GLN   A NE2 1 
ATOM   1808 N  N   . ALA   A 1 225 ? -15.467 -5.846  8.705   1.00 21.46 ? 244 ALA   A N   1 
ATOM   1809 C  CA  . ALA   A 1 225 ? -15.881 -6.365  10.008  1.00 22.94 ? 244 ALA   A CA  1 
ATOM   1810 C  C   . ALA   A 1 225 ? -17.393 -6.540  10.147  1.00 25.37 ? 244 ALA   A C   1 
ATOM   1811 O  O   . ALA   A 1 225 ? -17.849 -7.004  11.195  1.00 26.68 ? 244 ALA   A O   1 
ATOM   1812 C  CB  . ALA   A 1 225 ? -15.397 -5.447  11.106  1.00 24.49 ? 244 ALA   A CB  1 
ATOM   1813 N  N   . ASN   A 1 226 ? -18.176 -6.141  9.138   1.00 23.32 ? 245 ASN   A N   1 
ATOM   1814 C  CA  . ASN   A 1 226 ? -19.628 -6.130  9.291   1.00 25.91 ? 245 ASN   A CA  1 
ATOM   1815 C  C   . ASN   A 1 226 ? -20.264 -6.755  8.048   1.00 29.37 ? 245 ASN   A C   1 
ATOM   1816 O  O   . ASN   A 1 226 ? -21.463 -6.483  7.800   1.00 29.95 ? 245 ASN   A O   1 
ATOM   1817 C  CB  . ASN   A 1 226 ? -20.143 -4.726  9.588   1.00 24.61 ? 245 ASN   A CB  1 
ATOM   1818 C  CG  . ASN   A 1 226 ? -19.697 -4.261  10.950  1.00 24.58 ? 245 ASN   A CG  1 
ATOM   1819 O  OD1 . ASN   A 1 226 ? -20.330 -4.620  11.947  1.00 26.94 ? 245 ASN   A OD1 1 
ATOM   1820 N  ND2 . ASN   A 1 226 ? -18.633 -3.473  11.025  1.00 25.16 ? 245 ASN   A ND2 1 
ATOM   1821 O  OXT . ASN   A 1 226 ? -19.541 -7.538  7.394   1.00 32.87 ? 245 ASN   A OXT 1 
HETATM 1822 ZN ZN  . ZN    B 2 .   ? -38.871 5.187   -13.146 1.00 11.95 ? 301 ZN    A ZN  1 
HETATM 1823 N  N1  . A1AO8 C 3 .   ? -26.695 20.493  6.291   1.00 8.92  ? 302 A1AO8 A N1  1 
HETATM 1824 C  C4  . A1AO8 C 3 .   ? -27.052 20.114  8.487   1.00 9.52  ? 302 A1AO8 A C4  1 
HETATM 1825 C  C5  . A1AO8 C 3 .   ? -26.068 20.369  7.523   1.00 9.04  ? 302 A1AO8 A C5  1 
HETATM 1826 C  C6  . A1AO8 C 3 .   ? -26.009 20.854  5.062   1.00 9.08  ? 302 A1AO8 A C6  1 
HETATM 1827 C  C7  . A1AO8 C 3 .   ? -29.667 19.883  8.437   1.00 10.16 ? 302 A1AO8 A C7  1 
HETATM 1828 C  C8  . A1AO8 C 3 .   ? -29.749 18.540  9.122   1.00 10.14 ? 302 A1AO8 A C8  1 
HETATM 1829 C  C10 . A1AO8 C 3 .   ? -25.955 22.350  4.829   1.00 9.45  ? 302 A1AO8 A C10 1 
HETATM 1830 C  C13 . A1AO8 C 3 .   ? -25.380 22.878  3.634   1.00 8.76  ? 302 A1AO8 A C13 1 
HETATM 1831 C  C17 . A1AO8 C 3 .   ? -25.318 19.964  10.116  1.00 10.81 ? 302 A1AO8 A C17 1 
HETATM 1832 C  C20 . A1AO8 C 3 .   ? -24.330 20.217  9.168   1.00 10.08 ? 302 A1AO8 A C20 1 
HETATM 1833 C  C22 . A1AO8 C 3 .   ? -26.418 23.225  5.798   1.00 10.11 ? 302 A1AO8 A C22 1 
HETATM 1834 C  C24 . A1AO8 C 3 .   ? -30.047 16.128  8.926   1.00 9.97  ? 302 A1AO8 A C24 1 
HETATM 1835 C  C26 . A1AO8 C 3 .   ? -24.855 22.055  2.601   1.00 9.16  ? 302 A1AO8 A C26 1 
HETATM 1836 C  C28 . A1AO8 C 3 .   ? -24.796 24.818  2.250   1.00 10.04 ? 302 A1AO8 A C28 1 
HETATM 1837 C  C2  . A1AO8 C 3 .   ? -28.317 20.103  7.801   1.00 9.27  ? 302 A1AO8 A C2  1 
HETATM 1838 C  C3  . A1AO8 C 3 .   ? -28.062 20.369  6.486   1.00 9.66  ? 302 A1AO8 A C3  1 
HETATM 1839 C  C9  . A1AO8 C 3 .   ? -29.035 20.424  5.400   1.00 10.18 ? 302 A1AO8 A C9  1 
HETATM 1840 C  C11 . A1AO8 C 3 .   ? -24.714 20.422  7.852   1.00 9.40  ? 302 A1AO8 A C11 1 
HETATM 1841 C  C12 . A1AO8 C 3 .   ? -26.663 19.914  9.818   1.00 10.33 ? 302 A1AO8 A C12 1 
HETATM 1842 N  N14 . A1AO8 C 3 .   ? -29.964 17.468  8.348   1.00 10.03 ? 302 A1AO8 A N14 1 
HETATM 1843 O  O15 . A1AO8 C 3 .   ? -29.613 18.445  10.320  1.00 11.78 ? 302 A1AO8 A O15 1 
HETATM 1844 O  O16 . A1AO8 C 3 .   ? -30.102 20.982  5.522   1.00 11.88 ? 302 A1AO8 A O16 1 
HETATM 1845 C  C18 . A1AO8 C 3 .   ? -25.337 24.299  3.449   1.00 9.29  ? 302 A1AO8 A C18 1 
HETATM 1846 O  O19 . A1AO8 C 3 .   ? -28.730 19.710  4.355   1.00 10.56 ? 302 A1AO8 A O19 1 
HETATM 1847 F  F21 . A1AO8 C 3 .   ? -24.940 19.785  11.426  1.00 12.82 ? 302 A1AO8 A F21 1 
HETATM 1848 C  C23 . A1AO8 C 3 .   ? -26.365 24.605  5.608   1.00 10.48 ? 302 A1AO8 A C23 1 
HETATM 1849 C  C25 . A1AO8 C 3 .   ? -30.127 17.547  6.917   1.00 10.05 ? 302 A1AO8 A C25 1 
HETATM 1850 C  C27 . A1AO8 C 3 .   ? -25.860 25.137  4.459   1.00 9.91  ? 302 A1AO8 A C27 1 
HETATM 1851 C  C29 . A1AO8 C 3 .   ? -24.318 22.602  1.466   1.00 8.99  ? 302 A1AO8 A C29 1 
HETATM 1852 C  C30 . A1AO8 C 3 .   ? -24.281 23.981  1.296   1.00 9.62  ? 302 A1AO8 A C30 1 
HETATM 1853 S  S   . DMS   D 4 .   ? -18.232 32.352  6.778   1.00 22.69 ? 303 DMS   A S   1 
HETATM 1854 O  O   . DMS   D 4 .   ? -19.287 32.092  5.745   1.00 17.86 ? 303 DMS   A O   1 
HETATM 1855 C  C1  . DMS   D 4 .   ? -18.935 33.428  8.031   1.00 22.04 ? 303 DMS   A C1  1 
HETATM 1856 C  C2  . DMS   D 4 .   ? -18.143 30.855  7.739   1.00 21.50 ? 303 DMS   A C2  1 
HETATM 1857 S  S   . DMS   E 4 .   ? -19.086 25.237  11.444  0.50 38.94 ? 304 DMS   A S   1 
HETATM 1858 O  O   . DMS   E 4 .   ? -19.730 24.238  12.348  0.50 34.22 ? 304 DMS   A O   1 
HETATM 1859 C  C1  . DMS   E 4 .   ? -17.872 24.314  10.547  0.50 36.56 ? 304 DMS   A C1  1 
HETATM 1860 C  C2  . DMS   E 4 .   ? -20.246 25.485  10.129  0.50 37.84 ? 304 DMS   A C2  1 
