data_9FPQ
# 
_entry.id   9FPQ 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.404 
_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   9FPQ         pdb_00009fpq 10.2210/pdb9fpq/pdb 
WWPDB D_1292139126 ?            ?                   
# 
_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       2025-06-25 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9FPQ 
_pdbx_database_status.recvd_initial_deposition_date   2024-06-13 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              alexeyus1@gmail.com 
_pdbx_contact_author.name_first         Alexey 
_pdbx_contact_author.name_last          Smirnov 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-5080-9367 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Smirnov, A.'    1 0000-0001-5080-9367 
'Manakova, E.N.' 2 0000-0002-6027-2265 
'Grazulis, S.'   3 0000-0002-7928-5218 
'Paketuryte, V.' 4 0000-0003-0919-7826 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Crystal structure of carbonic anhydrase II with methyl 4-benzylsulfanyl-3-sulfamoyl-benzoate' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Smirnov, A.'    1 0000-0001-5080-9367 
primary 'Manakova, E.N.' 2 0000-0002-6027-2265 
primary 'Grazulis, S.'   3 0000-0002-7928-5218 
primary 'Paketuryte, V.' 4 0000-0003-0919-7826 
# 
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 'Carbonic anhydrase 2'                                 29289.062 1   4.2.1.1 ? ? ? 
2 non-polymer syn 'ZINC ION'                                             65.409    1   ?       ? ? ? 
3 non-polymer syn 'methyl 4-(phenylmethylsulfanyl)-3-sulfamoyl-benzoate' 337.414   1   ?       ? ? ? 
4 non-polymer syn BICINE                                                 163.172   1   ?       ? ? ? 
5 non-polymer syn 'DIMETHYL SULFOXIDE'                                   78.133    1   ?       ? ? ? 
6 water       nat water                                                  18.015    265 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Carbonate dehydratase II,Carbonic anhydrase C,CAC,Carbonic anhydrase II,CA-II' 
# 
_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       
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_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 'methyl 4-(phenylmethylsulfanyl)-3-sulfamoyl-benzoate' A1IEL 
4 BICINE                                                 BCN   
5 'DIMETHYL SULFOXIDE'                                   DMS   
6 water                                                  HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   SER n 
1 3   HIS n 
1 4   HIS n 
1 5   TRP n 
1 6   GLY n 
1 7   TYR n 
1 8   GLY n 
1 9   LYS n 
1 10  HIS n 
1 11  ASN n 
1 12  GLY n 
1 13  PRO n 
1 14  GLU n 
1 15  HIS n 
1 16  TRP n 
1 17  HIS n 
1 18  LYS n 
1 19  ASP n 
1 20  PHE n 
1 21  PRO n 
1 22  ILE n 
1 23  ALA n 
1 24  LYS n 
1 25  GLY n 
1 26  GLU n 
1 27  ARG n 
1 28  GLN n 
1 29  SER n 
1 30  PRO n 
1 31  VAL n 
1 32  ASP n 
1 33  ILE n 
1 34  ASP n 
1 35  THR n 
1 36  HIS n 
1 37  THR n 
1 38  ALA n 
1 39  LYS n 
1 40  TYR n 
1 41  ASP n 
1 42  PRO n 
1 43  SER n 
1 44  LEU n 
1 45  LYS n 
1 46  PRO n 
1 47  LEU n 
1 48  SER n 
1 49  VAL n 
1 50  SER n 
1 51  TYR n 
1 52  ASP n 
1 53  GLN n 
1 54  ALA n 
1 55  THR n 
1 56  SER n 
1 57  LEU n 
1 58  ARG n 
1 59  ILE n 
1 60  LEU n 
1 61  ASN n 
1 62  ASN n 
1 63  GLY n 
1 64  HIS n 
1 65  ALA n 
1 66  PHE n 
1 67  ASN n 
1 68  VAL n 
1 69  GLU n 
1 70  PHE n 
1 71  ASP n 
1 72  ASP n 
1 73  SER n 
1 74  GLN n 
1 75  ASP n 
1 76  LYS n 
1 77  ALA n 
1 78  VAL n 
1 79  LEU n 
1 80  LYS n 
1 81  GLY n 
1 82  GLY n 
1 83  PRO n 
1 84  LEU n 
1 85  ASP n 
1 86  GLY n 
1 87  THR n 
1 88  TYR n 
1 89  ARG n 
1 90  LEU n 
1 91  ILE n 
1 92  GLN n 
1 93  PHE n 
1 94  HIS n 
1 95  PHE n 
1 96  HIS n 
1 97  TRP n 
1 98  GLY n 
1 99  SER n 
1 100 LEU n 
1 101 ASP n 
1 102 GLY n 
1 103 GLN n 
1 104 GLY n 
1 105 SER n 
1 106 GLU n 
1 107 HIS n 
1 108 THR n 
1 109 VAL n 
1 110 ASP n 
1 111 LYS n 
1 112 LYS n 
1 113 LYS n 
1 114 TYR n 
1 115 ALA n 
1 116 ALA n 
1 117 GLU n 
1 118 LEU n 
1 119 HIS n 
1 120 LEU n 
1 121 VAL n 
1 122 HIS n 
1 123 TRP n 
1 124 ASN n 
1 125 THR n 
1 126 LYS n 
1 127 TYR n 
1 128 GLY n 
1 129 ASP n 
1 130 PHE n 
1 131 GLY n 
1 132 LYS n 
1 133 ALA n 
1 134 VAL n 
1 135 GLN n 
1 136 GLN n 
1 137 PRO n 
1 138 ASP n 
1 139 GLY n 
1 140 LEU n 
1 141 ALA n 
1 142 VAL n 
1 143 LEU n 
1 144 GLY n 
1 145 ILE n 
1 146 PHE n 
1 147 LEU n 
1 148 LYS n 
1 149 VAL n 
1 150 GLY n 
1 151 SER n 
1 152 ALA n 
1 153 LYS n 
1 154 PRO n 
1 155 GLY n 
1 156 LEU n 
1 157 GLN n 
1 158 LYS n 
1 159 VAL n 
1 160 VAL n 
1 161 ASP n 
1 162 VAL n 
1 163 LEU n 
1 164 ASP n 
1 165 SER n 
1 166 ILE n 
1 167 LYS n 
1 168 THR n 
1 169 LYS n 
1 170 GLY n 
1 171 LYS n 
1 172 SER n 
1 173 ALA n 
1 174 ASP n 
1 175 PHE n 
1 176 THR n 
1 177 ASN n 
1 178 PHE n 
1 179 ASP n 
1 180 PRO n 
1 181 ARG n 
1 182 GLY n 
1 183 LEU n 
1 184 LEU n 
1 185 PRO n 
1 186 GLU n 
1 187 SER n 
1 188 LEU n 
1 189 ASP n 
1 190 TYR n 
1 191 TRP n 
1 192 THR n 
1 193 TYR n 
1 194 PRO n 
1 195 GLY n 
1 196 SER n 
1 197 LEU n 
1 198 THR n 
1 199 THR n 
1 200 PRO n 
1 201 PRO n 
1 202 LEU n 
1 203 LEU n 
1 204 GLU n 
1 205 CYS n 
1 206 VAL n 
1 207 THR n 
1 208 TRP n 
1 209 ILE n 
1 210 VAL n 
1 211 LEU n 
1 212 LYS n 
1 213 GLU n 
1 214 PRO n 
1 215 ILE n 
1 216 SER n 
1 217 VAL n 
1 218 SER n 
1 219 SER n 
1 220 GLU n 
1 221 GLN n 
1 222 VAL n 
1 223 LEU n 
1 224 LYS n 
1 225 PHE n 
1 226 ARG n 
1 227 LYS n 
1 228 LEU n 
1 229 ASN n 
1 230 PHE n 
1 231 ASN n 
1 232 GLY n 
1 233 GLU n 
1 234 GLY n 
1 235 GLU n 
1 236 PRO n 
1 237 GLU n 
1 238 GLU n 
1 239 LEU n 
1 240 MET n 
1 241 VAL n 
1 242 ASP n 
1 243 ASN n 
1 244 TRP n 
1 245 ARG n 
1 246 PRO n 
1 247 ALA n 
1 248 GLN n 
1 249 PRO n 
1 250 LEU n 
1 251 LYS n 
1 252 ASN n 
1 253 ARG n 
1 254 GLN n 
1 255 ILE n 
1 256 LYS n 
1 257 ALA n 
1 258 SER n 
1 259 PHE n 
1 260 LYS 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                   260 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 CA2 
_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 BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_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          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pET15b 
_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 
A1IEL non-polymer         . 'methyl 4-(phenylmethylsulfanyl)-3-sulfamoyl-benzoate' ? 'C15 H15 N O4 S2' 337.414 
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 
BCN   non-polymer         . BICINE                                                 ? 'C6 H13 N O4'     163.172 
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   MET 1   1   ?   ?   ?   A . n 
A 1 2   SER 2   2   ?   ?   ?   A . n 
A 1 3   HIS 3   3   3   HIS HIS A . n 
A 1 4   HIS 4   4   4   HIS HIS A . n 
A 1 5   TRP 5   5   5   TRP TRP A . n 
A 1 6   GLY 6   6   6   GLY GLY A . n 
A 1 7   TYR 7   7   7   TYR TYR A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   LYS 9   9   9   LYS LYS A . n 
A 1 10  HIS 10  10  10  HIS HIS A . n 
A 1 11  ASN 11  11  11  ASN ASN A . n 
A 1 12  GLY 12  12  12  GLY GLY A . n 
A 1 13  PRO 13  13  13  PRO PRO A . n 
A 1 14  GLU 14  14  14  GLU GLU A . n 
A 1 15  HIS 15  15  15  HIS HIS A . n 
A 1 16  TRP 16  16  16  TRP TRP A . n 
A 1 17  HIS 17  17  17  HIS HIS A . n 
A 1 18  LYS 18  18  18  LYS LYS A . n 
A 1 19  ASP 19  19  19  ASP ASP A . n 
A 1 20  PHE 20  20  20  PHE PHE A . n 
A 1 21  PRO 21  21  21  PRO PRO A . n 
A 1 22  ILE 22  22  22  ILE ILE A . n 
A 1 23  ALA 23  23  23  ALA ALA A . n 
A 1 24  LYS 24  24  24  LYS LYS A . n 
A 1 25  GLY 25  25  25  GLY GLY A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  ARG 27  27  27  ARG ARG A . n 
A 1 28  GLN 28  28  28  GLN GLN A . n 
A 1 29  SER 29  29  29  SER SER A . n 
A 1 30  PRO 30  30  30  PRO PRO A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  ASP 32  32  32  ASP ASP A . n 
A 1 33  ILE 33  33  33  ILE ILE A . n 
A 1 34  ASP 34  34  34  ASP ASP A . n 
A 1 35  THR 35  35  35  THR THR A . n 
A 1 36  HIS 36  36  36  HIS HIS A . n 
A 1 37  THR 37  37  37  THR THR A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  LYS 39  39  39  LYS LYS A . n 
A 1 40  TYR 40  40  40  TYR TYR A . n 
A 1 41  ASP 41  41  41  ASP ASP A . n 
A 1 42  PRO 42  42  42  PRO PRO A . n 
A 1 43  SER 43  43  43  SER SER A . n 
A 1 44  LEU 44  44  44  LEU LEU A . n 
A 1 45  LYS 45  45  45  LYS LYS A . n 
A 1 46  PRO 46  46  46  PRO PRO A . n 
A 1 47  LEU 47  47  47  LEU LEU A . n 
A 1 48  SER 48  48  48  SER SER A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  SER 50  50  50  SER SER A . n 
A 1 51  TYR 51  51  51  TYR TYR A . n 
A 1 52  ASP 52  52  52  ASP ASP A . n 
A 1 53  GLN 53  53  53  GLN GLN A . n 
A 1 54  ALA 54  54  54  ALA ALA A . n 
A 1 55  THR 55  55  55  THR THR A . n 
A 1 56  SER 56  56  56  SER SER A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  ARG 58  58  58  ARG ARG A . n 
A 1 59  ILE 59  59  59  ILE ILE A . n 
A 1 60  LEU 60  60  60  LEU LEU A . n 
A 1 61  ASN 61  61  61  ASN ASN A . n 
A 1 62  ASN 62  62  62  ASN ASN A . n 
A 1 63  GLY 63  63  63  GLY GLY A . n 
A 1 64  HIS 64  64  64  HIS HIS A . n 
A 1 65  ALA 65  65  65  ALA ALA A . n 
A 1 66  PHE 66  66  66  PHE PHE A . n 
A 1 67  ASN 67  67  67  ASN ASN A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  GLU 69  69  69  GLU GLU A . n 
A 1 70  PHE 70  70  70  PHE PHE A . n 
A 1 71  ASP 71  71  71  ASP ASP A . n 
A 1 72  ASP 72  72  72  ASP ASP A . n 
A 1 73  SER 73  73  73  SER SER A . n 
A 1 74  GLN 74  74  74  GLN GLN A . n 
A 1 75  ASP 75  75  75  ASP ASP A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  ALA 77  77  77  ALA ALA A . n 
A 1 78  VAL 78  78  78  VAL VAL A . n 
A 1 79  LEU 79  79  79  LEU LEU A . n 
A 1 80  LYS 80  80  80  LYS LYS A . n 
A 1 81  GLY 81  81  81  GLY GLY A . n 
A 1 82  GLY 82  82  82  GLY GLY A . n 
A 1 83  PRO 83  83  83  PRO PRO A . n 
A 1 84  LEU 84  84  84  LEU LEU A . n 
A 1 85  ASP 85  85  85  ASP ASP A . n 
A 1 86  GLY 86  86  86  GLY GLY A . n 
A 1 87  THR 87  87  87  THR THR A . n 
A 1 88  TYR 88  88  88  TYR TYR A . n 
A 1 89  ARG 89  89  89  ARG ARG A . n 
A 1 90  LEU 90  90  90  LEU LEU A . n 
A 1 91  ILE 91  91  91  ILE ILE A . n 
A 1 92  GLN 92  92  92  GLN GLN A . n 
A 1 93  PHE 93  93  93  PHE PHE A . n 
A 1 94  HIS 94  94  94  HIS HIS A . n 
A 1 95  PHE 95  95  95  PHE PHE A . n 
A 1 96  HIS 96  96  96  HIS HIS A . n 
A 1 97  TRP 97  97  97  TRP TRP A . n 
A 1 98  GLY 98  98  98  GLY GLY A . n 
A 1 99  SER 99  99  99  SER SER A . n 
A 1 100 LEU 100 100 100 LEU LEU A . n 
A 1 101 ASP 101 101 101 ASP ASP A . n 
A 1 102 GLY 102 102 102 GLY GLY A . n 
A 1 103 GLN 103 103 103 GLN GLN A . n 
A 1 104 GLY 104 104 104 GLY GLY A . n 
A 1 105 SER 105 105 105 SER SER A . n 
A 1 106 GLU 106 106 106 GLU GLU A . n 
A 1 107 HIS 107 107 107 HIS HIS A . n 
A 1 108 THR 108 108 108 THR THR A . n 
A 1 109 VAL 109 109 109 VAL VAL A . n 
A 1 110 ASP 110 110 110 ASP ASP A . n 
A 1 111 LYS 111 111 111 LYS LYS A . n 
A 1 112 LYS 112 112 112 LYS LYS A . n 
A 1 113 LYS 113 113 113 LYS LYS A . n 
A 1 114 TYR 114 114 114 TYR TYR A . n 
A 1 115 ALA 115 115 115 ALA ALA A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 GLU 117 117 117 GLU GLU A . n 
A 1 118 LEU 118 118 118 LEU LEU A . n 
A 1 119 HIS 119 119 119 HIS HIS A . n 
A 1 120 LEU 120 120 120 LEU LEU A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 HIS 122 122 122 HIS HIS A . n 
A 1 123 TRP 123 123 123 TRP TRP A . n 
A 1 124 ASN 124 124 124 ASN ASN A . n 
A 1 125 THR 125 125 125 THR THR A . n 
A 1 126 LYS 126 127 127 LYS LYS A . n 
A 1 127 TYR 127 128 128 TYR TYR A . n 
A 1 128 GLY 128 129 129 GLY GLY A . n 
A 1 129 ASP 129 130 130 ASP ASP A . n 
A 1 130 PHE 130 131 131 PHE PHE A . n 
A 1 131 GLY 131 132 132 GLY GLY A . n 
A 1 132 LYS 132 133 133 LYS LYS A . n 
A 1 133 ALA 133 134 134 ALA ALA A . n 
A 1 134 VAL 134 135 135 VAL VAL A . n 
A 1 135 GLN 135 136 136 GLN GLN A . n 
A 1 136 GLN 136 137 137 GLN GLN A . n 
A 1 137 PRO 137 138 138 PRO PRO A . n 
A 1 138 ASP 138 139 139 ASP ASP A . n 
A 1 139 GLY 139 140 140 GLY GLY A . n 
A 1 140 LEU 140 141 141 LEU LEU A . n 
A 1 141 ALA 141 142 142 ALA ALA A . n 
A 1 142 VAL 142 143 143 VAL VAL A . n 
A 1 143 LEU 143 144 144 LEU LEU A . n 
A 1 144 GLY 144 145 145 GLY GLY A . n 
A 1 145 ILE 145 146 146 ILE ILE A . n 
A 1 146 PHE 146 147 147 PHE PHE A . n 
A 1 147 LEU 147 148 148 LEU LEU A . n 
A 1 148 LYS 148 149 149 LYS LYS A . n 
A 1 149 VAL 149 150 150 VAL VAL A . n 
A 1 150 GLY 150 151 151 GLY GLY A . n 
A 1 151 SER 151 152 152 SER SER A . n 
A 1 152 ALA 152 153 153 ALA ALA A . n 
A 1 153 LYS 153 154 154 LYS LYS A . n 
A 1 154 PRO 154 155 155 PRO PRO A . n 
A 1 155 GLY 155 156 156 GLY GLY A . n 
A 1 156 LEU 156 157 157 LEU LEU A . n 
A 1 157 GLN 157 158 158 GLN GLN A . n 
A 1 158 LYS 158 159 159 LYS LYS A . n 
A 1 159 VAL 159 160 160 VAL VAL A . n 
A 1 160 VAL 160 161 161 VAL VAL A . n 
A 1 161 ASP 161 162 162 ASP ASP A . n 
A 1 162 VAL 162 163 163 VAL VAL A . n 
A 1 163 LEU 163 164 164 LEU LEU A . n 
A 1 164 ASP 164 165 165 ASP ASP A . n 
A 1 165 SER 165 166 166 SER SER A . n 
A 1 166 ILE 166 167 167 ILE ILE A . n 
A 1 167 LYS 167 168 168 LYS LYS A . n 
A 1 168 THR 168 169 169 THR THR A . n 
A 1 169 LYS 169 170 170 LYS LYS A . n 
A 1 170 GLY 170 171 171 GLY GLY A . n 
A 1 171 LYS 171 172 172 LYS LYS A . n 
A 1 172 SER 172 173 173 SER SER A . n 
A 1 173 ALA 173 174 174 ALA ALA A . n 
A 1 174 ASP 174 175 175 ASP ASP A . n 
A 1 175 PHE 175 176 176 PHE PHE A . n 
A 1 176 THR 176 177 177 THR THR A . n 
A 1 177 ASN 177 178 178 ASN ASN A . n 
A 1 178 PHE 178 179 179 PHE PHE A . n 
A 1 179 ASP 179 180 180 ASP ASP A . n 
A 1 180 PRO 180 181 181 PRO PRO A . n 
A 1 181 ARG 181 182 182 ARG ARG A . n 
A 1 182 GLY 182 183 183 GLY GLY A . n 
A 1 183 LEU 183 184 184 LEU LEU A . n 
A 1 184 LEU 184 185 185 LEU LEU A . n 
A 1 185 PRO 185 186 186 PRO PRO A . n 
A 1 186 GLU 186 187 187 GLU GLU A . n 
A 1 187 SER 187 188 188 SER SER A . n 
A 1 188 LEU 188 189 189 LEU LEU A . n 
A 1 189 ASP 189 190 190 ASP ASP A . n 
A 1 190 TYR 190 191 191 TYR TYR A . n 
A 1 191 TRP 191 192 192 TRP TRP A . n 
A 1 192 THR 192 193 193 THR THR A . n 
A 1 193 TYR 193 194 194 TYR TYR A . n 
A 1 194 PRO 194 195 195 PRO PRO A . n 
A 1 195 GLY 195 196 196 GLY GLY A . n 
A 1 196 SER 196 197 197 SER SER A . n 
A 1 197 LEU 197 198 198 LEU LEU A . n 
A 1 198 THR 198 199 199 THR THR A . n 
A 1 199 THR 199 200 200 THR THR A . n 
A 1 200 PRO 200 201 201 PRO PRO A . n 
A 1 201 PRO 201 202 202 PRO PRO A . n 
A 1 202 LEU 202 203 203 LEU LEU A . n 
A 1 203 LEU 203 204 204 LEU LEU A . n 
A 1 204 GLU 204 205 205 GLU GLU A . n 
A 1 205 CYS 205 206 206 CYS CYS A . n 
A 1 206 VAL 206 207 207 VAL VAL A . n 
A 1 207 THR 207 208 208 THR THR A . n 
A 1 208 TRP 208 209 209 TRP TRP A . n 
A 1 209 ILE 209 210 210 ILE ILE A . n 
A 1 210 VAL 210 211 211 VAL VAL A . n 
A 1 211 LEU 211 212 212 LEU LEU A . n 
A 1 212 LYS 212 213 213 LYS LYS A . n 
A 1 213 GLU 213 214 214 GLU GLU A . n 
A 1 214 PRO 214 215 215 PRO PRO A . n 
A 1 215 ILE 215 216 216 ILE ILE A . n 
A 1 216 SER 216 217 217 SER SER A . n 
A 1 217 VAL 217 218 218 VAL VAL A . n 
A 1 218 SER 218 219 219 SER SER A . n 
A 1 219 SER 219 220 220 SER SER A . n 
A 1 220 GLU 220 221 221 GLU GLU A . n 
A 1 221 GLN 221 222 222 GLN GLN A . n 
A 1 222 VAL 222 223 223 VAL VAL A . n 
A 1 223 LEU 223 224 224 LEU LEU A . n 
A 1 224 LYS 224 225 225 LYS LYS A . n 
A 1 225 PHE 225 226 226 PHE PHE A . n 
A 1 226 ARG 226 227 227 ARG ARG A . n 
A 1 227 LYS 227 228 228 LYS LYS A . n 
A 1 228 LEU 228 229 229 LEU LEU A . n 
A 1 229 ASN 229 230 230 ASN ASN A . n 
A 1 230 PHE 230 231 231 PHE PHE A . n 
A 1 231 ASN 231 232 232 ASN ASN A . n 
A 1 232 GLY 232 233 233 GLY GLY A . n 
A 1 233 GLU 233 234 234 GLU GLU A . n 
A 1 234 GLY 234 235 235 GLY GLY A . n 
A 1 235 GLU 235 236 236 GLU GLU A . n 
A 1 236 PRO 236 237 237 PRO PRO A . n 
A 1 237 GLU 237 238 238 GLU GLU A . n 
A 1 238 GLU 238 239 239 GLU GLU A . n 
A 1 239 LEU 239 240 240 LEU LEU A . n 
A 1 240 MET 240 241 241 MET MET A . n 
A 1 241 VAL 241 242 242 VAL VAL A . n 
A 1 242 ASP 242 243 243 ASP ASP A . n 
A 1 243 ASN 243 244 244 ASN ASN A . n 
A 1 244 TRP 244 245 245 TRP TRP A . n 
A 1 245 ARG 245 246 246 ARG ARG A . n 
A 1 246 PRO 246 247 247 PRO PRO A . n 
A 1 247 ALA 247 248 248 ALA ALA A . n 
A 1 248 GLN 248 249 249 GLN GLN A . n 
A 1 249 PRO 249 250 250 PRO PRO A . n 
A 1 250 LEU 250 251 251 LEU LEU A . n 
A 1 251 LYS 251 252 252 LYS LYS A . n 
A 1 252 ASN 252 253 253 ASN ASN A . n 
A 1 253 ARG 253 254 254 ARG ARG A . n 
A 1 254 GLN 254 255 255 GLN GLN A . n 
A 1 255 ILE 255 256 256 ILE ILE A . n 
A 1 256 LYS 256 257 257 LYS LYS A . n 
A 1 257 ALA 257 258 258 ALA ALA A . n 
A 1 258 SER 258 259 259 SER SER A . n 
A 1 259 PHE 259 260 260 PHE PHE A . n 
A 1 260 LYS 260 261 261 LYS LYS A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1IEL 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1IEL 
_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 1   ZN    ZN  A . 
C 3 A1IEL 1   302 1   A1IEL J13 A . 
D 4 BCN   1   303 1   BCN   BCN A . 
E 5 DMS   1   304 2   DMS   DMS A . 
F 6 HOH   1   401 182 HOH   HOH A . 
F 6 HOH   2   402 127 HOH   HOH A . 
F 6 HOH   3   403 197 HOH   HOH A . 
F 6 HOH   4   404 155 HOH   HOH A . 
F 6 HOH   5   405 208 HOH   HOH A . 
F 6 HOH   6   406 211 HOH   HOH A . 
F 6 HOH   7   407 117 HOH   HOH A . 
F 6 HOH   8   408 218 HOH   HOH A . 
F 6 HOH   9   409 80  HOH   HOH A . 
F 6 HOH   10  410 113 HOH   HOH A . 
F 6 HOH   11  411 99  HOH   HOH A . 
F 6 HOH   12  412 215 HOH   HOH A . 
F 6 HOH   13  413 151 HOH   HOH A . 
F 6 HOH   14  414 24  HOH   HOH A . 
F 6 HOH   15  415 263 HOH   HOH A . 
F 6 HOH   16  416 78  HOH   HOH A . 
F 6 HOH   17  417 29  HOH   HOH A . 
F 6 HOH   18  418 164 HOH   HOH A . 
F 6 HOH   19  419 250 HOH   HOH A . 
F 6 HOH   20  420 17  HOH   HOH A . 
F 6 HOH   21  421 173 HOH   HOH A . 
F 6 HOH   22  422 43  HOH   HOH A . 
F 6 HOH   23  423 167 HOH   HOH A . 
F 6 HOH   24  424 92  HOH   HOH A . 
F 6 HOH   25  425 16  HOH   HOH A . 
F 6 HOH   26  426 123 HOH   HOH A . 
F 6 HOH   27  427 246 HOH   HOH A . 
F 6 HOH   28  428 14  HOH   HOH A . 
F 6 HOH   29  429 265 HOH   HOH A . 
F 6 HOH   30  430 53  HOH   HOH A . 
F 6 HOH   31  431 142 HOH   HOH A . 
F 6 HOH   32  432 18  HOH   HOH A . 
F 6 HOH   33  433 140 HOH   HOH A . 
F 6 HOH   34  434 6   HOH   HOH A . 
F 6 HOH   35  435 213 HOH   HOH A . 
F 6 HOH   36  436 74  HOH   HOH A . 
F 6 HOH   37  437 201 HOH   HOH A . 
F 6 HOH   38  438 15  HOH   HOH A . 
F 6 HOH   39  439 225 HOH   HOH A . 
F 6 HOH   40  440 168 HOH   HOH A . 
F 6 HOH   41  441 58  HOH   HOH A . 
F 6 HOH   42  442 87  HOH   HOH A . 
F 6 HOH   43  443 31  HOH   HOH A . 
F 6 HOH   44  444 152 HOH   HOH A . 
F 6 HOH   45  445 137 HOH   HOH A . 
F 6 HOH   46  446 48  HOH   HOH A . 
F 6 HOH   47  447 45  HOH   HOH A . 
F 6 HOH   48  448 9   HOH   HOH A . 
F 6 HOH   49  449 183 HOH   HOH A . 
F 6 HOH   50  450 64  HOH   HOH A . 
F 6 HOH   51  451 192 HOH   HOH A . 
F 6 HOH   52  452 158 HOH   HOH A . 
F 6 HOH   53  453 13  HOH   HOH A . 
F 6 HOH   54  454 23  HOH   HOH A . 
F 6 HOH   55  455 95  HOH   HOH A . 
F 6 HOH   56  456 3   HOH   HOH A . 
F 6 HOH   57  457 27  HOH   HOH A . 
F 6 HOH   58  458 125 HOH   HOH A . 
F 6 HOH   59  459 110 HOH   HOH A . 
F 6 HOH   60  460 55  HOH   HOH A . 
F 6 HOH   61  461 81  HOH   HOH A . 
F 6 HOH   62  462 169 HOH   HOH A . 
F 6 HOH   63  463 121 HOH   HOH A . 
F 6 HOH   64  464 146 HOH   HOH A . 
F 6 HOH   65  465 264 HOH   HOH A . 
F 6 HOH   66  466 57  HOH   HOH A . 
F 6 HOH   67  467 248 HOH   HOH A . 
F 6 HOH   68  468 7   HOH   HOH A . 
F 6 HOH   69  469 5   HOH   HOH A . 
F 6 HOH   70  470 10  HOH   HOH A . 
F 6 HOH   71  471 122 HOH   HOH A . 
F 6 HOH   72  472 238 HOH   HOH A . 
F 6 HOH   73  473 75  HOH   HOH A . 
F 6 HOH   74  474 131 HOH   HOH A . 
F 6 HOH   75  475 61  HOH   HOH A . 
F 6 HOH   76  476 56  HOH   HOH A . 
F 6 HOH   77  477 30  HOH   HOH A . 
F 6 HOH   78  478 139 HOH   HOH A . 
F 6 HOH   79  479 40  HOH   HOH A . 
F 6 HOH   80  480 89  HOH   HOH A . 
F 6 HOH   81  481 189 HOH   HOH A . 
F 6 HOH   82  482 66  HOH   HOH A . 
F 6 HOH   83  483 11  HOH   HOH A . 
F 6 HOH   84  484 33  HOH   HOH A . 
F 6 HOH   85  485 185 HOH   HOH A . 
F 6 HOH   86  486 237 HOH   HOH A . 
F 6 HOH   87  487 41  HOH   HOH A . 
F 6 HOH   88  488 65  HOH   HOH A . 
F 6 HOH   89  489 1   HOH   HOH A . 
F 6 HOH   90  490 22  HOH   HOH A . 
F 6 HOH   91  491 154 HOH   HOH A . 
F 6 HOH   92  492 44  HOH   HOH A . 
F 6 HOH   93  493 126 HOH   HOH A . 
F 6 HOH   94  494 186 HOH   HOH A . 
F 6 HOH   95  495 2   HOH   HOH A . 
F 6 HOH   96  496 247 HOH   HOH A . 
F 6 HOH   97  497 4   HOH   HOH A . 
F 6 HOH   98  498 147 HOH   HOH A . 
F 6 HOH   99  499 224 HOH   HOH A . 
F 6 HOH   100 500 255 HOH   HOH A . 
F 6 HOH   101 501 20  HOH   HOH A . 
F 6 HOH   102 502 249 HOH   HOH A . 
F 6 HOH   103 503 54  HOH   HOH A . 
F 6 HOH   104 504 100 HOH   HOH A . 
F 6 HOH   105 505 26  HOH   HOH A . 
F 6 HOH   106 506 145 HOH   HOH A . 
F 6 HOH   107 507 116 HOH   HOH A . 
F 6 HOH   108 508 159 HOH   HOH A . 
F 6 HOH   109 509 141 HOH   HOH A . 
F 6 HOH   110 510 104 HOH   HOH A . 
F 6 HOH   111 511 170 HOH   HOH A . 
F 6 HOH   112 512 148 HOH   HOH A . 
F 6 HOH   113 513 262 HOH   HOH A . 
F 6 HOH   114 514 39  HOH   HOH A . 
F 6 HOH   115 515 143 HOH   HOH A . 
F 6 HOH   116 516 72  HOH   HOH A . 
F 6 HOH   117 517 118 HOH   HOH A . 
F 6 HOH   118 518 180 HOH   HOH A . 
F 6 HOH   119 519 162 HOH   HOH A . 
F 6 HOH   120 520 150 HOH   HOH A . 
F 6 HOH   121 521 120 HOH   HOH A . 
F 6 HOH   122 522 73  HOH   HOH A . 
F 6 HOH   123 523 253 HOH   HOH A . 
F 6 HOH   124 524 79  HOH   HOH A . 
F 6 HOH   125 525 25  HOH   HOH A . 
F 6 HOH   126 526 135 HOH   HOH A . 
F 6 HOH   127 527 51  HOH   HOH A . 
F 6 HOH   128 528 157 HOH   HOH A . 
F 6 HOH   129 529 153 HOH   HOH A . 
F 6 HOH   130 530 119 HOH   HOH A . 
F 6 HOH   131 531 71  HOH   HOH A . 
F 6 HOH   132 532 12  HOH   HOH A . 
F 6 HOH   133 533 52  HOH   HOH A . 
F 6 HOH   134 534 60  HOH   HOH A . 
F 6 HOH   135 535 188 HOH   HOH A . 
F 6 HOH   136 536 8   HOH   HOH A . 
F 6 HOH   137 537 124 HOH   HOH A . 
F 6 HOH   138 538 19  HOH   HOH A . 
F 6 HOH   139 539 85  HOH   HOH A . 
F 6 HOH   140 540 191 HOH   HOH A . 
F 6 HOH   141 541 254 HOH   HOH A . 
F 6 HOH   142 542 63  HOH   HOH A . 
F 6 HOH   143 543 109 HOH   HOH A . 
F 6 HOH   144 544 133 HOH   HOH A . 
F 6 HOH   145 545 144 HOH   HOH A . 
F 6 HOH   146 546 94  HOH   HOH A . 
F 6 HOH   147 547 136 HOH   HOH A . 
F 6 HOH   148 548 223 HOH   HOH A . 
F 6 HOH   149 549 97  HOH   HOH A . 
F 6 HOH   150 550 62  HOH   HOH A . 
F 6 HOH   151 551 205 HOH   HOH A . 
F 6 HOH   152 552 32  HOH   HOH A . 
F 6 HOH   153 553 161 HOH   HOH A . 
F 6 HOH   154 554 210 HOH   HOH A . 
F 6 HOH   155 555 77  HOH   HOH A . 
F 6 HOH   156 556 90  HOH   HOH A . 
F 6 HOH   157 557 70  HOH   HOH A . 
F 6 HOH   158 558 160 HOH   HOH A . 
F 6 HOH   159 559 37  HOH   HOH A . 
F 6 HOH   160 560 59  HOH   HOH A . 
F 6 HOH   161 561 138 HOH   HOH A . 
F 6 HOH   162 562 68  HOH   HOH A . 
F 6 HOH   163 563 129 HOH   HOH A . 
F 6 HOH   164 564 35  HOH   HOH A . 
F 6 HOH   165 565 242 HOH   HOH A . 
F 6 HOH   166 566 103 HOH   HOH A . 
F 6 HOH   167 567 200 HOH   HOH A . 
F 6 HOH   168 568 258 HOH   HOH A . 
F 6 HOH   169 569 106 HOH   HOH A . 
F 6 HOH   170 570 47  HOH   HOH A . 
F 6 HOH   171 571 91  HOH   HOH A . 
F 6 HOH   172 572 199 HOH   HOH A . 
F 6 HOH   173 573 232 HOH   HOH A . 
F 6 HOH   174 574 69  HOH   HOH A . 
F 6 HOH   175 575 83  HOH   HOH A . 
F 6 HOH   176 576 111 HOH   HOH A . 
F 6 HOH   177 577 149 HOH   HOH A . 
F 6 HOH   178 578 134 HOH   HOH A . 
F 6 HOH   179 579 21  HOH   HOH A . 
F 6 HOH   180 580 93  HOH   HOH A . 
F 6 HOH   181 581 203 HOH   HOH A . 
F 6 HOH   182 582 50  HOH   HOH A . 
F 6 HOH   183 583 34  HOH   HOH A . 
F 6 HOH   184 584 178 HOH   HOH A . 
F 6 HOH   185 585 101 HOH   HOH A . 
F 6 HOH   186 586 36  HOH   HOH A . 
F 6 HOH   187 587 112 HOH   HOH A . 
F 6 HOH   188 588 132 HOH   HOH A . 
F 6 HOH   189 589 221 HOH   HOH A . 
F 6 HOH   190 590 28  HOH   HOH A . 
F 6 HOH   191 591 175 HOH   HOH A . 
F 6 HOH   192 592 156 HOH   HOH A . 
F 6 HOH   193 593 38  HOH   HOH A . 
F 6 HOH   194 594 67  HOH   HOH A . 
F 6 HOH   195 595 244 HOH   HOH A . 
F 6 HOH   196 596 114 HOH   HOH A . 
F 6 HOH   197 597 88  HOH   HOH A . 
F 6 HOH   198 598 219 HOH   HOH A . 
F 6 HOH   199 599 84  HOH   HOH A . 
F 6 HOH   200 600 115 HOH   HOH A . 
F 6 HOH   201 601 177 HOH   HOH A . 
F 6 HOH   202 602 251 HOH   HOH A . 
F 6 HOH   203 603 96  HOH   HOH A . 
F 6 HOH   204 604 107 HOH   HOH A . 
F 6 HOH   205 605 259 HOH   HOH A . 
F 6 HOH   206 606 49  HOH   HOH A . 
F 6 HOH   207 607 214 HOH   HOH A . 
F 6 HOH   208 608 46  HOH   HOH A . 
F 6 HOH   209 609 260 HOH   HOH A . 
F 6 HOH   210 610 245 HOH   HOH A . 
F 6 HOH   211 611 193 HOH   HOH A . 
F 6 HOH   212 612 261 HOH   HOH A . 
F 6 HOH   213 613 195 HOH   HOH A . 
F 6 HOH   214 614 187 HOH   HOH A . 
F 6 HOH   215 615 209 HOH   HOH A . 
F 6 HOH   216 616 174 HOH   HOH A . 
F 6 HOH   217 617 207 HOH   HOH A . 
F 6 HOH   218 618 243 HOH   HOH A . 
F 6 HOH   219 619 105 HOH   HOH A . 
F 6 HOH   220 620 229 HOH   HOH A . 
F 6 HOH   221 621 190 HOH   HOH A . 
F 6 HOH   222 622 235 HOH   HOH A . 
F 6 HOH   223 623 216 HOH   HOH A . 
F 6 HOH   224 624 194 HOH   HOH A . 
F 6 HOH   225 625 202 HOH   HOH A . 
F 6 HOH   226 626 42  HOH   HOH A . 
F 6 HOH   227 627 227 HOH   HOH A . 
F 6 HOH   228 628 240 HOH   HOH A . 
F 6 HOH   229 629 165 HOH   HOH A . 
F 6 HOH   230 630 98  HOH   HOH A . 
F 6 HOH   231 631 172 HOH   HOH A . 
F 6 HOH   232 632 212 HOH   HOH A . 
F 6 HOH   233 633 234 HOH   HOH A . 
F 6 HOH   234 634 184 HOH   HOH A . 
F 6 HOH   235 635 166 HOH   HOH A . 
F 6 HOH   236 636 181 HOH   HOH A . 
F 6 HOH   237 637 222 HOH   HOH A . 
F 6 HOH   238 638 179 HOH   HOH A . 
F 6 HOH   239 639 163 HOH   HOH A . 
F 6 HOH   240 640 220 HOH   HOH A . 
F 6 HOH   241 641 76  HOH   HOH A . 
F 6 HOH   242 642 102 HOH   HOH A . 
F 6 HOH   243 643 171 HOH   HOH A . 
F 6 HOH   244 644 108 HOH   HOH A . 
F 6 HOH   245 645 256 HOH   HOH A . 
F 6 HOH   246 646 204 HOH   HOH A . 
F 6 HOH   247 647 82  HOH   HOH A . 
F 6 HOH   248 648 198 HOH   HOH A . 
F 6 HOH   249 649 206 HOH   HOH A . 
F 6 HOH   250 650 252 HOH   HOH A . 
F 6 HOH   251 651 128 HOH   HOH A . 
F 6 HOH   252 652 236 HOH   HOH A . 
F 6 HOH   253 653 176 HOH   HOH A . 
F 6 HOH   254 654 230 HOH   HOH A . 
F 6 HOH   255 655 239 HOH   HOH A . 
F 6 HOH   256 656 130 HOH   HOH A . 
F 6 HOH   257 657 228 HOH   HOH A . 
F 6 HOH   258 658 257 HOH   HOH A . 
F 6 HOH   259 659 226 HOH   HOH A . 
F 6 HOH   260 660 241 HOH   HOH A . 
F 6 HOH   261 661 196 HOH   HOH A . 
F 6 HOH   262 662 233 HOH   HOH A . 
F 6 HOH   263 663 217 HOH   HOH A . 
F 6 HOH   264 664 231 HOH   HOH A . 
F 6 HOH   265 665 86  HOH   HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 45  ? CE ? A LYS 45  CE 
2  1 Y 1 A LYS 45  ? NZ ? A LYS 45  NZ 
3  1 Y 1 A LYS 80  ? CE ? A LYS 80  CE 
4  1 Y 1 A LYS 80  ? NZ ? A LYS 80  NZ 
5  1 Y 1 A LYS 159 ? CD ? A LYS 158 CD 
6  1 Y 1 A LYS 159 ? CE ? A LYS 158 CE 
7  1 Y 1 A LYS 159 ? NZ ? A LYS 158 NZ 
8  1 Y 1 A LYS 168 ? CE ? A LYS 167 CE 
9  1 Y 1 A LYS 168 ? NZ ? A LYS 167 NZ 
10 1 Y 1 A LYS 257 ? CE ? A LYS 256 CE 
11 1 Y 1 A LYS 257 ? NZ ? A LYS 256 NZ 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? SCALA       ? ? ? 3.3.22   1 
? refinement        ? ? ? ? ? ? ? ? ? ? ? REFMAC      ? ? ? 5.8.0232 2 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.27     3 
? phasing           ? ? ? ? ? ? ? ? ? ? ? MOLREP      ? ? ? .        4 
? 'model building'  ? ? ? ? ? ? ? ? ? ? ? Coot        ? ? ? .        5 
? 'data processing' ? ? ? ? ? ? ? ? ? ? ? XDS         ? ? ? .        6 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   104.210 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9FPQ 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     42.302 
_cell.length_a_esd                 ? 
_cell.length_b                     41.279 
_cell.length_b_esd                 ? 
_cell.length_c                     72.213 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        2 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9FPQ 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9FPQ 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.04 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          39.2 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
'0.1M sodium BICINE, pH 9, 0.2 M ammonium sulfate and 2M sodium malonate pH 7 made from 1M sodium BICINE and 3.4M sodium malonate' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2017-12-19 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.976200 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'PETRA III, EMBL c/o DESY BEAMLINE P13 (MX1)' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.976200 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'P13 (MX1)' 
_diffrn_source.pdbx_synchrotron_site       'PETRA III, EMBL c/o DESY' 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9FPQ 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.500 
_reflns.d_resolution_low                               70.002 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     38824 
_reflns.number_obs                                     38824 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.600 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.600 
_reflns.pdbx_netI_over_av_sigmaI                       8.600 
_reflns.pdbx_netI_over_sigmaI                          15.900 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.057 
_reflns.pdbx_Rpim_I_all                                0.022 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       258122 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                0.049 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.meanI_over_sigI_gt 
_reflns_shell.meanI_over_uI_all 
_reflns_shell.meanI_over_uI_gt 
_reflns_shell.number_measured_gt 
_reflns_shell.number_unique_gt 
_reflns_shell.percent_possible_gt 
_reflns_shell.Rmerge_F_gt 
_reflns_shell.Rmerge_I_gt 
_reflns_shell.pdbx_redundancy 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
_reflns_shell.pdbx_R_split 
_reflns_shell.percent_possible_all 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_percent_possible_ellipsoidal 
_reflns_shell.pdbx_percent_possible_spherical 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous 
_reflns_shell.pdbx_percent_possible_spherical_anomalous 
_reflns_shell.pdbx_redundancy_anomalous 
_reflns_shell.pdbx_CC_half_anomalous 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous 
_reflns_shell.pdbx_percent_possible_anomalous 
1.500 1.580  ? 2.900  35751 ? ? ? 5605 ? ? ? ? ? ? ? ? ? ? ? 6.400 ? ? 4.900  0.288 0.112 ? 1  1 ? ? ? 99.200  ? 0.248 0.248 ? ? ? 
? ? ? ? ? 
1.580 1.680  ? 3.900  36083 ? ? ? 5353 ? ? ? ? ? ? ? ? ? ? ? 6.700 ? ? 6.500  0.211 0.080 ? 2  1 ? ? ? 100.000 ? 0.181 0.181 ? ? ? 
? ? ? ? ? 
1.680 1.790  ? 5.200  33750 ? ? ? 5044 ? ? ? ? ? ? ? ? ? ? ? 6.700 ? ? 8.300  0.155 0.059 ? 3  1 ? ? ? 99.900  ? 0.133 0.133 ? ? ? 
? ? ? ? ? 
1.790 1.940  ? 6.800  28908 ? ? ? 4625 ? ? ? ? ? ? ? ? ? ? ? 6.300 ? ? 11.100 0.116 0.045 ? 4  1 ? ? ? 99.100  ? 0.098 0.098 ? ? ? 
? ? ? ? ? 
1.940 2.120  ? 9.100  30428 ? ? ? 4335 ? ? ? ? ? ? ? ? ? ? ? 7.000 ? ? 16.600 0.084 0.032 ? 5  1 ? ? ? 99.900  ? 0.072 0.072 ? ? ? 
? ? ? ? ? 
2.120 2.370  ? 10.700 26915 ? ? ? 3898 ? ? ? ? ? ? ? ? ? ? ? 6.900 ? ? 20.600 0.072 0.027 ? 6  1 ? ? ? 99.800  ? 0.061 0.061 ? ? ? 
? ? ? ? ? 
2.370 2.740  ? 11.100 21548 ? ? ? 3428 ? ? ? ? ? ? ? ? ? ? ? 6.300 ? ? 22.700 0.069 0.027 ? 7  1 ? ? ? 99.200  ? 0.058 0.058 ? ? ? 
? ? ? ? ? 
2.740 3.350  ? 14.400 20750 ? ? ? 2946 ? ? ? ? ? ? ? ? ? ? ? 7.000 ? ? 31.800 0.053 0.020 ? 8  1 ? ? ? 100.000 ? 0.045 0.045 ? ? ? 
? ? ? ? ? 
3.350 4.740  ? 18.300 15383 ? ? ? 2286 ? ? ? ? ? ? ? ? ? ? ? 6.700 ? ? 39.400 0.039 0.015 ? 9  1 ? ? ? 99.700  ? 0.034 0.034 ? ? ? 
? ? ? ? ? 
4.740 70.002 ? 15.900 8606  ? ? ? 1304 ? ? ? ? ? ? ? ? ? ? ? 6.600 ? ? 37.000 0.039 0.015 ? 10 1 ? ? ? 99.700  ? 0.032 0.032 ? ? ? 
? ? ? ? ? 
# 
_refine.aniso_B[1][1]                            0.1500 
_refine.aniso_B[1][2]                            0.0000 
_refine.aniso_B[1][3]                            -0.3100 
_refine.aniso_B[2][2]                            -1.0000 
_refine.aniso_B[2][3]                            0.0000 
_refine.aniso_B[3][3]                            0.8900 
_refine.B_iso_max                                75.260 
_refine.B_iso_mean                               21.5830 
_refine.B_iso_min                                10.330 
_refine.correlation_coeff_Fo_to_Fc               0.9710 
_refine.correlation_coeff_Fo_to_Fc_free          0.9630 
_refine.details                                  
'HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT U VALUES      : REFINED INDIVIDUALLY' 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9FPQ 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.5000 
_refine.ls_d_res_low                             70.0000 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     34677 
_refine.ls_number_reflns_R_free                  4014 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.2600 
_refine.ls_percent_reflns_R_free                 10.4000 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1720 
_refine.ls_R_factor_R_free                       0.1973 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1690 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.0820 
_refine.pdbx_overall_ESU_R_Free                  0.0810 
_refine.pdbx_solvent_vdw_probe_radii             1.4000 
_refine.pdbx_solvent_ion_probe_radii             0.8000 
_refine.pdbx_solvent_shrinkage_radii             0.8000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         final 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.5000 
_refine_hist.d_res_low                        70.0000 
_refine_hist.number_atoms_solvent             265 
_refine_hist.number_atoms_total               2351 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       258 
_refine_hist.pdbx_B_iso_mean_ligand           31.56 
_refine_hist.pdbx_B_iso_mean_solvent          32.62 
_refine_hist.pdbx_number_atoms_protein        2048 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         38 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.011  0.012  2221 ? r_bond_refined_d       ? ? 
'X-RAY DIFFRACTION' ? 1.801  1.649  3025 ? r_angle_refined_deg    ? ? 
'X-RAY DIFFRACTION' ? 6.981  5.000  272  ? r_dihedral_angle_1_deg ? ? 
'X-RAY DIFFRACTION' ? 34.665 23.738 107  ? r_dihedral_angle_2_deg ? ? 
'X-RAY DIFFRACTION' ? 12.582 15.000 357  ? r_dihedral_angle_3_deg ? ? 
'X-RAY DIFFRACTION' ? 21.333 15.000 7    ? r_dihedral_angle_4_deg ? ? 
'X-RAY DIFFRACTION' ? 0.125  0.200  268  ? r_chiral_restr         ? ? 
'X-RAY DIFFRACTION' ? 0.012  0.020  1744 ? r_gen_planes_refined   ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.5000 
_refine_ls_shell.d_res_low                        1.5390 
_refine_ls_shell.number_reflns_all                2799 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             281 
_refine_ls_shell.number_reflns_R_work             2518 
_refine_ls_shell.percent_reflns_obs               97.5600 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            0.0000 
_refine_ls_shell.R_factor_R_work                  0.1850 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.2290 
# 
_struct.entry_id                     9FPQ 
_struct.title                        'Crystal structure of carbonic anhydrase II with methyl 4-benzylsulfanyl-3-sulfamoyl-benzoate' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9FPQ 
_struct_keywords.text            'DRUG DESIGN, CARBONIC ANHYDRASE, BENZENESULFONAMIDE, LYASE-LYASE INHIBITOR COMPLEX, LYASE' 
_struct_keywords.pdbx_keywords   LYASE 
# 
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 5 ? 
F N N 6 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CAH2_HUMAN 
_struct_ref.pdbx_db_accession          P00918 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              9FPQ 
_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                 260 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P00918 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  260 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       261 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 510   ? 
1 MORE         3     ? 
1 'SSA (A^2)'  11650 ? 
# 
_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_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 GLY A 12  ? ASP A 19  ? GLY A 12  ASP A 19  5 ? 8 
HELX_P HELX_P2 AA2 PHE A 20  ? GLY A 25  ? PHE A 20  GLY A 25  5 ? 6 
HELX_P HELX_P3 AA3 LYS A 126 ? GLY A 128 ? LYS A 127 GLY A 129 5 ? 3 
HELX_P HELX_P4 AA4 ASP A 129 ? VAL A 134 ? ASP A 130 VAL A 135 1 ? 6 
HELX_P HELX_P5 AA5 LYS A 153 ? GLY A 155 ? LYS A 154 GLY A 156 5 ? 3 
HELX_P HELX_P6 AA6 LEU A 156 ? LEU A 163 ? LEU A 157 LEU A 164 1 ? 8 
HELX_P HELX_P7 AA7 ASP A 164 ? LYS A 167 ? ASP A 165 LYS A 168 5 ? 4 
HELX_P HELX_P8 AA8 ASP A 179 ? LEU A 184 ? ASP A 180 LEU A 185 5 ? 6 
HELX_P HELX_P9 AA9 SER A 218 ? ARG A 226 ? SER A 219 ARG A 227 1 ? 9 
# 
_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 
metalc1 metalc ? ? A HIS 94  NE2 ? ? ? 1_555 B ZN    . ZN  ? ? A HIS 94  A ZN    301 1_555 ? ? ? ? ? ? ? 2.048 ? ? 
metalc2 metalc ? ? A HIS 96  NE2 ? ? ? 1_555 B ZN    . ZN  ? ? A HIS 96  A ZN    301 1_555 ? ? ? ? ? ? ? 2.059 ? ? 
metalc3 metalc ? ? A HIS 119 ND1 ? ? ? 1_555 B ZN    . ZN  ? ? A HIS 119 A ZN    301 1_555 ? ? ? ? ? ? ? 2.059 ? ? 
metalc4 metalc ? ? B ZN  .   ZN  ? ? ? 1_555 C A1IEL . N13 ? ? A ZN  301 A A1IEL 302 1_555 ? ? ? ? ? ? ? 1.908 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
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 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 NE2 ? A HIS   96  ? A HIS   96  ? 1_555 104.8 ? 
2 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS   119 ? A HIS   119 ? 1_555 110.2 ? 
3 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS   119 ? A HIS   119 ? 1_555 99.0  ? 
4 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N13 ? C A1IEL .   ? A A1IEL 302 ? 1_555 114.8 ? 
5 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N13 ? C A1IEL .   ? A A1IEL 302 ? 1_555 109.7 ? 
6 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N13 ? C A1IEL .   ? A A1IEL 302 ? 1_555 116.5 ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 SER 29  A . ? SER 29  A PRO 30  A ? PRO 30  A 1 0.49 
2 PRO 200 A . ? PRO 201 A PRO 201 A ? PRO 202 A 1 8.48 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2  ? 
AA2 ? 10 ? 
AA3 ? 6  ? 
# 
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  ? parallel      
AA2 1 2  ? parallel      
AA2 2 3  ? anti-parallel 
AA2 3 4  ? anti-parallel 
AA2 4 5  ? parallel      
AA2 5 6  ? anti-parallel 
AA2 6 7  ? anti-parallel 
AA2 7 8  ? anti-parallel 
AA2 8 9  ? anti-parallel 
AA2 9 10 ? anti-parallel 
AA3 1 2  ? anti-parallel 
AA3 2 3  ? anti-parallel 
AA3 3 4  ? anti-parallel 
AA3 4 5  ? anti-parallel 
AA3 5 6  ? 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  ASP A 32  ? ILE A 33  ? ASP A 32  ILE A 33  
AA1 2  THR A 108 ? VAL A 109 ? THR A 108 VAL A 109 
AA2 1  LYS A 39  ? TYR A 40  ? LYS A 39  TYR A 40  
AA2 2  LYS A 256 ? ALA A 257 ? LYS A 257 ALA A 258 
AA2 3  TYR A 190 ? GLY A 195 ? TYR A 191 GLY A 196 
AA2 4  VAL A 206 ? LEU A 211 ? VAL A 207 LEU A 212 
AA2 5  LEU A 140 ? VAL A 149 ? LEU A 141 VAL A 150 
AA2 6  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
AA2 7  TYR A 88  ? TRP A 97  ? TYR A 88  TRP A 97  
AA2 8  PHE A 66  ? PHE A 70  ? PHE A 66  PHE A 70  
AA2 9  SER A 56  ? ASN A 61  ? SER A 56  ASN A 61  
AA2 10 SER A 172 ? ASP A 174 ? SER A 173 ASP A 175 
AA3 1  LEU A 47  ? SER A 50  ? LEU A 47  SER A 50  
AA3 2  VAL A 78  ? GLY A 81  ? VAL A 78  GLY A 81  
AA3 3  TYR A 88  ? TRP A 97  ? TYR A 88  TRP A 97  
AA3 4  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
AA3 5  LEU A 140 ? VAL A 149 ? LEU A 141 VAL A 150 
AA3 6  ILE A 215 ? VAL A 217 ? ILE A 216 VAL A 218 
# 
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 ILE A 33  ? N ILE A 33  O THR A 108 ? O THR A 108 
AA2 1 2  N LYS A 39  ? N LYS A 39  O ALA A 257 ? O ALA A 258 
AA2 2 3  O LYS A 256 ? O LYS A 257 N THR A 192 ? N THR A 193 
AA2 3 4  N GLY A 195 ? N GLY A 196 O VAL A 206 ? O VAL A 207 
AA2 4 5  O ILE A 209 ? O ILE A 210 N GLY A 144 ? N GLY A 145 
AA2 5 6  O ILE A 145 ? O ILE A 146 N LEU A 118 ? N LEU A 118 
AA2 6 7  O HIS A 119 ? O HIS A 119 N HIS A 94  ? N HIS A 94  
AA2 7 8  O PHE A 93  ? O PHE A 93  N VAL A 68  ? N VAL A 68  
AA2 8 9  O GLU A 69  ? O GLU A 69  N ARG A 58  ? N ARG A 58  
AA2 9 10 N ILE A 59  ? N ILE A 59  O ALA A 173 ? O ALA A 174 
AA3 1 2  N SER A 50  ? N SER A 50  O VAL A 78  ? O VAL A 78  
AA3 2 3  N LEU A 79  ? N LEU A 79  O TYR A 88  ? O TYR A 88  
AA3 3 4  N HIS A 94  ? N HIS A 94  O HIS A 119 ? O HIS A 119 
AA3 4 5  N LEU A 118 ? N LEU A 118 O ILE A 145 ? O ILE A 146 
AA3 5 6  N PHE A 146 ? N PHE A 147 O ILE A 215 ? O ILE A 216 
# 
_pdbx_entry_details.entry_id                   9FPQ 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   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 ARG A 27  ? ? -142.02 57.11   
2 1 LYS A 76  ? ? -111.53 -83.93  
3 1 LYS A 111 ? ? 74.12   -0.19   
4 1 PHE A 176 ? ? -151.64 73.27   
5 1 ASN A 244 ? ? -97.85  48.64   
6 1 LYS A 252 ? ? 60.93   -137.42 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A MET 1 ? A MET 1 
2 1 Y 1 A SER 2 ? A SER 2 
# 
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 
A1IEL C1   C  Y N 1   
A1IEL C2   C  Y N 2   
A1IEL C3   C  Y N 3   
A1IEL C4   C  Y N 4   
A1IEL C5   C  Y N 5   
A1IEL C6   C  Y N 6   
A1IEL C9   C  N N 7   
A1IEL C16  C  N N 8   
A1IEL C20  C  Y N 9   
A1IEL O14  O  N N 10  
A1IEL S11  S  N N 11  
A1IEL O12  O  N N 12  
A1IEL N13  N  N N 13  
A1IEL C7   C  N N 14  
A1IEL O10  O  N N 15  
A1IEL O8   O  N N 16  
A1IEL S15  S  N N 17  
A1IEL C17  C  Y N 18  
A1IEL C21  C  Y N 19  
A1IEL C22  C  Y N 20  
A1IEL C19  C  Y N 21  
A1IEL C18  C  Y N 22  
A1IEL H1   H  N N 23  
A1IEL H2   H  N N 24  
A1IEL H3   H  N N 25  
A1IEL H4   H  N N 26  
A1IEL H5   H  N N 27  
A1IEL H6   H  N N 28  
A1IEL H7   H  N N 29  
A1IEL H8   H  N N 30  
A1IEL H9   H  N N 31  
A1IEL H10  H  N N 32  
A1IEL H11  H  N N 33  
A1IEL H12  H  N N 34  
A1IEL H13  H  N N 35  
A1IEL H14  H  N N 36  
A1IEL H15  H  N N 37  
ALA   N    N  N N 38  
ALA   CA   C  N S 39  
ALA   C    C  N N 40  
ALA   O    O  N N 41  
ALA   CB   C  N N 42  
ALA   OXT  O  N N 43  
ALA   H    H  N N 44  
ALA   H2   H  N N 45  
ALA   HA   H  N N 46  
ALA   HB1  H  N N 47  
ALA   HB2  H  N N 48  
ALA   HB3  H  N N 49  
ALA   HXT  H  N N 50  
ARG   N    N  N N 51  
ARG   CA   C  N S 52  
ARG   C    C  N N 53  
ARG   O    O  N N 54  
ARG   CB   C  N N 55  
ARG   CG   C  N N 56  
ARG   CD   C  N N 57  
ARG   NE   N  N N 58  
ARG   CZ   C  N N 59  
ARG   NH1  N  N N 60  
ARG   NH2  N  N N 61  
ARG   OXT  O  N N 62  
ARG   H    H  N N 63  
ARG   H2   H  N N 64  
ARG   HA   H  N N 65  
ARG   HB2  H  N N 66  
ARG   HB3  H  N N 67  
ARG   HG2  H  N N 68  
ARG   HG3  H  N N 69  
ARG   HD2  H  N N 70  
ARG   HD3  H  N N 71  
ARG   HE   H  N N 72  
ARG   HH11 H  N N 73  
ARG   HH12 H  N N 74  
ARG   HH21 H  N N 75  
ARG   HH22 H  N N 76  
ARG   HXT  H  N N 77  
ASN   N    N  N N 78  
ASN   CA   C  N S 79  
ASN   C    C  N N 80  
ASN   O    O  N N 81  
ASN   CB   C  N N 82  
ASN   CG   C  N N 83  
ASN   OD1  O  N N 84  
ASN   ND2  N  N N 85  
ASN   OXT  O  N N 86  
ASN   H    H  N N 87  
ASN   H2   H  N N 88  
ASN   HA   H  N N 89  
ASN   HB2  H  N N 90  
ASN   HB3  H  N N 91  
ASN   HD21 H  N N 92  
ASN   HD22 H  N N 93  
ASN   HXT  H  N N 94  
ASP   N    N  N N 95  
ASP   CA   C  N S 96  
ASP   C    C  N N 97  
ASP   O    O  N N 98  
ASP   CB   C  N N 99  
ASP   CG   C  N N 100 
ASP   OD1  O  N N 101 
ASP   OD2  O  N N 102 
ASP   OXT  O  N N 103 
ASP   H    H  N N 104 
ASP   H2   H  N N 105 
ASP   HA   H  N N 106 
ASP   HB2  H  N N 107 
ASP   HB3  H  N N 108 
ASP   HD2  H  N N 109 
ASP   HXT  H  N N 110 
BCN   N1   N  N N 111 
BCN   C1   C  N N 112 
BCN   C2   C  N N 113 
BCN   O21  O  N N 114 
BCN   O22  O  N N 115 
BCN   C3   C  N N 116 
BCN   C4   C  N N 117 
BCN   O4   O  N N 118 
BCN   C5   C  N N 119 
BCN   C6   C  N N 120 
BCN   O6   O  N N 121 
BCN   H11  H  N N 122 
BCN   H12  H  N N 123 
BCN   HO2  H  N N 124 
BCN   H31  H  N N 125 
BCN   H32  H  N N 126 
BCN   H41  H  N N 127 
BCN   H42  H  N N 128 
BCN   HO4  H  N N 129 
BCN   H51  H  N N 130 
BCN   H52  H  N N 131 
BCN   H61  H  N N 132 
BCN   H62  H  N N 133 
BCN   HO6  H  N N 134 
CYS   N    N  N N 135 
CYS   CA   C  N R 136 
CYS   C    C  N N 137 
CYS   O    O  N N 138 
CYS   CB   C  N N 139 
CYS   SG   S  N N 140 
CYS   OXT  O  N N 141 
CYS   H    H  N N 142 
CYS   H2   H  N N 143 
CYS   HA   H  N N 144 
CYS   HB2  H  N N 145 
CYS   HB3  H  N N 146 
CYS   HG   H  N N 147 
CYS   HXT  H  N N 148 
DMS   S    S  N N 149 
DMS   O    O  N N 150 
DMS   C1   C  N N 151 
DMS   C2   C  N N 152 
DMS   H11  H  N N 153 
DMS   H12  H  N N 154 
DMS   H13  H  N N 155 
DMS   H21  H  N N 156 
DMS   H22  H  N N 157 
DMS   H23  H  N N 158 
GLN   N    N  N N 159 
GLN   CA   C  N S 160 
GLN   C    C  N N 161 
GLN   O    O  N N 162 
GLN   CB   C  N N 163 
GLN   CG   C  N N 164 
GLN   CD   C  N N 165 
GLN   OE1  O  N N 166 
GLN   NE2  N  N N 167 
GLN   OXT  O  N N 168 
GLN   H    H  N N 169 
GLN   H2   H  N N 170 
GLN   HA   H  N N 171 
GLN   HB2  H  N N 172 
GLN   HB3  H  N N 173 
GLN   HG2  H  N N 174 
GLN   HG3  H  N N 175 
GLN   HE21 H  N N 176 
GLN   HE22 H  N N 177 
GLN   HXT  H  N N 178 
GLU   N    N  N N 179 
GLU   CA   C  N S 180 
GLU   C    C  N N 181 
GLU   O    O  N N 182 
GLU   CB   C  N N 183 
GLU   CG   C  N N 184 
GLU   CD   C  N N 185 
GLU   OE1  O  N N 186 
GLU   OE2  O  N N 187 
GLU   OXT  O  N N 188 
GLU   H    H  N N 189 
GLU   H2   H  N N 190 
GLU   HA   H  N N 191 
GLU   HB2  H  N N 192 
GLU   HB3  H  N N 193 
GLU   HG2  H  N N 194 
GLU   HG3  H  N N 195 
GLU   HE2  H  N N 196 
GLU   HXT  H  N N 197 
GLY   N    N  N N 198 
GLY   CA   C  N N 199 
GLY   C    C  N N 200 
GLY   O    O  N N 201 
GLY   OXT  O  N N 202 
GLY   H    H  N N 203 
GLY   H2   H  N N 204 
GLY   HA2  H  N N 205 
GLY   HA3  H  N N 206 
GLY   HXT  H  N N 207 
HIS   N    N  N N 208 
HIS   CA   C  N S 209 
HIS   C    C  N N 210 
HIS   O    O  N N 211 
HIS   CB   C  N N 212 
HIS   CG   C  Y N 213 
HIS   ND1  N  Y N 214 
HIS   CD2  C  Y N 215 
HIS   CE1  C  Y N 216 
HIS   NE2  N  Y N 217 
HIS   OXT  O  N N 218 
HIS   H    H  N N 219 
HIS   H2   H  N N 220 
HIS   HA   H  N N 221 
HIS   HB2  H  N N 222 
HIS   HB3  H  N N 223 
HIS   HD1  H  N N 224 
HIS   HD2  H  N N 225 
HIS   HE1  H  N N 226 
HIS   HE2  H  N N 227 
HIS   HXT  H  N N 228 
HOH   O    O  N N 229 
HOH   H1   H  N N 230 
HOH   H2   H  N N 231 
ILE   N    N  N N 232 
ILE   CA   C  N S 233 
ILE   C    C  N N 234 
ILE   O    O  N N 235 
ILE   CB   C  N S 236 
ILE   CG1  C  N N 237 
ILE   CG2  C  N N 238 
ILE   CD1  C  N N 239 
ILE   OXT  O  N N 240 
ILE   H    H  N N 241 
ILE   H2   H  N N 242 
ILE   HA   H  N N 243 
ILE   HB   H  N N 244 
ILE   HG12 H  N N 245 
ILE   HG13 H  N N 246 
ILE   HG21 H  N N 247 
ILE   HG22 H  N N 248 
ILE   HG23 H  N N 249 
ILE   HD11 H  N N 250 
ILE   HD12 H  N N 251 
ILE   HD13 H  N N 252 
ILE   HXT  H  N N 253 
LEU   N    N  N N 254 
LEU   CA   C  N S 255 
LEU   C    C  N N 256 
LEU   O    O  N N 257 
LEU   CB   C  N N 258 
LEU   CG   C  N N 259 
LEU   CD1  C  N N 260 
LEU   CD2  C  N N 261 
LEU   OXT  O  N N 262 
LEU   H    H  N N 263 
LEU   H2   H  N N 264 
LEU   HA   H  N N 265 
LEU   HB2  H  N N 266 
LEU   HB3  H  N N 267 
LEU   HG   H  N N 268 
LEU   HD11 H  N N 269 
LEU   HD12 H  N N 270 
LEU   HD13 H  N N 271 
LEU   HD21 H  N N 272 
LEU   HD22 H  N N 273 
LEU   HD23 H  N N 274 
LEU   HXT  H  N N 275 
LYS   N    N  N N 276 
LYS   CA   C  N S 277 
LYS   C    C  N N 278 
LYS   O    O  N N 279 
LYS   CB   C  N N 280 
LYS   CG   C  N N 281 
LYS   CD   C  N N 282 
LYS   CE   C  N N 283 
LYS   NZ   N  N N 284 
LYS   OXT  O  N N 285 
LYS   H    H  N N 286 
LYS   H2   H  N N 287 
LYS   HA   H  N N 288 
LYS   HB2  H  N N 289 
LYS   HB3  H  N N 290 
LYS   HG2  H  N N 291 
LYS   HG3  H  N N 292 
LYS   HD2  H  N N 293 
LYS   HD3  H  N N 294 
LYS   HE2  H  N N 295 
LYS   HE3  H  N N 296 
LYS   HZ1  H  N N 297 
LYS   HZ2  H  N N 298 
LYS   HZ3  H  N N 299 
LYS   HXT  H  N N 300 
MET   N    N  N N 301 
MET   CA   C  N S 302 
MET   C    C  N N 303 
MET   O    O  N N 304 
MET   CB   C  N N 305 
MET   CG   C  N N 306 
MET   SD   S  N N 307 
MET   CE   C  N N 308 
MET   OXT  O  N N 309 
MET   H    H  N N 310 
MET   H2   H  N N 311 
MET   HA   H  N N 312 
MET   HB2  H  N N 313 
MET   HB3  H  N N 314 
MET   HG2  H  N N 315 
MET   HG3  H  N N 316 
MET   HE1  H  N N 317 
MET   HE2  H  N N 318 
MET   HE3  H  N N 319 
MET   HXT  H  N N 320 
PHE   N    N  N N 321 
PHE   CA   C  N S 322 
PHE   C    C  N N 323 
PHE   O    O  N N 324 
PHE   CB   C  N N 325 
PHE   CG   C  Y N 326 
PHE   CD1  C  Y N 327 
PHE   CD2  C  Y N 328 
PHE   CE1  C  Y N 329 
PHE   CE2  C  Y N 330 
PHE   CZ   C  Y N 331 
PHE   OXT  O  N N 332 
PHE   H    H  N N 333 
PHE   H2   H  N N 334 
PHE   HA   H  N N 335 
PHE   HB2  H  N N 336 
PHE   HB3  H  N N 337 
PHE   HD1  H  N N 338 
PHE   HD2  H  N N 339 
PHE   HE1  H  N N 340 
PHE   HE2  H  N N 341 
PHE   HZ   H  N N 342 
PHE   HXT  H  N N 343 
PRO   N    N  N N 344 
PRO   CA   C  N S 345 
PRO   C    C  N N 346 
PRO   O    O  N N 347 