HETATM 1861 O  O   . HOH   F 5 .   ? -21.205 23.243  13.853  1.00 43.36 ? 401 HOH   A O   1 
HETATM 1862 O  O   . HOH   F 5 .   ? -16.433 40.563  -11.962 1.00 24.46 ? 402 HOH   A O   1 
HETATM 1863 O  O   . HOH   F 5 .   ? -13.456 -3.085  1.724   1.00 32.18 ? 403 HOH   A O   1 
HETATM 1864 O  O   . HOH   F 5 .   ? -39.476 14.188  -14.623 1.00 31.60 ? 404 HOH   A O   1 
HETATM 1865 O  O   . HOH   F 5 .   ? -9.353  25.299  -9.298  1.00 26.18 ? 405 HOH   A O   1 
HETATM 1866 O  O   . HOH   F 5 .   ? -40.464 16.850  -2.396  1.00 31.50 ? 406 HOH   A O   1 
HETATM 1867 O  O   . HOH   F 5 .   ? -6.144  11.322  1.065   1.00 13.88 ? 407 HOH   A O   1 
HETATM 1868 O  O   . HOH   F 5 .   ? -22.977 -6.429  0.765   1.00 30.59 ? 408 HOH   A O   1 
HETATM 1869 O  O   . HOH   F 5 .   ? -27.161 11.816  -14.970 1.00 23.62 ? 409 HOH   A O   1 
HETATM 1870 O  O   . HOH   F 5 .   ? -22.309 8.049   -12.303 1.00 18.66 ? 410 HOH   A O   1 
HETATM 1871 O  O   . HOH   F 5 .   ? -12.464 14.941  16.235  1.00 31.75 ? 411 HOH   A O   1 
HETATM 1872 O  O   . HOH   F 5 .   ? -7.141  18.645  11.056  1.00 36.26 ? 412 HOH   A O   1 
HETATM 1873 O  O   . HOH   F 5 .   ? -3.084  26.833  -0.948  1.00 34.97 ? 413 HOH   A O   1 
HETATM 1874 O  O   . HOH   F 5 .   ? -26.152 37.007  2.085   1.00 27.93 ? 414 HOH   A O   1 
HETATM 1875 O  O   . HOH   F 5 .   ? -21.373 36.131  -10.859 1.00 28.06 ? 415 HOH   A O   1 
HETATM 1876 O  O   . HOH   F 5 .   ? -15.358 25.346  15.833  1.00 30.74 ? 416 HOH   A O   1 
HETATM 1877 O  O   . HOH   F 5 .   ? -3.705  20.091  6.693   1.00 22.32 ? 417 HOH   A O   1 
HETATM 1878 O  O   . HOH   F 5 .   ? -38.755 18.549  -11.010 1.00 32.40 ? 418 HOH   A O   1 
HETATM 1879 O  O   . HOH   F 5 .   ? -21.523 -6.194  2.745   1.00 25.71 ? 419 HOH   A O   1 
HETATM 1880 O  O   . HOH   F 5 .   ? -35.155 1.731   9.072   1.00 12.70 ? 420 HOH   A O   1 
HETATM 1881 O  O   . HOH   F 5 .   ? -41.995 11.837  5.252   1.00 21.50 ? 421 HOH   A O   1 
HETATM 1882 O  O   . HOH   F 5 .   ? -30.777 29.146  4.116   1.00 19.13 ? 422 HOH   A O   1 
HETATM 1883 O  O   . HOH   F 5 .   ? -3.327  20.055  3.545   1.00 26.12 ? 423 HOH   A O   1 
HETATM 1884 O  O   . HOH   F 5 .   ? -17.719 2.044   -9.068  1.00 24.23 ? 424 HOH   A O   1 
HETATM 1885 O  O   . HOH   F 5 .   ? -21.094 -4.234  14.463  1.00 40.44 ? 425 HOH   A O   1 
HETATM 1886 O  O   . HOH   F 5 .   ? -15.603 -0.203  -2.006  1.00 25.89 ? 426 HOH   A O   1 
HETATM 1887 O  O   . HOH   F 5 .   ? -8.944  33.147  0.426   1.00 29.05 ? 427 HOH   A O   1 
HETATM 1888 O  O   . HOH   F 5 .   ? -12.171 -4.738  9.806   1.00 27.16 ? 428 HOH   A O   1 
HETATM 1889 O  O   . HOH   F 5 .   ? -19.695 33.724  -13.903 1.00 23.10 ? 429 HOH   A O   1 
HETATM 1890 O  O   . HOH   F 5 .   ? -45.084 17.929  -5.249  1.00 31.53 ? 430 HOH   A O   1 
HETATM 1891 O  O   . HOH   F 5 .   ? -39.322 7.824   -8.385  1.00 9.94  ? 431 HOH   A O   1 
HETATM 1892 O  O   . HOH   F 5 .   ? -26.412 23.365  -14.821 1.00 27.02 ? 432 HOH   A O   1 
HETATM 1893 O  O   . HOH   F 5 .   ? -29.633 2.927   -14.860 1.00 12.10 ? 433 HOH   A O   1 
HETATM 1894 O  O   . HOH   F 5 .   ? -37.339 7.033   8.597   1.00 25.43 ? 434 HOH   A O   1 
HETATM 1895 O  O   . HOH   F 5 .   ? -17.723 4.697   -4.555  1.00 15.22 ? 435 HOH   A O   1 
HETATM 1896 O  O   . HOH   F 5 .   ? -29.481 14.257  11.528  1.00 24.50 ? 436 HOH   A O   1 
HETATM 1897 O  O   . HOH   F 5 .   ? -23.163 27.232  -1.733  1.00 22.93 ? 437 HOH   A O   1 
HETATM 1898 O  O   . HOH   F 5 .   ? -34.630 7.029   -17.837 1.00 28.11 ? 438 HOH   A O   1 
HETATM 1899 O  O   . HOH   F 5 .   ? -33.764 -7.683  -9.896  1.00 14.35 ? 439 HOH   A O   1 
HETATM 1900 O  O   . HOH   F 5 .   ? -37.362 23.583  -5.794  1.00 24.78 ? 440 HOH   A O   1 
HETATM 1901 O  O   . HOH   F 5 .   ? -32.750 27.606  2.568   1.00 18.56 ? 441 HOH   A O   1 
HETATM 1902 O  O   . HOH   F 5 .   ? -30.099 -8.520  8.848   1.00 24.79 ? 442 HOH   A O   1 
HETATM 1903 O  O   . HOH   F 5 .   ? -7.934  18.564  -10.352 1.00 22.54 ? 443 HOH   A O   1 
HETATM 1904 O  O   . HOH   F 5 .   ? -27.385 -6.936  5.961   1.00 17.48 ? 444 HOH   A O   1 
HETATM 1905 O  O   . HOH   F 5 .   ? -36.861 18.196  12.398  1.00 22.57 ? 445 HOH   A O   1 
HETATM 1906 O  O   . HOH   F 5 .   ? -12.201 29.456  -10.587 1.00 35.61 ? 446 HOH   A O   1 
HETATM 1907 O  O   . HOH   F 5 .   ? -30.988 4.448   -6.734  1.00 8.09  ? 447 HOH   A O   1 
HETATM 1908 O  O   . HOH   F 5 .   ? -17.112 18.463  7.214   1.00 7.90  ? 448 HOH   A O   1 
HETATM 1909 O  O   . HOH   F 5 .   ? -35.398 -4.731  -2.057  1.00 10.26 ? 449 HOH   A O   1 
HETATM 1910 O  O   . HOH   F 5 .   ? -21.671 -1.734  -9.758  1.00 22.64 ? 450 HOH   A O   1 
HETATM 1911 O  O   . HOH   F 5 .   ? -25.847 29.778  -5.055  1.00 14.95 ? 451 HOH   A O   1 
HETATM 1912 O  O   . HOH   F 5 .   ? -8.593  -0.575  6.563   1.00 21.85 ? 452 HOH   A O   1 