PRO   CB   C  N N 348 
PRO   CG   C  N N 349 
PRO   CD   C  N N 350 
PRO   OXT  O  N N 351 
PRO   H    H  N N 352 
PRO   HA   H  N N 353 
PRO   HB2  H  N N 354 
PRO   HB3  H  N N 355 
PRO   HG2  H  N N 356 
PRO   HG3  H  N N 357 
PRO   HD2  H  N N 358 
PRO   HD3  H  N N 359 
PRO   HXT  H  N N 360 
SER   N    N  N N 361 
SER   CA   C  N S 362 
SER   C    C  N N 363 
SER   O    O  N N 364 
SER   CB   C  N N 365 
SER   OG   O  N N 366 
SER   OXT  O  N N 367 
SER   H    H  N N 368 
SER   H2   H  N N 369 
SER   HA   H  N N 370 
SER   HB2  H  N N 371 
SER   HB3  H  N N 372 
SER   HG   H  N N 373 
SER   HXT  H  N N 374 
THR   N    N  N N 375 
THR   CA   C  N S 376 
THR   C    C  N N 377 
THR   O    O  N N 378 
THR   CB   C  N R 379 
THR   OG1  O  N N 380 
THR   CG2  C  N N 381 
THR   OXT  O  N N 382 
THR   H    H  N N 383 
THR   H2   H  N N 384 
THR   HA   H  N N 385 
THR   HB   H  N N 386 
THR   HG1  H  N N 387 
THR   HG21 H  N N 388 
THR   HG22 H  N N 389 
THR   HG23 H  N N 390 
THR   HXT  H  N N 391 
TRP   N    N  N N 392 
TRP   CA   C  N S 393 
TRP   C    C  N N 394 
TRP   O    O  N N 395 
TRP   CB   C  N N 396 
TRP   CG   C  Y N 397 
TRP   CD1  C  Y N 398 
TRP   CD2  C  Y N 399 
TRP   NE1  N  Y N 400 
TRP   CE2  C  Y N 401 
TRP   CE3  C  Y N 402 
TRP   CZ2  C  Y N 403 
TRP   CZ3  C  Y N 404 
TRP   CH2  C  Y N 405 
TRP   OXT  O  N N 406 
TRP   H    H  N N 407 
TRP   H2   H  N N 408 
TRP   HA   H  N N 409 
TRP   HB2  H  N N 410 
TRP   HB3  H  N N 411 
TRP   HD1  H  N N 412 
TRP   HE1  H  N N 413 
TRP   HE3  H  N N 414 
TRP   HZ2  H  N N 415 
TRP   HZ3  H  N N 416 
TRP   HH2  H  N N 417 
TRP   HXT  H  N N 418 
TYR   N    N  N N 419 
TYR   CA   C  N S 420 
TYR   C    C  N N 421 
TYR   O    O  N N 422 
TYR   CB   C  N N 423 
TYR   CG   C  Y N 424 
TYR   CD1  C  Y N 425 
TYR   CD2  C  Y N 426 
TYR   CE1  C  Y N 427 
TYR   CE2  C  Y N 428 
TYR   CZ   C  Y N 429 
TYR   OH   O  N N 430 
TYR   OXT  O  N N 431 
TYR   H    H  N N 432 
TYR   H2   H  N N 433 
TYR   HA   H  N N 434 
TYR   HB2  H  N N 435 
TYR   HB3  H  N N 436 
TYR   HD1  H  N N 437 
TYR   HD2  H  N N 438 
TYR   HE1  H  N N 439 
TYR   HE2  H  N N 440 
TYR   HH   H  N N 441 
TYR   HXT  H  N N 442 
VAL   N    N  N N 443 
VAL   CA   C  N S 444 
VAL   C    C  N N 445 
VAL   O    O  N N 446 
VAL   CB   C  N N 447 
VAL   CG1  C  N N 448 
VAL   CG2  C  N N 449 
VAL   OXT  O  N N 450 
VAL   H    H  N N 451 
VAL   H2   H  N N 452 
VAL   HA   H  N N 453 
VAL   HB   H  N N 454 
VAL   HG11 H  N N 455 
VAL   HG12 H  N N 456 
VAL   HG13 H  N N 457 
VAL   HG21 H  N N 458 
VAL   HG22 H  N N 459 
VAL   HG23 H  N N 460 
VAL   HXT  H  N N 461 
ZN    ZN   ZN N N 462 
# 
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 
A1IEL C9  O8   sing N N 1   
A1IEL O8  C7   sing N N 2   
A1IEL O10 C7   doub N N 3   
A1IEL C7  C1   sing N N 4   
A1IEL C1  C2   doub Y N 5   
A1IEL C1  C6   sing Y N 6   
A1IEL N13 S11  sing N N 7   
A1IEL C2  C3   sing Y N 8   
A1IEL C6  C5   doub Y N 9   
A1IEL C3  S11  sing N N 10  
A1IEL C3  C4   doub Y N 11  
A1IEL S11 O12  doub N N 12  
A1IEL S11 O14  doub N N 13  
A1IEL C5  C4   sing Y N 14  
A1IEL C4  S15  sing N N 15  
A1IEL S15 C16  sing N N 16  
A1IEL C16 C17  sing N N 17  
A1IEL C20 C17  doub Y N 18  
A1IEL C20 C21  sing Y N 19  
A1IEL C17 C18  sing Y N 20  
A1IEL C21 C22  doub Y N 21  
A1IEL C18 C19  doub Y N 22  
A1IEL C22 C19  sing Y N 23  
A1IEL C2  H1   sing N N 24  
A1IEL C5  H2   sing N N 25  
A1IEL C6  H3   sing N N 26  
A1IEL C9  H4   sing N N 27  
A1IEL C9  H5   sing N N 28  
A1IEL C9  H6   sing N N 29  
A1IEL C16 H7   sing N N 30  
A1IEL C16 H8   sing N N 31  
A1IEL C20 H9   sing N N 32  
A1IEL N13 H10  sing N N 33  
A1IEL N13 H11  sing N N 34  
A1IEL C21 H12  sing N N 35  
A1IEL C22 H13  sing N N 36  
A1IEL C19 H14  sing N N 37  
A1IEL C18 H15  sing N N 38  
ALA   N   CA   sing N N 39  
ALA   N   H    sing N N 40  
ALA   N   H2   sing N N 41  
ALA   CA  C    sing N N 42  
ALA   CA  CB   sing N N 43  
ALA   CA  HA   sing N N 44  
ALA   C   O    doub N N 45  
ALA   C   OXT  sing N N 46  
ALA   CB  HB1  sing N N 47  
ALA   CB  HB2  sing N N 48  
ALA   CB  HB3  sing N N 49  
ALA   OXT HXT  sing N N 50  
ARG   N   CA   sing N N 51  
ARG   N   H    sing N N 52  
ARG   N   H2   sing N N 53  
ARG   CA  C    sing N N 54  
ARG   CA  CB   sing N N 55  
ARG   CA  HA   sing N N 56  
ARG   C   O    doub N N 57  
ARG   C   OXT  sing N N 58  
ARG   CB  CG   sing N N 59  
ARG   CB  HB2  sing N N 60  
ARG   CB  HB3  sing N N 61  
ARG   CG  CD   sing N N 62  
ARG   CG  HG2  sing N N 63  
ARG   CG  HG3  sing N N 64  
ARG   CD  NE   sing N N 65  
ARG   CD  HD2  sing N N 66  
ARG   CD  HD3  sing N N 67  
ARG   NE  CZ   sing N N 68  
ARG   NE  HE   sing N N 69  
ARG   CZ  NH1  sing N N 70  
ARG   CZ  NH2  doub N N 71  
ARG   NH1 HH11 sing N N 72  
ARG   NH1 HH12 sing N N 73  
ARG   NH2 HH21 sing N N 74  
ARG   NH2 HH22 sing N N 75  
ARG   OXT HXT  sing N N 76  
ASN   N   CA   sing N N 77  
ASN   N   H    sing N N 78  
ASN   N   H2   sing N N 79  
ASN   CA  C    sing N N 80  
ASN   CA  CB   sing N N 81  
ASN   CA  HA   sing N N 82  
ASN   C   O    doub N N 83  
ASN   C   OXT  sing N N 84  
ASN   CB  CG   sing N N 85  
ASN   CB  HB2  sing N N 86  
ASN   CB  HB3  sing N N 87  
ASN   CG  OD1  doub N N 88  
ASN   CG  ND2  sing N N 89  
ASN   ND2 HD21 sing N N 90  
ASN   ND2 HD22 sing N N 91  
ASN   OXT HXT  sing N N 92  
ASP   N   CA   sing N N 93  
ASP   N   H    sing N N 94  
ASP   N   H2   sing N N 95  
ASP   CA  C    sing N N 96  
ASP   CA  CB   sing N N 97  
ASP   CA  HA   sing N N 98  
ASP   C   O    doub N N 99  
ASP   C   OXT  sing N N 100 
ASP   CB  CG   sing N N 101 
ASP   CB  HB2  sing N N 102 
ASP   CB  HB3  sing N N 103 
ASP   CG  OD1  doub N N 104 
ASP   CG  OD2  sing N N 105 
ASP   OD2 HD2  sing N N 106 
ASP   OXT HXT  sing N N 107 
BCN   N1  C1   sing N N 108 
BCN   N1  C3   sing N N 109 
BCN   N1  C5   sing N N 110 
BCN   C1  C2   sing N N 111 
BCN   C1  H11  sing N N 112 
BCN   C1  H12  sing N N 113 
BCN   C2  O21  doub N N 114 
BCN   C2  O22  sing N N 115 
BCN   O22 HO2  sing N N 116 
BCN   C3  C4   sing N N 117 
BCN   C3  H31  sing N N 118 
BCN   C3  H32  sing N N 119 
BCN   C4  O4   sing N N 120 
BCN   C4  H41  sing N N 121 
BCN   C4  H42  sing N N 122 
BCN   O4  HO4  sing N N 123 
BCN   C5  C6   sing N N 124 
BCN   C5  H51  sing N N 125 
BCN   C5  H52  sing N N 126 
BCN   C6  O6   sing N N 127 
BCN   C6  H61  sing N N 128 
BCN   C6  H62  sing N N 129 
BCN   O6  HO6  sing N N 130 
CYS   N   CA   sing N N 131 
CYS   N   H    sing N N 132 
CYS   N   H2   sing N N 133 
CYS   CA  C    sing N N 134 
CYS   CA  CB   sing N N 135 
CYS   CA  HA   sing N N 136 
CYS   C   O    doub N N 137 
CYS   C   OXT  sing N N 138 
CYS   CB  SG   sing N N 139 
CYS   CB  HB2  sing N N 140 
CYS   CB  HB3  sing N N 141 
CYS   SG  HG   sing N N 142 
CYS   OXT HXT  sing N N 143 
DMS   S   O    doub N N 144 
DMS   S   C1   sing N N 145 
DMS   S   C2   sing N N 146 
DMS   C1  H11  sing N N 147 
DMS   C1  H12  sing N N 148 
DMS   C1  H13  sing N N 149 
DMS   C2  H21  sing N N 150 
DMS   C2  H22  sing N N 151 
DMS   C2  H23  sing N N 152 
GLN   N   CA   sing N N 153 
GLN   N   H    sing N N 154 
GLN   N   H2   sing N N 155 
GLN   CA  C    sing N N 156 
GLN   CA  CB   sing N N 157 
GLN   CA  HA   sing N N 158 
GLN   C   O    doub N N 159 
GLN   C   OXT  sing N N 160 
GLN   CB  CG   sing N N 161 
GLN   CB  HB2  sing N N 162 
GLN   CB  HB3  sing N N 163 
GLN   CG  CD   sing N N 164 
GLN   CG  HG2  sing N N 165 
GLN   CG  HG3  sing N N 166 
GLN   CD  OE1  doub N N 167 
GLN   CD  NE2  sing N N 168 
GLN   NE2 HE21 sing N N 169 
GLN   NE2 HE22 sing N N 170 
GLN   OXT HXT  sing N N 171 
GLU   N   CA   sing N N 172 
GLU   N   H    sing N N 173 
GLU   N   H2   sing N N 174 
GLU   CA  C    sing N N 175 
GLU   CA  CB   sing N N 176 
GLU   CA  HA   sing N N 177 
GLU   C   O    doub N N 178 
GLU   C   OXT  sing N N 179 
GLU   CB  CG   sing N N 180 
GLU   CB  HB2  sing N N 181 
GLU   CB  HB3  sing N N 182 
GLU   CG  CD   sing N N 183 
GLU   CG  HG2  sing N N 184 
GLU   CG  HG3  sing N N 185 
GLU   CD  OE1  doub N N 186 
GLU   CD  OE2  sing N N 187 
GLU   OE2 HE2  sing N N 188 
GLU   OXT HXT  sing N N 189 
GLY   N   CA   sing N N 190 
GLY   N   H    sing N N 191 
GLY   N   H2   sing N N 192 
GLY   CA  C    sing N N 193 
GLY   CA  HA2  sing N N 194 
GLY   CA  HA3  sing N N 195 
GLY   C   O    doub N N 196 
GLY   C   OXT  sing N N 197 
GLY   OXT HXT  sing N N 198 
HIS   N   CA   sing N N 199 
HIS   N   H    sing N N 200 
HIS   N   H2   sing N N 201 
HIS   CA  C    sing N N 202 
HIS   CA  CB   sing N N 203 
HIS   CA  HA   sing N N 204 
HIS   C   O    doub N N 205 
HIS   C   OXT  sing N N 206 
HIS   CB  CG   sing N N 207 
HIS   CB  HB2  sing N N 208 
HIS   CB  HB3  sing N N 209 
HIS   CG  ND1  sing Y N 210 
HIS   CG  CD2  doub Y N 211 
HIS   ND1 CE1  doub Y N 212 
HIS   ND1 HD1  sing N N 213 
HIS   CD2 NE2  sing Y N 214 
HIS   CD2 HD2  sing N N 215 
HIS   CE1 NE2  sing Y N 216 
HIS   CE1 HE1  sing N N 217 
HIS   NE2 HE2  sing N N 218 
HIS   OXT HXT  sing N N 219 
HOH   O   H1   sing N N 220 
HOH   O   H2   sing N N 221 
ILE   N   CA   sing N N 222 
ILE   N   H    sing N N 223 
ILE   N   H2   sing N N 224 
ILE   CA  C    sing N N 225 
ILE   CA  CB   sing N N 226 
ILE   CA  HA   sing N N 227 
ILE   C   O    doub N N 228 
ILE   C   OXT  sing N N 229 
ILE   CB  CG1  sing N N 230 
ILE   CB  CG2  sing N N 231 
ILE   CB  HB   sing N N 232 
ILE   CG1 CD1  sing N N 233 
ILE   CG1 HG12 sing N N 234 
ILE   CG1 HG13 sing N N 235 
ILE   CG2 HG21 sing N N 236 
ILE   CG2 HG22 sing N N 237 
ILE   CG2 HG23 sing N N 238 
ILE   CD1 HD11 sing N N 239 
ILE   CD1 HD12 sing N N 240 
ILE   CD1 HD13 sing N N 241 
ILE   OXT HXT  sing N N 242 
LEU   N   CA   sing N N 243 
LEU   N   H    sing N N 244 
LEU   N   H2   sing N N 245 
LEU   CA  C    sing N N 246 
LEU   CA  CB   sing N N 247 
LEU   CA  HA   sing N N 248 
LEU   C   O    doub N N 249 
LEU   C   OXT  sing N N 250 
LEU   CB  CG   sing N N 251 
LEU   CB  HB2  sing N N 252 
LEU   CB  HB3  sing N N 253 
LEU   CG  CD1  sing N N 254 
LEU   CG  CD2  sing N N 255 
LEU   CG  HG   sing N N 256 
LEU   CD1 HD11 sing N N 257 
LEU   CD1 HD12 sing N N 258 
LEU   CD1 HD13 sing N N 259 
LEU   CD2 HD21 sing N N 260 
LEU   CD2 HD22 sing N N 261 
LEU   CD2 HD23 sing N N 262 
LEU   OXT HXT  sing N N 263 
LYS   N   CA   sing N N 264 
LYS   N   H    sing N N 265 
LYS   N   H2   sing N N 266 
LYS   CA  C    sing N N 267 
LYS   CA  CB   sing N N 268 
LYS   CA  HA   sing N N 269 
LYS   C   O    doub N N 270 
LYS   C   OXT  sing N N 271 
LYS   CB  CG   sing N N 272 
LYS   CB  HB2  sing N N 273 
LYS   CB  HB3  sing N N 274 
LYS   CG  CD   sing N N 275 
LYS   CG  HG2  sing N N 276 
LYS   CG  HG3  sing N N 277 
LYS   CD  CE   sing N N 278 
LYS   CD  HD2  sing N N 279 
LYS   CD  HD3  sing N N 280 
LYS   CE  NZ   sing N N 281 
LYS   CE  HE2  sing N N 282 
LYS   CE  HE3  sing N N 283 
LYS   NZ  HZ1  sing N N 284 
LYS   NZ  HZ2  sing N N 285 
LYS   NZ  HZ3  sing N N 286 
LYS   OXT HXT  sing N N 287 
MET   N   CA   sing N N 288 
MET   N   H    sing N N 289 
MET   N   H2   sing N N 290 
MET   CA  C    sing N N 291 
MET   CA  CB   sing N N 292 
MET   CA  HA   sing N N 293 
MET   C   O    doub N N 294 
MET   C   OXT  sing N N 295 
MET   CB  CG   sing N N 296 
MET   CB  HB2  sing N N 297 
MET   CB  HB3  sing N N 298 
MET   CG  SD   sing N N 299 
MET   CG  HG2  sing N N 300 
MET   CG  HG3  sing N N 301 
MET   SD  CE   sing N N 302 
MET   CE  HE1  sing N N 303 
MET   CE  HE2  sing N N 304 
MET   CE  HE3  sing N N 305 
MET   OXT HXT  sing N N 306 
PHE   N   CA   sing N N 307 
PHE   N   H    sing N N 308 
PHE   N   H2   sing N N 309 
PHE   CA  C    sing N N 310 
PHE   CA  CB   sing N N 311 
PHE   CA  HA   sing N N 312 
PHE   C   O    doub N N 313 
PHE   C   OXT  sing N N 314 
PHE   CB  CG   sing N N 315 
PHE   CB  HB2  sing N N 316 
PHE   CB  HB3  sing N N 317 
PHE   CG  CD1  doub Y N 318 
PHE   CG  CD2  sing Y N 319 
PHE   CD1 CE1  sing Y N 320 
PHE   CD1 HD1  sing N N 321 
PHE   CD2 CE2  doub Y N 322 
PHE   CD2 HD2  sing N N 323 
PHE   CE1 CZ   doub Y N 324 
PHE   CE1 HE1  sing N N 325 
PHE   CE2 CZ   sing Y N 326 
PHE   CE2 HE2  sing N N 327 
PHE   CZ  HZ   sing N N 328 
PHE   OXT HXT  sing N N 329 
PRO   N   CA   sing N N 330 
PRO   N   CD   sing N N 331 
PRO   N   H    sing N N 332 
PRO   CA  C    sing N N 333 
PRO   CA  CB   sing N N 334 
PRO   CA  HA   sing N N 335 
PRO   C   O    doub N N 336 
PRO   C   OXT  sing N N 337 
PRO   CB  CG   sing N N 338 
PRO   CB  HB2  sing N N 339 
PRO   CB  HB3  sing N N 340 
PRO   CG  CD   sing N N 341 
PRO   CG  HG2  sing N N 342 
PRO   CG  HG3  sing N N 343 
PRO   CD  HD2  sing N N 344 
PRO   CD  HD3  sing N N 345 
PRO   OXT HXT  sing N N 346 
SER   N   CA   sing N N 347 
SER   N   H    sing N N 348 
SER   N   H2   sing N N 349 
SER   CA  C    sing N N 350 
SER   CA  CB   sing N N 351 
SER   CA  HA   sing N N 352 
SER   C   O    doub N N 353 
SER   C   OXT  sing N N 354 
SER   CB  OG   sing N N 355 
SER   CB  HB2  sing N N 356 
SER   CB  HB3  sing N N 357 
SER   OG  HG   sing N N 358 
SER   OXT HXT  sing N N 359 
THR   N   CA   sing N N 360 
THR   N   H    sing N N 361 
THR   N   H2   sing N N 362 
THR   CA  C    sing N N 363 
THR   CA  CB   sing N N 364 
THR   CA  HA   sing N N 365 
THR   C   O    doub N N 366 
THR   C   OXT  sing N N 367 
THR   CB  OG1  sing N N 368 
THR   CB  CG2  sing N N 369 
THR   CB  HB   sing N N 370 
THR   OG1 HG1  sing N N 371 
THR   CG2 HG21 sing N N 372 
THR   CG2 HG22 sing N N 373 
THR   CG2 HG23 sing N N 374 
THR   OXT HXT  sing N N 375 
TRP   N   CA   sing N N 376 
TRP   N   H    sing N N 377 
TRP   N   H2   sing N N 378 
TRP   CA  C    sing N N 379 
TRP   CA  CB   sing N N 380 
TRP   CA  HA   sing N N 381 
TRP   C   O    doub N N 382 
TRP   C   OXT  sing N N 383 
TRP   CB  CG   sing N N 384 
TRP   CB  HB2  sing N N 385 
TRP   CB  HB3  sing N N 386 
TRP   CG  CD1  doub Y N 387 
TRP   CG  CD2  sing Y N 388 
TRP   CD1 NE1  sing Y N 389 
TRP   CD1 HD1  sing N N 390 
TRP   CD2 CE2  doub Y N 391 
TRP   CD2 CE3  sing Y N 392 
TRP   NE1 CE2  sing Y N 393 
TRP   NE1 HE1  sing N N 394 
TRP   CE2 CZ2  sing Y N 395 
TRP   CE3 CZ3  doub Y N 396 
TRP   CE3 HE3  sing N N 397 
TRP   CZ2 CH2  doub Y N 398 
TRP   CZ2 HZ2  sing N N 399 
TRP   CZ3 CH2  sing Y N 400 
TRP   CZ3 HZ3  sing N N 401 
TRP   CH2 HH2  sing N N 402 
TRP   OXT HXT  sing N N 403 
TYR   N   CA   sing N N 404 
TYR   N   H    sing N N 405 
TYR   N   H2   sing N N 406 
TYR   CA  C    sing N N 407 
TYR   CA  CB   sing N N 408 
TYR   CA  HA   sing N N 409 
TYR   C   O    doub N N 410 
TYR   C   OXT  sing N N 411 
TYR   CB  CG   sing N N 412 
TYR   CB  HB2  sing N N 413 
TYR   CB  HB3  sing N N 414 
TYR   CG  CD1  doub Y N 415 
TYR   CG  CD2  sing Y N 416 
TYR   CD1 CE1  sing Y N 417 
TYR   CD1 HD1  sing N N 418 
TYR   CD2 CE2  doub Y N 419 
TYR   CD2 HD2  sing N N 420 
TYR   CE1 CZ   doub Y N 421 
TYR   CE1 HE1  sing N N 422 
TYR   CE2 CZ   sing Y N 423 
TYR   CE2 HE2  sing N N 424 
TYR   CZ  OH   sing N N 425 
TYR   OH  HH   sing N N 426 
TYR   OXT HXT  sing N N 427 
VAL   N   CA   sing N N 428 
VAL   N   H    sing N N 429 
VAL   N   H2   sing N N 430 
VAL   CA  C    sing N N 431 
VAL   CA  CB   sing N N 432 
VAL   CA  HA   sing N N 433 
VAL   C   O    doub N N 434 
VAL   C   OXT  sing N N 435 
VAL   CB  CG1  sing N N 436 
VAL   CB  CG2  sing N N 437 
VAL   CB  HB   sing N N 438 
VAL   CG1 HG11 sing N N 439 
VAL   CG1 HG12 sing N N 440 
VAL   CG1 HG13 sing N N 441 
VAL   CG2 HG21 sing N N 442 
VAL   CG2 HG22 sing N N 443 
VAL   CG2 HG23 sing N N 444 
VAL   OXT HXT  sing N N 445 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   4HT0 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9FPQ 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.023640 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.005988 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.024225 
_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]   0.014285 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
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   . HIS   A 1 3   ? 13.817  -0.280  6.417   1.00 30.81 ? 3   HIS   A N   1 
ATOM   2    C  CA  . HIS   A 1 3   ? 13.497  -1.312  7.470   1.00 33.49 ? 3   HIS   A CA  1 
ATOM   3    C  C   . HIS   A 1 3   ? 12.420  -0.798  8.431   1.00 37.52 ? 3   HIS   A C   1 
ATOM   4    O  O   . HIS   A 1 3   ? 12.668  -0.554  9.624   1.00 38.70 ? 3   HIS   A O   1 
ATOM   5    C  CB  . HIS   A 1 3   ? 14.758  -1.685  8.269   1.00 35.55 ? 3   HIS   A CB  1 
ATOM   6    C  CG  . HIS   A 1 3   ? 14.573  -2.941  9.052   1.00 35.30 ? 3   HIS   A CG  1 
ATOM   7    N  ND1 . HIS   A 1 3   ? 14.108  -2.946  10.372  1.00 32.78 ? 3   HIS   A ND1 1 
ATOM   8    C  CD2 . HIS   A 1 3   ? 14.757  -4.236  8.696   1.00 36.64 ? 3   HIS   A CD2 1 
ATOM   9    C  CE1 . HIS   A 1 3   ? 14.036  -4.195  10.790  1.00 32.45 ? 3   HIS   A CE1 1 
ATOM   10   N  NE2 . HIS   A 1 3   ? 14.426  -5.007  9.786   1.00 35.94 ? 3   HIS   A NE2 1 
ATOM   11   N  N   . HIS   A 1 4   ? 11.196  -0.660  7.915   1.00 32.77 ? 4   HIS   A N   1 
ATOM   12   C  CA  . HIS   A 1 4   ? 10.148  -0.059  8.724   1.00 30.87 ? 4   HIS   A CA  1 
ATOM   13   C  C   . HIS   A 1 4   ? 9.419   -1.148  9.510   1.00 25.30 ? 4   HIS   A C   1 
ATOM   14   O  O   . HIS   A 1 4   ? 9.588   -2.333  9.259   1.00 24.09 ? 4   HIS   A O   1 
ATOM   15   C  CB  . HIS   A 1 4   ? 9.206   0.739   7.818   1.00 38.42 ? 4   HIS   A CB  1 
ATOM   16   C  CG  . HIS   A 1 4   ? 8.977   2.128   8.310   1.00 54.42 ? 4   HIS   A CG  1 
ATOM   17   N  ND1 . HIS   A 1 4   ? 7.933   2.913   7.851   1.00 62.46 ? 4   HIS   A ND1 1 
ATOM   18   C  CD2 . HIS   A 1 4   ? 9.644   2.870   9.226   1.00 61.67 ? 4   HIS   A CD2 1 
ATOM   19   C  CE1 . HIS   A 1 4   ? 7.970   4.087   8.458   1.00 75.26 ? 4   HIS   A CE1 1 
ATOM   20   N  NE2 . HIS   A 1 4   ? 9.017   4.085   9.309   1.00 74.77 ? 4   HIS   A NE2 1 
ATOM   21   N  N   . TRP   A 1 5   ? 8.576   -0.727  10.449  1.00 22.33 ? 5   TRP   A N   1 
ATOM   22   C  CA  . TRP   A 1 5   ? 7.864   -1.676  11.290  1.00 18.39 ? 5   TRP   A CA  1 
ATOM   23   C  C   . TRP   A 1 5   ? 6.829   -2.429  10.474  1.00 16.87 ? 5   TRP   A C   1 
ATOM   24   O  O   . TRP   A 1 5   ? 6.322   -1.961  9.436   1.00 19.69 ? 5   TRP   A O   1 
ATOM   25   C  CB  . TRP   A 1 5   ? 7.222   -0.950  12.475  1.00 19.64 ? 5   TRP   A CB  1 
ATOM   26   C  CG  . TRP   A 1 5   ? 6.063   -0.062  12.105  1.00 18.63 ? 5   TRP   A CG  1 
ATOM   27   C  CD1 . TRP   A 1 5   ? 6.077   1.293   11.853  1.00 19.84 ? 5   TRP   A CD1 1 
ATOM   28   C  CD2 . TRP   A 1 5   ? 4.679   -0.460  12.030  1.00 18.69 ? 5   TRP   A CD2 1 
ATOM   29   N  NE1 . TRP   A 1 5   ? 4.813   1.726   11.553  1.00 19.69 ? 5   TRP   A NE1 1 
ATOM   30   C  CE2 . TRP   A 1 5   ? 3.933   0.689   11.664  1.00 18.52 ? 5   TRP   A CE2 1 
ATOM   31   C  CE3 . TRP   A 1 5   ? 3.996   -1.665  12.266  1.00 16.58 ? 5   TRP   A CE3 1 
ATOM   32   C  CZ2 . TRP   A 1 5   ? 2.548   0.662   11.488  1.00 19.72 ? 5   TRP   A CZ2 1 
ATOM   33   C  CZ3 . TRP   A 1 5   ? 2.624   -1.704  12.036  1.00 17.85 ? 5   TRP   A CZ3 1 
ATOM   34   C  CH2 . TRP   A 1 5   ? 1.913   -0.536  11.717  1.00 18.89 ? 5   TRP   A CH2 1 
ATOM   35   N  N   . GLY   A 1 6   ? 6.506   -3.620  10.975  1.00 15.96 ? 6   GLY   A N   1 
ATOM   36   C  CA  . GLY   A 1 6   ? 5.429   -4.394  10.394  1.00 17.26 ? 6   GLY   A CA  1 
ATOM   37   C  C   . GLY   A 1 6   ? 5.111   -5.605  11.279  1.00 16.99 ? 6   GLY   A C   1 
ATOM   38   O  O   . GLY   A 1 6   ? 5.158   -5.526  12.504  1.00 16.74 ? 6   GLY   A O   1 
ATOM   39   N  N   . TYR   A 1 7   ? 4.752   -6.705  10.621  1.00 20.80 ? 7   TYR   A N   1 
ATOM   40   C  CA  . TYR   A 1 7   ? 4.370   -7.906  11.332  1.00 21.10 ? 7   TYR   A CA  1 
ATOM   41   C  C   . TYR   A 1 7   ? 5.029   -9.075  10.614  1.00 29.35 ? 7   TYR   A C   1 
ATOM   42   O  O   . TYR   A 1 7   ? 4.507   -10.199 10.594  1.00 33.52 ? 7   TYR   A O   1 
ATOM   43   C  CB  . TYR   A 1 7   ? 2.872   -8.117  11.159  1.00 22.62 ? 7   TYR   A CB  1 
ATOM   44   C  CG  . TYR   A 1 7   ? 2.015   -7.039  11.775  1.00 16.93 ? 7   TYR   A CG  1 
ATOM   45   C  CD1 . TYR   A 1 7   ? 1.651   -7.098  13.121  1.00 17.10 ? 7   TYR   A CD1 1 
ATOM   46   C  CD2 . TYR   A 1 7   ? 1.559   -5.989  10.992  1.00 18.63 ? 7   TYR   A CD2 1 
ATOM   47   C  CE1 . TYR   A 1 7   ? 0.831   -6.098  13.648  1.00 17.03 ? 7   TYR   A CE1 1 
ATOM   48   C  CE2 . TYR   A 1 7   ? 0.777   -4.978  11.525  1.00 16.78 ? 7   TYR   A CE2 1 
ATOM   49   C  CZ  . TYR   A 1 7   ? 0.407   -5.053  12.856  1.00 17.77 ? 7   TYR   A CZ  1 
ATOM   50   O  OH  . TYR   A 1 7   ? -0.378  -4.031  13.290  1.00 17.19 ? 7   TYR   A OH  1 
ATOM   51   N  N   . GLY   A 1 8   ? 6.173   -8.784  9.999   1.00 27.24 ? 8   GLY   A N   1 
ATOM   52   C  CA  . GLY   A 1 8   ? 6.892   -9.819  9.291   1.00 25.97 ? 8   GLY   A CA  1 
ATOM   53   C  C   . GLY   A 1 8   ? 7.796   -10.584 10.253  1.00 24.85 ? 8   GLY   A C   1 
ATOM   54   O  O   . GLY   A 1 8   ? 7.681   -10.488 11.467  1.00 25.01 ? 8   GLY   A O   1 
ATOM   55   N  N   . LYS   A 1 9   ? 8.771   -11.289 9.677   1.00 25.11 ? 9   LYS   A N   1 
ATOM   56   C  CA  . LYS   A 1 9   ? 9.624   -12.133 10.494  1.00 28.78 ? 9   LYS   A CA  1 
ATOM   57   C  C   . LYS   A 1 9   ? 10.692  -11.344 11.262  1.00 26.72 ? 9   LYS   A C   1 
ATOM   58   O  O   . LYS   A 1 9   ? 11.240  -11.898 12.213  1.00 29.61 ? 9   LYS   A O   1 
ATOM   59   C  CB  . LYS   A 1 9   ? 10.212  -13.239 9.611   1.00 29.87 ? 9   LYS   A CB  1 
ATOM   60   C  CG  . LYS   A 1 9   ? 9.290   -14.428 9.369   1.00 37.67 ? 9   LYS   A CG  1 
ATOM   61   C  CD  . LYS   A 1 9   ? 9.972   -15.573 8.590   1.00 45.81 ? 9   LYS   A CD  1 
ATOM   62   C  CE  . LYS   A 1 9   ? 9.696   -15.623 7.095   1.00 43.75 ? 9   LYS   A CE  1 
ATOM   63   N  NZ  . LYS   A 1 9   ? 8.276   -15.943 6.793   1.00 41.68 ? 9   LYS   A NZ  1 
ATOM   64   N  N   . HIS   A 1 10  ? 11.006  -10.084 10.869  1.00 25.12 ? 10  HIS   A N   1 
ATOM   65   C  CA  . HIS   A 1 10  ? 12.135  -9.343  11.434  1.00 22.85 ? 10  HIS   A CA  1 
ATOM   66   C  C   . HIS   A 1 10  ? 11.784  -7.920  11.915  1.00 22.82 ? 10  HIS   A C   1 
ATOM   67   O  O   . HIS   A 1 10  ? 12.636  -7.164  12.386  1.00 24.33 ? 10  HIS   A O   1 
ATOM   68   C  CB  . HIS   A 1 10  ? 13.195  -9.186  10.311  1.00 22.60 ? 10  HIS   A CB  1 
ATOM   69   C  CG  . HIS   A 1 10  ? 13.745  -10.518 9.899   1.00 28.71 ? 10  HIS   A CG  1 
ATOM   70   N  ND1 . HIS   A 1 10  ? 14.736  -11.148 10.630  1.00 30.18 ? 10  HIS   A ND1 1 
ATOM   71   C  CD2 . HIS   A 1 10  ? 13.430  -11.338 8.859   1.00 30.66 ? 10  HIS   A CD2 1 
ATOM   72   C  CE1 . HIS   A 1 10  ? 14.997  -12.329 10.074  1.00 24.63 ? 10  HIS   A CE1 1 
ATOM   73   N  NE2 . HIS   A 1 10  ? 14.214  -12.466 8.974   1.00 30.22 ? 10  HIS   A NE2 1 
ATOM   74   N  N   . ASN   A 1 11  ? 10.503  -7.515  11.759  1.00 21.42 ? 11  ASN   A N   1 
ATOM   75   C  CA  . ASN   A 1 11  ? 10.162  -6.131  12.082  1.00 21.30 ? 11  ASN   A CA  1 
ATOM   76   C  C   . ASN   A 1 11  ? 8.843   -6.069  12.873  1.00 20.85 ? 11  ASN   A C   1 
ATOM   77   O  O   . ASN   A 1 11  ? 8.160   -5.030  12.917  1.00 18.80 ? 11  ASN   A O   1 
ATOM   78   C  CB  . ASN   A 1 11  ? 9.987   -5.339  10.787  1.00 20.53 ? 11  ASN   A CB  1 
ATOM   79   C  CG  . ASN   A 1 11  ? 8.883   -5.875  9.897   1.00 22.25 ? 11  ASN   A CG  1 
ATOM   80   O  OD1 . ASN   A 1 11  ? 8.284   -6.921  10.175  1.00 22.03 ? 11  ASN   A OD1 1 
ATOM   81   N  ND2 . ASN   A 1 11  ? 8.588   -5.178  8.811   1.00 21.77 ? 11  ASN   A ND2 1 
ATOM   82   N  N   . GLY   A 1 12  ? 8.509   -7.188  13.516  1.00 21.24 ? 12  GLY   A N   1 
ATOM   83   C  CA  . GLY   A 1 12  ? 7.198   -7.362  14.129  1.00 19.70 ? 12  GLY   A CA  1 
ATOM   84   C  C   . GLY   A 1 12  ? 7.140   -6.779  15.544  1.00 19.67 ? 12  GLY   A C   1 
ATOM   85   O  O   . GLY   A 1 12  ? 8.043   -6.074  16.008  1.00 18.39 ? 12  GLY   A O   1 
ATOM   86   N  N   . PRO   A 1 13  ? 6.019   -7.016  16.277  1.00 17.22 ? 13  PRO   A N   1 
ATOM   87   C  CA  . PRO   A 1 13  ? 5.769   -6.358  17.552  1.00 17.44 ? 13  PRO   A CA  1 
ATOM   88   C  C   . PRO   A 1 13  ? 6.885   -6.358  18.590  1.00 18.44 ? 13  PRO   A C   1 
ATOM   89   O  O   . PRO   A 1 13  ? 7.056   -5.361  19.291  1.00 18.83 ? 13  PRO   A O   1 
ATOM   90   C  CB  . PRO   A 1 13  ? 4.518   -7.095  18.065  1.00 18.41 ? 13  PRO   A CB  1 
ATOM   91   C  CG  . PRO   A 1 13  ? 3.771   -7.400  16.812  1.00 17.66 ? 13  PRO   A CG  1 
ATOM   92   C  CD  . PRO   A 1 13  ? 4.846   -7.776  15.799  1.00 18.85 ? 13  PRO   A CD  1 
ATOM   93   N  N   . GLU   A 1 14  ? 7.687   -7.425  18.607  1.00 19.28 ? 14  GLU   A N   1 
ATOM   94   C  CA  . GLU   A 1 14  ? 8.753   -7.530  19.588  1.00 18.10 ? 14  GLU   A CA  1 
ATOM   95   C  C   . GLU   A 1 14  ? 9.912   -6.554  19.299  1.00 19.09 ? 14  GLU   A C   1 
ATOM   96   O  O   . GLU   A 1 14  ? 10.778  -6.347  20.144  1.00 19.86 ? 14  GLU   A O   1 
ATOM   97   C  CB  . GLU   A 1 14  ? 9.144   -9.004  19.692  1.00 23.23 ? 14  GLU   A CB  1 
ATOM   98   C  CG  . GLU   A 1 14  ? 9.803   -9.551  18.406  1.00 24.00 ? 14  GLU   A CG  1 
ATOM   99   C  CD  . GLU   A 1 14  ? 9.037   -10.042 17.170  1.00 32.05 ? 14  GLU   A CD  1 
ATOM   100  O  OE1 . GLU   A 1 14  ? 7.841   -9.677  16.972  1.00 25.75 ? 14  GLU   A OE1 1 
ATOM   101  O  OE2 . GLU   A 1 14  ? 9.689   -10.774 16.344  1.00 31.81 ? 14  GLU   A OE2 1 
ATOM   102  N  N   . HIS   A 1 15  ? 9.916   -5.945  18.091  1.00 17.38 ? 15  HIS   A N   1 
ATOM   103  C  CA  . HIS   A 1 15  ? 10.953  -5.008  17.666  1.00 16.40 ? 15  HIS   A CA  1 
ATOM   104  C  C   . HIS   A 1 15  ? 10.542  -3.544  17.825  1.00 17.48 ? 15  HIS   A C   1 
ATOM   105  O  O   . HIS   A 1 15  ? 11.389  -2.644  17.772  1.00 18.55 ? 15  HIS   A O   1 
ATOM   106  C  CB  . HIS   A 1 15  ? 11.326  -5.235  16.179  1.00 16.98 ? 15  HIS   A CB  1 
ATOM   107  C  CG  . HIS   A 1 15  ? 11.970  -6.566  15.954  1.00 19.05 ? 15  HIS   A CG  1 
ATOM   108  N  ND1 . HIS   A 1 15  ? 13.321  -6.764  16.170  1.00 22.78 ? 15  HIS   A ND1 1 
ATOM   109  C  CD2 . HIS   A 1 15  ? 11.472  -7.745  15.510  1.00 20.34 ? 15  HIS   A CD2 1 
ATOM   110  C  CE1 . HIS   A 1 15  ? 13.598  -8.045  15.944  1.00 21.44 ? 15  HIS   A CE1 1 
ATOM   111  N  NE2 . HIS   A 1 15  ? 12.521  -8.658  15.481  1.00 23.51 ? 15  HIS   A NE2 1 
ATOM   112  N  N   . TRP   A 1 16  ? 9.232   -3.301  17.993  1.00 15.95 ? 16  TRP   A N   1 
ATOM   113  C  CA  . TRP   A 1 16  ? 8.728   -1.941  17.866  1.00 14.99 ? 16  TRP   A CA  1 
ATOM   114  C  C   . TRP   A 1 16  ? 9.307   -0.966  18.898  1.00 15.01 ? 16  TRP   A C   1 
ATOM   115  O  O   . TRP   A 1 16  ? 9.392   0.253   18.633  1.00 16.14 ? 16  TRP   A O   1 
ATOM   116  C  CB  . TRP   A 1 16  ? 7.186   -1.978  17.973  1.00 14.63 ? 16  TRP   A CB  1 
ATOM   117  C  CG  . TRP   A 1 16  ? 6.518   -2.690  16.829  1.00 14.52 ? 16  TRP   A CG  1 
ATOM   118  C  CD1 . TRP   A 1 16  ? 7.029   -3.115  15.631  1.00 13.62 ? 16  TRP   A CD1 1 
ATOM   119  C  CD2 . TRP   A 1 16  ? 5.105   -2.989  16.759  1.00 13.99 ? 16  TRP   A CD2 1 
ATOM   120  N  NE1 . TRP   A 1 16  ? 6.060   -3.684  14.849  1.00 14.94 ? 16  TRP   A NE1 1 
ATOM   121  C  CE2 . TRP   A 1 16  ? 4.850   -3.563  15.492  1.00 14.47 ? 16  TRP   A CE2 1 
ATOM   122  C  CE3 . TRP   A 1 16  ? 4.030   -2.702  17.608  1.00 13.62 ? 16  TRP   A CE3 1 
ATOM   123  C  CZ2 . TRP   A 1 16  ? 3.567   -3.973  15.092  1.00 15.10 ? 16  TRP   A CZ2 1 
ATOM   124  C  CZ3 . TRP   A 1 16  ? 2.779   -3.131  17.237  1.00 15.70 ? 16  TRP   A CZ3 1 
ATOM   125  C  CH2 . TRP   A 1 16  ? 2.537   -3.725  15.998  1.00 14.24 ? 16  TRP   A CH2 1 
ATOM   126  N  N   . HIS   A 1 17  ? 9.703   -1.480  20.083  1.00 17.09 ? 17  HIS   A N   1 
ATOM   127  C  CA  . HIS   A 1 17  ? 10.181  -0.621  21.146  1.00 15.97 ? 17  HIS   A CA  1 
ATOM   128  C  C   . HIS   A 1 17  ? 11.453  0.162   20.764  1.00 17.06 ? 17  HIS   A C   1 
ATOM   129  O  O   . HIS   A 1 17  ? 11.688  1.221   21.334  1.00 17.96 ? 17  HIS   A O   1 
ATOM   130  C  CB  . HIS   A 1 17  ? 10.453  -1.416  22.432  1.00 16.07 ? 17  HIS   A CB  1 
ATOM   131  C  CG  . HIS   A 1 17  ? 11.615  -2.341  22.317  1.00 17.72 ? 17  HIS   A CG  1 
ATOM   132  N  ND1 . HIS   A 1 17  ? 12.874  -1.979  22.803  1.00 22.62 ? 17  HIS   A ND1 1 
ATOM   133  C  CD2 . HIS   A 1 17  ? 11.750  -3.546  21.731  1.00 19.28 ? 17  HIS   A CD2 1 
ATOM   134  C  CE1 . HIS   A 1 17  ? 13.717  -2.949  22.526  1.00 20.22 ? 17  HIS   A CE1 1 
ATOM   135  N  NE2 . HIS   A 1 17  ? 13.097  -3.889  21.865  1.00 22.36 ? 17  HIS   A NE2 1 
ATOM   136  N  N   . LYS   A 1 18  ? 12.213  -0.367  19.793  1.00 18.80 ? 18  LYS   A N   1 
ATOM   137  C  CA  . LYS   A 1 18  ? 13.447  0.309   19.377  1.00 20.94 ? 18  LYS   A CA  1 
ATOM   138  C  C   . LYS   A 1 18  ? 13.133  1.647   18.698  1.00 21.87 ? 18  LYS   A C   1 
ATOM   139  O  O   . LYS   A 1 18  ? 13.774  2.648   18.994  1.00 23.79 ? 18  LYS   A O   1 
ATOM   140  C  CB  . LYS   A 1 18  ? 14.268  -0.618  18.476  1.00 21.48 ? 18  LYS   A CB  1 
ATOM   141  C  CG  . LYS   A 1 18  ? 14.891  -1.813  19.200  1.00 21.24 ? 18  LYS   A CG  1 
ATOM   142  C  CD  . LYS   A 1 18  ? 15.568  -2.806  18.259  1.00 22.42 ? 18  LYS   A CD  1 
ATOM   143  C  CE  . LYS   A 1 18  ? 14.605  -3.749  17.585  1.00 22.56 ? 18  LYS   A CE  1 
ATOM   144  N  NZ  . LYS   A 1 18  ? 15.234  -4.667  16.588  1.00 19.84 ? 18  LYS   A NZ  1 
ATOM   145  N  N   . ASP   A 1 19  ? 12.110  1.702   17.834  1.00 21.36 ? 19  ASP   A N   1 
ATOM   146  C  CA  . ASP   A 1 19  ? 11.699  2.987   17.275  1.00 24.21 ? 19  ASP   A CA  1 
ATOM   147  C  C   . ASP   A 1 19  ? 10.699  3.758   18.141  1.00 22.69 ? 19  ASP   A C   1 
ATOM   148  O  O   . ASP   A 1 19  ? 10.611  4.974   18.016  1.00 21.40 ? 19  ASP   A O   1 
ATOM   149  C  CB  . ASP   A 1 19  ? 11.174  2.855   15.853  1.00 29.89 ? 19  ASP   A CB  1 
ATOM   150  C  CG  . ASP   A 1 19  ? 12.302  2.710   14.855  1.00 39.25 ? 19  ASP   A CG  1 
ATOM   151  O  OD1 . ASP   A 1 19  ? 13.214  3.552   14.885  1.00 43.67 ? 19  ASP   A OD1 1 
ATOM   152  O  OD2 . ASP   A 1 19  ? 12.276  1.727   14.103  1.00 54.90 ? 19  ASP   A OD2 1 
ATOM   153  N  N   . PHE   A 1 20  ? 9.921   3.045   18.987  1.00 19.16 ? 20  PHE   A N   1 
ATOM   154  C  CA  . PHE   A 1 20  ? 8.811   3.623   19.730  1.00 18.33 ? 20  PHE   A CA  1 
ATOM   155  C  C   . PHE   A 1 20  ? 8.918   3.140   21.162  1.00 18.12 ? 20  PHE   A C   1 
ATOM   156  O  O   . PHE   A 1 20  ? 8.264   2.161   21.534  1.00 16.84 ? 20  PHE   A O   1 
ATOM   157  C  CB  . PHE   A 1 20  ? 7.482   3.187   19.093  1.00 18.28 ? 20  PHE   A CB  1 
ATOM   158  C  CG  . PHE   A 1 20  ? 7.393   3.586   17.645  1.00 17.88 ? 20  PHE   A CG  1 
ATOM   159  C  CD1 . PHE   A 1 20  ? 7.109   4.898   17.298  1.00 21.36 ? 20  PHE   A CD1 1 
ATOM   160  C  CD2 . PHE   A 1 20  ? 7.679   2.662   16.643  1.00 19.22 ? 20  PHE   A CD2 1 
ATOM   161  C  CE1 . PHE   A 1 20  ? 7.066   5.239   15.951  1.00 20.80 ? 20  PHE   A CE1 1 
ATOM   162  C  CE2 . PHE   A 1 20  ? 7.696   3.021   15.307  1.00 18.45 ? 20  PHE   A CE2 1 
ATOM   163  C  CZ  . PHE   A 1 20  ? 7.383   4.320   14.975  1.00 20.40 ? 20  PHE   A CZ  1 
ATOM   164  N  N   A PRO   A 1 21  ? 9.793   3.743   22.003  0.50 17.17 ? 21  PRO   A N   1 
ATOM   165  N  N   B PRO   A 1 21  ? 9.790   3.751   21.995  0.50 18.29 ? 21  PRO   A N   1 
ATOM   166  C  CA  A PRO   A 1 21  ? 10.006  3.237   23.362  0.50 17.27 ? 21  PRO   A CA  1 
ATOM   167  C  CA  B PRO   A 1 21  ? 10.012  3.257   23.359  0.50 18.88 ? 21  PRO   A CA  1 
ATOM   168  C  C   A PRO   A 1 21  ? 8.744   3.152   24.219  0.50 18.95 ? 21  PRO   A C   1 
ATOM   169  C  C   B PRO   A 1 21  ? 8.771   3.164   24.252  0.50 20.94 ? 21  PRO   A C   1 
ATOM   170  O  O   A PRO   A 1 21  ? 8.729   2.422   25.213  0.50 18.24 ? 21  PRO   A O   1 
ATOM   171  O  O   B PRO   A 1 21  ? 8.782   2.416   25.233  0.50 20.10 ? 21  PRO   A O   1 
ATOM   172  C  CB  A PRO   A 1 21  ? 11.053  4.199   23.953  0.50 18.05 ? 21  PRO   A CB  1 
ATOM   173  C  CB  B PRO   A 1 21  ? 11.095  4.235   23.852  0.50 19.91 ? 21  PRO   A CB  1 
ATOM   174  C  CG  A PRO   A 1 21  ? 11.098  5.389   23.012  0.50 17.19 ? 21  PRO   A CG  1 
ATOM   175  C  CG  B PRO   A 1 21  ? 11.830  4.623   22.580  0.50 19.61 ? 21  PRO   A CG  1 
ATOM   176  C  CD  A PRO   A 1 21  ? 10.670  4.879   21.655  0.50 17.76 ? 21  PRO   A CD  1 
ATOM   177  C  CD  B PRO   A 1 21  ? 10.692  4.858   21.615  0.50 19.24 ? 21  PRO   A CD  1 
ATOM   178  N  N   A ILE   A 1 22  ? 7.686   3.879   23.808  0.50 16.09 ? 22  ILE   A N   1 
ATOM   179  N  N   B ILE   A 1 22  ? 7.693   3.886   23.885  0.50 18.51 ? 22  ILE   A N   1 
ATOM   180  C  CA  A ILE   A 1 22  ? 6.430   3.844   24.540  0.50 16.20 ? 22  ILE   A CA  1 
ATOM   181  C  CA  B ILE   A 1 22  ? 6.446   3.813   24.635  0.50 19.15 ? 22  ILE   A CA  1 
ATOM   182  C  C   A ILE   A 1 22  ? 5.838   2.438   24.482  0.50 16.51 ? 22  ILE   A C   1 
ATOM   183  C  C   B ILE   A 1 22  ? 5.866   2.402   24.537  0.50 18.34 ? 22  ILE   A C   1 
ATOM   184  O  O   A ILE   A 1 22  ? 4.942   2.127   25.266  0.50 15.67 ? 22  ILE   A O   1 
ATOM   185  O  O   B ILE   A 1 22  ? 4.983   2.056   25.323  0.50 17.10 ? 22  ILE   A O   1 
ATOM   186  C  CB  A ILE   A 1 22  ? 5.452   4.944   24.073  0.50 14.92 ? 22  ILE   A CB  1 
ATOM   187  C  CB  B ILE   A 1 22  ? 5.438   4.908   24.211  0.50 18.78 ? 22  ILE   A CB  1 
ATOM   188  C  CG1 A ILE   A 1 22  ? 4.421   5.270   25.148  0.50 14.25 ? 22  ILE   A CG1 1 
ATOM   189  C  CG1 B ILE   A 1 22  ? 4.378   5.175   25.280  0.50 20.45 ? 22  ILE   A CG1 1 
ATOM   190  C  CG2 A ILE   A 1 22  ? 4.798   4.578   22.743  0.50 15.93 ? 22  ILE   A CG2 1 
ATOM   191  C  CG2 B ILE   A 1 22  ? 4.792   4.565   22.874  0.50 20.34 ? 22  ILE   A CG2 1 
ATOM   192  C  CD1 A ILE   A 1 22  ? 3.432   6.338   24.781  0.50 13.12 ? 22  ILE   A CD1 1 
ATOM   193  C  CD1 B ILE   A 1 22  ? 4.921   5.632   26.619  0.50 21.77 ? 22  ILE   A CD1 1 
ATOM   194  N  N   . ALA   A 1 23  ? 6.391   1.575   23.627  1.00 16.83 ? 23  ALA   A N   1 
ATOM   195  C  CA  . ALA   A 1 23  ? 5.946   0.178   23.525  1.00 15.71 ? 23  ALA   A CA  1 
ATOM   196  C  C   . ALA   A 1 23  ? 6.011   -0.549  24.869  1.00 17.04 ? 23  ALA   A C   1 
ATOM   197  O  O   . ALA   A 1 23  ? 5.307   -1.566  25.051  1.00 16.76 ? 23  ALA   A O   1 
ATOM   198  C  CB  . ALA   A 1 23  ? 6.730   -0.591  22.458  1.00 15.90 ? 23  ALA   A CB  1 
ATOM   199  N  N   . LYS   A 1 24  ? 6.952   -0.132  25.747  1.00 17.17 ? 24  LYS   A N   1 
ATOM   200  C  CA  . LYS   A 1 24  ? 7.116   -0.779  27.052  1.00 17.96 ? 24  LYS   A CA  1 
ATOM   201  C  C   . LYS   A 1 24  ? 6.513   0.131   28.118  1.00 19.17 ? 24  LYS   A C   1 
ATOM   202  O  O   . LYS   A 1 24  ? 6.889   0.065   29.297  1.00 21.39 ? 24  LYS   A O   1 
ATOM   203  C  CB  . LYS   A 1 24  ? 8.612   -1.042  27.325  1.00 20.31 ? 24  LYS   A CB  1 
ATOM   204  C  CG  . LYS   A 1 24  ? 9.265   -1.997  26.348  1.00 22.85 ? 24  LYS   A CG  1 
ATOM   205  C  CD  . LYS   A 1 24  ? 10.755  -2.099  26.704  1.00 26.76 ? 24  LYS   A CD  1 
ATOM   206  C  CE  . LYS   A 1 24  ? 11.504  -3.060  25.803  1.00 28.56 ? 24  LYS   A CE  1 
ATOM   207  N  NZ  . LYS   A 1 24  ? 11.122  -4.467  26.058  1.00 32.18 ? 24  LYS   A NZ  1 
ATOM   208  N  N   . GLY   A 1 25  ? 5.527   0.970   27.727  1.00 18.47 ? 25  GLY   A N   1 
ATOM   209  C  CA  . GLY   A 1 25  ? 4.906   1.902   28.670  1.00 18.20 ? 25  GLY   A CA  1 
ATOM   210  C  C   . GLY   A 1 25  ? 3.900   1.320   29.678  1.00 16.72 ? 25  GLY   A C   1 
ATOM   211  O  O   . GLY   A 1 25  ? 3.718   0.104   29.799  1.00 19.22 ? 25  GLY   A O   1 
ATOM   212  N  N   . GLU   A 1 26  ? 3.243   2.249   30.370  1.00 17.62 ? 26  GLU   A N   1 
ATOM   213  C  CA  . GLU   A 1 26  ? 2.386   1.896   31.490  1.00 20.80 ? 26  GLU   A CA  1 
ATOM   214  C  C   . GLU   A 1 26  ? 0.939   1.608   31.094  1.00 17.06 ? 26  GLU   A C   1 
ATOM   215  O  O   . GLU   A 1 26  ? 0.188   1.107   31.948  1.00 19.44 ? 26  GLU   A O   1 
ATOM   216  C  CB  . GLU   A 1 26  ? 2.411   3.008   32.552  1.00 23.36 ? 26  GLU   A CB  1 
ATOM   217  C  CG  . GLU   A 1 26  ? 3.761   3.195   33.261  1.00 29.72 ? 26  GLU   A CG  1 
ATOM   218  C  CD  . GLU   A 1 26  ? 4.329   1.942   33.918  1.00 35.53 ? 26  GLU   A CD  1 
ATOM   219  O  OE1 . GLU   A 1 26  ? 3.657   1.358   34.826  1.00 37.45 ? 26  GLU   A OE1 1 
ATOM   220  O  OE2 . GLU   A 1 26  ? 5.448   1.520   33.518  1.00 38.89 ? 26  GLU   A OE2 1 
ATOM   221  N  N   . ARG   A 1 27  ? 0.531   1.941   29.859  1.00 16.06 ? 27  ARG   A N   1 
ATOM   222  C  CA  . ARG   A 1 27  ? -0.868  1.718   29.483  1.00 15.34 ? 27  ARG   A CA  1 
ATOM   223  C  C   . ARG   A 1 27  ? -0.946  1.244   28.023  1.00 14.36 ? 27  ARG   A C   1 
ATOM   224  O  O   . ARG   A 1 27  ? -1.649  1.870   27.189  1.00 14.14 ? 27  ARG   A O   1 
ATOM   225  C  CB  . ARG   A 1 27  ? -1.782  2.908   29.824  1.00 19.73 ? 27  ARG   A CB  1 
ATOM   226  C  CG  . ARG   A 1 27  ? -1.454  4.234   29.172  1.00 21.87 ? 27  ARG   A CG  1 
ATOM   227  C  CD  . ARG   A 1 27  ? -2.476  5.349   29.388  1.00 23.93 ? 27  ARG   A CD  1 
ATOM   228  N  NE  . ARG   A 1 27  ? -3.636  5.306   28.480  1.00 21.12 ? 27  ARG   A NE  1 
ATOM   229  C  CZ  . ARG   A 1 27  ? -4.575  6.220   28.447  1.00 21.29 ? 27  ARG   A CZ  1 
ATOM   230  N  NH1 . ARG   A 1 27  ? -4.511  7.311   29.217  1.00 20.78 ? 27  ARG   A NH1 1 
ATOM   231  N  NH2 . ARG   A 1 27  ? -5.561  6.062   27.603  1.00 21.67 ? 27  ARG   A NH2 1 
ATOM   232  N  N   . GLN   A 1 28  ? -0.239  0.122   27.748  1.00 13.35 ? 28  GLN   A N   1 
ATOM   233  C  CA  . GLN   A 1 28  ? -0.177  -0.380  26.364  1.00 13.11 ? 28  GLN   A CA  1 
ATOM   234  C  C   . GLN   A 1 28  ? -1.351  -1.335  26.096  1.00 12.51 ? 28  GLN   A C   1 
ATOM   235  O  O   . GLN   A 1 28  ? -1.852  -1.997  26.992  1.00 14.39 ? 28  GLN   A O   1 
ATOM   236  C  CB  . GLN   A 1 28  ? 1.166   -1.049  26.095  1.00 13.68 ? 28  GLN   A CB  1 
ATOM   237  C  CG  . GLN   A 1 28  ? 2.263   0.030   25.998  1.00 13.72 ? 28  GLN   A CG  1 
ATOM   238  C  CD  . GLN   A 1 28  ? 2.121   0.822   24.702  1.00 12.01 ? 28  GLN   A CD  1 
ATOM   239  O  OE1 . GLN   A 1 28  ? 2.333   0.293   23.600  1.00 14.00 ? 28  GLN   A OE1 1 
ATOM   240  N  NE2 . GLN   A 1 28  ? 1.802   2.097   24.798  1.00 13.08 ? 28  GLN   A NE2 1 
ATOM   241  N  N   . SER   A 1 29  ? -1.746  -1.388  24.813  1.00 11.79 ? 29  SER   A N   1 
ATOM   242  C  CA  . SER   A 1 29  ? -2.799  -2.283  24.346  1.00 12.19 ? 29  SER   A CA  1 
ATOM   243  C  C   . SER   A 1 29  ? -2.309  -3.172  23.220  1.00 13.59 ? 29  SER   A C   1 
ATOM   244  O  O   . SER   A 1 29  ? -1.354  -2.832  22.538  1.00 12.23 ? 29  SER   A O   1 
ATOM   245  C  CB  . SER   A 1 29  ? -3.936  -1.451  23.784  1.00 11.69 ? 29  SER   A CB  1 
ATOM   246  O  OG  . SER   A 1 29  ? -4.594  -0.749  24.854  1.00 11.81 ? 29  SER   A OG  1 
ATOM   247  N  N   . PRO   A 1 30  ? -2.939  -4.328  22.958  1.00 12.72 ? 30  PRO   A N   1 
ATOM   248  C  CA  . PRO   A 1 30  ? -4.114  -4.825  23.687  1.00 13.61 ? 30  PRO   A CA  1 
ATOM   249  C  C   . PRO   A 1 30  ? -3.692  -5.504  24.991  1.00 14.01 ? 30  PRO   A C   1 
ATOM   250  O  O   . PRO   A 1 30  ? -2.497  -5.545  25.340  1.00 13.70 ? 30  PRO   A O   1 
ATOM   251  C  CB  . PRO   A 1 30  ? -4.638  -5.881  22.679  1.00 12.71 ? 30  PRO   A CB  1 
ATOM   252  C  CG  . PRO   A 1 30  ? -3.327  -6.495  22.116  1.00 12.83 ? 30  PRO   A CG  1 
ATOM   253  C  CD  . PRO   A 1 30  ? -2.470  -5.239  21.898  1.00 13.72 ? 30  PRO   A CD  1 
ATOM   254  N  N   . VAL   A 1 31  ? -4.692  -6.063  25.678  1.00 13.19 ? 31  VAL   A N   1 
ATOM   255  C  CA  . VAL   A 1 31  ? -4.519  -6.811  26.923  1.00 13.71 ? 31  VAL   A CA  1 
ATOM   256  C  C   . VAL   A 1 31  ? -5.407  -8.045  26.908  1.00 13.29 ? 31  VAL   A C   1 
ATOM   257  O  O   . VAL   A 1 31  ? -6.382  -8.160  26.148  1.00 13.26 ? 31  VAL   A O   1 
ATOM   258  C  CB  . VAL   A 1 31  ? -4.791  -5.980  28.202  1.00 13.06 ? 31  VAL   A CB  1 
ATOM   259  C  CG1 . VAL   A 1 31  ? -3.868  -4.777  28.329  1.00 14.99 ? 31  VAL   A CG1 1 
ATOM   260  C  CG2 . VAL   A 1 31  ? -6.270  -5.529  28.304  1.00 14.28 ? 31  VAL   A CG2 1 
ATOM   261  N  N   . ASP   A 1 32  ? -5.028  -9.022  27.766  1.00 13.59 ? 32  ASP   A N   1 
ATOM   262  C  CA  . ASP   A 1 32  ? -5.932  -10.123 28.047  1.00 13.98 ? 32  ASP   A CA  1 
ATOM   263  C  C   . ASP   A 1 32  ? -6.982  -9.624  29.028  1.00 13.54 ? 32  ASP   A C   1 
ATOM   264  O  O   . ASP   A 1 32  ? -6.676  -8.986  30.027  1.00 16.42 ? 32  ASP   A O   1 
ATOM   265  C  CB  . ASP   A 1 32  ? -5.179  -11.305 28.665  1.00 14.22 ? 32  ASP   A CB  1 
ATOM   266  C  CG  . ASP   A 1 32  ? -6.095  -12.494 28.966  1.00 17.46 ? 32  ASP   A CG  1 
ATOM   267  O  OD1 . ASP   A 1 32  ? -6.823  -12.949 28.033  1.00 16.07 ? 32  ASP   A OD1 1 
ATOM   268  O  OD2 . ASP   A 1 32  ? -6.167  -12.887 30.187  1.00 18.89 ? 32  ASP   A OD2 1 
ATOM   269  N  N   . ILE   A 1 33  ? -8.241  -9.920  28.717  1.00 13.55 ? 33  ILE   A N   1 
ATOM   270  C  CA  . ILE   A 1 33  ? -9.344  -9.565  29.602  1.00 14.91 ? 33  ILE   A CA  1 
ATOM   271  C  C   . ILE   A 1 33  ? -9.661  -10.787 30.458  1.00 15.73 ? 33  ILE   A C   1 
ATOM   272  O  O   . ILE   A 1 33  ? -10.222 -11.790 29.976  1.00 17.24 ? 33  ILE   A O   1 
ATOM   273  C  CB  . ILE   A 1 33  ? -10.577 -9.112  28.779  1.00 14.56 ? 33  ILE   A CB  1 
ATOM   274  C  CG1 . ILE   A 1 33  ? -10.231 -7.851  27.974  1.00 15.85 ? 33  ILE   A CG1 1 
ATOM   275  C  CG2 . ILE   A 1 33  ? -11.765 -8.910  29.750  1.00 15.69 ? 33  ILE   A CG2 1 
ATOM   276  C  CD1 . ILE   A 1 33  ? -11.252 -7.533  26.881  1.00 16.92 ? 33  ILE   A CD1 1 
ATOM   277  N  N   . ASP   A 1 34  ? -9.289  -10.685 31.734  1.00 17.14 ? 34  ASP   A N   1 
ATOM   278  C  CA  . ASP   A 1 34  ? -9.540  -11.748 32.718  1.00 18.88 ? 34  ASP   A CA  1 
ATOM   279  C  C   . ASP   A 1 34  ? -10.954 -11.532 33.258  1.00 19.96 ? 34  ASP   A C   1 
ATOM   280  O  O   . ASP   A 1 34  ? -11.191 -10.578 34.008  1.00 20.07 ? 34  ASP   A O   1 
ATOM   281  C  CB  . ASP   A 1 34  ? -8.456  -11.754 33.801  1.00 20.90 ? 34  ASP   A CB  1 
ATOM   282  C  CG  . ASP   A 1 34  ? -8.669  -12.732 34.971  1.00 28.11 ? 34  ASP   A CG  1 
ATOM   283  O  OD1 . ASP   A 1 34  ? -9.812  -13.132 35.228  1.00 29.27 ? 34  ASP   A OD1 1 
ATOM   284  O  OD2 . ASP   A 1 34  ? -7.664  -13.124 35.621  1.00 33.73 ? 34  ASP   A OD2 1 
ATOM   285  N  N   . THR   A 1 35  ? -11.914 -12.318 32.789  1.00 19.54 ? 35  THR   A N   1 
ATOM   286  C  CA  . THR   A 1 35  ? -13.321 -11.985 33.010  1.00 19.10 ? 35  THR   A CA  1 
ATOM   287  C  C   . THR   A 1 35  ? -13.699 -12.123 34.475  1.00 22.41 ? 35  THR   A C   1 
ATOM   288  O  O   . THR   A 1 35  ? -14.644 -11.453 34.911  1.00 24.35 ? 35  THR   A O   1 
ATOM   289  C  CB  . THR   A 1 35  ? -14.234 -12.907 32.196  1.00 22.05 ? 35  THR   A CB  1 
ATOM   290  O  OG1 . THR   A 1 35  ? -14.037 -14.237 32.679  1.00 20.19 ? 35  THR   A OG1 1 
ATOM   291  C  CG2 . THR   A 1 35  ? -13.987 -12.827 30.703  1.00 21.53 ? 35  THR   A CG2 1 
ATOM   292  N  N   . HIS   A 1 36  ? -12.960 -12.983 35.206  1.00 20.13 ? 36  HIS   A N   1 
ATOM   293  C  CA  . HIS   A 1 36  ? -13.218 -13.167 36.617  1.00 23.20 ? 36  HIS   A CA  1 
ATOM   294  C  C   . HIS   A 1 36  ? -12.715 -11.976 37.433  1.00 25.02 ? 36  HIS   A C   1 
ATOM   295  O  O   . HIS   A 1 36  ? -13.336 -11.661 38.457  1.00 29.96 ? 36  HIS   A O   1 
ATOM   296  C  CB  . HIS   A 1 36  ? -12.764 -14.588 37.009  1.00 22.23 ? 36  HIS   A CB  1 
ATOM   297  C  CG  . HIS   A 1 36  ? -13.639 -15.642 36.405  1.00 23.15 ? 36  HIS   A CG  1 
ATOM   298  N  ND1 . HIS   A 1 36  ? -14.972 -15.774 36.776  1.00 29.17 ? 36  HIS   A ND1 1 
ATOM   299  C  CD2 . HIS   A 1 36  ? -13.401 -16.600 35.478  1.00 23.67 ? 36  HIS   A CD2 1 
ATOM   300  C  CE1 . HIS   A 1 36  ? -15.523 -16.750 36.083  1.00 33.85 ? 36  HIS   A CE1 1 
ATOM   301  N  NE2 . HIS   A 1 36  ? -14.573 -17.258 35.278  1.00 31.39 ? 36  HIS   A NE2 1 
ATOM   302  N  N   . THR   A 1 37  ? -11.666 -11.273 36.970  1.00 24.08 ? 37  THR   A N   1 
ATOM   303  C  CA  . THR   A 1 37  ? -11.044 -10.169 37.682  1.00 24.16 ? 37  THR   A CA  1 
ATOM   304  C  C   . THR   A 1 37  ? -11.672 -8.819  37.293  1.00 23.03 ? 37  THR   A C   1 
ATOM   305  O  O   . THR   A 1 37  ? -11.476 -7.822  37.976  1.00 25.14 ? 37  THR   A O   1 
ATOM   306  C  CB  . THR   A 1 37  ? -9.526  -10.237 37.498  1.00 30.61 ? 37  THR   A CB  1 
ATOM   307  O  OG1 . THR   A 1 37  ? -9.215  -11.439 38.197  1.00 36.54 ? 37  THR   A OG1 1 
ATOM   308  C  CG2 . THR   A 1 37  ? -8.772  -9.099  38.146  1.00 35.52 ? 37  THR   A CG2 1 
ATOM   309  N  N   . ALA   A 1 38  ? -12.359 -8.755  36.149  1.00 21.80 ? 38  ALA   A N   1 
ATOM   310  C  CA  . ALA   A 1 38  ? -12.951 -7.487  35.724  1.00 20.48 ? 38  ALA   A CA  1 
ATOM   311  C  C   . ALA   A 1 38  ? -14.036 -7.105  36.728  1.00 25.33 ? 38  ALA   A C   1 
ATOM   312  O  O   . ALA   A 1 38  ? -14.784 -7.964  37.166  1.00 26.66 ? 38  ALA   A O   1 
ATOM   313  C  CB  . ALA   A 1 38  ? -13.461 -7.554  34.300  1.00 20.99 ? 38  ALA   A CB  1 
ATOM   314  N  N   . LYS   A 1 39  ? -14.066 -5.835  37.129  1.00 23.91 ? 39  LYS   A N   1 
ATOM   315  C  CA  . LYS   A 1 39  ? -15.081 -5.481  38.112  1.00 25.04 ? 39  LYS   A CA  1 
ATOM   316  C  C   . LYS   A 1 39  ? -16.324 -4.901  37.438  1.00 21.12 ? 39  LYS   A C   1 
ATOM   317  O  O   . LYS   A 1 39  ? -16.270 -3.899  36.712  1.00 19.15 ? 39  LYS   A O   1 
ATOM   318  C  CB  . LYS   A 1 39  ? -14.551 -4.545  39.195  1.00 34.23 ? 39  LYS   A CB  1 
ATOM   319  C  CG  . LYS   A 1 39  ? -15.426 -4.540  40.449  1.00 37.15 ? 39  LYS   A CG  1 
ATOM   320  C  CD  . LYS   A 1 39  ? -14.959 -3.548  41.485  1.00 37.11 ? 39  LYS   A CD  1 
ATOM   321  C  CE  . LYS   A 1 39  ? -16.042 -3.038  42.410  1.00 40.91 ? 39  LYS   A CE  1 
ATOM   322  N  NZ  . LYS   A 1 39  ? -16.532 -4.134  43.274  1.00 42.59 ? 39  LYS   A NZ  1 
ATOM   323  N  N   . TYR   A 1 40  ? -17.470 -5.466  37.803  1.00 24.03 ? 40  TYR   A N   1 
ATOM   324  C  CA  . TYR   A 1 40  ? -18.712 -4.808  37.433  1.00 22.03 ? 40  TYR   A CA  1 
ATOM   325  C  C   . TYR   A 1 40  ? -18.790 -3.411  38.043  1.00 22.04 ? 40  TYR   A C   1 
ATOM   326  O  O   . TYR   A 1 40  ? -18.636 -3.223  39.277  1.00 21.25 ? 40  TYR   A O   1 
ATOM   327  C  CB  . TYR   A 1 40  ? -19.935 -5.642  37.833  1.00 26.20 ? 40  TYR   A CB  1 
ATOM   328  C  CG  . TYR   A 1 40  ? -21.261 -4.940  37.714  1.00 29.49 ? 40  TYR   A CG  1 
ATOM   329  C  CD1 . TYR   A 1 40  ? -21.707 -4.466  36.495  1.00 25.67 ? 40  TYR   A CD1 1 
ATOM   330  C  CD2 . TYR   A 1 40  ? -22.097 -4.778  38.810  1.00 36.47 ? 40  TYR   A CD2 1 
ATOM   331  C  CE1 . TYR   A 1 40  ? -22.929 -3.851  36.337  1.00 29.88 ? 40  TYR   A CE1 1 
ATOM   332  C  CE2 . TYR   A 1 40  ? -23.330 -4.147  38.680  1.00 35.97 ? 40  TYR   A CE2 1 
ATOM   333  C  CZ  . TYR   A 1 40  ? -23.740 -3.672  37.446  1.00 35.87 ? 40  TYR   A CZ  1 
ATOM   334  O  OH  . TYR   A 1 40  ? -24.937 -3.034  37.302  1.00 38.35 ? 40  TYR   A OH  1 
ATOM   335  N  N   . ASP   A 1 41  ? -19.113 -2.430  37.194  1.00 20.08 ? 41  ASP   A N   1 
ATOM   336  C  CA  . ASP   A 1 41  ? -19.194 -1.045  37.651  1.00 22.09 ? 41  ASP   A CA  1 
ATOM   337  C  C   . ASP   A 1 41  ? -20.596 -0.518  37.394  1.00 28.02 ? 41  ASP   A C   1 
ATOM   338  O  O   . ASP   A 1 41  ? -20.927 -0.164  36.271  1.00 24.32 ? 41  ASP   A O   1 
ATOM   339  C  CB  . ASP   A 1 41  ? -18.147 -0.137  37.000  1.00 27.34 ? 41  ASP   A CB  1 
ATOM   340  C  CG  . ASP   A 1 41  ? -18.186 1.289   37.531  1.00 30.69 ? 41  ASP   A CG  1 
ATOM   341  O  OD1 . ASP   A 1 41  ? -19.096 1.604   38.356  1.00 31.90 ? 41  ASP   A OD1 1 
ATOM   342  O  OD2 . ASP   A 1 41  ? -17.304 2.061   37.143  1.00 34.37 ? 41  ASP   A OD2 1 
ATOM   343  N  N   . PRO   A 1 42  ? -21.468 -0.447  38.427  1.00 28.20 ? 42  PRO   A N   1 
ATOM   344  C  CA  . PRO   A 1 42  ? -22.868 -0.074  38.209  1.00 32.02 ? 42  PRO   A CA  1 
ATOM   345  C  C   . PRO   A 1 42  ? -22.969 1.405   37.839  1.00 30.23 ? 42  PRO   A C   1 
ATOM   346  O  O   . PRO   A 1 42  ? -24.012 1.832   37.341  1.00 35.04 ? 42  PRO   A O   1 
ATOM   347  C  CB  . PRO   A 1 42  ? -23.503 -0.405  39.579  1.00 31.74 ? 42  PRO   A CB  1 
ATOM   348  C  CG  . PRO   A 1 42  ? -22.374 -0.131  40.555  1.00 33.58 ? 42  PRO   A CG  1 
ATOM   349  C  CD  . PRO   A 1 42  ? -21.161 -0.722  39.848  1.00 32.75 ? 42  PRO   A CD  1 
ATOM   350  N  N   . SER   A 1 43  ? -21.883 2.172   38.031  1.00 29.77 ? 43  SER   A N   1 
ATOM   351  C  CA  . SER   A 1 43  ? -21.877 3.564   37.578  1.00 30.82 ? 43  SER   A CA  1 