HETATM 1913 O  O   . HOH   F 5 .   ? -33.314 22.182  -13.061 1.00 26.83 ? 453 HOH   A O   1 
HETATM 1914 O  O   . HOH   F 5 .   ? -13.237 15.853  7.659   1.00 9.24  ? 454 HOH   A O   1 
HETATM 1915 O  O   . HOH   F 5 .   ? -29.574 17.281  3.491   1.00 14.27 ? 455 HOH   A O   1 
HETATM 1916 O  O   . HOH   F 5 .   ? -9.561  4.445   -10.601 1.00 34.86 ? 456 HOH   A O   1 
HETATM 1917 O  O   . HOH   F 5 .   ? -14.760 21.787  8.913   1.00 7.95  ? 457 HOH   A O   1 
HETATM 1918 O  O   . HOH   F 5 .   ? -29.669 -10.282 2.416   1.00 27.00 ? 458 HOH   A O   1 
HETATM 1919 O  O   . HOH   F 5 .   ? -37.712 5.478   10.937  1.00 29.15 ? 459 HOH   A O   1 
HETATM 1920 O  O   . HOH   F 5 .   ? -18.770 29.912  0.405   1.00 8.81  ? 460 HOH   A O   1 
HETATM 1921 O  O   . HOH   F 5 .   ? -9.595  33.812  5.245   1.00 15.03 ? 461 HOH   A O   1 
HETATM 1922 O  O   . HOH   F 5 .   ? -25.944 32.885  -2.959  1.00 34.83 ? 462 HOH   A O   1 
HETATM 1923 O  O   . HOH   F 5 .   ? -22.487 -7.725  5.595   1.00 23.86 ? 463 HOH   A O   1 
HETATM 1924 O  O   . HOH   F 5 .   ? -20.199 27.345  -8.611  1.00 11.70 ? 464 HOH   A O   1 
HETATM 1925 O  O   . HOH   F 5 .   ? -42.193 11.731  8.069   1.00 17.99 ? 465 HOH   A O   1 
HETATM 1926 O  O   . HOH   F 5 .   ? -12.154 7.540   -13.844 1.00 35.51 ? 466 HOH   A O   1 
HETATM 1927 O  O   . HOH   F 5 .   ? -35.435 14.446  12.189  1.00 21.82 ? 467 HOH   A O   1 
HETATM 1928 O  O   . HOH   F 5 .   ? -43.446 16.456  -8.848  1.00 20.17 ? 468 HOH   A O   1 
HETATM 1929 O  O   . HOH   F 5 .   ? -35.140 -1.391  -8.242  1.00 7.83  ? 469 HOH   A O   1 
HETATM 1930 O  O   . HOH   F 5 .   ? -41.814 -3.055  -13.192 1.00 9.65  ? 470 HOH   A O   1 
HETATM 1931 O  O   . HOH   F 5 .   ? -15.497 33.355  8.776   1.00 20.32 ? 471 HOH   A O   1 
HETATM 1932 O  O   . HOH   F 5 .   ? -19.306 9.448   16.313  1.00 18.08 ? 472 HOH   A O   1 
HETATM 1933 O  O   . HOH   F 5 .   ? -18.882 3.722   13.828  1.00 20.92 ? 473 HOH   A O   1 
HETATM 1934 O  O   . HOH   F 5 .   ? -4.889  17.942  8.696   1.00 33.51 ? 474 HOH   A O   1 
HETATM 1935 O  O   . HOH   F 5 .   ? -3.983  24.528  -8.241  1.00 42.92 ? 475 HOH   A O   1 
HETATM 1936 O  O   . HOH   F 5 .   ? -3.853  21.602  -8.720  1.00 27.26 ? 476 HOH   A O   1 
HETATM 1937 O  O   . HOH   F 5 .   ? -16.667 8.037   19.322  1.00 33.36 ? 477 HOH   A O   1 
HETATM 1938 O  O   . HOH   F 5 .   ? -26.469 5.640   -16.259 1.00 25.92 ? 478 HOH   A O   1 
HETATM 1939 O  O   . HOH   F 5 .   ? -9.238  8.932   -4.243  1.00 26.83 ? 479 HOH   A O   1 
HETATM 1940 O  O   . HOH   F 5 .   ? -30.049 20.544  12.048  1.00 28.54 ? 480 HOH   A O   1 
HETATM 1941 O  O   . HOH   F 5 .   ? -9.167  17.247  13.065  1.00 21.81 ? 481 HOH   A O   1 
HETATM 1942 O  O   . HOH   F 5 .   ? -2.542  12.689  6.040   1.00 32.39 ? 482 HOH   A O   1 
HETATM 1943 O  O   . HOH   F 5 .   ? -26.510 27.192  -13.838 1.00 27.27 ? 483 HOH   A O   1 
HETATM 1944 O  O   . HOH   F 5 .   ? -9.407  21.231  -0.556  1.00 9.68  ? 484 HOH   A O   1 
HETATM 1945 O  O   . HOH   F 5 .   ? -18.277 -8.606  5.186   1.00 43.87 ? 485 HOH   A O   1 
HETATM 1946 O  O   . HOH   F 5 .   ? -46.920 -2.418  -9.640  1.00 9.05  ? 486 HOH   A O   1 
HETATM 1947 O  O   . HOH   F 5 .   ? -5.970  8.742   6.210   1.00 28.49 ? 487 HOH   A O   1 
HETATM 1948 O  O   . HOH   F 5 .   ? -29.075 30.121  -10.150 1.00 36.85 ? 488 HOH   A O   1 
HETATM 1949 O  O   . HOH   F 5 .   ? -38.440 18.848  8.824   1.00 20.90 ? 489 HOH   A O   1 
HETATM 1950 O  O   . HOH   F 5 .   ? -11.211 11.898  -2.472  1.00 10.01 ? 490 HOH   A O   1 
HETATM 1951 O  O   . HOH   F 5 .   ? -36.078 26.211  -8.786  1.00 38.51 ? 491 HOH   A O   1 
HETATM 1952 O  O   . HOH   F 5 .   ? -12.975 -9.558  5.939   1.00 45.06 ? 492 HOH   A O   1 
HETATM 1953 O  O   . HOH   F 5 .   ? -29.005 16.182  -16.411 1.00 19.29 ? 493 HOH   A O   1 
HETATM 1954 O  O   . HOH   F 5 .   ? -11.546 10.633  -9.965  1.00 16.05 ? 494 HOH   A O   1 
HETATM 1955 O  O   . HOH   F 5 .   ? -12.178 18.577  15.108  1.00 20.14 ? 495 HOH   A O   1 
HETATM 1956 O  O   . HOH   F 5 .   ? -2.230  10.513  -3.352  1.00 35.48 ? 496 HOH   A O   1 
HETATM 1957 O  O   . HOH   F 5 .   ? -23.949 1.746   -10.233 1.00 21.75 ? 497 HOH   A O   1 
HETATM 1958 O  O   . HOH   F 5 .   ? -33.839 23.395  4.919   1.00 35.61 ? 498 HOH   A O   1 
HETATM 1959 O  O   . HOH   F 5 .   ? -13.268 32.098  -9.299  1.00 15.73 ? 499 HOH   A O   1 
HETATM 1960 O  O   . HOH   F 5 .   ? -40.205 10.943  15.523  1.00 25.58 ? 500 HOH   A O   1 
HETATM 1961 O  O   . HOH   F 5 .   ? -22.508 1.519   15.560  1.00 35.92 ? 501 HOH   A O   1 
HETATM 1962 O  O   . HOH   F 5 .   ? -38.266 12.785  13.077  1.00 16.11 ? 502 HOH   A O   1 
HETATM 1963 O  O   . HOH   F 5 .   ? -36.574 -5.297  6.682   1.00 30.08 ? 503 HOH   A O   1 
HETATM 1964 O  O   . HOH   F 5 .   ? -31.917 19.312  -5.931  1.00 8.11  ? 504 HOH   A O   1 
HETATM 1965 O  O   . HOH   F 5 .   ? -25.757 19.249  -15.192 1.00 17.35 ? 505 HOH   A O   1 