ATOM   352  C  C   . SER   A 1 43  ? -21.715 3.734   36.055  1.00 32.80 ? 43  SER   A C   1 
ATOM   353  O  O   . SER   A 1 43  ? -21.893 4.850   35.557  1.00 31.89 ? 43  SER   A O   1 
ATOM   354  C  CB  . SER   A 1 43  ? -20.867 4.424   38.326  1.00 30.99 ? 43  SER   A CB  1 
ATOM   355  O  OG  . SER   A 1 43  ? -19.526 4.072   38.011  1.00 37.53 ? 43  SER   A OG  1 
ATOM   356  N  N   . LEU   A 1 44  ? -21.272 2.694   35.321  1.00 33.38 ? 44  LEU   A N   1 
ATOM   357  C  CA  . LEU   A 1 44  ? -21.091 2.826   33.874  1.00 29.06 ? 44  LEU   A CA  1 
ATOM   358  C  C   . LEU   A 1 44  ? -22.462 2.973   33.215  1.00 32.35 ? 44  LEU   A C   1 
ATOM   359  O  O   . LEU   A 1 44  ? -23.415 2.339   33.641  1.00 32.43 ? 44  LEU   A O   1 
ATOM   360  C  CB  . LEU   A 1 44  ? -20.389 1.584   33.320  1.00 25.13 ? 44  LEU   A CB  1 
ATOM   361  C  CG  . LEU   A 1 44  ? -18.898 1.458   33.608  1.00 22.52 ? 44  LEU   A CG  1 
ATOM   362  C  CD1 . LEU   A 1 44  ? -18.416 0.061   33.205  1.00 22.10 ? 44  LEU   A CD1 1 
ATOM   363  C  CD2 . LEU   A 1 44  ? -18.105 2.550   32.897  1.00 22.77 ? 44  LEU   A CD2 1 
ATOM   364  N  N   . LYS   A 1 45  ? -22.552 3.824   32.188  1.00 32.50 ? 45  LYS   A N   1 
ATOM   365  C  CA  . LYS   A 1 45  ? -23.796 4.005   31.453  1.00 28.80 ? 45  LYS   A CA  1 
ATOM   366  C  C   . LYS   A 1 45  ? -23.828 3.073   30.248  1.00 28.20 ? 45  LYS   A C   1 
ATOM   367  O  O   . LYS   A 1 45  ? -22.795 2.564   29.805  1.00 28.42 ? 45  LYS   A O   1 
ATOM   368  C  CB  . LYS   A 1 45  ? -23.885 5.439   30.944  1.00 29.88 ? 45  LYS   A CB  1 
ATOM   369  C  CG  . LYS   A 1 45  ? -23.729 6.524   31.997  1.00 34.32 ? 45  LYS   A CG  1 
ATOM   370  C  CD  . LYS   A 1 45  ? -23.868 7.925   31.440  0.01 32.47 ? 45  LYS   A CD  1 
ATOM   371  N  N   . PRO   A 1 46  ? -25.028 2.791   29.678  1.00 25.94 ? 46  PRO   A N   1 
ATOM   372  C  CA  . PRO   A 1 46  ? -25.106 2.111   28.386  1.00 25.10 ? 46  PRO   A CA  1 
ATOM   373  C  C   . PRO   A 1 46  ? -24.313 2.931   27.374  1.00 21.04 ? 46  PRO   A C   1 
ATOM   374  O  O   . PRO   A 1 46  ? -24.282 4.167   27.426  1.00 20.35 ? 46  PRO   A O   1 
ATOM   375  C  CB  . PRO   A 1 46  ? -26.618 2.083   28.051  1.00 25.72 ? 46  PRO   A CB  1 
ATOM   376  C  CG  . PRO   A 1 46  ? -27.277 2.166   29.415  1.00 28.68 ? 46  PRO   A CG  1 
ATOM   377  C  CD  . PRO   A 1 46  ? -26.364 3.065   30.249  1.00 26.92 ? 46  PRO   A CD  1 
ATOM   378  N  N   . LEU   A 1 47  ? -23.706 2.207   26.446  1.00 25.32 ? 47  LEU   A N   1 
ATOM   379  C  CA  . LEU   A 1 47  ? -22.984 2.846   25.376  1.00 21.72 ? 47  LEU   A CA  1 
ATOM   380  C  C   . LEU   A 1 47  ? -24.032 3.373   24.393  1.00 24.40 ? 47  LEU   A C   1 
ATOM   381  O  O   . LEU   A 1 47  ? -25.043 2.705   24.162  1.00 25.98 ? 47  LEU   A O   1 
ATOM   382  C  CB  . LEU   A 1 47  ? -22.119 1.754   24.752  1.00 24.56 ? 47  LEU   A CB  1 
ATOM   383  C  CG  . LEU   A 1 47  ? -21.106 2.174   23.707  1.00 26.50 ? 47  LEU   A CG  1 
ATOM   384  C  CD1 . LEU   A 1 47  ? -20.023 2.974   24.419  1.00 25.18 ? 47  LEU   A CD1 1 
ATOM   385  C  CD2 . LEU   A 1 47  ? -20.521 0.914   23.059  1.00 26.65 ? 47  LEU   A CD2 1 
ATOM   386  N  N   . SER   A 1 48  ? -23.769 4.544   23.818  1.00 19.05 ? 48  SER   A N   1 
ATOM   387  C  CA  . SER   A 1 48  ? -24.598 5.163   22.784  1.00 18.85 ? 48  SER   A CA  1 
ATOM   388  C  C   . SER   A 1 48  ? -23.805 5.182   21.483  1.00 19.51 ? 48  SER   A C   1 
ATOM   389  O  O   . SER   A 1 48  ? -22.783 5.881   21.361  1.00 20.10 ? 48  SER   A O   1 
ATOM   390  C  CB  . SER   A 1 48  ? -25.001 6.559   23.223  1.00 22.27 ? 48  SER   A CB  1 
ATOM   391  O  OG  . SER   A 1 48  ? -25.626 7.277   22.164  1.00 24.49 ? 48  SER   A OG  1 
ATOM   392  N  N   . VAL   A 1 49  ? -24.291 4.443   20.506  1.00 19.87 ? 49  VAL   A N   1 
ATOM   393  C  CA  . VAL   A 1 49  ? -23.650 4.334   19.212  1.00 21.81 ? 49  VAL   A CA  1 
ATOM   394  C  C   . VAL   A 1 49  ? -24.652 4.941   18.235  1.00 23.85 ? 49  VAL   A C   1 
ATOM   395  O  O   . VAL   A 1 49  ? -25.760 4.428   18.034  1.00 25.31 ? 49  VAL   A O   1 
ATOM   396  C  CB  . VAL   A 1 49  ? -23.312 2.870   18.850  1.00 23.55 ? 49  VAL   A CB  1 
ATOM   397  C  CG1 . VAL   A 1 49  ? -22.403 2.771   17.634  1.00 30.58 ? 49  VAL   A CG1 1 
ATOM   398  C  CG2 . VAL   A 1 49  ? -22.729 2.064   20.001  1.00 22.56 ? 49  VAL   A CG2 1 
ATOM   399  N  N   . SER   A 1 50  ? -24.336 6.108   17.689  1.00 21.68 ? 50  SER   A N   1 
ATOM   400  C  CA  . SER   A 1 50  ? -25.289 6.773   16.815  1.00 22.71 ? 50  SER   A CA  1 
ATOM   401  C  C   . SER   A 1 50  ? -24.666 6.846   15.436  1.00 22.71 ? 50  SER   A C   1 
ATOM   402  O  O   . SER   A 1 50  ? -24.022 7.841   15.117  1.00 22.38 ? 50  SER   A O   1 
ATOM   403  C  CB  . SER   A 1 50  ? -25.669 8.156   17.287  1.00 25.01 ? 50  SER   A CB  1 
ATOM   404  O  OG  . SER   A 1 50  ? -26.202 8.138   18.596  1.00 35.40 ? 50  SER   A OG  1 
ATOM   405  N  N   . TYR   A 1 51  ? -24.902 5.806   14.632  1.00 22.54 ? 51  TYR   A N   1 
ATOM   406  C  CA  . TYR   A 1 51  ? -24.342 5.682   13.293  1.00 19.01 ? 51  TYR   A CA  1 
ATOM   407  C  C   . TYR   A 1 51  ? -25.349 5.919   12.155  1.00 19.98 ? 51  TYR   A C   1 
ATOM   408  O  O   . TYR   A 1 51  ? -24.966 5.675   11.019  1.00 20.12 ? 51  TYR   A O   1 
ATOM   409  C  CB  . TYR   A 1 51  ? -23.623 4.332   13.127  1.00 19.42 ? 51  TYR   A CB  1 
ATOM   410  C  CG  . TYR   A 1 51  ? -22.319 4.071   13.875  1.00 17.80 ? 51  TYR   A CG  1 
ATOM   411  C  CD1 . TYR   A 1 51  ? -21.597 5.090   14.489  1.00 19.20 ? 51  TYR   A CD1 1 
ATOM   412  C  CD2 . TYR   A 1 51  ? -21.828 2.776   13.991  1.00 17.90 ? 51  TYR   A CD2 1 
ATOM   413  C  CE1 . TYR   A 1 51  ? -20.425 4.809   15.187  1.00 16.44 ? 51  TYR   A CE1 1 
ATOM   414  C  CE2 . TYR   A 1 51  ? -20.657 2.479   14.675  1.00 16.36 ? 51  TYR   A CE2 1 
ATOM   415  C  CZ  . TYR   A 1 51  ? -19.945 3.512   15.266  1.00 17.48 ? 51  TYR   A CZ  1 
ATOM   416  O  OH  . TYR   A 1 51  ? -18.808 3.164   15.945  1.00 18.72 ? 51  TYR   A OH  1 
ATOM   417  N  N   . ASP   A 1 52  ? -26.575 6.419   12.449  1.00 23.69 ? 52  ASP   A N   1 
ATOM   418  C  CA  . ASP   A 1 52  ? -27.590 6.599   11.409  1.00 26.29 ? 52  ASP   A CA  1 
ATOM   419  C  C   . ASP   A 1 52  ? -27.103 7.497   10.264  1.00 26.89 ? 52  ASP   A C   1 
ATOM   420  O  O   . ASP   A 1 52  ? -27.429 7.230   9.107   1.00 27.54 ? 52  ASP   A O   1 
ATOM   421  C  CB  . ASP   A 1 52  ? -28.933 7.097   11.964  1.00 30.01 ? 52  ASP   A CB  1 
ATOM   422  C  CG  . ASP   A 1 52  ? -28.788 8.208   12.997  1.00 43.37 ? 52  ASP   A CG  1 
ATOM   423  O  OD1 . ASP   A 1 52  ? -28.077 7.983   14.038  1.00 46.77 ? 52  ASP   A OD1 1 
ATOM   424  O  OD2 . ASP   A 1 52  ? -29.391 9.292   12.774  1.00 52.46 ? 52  ASP   A OD2 1 
ATOM   425  N  N   . GLN   A 1 53  ? -26.326 8.543   10.559  1.00 25.42 ? 53  GLN   A N   1 
ATOM   426  C  CA  . GLN   A 1 53  ? -25.908 9.455   9.488   1.00 26.69 ? 53  GLN   A CA  1 
ATOM   427  C  C   . GLN   A 1 53  ? -24.439 9.264   9.070   1.00 24.80 ? 53  GLN   A C   1 
ATOM   428  O  O   . GLN   A 1 53  ? -23.864 10.144  8.414   1.00 23.34 ? 53  GLN   A O   1 
ATOM   429  C  CB  . GLN   A 1 53  ? -26.132 10.905  9.917   1.00 32.25 ? 53  GLN   A CB  1 
ATOM   430  C  CG  . GLN   A 1 53  ? -27.544 11.200  10.414  1.00 40.12 ? 53  GLN   A CG  1 
ATOM   431  C  CD  . GLN   A 1 53  ? -28.434 11.588  9.261   1.00 49.07 ? 53  GLN   A CD  1 
ATOM   432  O  OE1 . GLN   A 1 53  ? -28.589 12.769  8.945   1.00 64.11 ? 53  GLN   A OE1 1 
ATOM   433  N  NE2 . GLN   A 1 53  ? -28.990 10.589  8.588   1.00 54.42 ? 53  GLN   A NE2 1 
ATOM   434  N  N   . ALA   A 1 54  ? -23.834 8.100   9.370   1.00 21.84 ? 54  ALA   A N   1 
ATOM   435  C  CA  . ALA   A 1 54  ? -22.447 7.848   8.985   1.00 19.10 ? 54  ALA   A CA  1 
ATOM   436  C  C   . ALA   A 1 54  ? -22.272 7.972   7.467   1.00 22.50 ? 54  ALA   A C   1 
ATOM   437  O  O   . ALA   A 1 54  ? -23.140 7.541   6.684   1.00 27.11 ? 54  ALA   A O   1 
ATOM   438  C  CB  . ALA   A 1 54  ? -21.961 6.493   9.513   1.00 20.02 ? 54  ALA   A CB  1 
ATOM   439  N  N   . THR   A 1 55  ? -21.183 8.635   7.045   1.00 20.51 ? 55  THR   A N   1 
ATOM   440  C  CA  . THR   A 1 55  ? -20.887 8.838   5.635   1.00 21.46 ? 55  THR   A CA  1 
ATOM   441  C  C   . THR   A 1 55  ? -19.526 8.241   5.288   1.00 18.11 ? 55  THR   A C   1 
ATOM   442  O  O   . THR   A 1 55  ? -18.491 8.877   5.499   1.00 18.48 ? 55  THR   A O   1 
ATOM   443  C  CB  . THR   A 1 55  ? -20.830 10.336  5.293   1.00 25.33 ? 55  THR   A CB  1 
ATOM   444  O  OG1 . THR   A 1 55  ? -22.146 10.853  5.439   1.00 34.45 ? 55  THR   A OG1 1 
ATOM   445  C  CG2 . THR   A 1 55  ? -20.411 10.566  3.856   1.00 30.34 ? 55  THR   A CG2 1 
ATOM   446  N  N   . SER   A 1 56  ? -19.498 7.005   4.784   1.00 18.07 ? 56  SER   A N   1 
ATOM   447  C  CA  . SER   A 1 56  ? -18.229 6.429   4.383   1.00 19.35 ? 56  SER   A CA  1 
ATOM   448  C  C   . SER   A 1 56  ? -17.780 7.079   3.088   1.00 21.97 ? 56  SER   A C   1 
ATOM   449  O  O   . SER   A 1 56  ? -18.618 7.532   2.292   1.00 23.88 ? 56  SER   A O   1 
ATOM   450  C  CB  . SER   A 1 56  ? -18.290 4.903   4.255   1.00 20.97 ? 56  SER   A CB  1 
ATOM   451  O  OG  . SER   A 1 56  ? -19.156 4.531   3.161   1.00 21.51 ? 56  SER   A OG  1 
ATOM   452  N  N   . LEU   A 1 57  ? -16.475 7.067   2.850   1.00 19.55 ? 57  LEU   A N   1 
ATOM   453  C  CA  . LEU   A 1 57  ? -15.960 7.728   1.649   1.00 23.19 ? 57  LEU   A CA  1 
ATOM   454  C  C   . LEU   A 1 57  ? -15.095 6.820   0.788   1.00 22.46 ? 57  LEU   A C   1 
ATOM   455  O  O   . LEU   A 1 57  ? -15.147 6.868   -0.442  1.00 22.80 ? 57  LEU   A O   1 
ATOM   456  C  CB  . LEU   A 1 57  ? -15.140 8.948   2.055   1.00 24.09 ? 57  LEU   A CB  1 
ATOM   457  C  CG  . LEU   A 1 57  ? -15.919 10.039  2.797   1.00 31.82 ? 57  LEU   A CG  1 
ATOM   458  C  CD1 . LEU   A 1 57  ? -14.993 11.189  3.191   1.00 33.56 ? 57  LEU   A CD1 1 
ATOM   459  C  CD2 . LEU   A 1 57  ? -17.116 10.523  1.967   1.00 32.41 ? 57  LEU   A CD2 1 
ATOM   460  N  N   . ARG   A 1 58  ? -14.229 6.031   1.420   1.00 19.56 ? 58  ARG   A N   1 
ATOM   461  C  CA  . ARG   A 1 58  ? -13.134 5.406   0.715   1.00 18.54 ? 58  ARG   A CA  1 
ATOM   462  C  C   . ARG   A 1 58  ? -12.625 4.242   1.559   1.00 19.33 ? 58  ARG   A C   1 
ATOM   463  O  O   . ARG   A 1 58  ? -12.753 4.240   2.801   1.00 18.95 ? 58  ARG   A O   1 
ATOM   464  C  CB  . ARG   A 1 58  ? -11.982 6.401   0.600   1.00 20.07 ? 58  ARG   A CB  1 
ATOM   465  C  CG  . ARG   A 1 58  ? -11.005 6.092   -0.523  1.00 22.77 ? 58  ARG   A CG  1 
ATOM   466  C  CD  . ARG   A 1 58  ? -9.949  7.179   -0.694  1.00 23.61 ? 58  ARG   A CD  1 
ATOM   467  N  NE  . ARG   A 1 58  ? -9.145  7.151   0.517   1.00 23.58 ? 58  ARG   A NE  1 
ATOM   468  C  CZ  . ARG   A 1 58  ? -7.828  7.331   0.520   1.00 20.87 ? 58  ARG   A CZ  1 
ATOM   469  N  NH1 . ARG   A 1 58  ? -7.217  7.521   -0.632  1.00 25.56 ? 58  ARG   A NH1 1 
ATOM   470  N  NH2 . ARG   A 1 58  ? -7.146  7.319   1.651   1.00 23.50 ? 58  ARG   A NH2 1 
ATOM   471  N  N   . ILE   A 1 59  ? -12.008 3.300   0.878   1.00 18.42 ? 59  ILE   A N   1 
ATOM   472  C  CA  . ILE   A 1 59  ? -11.363 2.178   1.519   1.00 17.43 ? 59  ILE   A CA  1 
ATOM   473  C  C   . ILE   A 1 59  ? -9.933  2.173   1.036   1.00 16.87 ? 59  ILE   A C   1 
ATOM   474  O  O   . ILE   A 1 59  ? -9.690  2.322   -0.159  1.00 17.42 ? 59  ILE   A O   1 
ATOM   475  C  CB  . ILE   A 1 59  ? -12.131 0.855   1.294   1.00 16.09 ? 59  ILE   A CB  1 
ATOM   476  C  CG1 . ILE   A 1 59  ? -11.566 -0.278  2.176   1.00 18.38 ? 59  ILE   A CG1 1 
ATOM   477  C  CG2 . ILE   A 1 59  ? -12.134 0.465   -0.185  1.00 18.23 ? 59  ILE   A CG2 1 
ATOM   478  C  CD1 . ILE   A 1 59  ? -12.336 -1.584  2.084   1.00 17.80 ? 59  ILE   A CD1 1 
ATOM   479  N  N   . LEU   A 1 60  ? -8.976  1.974   1.946   1.00 15.87 ? 60  LEU   A N   1 
ATOM   480  C  CA  . LEU   A 1 60  ? -7.563  2.078   1.657   1.00 15.44 ? 60  LEU   A CA  1 
ATOM   481  C  C   . LEU   A 1 60  ? -6.795  0.877   2.207   1.00 17.13 ? 60  LEU   A C   1 
ATOM   482  O  O   . LEU   A 1 60  ? -6.936  0.516   3.377   1.00 17.76 ? 60  LEU   A O   1 
ATOM   483  C  CB  . LEU   A 1 60  ? -7.031  3.343   2.369   1.00 17.17 ? 60  LEU   A CB  1 
ATOM   484  C  CG  . LEU   A 1 60  ? -5.504  3.480   2.298   1.00 16.36 ? 60  LEU   A CG  1 
ATOM   485  C  CD1 . LEU   A 1 60  ? -5.038  3.664   0.839   1.00 20.12 ? 60  LEU   A CD1 1 
ATOM   486  C  CD2 . LEU   A 1 60  ? -4.980  4.640   3.185   1.00 18.32 ? 60  LEU   A CD2 1 
ATOM   487  N  N   . ASN   A 1 61  ? -5.918  0.296   1.388   1.00 15.46 ? 61  ASN   A N   1 
ATOM   488  C  CA  . ASN   A 1 61  ? -4.938  -0.662  1.866   1.00 15.64 ? 61  ASN   A CA  1 
ATOM   489  C  C   . ASN   A 1 61  ? -3.757  0.147   2.382   1.00 20.30 ? 61  ASN   A C   1 
ATOM   490  O  O   . ASN   A 1 61  ? -3.016  0.740   1.604   1.00 19.17 ? 61  ASN   A O   1 
ATOM   491  C  CB  . ASN   A 1 61  ? -4.524  -1.683  0.781   1.00 17.38 ? 61  ASN   A CB  1 
ATOM   492  C  CG  . ASN   A 1 61  ? -3.485  -2.688  1.239   1.00 16.24 ? 61  ASN   A CG  1 
ATOM   493  O  OD1 . ASN   A 1 61  ? -2.623  -2.442  2.123   1.00 18.62 ? 61  ASN   A OD1 1 
ATOM   494  N  ND2 . ASN   A 1 61  ? -3.537  -3.877  0.659   1.00 17.19 ? 61  ASN   A ND2 1 
ATOM   495  N  N   . ASN   A 1 62  ? -3.552  0.150   3.706   1.00 18.21 ? 62  ASN   A N   1 
ATOM   496  C  CA  . ASN   A 1 62  ? -2.580  1.068   4.293   1.00 20.25 ? 62  ASN   A CA  1 
ATOM   497  C  C   . ASN   A 1 62  ? -1.227  0.389   4.440   1.00 20.35 ? 62  ASN   A C   1 
ATOM   498  O  O   . ASN   A 1 62  ? -0.327  0.953   5.057   1.00 23.57 ? 62  ASN   A O   1 
ATOM   499  C  CB  . ASN   A 1 62  ? -3.064  1.621   5.660   1.00 21.80 ? 62  ASN   A CB  1 
ATOM   500  C  CG  . ASN   A 1 62  ? -3.216  0.549   6.725   1.00 20.97 ? 62  ASN   A CG  1 
ATOM   501  O  OD1 . ASN   A 1 62  ? -2.430  -0.382  6.800   1.00 18.10 ? 62  ASN   A OD1 1 
ATOM   502  N  ND2 . ASN   A 1 62  ? -4.275  0.619   7.535   1.00 25.02 ? 62  ASN   A ND2 1 
ATOM   503  N  N   . GLY   A 1 63  ? -1.107  -0.863  3.949   1.00 18.23 ? 63  GLY   A N   1 
ATOM   504  C  CA  . GLY   A 1 63  ? 0.096   -1.668  4.032   1.00 17.07 ? 63  GLY   A CA  1 
ATOM   505  C  C   . GLY   A 1 63  ? 0.154   -2.659  5.201   1.00 17.74 ? 63  GLY   A C   1 
ATOM   506  O  O   . GLY   A 1 63  ? 1.068   -3.475  5.299   1.00 19.62 ? 63  GLY   A O   1 
ATOM   507  N  N   . HIS   A 1 64  ? -0.756  -2.456  6.161   1.00 16.90 ? 64  HIS   A N   1 
ATOM   508  C  CA  . HIS   A 1 64  ? -0.806  -3.269  7.390   1.00 18.79 ? 64  HIS   A CA  1 
ATOM   509  C  C   . HIS   A 1 64  ? -2.185  -3.898  7.580   1.00 16.45 ? 64  HIS   A C   1 
ATOM   510  O  O   . HIS   A 1 64  ? -2.287  -5.043  8.027   1.00 17.53 ? 64  HIS   A O   1 
ATOM   511  C  CB  . HIS   A 1 64  ? -0.479  -2.433  8.635   1.00 19.34 ? 64  HIS   A CB  1 
ATOM   512  C  CG  . HIS   A 1 64  ? 0.856   -1.771  8.521   1.00 22.98 ? 64  HIS   A CG  1 
ATOM   513  N  ND1 . HIS   A 1 64  ? 1.013   -0.407  8.318   1.00 26.28 ? 64  HIS   A ND1 1 
ATOM   514  C  CD2 . HIS   A 1 64  ? 2.086   -2.305  8.633   1.00 23.19 ? 64  HIS   A CD2 1 
ATOM   515  C  CE1 . HIS   A 1 64  ? 2.321   -0.144  8.290   1.00 21.65 ? 64  HIS   A CE1 1 
ATOM   516  N  NE2 . HIS   A 1 64  ? 2.978   -1.286  8.475   1.00 22.79 ? 64  HIS   A NE2 1 
ATOM   517  N  N   . ALA   A 1 65  ? -3.225  -3.166  7.177   1.00 16.29 ? 65  ALA   A N   1 
ATOM   518  C  CA  . ALA   A 1 65  ? -4.621  -3.586  7.195   1.00 14.88 ? 65  ALA   A CA  1 
ATOM   519  C  C   . ALA   A 1 65  ? -5.342  -2.763  6.122   1.00 15.28 ? 65  ALA   A C   1 
ATOM   520  O  O   . ALA   A 1 65  ? -4.672  -2.071  5.332   1.00 17.57 ? 65  ALA   A O   1 
ATOM   521  C  CB  . ALA   A 1 65  ? -5.251  -3.458  8.596   1.00 13.73 ? 65  ALA   A CB  1 
ATOM   522  N  N   . PHE   A 1 66  ? -6.665  -2.764  6.129   1.00 13.92 ? 66  PHE   A N   1 
ATOM   523  C  CA  . PHE   A 1 66  ? -7.424  -1.814  5.319   1.00 14.71 ? 66  PHE   A CA  1 
ATOM   524  C  C   . PHE   A 1 66  ? -8.290  -0.906  6.195   1.00 15.56 ? 66  PHE   A C   1 
ATOM   525  O  O   . PHE   A 1 66  ? -8.850  -1.324  7.227   1.00 15.34 ? 66  PHE   A O   1 
ATOM   526  C  CB  . PHE   A 1 66  ? -8.204  -2.502  4.190   1.00 15.32 ? 66  PHE   A CB  1 
ATOM   527  C  CG  . PHE   A 1 66  ? -9.278  -3.427  4.672   1.00 14.80 ? 66  PHE   A CG  1 
ATOM   528  C  CD1 . PHE   A 1 66  ? -10.532 -2.943  5.054   1.00 15.81 ? 66  PHE   A CD1 1 
ATOM   529  C  CD2 . PHE   A 1 66  ? -9.005  -4.794  4.807   1.00 17.18 ? 66  PHE   A CD2 1 
ATOM   530  C  CE1 . PHE   A 1 66  ? -11.503 -3.814  5.538   1.00 15.07 ? 66  PHE   A CE1 1 
ATOM   531  C  CE2 . PHE   A 1 66  ? -9.976  -5.655  5.317   1.00 17.48 ? 66  PHE   A CE2 1 
ATOM   532  C  CZ  . PHE   A 1 66  ? -11.229 -5.175  5.662   1.00 17.02 ? 66  PHE   A CZ  1 
ATOM   533  N  N   . ASN   A 1 67  ? -8.328  0.388   5.839   1.00 16.55 ? 67  ASN   A N   1 
ATOM   534  C  CA  . ASN   A 1 67  ? -9.145  1.359   6.552   1.00 15.96 ? 67  ASN   A CA  1 
ATOM   535  C  C   . ASN   A 1 67  ? -10.378 1.675   5.728   1.00 17.03 ? 67  ASN   A C   1 
ATOM   536  O  O   . ASN   A 1 67  ? -10.220 2.050   4.562   1.00 18.21 ? 67  ASN   A O   1 
ATOM   537  C  CB  . ASN   A 1 67  ? -8.372  2.669   6.777   1.00 17.63 ? 67  ASN   A CB  1 
ATOM   538  C  CG  . ASN   A 1 67  ? -7.128  2.494   7.603   1.00 19.58 ? 67  ASN   A CG  1 
ATOM   539  O  OD1 . ASN   A 1 67  ? -6.976  1.520   8.339   1.00 19.88 ? 67  ASN   A OD1 1 
ATOM   540  N  ND2 . ASN   A 1 67  ? -6.187  3.418   7.474   1.00 22.77 ? 67  ASN   A ND2 1 
ATOM   541  N  N   . VAL   A 1 68  ? -11.559 1.614   6.340   1.00 13.78 ? 68  VAL   A N   1 
ATOM   542  C  CA  . VAL   A 1 68  ? -12.756 2.216   5.767   1.00 15.29 ? 68  VAL   A CA  1 
ATOM   543  C  C   . VAL   A 1 68  ? -12.922 3.607   6.389   1.00 17.14 ? 68  VAL   A C   1 
ATOM   544  O  O   . VAL   A 1 68  ? -13.064 3.698   7.627   1.00 15.49 ? 68  VAL   A O   1 
ATOM   545  C  CB  . VAL   A 1 68  ? -14.006 1.357   5.975   1.00 16.54 ? 68  VAL   A CB  1 
ATOM   546  C  CG1 . VAL   A 1 68  ? -15.272 2.129   5.522   1.00 17.60 ? 68  VAL   A CG1 1 
ATOM   547  C  CG2 . VAL   A 1 68  ? -13.857 0.045   5.218   1.00 18.48 ? 68  VAL   A CG2 1 
ATOM   548  N  N   . GLU   A 1 69  ? -12.852 4.686   5.580   1.00 18.79 ? 69  GLU   A N   1 
ATOM   549  C  CA  . GLU   A 1 69  ? -12.718 6.056   6.067   1.00 18.30 ? 69  GLU   A CA  1 
ATOM   550  C  C   . GLU   A 1 69  ? -14.081 6.730   5.988   1.00 19.02 ? 69  GLU   A C   1 
ATOM   551  O  O   . GLU   A 1 69  ? -14.858 6.478   5.066   1.00 19.64 ? 69  GLU   A O   1 
ATOM   552  C  CB  . GLU   A 1 69  ? -11.831 6.843   5.123   1.00 20.56 ? 69  GLU   A CB  1 
ATOM   553  C  CG  . GLU   A 1 69  ? -10.422 6.302   5.177   1.00 20.13 ? 69  GLU   A CG  1 
ATOM   554  C  CD  . GLU   A 1 69  ? -9.667  6.668   3.929   1.00 21.98 ? 69  GLU   A CD  1 
ATOM   555  O  OE1 . GLU   A 1 69  ? -10.270 7.357   3.060   1.00 23.11 ? 69  GLU   A OE1 1 
ATOM   556  O  OE2 . GLU   A 1 69  ? -8.488  6.269   3.843   1.00 21.30 ? 69  GLU   A OE2 1 
ATOM   557  N  N   . PHE   A 1 70  ? -14.346 7.582   6.981   1.00 17.31 ? 70  PHE   A N   1 
ATOM   558  C  CA  . PHE   A 1 70  ? -15.620 8.295   7.098   1.00 16.90 ? 70  PHE   A CA  1 
ATOM   559  C  C   . PHE   A 1 70  ? -15.382 9.796   7.020   1.00 16.17 ? 70  PHE   A C   1 
ATOM   560  O  O   . PHE   A 1 70  ? -14.326 10.277  7.397   1.00 19.20 ? 70  PHE   A O   1 
ATOM   561  C  CB  . PHE   A 1 70  ? -16.291 7.901   8.413   1.00 16.51 ? 70  PHE   A CB  1 
ATOM   562  C  CG  . PHE   A 1 70  ? -16.866 6.513   8.343   1.00 15.83 ? 70  PHE   A CG  1 
ATOM   563  C  CD1 . PHE   A 1 70  ? -16.046 5.402   8.552   1.00 17.46 ? 70  PHE   A CD1 1 
ATOM   564  C  CD2 . PHE   A 1 70  ? -18.210 6.301   8.029   1.00 15.48 ? 70  PHE   A CD2 1 
ATOM   565  C  CE1 . PHE   A 1 70  ? -16.570 4.115   8.435   1.00 17.67 ? 70  PHE   A CE1 1 
ATOM   566  C  CE2 . PHE   A 1 70  ? -18.741 5.019   7.926   1.00 16.09 ? 70  PHE   A CE2 1 
ATOM   567  C  CZ  . PHE   A 1 70  ? -17.895 3.919   8.103   1.00 17.11 ? 70  PHE   A CZ  1 
ATOM   568  N  N   . ASP   A 1 71  ? -16.403 10.507  6.526   1.00 18.97 ? 71  ASP   A N   1 
ATOM   569  C  CA  . ASP   A 1 71  ? -16.375 11.961  6.582   1.00 20.72 ? 71  ASP   A CA  1 
ATOM   570  C  C   . ASP   A 1 71  ? -16.626 12.372  8.032   1.00 20.49 ? 71  ASP   A C   1 
ATOM   571  O  O   . ASP   A 1 71  ? -17.750 12.205  8.499   1.00 24.68 ? 71  ASP   A O   1 
ATOM   572  C  CB  . ASP   A 1 71  ? -17.434 12.535  5.655   1.00 24.52 ? 71  ASP   A CB  1 
ATOM   573  C  CG  . ASP   A 1 71  ? -17.581 14.049  5.749   1.00 28.21 ? 71  ASP   A CG  1 
ATOM   574  O  OD1 . ASP   A 1 71  ? -16.723 14.688  6.342   1.00 30.20 ? 71  ASP   A OD1 1 
ATOM   575  O  OD2 . ASP   A 1 71  ? -18.578 14.562  5.240   1.00 36.44 ? 71  ASP   A OD2 1 
ATOM   576  N  N   . ASP   A 1 72  ? -15.611 12.918  8.725   1.00 20.15 ? 72  ASP   A N   1 
ATOM   577  C  CA  . ASP   A 1 72  ? -15.751 13.309  10.125  1.00 18.82 ? 72  ASP   A CA  1 
ATOM   578  C  C   . ASP   A 1 72  ? -15.673 14.836  10.285  1.00 22.14 ? 72  ASP   A C   1 
ATOM   579  O  O   . ASP   A 1 72  ? -15.198 15.316  11.311  1.00 24.94 ? 72  ASP   A O   1 
ATOM   580  C  CB  . ASP   A 1 72  ? -14.646 12.702  10.996  1.00 21.04 ? 72  ASP   A CB  1 
ATOM   581  C  CG  . ASP   A 1 72  ? -13.245 13.136  10.582  1.00 23.38 ? 72  ASP   A CG  1 
ATOM   582  O  OD1 . ASP   A 1 72  ? -13.066 13.733  9.463   1.00 26.56 ? 72  ASP   A OD1 1 
ATOM   583  O  OD2 . ASP   A 1 72  ? -12.308 12.877  11.351  1.00 22.84 ? 72  ASP   A OD2 1 
ATOM   584  N  N   . SER   A 1 73  ? -16.148 15.568  9.279   1.00 22.68 ? 73  SER   A N   1 
ATOM   585  C  CA  . SER   A 1 73  ? -16.086 17.037  9.314   1.00 24.26 ? 73  SER   A CA  1 
ATOM   586  C  C   . SER   A 1 73  ? -17.359 17.644  9.912   1.00 29.11 ? 73  SER   A C   1 
ATOM   587  O  O   . SER   A 1 73  ? -17.514 18.863  10.031  1.00 25.95 ? 73  SER   A O   1 
ATOM   588  C  CB  . SER   A 1 73  ? -15.836 17.565  7.938   1.00 25.10 ? 73  SER   A CB  1 
ATOM   589  O  OG  . SER   A 1 73  ? -16.981 17.391  7.127   1.00 27.32 ? 73  SER   A OG  1 
ATOM   590  N  N   . GLN   A 1 74  ? -18.277 16.790  10.350  1.00 29.53 ? 74  GLN   A N   1 
ATOM   591  C  CA  . GLN   A 1 74  ? -19.518 17.242  10.962  1.00 29.75 ? 74  GLN   A CA  1 
ATOM   592  C  C   . GLN   A 1 74  ? -19.894 16.170  11.959  1.00 29.21 ? 74  GLN   A C   1 
ATOM   593  O  O   . GLN   A 1 74  ? -19.409 15.057  11.813  1.00 24.78 ? 74  GLN   A O   1 
ATOM   594  C  CB  . GLN   A 1 74  ? -20.675 17.231  9.960   1.00 33.86 ? 74  GLN   A CB  1 
ATOM   595  C  CG  . GLN   A 1 74  ? -20.751 18.460  9.074   1.00 39.00 ? 74  GLN   A CG  1 
ATOM   596  C  CD  . GLN   A 1 74  ? -21.983 18.386  8.212   1.00 42.75 ? 74  GLN   A CD  1 
ATOM   597  O  OE1 . GLN   A 1 74  ? -21.919 18.031  7.041   1.00 39.89 ? 74  GLN   A OE1 1 
ATOM   598  N  NE2 . GLN   A 1 74  ? -23.126 18.689  8.807   1.00 45.21 ? 74  GLN   A NE2 1 
ATOM   599  N  N   . ASP   A 1 75  ? -20.798 16.501  12.892  1.00 34.44 ? 75  ASP   A N   1 
ATOM   600  C  CA  . ASP   A 1 75  ? -21.209 15.598  13.953  1.00 35.45 ? 75  ASP   A CA  1 
ATOM   601  C  C   . ASP   A 1 75  ? -22.247 14.652  13.365  1.00 34.95 ? 75  ASP   A C   1 
ATOM   602  O  O   . ASP   A 1 75  ? -23.450 14.938  13.359  1.00 37.73 ? 75  ASP   A O   1 
ATOM   603  C  CB  . ASP   A 1 75  ? -21.783 16.362  15.155  1.00 47.79 ? 75  ASP   A CB  1 
ATOM   604  C  CG  . ASP   A 1 75  ? -21.070 16.136  16.484  1.00 53.01 ? 75  ASP   A CG  1 
ATOM   605  O  OD1 . ASP   A 1 75  ? -19.921 15.604  16.479  1.00 47.67 ? 75  ASP   A OD1 1 
ATOM   606  O  OD2 . ASP   A 1 75  ? -21.665 16.507  17.529  1.00 60.09 ? 75  ASP   A OD2 1 
ATOM   607  N  N   . LYS   A 1 76  ? -21.758 13.548  12.828  1.00 30.84 ? 76  LYS   A N   1 
ATOM   608  C  CA  . LYS   A 1 76  ? -22.645 12.573  12.207  1.00 34.65 ? 76  LYS   A CA  1 
ATOM   609  C  C   . LYS   A 1 76  ? -22.657 11.304  13.063  1.00 39.23 ? 76  LYS   A C   1 
ATOM   610  O  O   . LYS   A 1 76  ? -23.512 11.151  13.939  1.00 48.72 ? 76  LYS   A O   1 
ATOM   611  C  CB  . LYS   A 1 76  ? -22.273 12.357  10.739  1.00 34.48 ? 76  LYS   A CB  1 
ATOM   612  C  CG  . LYS   A 1 76  ? -22.807 13.412  9.765   1.00 36.38 ? 76  LYS   A CG  1 
ATOM   613  C  CD  . LYS   A 1 76  ? -22.138 13.292  8.407   1.00 38.20 ? 76  LYS   A CD  1 
ATOM   614  C  CE  . LYS   A 1 76  ? -22.507 14.325  7.359   1.00 41.82 ? 76  LYS   A CE  1 
ATOM   615  N  NZ  . LYS   A 1 76  ? -21.487 14.349  6.282   1.00 41.05 ? 76  LYS   A NZ  1 
ATOM   616  N  N   . ALA   A 1 77  ? -21.664 10.448  12.837  1.00 29.37 ? 77  ALA   A N   1 
ATOM   617  C  CA  . ALA   A 1 77  ? -21.501 9.137   13.457  1.00 23.01 ? 77  ALA   A CA  1 
ATOM   618  C  C   . ALA   A 1 77  ? -20.753 9.300   14.776  1.00 23.84 ? 77  ALA   A C   1 
ATOM   619  O  O   . ALA   A 1 77  ? -19.555 9.580   14.734  1.00 28.64 ? 77  ALA   A O   1 
ATOM   620  C  CB  . ALA   A 1 77  ? -20.631 8.351   12.515  1.00 25.18 ? 77  ALA   A CB  1 
ATOM   621  N  N   . VAL   A 1 78  ? -21.441 9.163   15.905  1.00 19.41 ? 78  VAL   A N   1 
ATOM   622  C  CA  . VAL   A 1 78  ? -20.763 9.431   17.168  1.00 20.83 ? 78  VAL   A CA  1 
ATOM   623  C  C   . VAL   A 1 78  ? -20.989 8.330   18.193  1.00 20.48 ? 78  VAL   A C   1 
ATOM   624  O  O   . VAL   A 1 78  ? -22.013 7.611   18.225  1.00 20.18 ? 78  VAL   A O   1 
ATOM   625  C  CB  . VAL   A 1 78  ? -21.186 10.783  17.772  1.00 27.32 ? 78  VAL   A CB  1 
ATOM   626  C  CG1 . VAL   A 1 78  ? -21.011 11.956  16.827  1.00 26.45 ? 78  VAL   A CG1 1 
ATOM   627  C  CG2 . VAL   A 1 78  ? -22.584 10.717  18.313  1.00 28.72 ? 78  VAL   A CG2 1 
ATOM   628  N  N   . LEU   A 1 79  ? -19.941 8.191   19.025  1.00 16.89 ? 79  LEU   A N   1 
ATOM   629  C  CA  . LEU   A 1 79  ? -19.939 7.333   20.182  1.00 19.02 ? 79  LEU   A CA  1 
ATOM   630  C  C   . LEU   A 1 79  ? -19.902 8.219   21.409  1.00 19.15 ? 79  LEU   A C   1 
ATOM   631  O  O   . LEU   A 1 79  ? -19.109 9.150   21.520  1.00 18.16 ? 79  LEU   A O   1 
ATOM   632  C  CB  . LEU   A 1 79  ? -18.709 6.425   20.102  1.00 19.49 ? 79  LEU   A CB  1 
ATOM   633  C  CG  . LEU   A 1 79  ? -18.570 5.369   21.189  1.00 18.51 ? 79  LEU   A CG  1 
ATOM   634  C  CD1 . LEU   A 1 79  ? -19.630 4.279   21.003  1.00 23.08 ? 79  LEU   A CD1 1 
ATOM   635  C  CD2 . LEU   A 1 79  ? -17.193 4.738   21.109  1.00 18.05 ? 79  LEU   A CD2 1 
ATOM   636  N  N   . LYS   A 1 80  ? -20.808 7.918   22.330  1.00 18.59 ? 80  LYS   A N   1 
ATOM   637  C  CA  . LYS   A 1 80  ? -20.843 8.577   23.629  1.00 20.83 ? 80  LYS   A CA  1 
ATOM   638  C  C   . LYS   A 1 80  ? -21.413 7.643   24.696  1.00 20.98 ? 80  LYS   A C   1 
ATOM   639  O  O   . LYS   A 1 80  ? -21.704 6.482   24.426  1.00 18.67 ? 80  LYS   A O   1 
ATOM   640  C  CB  . LYS   A 1 80  ? -21.606 9.907   23.573  1.00 25.33 ? 80  LYS   A CB  1 
ATOM   641  C  CG  . LYS   A 1 80  ? -23.099 9.778   23.285  1.00 27.25 ? 80  LYS   A CG  1 
ATOM   642  C  CD  . LYS   A 1 80  ? -23.687 11.158  23.002  1.00 30.16 ? 80  LYS   A CD  1 
ATOM   643  N  N   . GLY   A 1 81  ? -21.533 8.173   25.913  1.00 20.24 ? 81  GLY   A N   1 
ATOM   644  C  CA  . GLY   A 1 81  ? -22.023 7.345   26.984  1.00 21.28 ? 81  GLY   A CA  1 
ATOM   645  C  C   . GLY   A 1 81  ? -21.004 6.292   27.368  1.00 24.05 ? 81  GLY   A C   1 
ATOM   646  O  O   . GLY   A 1 81  ? -19.804 6.494   27.187  1.00 19.66 ? 81  GLY   A O   1 
ATOM   647  N  N   . GLY   A 1 82  ? -21.492 5.172   27.915  1.00 24.59 ? 82  GLY   A N   1 
ATOM   648  C  CA  . GLY   A 1 82  ? -20.547 4.165   28.376  1.00 23.91 ? 82  GLY   A CA  1 
ATOM   649  C  C   . GLY   A 1 82  ? -19.631 4.769   29.436  1.00 23.64 ? 82  GLY   A C   1 
ATOM   650  O  O   . GLY   A 1 82  ? -20.086 5.539   30.293  1.00 25.22 ? 82  GLY   A O   1 
ATOM   651  N  N   . PRO   A 1 83  ? -18.288 4.553   29.359  1.00 20.28 ? 83  PRO   A N   1 
ATOM   652  C  CA  . PRO   A 1 83  ? -17.357 5.218   30.255  1.00 19.68 ? 83  PRO   A CA  1 
ATOM   653  C  C   . PRO   A 1 83  ? -16.947 6.633   29.824  1.00 21.60 ? 83  PRO   A C   1 
ATOM   654  O  O   . PRO   A 1 83  ? -16.111 7.261   30.480  1.00 26.05 ? 83  PRO   A O   1 
ATOM   655  C  CB  . PRO   A 1 83  ? -16.105 4.321   30.090  1.00 20.47 ? 83  PRO   A CB  1 
ATOM   656  C  CG  . PRO   A 1 83  ? -16.143 3.929   28.622  1.00 18.47 ? 83  PRO   A CG  1 
ATOM   657  C  CD  . PRO   A 1 83  ? -17.618 3.736   28.318  1.00 19.91 ? 83  PRO   A CD  1 
ATOM   658  N  N   . LEU   A 1 84  ? -17.510 7.154   28.717  1.00 21.65 ? 84  LEU   A N   1 
ATOM   659  C  CA  . LEU   A 1 84  ? -16.913 8.339   28.109  1.00 19.37 ? 84  LEU   A CA  1 
ATOM   660  C  C   . LEU   A 1 84  ? -17.571 9.602   28.659  1.00 20.67 ? 84  LEU   A C   1 
ATOM   661  O  O   . LEU   A 1 84  ? -18.766 9.596   28.953  1.00 22.55 ? 84  LEU   A O   1 
ATOM   662  C  CB  . LEU   A 1 84  ? -17.094 8.292   26.595  1.00 17.49 ? 84  LEU   A CB  1 
ATOM   663  C  CG  . LEU   A 1 84  ? -16.566 7.019   25.905  1.00 15.87 ? 84  LEU   A CG  1 
ATOM   664  C  CD1 . LEU   A 1 84  ? -17.123 6.942   24.492  1.00 16.48 ? 84  LEU   A CD1 1 
ATOM   665  C  CD2 . LEU   A 1 84  ? -15.008 7.018   25.931  1.00 15.41 ? 84  LEU   A CD2 1 
ATOM   666  N  N   . ASP   A 1 85  ? -16.768 10.668  28.693  1.00 22.64 ? 85  ASP   A N   1 
ATOM   667  C  CA  . ASP   A 1 85  ? -17.219 12.043  28.879  1.00 27.10 ? 85  ASP   A CA  1 
ATOM   668  C  C   . ASP   A 1 85  ? -17.216 12.716  27.514  1.00 29.63 ? 85  ASP   A C   1 
ATOM   669  O  O   . ASP   A 1 85  ? -16.223 12.684  26.798  1.00 33.87 ? 85  ASP   A O   1 
ATOM   670  C  CB  . ASP   A 1 85  ? -16.269 12.772  29.831  1.00 31.58 ? 85  ASP   A CB  1 
ATOM   671  C  CG  . ASP   A 1 85  ? -16.387 12.311  31.271  1.00 40.76 ? 85  ASP   A CG  1 
ATOM   672  O  OD1 . ASP   A 1 85  ? -17.458 11.728  31.630  1.00 40.69 ? 85  ASP   A OD1 1 
ATOM   673  O  OD2 . ASP   A 1 85  ? -15.423 12.562  32.048  1.00 45.51 ? 85  ASP   A OD2 1 
ATOM   674  N  N   . GLY   A 1 86  ? -18.327 13.350  27.144  1.00 31.65 ? 86  GLY   A N   1 
ATOM   675  C  CA  . GLY   A 1 86  ? -18.408 14.015  25.858  1.00 27.20 ? 86  GLY   A CA  1 
ATOM   676  C  C   . GLY   A 1 86  ? -18.554 13.042  24.681  1.00 27.42 ? 86  GLY   A C   1 
ATOM   677  O  O   . GLY   A 1 86  ? -18.964 11.887  24.826  1.00 29.23 ? 86  GLY   A O   1 
ATOM   678  N  N   . THR   A 1 87  ? -18.175 13.533  23.508  1.00 20.76 ? 87  THR   A N   1 
ATOM   679  C  CA  . THR   A 1 87  ? -18.660 12.997  22.260  1.00 21.99 ? 87  THR   A CA  1 
ATOM   680  C  C   . THR   A 1 87  ? -17.446 12.680  21.404  1.00 20.26 ? 87  THR   A C   1 
ATOM   681  O  O   . THR   A 1 87  ? -16.545 13.503  21.262  1.00 19.26 ? 87  THR   A O   1 
ATOM   682  C  CB  . THR   A 1 87  ? -19.529 14.032  21.527  1.00 27.83 ? 87  THR   A CB  1 
ATOM   683  O  OG1 . THR   A 1 87  ? -20.708 14.189  22.322  1.00 34.39 ? 87  THR   A OG1 1 
ATOM   684  C  CG2 . THR   A 1 87  ? -19.917 13.593  20.128  1.00 28.80 ? 87  THR   A CG2 1 
ATOM   685  N  N   . TYR   A 1 88  ? -17.460 11.455  20.854  1.00 17.16 ? 88  TYR   A N   1 
ATOM   686  C  CA  . TYR   A 1 88  ? -16.347 11.038  20.016  1.00 15.53 ? 88  TYR   A CA  1 
ATOM   687  C  C   . TYR   A 1 88  ? -16.841 10.711  18.608  1.00 15.85 ? 88  TYR   A C   1 
ATOM   688  O  O   . TYR   A 1 88  ? -17.811 9.953   18.453  1.00 19.02 ? 88  TYR   A O   1 
ATOM   689  C  CB  . TYR   A 1 88  ? -15.722 9.797   20.630  1.00 14.57 ? 88  TYR   A CB  1 
ATOM   690  C  CG  . TYR   A 1 88  ? -14.963 9.994   21.912  1.00 13.37 ? 88  TYR   A CG  1 
ATOM   691  C  CD1 . TYR   A 1 88  ? -15.614 10.314  23.092  1.00 13.99 ? 88  TYR   A CD1 1 
ATOM   692  C  CD2 . TYR   A 1 88  ? -13.574 9.861   21.945  1.00 14.83 ? 88  TYR   A CD2 1 
ATOM   693  C  CE1 . TYR   A 1 88  ? -14.924 10.535  24.287  1.00 14.71 ? 88  TYR   A CE1 1 
ATOM   694  C  CE2 . TYR   A 1 88  ? -12.872 9.985   23.143  1.00 14.32 ? 88  TYR   A CE2 1 
ATOM   695  C  CZ  . TYR   A 1 88  ? -13.544 10.322  24.299  1.00 13.75 ? 88  TYR   A CZ  1 
ATOM   696  O  OH  . TYR   A 1 88  ? -12.847 10.425  25.466  1.00 16.14 ? 88  TYR   A OH  1 
ATOM   697  N  N   . ARG   A 1 89  ? -16.137 11.193  17.593  1.00 14.31 ? 89  ARG   A N   1 
ATOM   698  C  CA  . ARG   A 1 89  ? -16.609 11.109  16.220  1.00 14.37 ? 89  ARG   A CA  1 
ATOM   699  C  C   . ARG   A 1 89  ? -15.892 9.994   15.464  1.00 14.29 ? 89  ARG   A C   1 
ATOM   700  O  O   . ARG   A 1 89  ? -14.662 9.887   15.521  1.00 13.39 ? 89  ARG   A O   1 
ATOM   701  C  CB  . ARG   A 1 89  ? -16.351 12.457  15.557  1.00 18.12 ? 89  ARG   A CB  1 
ATOM   702  C  CG  . ARG   A 1 89  ? -17.001 12.591  14.206  1.00 21.82 ? 89  ARG   A CG  1 
ATOM   703  C  CD  . ARG   A 1 89  ? -16.806 14.049  13.805  1.00 24.12 ? 89  ARG   A CD  1 
ATOM   704  N  NE  . ARG   A 1 89  ? -17.542 15.041  14.584  1.00 23.60 ? 89  ARG   A NE  1 
ATOM   705  C  CZ  . ARG   A 1 89  ? -17.436 16.361  14.411  1.00 24.66 ? 89  ARG   A CZ  1 
ATOM   706  N  NH1 . ARG   A 1 89  ? -16.665 16.880  13.464  1.00 25.60 ? 89  ARG   A NH1 1 
ATOM   707  N  NH2 . ARG   A 1 89  ? -18.151 17.175  15.168  1.00 26.94 ? 89  ARG   A NH2 1 
ATOM   708  N  N   . LEU   A 1 90  ? -16.663 9.152   14.745  1.00 14.38 ? 90  LEU   A N   1 
ATOM   709  C  CA  . LEU   A 1 90  ? -16.054 8.070   13.963  1.00 14.58 ? 90  LEU   A CA  1 
ATOM   710  C  C   . LEU   A 1 90  ? -15.237 8.610   12.790  1.00 14.53 ? 90  LEU   A C   1 
ATOM   711  O  O   . LEU   A 1 90  ? -15.738 9.422   11.992  1.00 16.41 ? 90  LEU   A O   1 
ATOM   712  C  CB  . LEU   A 1 90  ? -17.184 7.212   13.391  1.00 14.97 ? 90  LEU   A CB  1 
ATOM   713  C  CG  . LEU   A 1 90  ? -16.750 6.018   12.537  1.00 15.07 ? 90  LEU   A CG  1 
ATOM   714  C  CD1 . LEU   A 1 90  ? -16.012 4.993   13.372  1.00 16.86 ? 90  LEU   A CD1 1 
ATOM   715  C  CD2 . LEU   A 1 90  ? -17.977 5.357   11.856  1.00 14.73 ? 90  LEU   A CD2 1 
ATOM   716  N  N   . ILE   A 1 91  ? -13.983 8.169   12.715  1.00 13.29 ? 91  ILE   A N   1 
ATOM   717  C  CA  . ILE   A 1 91  ? -13.068 8.529   11.643  1.00 14.65 ? 91  ILE   A CA  1 
ATOM   718  C  C   . ILE   A 1 91  ? -12.805 7.361   10.687  1.00 15.41 ? 91  ILE   A C   1 
ATOM   719  O  O   . ILE   A 1 91  ? -12.746 7.554   9.467   1.00 14.67 ? 91  ILE   A O   1 
ATOM   720  C  CB  . ILE   A 1 91  ? -11.791 9.225   12.172  1.00 14.96 ? 91  ILE   A CB  1 
ATOM   721  C  CG1 . ILE   A 1 91  ? -10.892 9.596   10.996  1.00 16.28 ? 91  ILE   A CG1 1 
ATOM   722  C  CG2 . ILE   A 1 91  ? -11.017 8.389   13.191  1.00 16.61 ? 91  ILE   A CG2 1 
ATOM   723  C  CD1 . ILE   A 1 91  ? -9.727  10.537  11.395  1.00 18.62 ? 91  ILE   A CD1 1 
ATOM   724  N  N   . GLN   A 1 92  ? -12.663 6.126   11.201  1.00 14.12 ? 92  GLN   A N   1 
ATOM   725  C  CA  . GLN   A 1 92  ? -12.350 5.000   10.322  1.00 13.61 ? 92  GLN   A CA  1 
ATOM   726  C  C   . GLN   A 1 92  ? -12.587 3.715   11.107  1.00 13.51 ? 92  GLN   A C   1 
ATOM   727  O  O   . GLN   A 1 92  ? -12.685 3.752   12.333  1.00 13.73 ? 92  GLN   A O   1 
ATOM   728  C  CB  . GLN   A 1 92  ? -10.885 5.013   9.852   1.00 14.28 ? 92  GLN   A CB  1 
ATOM   729  C  CG  . GLN   A 1 92  ? -9.857  5.009   10.993  1.00 15.77 ? 92  GLN   A CG  1 
ATOM   730  C  CD  . GLN   A 1 92  ? -9.154  3.667   11.001  1.00 17.39 ? 92  GLN   A CD  1 
ATOM   731  O  OE1 . GLN   A 1 92  ? -9.720  2.649   11.340  1.00 15.91 ? 92  GLN   A OE1 1 
ATOM   732  N  NE2 . GLN   A 1 92  ? -7.929  3.640   10.538  1.00 19.42 ? 92  GLN   A NE2 1 
ATOM   733  N  N   . PHE   A 1 93  ? -12.753 2.593   10.384  1.00 12.66 ? 93  PHE   A N   1 
ATOM   734  C  CA  . PHE   A 1 93  ? -12.617 1.294   11.024  1.00 13.40 ? 93  PHE   A CA  1 
ATOM   735  C  C   . PHE   A 1 93  ? -11.637 0.465   10.251  1.00 12.61 ? 93  PHE   A C   1 
ATOM   736  O  O   . PHE   A 1 93  ? -11.413 0.675   9.064   1.00 13.49 ? 93  PHE   A O   1 
ATOM   737  C  CB  . PHE   A 1 93  ? -13.946 0.556   11.265  1.00 13.91 ? 93  PHE   A CB  1 
ATOM   738  C  CG  . PHE   A 1 93  ? -14.686 0.084   10.025  1.00 15.04 ? 93  PHE   A CG  1 
ATOM   739  C  CD1 . PHE   A 1 93  ? -14.313 -1.060  9.330   1.00 14.90 ? 93  PHE   A CD1 1 
ATOM   740  C  CD2 . PHE   A 1 93  ? -15.791 0.809   9.566   1.00 15.58 ? 93  PHE   A CD2 1 
ATOM   741  C  CE1 . PHE   A 1 93  ? -15.047 -1.516  8.240   1.00 15.16 ? 93  PHE   A CE1 1 
ATOM   742  C  CE2 . PHE   A 1 93  ? -16.543 0.348   8.487   1.00 16.91 ? 93  PHE   A CE2 1 
ATOM   743  C  CZ  . PHE   A 1 93  ? -16.158 -0.800  7.815   1.00 16.64 ? 93  PHE   A CZ  1 
ATOM   744  N  N   . HIS   A 1 94  ? -11.105 -0.573  10.910  1.00 13.12 ? 94  HIS   A N   1 
ATOM   745  C  CA  . HIS   A 1 94  ? -10.214 -1.550  10.315  1.00 12.31 ? 94  HIS   A CA  1 
ATOM   746  C  C   . HIS   A 1 94  ? -10.326 -2.828  11.142  1.00 12.01 ? 94  HIS   A C   1 
ATOM   747  O  O   . HIS   A 1 94  ? -10.991 -2.834  12.181  1.00 12.83 ? 94  HIS   A O   1 
ATOM   748  C  CB  . HIS   A 1 94  ? -8.751  -1.065  10.262  1.00 13.36 ? 94  HIS   A CB  1 
ATOM   749  C  CG  . HIS   A 1 94  ? -8.257  -0.818  11.660  1.00 13.19 ? 94  HIS   A CG  1 
ATOM   750  N  ND1 . HIS   A 1 94  ? -8.455  0.379   12.300  1.00 12.37 ? 94  HIS   A ND1 1 
ATOM   751  C  CD2 . HIS   A 1 94  ? -7.691  -1.656  12.540  1.00 13.75 ? 94  HIS   A CD2 1 
ATOM   752  C  CE1 . HIS   A 1 94  ? -8.049  0.254   13.584  1.00 10.47 ? 94  HIS   A CE1 1 
ATOM   753  N  NE2 . HIS   A 1 94  ? -7.575  -0.995  13.728  1.00 10.33 ? 94  HIS   A NE2 1 
ATOM   754  N  N   . PHE   A 1 95  ? -9.674  -3.882  10.674  1.00 12.52 ? 95  PHE   A N   1 
ATOM   755  C  CA  . PHE   A 1 95  ? -9.654  -5.174  11.339  1.00 11.91 ? 95  PHE   A CA  1 
ATOM   756  C  C   . PHE   A 1 95  ? -8.209  -5.614  11.526  1.00 12.40 ? 95  PHE   A C   1 
ATOM   757  O  O   . PHE   A 1 95  ? -7.267  -5.168  10.864  1.00 12.58 ? 95  PHE   A O   1 
ATOM   758  C  CB  . PHE   A 1 95  ? -10.343 -6.252  10.477  1.00 11.96 ? 95  PHE   A CB  1 
ATOM   759  C  CG  . PHE   A 1 95  ? -11.790 -5.974  10.120  1.00 12.64 ? 95  PHE   A CG  1 
ATOM   760  C  CD1 . PHE   A 1 95  ? -12.133 -5.107  9.086   1.00 14.32 ? 95  PHE   A CD1 1 
ATOM   761  C  CD2 . PHE   A 1 95  ? -12.808 -6.645  10.781  1.00 13.28 ? 95  PHE   A CD2 1 
ATOM   762  C  CE1 . PHE   A 1 95  ? -13.465 -4.911  8.747   1.00 13.78 ? 95  PHE   A CE1 1 
ATOM   763  C  CE2 . PHE   A 1 95  ? -14.155 -6.423  10.490  1.00 14.00 ? 95  PHE   A CE2 1 
ATOM   764  C  CZ  . PHE   A 1 95  ? -14.460 -5.576  9.432   1.00 14.08 ? 95  PHE   A CZ  1 
ATOM   765  N  N   . HIS   A 1 96  ? -8.074  -6.581  12.436  1.00 12.89 ? 96  HIS   A N   1 
ATOM   766  C  CA  . HIS   A 1 96  ? -6.870  -7.384  12.578  1.00 12.48 ? 96  HIS   A CA  1 
ATOM   767  C  C   . HIS   A 1 96  ? -7.286  -8.849  12.455  1.00 13.82 ? 96  HIS   A C   1 
ATOM   768  O  O   . HIS   A 1 96  ? -8.354  -9.208  12.967  1.00 13.96 ? 96  HIS   A O   1 
ATOM   769  C  CB  . HIS   A 1 96  ? -6.219  -7.159  13.970  1.00 12.42 ? 96  HIS   A CB  1 
ATOM   770  C  CG  . HIS   A 1 96  ? -5.954  -5.722  14.246  1.00 12.45 ? 96  HIS   A CG  1 
ATOM   771  N  ND1 . HIS   A 1 96  ? -4.671  -5.197  14.129  1.00 11.74 ? 96  HIS   A ND1 1 
ATOM   772  C  CD2 . HIS   A 1 96  ? -6.765  -4.739  14.698  1.00 12.97 ? 96  HIS   A CD2 1 
ATOM   773  C  CE1 . HIS   A 1 96  ? -4.699  -3.892  14.474  1.00 12.06 ? 96  HIS   A CE1 1 
ATOM   774  N  NE2 . HIS   A 1 96  ? -5.970  -3.612  14.806  1.00 12.44 ? 96  HIS   A NE2 1 
ATOM   775  N  N   . TRP   A 1 97  ? -6.479  -9.693  11.823  1.00 11.94 ? 97  TRP   A N   1 
ATOM   776  C  CA  . TRP   A 1 97  ? -6.911  -11.075 11.617  1.00 11.81 ? 97  TRP   A CA  1 
ATOM   777  C  C   . TRP   A 1 97  ? -5.692  -11.972 11.495  1.00 12.71 ? 97  TRP   A C   1 
ATOM   778  O  O   . TRP   A 1 97  ? -4.523  -11.538 11.420  1.00 14.42 ? 97  TRP   A O   1 
ATOM   779  C  CB  . TRP   A 1 97  ? -7.811  -11.193 10.375  1.00 12.36 ? 97  TRP   A CB  1 
ATOM   780  C  CG  . TRP   A 1 97  ? -7.188  -10.770 9.067   1.00 12.99 ? 97  TRP   A CG  1 
ATOM   781  C  CD1 . TRP   A 1 97  ? -6.462  -11.581 8.252   1.00 15.07 ? 97  TRP   A CD1 1 
ATOM   782  C  CD2 . TRP   A 1 97  ? -7.118  -9.448  8.498   1.00 14.95 ? 97  TRP   A CD2 1 
ATOM   783  N  NE1 . TRP   A 1 97  ? -6.018  -10.886 7.140   1.00 15.43 ? 97  TRP   A NE1 1 
ATOM   784  C  CE2 . TRP   A 1 97  ? -6.390  -9.559  7.281   1.00 14.15 ? 97  TRP   A CE2 1 
ATOM   785  C  CE3 . TRP   A 1 97  ? -7.642  -8.197  8.871   1.00 14.65 ? 97  TRP   A CE3 1 
ATOM   786  C  CZ2 . TRP   A 1 97  ? -6.195  -8.467  6.437   1.00 15.65 ? 97  TRP   A CZ2 1 
ATOM   787  C  CZ3 . TRP   A 1 97  ? -7.421  -7.109  8.038   1.00 14.94 ? 97  TRP   A CZ3 1 
ATOM   788  C  CH2 . TRP   A 1 97  ? -6.705  -7.253  6.840   1.00 14.07 ? 97  TRP   A CH2 1 
ATOM   789  N  N   . GLY   A 1 98  ? -5.996  -13.275 11.479  1.00 12.98 ? 98  GLY   A N   1 
ATOM   790  C  CA  . GLY   A 1 98  ? -4.966  -14.298 11.556  1.00 13.95 ? 98  GLY   A CA  1 
ATOM   791  C  C   . GLY   A 1 98  ? -4.741  -15.034 10.234  1.00 14.38 ? 98  GLY   A C   1 
ATOM   792  O  O   . GLY   A 1 98  ? -5.467  -14.809 9.243   1.00 15.21 ? 98  GLY   A O   1 
ATOM   793  N  N   . SER   A 1 99  ? -3.713  -15.896 10.253  1.00 16.61 ? 99  SER   A N   1 
ATOM   794  C  CA  . SER   A 1 99  ? -3.469  -16.809 9.145   1.00 17.37 ? 99  SER   A CA  1 
ATOM   795  C  C   . SER   A 1 99  ? -4.361  -18.046 9.260   1.00 19.11 ? 99  SER   A C   1 
ATOM   796  O  O   . SER   A 1 99  ? -4.475  -18.771 8.267   1.00 20.18 ? 99  SER   A O   1 
ATOM   797  C  CB  . SER   A 1 99  ? -2.020  -17.215 9.092   1.00 19.25 ? 99  SER   A CB  1 
ATOM   798  O  OG  . SER   A 1 99  ? -1.557  -17.702 10.350  1.00 19.68 ? 99  SER   A OG  1 
ATOM   799  N  N   . LEU   A 1 100 ? -4.941  -18.280 10.448  1.00 17.25 ? 100 LEU   A N   1 
ATOM   800  C  CA  . LEU   A 1 100 ? -5.792  -19.422 10.761  1.00 20.45 ? 100 LEU   A CA  1 
ATOM   801  C  C   . LEU   A 1 100 ? -6.927  -18.914 11.641  1.00 18.21 ? 100 LEU   A C   1 
ATOM   802  O  O   . LEU   A 1 100 ? -6.765  -17.916 12.357  1.00 16.58 ? 100 LEU   A O   1 
ATOM   803  C  CB  . LEU   A 1 100 ? -4.940  -20.404 11.569  1.00 23.15 ? 100 LEU   A CB  1 
ATOM   804  C  CG  . LEU   A 1 100 ? -3.605  -20.781 10.940  1.00 25.83 ? 100 LEU   A CG  1 
ATOM   805  C  CD1 . LEU   A 1 100 ? -2.566  -21.080 12.010  1.00 30.03 ? 100 LEU   A CD1 1 
ATOM   806  C  CD2 . LEU   A 1 100 ? -3.805  -21.988 10.030  1.00 30.42 ? 100 LEU   A CD2 1 
ATOM   807  N  N   . ASP   A 1 101 ? -8.003  -19.695 11.734  1.00 18.38 ? 101 ASP   A N   1 
ATOM   808  C  CA  . ASP   A 1 101 ? -9.148  -19.190 12.485  1.00 17.78 ? 101 ASP   A CA  1 
ATOM   809  C  C   . ASP   A 1 101 ? -8.840  -19.137 13.996  1.00 17.63 ? 101 ASP   A C   1 
ATOM   810  O  O   . ASP   A 1 101 ? -9.524  -18.459 14.753  1.00 20.76 ? 101 ASP   A O   1 
ATOM   811  C  CB  . ASP   A 1 101 ? -10.401 -20.015 12.199  1.00 19.69 ? 101 ASP   A CB  1 
ATOM   812  C  CG  . ASP   A 1 101 ? -10.848 -20.107 10.746  1.00 23.29 ? 101 ASP   A CG  1 
ATOM   813  O  OD1 . ASP   A 1 101 ? -10.482 -19.231 9.903   1.00 22.33 ? 101 ASP   A OD1 1 
ATOM   814  O  OD2 . ASP   A 1 101 ? -11.629 -21.044 10.462  1.00 27.74 ? 101 ASP   A OD2 1 
ATOM   815  N  N   . GLY   A 1 102 ? -7.820  -19.880 14.459  1.00 17.06 ? 102 GLY   A N   1 
ATOM   816  C  CA  . GLY   A 1 102 ? -7.532  -19.888 15.891  1.00 16.20 ? 102 GLY   A CA  1 
ATOM   817  C  C   . GLY   A 1 102 ? -6.728  -18.716 16.449  1.00 15.34 ? 102 GLY   A C   1 
ATOM   818  O  O   . GLY   A 1 102 ? -6.424  -18.689 17.638  1.00 15.69 ? 102 GLY   A O   1 
ATOM   819  N  N   A GLN   A 1 103 ? -6.481  -17.700 15.617  0.50 14.50 ? 103 GLN   A N   1 
ATOM   820  N  N   B GLN   A 1 103 ? -6.456  -17.722 15.601  0.50 14.77 ? 103 GLN   A N   1 
ATOM   821  C  CA  A GLN   A 1 103 ? -5.734  -16.540 16.062  0.50 13.66 ? 103 GLN   A CA  1 
ATOM   822  C  CA  B GLN   A 1 103 ? -5.766  -16.531 16.053  0.50 13.98 ? 103 GLN   A CA  1 
ATOM   823  C  C   A GLN   A 1 103 ? -6.067  -15.366 15.151  0.50 13.64 ? 103 GLN   A C   1 
ATOM   824  C  C   B GLN   A 1 103 ? -6.207  -15.353 15.192  0.50 13.87 ? 103 GLN   A C   1 
ATOM   825  O  O   A GLN   A 1 103 ? -6.527  -15.576 14.030  0.50 14.79 ? 103 GLN   A O   1 
ATOM   826  O  O   B GLN   A 1 103 ? -6.895  -15.549 14.176  0.50 14.44 ? 103 GLN   A O   1 
ATOM   827  C  CB  A GLN   A 1 103 ? -4.242  -16.868 16.018  0.50 15.06 ? 103 GLN   A CB  1 
ATOM   828  C  CB  B GLN   A 1 103 ? -4.253  -16.775 16.031  0.50 16.01 ? 103 GLN   A CB  1 
ATOM   829  C  CG  A GLN   A 1 103 ? -3.682  -16.939 14.604  0.50 15.41 ? 103 GLN   A CG  1 
ATOM   830  C  CG  B GLN   A 1 103 ? -3.688  -17.001 14.635  0.50 16.61 ? 103 GLN   A CG  1 
ATOM   831  C  CD  A GLN   A 1 103 ? -2.352  -17.648 14.657  0.50 16.25 ? 103 GLN   A CD  1 
ATOM   832  C  CD  B GLN   A 1 103 ? -2.214  -17.322 14.719  0.50 17.90 ? 103 GLN   A CD  1 
ATOM   833  O  OE1 A GLN   A 1 103 ? -2.275  -18.799 15.098  0.50 17.93 ? 103 GLN   A OE1 1 
ATOM   834  O  OE1 B GLN   A 1 103 ? -1.728  -17.795 15.755  0.50 20.34 ? 103 GLN   A OE1 1 
ATOM   835  N  NE2 A GLN   A 1 103 ? -1.271  -16.947 14.306  0.50 15.06 ? 103 GLN   A NE2 1 
ATOM   836  N  NE2 B GLN   A 1 103 ? -1.487  -17.096 13.627  0.50 16.38 ? 103 GLN   A NE2 1 
ATOM   837  N  N   . GLY   A 1 104 ? -5.850  -14.143 15.655  1.00 13.77 ? 104 GLY   A N   1 
ATOM   838  C  CA  . GLY   A 1 104 ? -6.093  -12.943 14.869  1.00 13.98 ? 104 GLY   A CA  1 
ATOM   839  C  C   . GLY   A 1 104 ? -6.574  -11.767 15.683  1.00 15.57 ? 104 GLY   A C   1 
ATOM   840  O  O   . GLY   A 1 104 ? -6.368  -10.607 15.284  1.00 15.03 ? 104 GLY   A O   1 
ATOM   841  N  N   . SER   A 1 105 ? -7.257  -12.050 16.809  1.00 13.50 ? 105 SER   A N   1 
ATOM   842  C  CA  . SER   A 1 105 ? -7.686  -10.908 17.631  1.00 13.73 ? 105 SER   A CA  1 
ATOM   843  C  C   . SER   A 1 105 ? -6.470  -10.328 18.392  1.00 12.92 ? 105 SER   A C   1 
ATOM   844  O  O   . SER   A 1 105 ? -5.453  -10.997 18.564  1.00 13.76 ? 105 SER   A O   1 
ATOM   845  C  CB  . SER   A 1 105 ? -8.806  -11.258 18.553  1.00 13.58 ? 105 SER   A CB  1 
ATOM   846  O  OG  . SER   A 1 105 ? -8.403  -12.156 19.554  1.00 13.47 ? 105 SER   A OG  1 
ATOM   847  N  N   . GLU   A 1 106 ? -6.600  -9.068  18.770  1.00 13.24 ? 106 GLU   A N   1 
ATOM   848  C  CA  . GLU   A 1 106 ? -5.589  -8.398  19.602  1.00 13.07 ? 106 GLU   A CA  1 
ATOM   849  C  C   . GLU   A 1 106 ? -5.938  -8.591  21.090  1.00 14.17 ? 106 GLU   A C   1 
ATOM   850  O  O   . GLU   A 1 106 ? -5.120  -9.139  21.848  1.00 13.92 ? 106 GLU   A O   1 
ATOM   851  C  CB  . GLU   A 1 106 ? -5.507  -6.927  19.164  1.00 12.80 ? 106 GLU   A CB  1 
ATOM   852  C  CG  . GLU   A 1 106 ? -5.044  -6.791  17.711  1.00 13.87 ? 106 GLU   A CG  1 
ATOM   853  C  CD  . GLU   A 1 106 ? -4.338  -5.475  17.491  1.00 14.62 ? 106 GLU   A CD  1 
ATOM   854  O  OE1 . GLU   A 1 106 ? -4.957  -4.401  17.759  1.00 15.44 ? 106 GLU   A OE1 1 
ATOM   855  O  OE2 . GLU   A 1 106 ? -3.189  -5.516  16.959  1.00 16.41 ? 106 GLU   A OE2 1 
ATOM   856  N  N   . HIS   A 1 107 ? -7.151  -8.180  21.491  1.00 13.02 ? 107 HIS   A N   1 
ATOM   857  C  CA  . HIS   A 1 107 ? -7.569  -8.493  22.855  1.00 11.90 ? 107 HIS   A CA  1 
ATOM   858  C  C   . HIS   A 1 107 ? -7.840  -9.990  22.880  1.00 13.26 ? 107 HIS   A C   1 
ATOM   859  O  O   . HIS   A 1 107 ? -8.195  -10.573 21.857  1.00 13.71 ? 107 HIS   A O   1 
ATOM   860  C  CB  . HIS   A 1 107 ? -8.832  -7.688  23.214  1.00 12.12 ? 107 HIS   A CB  1 
ATOM   861  C  CG  . HIS   A 1 107 ? -8.472  -6.245  23.351  1.00 11.28 ? 107 HIS   A CG  1 
ATOM   862  N  ND1 . HIS   A 1 107 ? -8.573  -5.344  22.325  1.00 12.65 ? 107 HIS   A ND1 1 
ATOM   863  C  CD2 . HIS   A 1 107 ? -8.021  -5.538  24.426  1.00 13.33 ? 107 HIS   A CD2 1 
ATOM   864  C  CE1 . HIS   A 1 107 ? -8.130  -4.143  22.732  1.00 13.12 ? 107 HIS   A CE1 1 
ATOM   865  N  NE2 . HIS   A 1 107 ? -7.800  -4.232  24.052  1.00 11.38 ? 107 HIS   A NE2 1 
ATOM   866  N  N   . THR   A 1 108 ? -7.691  -10.556 24.073  1.00 13.70 ? 108 THR   A N   1 
ATOM   867  C  CA  . THR   A 1 108 ? -8.039  -11.952 24.311  1.00 12.72 ? 108 THR   A CA  1 
ATOM   868  C  C   . THR   A 1 108 ? -8.983  -12.002 25.520  1.00 12.49 ? 108 THR   A C   1 
ATOM   869  O  O   . THR   A 1 108 ? -9.035  -11.043 26.291  1.00 14.17 ? 108 THR   A O   1 
ATOM   870  C  CB  . THR   A 1 108 ? -6.824  -12.865 24.494  1.00 13.69 ? 108 THR   A CB  1 
ATOM   871  O  OG1 . THR   A 1 108 ? -5.984  -12.391 25.549  1.00 15.02 ? 108 THR   A OG1 1 
ATOM   872  C  CG2 . THR   A 1 108 ? -6.040  -12.989 23.205  1.00 14.14 ? 108 THR   A CG2 1 
ATOM   873  N  N   . VAL   A 1 109 ? -9.797  -13.056 25.634  1.00 13.75 ? 109 VAL   A N   1 
ATOM   874  C  CA  . VAL   A 1 109 ? -10.759 -13.145 26.743  1.00 13.66 ? 109 VAL   A CA  1 
ATOM   875  C  C   . VAL   A 1 109 ? -10.434 -14.448 27.499  1.00 15.52 ? 109 VAL   A C   1 