HETATM 1966 O  O   . HOH   F 5 .   ? -28.590 34.345  -0.853  1.00 20.67 ? 506 HOH   A O   1 
HETATM 1967 O  O   . HOH   F 5 .   ? -8.195  19.326  -3.587  1.00 11.59 ? 507 HOH   A O   1 
HETATM 1968 O  O   . HOH   F 5 .   ? -24.014 17.033  -14.204 1.00 21.13 ? 508 HOH   A O   1 
HETATM 1969 O  O   . HOH   F 5 .   ? -23.303 -9.193  -2.072  1.00 22.49 ? 509 HOH   A O   1 
HETATM 1970 O  O   . HOH   F 5 .   ? -32.741 4.947   -10.037 1.00 7.60  ? 510 HOH   A O   1 
HETATM 1971 O  O   . HOH   F 5 .   ? -27.263 13.726  13.963  1.00 32.17 ? 511 HOH   A O   1 
HETATM 1972 O  O   . HOH   F 5 .   ? -30.493 23.050  7.380   1.00 19.82 ? 512 HOH   A O   1 
HETATM 1973 O  O   . HOH   F 5 .   ? -9.692  -0.589  -9.237  1.00 35.77 ? 513 HOH   A O   1 
HETATM 1974 O  O   . HOH   F 5 .   ? -30.941 22.412  -9.987  1.00 10.88 ? 514 HOH   A O   1 
HETATM 1975 O  O   . HOH   F 5 .   ? -36.398 7.008   2.435   1.00 11.47 ? 515 HOH   A O   1 
HETATM 1976 O  O   . HOH   F 5 .   ? -19.769 33.155  -3.932  1.00 12.99 ? 516 HOH   A O   1 
HETATM 1977 O  O   . HOH   F 5 .   ? -16.677 -5.388  1.314   1.00 36.11 ? 517 HOH   A O   1 
HETATM 1978 O  O   . HOH   F 5 .   ? -19.328 6.302   16.385  1.00 36.41 ? 518 HOH   A O   1 
HETATM 1979 O  O   . HOH   F 5 .   ? -24.429 16.740  14.036  1.00 26.19 ? 519 HOH   A O   1 
HETATM 1980 O  O   . HOH   F 5 .   ? -7.931  9.536   -7.091  1.00 32.15 ? 520 HOH   A O   1 
HETATM 1981 O  O   . HOH   F 5 .   ? -10.347 7.689   9.700   1.00 21.91 ? 521 HOH   A O   1 
HETATM 1982 O  O   . HOH   F 5 .   ? -33.181 9.230   -10.868 1.00 8.69  ? 522 HOH   A O   1 
HETATM 1983 O  O   . HOH   F 5 .   ? -21.025 23.367  -3.962  1.00 10.09 ? 523 HOH   A O   1 
HETATM 1984 O  O   . HOH   F 5 .   ? -15.905 16.072  6.668   1.00 8.18  ? 524 HOH   A O   1 
HETATM 1985 O  O   . HOH   F 5 .   ? -40.368 11.349  11.651  1.00 17.88 ? 525 HOH   A O   1 
HETATM 1986 O  O   . HOH   F 5 .   ? -22.533 -6.164  -2.195  1.00 20.32 ? 526 HOH   A O   1 
HETATM 1987 O  O   . HOH   F 5 .   ? -42.061 7.884   -10.392 1.00 18.31 ? 527 HOH   A O   1 
HETATM 1988 O  O   . HOH   F 5 .   ? -12.103 32.387  1.471   1.00 16.50 ? 528 HOH   A O   1 
HETATM 1989 O  O   . HOH   F 5 .   ? -24.659 13.161  14.149  1.00 14.92 ? 529 HOH   A O   1 
HETATM 1990 O  O   . HOH   F 5 .   ? -36.258 19.262  -16.486 1.00 41.57 ? 530 HOH   A O   1 
HETATM 1991 O  O   . HOH   F 5 .   ? -45.144 0.482   -7.714  1.00 24.59 ? 531 HOH   A O   1 
HETATM 1992 O  O   . HOH   F 5 .   ? -36.667 21.027  -9.197  1.00 23.57 ? 532 HOH   A O   1 
HETATM 1993 O  O   . HOH   F 5 .   ? -30.637 7.955   -10.705 1.00 8.38  ? 533 HOH   A O   1 
HETATM 1994 O  O   . HOH   F 5 .   ? -30.299 14.645  -1.736  1.00 7.69  ? 534 HOH   A O   1 
HETATM 1995 O  O   . HOH   F 5 .   ? -25.895 -7.025  11.116  1.00 28.00 ? 535 HOH   A O   1 
HETATM 1996 O  O   . HOH   F 5 .   ? -41.588 -0.407  -5.506  1.00 14.41 ? 536 HOH   A O   1 
HETATM 1997 O  O   . HOH   F 5 .   ? -31.775 6.793   -8.132  1.00 7.24  ? 537 HOH   A O   1 
HETATM 1998 O  O   . HOH   F 5 .   ? -28.165 27.168  7.937   1.00 30.03 ? 538 HOH   A O   1 
HETATM 1999 O  O   . HOH   F 5 .   ? -27.560 14.365  -2.346  1.00 6.97  ? 539 HOH   A O   1 
HETATM 2000 O  O   . HOH   F 5 .   ? -33.462 -1.617  12.474  1.00 10.01 ? 540 HOH   A O   1 
HETATM 2001 O  O   . HOH   F 5 .   ? -40.310 12.319  1.106   1.00 16.60 ? 541 HOH   A O   1 
HETATM 2002 O  O   . HOH   F 5 .   ? -22.350 5.230   15.217  1.00 26.45 ? 542 HOH   A O   1 
HETATM 2003 O  O   . HOH   F 5 .   ? -32.231 18.040  -17.648 1.00 40.85 ? 543 HOH   A O   1 
HETATM 2004 O  O   . HOH   F 5 .   ? -32.482 19.767  4.484   1.00 27.62 ? 544 HOH   A O   1 
HETATM 2005 O  O   . HOH   F 5 .   ? -10.427 21.274  -3.090  1.00 9.25  ? 545 HOH   A O   1 
HETATM 2006 O  O   . HOH   F 5 .   ? -31.342 25.281  -12.707 1.00 28.02 ? 546 HOH   A O   1 
HETATM 2007 O  O   . HOH   F 5 .   ? -33.087 6.509   -4.826  1.00 6.04  ? 547 HOH   A O   1 
HETATM 2008 O  O   . HOH   F 5 .   ? -31.509 26.576  -9.239  1.00 13.64 ? 548 HOH   A O   1 
HETATM 2009 O  O   . HOH   F 5 .   ? -3.660  4.914   -4.355  1.00 30.08 ? 549 HOH   A O   1 
HETATM 2010 O  O   . HOH   F 5 .   ? -17.261 -2.307  13.273  1.00 27.96 ? 550 HOH   A O   1 
HETATM 2011 O  O   . HOH   F 5 .   ? -13.838 32.003  -2.290  1.00 8.60  ? 551 HOH   A O   1 
HETATM 2012 O  O   . HOH   F 5 .   ? -38.796 7.876   3.156   1.00 36.29 ? 552 HOH   A O   1 
HETATM 2013 O  O   . HOH   F 5 .   ? -8.757  13.214  -2.589  1.00 10.44 ? 553 HOH   A O   1 
HETATM 2014 O  O   . HOH   F 5 .   ? -37.438 -2.857  -8.804  1.00 9.09  ? 554 HOH   A O   1 
HETATM 2015 O  O   . HOH   F 5 .   ? -21.016 30.251  7.154   1.00 30.35 ? 555 HOH   A O   1 
HETATM 2016 O  O   . HOH   F 5 .   ? -5.639  13.087  3.149   1.00 19.47 ? 556 HOH   A O   1 
HETATM 2017 O  O   . HOH   F 5 .   ? -27.727 -0.517  -12.819 1.00 19.66 ? 557 HOH   A O   1 
HETATM 2018 O  O   . HOH   F 5 .   ? -11.325 -0.321  -0.950  1.00 27.29 ? 558 HOH   A O   1 