ATOM   876  O  O   . VAL   A 1 109 ? -10.592 -15.523 26.932  1.00 14.86 ? 109 VAL   A O   1 
ATOM   877  C  CB  . VAL   A 1 109 ? -12.204 -13.146 26.197  1.00 16.60 ? 109 VAL   A CB  1 
ATOM   878  C  CG1 . VAL   A 1 109 ? -13.209 -13.217 27.340  1.00 17.63 ? 109 VAL   A CG1 1 
ATOM   879  C  CG2 . VAL   A 1 109 ? -12.526 -11.891 25.364  1.00 17.44 ? 109 VAL   A CG2 1 
ATOM   880  N  N   . ASP   A 1 110 ? -9.938  -14.334 28.737  1.00 15.23 ? 110 ASP   A N   1 
ATOM   881  C  CA  . ASP   A 1 110 ? -9.438  -15.518 29.450  1.00 15.89 ? 110 ASP   A CA  1 
ATOM   882  C  C   . ASP   A 1 110 ? -8.483  -16.323 28.569  1.00 17.83 ? 110 ASP   A C   1 
ATOM   883  O  O   . ASP   A 1 110 ? -8.588  -17.548 28.496  1.00 17.35 ? 110 ASP   A O   1 
ATOM   884  C  CB  . ASP   A 1 110 ? -10.613 -16.329 30.012  1.00 18.67 ? 110 ASP   A CB  1 
ATOM   885  C  CG  . ASP   A 1 110 ? -11.425 -15.540 31.027  1.00 18.25 ? 110 ASP   A CG  1 
ATOM   886  O  OD1 . ASP   A 1 110 ? -10.852 -14.693 31.756  1.00 21.40 ? 110 ASP   A OD1 1 
ATOM   887  O  OD2 . ASP   A 1 110 ? -12.627 -15.826 31.094  1.00 23.01 ? 110 ASP   A OD2 1 
ATOM   888  N  N   . LYS   A 1 111 ? -7.603  -15.613 27.852  1.00 15.61 ? 111 LYS   A N   1 
ATOM   889  C  CA  . LYS   A 1 111 ? -6.574  -16.140 26.942  1.00 16.55 ? 111 LYS   A CA  1 
ATOM   890  C  C   . LYS   A 1 111 ? -7.119  -16.671 25.606  1.00 15.85 ? 111 LYS   A C   1 
ATOM   891  O  O   . LYS   A 1 111 ? -6.326  -17.052 24.738  1.00 17.50 ? 111 LYS   A O   1 
ATOM   892  C  CB  . LYS   A 1 111 ? -5.606  -17.128 27.619  1.00 18.65 ? 111 LYS   A CB  1 
ATOM   893  C  CG  . LYS   A 1 111 ? -4.887  -16.600 28.864  1.00 21.92 ? 111 LYS   A CG  1 
ATOM   894  C  CD  . LYS   A 1 111 ? -3.961  -15.438 28.587  1.00 26.02 ? 111 LYS   A CD  1 
ATOM   895  C  CE  . LYS   A 1 111 ? -3.319  -14.892 29.860  1.00 27.25 ? 111 LYS   A CE  1 
ATOM   896  N  NZ  . LYS   A 1 111 ? -2.134  -15.690 30.223  1.00 34.62 ? 111 LYS   A NZ  1 
ATOM   897  N  N   . LYS   A 1 112 ? -8.451  -16.616 25.386  1.00 14.13 ? 112 LYS   A N   1 
ATOM   898  C  CA  . LYS   A 1 112 ? -9.033  -17.042 24.134  1.00 15.69 ? 112 LYS   A CA  1 
ATOM   899  C  C   . LYS   A 1 112 ? -8.751  -15.973 23.071  1.00 14.90 ? 112 LYS   A C   1 
ATOM   900  O  O   . LYS   A 1 112 ? -9.028  -14.778 23.299  1.00 15.61 ? 112 LYS   A O   1 
ATOM   901  C  CB  . LYS   A 1 112 ? -10.555 -17.180 24.279  1.00 17.88 ? 112 LYS   A CB  1 
ATOM   902  C  CG  . LYS   A 1 112 ? -11.230 -17.524 22.945  1.00 17.02 ? 112 LYS   A CG  1 
ATOM   903  C  CD  . LYS   A 1 112 ? -12.765 -17.531 23.097  1.00 21.12 ? 112 LYS   A CD  1 
ATOM   904  C  CE  . LYS   A 1 112 ? -13.482 -17.643 21.762  1.00 24.30 ? 112 LYS   A CE  1 
ATOM   905  N  NZ  . LYS   A 1 112 ? -13.252 -18.979 21.196  1.00 25.34 ? 112 LYS   A NZ  1 
ATOM   906  N  N   A LYS   A 1 113 ? -8.207  -16.422 21.931  0.50 15.69 ? 113 LYS   A N   1 
ATOM   907  N  N   B LYS   A 1 113 ? -8.190  -16.436 21.949  0.50 15.46 ? 113 LYS   A N   1 
ATOM   908  C  CA  A LYS   A 1 113 ? -8.034  -15.614 20.726  0.50 14.88 ? 113 LYS   A CA  1 
ATOM   909  C  CA  B LYS   A 1 113 ? -8.063  -15.681 20.709  0.50 14.54 ? 113 LYS   A CA  1 
ATOM   910  C  C   A LYS   A 1 113 ? -9.128  -15.881 19.693  0.50 14.22 ? 113 LYS   A C   1 
ATOM   911  C  C   B LYS   A 1 113 ? -9.268  -15.903 19.800  0.50 13.90 ? 113 LYS   A C   1 
ATOM   912  O  O   A LYS   A 1 113 ? -9.331  -17.017 19.273  0.50 14.59 ? 113 LYS   A O   1 
ATOM   913  O  O   B LYS   A 1 113 ? -9.729  -17.029 19.633  0.50 13.46 ? 113 LYS   A O   1 
ATOM   914  C  CB  A LYS   A 1 113 ? -6.679  -15.919 20.080  0.50 15.14 ? 113 LYS   A CB  1 
ATOM   915  C  CB  B LYS   A 1 113 ? -6.787  -16.119 19.987  0.50 14.83 ? 113 LYS   A CB  1 
ATOM   916  C  CG  A LYS   A 1 113 ? -5.460  -15.448 20.862  0.50 14.76 ? 113 LYS   A CG  1 
ATOM   917  C  CG  B LYS   A 1 113 ? -5.509  -15.916 20.787  0.50 15.56 ? 113 LYS   A CG  1 
ATOM   918  C  CD  A LYS   A 1 113 ? -4.180  -16.012 20.273  0.50 16.98 ? 113 LYS   A CD  1 
ATOM   919  C  CD  B LYS   A 1 113 ? -4.304  -16.435 20.037  0.50 16.32 ? 113 LYS   A CD  1 
ATOM   920  C  CE  A LYS   A 1 113 ? -2.929  -15.576 21.008  0.50 18.29 ? 113 LYS   A CE  1 
ATOM   921  C  CE  B LYS   A 1 113 ? -2.994  -15.869 20.550  0.50 18.59 ? 113 LYS   A CE  1 
ATOM   922  N  NZ  A LYS   A 1 113 ? -1.762  -16.389 20.588  0.50 20.44 ? 113 LYS   A NZ  1 
ATOM   923  N  NZ  B LYS   A 1 113 ? -2.562  -16.496 21.823  0.50 19.02 ? 113 LYS   A NZ  1 
ATOM   924  N  N   . TYR   A 1 114 ? -9.779  -14.806 19.238  1.00 14.00 ? 114 TYR   A N   1 
ATOM   925  C  CA  . TYR   A 1 114 ? -10.765 -14.887 18.167  1.00 12.69 ? 114 TYR   A CA  1 
ATOM   926  C  C   . TYR   A 1 114 ? -10.110 -14.827 16.796  1.00 13.29 ? 114 TYR   A C   1 
ATOM   927  O  O   . TYR   A 1 114 ? -8.935  -14.507 16.697  1.00 14.88 ? 114 TYR   A O   1 
ATOM   928  C  CB  . TYR   A 1 114 ? -11.843 -13.819 18.348  1.00 13.53 ? 114 TYR   A CB  1 
ATOM   929  C  CG  . TYR   A 1 114 ? -12.767 -14.013 19.525  1.00 13.58 ? 114 TYR   A CG  1 
ATOM   930  C  CD1 . TYR   A 1 114 ? -12.442 -13.583 20.790  1.00 15.65 ? 114 TYR   A CD1 1 
ATOM   931  C  CD2 . TYR   A 1 114 ? -13.993 -14.629 19.317  1.00 16.27 ? 114 TYR   A CD2 1 
ATOM   932  C  CE1 . TYR   A 1 114 ? -13.319 -13.793 21.845  1.00 16.94 ? 114 TYR   A CE1 1 
ATOM   933  C  CE2 . TYR   A 1 114 ? -14.894 -14.798 20.359  1.00 15.37 ? 114 TYR   A CE2 1 
ATOM   934  C  CZ  . TYR   A 1 114 ? -14.538 -14.402 21.626  1.00 17.22 ? 114 TYR   A CZ  1 
ATOM   935  O  OH  . TYR   A 1 114 ? -15.385 -14.529 22.724  1.00 21.18 ? 114 TYR   A OH  1 
ATOM   936  N  N   . ALA   A 1 115 ? -10.889 -15.138 15.742  1.00 13.49 ? 115 ALA   A N   1 
ATOM   937  C  CA  . ALA   A 1 115 ? -10.350 -15.163 14.382  1.00 13.35 ? 115 ALA   A CA  1 
ATOM   938  C  C   . ALA   A 1 115 ? -9.916  -13.775 13.906  1.00 12.85 ? 115 ALA   A C   1 
ATOM   939  O  O   . ALA   A 1 115 ? -9.089  -13.626 12.996  1.00 13.38 ? 115 ALA   A O   1 
ATOM   940  C  CB  . ALA   A 1 115 ? -11.400 -15.742 13.439  1.00 14.46 ? 115 ALA   A CB  1 
ATOM   941  N  N   . ALA   A 1 116 ? -10.593 -12.755 14.433  1.00 13.49 ? 116 ALA   A N   1 
ATOM   942  C  CA  . ALA   A 1 116 ? -10.275 -11.398 14.029  1.00 13.38 ? 116 ALA   A CA  1 
ATOM   943  C  C   . ALA   A 1 116 ? -10.925 -10.430 15.012  1.00 12.67 ? 116 ALA   A C   1 
ATOM   944  O  O   . ALA   A 1 116 ? -11.668 -10.817 15.934  1.00 12.48 ? 116 ALA   A O   1 
ATOM   945  C  CB  . ALA   A 1 116 ? -10.791 -11.134 12.608  1.00 13.69 ? 116 ALA   A CB  1 
ATOM   946  N  N   . GLU   A 1 117 ? -10.597 -9.141  14.850  1.00 12.71 ? 117 GLU   A N   1 
ATOM   947  C  CA  . GLU   A 1 117 ? -11.125 -8.089  15.702  1.00 12.69 ? 117 GLU   A CA  1 
ATOM   948  C  C   . GLU   A 1 117 ? -11.299 -6.830  14.869  1.00 13.96 ? 117 GLU   A C   1 
ATOM   949  O  O   . GLU   A 1 117 ? -10.391 -6.420  14.155  1.00 14.51 ? 117 GLU   A O   1 
ATOM   950  C  CB  . GLU   A 1 117 ? -10.173 -7.807  16.872  1.00 13.30 ? 117 GLU   A CB  1 
ATOM   951  C  CG  . GLU   A 1 117 ? -10.724 -6.940  18.010  1.00 13.29 ? 117 GLU   A CG  1 
ATOM   952  C  CD  . GLU   A 1 117 ? -9.754  -6.837  19.197  1.00 15.33 ? 117 GLU   A CD  1 
ATOM   953  O  OE1 . GLU   A 1 117 ? -9.077  -7.829  19.501  1.00 14.61 ? 117 GLU   A OE1 1 
ATOM   954  O  OE2 . GLU   A 1 117 ? -9.740  -5.756  19.836  1.00 15.88 ? 117 GLU   A OE2 1 
ATOM   955  N  N   . LEU   A 1 118 ? -12.485 -6.256  14.949  1.00 11.74 ? 118 LEU   A N   1 
ATOM   956  C  CA  . LEU   A 1 118 ? -12.872 -4.999  14.340  1.00 11.73 ? 118 LEU   A CA  1 
ATOM   957  C  C   . LEU   A 1 118 ? -12.633 -3.857  15.320  1.00 12.24 ? 118 LEU   A C   1 
ATOM   958  O  O   . LEU   A 1 118 ? -13.093 -3.936  16.471  1.00 12.65 ? 118 LEU   A O   1 
ATOM   959  C  CB  . LEU   A 1 118 ? -14.374 -5.084  14.028  1.00 12.14 ? 118 LEU   A CB  1 
ATOM   960  C  CG  . LEU   A 1 118 ? -15.110 -3.789  13.612  1.00 12.69 ? 118 LEU   A CG  1 
ATOM   961  C  CD1 . LEU   A 1 118 ? -14.491 -3.175  12.326  1.00 14.83 ? 118 LEU   A CD1 1 
ATOM   962  C  CD2 . LEU   A 1 118 ? -16.610 -4.122  13.384  1.00 14.39 ? 118 LEU   A CD2 1 
ATOM   963  N  N   . HIS   A 1 119 ? -12.029 -2.763  14.829  1.00 12.15 ? 119 HIS   A N   1 
ATOM   964  C  CA  . HIS   A 1 119 ? -11.760 -1.566  15.620  1.00 11.77 ? 119 HIS   A CA  1 
ATOM   965  C  C   . HIS   A 1 119 ? -12.413 -0.362  14.966  1.00 11.36 ? 119 HIS   A C   1 
ATOM   966  O  O   . HIS   A 1 119 ? -12.024 -0.054  13.817  1.00 12.83 ? 119 HIS   A O   1 
ATOM   967  C  CB  . HIS   A 1 119 ? -10.238 -1.317  15.693  1.00 12.03 ? 119 HIS   A CB  1 
ATOM   968  C  CG  . HIS   A 1 119 ? -9.624  -2.327  16.606  1.00 11.95 ? 119 HIS   A CG  1 
ATOM   969  N  ND1 . HIS   A 1 119 ? -8.235  -2.507  16.666  1.00 12.12 ? 119 HIS   A ND1 1 
ATOM   970  C  CD2 . HIS   A 1 119 ? -10.155 -3.091  17.590  1.00 12.88 ? 119 HIS   A CD2 1 
ATOM   971  C  CE1 . HIS   A 1 119 ? -7.943  -3.452  17.551  1.00 11.19 ? 119 HIS   A CE1 1 
ATOM   972  N  NE2 . HIS   A 1 119 ? -9.098  -3.837  18.152  1.00 12.63 ? 119 HIS   A NE2 1 
ATOM   973  N  N   . LEU   A 1 120 ? -13.443 0.244   15.594  1.00 12.11 ? 120 LEU   A N   1 
ATOM   974  C  CA  . LEU   A 1 120 ? -14.051 1.486   15.120  1.00 12.02 ? 120 LEU   A CA  1 
ATOM   975  C  C   . LEU   A 1 120 ? -13.430 2.613   15.920  1.00 12.35 ? 120 LEU   A C   1 
ATOM   976  O  O   . LEU   A 1 120 ? -13.574 2.646   17.165  1.00 11.90 ? 120 LEU   A O   1 
ATOM   977  C  CB  . LEU   A 1 120 ? -15.566 1.360   15.274  1.00 12.14 ? 120 LEU   A CB  1 
ATOM   978  C  CG  . LEU   A 1 120 ? -16.205 0.257   14.415  1.00 13.06 ? 120 LEU   A CG  1 
ATOM   979  C  CD1 . LEU   A 1 120 ? -17.059 -0.619  15.300  1.00 17.15 ? 120 LEU   A CD1 1 
ATOM   980  C  CD2 . LEU   A 1 120 ? -17.060 0.934   13.339  1.00 16.46 ? 120 LEU   A CD2 1 
ATOM   981  N  N   . VAL   A 1 121 ? -12.700 3.477   15.205  1.00 12.47 ? 121 VAL   A N   1 
ATOM   982  C  CA  . VAL   A 1 121 ? -11.860 4.466   15.871  1.00 12.10 ? 121 VAL   A CA  1 
ATOM   983  C  C   . VAL   A 1 121 ? -12.569 5.820   15.859  1.00 12.13 ? 121 VAL   A C   1 
ATOM   984  O  O   . VAL   A 1 121 ? -13.003 6.300   14.797  1.00 13.44 ? 121 VAL   A O   1 
ATOM   985  C  CB  . VAL   A 1 121 ? -10.529 4.579   15.102  1.00 12.60 ? 121 VAL   A CB  1 
ATOM   986  C  CG1 . VAL   A 1 121 ? -9.616  5.636   15.732  1.00 13.26 ? 121 VAL   A CG1 1 
ATOM   987  C  CG2 . VAL   A 1 121 ? -9.808  3.225   14.912  1.00 12.56 ? 121 VAL   A CG2 1 
ATOM   988  N  N   . HIS   A 1 122 ? -12.669 6.425   17.057  1.00 11.69 ? 122 HIS   A N   1 
ATOM   989  C  CA  . HIS   A 1 122 ? -13.336 7.702   17.200  1.00 12.39 ? 122 HIS   A CA  1 
ATOM   990  C  C   . HIS   A 1 122 ? -12.439 8.699   17.929  1.00 13.56 ? 122 HIS   A C   1 
ATOM   991  O  O   . HIS   A 1 122 ? -11.742 8.323   18.872  1.00 13.10 ? 122 HIS   A O   1 
ATOM   992  C  CB  . HIS   A 1 122 ? -14.631 7.529   18.019  1.00 14.22 ? 122 HIS   A CB  1 
ATOM   993  C  CG  . HIS   A 1 122 ? -15.528 6.383   17.631  1.00 12.26 ? 122 HIS   A CG  1 
ATOM   994  N  ND1 . HIS   A 1 122 ? -15.205 5.046   17.906  1.00 13.34 ? 122 HIS   A ND1 1 
ATOM   995  C  CD2 . HIS   A 1 122 ? -16.771 6.321   17.035  1.00 13.85 ? 122 HIS   A CD2 1 
ATOM   996  C  CE1 . HIS   A 1 122 ? -16.205 4.248   17.494  1.00 14.55 ? 122 HIS   A CE1 1 
ATOM   997  N  NE2 . HIS   A 1 122 ? -17.161 5.011   16.957  1.00 14.12 ? 122 HIS   A NE2 1 
ATOM   998  N  N   . TRP   A 1 123 ? -12.557 9.986   17.584  1.00 11.96 ? 123 TRP   A N   1 
ATOM   999  C  CA  . TRP   A 1 123 ? -11.790 10.996  18.312  1.00 13.03 ? 123 TRP   A CA  1 
ATOM   1000 C  C   . TRP   A 1 123 ? -12.682 11.966  19.100  1.00 13.23 ? 123 TRP   A C   1 
ATOM   1001 O  O   . TRP   A 1 123 ? -13.757 12.381  18.641  1.00 14.25 ? 123 TRP   A O   1 
ATOM   1002 C  CB  . TRP   A 1 123 ? -10.843 11.765  17.377  1.00 15.03 ? 123 TRP   A CB  1 
ATOM   1003 C  CG  . TRP   A 1 123 ? -11.541 12.353  16.191  1.00 14.97 ? 123 TRP   A CG  1 
ATOM   1004 C  CD1 . TRP   A 1 123 ? -11.696 11.781  14.960  1.00 15.93 ? 123 TRP   A CD1 1 
ATOM   1005 C  CD2 . TRP   A 1 123 ? -11.984 13.715  16.074  1.00 16.17 ? 123 TRP   A CD2 1 
ATOM   1006 N  NE1 . TRP   A 1 123 ? -12.352 12.637  14.130  1.00 17.56 ? 123 TRP   A NE1 1 
ATOM   1007 C  CE2 . TRP   A 1 123 ? -12.486 13.860  14.759  1.00 16.87 ? 123 TRP   A CE2 1 
ATOM   1008 C  CE3 . TRP   A 1 123 ? -11.991 14.824  16.941  1.00 17.37 ? 123 TRP   A CE3 1 
ATOM   1009 C  CZ2 . TRP   A 1 123 ? -13.072 15.054  14.310  1.00 18.67 ? 123 TRP   A CZ2 1 
ATOM   1010 C  CZ3 . TRP   A 1 123 ? -12.569 16.006  16.495  1.00 17.51 ? 123 TRP   A CZ3 1 
ATOM   1011 C  CH2 . TRP   A 1 123 ? -13.075 16.123  15.191  1.00 18.21 ? 123 TRP   A CH2 1 
ATOM   1012 N  N   . ASN   A 1 124 ? -12.141 12.444  20.223  1.00 13.00 ? 124 ASN   A N   1 
ATOM   1013 C  CA  . ASN   A 1 124 ? -12.860 13.361  21.105  1.00 13.77 ? 124 ASN   A CA  1 
ATOM   1014 C  C   . ASN   A 1 124 ? -13.023 14.752  20.486  1.00 14.05 ? 124 ASN   A C   1 
ATOM   1015 O  O   . ASN   A 1 124 ? -12.031 15.430  20.225  1.00 14.41 ? 124 ASN   A O   1 
ATOM   1016 C  CB  . ASN   A 1 124 ? -12.135 13.374  22.459  1.00 13.87 ? 124 ASN   A CB  1 
ATOM   1017 C  CG  . ASN   A 1 124 ? -12.921 13.989  23.587  1.00 15.52 ? 124 ASN   A CG  1 
ATOM   1018 O  OD1 . ASN   A 1 124 ? -13.732 14.869  23.343  1.00 17.32 ? 124 ASN   A OD1 1 
ATOM   1019 N  ND2 . ASN   A 1 124 ? -12.650 13.549  24.821  1.00 17.49 ? 124 ASN   A ND2 1 
ATOM   1020 N  N   . THR   A 1 125 ? -14.296 15.165  20.292  1.00 16.53 ? 125 THR   A N   1 
ATOM   1021 C  CA  . THR   A 1 125 ? -14.579 16.458  19.611  1.00 17.55 ? 125 THR   A CA  1 
ATOM   1022 C  C   . THR   A 1 125 ? -14.109 17.668  20.441  1.00 17.53 ? 125 THR   A C   1 
ATOM   1023 O  O   . THR   A 1 125 ? -14.253 18.798  19.934  1.00 19.58 ? 125 THR   A O   1 
ATOM   1024 C  CB  . THR   A 1 125 ? -16.046 16.517  19.169  1.00 17.96 ? 125 THR   A CB  1 
ATOM   1025 O  OG1 . THR   A 1 125 ? -16.750 16.444  20.407  1.00 23.82 ? 125 THR   A OG1 1 
ATOM   1026 C  CG2 . THR   A 1 125 ? -16.443 15.387  18.236  1.00 21.23 ? 125 THR   A CG2 1 
ATOM   1027 N  N   A LYS   A 1 126 ? -13.699 17.517  21.593  0.50 13.54 ? 127 LYS   A N   1 
ATOM   1028 N  N   B LYS   A 1 126 ? -13.627 17.462  21.675  0.50 17.32 ? 127 LYS   A N   1 
ATOM   1029 C  CA  A LYS   A 1 126 ? -13.224 18.709  22.343  0.50 16.09 ? 127 LYS   A CA  1 
ATOM   1030 C  CA  B LYS   A 1 126 ? -13.130 18.596  22.512  0.50 19.38 ? 127 LYS   A CA  1 
ATOM   1031 C  C   A LYS   A 1 126 ? -11.807 19.075  21.876  0.50 17.34 ? 127 LYS   A C   1 
ATOM   1032 C  C   B LYS   A 1 126 ? -11.765 19.039  21.965  0.50 19.62 ? 127 LYS   A C   1 
ATOM   1033 O  O   A LYS   A 1 126 ? -11.293 20.084  22.354  0.50 19.38 ? 127 LYS   A O   1 
ATOM   1034 O  O   B LYS   A 1 126 ? -11.319 20.170  22.177  0.50 21.28 ? 127 LYS   A O   1 
ATOM   1035 C  CB  A LYS   A 1 126 ? -13.382 18.530  23.856  0.50 16.34 ? 127 LYS   A CB  1 
ATOM   1036 C  CB  B LYS   A 1 126 ? -13.092 18.208  24.001  0.50 20.41 ? 127 LYS   A CB  1 
ATOM   1037 C  CG  A LYS   A 1 126 ? -12.434 17.530  24.497  0.50 16.94 ? 127 LYS   A CG  1 
ATOM   1038 C  CG  B LYS   A 1 126 ? -11.920 17.354  24.494  0.50 21.51 ? 127 LYS   A CG  1 
ATOM   1039 C  CD  A LYS   A 1 126 ? -12.722 17.240  25.960  0.50 16.72 ? 127 LYS   A CD  1 
ATOM   1040 C  CD  B LYS   A 1 126 ? -11.952 17.048  25.993  0.50 23.60 ? 127 LYS   A CD  1 
ATOM   1041 C  CE  A LYS   A 1 126 ? -11.657 16.348  26.560  0.50 20.43 ? 127 LYS   A CE  1 
ATOM   1042 C  CE  B LYS   A 1 126 ? -11.990 18.299  26.850  0.50 24.54 ? 127 LYS   A CE  1 
ATOM   1043 N  NZ  A LYS   A 1 126 ? -11.859 16.203  28.024  0.50 25.18 ? 127 LYS   A NZ  1 
ATOM   1044 N  NZ  B LYS   A 1 126 ? -11.896 17.983  28.298  0.50 30.51 ? 127 LYS   A NZ  1 
ATOM   1045 N  N   . TYR   A 1 127 ? -11.115 18.160  21.193  1.00 16.26 ? 128 TYR   A N   1 
ATOM   1046 C  CA  . TYR   A 1 127 ? -9.771  18.464  20.678  1.00 16.42 ? 128 TYR   A CA  1 
ATOM   1047 C  C   . TYR   A 1 127 ? -9.740  18.853  19.194  1.00 16.29 ? 128 TYR   A C   1 
ATOM   1048 O  O   . TYR   A 1 127 ? -8.647  19.073  18.664  1.00 18.69 ? 128 TYR   A O   1 
ATOM   1049 C  CB  . TYR   A 1 127 ? -8.835  17.279  20.940  1.00 16.27 ? 128 TYR   A CB  1 
ATOM   1050 C  CG  . TYR   A 1 127 ? -8.752  16.981  22.409  1.00 15.33 ? 128 TYR   A CG  1 
ATOM   1051 C  CD1 . TYR   A 1 127 ? -8.359  17.981  23.294  1.00 17.23 ? 128 TYR   A CD1 1 
ATOM   1052 C  CD2 . TYR   A 1 127 ? -9.004  15.710  22.937  1.00 14.28 ? 128 TYR   A CD2 1 
ATOM   1053 C  CE1 . TYR   A 1 127 ? -8.266  17.718  24.653  1.00 19.03 ? 128 TYR   A CE1 1 
ATOM   1054 C  CE2 . TYR   A 1 127 ? -8.908  15.438  24.289  1.00 15.89 ? 128 TYR   A CE2 1 
ATOM   1055 C  CZ  . TYR   A 1 127 ? -8.529  16.458  25.143  1.00 16.98 ? 128 TYR   A CZ  1 
ATOM   1056 O  OH  . TYR   A 1 127 ? -8.433  16.165  26.470  1.00 21.32 ? 128 TYR   A OH  1 
ATOM   1057 N  N   . GLY   A 1 128 ? -10.903 18.952  18.546  1.00 16.57 ? 129 GLY   A N   1 
ATOM   1058 C  CA  . GLY   A 1 128 ? -10.977 19.644  17.264  1.00 17.64 ? 129 GLY   A CA  1 
ATOM   1059 C  C   . GLY   A 1 128 ? -10.618 18.768  16.066  1.00 18.87 ? 129 GLY   A C   1 
ATOM   1060 O  O   . GLY   A 1 128 ? -11.253 18.900  15.003  1.00 20.19 ? 129 GLY   A O   1 
ATOM   1061 N  N   . ASP   A 1 129 ? -9.562  17.928  16.189  1.00 17.96 ? 130 ASP   A N   1 
ATOM   1062 C  CA  . ASP   A 1 129 ? -9.306  16.960  15.138  1.00 19.59 ? 130 ASP   A CA  1 
ATOM   1063 C  C   . ASP   A 1 129 ? -8.491  15.790  15.668  1.00 21.43 ? 130 ASP   A C   1 
ATOM   1064 O  O   . ASP   A 1 129 ? -8.048  15.769  16.837  1.00 19.96 ? 130 ASP   A O   1 
ATOM   1065 C  CB  . ASP   A 1 129 ? -8.665  17.599  13.911  1.00 24.53 ? 130 ASP   A CB  1 
ATOM   1066 C  CG  . ASP   A 1 129 ? -7.251  18.066  14.084  1.00 26.24 ? 130 ASP   A CG  1 
ATOM   1067 O  OD1 . ASP   A 1 129 ? -6.613  17.802  15.146  1.00 31.18 ? 130 ASP   A OD1 1 
ATOM   1068 O  OD2 . ASP   A 1 129 ? -6.773  18.714  13.145  1.00 32.26 ? 130 ASP   A OD2 1 
ATOM   1069 N  N   . PHE   A 1 130 ? -8.302  14.811  14.772  1.00 18.95 ? 131 PHE   A N   1 
ATOM   1070 C  CA  . PHE   A 1 130 ? -7.700  13.555  15.167  1.00 21.30 ? 131 PHE   A CA  1 
ATOM   1071 C  C   . PHE   A 1 130 ? -6.259  13.776  15.620  1.00 19.85 ? 131 PHE   A C   1 
ATOM   1072 O  O   . PHE   A 1 130 ? -5.828  13.187  16.608  1.00 16.61 ? 131 PHE   A O   1 
ATOM   1073 C  CB  . PHE   A 1 130 ? -7.842  12.539  14.025  1.00 19.84 ? 131 PHE   A CB  1 
ATOM   1074 C  CG  . PHE   A 1 130 ? -7.151  11.229  14.276  1.00 21.47 ? 131 PHE   A CG  1 
ATOM   1075 C  CD1 . PHE   A 1 130 ? -5.811  11.079  13.955  1.00 22.79 ? 131 PHE   A CD1 1 
ATOM   1076 C  CD2 . PHE   A 1 130 ? -7.810  10.174  14.903  1.00 20.54 ? 131 PHE   A CD2 1 
ATOM   1077 C  CE1 . PHE   A 1 130 ? -5.144  9.889   14.218  1.00 23.37 ? 131 PHE   A CE1 1 
ATOM   1078 C  CE2 . PHE   A 1 130 ? -7.126  8.998   15.177  1.00 21.03 ? 131 PHE   A CE2 1 
ATOM   1079 C  CZ  . PHE   A 1 130 ? -5.796  8.859   14.859  1.00 22.89 ? 131 PHE   A CZ  1 
ATOM   1080 N  N   . GLY   A 1 131 ? -5.472  14.567  14.859  1.00 20.47 ? 132 GLY   A N   1 
ATOM   1081 C  CA  . GLY   A 1 131 ? -4.069  14.744  15.188  1.00 19.93 ? 132 GLY   A CA  1 
ATOM   1082 C  C   . GLY   A 1 131 ? -3.836  15.355  16.562  1.00 18.65 ? 132 GLY   A C   1 
ATOM   1083 O  O   . GLY   A 1 131 ? -2.818  15.076  17.191  1.00 20.93 ? 132 GLY   A O   1 
ATOM   1084 N  N   . LYS   A 1 132 ? -4.724  16.273  16.975  1.00 18.33 ? 133 LYS   A N   1 
ATOM   1085 C  CA  . LYS   A 1 132 ? -4.591  16.853  18.299  1.00 18.80 ? 133 LYS   A CA  1 
ATOM   1086 C  C   . LYS   A 1 132 ? -5.087  15.866  19.357  1.00 18.37 ? 133 LYS   A C   1 
ATOM   1087 O  O   . LYS   A 1 132 ? -4.511  15.762  20.447  1.00 17.56 ? 133 LYS   A O   1 
ATOM   1088 C  CB  . LYS   A 1 132 ? -5.369  18.165  18.399  1.00 20.35 ? 133 LYS   A CB  1 
ATOM   1089 C  CG  . LYS   A 1 132 ? -4.763  19.320  17.611  1.00 27.78 ? 133 LYS   A CG  1 
ATOM   1090 C  CD  . LYS   A 1 132 ? -3.370  19.732  18.074  1.00 34.83 ? 133 LYS   A CD  1 
ATOM   1091 C  CE  . LYS   A 1 132 ? -3.396  21.046  18.841  1.00 39.05 ? 133 LYS   A CE  1 
ATOM   1092 N  NZ  . LYS   A 1 132 ? -2.046  21.439  19.312  1.00 42.37 ? 133 LYS   A NZ  1 
ATOM   1093 N  N   . ALA   A 1 133 ? -6.159  15.149  19.016  1.00 16.63 ? 134 ALA   A N   1 
ATOM   1094 C  CA  . ALA   A 1 133 ? -6.728  14.183  19.966  1.00 15.69 ? 134 ALA   A CA  1 
ATOM   1095 C  C   . ALA   A 1 133 ? -5.720  13.099  20.385  1.00 15.62 ? 134 ALA   A C   1 
ATOM   1096 O  O   . ALA   A 1 133 ? -5.680  12.703  21.556  1.00 15.04 ? 134 ALA   A O   1 
ATOM   1097 C  CB  . ALA   A 1 133 ? -7.967  13.563  19.345  1.00 15.66 ? 134 ALA   A CB  1 
ATOM   1098 N  N   . VAL   A 1 134 ? -4.868  12.625  19.476  1.00 16.52 ? 135 VAL   A N   1 
ATOM   1099 C  CA  . VAL   A 1 134 ? -3.956  11.512  19.811  1.00 17.99 ? 135 VAL   A CA  1 
ATOM   1100 C  C   . VAL   A 1 134 ? -2.855  11.954  20.774  1.00 16.29 ? 135 VAL   A C   1 
ATOM   1101 O  O   . VAL   A 1 134 ? -2.161  11.125  21.349  1.00 17.83 ? 135 VAL   A O   1 
ATOM   1102 C  CB  . VAL   A 1 134 ? -3.339  10.807  18.581  1.00 18.36 ? 135 VAL   A CB  1 
ATOM   1103 C  CG1 . VAL   A 1 134 ? -4.396  10.130  17.750  1.00 20.42 ? 135 VAL   A CG1 1 
ATOM   1104 C  CG2 . VAL   A 1 134 ? -2.400  11.659  17.719  1.00 19.60 ? 135 VAL   A CG2 1 
ATOM   1105 N  N   . GLN   A 1 135 ? -2.744  13.270  21.007  1.00 16.62 ? 136 GLN   A N   1 
ATOM   1106 C  CA  . GLN   A 1 135 ? -1.752  13.738  21.975  1.00 18.60 ? 136 GLN   A CA  1 
ATOM   1107 C  C   . GLN   A 1 135 ? -2.302  13.842  23.385  1.00 18.83 ? 136 GLN   A C   1 
ATOM   1108 O  O   . GLN   A 1 135 ? -1.634  14.382  24.293  1.00 21.68 ? 136 GLN   A O   1 
ATOM   1109 C  CB  . GLN   A 1 135 ? -1.310  15.118  21.487  1.00 20.94 ? 136 GLN   A CB  1 
ATOM   1110 C  CG  . GLN   A 1 135 ? -0.571  14.991  20.170  1.00 22.77 ? 136 GLN   A CG  1 
ATOM   1111 C  CD  . GLN   A 1 135 ? -0.046  16.303  19.645  1.00 32.02 ? 136 GLN   A CD  1 
ATOM   1112 O  OE1 . GLN   A 1 135 ? 0.728   17.008  20.313  1.00 33.25 ? 136 GLN   A OE1 1 
ATOM   1113 N  NE2 . GLN   A 1 135 ? -0.491  16.633  18.442  1.00 30.26 ? 136 GLN   A NE2 1 
ATOM   1114 N  N   . GLN   A 1 136 ? -3.552  13.395  23.548  1.00 16.14 ? 137 GLN   A N   1 
ATOM   1115 C  CA  . GLN   A 1 136 ? -4.213  13.585  24.827  1.00 16.89 ? 137 GLN   A CA  1 
ATOM   1116 C  C   . GLN   A 1 136 ? -4.576  12.236  25.438  1.00 17.32 ? 137 GLN   A C   1 
ATOM   1117 O  O   . GLN   A 1 136 ? -4.939  11.277  24.741  1.00 15.79 ? 137 GLN   A O   1 
ATOM   1118 C  CB  . GLN   A 1 136 ? -5.509  14.367  24.671  1.00 18.45 ? 137 GLN   A CB  1 
ATOM   1119 C  CG  . GLN   A 1 136 ? -5.387  15.642  23.830  1.00 21.47 ? 137 GLN   A CG  1 
ATOM   1120 C  CD  . GLN   A 1 136 ? -4.400  16.622  24.413  1.00 27.50 ? 137 GLN   A CD  1 
ATOM   1121 O  OE1 . GLN   A 1 136 ? -4.222  16.705  25.613  1.00 24.71 ? 137 GLN   A OE1 1 
ATOM   1122 N  NE2 . GLN   A 1 136 ? -3.741  17.351  23.538  1.00 33.64 ? 137 GLN   A NE2 1 
ATOM   1123 N  N   . PRO   A 1 137 ? -4.581  12.088  26.786  1.00 18.21 ? 138 PRO   A N   1 
ATOM   1124 C  CA  . PRO   A 1 137 ? -4.867  10.799  27.398  1.00 17.07 ? 138 PRO   A CA  1 
ATOM   1125 C  C   . PRO   A 1 137 ? -6.291  10.311  27.216  1.00 18.02 ? 138 PRO   A C   1 
ATOM   1126 O  O   . PRO   A 1 137 ? -6.544  9.107   27.336  1.00 18.46 ? 138 PRO   A O   1 
ATOM   1127 C  CB  . PRO   A 1 137 ? -4.565  10.985  28.896  1.00 20.59 ? 138 PRO   A CB  1 
ATOM   1128 C  CG  . PRO   A 1 137 ? -4.463  12.489  29.097  1.00 24.68 ? 138 PRO   A CG  1 
ATOM   1129 C  CD  . PRO   A 1 137 ? -4.202  13.133  27.751  1.00 20.77 ? 138 PRO   A CD  1 
ATOM   1130 N  N   . ASP   A 1 138 ? -7.188  11.245  26.893  1.00 16.28 ? 139 ASP   A N   1 
ATOM   1131 C  CA  . ASP   A 1 138 ? -8.584  10.885  26.639  1.00 15.67 ? 139 ASP   A CA  1 
ATOM   1132 C  C   . ASP   A 1 138 ? -8.979  11.292  25.214  1.00 14.97 ? 139 ASP   A C   1 
ATOM   1133 O  O   . ASP   A 1 138 ? -10.107 11.710  24.949  1.00 15.15 ? 139 ASP   A O   1 
ATOM   1134 C  CB  . ASP   A 1 138 ? -9.573  11.543  27.613  1.00 18.11 ? 139 ASP   A CB  1 
ATOM   1135 C  CG  . ASP   A 1 138 ? -9.465  13.059  27.659  1.00 18.85 ? 139 ASP   A CG  1 
ATOM   1136 O  OD1 . ASP   A 1 138 ? -8.513  13.604  27.086  1.00 20.00 ? 139 ASP   A OD1 1 
ATOM   1137 O  OD2 . ASP   A 1 138 ? -10.327 13.673  28.343  1.00 21.86 ? 139 ASP   A OD2 1 