HETATM 2019 O  O   . HOH   F 5 .   ? -40.117 -1.064  -1.285  1.00 16.21 ? 559 HOH   A O   1 
HETATM 2020 O  O   . HOH   F 5 .   ? -27.213 7.498   15.405  1.00 24.37 ? 560 HOH   A O   1 
HETATM 2021 O  O   . HOH   F 5 .   ? -5.672  23.256  5.652   1.00 5.68  ? 561 HOH   A O   1 
HETATM 2022 O  O   . HOH   F 5 .   ? -21.756 27.358  0.559   1.00 11.64 ? 562 HOH   A O   1 
HETATM 2023 O  O   . HOH   F 5 .   ? -10.139 6.849   -6.168  1.00 28.95 ? 563 HOH   A O   1 
HETATM 2024 O  O   . HOH   F 5 .   ? -26.879 16.851  12.824  1.00 28.68 ? 564 HOH   A O   1 
HETATM 2025 O  O   . HOH   F 5 .   ? -12.209 1.842   1.293   1.00 21.69 ? 565 HOH   A O   1 
HETATM 2026 O  O   . HOH   F 5 .   ? -9.084  27.610  -7.439  1.00 15.18 ? 566 HOH   A O   1 
HETATM 2027 O  O   . HOH   F 5 .   ? -35.863 3.562   22.442  1.00 24.79 ? 567 HOH   A O   1 
HETATM 2028 O  O   . HOH   F 5 .   ? -15.606 27.984  12.816  1.00 28.50 ? 568 HOH   A O   1 
HETATM 2029 O  O   . HOH   F 5 .   ? -46.576 7.921   -4.439  1.00 28.04 ? 569 HOH   A O   1 
HETATM 2030 O  O   . HOH   F 5 .   ? -15.636 25.969  9.212   1.00 10.27 ? 570 HOH   A O   1 
HETATM 2031 O  O   . HOH   F 5 .   ? -23.789 40.026  -1.888  1.00 36.86 ? 571 HOH   A O   1 
HETATM 2032 O  O   . HOH   F 5 .   ? -12.493 7.019   -4.655  1.00 23.73 ? 572 HOH   A O   1 
HETATM 2033 O  O   . HOH   F 5 .   ? -30.467 4.483   17.055  1.00 24.71 ? 573 HOH   A O   1 
HETATM 2034 O  O   . HOH   F 5 .   ? -16.072 29.326  10.480  1.00 13.26 ? 574 HOH   A O   1 
HETATM 2035 O  O   . HOH   F 5 .   ? -4.680  15.413  8.644   1.00 22.17 ? 575 HOH   A O   1 
HETATM 2036 O  O   . HOH   F 5 .   ? -15.130 32.391  -13.291 1.00 33.11 ? 576 HOH   A O   1 
HETATM 2037 O  O   . HOH   F 5 .   ? -38.304 4.177   2.442   1.00 35.30 ? 577 HOH   A O   1 
HETATM 2038 O  O   . HOH   F 5 .   ? -7.516  1.889   2.271   1.00 35.35 ? 578 HOH   A O   1 
HETATM 2039 O  O   . HOH   F 5 .   ? -37.075 20.498  17.575  1.00 38.30 ? 579 HOH   A O   1 
HETATM 2040 O  O   . HOH   F 5 .   ? -37.724 6.695   15.537  1.00 20.37 ? 580 HOH   A O   1 
HETATM 2041 O  O   . HOH   F 5 .   ? -16.349 5.385   -6.757  1.00 13.52 ? 581 HOH   A O   1 
HETATM 2042 O  O   . HOH   F 5 .   ? -23.765 30.355  7.017   1.00 18.08 ? 582 HOH   A O   1 
HETATM 2043 O  O   . HOH   F 5 .   ? -35.033 6.807   21.819  1.00 35.49 ? 583 HOH   A O   1 
HETATM 2044 O  O   . HOH   F 5 .   ? -32.894 -3.406  4.209   1.00 16.94 ? 584 HOH   A O   1 
HETATM 2045 O  O   . HOH   F 5 .   ? -24.618 32.824  4.941   1.00 13.16 ? 585 HOH   A O   1 
HETATM 2046 O  O   . HOH   F 5 .   ? -22.164 32.527  6.330   1.00 31.14 ? 586 HOH   A O   1 
HETATM 2047 O  O   . HOH   F 5 .   ? -7.562  1.677   -9.366  1.00 35.49 ? 587 HOH   A O   1 
HETATM 2048 O  O   . HOH   F 5 .   ? -33.432 20.147  -16.515 1.00 28.80 ? 588 HOH   A O   1 
HETATM 2049 O  O   . HOH   F 5 .   ? -32.519 29.678  -7.425  1.00 34.62 ? 589 HOH   A O   1 
HETATM 2050 O  O   . HOH   F 5 .   ? -41.309 13.912  -12.591 1.00 23.00 ? 590 HOH   A O   1 
HETATM 2051 O  O   . HOH   F 5 .   ? -36.696 -5.987  -4.442  1.00 14.34 ? 591 HOH   A O   1 
HETATM 2052 O  O   . HOH   F 5 .   ? -12.387 18.348  -15.572 1.00 23.14 ? 592 HOH   A O   1 
HETATM 2053 O  O   . HOH   F 5 .   ? -34.143 -6.518  -0.608  1.00 19.16 ? 593 HOH   A O   1 
HETATM 2054 O  O   . HOH   F 5 .   ? -21.328 -9.506  2.576   1.00 30.90 ? 594 HOH   A O   1 
HETATM 2055 O  O   . HOH   F 5 .   ? -28.418 13.234  -16.668 1.00 26.10 ? 595 HOH   A O   1 
HETATM 2056 O  O   . HOH   F 5 .   ? -30.995 6.134   -17.132 1.00 18.24 ? 596 HOH   A O   1 
HETATM 2057 O  O   . HOH   F 5 .   ? -19.929 6.236   -12.200 1.00 31.63 ? 597 HOH   A O   1 
HETATM 2058 O  O   . HOH   F 5 .   ? -32.472 25.175  7.348   1.00 28.85 ? 598 HOH   A O   1 
HETATM 2059 O  O   . HOH   F 5 .   ? -33.586 11.594  18.548  1.00 22.29 ? 599 HOH   A O   1 
HETATM 2060 O  O   . HOH   F 5 .   ? -30.710 31.083  -3.845  1.00 18.93 ? 600 HOH   A O   1 
HETATM 2061 O  O   . HOH   F 5 .   ? -18.217 12.192  -13.061 1.00 16.62 ? 601 HOH   A O   1 
HETATM 2062 O  O   . HOH   F 5 .   ? -34.926 -1.015  -13.006 1.00 10.43 ? 602 HOH   A O   1 
HETATM 2063 O  O   . HOH   F 5 .   ? -18.690 16.441  18.988  1.00 29.84 ? 603 HOH   A O   1 
HETATM 2064 O  O   . HOH   F 5 .   ? -35.963 20.242  -13.280 1.00 30.24 ? 604 HOH   A O   1 
HETATM 2065 O  O   . HOH   F 5 .   ? -34.193 -4.012  -14.359 1.00 22.75 ? 605 HOH   A O   1 
HETATM 2066 O  O   . HOH   F 5 .   ? -18.408 25.603  -10.055 1.00 13.35 ? 606 HOH   A O   1 
HETATM 2067 O  O   . HOH   F 5 .   ? -28.747 -9.422  5.532   1.00 36.37 ? 607 HOH   A O   1 
HETATM 2068 O  O   . HOH   F 5 .   ? -23.623 19.737  14.635  1.00 34.79 ? 608 HOH   A O   1 
HETATM 2069 O  O   . HOH   F 5 .   ? -23.963 -3.467  -8.458  1.00 15.25 ? 609 HOH   A O   1 
HETATM 2070 O  O   . HOH   F 5 .   ? -16.377 14.567  -13.779 1.00 16.79 ? 610 HOH   A O   1 
HETATM 2071 O  O   . HOH   F 5 .   ? -12.088 27.798  14.595  1.00 37.35 ? 611 HOH   A O   1 
HETATM 2072 O  O   . HOH   F 5 .   ? -16.365 4.340   -9.480  1.00 22.50 ? 612 HOH   A O   1 
HETATM 2073 O  O   . HOH   F 5 .   ? -20.943 11.560  -13.004 1.00 15.25 ? 613 HOH   A O   1 
HETATM 2074 O  O   . HOH   F 5 .   ? -41.851 0.537   -2.753  1.00 28.15 ? 614 HOH   A O   1 
HETATM 2075 O  O   . HOH   F 5 .   ? -30.948 14.231  13.273  1.00 37.51 ? 615 HOH   A O   1 
HETATM 2076 O  O   . HOH   F 5 .   ? -14.184 -1.816  -3.550  1.00 31.70 ? 616 HOH   A O   1 
HETATM 2077 O  O   . HOH   F 5 .   ? -22.124 19.098  -18.471 1.00 44.29 ? 617 HOH   A O   1 
HETATM 2078 O  O   . HOH   F 5 .   ? -39.993 20.109  -7.339  1.00 20.80 ? 618 HOH   A O   1 
HETATM 2079 O  O   . HOH   F 5 .   ? -4.820  32.537  -4.337  1.00 28.79 ? 619 HOH   A O   1 
HETATM 2080 O  O   . HOH   F 5 .   ? -9.896  8.726   -10.568 1.00 30.07 ? 620 HOH   A O   1 
HETATM 2081 O  O   . HOH   F 5 .   ? -27.516 -3.435  -11.055 1.00 21.99 ? 621 HOH   A O   1 
HETATM 2082 O  O   . HOH   F 5 .   ? -39.895 9.200   -11.348 1.00 12.84 ? 622 HOH   A O   1 
HETATM 2083 O  O   . HOH   F 5 .   ? -35.856 -3.740  4.509   1.00 16.58 ? 623 HOH   A O   1 
HETATM 2084 O  O   . HOH   F 5 .   ? -10.644 7.349   -2.681  1.00 21.36 ? 624 HOH   A O   1 
HETATM 2085 O  O   . HOH   F 5 .   ? -3.038  19.820  -3.365  1.00 27.36 ? 625 HOH   A O   1 
HETATM 2086 O  O   . HOH   F 5 .   ? -19.956 37.660  -2.154  1.00 28.92 ? 626 HOH   A O   1 
HETATM 2087 O  O   . HOH   F 5 .   ? -40.756 20.735  -5.207  1.00 30.80 ? 627 HOH   A O   1 
HETATM 2088 O  O   . HOH   F 5 .   ? -34.375 31.594  -3.620  1.00 24.56 ? 628 HOH   A O   1 
HETATM 2089 O  O   . HOH   F 5 .   ? -9.850  31.541  12.823  1.00 16.77 ? 629 HOH   A O   1 
HETATM 2090 O  O   . HOH   F 5 .   ? -6.144  19.505  -11.887 1.00 31.55 ? 630 HOH   A O   1 
HETATM 2091 O  O   . HOH   F 5 .   ? -6.634  13.250  10.346  1.00 34.71 ? 631 HOH   A O   1 
HETATM 2092 O  O   . HOH   F 5 .   ? -20.224 18.570  -19.835 1.00 41.11 ? 632 HOH   A O   1 
HETATM 2093 O  O   . HOH   F 5 .   ? -10.013 12.920  -10.840 1.00 32.05 ? 633 HOH   A O   1 
HETATM 2094 O  O   . HOH   F 5 .   ? -9.330  6.485   7.445   1.00 16.07 ? 634 HOH   A O   1 
HETATM 2095 O  O   . HOH   F 5 .   ? -2.809  27.546  -4.794  1.00 28.65 ? 635 HOH   A O   1 
HETATM 2096 O  O   . HOH   F 5 .   ? -15.290 27.489  -13.412 1.00 24.13 ? 636 HOH   A O   1 
HETATM 2097 O  O   . HOH   F 5 .   ? -34.152 18.316  6.049   1.00 14.09 ? 637 HOH   A O   1 
HETATM 2098 O  O   . HOH   F 5 .   ? -24.144 21.808  -14.730 1.00 12.19 ? 638 HOH   A O   1 
HETATM 2099 O  O   . HOH   F 5 .   ? -10.455 -3.094  -5.145  1.00 41.03 ? 639 HOH   A O   1 
HETATM 2100 O  O   . HOH   F 5 .   ? -3.062  12.387  2.939   1.00 42.38 ? 640 HOH   A O   1 
HETATM 2101 O  O   . HOH   F 5 .   ? -24.006 5.600   -13.489 1.00 39.68 ? 641 HOH   A O   1 
HETATM 2102 O  O   . HOH   F 5 .   ? -42.020 12.651  -0.969  1.00 35.39 ? 642 HOH   A O   1 
HETATM 2103 O  O   . HOH   F 5 .   ? -1.686  17.974  0.052   1.00 33.57 ? 643 HOH   A O   1 
HETATM 2104 O  O   . HOH   F 5 .   ? -4.164  0.203   -6.497  1.00 40.36 ? 644 HOH   A O   1 
HETATM 2105 O  O   . HOH   F 5 .   ? -33.979 21.150  2.837   1.00 39.85 ? 645 HOH   A O   1 
HETATM 2106 O  O   . HOH   F 5 .   ? -24.068 30.445  -12.512 1.00 34.44 ? 646 HOH   A O   1 
HETATM 2107 O  O   . HOH   F 5 .   ? -30.229 16.476  12.792  1.00 30.96 ? 647 HOH   A O   1 
HETATM 2108 O  O   . HOH   F 5 .   ? -39.242 -0.880  4.450   1.00 28.86 ? 648 HOH   A O   1 
HETATM 2109 O  O   . HOH   F 5 .   ? -40.074 7.177   0.257   1.00 28.65 ? 649 HOH   A O   1 
HETATM 2110 O  O   . HOH   F 5 .   ? -34.814 1.211   11.779  1.00 11.65 ? 650 HOH   A O   1 
HETATM 2111 O  O   . HOH   F 5 .   ? -26.411 1.030   17.223  1.00 33.26 ? 651 HOH   A O   1 
HETATM 2112 O  O   . HOH   F 5 .   ? -37.214 -3.437  -0.489  1.00 26.13 ? 652 HOH   A O   1 
HETATM 2113 O  O   . HOH   F 5 .   ? -29.575 33.080  4.100   1.00 32.79 ? 653 HOH   A O   1 
HETATM 2114 O  O   . HOH   F 5 .   ? -22.867 33.960  -7.490  1.00 45.47 ? 654 HOH   A O   1 
HETATM 2115 O  O   . HOH   F 5 .   ? -6.902  24.933  -9.247  1.00 36.39 ? 655 HOH   A O   1 
HETATM 2116 O  O   . HOH   F 5 .   ? -38.891 14.355  22.420  1.00 33.52 ? 656 HOH   A O   1 
HETATM 2117 O  O   . HOH   F 5 .   ? -14.487 -2.162  12.430  1.00 38.40 ? 657 HOH   A O   1 
HETATM 2118 O  O   . HOH   F 5 .   ? -12.138 -3.612  12.614  1.00 40.07 ? 658 HOH   A O   1 
HETATM 2119 O  O   . HOH   F 5 .   ? -18.260 18.620  20.053  1.00 44.91 ? 659 HOH   A O   1 
HETATM 2120 O  O   . HOH   F 5 .   ? -24.791 26.949  7.959   1.00 38.18 ? 660 HOH   A O   1 
HETATM 2121 O  O   . HOH   F 5 .   ? -18.979 -5.564  2.881   1.00 31.86 ? 661 HOH   A O   1 
HETATM 2122 O  O   . HOH   F 5 .   ? -14.733 -9.841  2.680   1.00 27.02 ? 662 HOH   A O   1 
HETATM 2123 O  O   . HOH   F 5 .   ? -7.619  14.849  12.208  1.00 25.55 ? 663 HOH   A O   1 
HETATM 2124 O  O   . HOH   F 5 .   ? -21.686 -10.046 8.357   1.00 43.19 ? 664 HOH   A O   1 
HETATM 2125 O  O   . HOH   F 5 .   ? -24.519 10.363  -15.202 1.00 37.28 ? 665 HOH   A O   1 
HETATM 2126 O  O   . HOH   F 5 .   ? -15.801 2.971   14.228  1.00 23.79 ? 666 HOH   A O   1 
HETATM 2127 O  O   . HOH   F 5 .   ? -30.978 2.750   19.388  1.00 40.57 ? 667 HOH   A O   1 
HETATM 2128 O  O   . HOH   F 5 .   ? -28.593 10.004  16.881  1.00 43.94 ? 668 HOH   A O   1 
HETATM 2129 O  O   . HOH   F 5 .   ? -9.319  31.363  -3.883  1.00 23.84 ? 669 HOH   A O   1 
HETATM 2130 O  O   . HOH   F 5 .   ? -0.449  14.636  1.942   1.00 49.51 ? 670 HOH   A O   1 
HETATM 2131 O  O   . HOH   F 5 .   ? -8.974  10.467  10.406  1.00 40.97 ? 671 HOH   A O   1 
HETATM 2132 O  O   . HOH   F 5 .   ? -36.440 -8.688  -6.957  1.00 24.50 ? 672 HOH   A O   1 
HETATM 2133 O  O   . HOH   F 5 .   ? -33.448 15.013  -18.415 1.00 40.50 ? 673 HOH   A O   1 
HETATM 2134 O  O   . HOH   F 5 .   ? -23.618 38.277  3.958   1.00 41.29 ? 674 HOH   A O   1 
HETATM 2135 O  O   . HOH   F 5 .   ? -23.825 14.130  -17.335 1.00 48.80 ? 675 HOH   A O   1 
HETATM 2136 O  O   . HOH   F 5 .   ? -7.323  20.895  12.141  1.00 22.24 ? 676 HOH   A O   1 
HETATM 2137 O  O   . HOH   F 5 .   ? -16.627 -7.827  3.263   1.00 37.19 ? 677 HOH   A O   1 
HETATM 2138 O  O   . HOH   F 5 .   ? -12.613 29.642  -13.286 1.00 32.77 ? 678 HOH   A O   1 
HETATM 2139 O  O   . HOH   F 5 .   ? -8.947  35.855  10.280  1.00 37.96 ? 679 HOH   A O   1 
HETATM 2140 O  O   . HOH   F 5 .   ? -5.270  24.054  -10.849 1.00 44.73 ? 680 HOH   A O   1 
HETATM 2141 O  O   . HOH   F 5 .   ? -4.067  10.281  -0.342  1.00 46.28 ? 681 HOH   A O   1 
HETATM 2142 O  O   . HOH   F 5 .   ? -27.491 4.917   16.229  1.00 27.30 ? 682 HOH   A O   1 
HETATM 2143 O  O   . HOH   F 5 .   ? -38.577 -1.036  9.763   1.00 16.78 ? 683 HOH   A O   1 
HETATM 2144 O  O   . HOH   F 5 .   ? -11.523 35.131  11.171  1.00 38.49 ? 684 HOH   A O   1 
HETATM 2145 O  O   . HOH   F 5 .   ? -8.178  16.113  -14.247 1.00 43.88 ? 685 HOH   A O   1 
HETATM 2146 O  O   . HOH   F 5 .   ? -12.543 -7.404  10.236  1.00 38.10 ? 686 HOH   A O   1 
HETATM 2147 O  O   . HOH   F 5 .   ? -8.749  32.978  -2.170  1.00 32.48 ? 687 HOH   A O   1 
HETATM 2148 O  O   . HOH   F 5 .   ? -15.868 15.382  19.581  1.00 41.41 ? 688 HOH   A O   1 
HETATM 2149 O  O   . HOH   F 5 .   ? -28.706 6.491   -18.240 1.00 27.51 ? 689 HOH   A O   1 
HETATM 2150 O  O   . HOH   F 5 .   ? -13.991 -0.231  0.495   1.00 16.27 ? 690 HOH   A O   1 
HETATM 2151 O  O   . HOH   F 5 .   ? -35.423 22.877  -10.792 1.00 42.89 ? 691 HOH   A O   1 
HETATM 2152 O  O   . HOH   F 5 .   ? -19.819 39.367  -11.081 1.00 31.99 ? 692 HOH   A O   1 
HETATM 2153 O  O   . HOH   F 5 .   ? -37.539 4.765   17.539  1.00 15.23 ? 693 HOH   A O   1 
HETATM 2154 O  O   . HOH   F 5 .   ? -30.727 11.427  17.404  1.00 31.48 ? 694 HOH   A O   1 
HETATM 2155 O  O   . HOH   F 5 .   ? -37.090 2.212   13.101  1.00 11.72 ? 695 HOH   A O   1 
HETATM 2156 O  O   . HOH   F 5 .   ? -14.709 17.205  -16.893 1.00 46.56 ? 696 HOH   A O   1 
HETATM 2157 O  O   . HOH   F 5 .   ? -39.896 -2.748  7.997   1.00 25.65 ? 697 HOH   A O   1 
HETATM 2158 O  O   . HOH   F 5 .   ? -37.541 -8.705  -4.630  1.00 37.48 ? 698 HOH   A O   1 
HETATM 2159 O  O   . HOH   F 5 .   ? -12.379 -4.394  -0.871  1.00 40.25 ? 699 HOH   A O   1 
HETATM 2160 O  O   . HOH   F 5 .   ? -33.658 -6.623  -13.033 1.00 21.53 ? 700 HOH   A O   1 
HETATM 2161 O  O   . HOH   F 5 .   ? -27.480 -8.063  8.878   1.00 33.55 ? 701 HOH   A O   1 
HETATM 2162 O  O   . HOH   F 5 .   ? -17.804 26.364  -12.726 1.00 18.86 ? 702 HOH   A O   1 
HETATM 2163 O  O   . HOH   F 5 .   ? -37.721 1.103   8.345   1.00 18.74 ? 703 HOH   A O   1 
HETATM 2164 O  O   . HOH   F 5 .   ? -33.872 9.674   20.483  1.00 31.65 ? 704 HOH   A O   1 
HETATM 2165 O  O   . HOH   F 5 .   ? -9.882  -4.678  7.986   1.00 38.06 ? 705 HOH   A O   1 
HETATM 2166 O  O   . HOH   F 5 .   ? -38.654 1.372   5.547   1.00 24.37 ? 706 HOH   A O   1 
HETATM 2167 O  O   . HOH   F 5 .   ? -40.445 5.156   3.594   1.00 36.31 ? 707 HOH   A O   1 
HETATM 2168 O  O   . HOH   F 5 .   ? -20.384 2.513   15.559  1.00 38.77 ? 708 HOH   A O   1 
HETATM 2169 O  O   . HOH   F 5 .   ? -42.892 2.052   4.200   1.00 30.30 ? 709 HOH   A O   1 
HETATM 2170 O  O   . HOH   F 5 .   ? -34.572 -11.174 9.500   1.00 26.10 ? 710 HOH   A O   1 
HETATM 2171 O  O   . HOH   F 5 .   ? -24.633 32.672  -4.992  1.00 23.80 ? 711 HOH   A O   1 
HETATM 2172 O  O   . HOH   F 5 .   ? -33.335 -10.807 11.353  1.00 26.40 ? 712 HOH   A O   1 
HETATM 2173 O  O   . HOH   F 5 .   ? -31.694 31.464  5.255   1.00 36.65 ? 713 HOH   A O   1 
HETATM 2174 O  O   . HOH   F 5 .   ? -32.783 24.493  -10.642 1.00 22.82 ? 714 HOH   A O   1 
HETATM 2175 O  O   . HOH   F 5 .   ? -41.759 17.892  -10.934 1.00 43.68 ? 715 HOH   A O   1 
HETATM 2176 O  O   . HOH   F 5 .   ? -31.134 3.358   -17.128 1.00 18.02 ? 716 HOH   A O   1 
HETATM 2177 O  O   . HOH   F 5 .   ? -23.335 30.409  -14.646 1.00 41.45 ? 717 HOH   A O   1 
HETATM 2178 O  O   . HOH   F 5 .   ? -25.745 18.905  -18.317 1.00 41.20 ? 718 HOH   A O   1 
HETATM 2179 O  O   . HOH   F 5 .   ? -19.279 1.038   -10.914 1.00 38.86 ? 719 HOH   A O   1 
HETATM 2180 O  O   . HOH   F 5 .   ? -6.666  0.068   4.685   1.00 38.61 ? 720 HOH   A O   1 
HETATM 2181 O  O   . HOH   F 5 .   ? -40.964 3.314   5.732   1.00 27.19 ? 721 HOH   A O   1 
HETATM 2182 O  O   . HOH   F 5 .   ? -16.691 31.865  11.080  1.00 24.24 ? 722 HOH   A O   1 
HETATM 2183 O  O   . HOH   F 5 .   ? -23.689 22.745  12.282  1.00 43.68 ? 723 HOH   A O   1 
HETATM 2184 O  O   . HOH   F 5 .   ? -40.280 9.110   0.719   1.00 47.50 ? 724 HOH   A O   1 
HETATM 2185 O  O   . HOH   F 5 .   ? -32.701 31.436  -5.654  1.00 36.11 ? 725 HOH   A O   1 
HETATM 2186 O  O   . HOH   F 5 .   ? -36.569 -7.844  6.521   1.00 33.80 ? 726 HOH   A O   1 
HETATM 2187 O  O   . HOH   F 5 .   ? -33.275 34.105  -1.949  1.00 34.55 ? 727 HOH   A O   1 
HETATM 2188 O  O   . HOH   F 5 .   ? -38.249 22.284  -7.858  1.00 30.96 ? 728 HOH   A O   1 
HETATM 2189 O  O   . HOH   F 5 .   ? -30.083 30.899  -7.962  1.00 40.15 ? 729 HOH   A O   1 
HETATM 2190 O  O   . HOH   F 5 .   ? -25.045 -3.550  -10.514 1.00 29.71 ? 730 HOH   A O   1 
HETATM 2191 O  O   . HOH   F 5 .   ? -1.939  23.521  0.364   1.00 24.62 ? 731 HOH   A O   1 
HETATM 2192 O  O   . HOH   F 5 .   ? -33.429 20.060  8.526   1.00 36.27 ? 732 HOH   A O   1 
HETATM 2193 O  O   . HOH   F 5 .   ? -17.895 27.637  9.134   1.00 18.84 ? 733 HOH   A O   1 
HETATM 2194 O  O   . HOH   F 5 .   ? -14.293 29.506  14.307  1.00 39.17 ? 734 HOH   A O   1 
HETATM 2195 O  O   . HOH   F 5 .   ? -32.380 22.291  9.014   1.00 36.20 ? 735 HOH   A O   1 
HETATM 2196 O  O   . HOH   F 5 .   ? -30.175 6.945   19.095  1.00 40.16 ? 736 HOH   A O   1 
HETATM 2197 O  O   . HOH   F 5 .   ? -14.188 3.264   -10.629 1.00 36.36 ? 737 HOH   A O   1 
HETATM 2198 O  O   . HOH   F 5 .   ? -1.978  28.761  -7.366  1.00 30.20 ? 738 HOH   A O   1 
HETATM 2199 O  O   . HOH   F 5 .   ? -28.449 36.763  3.045   1.00 44.09 ? 739 HOH   A O   1 
HETATM 2200 O  O   . HOH   F 5 .   ? -23.834 24.568  9.061   1.00 40.68 ? 740 HOH   A O   1 
HETATM 2201 O  O   . HOH   F 5 .   ? -48.495 4.768   -11.934 1.00 34.45 ? 741 HOH   A O   1 
HETATM 2202 O  O   . HOH   F 5 .   ? -41.938 -1.534  1.017   1.00 25.75 ? 742 HOH   A O   1 
HETATM 2203 O  O   . HOH   F 5 .   ? -27.406 36.556  -1.326  1.00 37.60 ? 743 HOH   A O   1 
HETATM 2204 O  O   . HOH   F 5 .   ? -27.042 2.988   -15.849 1.00 26.01 ? 744 HOH   A O   1 
HETATM 2205 O  O   . HOH   F 5 .   ? -27.021 9.183   -18.811 1.00 43.81 ? 745 HOH   A O   1 
HETATM 2206 O  O   . HOH   F 5 .   ? -7.509  15.709  -11.202 1.00 29.06 ? 746 HOH   A O   1 
HETATM 2207 O  O   . HOH   F 5 .   ? -25.246 0.131   -11.916 1.00 17.70 ? 747 HOH   A O   1 
HETATM 2208 O  O   . HOH   F 5 .   ? -29.985 34.822  1.522   1.00 33.21 ? 748 HOH   A O   1 
HETATM 2209 O  O   . HOH   F 5 .   ? -22.430 34.325  8.325   1.00 45.44 ? 749 HOH   A O   1 
HETATM 2210 O  O   . HOH   F 5 .   ? -30.521 33.794  -2.906  1.00 21.20 ? 750 HOH   A O   1 
HETATM 2211 O  O   . HOH   F 5 .   ? -14.204 24.095  17.800  1.00 34.67 ? 751 HOH   A O   1 
HETATM 2212 O  O   . HOH   F 5 .   ? -28.361 23.893  9.003   1.00 26.11 ? 752 HOH   A O   1 
HETATM 2213 O  O   . HOH   F 5 .   ? -41.752 -0.834  3.652   1.00 27.67 ? 753 HOH   A O   1 
HETATM 2214 O  O   . HOH   F 5 .   ? -2.425  19.085  -10.387 1.00 50.16 ? 754 HOH   A O   1 
HETATM 2215 O  O   . HOH   F 5 .   ? -27.370 23.967  -17.291 1.00 35.48 ? 755 HOH   A O   1 
HETATM 2216 O  O   . HOH   F 5 .   ? -28.251 31.081  -5.139  1.00 19.56 ? 756 HOH   A O   1 
HETATM 2217 O  O   . HOH   F 5 .   ? -25.667 35.606  -3.577  1.00 42.30 ? 757 HOH   A O   1 
HETATM 2218 O  O   . HOH   F 5 .   ? -23.483 3.493   -12.205 1.00 27.83 ? 758 HOH   A O   1 
HETATM 2219 O  O   . HOH   F 5 .   ? -35.443 -6.906  1.818   1.00 25.81 ? 759 HOH   A O   1 
HETATM 2220 O  O   . HOH   F 5 .   ? -11.868 3.524   -11.475 1.00 38.47 ? 760 HOH   A O   1 
HETATM 2221 O  O   . HOH   F 5 .   ? -17.691 -0.347  14.776  1.00 28.23 ? 761 HOH   A O   1 
HETATM 2222 O  O   . HOH   F 5 .   ? -7.327  13.395  -10.051 1.00 32.38 ? 762 HOH   A O   1 
HETATM 2223 O  O   . HOH   F 5 .   ? -30.613 2.654   -19.698 1.00 22.17 ? 763 HOH   A O   1 
HETATM 2224 O  O   . HOH   F 5 .   ? -24.668 2.161   -14.248 1.00 26.56 ? 764 HOH   A O   1 
HETATM 2225 O  O   . HOH   F 5 .   ? -32.859 35.043  0.829   1.00 35.63 ? 765 HOH   A O   1 
HETATM 2226 O  O   . HOH   F 5 .   ? -36.214 7.621   23.938  1.00 34.91 ? 766 HOH   A O   1 
HETATM 2227 O  O   . HOH   F 5 .   ? -16.216 3.133   17.522  1.00 41.68 ? 767 HOH   A O   1 
HETATM 2228 O  O   . HOH   F 5 .   ? -15.304 32.291  13.467  1.00 32.25 ? 768 HOH   A O   1 
HETATM 2229 O  O   . HOH   F 5 .   ? -27.333 1.931   -18.509 1.00 43.22 ? 769 HOH   A O   1 
# 