ATOM   1138 N  N   . GLY   A 1 139 ? -8.042  11.209  24.257  1.00 13.16 ? 140 GLY   A N   1 
ATOM   1139 C  CA  . GLY   A 1 139 ? -8.250  11.660  22.894  1.00 14.56 ? 140 GLY   A CA  1 
ATOM   1140 C  C   . GLY   A 1 139 ? -9.137  10.760  22.031  1.00 12.31 ? 140 GLY   A C   1 
ATOM   1141 O  O   . GLY   A 1 139 ? -9.813  11.266  21.170  1.00 13.87 ? 140 GLY   A O   1 
ATOM   1142 N  N   . LEU   A 1 140 ? -9.007  9.443   22.222  1.00 13.13 ? 141 LEU   A N   1 
ATOM   1143 C  CA  . LEU   A 1 140 ? -9.622  8.482   21.324  1.00 14.23 ? 141 LEU   A CA  1 
ATOM   1144 C  C   . LEU   A 1 140 ? -10.484 7.522   22.131  1.00 13.55 ? 141 LEU   A C   1 
ATOM   1145 O  O   . LEU   A 1 140 ? -10.255 7.274   23.313  1.00 13.35 ? 141 LEU   A O   1 
ATOM   1146 C  CB  . LEU   A 1 140 ? -8.565  7.653   20.583  1.00 15.09 ? 141 LEU   A CB  1 
ATOM   1147 C  CG  . LEU   A 1 140 ? -7.675  8.343   19.545  1.00 17.91 ? 141 LEU   A CG  1 
ATOM   1148 C  CD1 . LEU   A 1 140 ? -6.966  7.313   18.676  1.00 17.84 ? 141 LEU   A CD1 1 
ATOM   1149 C  CD2 . LEU   A 1 140 ? -8.364  9.385   18.666  1.00 17.37 ? 141 LEU   A CD2 1 
ATOM   1150 N  N   . ALA   A 1 141 ? -11.527 7.028   21.452  1.00 12.80 ? 142 ALA   A N   1 
ATOM   1151 C  CA  . ALA   A 1 141 ? -12.302 5.894   21.957  1.00 12.00 ? 142 ALA   A CA  1 
ATOM   1152 C  C   . ALA   A 1 141 ? -12.385 4.876   20.832  1.00 12.29 ? 142 ALA   A C   1 
ATOM   1153 O  O   . ALA   A 1 141 ? -12.735 5.211   19.688  1.00 13.69 ? 142 ALA   A O   1 
ATOM   1154 C  CB  . ALA   A 1 141 ? -13.687 6.358   22.382  1.00 13.67 ? 142 ALA   A CB  1 
ATOM   1155 N  N   . VAL   A 1 142 ? -11.920 3.643   21.133  1.00 12.36 ? 143 VAL   A N   1 
ATOM   1156 C  CA  . VAL   A 1 142 ? -11.940 2.609   20.109  1.00 13.45 ? 143 VAL   A CA  1 
ATOM   1157 C  C   . VAL   A 1 142 ? -12.893 1.530   20.586  1.00 13.05 ? 143 VAL   A C   1 
ATOM   1158 O  O   . VAL   A 1 142 ? -12.749 1.015   21.708  1.00 13.61 ? 143 VAL   A O   1 
ATOM   1159 C  CB  . VAL   A 1 142 ? -10.556 2.033   19.752  1.00 12.94 ? 143 VAL   A CB  1 
ATOM   1160 C  CG1 . VAL   A 1 142 ? -10.684 1.013   18.599  1.00 13.09 ? 143 VAL   A CG1 1 
ATOM   1161 C  CG2 . VAL   A 1 142 ? -9.573  3.142   19.331  1.00 15.10 ? 143 VAL   A CG2 1 
ATOM   1162 N  N   . LEU   A 1 143 ? -13.880 1.253   19.739  1.00 12.13 ? 144 LEU   A N   1 
ATOM   1163 C  CA  . LEU   A 1 143 ? -14.844 0.207   19.995  1.00 12.82 ? 144 LEU   A CA  1 
ATOM   1164 C  C   . LEU   A 1 143 ? -14.305 -1.044  19.317  1.00 13.16 ? 144 LEU   A C   1 
ATOM   1165 O  O   . LEU   A 1 143 ? -14.134 -1.085  18.093  1.00 13.22 ? 144 LEU   A O   1 
ATOM   1166 C  CB  . LEU   A 1 143 ? -16.209 0.654   19.445  1.00 13.86 ? 144 LEU   A CB  1 
ATOM   1167 C  CG  . LEU   A 1 143 ? -17.339 -0.383  19.522  1.00 14.75 ? 144 LEU   A CG  1 
ATOM   1168 C  CD1 . LEU   A 1 143 ? -17.614 -0.716  20.980  1.00 16.77 ? 144 LEU   A CD1 1 
ATOM   1169 C  CD2 . LEU   A 1 143 ? -18.610 0.200   18.884  1.00 15.60 ? 144 LEU   A CD2 1 
ATOM   1170 N  N   . GLY   A 1 144 ? -14.082 -2.089  20.099  1.00 13.88 ? 145 GLY   A N   1 
ATOM   1171 C  CA  . GLY   A 1 144 ? -13.498 -3.346  19.629  1.00 12.62 ? 145 GLY   A CA  1 
ATOM   1172 C  C   . GLY   A 1 144 ? -14.549 -4.449  19.609  1.00 13.27 ? 145 GLY   A C   1 
ATOM   1173 O  O   . GLY   A 1 144 ? -15.272 -4.578  20.590  1.00 13.33 ? 145 GLY   A O   1 
ATOM   1174 N  N   . ILE   A 1 145 ? -14.661 -5.172  18.505  1.00 12.66 ? 146 ILE   A N   1 
ATOM   1175 C  CA  . ILE   A 1 145 ? -15.698 -6.205  18.369  1.00 12.19 ? 146 ILE   A CA  1 
ATOM   1176 C  C   . ILE   A 1 145 ? -14.963 -7.448  17.879  1.00 12.11 ? 146 ILE   A C   1 
ATOM   1177 O  O   . ILE   A 1 145 ? -14.282 -7.417  16.859  1.00 13.10 ? 146 ILE   A O   1 
ATOM   1178 C  CB  . ILE   A 1 145 ? -16.777 -5.724  17.366  1.00 13.23 ? 146 ILE   A CB  1 
ATOM   1179 C  CG1 . ILE   A 1 145 ? -17.424 -4.438  17.864  1.00 15.71 ? 146 ILE   A CG1 1 
ATOM   1180 C  CG2 . ILE   A 1 145 ? -17.835 -6.822  17.159  1.00 15.00 ? 146 ILE   A CG2 1 
ATOM   1181 C  CD1 . ILE   A 1 145 ? -18.467 -3.799  16.940  1.00 14.27 ? 146 ILE   A CD1 1 
ATOM   1182 N  N   . PHE   A 1 146 ? -15.145 -8.559  18.552  1.00 12.94 ? 147 PHE   A N   1 
ATOM   1183 C  CA  . PHE   A 1 146 ? -14.522 -9.798  18.121  1.00 13.01 ? 147 PHE   A CA  1 
ATOM   1184 C  C   . PHE   A 1 146 ? -15.271 -10.437 16.948  1.00 13.29 ? 147 PHE   A C   1 
ATOM   1185 O  O   . PHE   A 1 146 ? -16.508 -10.336 16.887  1.00 14.46 ? 147 PHE   A O   1 
ATOM   1186 C  CB  . PHE   A 1 146 ? -14.507 -10.775 19.294  1.00 12.98 ? 147 PHE   A CB  1 
ATOM   1187 C  CG  . PHE   A 1 146 ? -13.665 -10.335 20.452  1.00 11.64 ? 147 PHE   A CG  1 
ATOM   1188 C  CD1 . PHE   A 1 146 ? -12.291 -10.157 20.268  1.00 13.37 ? 147 PHE   A CD1 1 
ATOM   1189 C  CD2 . PHE   A 1 146 ? -14.220 -10.069 21.694  1.00 12.81 ? 147 PHE   A CD2 1 
ATOM   1190 C  CE1 . PHE   A 1 146 ? -11.477 -9.767  21.326  1.00 12.33 ? 147 PHE   A CE1 1 
ATOM   1191 C  CE2 . PHE   A 1 146 ? -13.411 -9.698  22.762  1.00 12.57 ? 147 PHE   A CE2 1 
ATOM   1192 C  CZ  . PHE   A 1 146 ? -12.033 -9.576  22.586  1.00 12.59 ? 147 PHE   A CZ  1 
ATOM   1193 N  N   . LEU   A 1 147 ? -14.527 -11.143 16.084  1.00 12.72 ? 148 LEU   A N   1 
ATOM   1194 C  CA  . LEU   A 1 147 ? -15.154 -11.983 15.050  1.00 13.45 ? 148 LEU   A CA  1 
ATOM   1195 C  C   . LEU   A 1 147 ? -14.767 -13.450 15.257  1.00 13.69 ? 148 LEU   A C   1 
ATOM   1196 O  O   . LEU   A 1 147 ? -13.594 -13.802 15.442  1.00 14.08 ? 148 LEU   A O   1 
ATOM   1197 C  CB  . LEU   A 1 147 ? -14.640 -11.561 13.675  1.00 14.05 ? 148 LEU   A CB  1 
ATOM   1198 C  CG  . LEU   A 1 147 ? -15.202 -10.296 13.007  1.00 13.91 ? 148 LEU   A CG  1 
ATOM   1199 C  CD1 . LEU   A 1 147 ? -14.899 -9.021  13.807  1.00 16.24 ? 148 LEU   A CD1 1 
ATOM   1200 C  CD2 . LEU   A 1 147 ? -14.663 -10.173 11.580  1.00 15.39 ? 148 LEU   A CD2 1 
ATOM   1201 N  N   . LYS   A 1 148 ? -15.820 -14.286 15.178  1.00 14.84 ? 149 LYS   A N   1 
ATOM   1202 C  CA  . LYS   A 1 148 ? -15.673 -15.734 15.150  1.00 14.30 ? 149 LYS   A CA  1 
ATOM   1203 C  C   . LYS   A 1 148 ? -16.148 -16.242 13.786  1.00 17.75 ? 149 LYS   A C   1 
ATOM   1204 O  O   . LYS   A 1 148 ? -16.948 -15.595 13.121  1.00 16.54 ? 149 LYS   A O   1 
ATOM   1205 C  CB  . LYS   A 1 148 ? -16.457 -16.381 16.299  1.00 17.30 ? 149 LYS   A CB  1 
ATOM   1206 C  CG  . LYS   A 1 148 ? -17.974 -16.312 16.228  1.00 19.45 ? 149 LYS   A CG  1 
ATOM   1207 C  CD  . LYS   A 1 148 ? -18.595 -16.894 17.512  1.00 24.07 ? 149 LYS   A CD  1 
ATOM   1208 C  CE  . LYS   A 1 148 ? -19.924 -17.572 17.263  1.00 31.89 ? 149 LYS   A CE  1 
ATOM   1209 N  NZ  . LYS   A 1 148 ? -20.189 -18.562 18.339  1.00 39.10 ? 149 LYS   A NZ  1 
ATOM   1210 N  N   . VAL   A 1 149 ? -15.650 -17.413 13.417  1.00 17.30 ? 150 VAL   A N   1 
ATOM   1211 C  CA  . VAL   A 1 149 ? -16.006 -18.004 12.129  1.00 16.57 ? 150 VAL   A CA  1 
ATOM   1212 C  C   . VAL   A 1 149 ? -17.227 -18.922 12.295  1.00 18.09 ? 150 VAL   A C   1 
ATOM   1213 O  O   . VAL   A 1 149 ? -17.222 -19.874 13.084  1.00 20.08 ? 150 VAL   A O   1 
ATOM   1214 C  CB  . VAL   A 1 149 ? -14.804 -18.758 11.525  1.00 17.40 ? 150 VAL   A CB  1 
ATOM   1215 C  CG1 . VAL   A 1 149 ? -15.225 -19.504 10.262  1.00 18.17 ? 150 VAL   A CG1 1 
ATOM   1216 C  CG2 . VAL   A 1 149 ? -13.730 -17.746 11.125  1.00 19.42 ? 150 VAL   A CG2 1 
ATOM   1217 N  N   . GLY   A 1 150 ? -18.269 -18.646 11.499  1.00 16.86 ? 151 GLY   A N   1 
ATOM   1218 C  CA  . GLY   A 1 150 ? -19.501 -19.425 11.575  1.00 18.83 ? 151 GLY   A CA  1 
ATOM   1219 C  C   . GLY   A 1 150 ? -20.410 -18.998 10.434  1.00 15.91 ? 151 GLY   A C   1 
ATOM   1220 O  O   . GLY   A 1 150 ? -20.036 -19.110 9.265   1.00 17.86 ? 151 GLY   A O   1 
ATOM   1221 N  N   A SER   A 1 151 ? -21.614 -18.526 10.771  0.50 18.12 ? 152 SER   A N   1 
ATOM   1222 N  N   B SER   A 1 151 ? -21.593 -18.497 10.793  0.50 17.22 ? 152 SER   A N   1 
ATOM   1223 C  CA  A SER   A 1 151 ? -22.503 -17.999 9.738   0.50 19.42 ? 152 SER   A CA  1 
ATOM   1224 C  CA  B SER   A 1 151 ? -22.491 -17.912 9.803   0.50 18.08 ? 152 SER   A CA  1 
ATOM   1225 C  C   A SER   A 1 151 ? -21.966 -16.667 9.211   0.50 19.05 ? 152 SER   A C   1 
ATOM   1226 C  C   B SER   A 1 151 ? -21.880 -16.653 9.187   0.50 18.27 ? 152 SER   A C   1 
ATOM   1227 O  O   A SER   A 1 151 ? -21.295 -15.929 9.940   0.50 20.12 ? 152 SER   A O   1 
ATOM   1228 O  O   B SER   A 1 151 ? -21.085 -15.946 9.819   0.50 18.31 ? 152 SER   A O   1 
ATOM   1229 C  CB  A SER   A 1 151 ? -23.891 -17.827 10.275  0.50 23.15 ? 152 SER   A CB  1 
ATOM   1230 C  CB  B SER   A 1 151 ? -23.801 -17.602 10.449  0.50 19.51 ? 152 SER   A CB  1 
ATOM   1231 O  OG  A SER   A 1 151 ? -23.915 -16.807 11.261  0.50 25.56 ? 152 SER   A OG  1 
ATOM   1232 O  OG  B SER   A 1 151 ? -24.333 -18.782 11.021  0.50 21.37 ? 152 SER   A OG  1 
ATOM   1233 N  N   . ALA   A 1 152 ? -22.243 -16.364 7.931   1.00 19.08 ? 153 ALA   A N   1 
ATOM   1234 C  CA  . ALA   A 1 152 ? -21.815 -15.129 7.289   1.00 18.96 ? 153 ALA   A CA  1 
ATOM   1235 C  C   . ALA   A 1 152 ? -22.436 -13.907 7.974   1.00 17.89 ? 153 ALA   A C   1 
ATOM   1236 O  O   . ALA   A 1 152 ? -23.552 -13.993 8.500   1.00 20.70 ? 153 ALA   A O   1 
ATOM   1237 C  CB  . ALA   A 1 152 ? -22.152 -15.120 5.813   1.00 21.50 ? 153 ALA   A CB  1 
ATOM   1238 N  N   . LYS   A 1 153 ? -21.705 -12.786 7.913   1.00 19.30 ? 154 LYS   A N   1 
ATOM   1239 C  CA  . LYS   A 1 153 ? -22.262 -11.500 8.308   1.00 19.88 ? 154 LYS   A CA  1 
ATOM   1240 C  C   . LYS   A 1 153 ? -22.659 -10.736 7.052   1.00 18.65 ? 154 LYS   A C   1 
ATOM   1241 O  O   . LYS   A 1 153 ? -21.832 -10.280 6.280   1.00 17.76 ? 154 LYS   A O   1 
ATOM   1242 C  CB  . LYS   A 1 153 ? -21.216 -10.749 9.139   1.00 20.49 ? 154 LYS   A CB  1 
ATOM   1243 C  CG  . LYS   A 1 153 ? -21.717 -9.521  9.873   1.00 21.17 ? 154 LYS   A CG  1 
ATOM   1244 C  CD  . LYS   A 1 153 ? -22.610 -9.884  11.023  1.00 23.88 ? 154 LYS   A CD  1 
ATOM   1245 C  CE  . LYS   A 1 153 ? -22.846 -8.734  11.977  1.00 27.55 ? 154 LYS   A CE  1 
ATOM   1246 N  NZ  . LYS   A 1 153 ? -23.762 -9.172  13.047  1.00 29.24 ? 154 LYS   A NZ  1 
ATOM   1247 N  N   . PRO   A 1 154 ? -23.969 -10.628 6.751   1.00 19.95 ? 155 PRO   A N   1 
ATOM   1248 C  CA  . PRO   A 1 154 ? -24.384 -10.043 5.467   1.00 19.54 ? 155 PRO   A CA  1 
ATOM   1249 C  C   . PRO   A 1 154 ? -23.941 -8.585  5.373   1.00 17.84 ? 155 PRO   A C   1 
ATOM   1250 O  O   . PRO   A 1 154 ? -23.522 -8.144  4.320   1.00 20.69 ? 155 PRO   A O   1 
ATOM   1251 C  CB  . PRO   A 1 154 ? -25.926 -10.170 5.550   1.00 21.16 ? 155 PRO   A CB  1 
ATOM   1252 C  CG  . PRO   A 1 154 ? -26.120 -11.355 6.476   1.00 22.65 ? 155 PRO   A CG  1 
ATOM   1253 C  CD  . PRO   A 1 154 ? -25.099 -11.108 7.568   1.00 21.58 ? 155 PRO   A CD  1 
ATOM   1254 N  N   . GLY   A 1 155 ? -23.836 -7.912  6.519   1.00 18.37 ? 156 GLY   A N   1 
ATOM   1255 C  CA  . GLY   A 1 155 ? -23.445 -6.507  6.515   1.00 17.68 ? 156 GLY   A CA  1 
ATOM   1256 C  C   . GLY   A 1 155 ? -21.957 -6.271  6.292   1.00 20.36 ? 156 GLY   A C   1 
ATOM   1257 O  O   . GLY   A 1 155 ? -21.539 -5.121  6.105   1.00 22.78 ? 156 GLY   A O   1 
ATOM   1258 N  N   . LEU   A 1 156 ? -21.166 -7.348  6.305   1.00 18.15 ? 157 LEU   A N   1 
ATOM   1259 C  CA  . LEU   A 1 156 ? -19.749 -7.288  5.949   1.00 17.25 ? 157 LEU   A CA  1 
ATOM   1260 C  C   . LEU   A 1 156 ? -19.478 -7.510  4.467   1.00 17.84 ? 157 LEU   A C   1 
ATOM   1261 O  O   . LEU   A 1 156 ? -18.395 -7.205  3.982   1.00 17.59 ? 157 LEU   A O   1 
ATOM   1262 C  CB  . LEU   A 1 156 ? -19.030 -8.358  6.774   1.00 17.85 ? 157 LEU   A CB  1 
ATOM   1263 C  CG  . LEU   A 1 156 ? -17.501 -8.445  6.657   1.00 19.56 ? 157 LEU   A CG  1 
ATOM   1264 C  CD1 . LEU   A 1 156 ? -16.804 -7.131  7.064   1.00 20.30 ? 157 LEU   A CD1 1 
ATOM   1265 C  CD2 . LEU   A 1 156 ? -16.986 -9.605  7.504   1.00 20.35 ? 157 LEU   A CD2 1 
ATOM   1266 N  N   . GLN   A 1 157 ? -20.462 -8.044  3.708   1.00 18.04 ? 158 GLN   A N   1 
ATOM   1267 C  CA  . GLN   A 1 157 ? -20.115 -8.528  2.382   1.00 19.88 ? 158 GLN   A CA  1 
ATOM   1268 C  C   . GLN   A 1 157 ? -19.676 -7.413  1.436   1.00 16.64 ? 158 GLN   A C   1 
ATOM   1269 O  O   . GLN   A 1 157 ? -18.797 -7.635  0.621   1.00 19.26 ? 158 GLN   A O   1 
ATOM   1270 C  CB  . GLN   A 1 157 ? -21.221 -9.382  1.778   1.00 20.89 ? 158 GLN   A CB  1 
ATOM   1271 C  CG  . GLN   A 1 157 ? -20.784 -10.059 0.461   1.00 21.83 ? 158 GLN   A CG  1 
ATOM   1272 C  CD  . GLN   A 1 157 ? -19.742 -11.127 0.688   1.00 21.06 ? 158 GLN   A CD  1 
ATOM   1273 O  OE1 . GLN   A 1 157 ? -19.630 -11.700 1.781   1.00 21.24 ? 158 GLN   A OE1 1 
ATOM   1274 N  NE2 . GLN   A 1 157 ? -18.902 -11.377 -0.295  1.00 22.96 ? 158 GLN   A NE2 1 
ATOM   1275 N  N   . LYS   A 1 158 ? -20.244 -6.198  1.580   1.00 19.24 ? 159 LYS   A N   1 
ATOM   1276 C  CA  . LYS   A 1 158 ? -19.855 -5.079  0.725   1.00 19.05 ? 159 LYS   A CA  1 
ATOM   1277 C  C   . LYS   A 1 158 ? -18.374 -4.749  0.903   1.00 18.54 ? 159 LYS   A C   1 
ATOM   1278 O  O   . LYS   A 1 158 ? -17.687 -4.404  -0.040  1.00 21.28 ? 159 LYS   A O   1 
ATOM   1279 C  CB  . LYS   A 1 158 ? -20.735 -3.840  0.969   1.00 23.48 ? 159 LYS   A CB  1 
ATOM   1280 C  CG  . LYS   A 1 158 ? -22.127 -3.859  0.332   1.00 28.71 ? 159 LYS   A CG  1 
ATOM   1281 N  N   . VAL   A 1 159 ? -17.854 -4.922  2.133   1.00 19.06 ? 160 VAL   A N   1 
ATOM   1282 C  CA  . VAL   A 1 159 ? -16.430 -4.728  2.359   1.00 18.53 ? 160 VAL   A CA  1 
ATOM   1283 C  C   . VAL   A 1 159 ? -15.644 -5.855  1.683   1.00 17.73 ? 160 VAL   A C   1 
ATOM   1284 O  O   . VAL   A 1 159 ? -14.656 -5.600  0.982   1.00 18.67 ? 160 VAL   A O   1 
ATOM   1285 C  CB  . VAL   A 1 159 ? -16.147 -4.667  3.884   1.00 17.58 ? 160 VAL   A CB  1 
ATOM   1286 C  CG1 . VAL   A 1 159 ? -14.667 -4.737  4.242   1.00 18.10 ? 160 VAL   A CG1 1 
ATOM   1287 C  CG2 . VAL   A 1 159 ? -16.811 -3.453  4.514   1.00 20.13 ? 160 VAL   A CG2 1 
ATOM   1288 N  N   . VAL   A 1 160 ? -16.075 -7.107  1.853   1.00 18.49 ? 161 VAL   A N   1 
ATOM   1289 C  CA  . VAL   A 1 160 ? -15.266 -8.214  1.354   1.00 20.94 ? 161 VAL   A CA  1 
ATOM   1290 C  C   . VAL   A 1 160 ? -15.205 -8.105  -0.172  1.00 19.90 ? 161 VAL   A C   1 
ATOM   1291 O  O   . VAL   A 1 160 ? -14.178 -8.371  -0.773  1.00 20.33 ? 161 VAL   A O   1 
ATOM   1292 C  CB  . VAL   A 1 160 ? -15.874 -9.569  1.808   1.00 22.30 ? 161 VAL   A CB  1 
ATOM   1293 C  CG1 . VAL   A 1 160 ? -15.456 -10.755 0.929   1.00 28.02 ? 161 VAL   A CG1 1 
ATOM   1294 C  CG2 . VAL   A 1 160 ? -15.590 -9.820  3.285   1.00 24.23 ? 161 VAL   A CG2 1 
ATOM   1295 N  N   . ASP   A 1 161 ? -16.311 -7.653  -0.786  1.00 21.87 ? 162 ASP   A N   1 
ATOM   1296 C  CA  . ASP   A 1 161 ? -16.351 -7.694  -2.248  1.00 22.29 ? 162 ASP   A CA  1 
ATOM   1297 C  C   . ASP   A 1 161 ? -15.391 -6.677  -2.884  1.00 25.11 ? 162 ASP   A C   1 
ATOM   1298 O  O   . ASP   A 1 161 ? -14.940 -6.875  -4.008  1.00 27.68 ? 162 ASP   A O   1 
ATOM   1299 C  CB  . ASP   A 1 161 ? -17.788 -7.623  -2.744  1.00 27.17 ? 162 ASP   A CB  1 
ATOM   1300 C  CG  . ASP   A 1 161 ? -18.453 -8.993  -2.696  1.00 30.67 ? 162 ASP   A CG  1 
ATOM   1301 O  OD1 . ASP   A 1 161 ? -17.708 -10.021 -2.616  1.00 35.31 ? 162 ASP   A OD1 1 
ATOM   1302 O  OD2 . ASP   A 1 161 ? -19.710 -9.024  -2.711  1.00 35.76 ? 162 ASP   A OD2 1 
ATOM   1303 N  N   . VAL   A 1 162 ? -15.069 -5.589  -2.178  1.00 21.07 ? 163 VAL   A N   1 
ATOM   1304 C  CA  . VAL   A 1 162 ? -14.255 -4.538  -2.755  1.00 22.39 ? 163 VAL   A CA  1 
ATOM   1305 C  C   . VAL   A 1 162 ? -12.757 -4.830  -2.555  1.00 21.55 ? 163 VAL   A C   1 
ATOM   1306 O  O   . VAL   A 1 162 ? -11.898 -4.147  -3.112  1.00 19.73 ? 163 VAL   A O   1 
ATOM   1307 C  CB  . VAL   A 1 162 ? -14.700 -3.178  -2.173  1.00 23.32 ? 163 VAL   A CB  1 
ATOM   1308 C  CG1 . VAL   A 1 162 ? -14.092 -2.907  -0.806  1.00 23.73 ? 163 VAL   A CG1 1 
ATOM   1309 C  CG2 . VAL   A 1 162 ? -14.441 -1.994  -3.095  1.00 26.60 ? 163 VAL   A CG2 1 
ATOM   1310 N  N   . LEU   A 1 163 ? -12.382 -5.830  -1.728  1.00 21.32 ? 164 LEU   A N   1 
ATOM   1311 C  CA  . LEU   A 1 163 ? -10.982 -6.074  -1.401  1.00 18.70 ? 164 LEU   A CA  1 
ATOM   1312 C  C   . LEU   A 1 163 ? -10.112 -6.442  -2.605  1.00 20.31 ? 164 LEU   A C   1 
ATOM   1313 O  O   . LEU   A 1 163 ? -8.931  -6.112  -2.627  1.00 19.56 ? 164 LEU   A O   1 
ATOM   1314 C  CB  . LEU   A 1 163 ? -10.809 -7.100  -0.271  1.00 19.95 ? 164 LEU   A CB  1 
ATOM   1315 C  CG  . LEU   A 1 163 ? -11.493 -6.779  1.064   1.00 18.63 ? 164 LEU   A CG  1 
ATOM   1316 C  CD1 . LEU   A 1 163 ? -11.282 -7.956  2.022   1.00 21.05 ? 164 LEU   A CD1 1 
ATOM   1317 C  CD2 . LEU   A 1 163 ? -11.017 -5.475  1.692   1.00 19.17 ? 164 LEU   A CD2 1 
ATOM   1318 N  N   . ASP   A 1 164 ? -10.692 -7.135  -3.600  1.00 24.58 ? 165 ASP   A N   1 
ATOM   1319 C  CA  . ASP   A 1 164 ? -9.871  -7.447  -4.763  1.00 29.70 ? 165 ASP   A CA  1 
ATOM   1320 C  C   . ASP   A 1 164 ? -9.447  -6.170  -5.515  1.00 28.91 ? 165 ASP   A C   1 
ATOM   1321 O  O   . ASP   A 1 164 ? -8.449  -6.205  -6.244  1.00 33.20 ? 165 ASP   A O   1 
ATOM   1322 C  CB  . ASP   A 1 164 ? -10.548 -8.489  -5.655  1.00 33.89 ? 165 ASP   A CB  1 
ATOM   1323 C  CG  . ASP   A 1 164 ? -11.650 -7.880  -6.493  1.00 41.35 ? 165 ASP   A CG  1 
ATOM   1324 O  OD1 . ASP   A 1 164 ? -12.342 -6.964  -5.981  1.00 47.11 ? 165 ASP   A OD1 1 
ATOM   1325 O  OD2 . ASP   A 1 164 ? -11.816 -8.317  -7.649  1.00 68.48 ? 165 ASP   A OD2 1 
ATOM   1326 N  N   . SER   A 1 165 ? -10.113 -5.034  -5.272  1.00 24.84 ? 166 SER   A N   1 
ATOM   1327 C  CA  . SER   A 1 165 ? -9.724  -3.793  -5.928  1.00 24.03 ? 166 SER   A CA  1 
ATOM   1328 C  C   . SER   A 1 165 ? -8.644  -3.016  -5.165  1.00 22.25 ? 166 SER   A C   1 
ATOM   1329 O  O   . SER   A 1 165 ? -8.132  -2.001  -5.671  1.00 24.20 ? 166 SER   A O   1 
ATOM   1330 C  CB  . SER   A 1 165 ? -10.899 -2.932  -6.231  1.00 26.54 ? 166 SER   A CB  1 
ATOM   1331 O  OG  . SER   A 1 165 ? -11.351 -2.262  -5.068  1.00 30.00 ? 166 SER   A OG  1 
ATOM   1332 N  N   . ILE   A 1 166 ? -8.311  -3.448  -3.926  1.00 18.56 ? 167 ILE   A N   1 
ATOM   1333 C  CA  . ILE   A 1 166 ? -7.268  -2.788  -3.152  1.00 18.19 ? 167 ILE   A CA  1 
ATOM   1334 C  C   . ILE   A 1 166 ? -6.254  -3.810  -2.627  1.00 18.70 ? 167 ILE   A C   1 
ATOM   1335 O  O   . ILE   A 1 166 ? -5.855  -3.815  -1.444  1.00 17.96 ? 167 ILE   A O   1 
ATOM   1336 C  CB  . ILE   A 1 166 ? -7.863  -1.958  -1.973  1.00 19.12 ? 167 ILE   A CB  1 
ATOM   1337 C  CG1 . ILE   A 1 166 ? -8.706  -2.794  -1.010  1.00 19.16 ? 167 ILE   A CG1 1 
ATOM   1338 C  CG2 . ILE   A 1 166 ? -8.632  -0.770  -2.530  1.00 21.58 ? 167 ILE   A CG2 1 
ATOM   1339 C  CD1 . ILE   A 1 166 ? -8.708  -2.237  0.416   1.00 21.87 ? 167 ILE   A CD1 1 
ATOM   1340 N  N   . LYS   A 1 167 ? -5.867  -4.755  -3.481  1.00 19.72 ? 168 LYS   A N   1 
ATOM   1341 C  CA  . LYS   A 1 167 ? -5.114  -5.902  -3.022  1.00 18.20 ? 168 LYS   A CA  1 
ATOM   1342 C  C   . LYS   A 1 167 ? -3.779  -5.488  -2.394  1.00 18.83 ? 168 LYS   A C   1 
ATOM   1343 O  O   . LYS   A 1 167 ? -3.352  -6.080  -1.399  1.00 18.00 ? 168 LYS   A O   1 
ATOM   1344 C  CB  . LYS   A 1 167 ? -4.864  -6.825  -4.220  1.00 19.39 ? 168 LYS   A CB  1 
ATOM   1345 C  CG  . LYS   A 1 167 ? -4.012  -8.034  -3.841  1.00 21.10 ? 168 LYS   A CG  1 
ATOM   1346 C  CD  . LYS   A 1 167 ? -3.882  -9.081  -4.981  1.00 27.12 ? 168 LYS   A CD  1 
ATOM   1347 N  N   . THR   A 1 168 ? -3.120  -4.459  -2.963  1.00 17.99 ? 169 THR   A N   1 
ATOM   1348 C  CA  . THR   A 1 168 ? -1.763  -4.127  -2.565  1.00 16.79 ? 169 THR   A CA  1 
ATOM   1349 C  C   . THR   A 1 168 ? -1.672  -2.758  -1.883  1.00 16.58 ? 169 THR   A C   1 
ATOM   1350 O  O   . THR   A 1 168 ? -2.549  -1.908  -2.008  1.00 17.94 ? 169 THR   A O   1 
ATOM   1351 C  CB  . THR   A 1 168 ? -0.820  -4.205  -3.777  1.00 21.47 ? 169 THR   A CB  1 
ATOM   1352 O  OG1 . THR   A 1 168 ? -1.408  -3.459  -4.848  1.00 22.36 ? 169 THR   A OG1 1 
ATOM   1353 C  CG2 . THR   A 1 168 ? -0.521  -5.617  -4.220  1.00 21.48 ? 169 THR   A CG2 1 
ATOM   1354 N  N   . LYS   A 1 169 ? -0.618  -2.610  -1.114  1.00 18.65 ? 170 LYS   A N   1 
ATOM   1355 C  CA  . LYS   A 1 169 ? -0.311  -1.435  -0.323  1.00 19.35 ? 170 LYS   A CA  1 
ATOM   1356 C  C   . LYS   A 1 169 ? -0.417  -0.169  -1.139  1.00 21.44 ? 170 LYS   A C   1 
ATOM   1357 O  O   . LYS   A 1 169 ? 0.162   -0.108  -2.227  1.00 23.46 ? 170 LYS   A O   1 
ATOM   1358 C  CB  . LYS   A 1 169 ? 1.099   -1.571  0.230   1.00 18.57 ? 170 LYS   A CB  1 
ATOM   1359 C  CG  . LYS   A 1 169 ? 1.552   -0.403  1.097   1.00 20.59 ? 170 LYS   A CG  1 
ATOM   1360 C  CD  . LYS   A 1 169 ? 2.891   -0.608  1.759   1.00 22.94 ? 170 LYS   A CD  1 
ATOM   1361 C  CE  . LYS   A 1 169 ? 3.989   -0.837  0.733   1.00 27.01 ? 170 LYS   A CE  1 
ATOM   1362 N  NZ  . LYS   A 1 169 ? 5.226   -1.396  1.330   1.00 35.29 ? 170 LYS   A NZ  1 
ATOM   1363 N  N   . GLY   A 1 170 ? -1.214  0.767   -0.623  1.00 21.93 ? 171 GLY   A N   1 
ATOM   1364 C  CA  . GLY   A 1 170 ? -1.364  2.108   -1.191  1.00 20.80 ? 171 GLY   A CA  1 
ATOM   1365 C  C   . GLY   A 1 170 ? -2.531  2.218   -2.172  1.00 23.04 ? 171 GLY   A C   1 
ATOM   1366 O  O   . GLY   A 1 170 ? -2.863  3.338   -2.583  1.00 25.14 ? 171 GLY   A O   1 
ATOM   1367 N  N   . LYS   A 1 171 ? -3.156  1.080   -2.536  1.00 19.00 ? 172 LYS   A N   1 
ATOM   1368 C  CA  . LYS   A 1 171 ? -4.366  1.117   -3.339  1.00 21.37 ? 172 LYS   A CA  1 
ATOM   1369 C  C   . LYS   A 1 171 ? -5.563  1.620   -2.539  1.00 21.23 ? 172 LYS   A C   1 
ATOM   1370 O  O   . LYS   A 1 171 ? -5.732  1.237   -1.380  1.00 22.58 ? 172 LYS   A O   1 
ATOM   1371 C  CB  . LYS   A 1 171 ? -4.642  -0.221  -4.038  1.00 23.20 ? 172 LYS   A CB  1 
ATOM   1372 C  CG  . LYS   A 1 171 ? -3.608  -0.572  -5.090  1.00 25.69 ? 172 LYS   A CG  1 
ATOM   1373 C  CD  . LYS   A 1 171 ? -4.020  -1.654  -6.090  1.00 33.87 ? 172 LYS   A CD  1 
ATOM   1374 C  CE  . LYS   A 1 171 ? -5.060  -1.201  -7.106  1.00 40.51 ? 172 LYS   A CE  1 
ATOM   1375 N  NZ  . LYS   A 1 171 ? -5.673  -2.336  -7.858  1.00 39.50 ? 172 LYS   A NZ  1 
ATOM   1376 N  N   . SER   A 1 172 ? -6.432  2.435   -3.152  1.00 19.28 ? 173 SER   A N   1 
ATOM   1377 C  CA  . SER   A 1 172 ? -7.700  2.853   -2.581  1.00 20.02 ? 173 SER   A CA  1 
ATOM   1378 C  C   . SER   A 1 172 ? -8.824  2.727   -3.605  1.00 19.95 ? 173 SER   A C   1 
ATOM   1379 O  O   . SER   A 1 172 ? -8.613  2.634   -4.839  1.00 19.74 ? 173 SER   A O   1 
ATOM   1380 C  CB  . SER   A 1 172 ? -7.628  4.280   -2.082  1.00 22.05 ? 173 SER   A CB  1 
ATOM   1381 O  OG  . SER   A 1 172 ? -7.288  5.145   -3.155  1.00 24.69 ? 173 SER   A OG  1 
ATOM   1382 N  N   . ALA   A 1 173 ? -10.040 2.738   -3.086  1.00 21.64 ? 174 ALA   A N   1 
ATOM   1383 C  CA  . ALA   A 1 173 ? -11.245 2.632   -3.887  1.00 23.60 ? 174 ALA   A CA  1 
ATOM   1384 C  C   . ALA   A 1 173 ? -12.360 3.440   -3.233  1.00 23.25 ? 174 ALA   A C   1 
ATOM   1385 O  O   . ALA   A 1 173 ? -12.506 3.461   -2.001  1.00 20.35 ? 174 ALA   A O   1 
ATOM   1386 C  CB  . ALA   A 1 173 ? -11.635 1.201   -4.072  1.00 23.05 ? 174 ALA   A CB  1 
ATOM   1387 N  N   . ASP   A 1 174 ? -13.197 4.068   -4.056  1.00 24.14 ? 175 ASP   A N   1 
ATOM   1388 C  CA  . ASP   A 1 174 ? -14.378 4.742   -3.544  1.00 25.91 ? 175 ASP   A CA  1 
ATOM   1389 C  C   . ASP   A 1 174 ? -15.239 3.745   -2.779  1.00 27.36 ? 175 ASP   A C   1 
ATOM   1390 O  O   . ASP   A 1 174 ? -15.430 2.599   -3.207  1.00 24.63 ? 175 ASP   A O   1 
ATOM   1391 C  CB  . ASP   A 1 174 ? -15.211 5.356   -4.684  1.00 29.84 ? 175 ASP   A CB  1 
ATOM   1392 C  CG  . ASP   A 1 174 ? -14.393 6.338   -5.487  1.00 39.16 ? 175 ASP   A CG  1 
ATOM   1393 O  OD1 . ASP   A 1 174 ? -13.749 7.204   -4.855  1.00 37.82 ? 175 ASP   A OD1 1 
ATOM   1394 O  OD2 . ASP   A 1 174 ? -14.379 6.211   -6.739  1.00 42.24 ? 175 ASP   A OD2 1 
ATOM   1395 N  N   . PHE   A 1 175 ? -15.796 4.235   -1.652  1.00 22.65 ? 176 PHE   A N   1 
ATOM   1396 C  CA  . PHE   A 1 175 ? -16.528 3.325   -0.772  1.00 22.60 ? 176 PHE   A CA  1 
ATOM   1397 C  C   . PHE   A 1 175 ? -17.597 4.105   -0.030  1.00 21.75 ? 176 PHE   A C   1 
ATOM   1398 O  O   . PHE   A 1 175 ? -17.457 4.352   1.160   1.00 23.19 ? 176 PHE   A O   1 
ATOM   1399 C  CB  . PHE   A 1 175 ? -15.577 2.550   0.161   1.00 21.58 ? 176 PHE   A CB  1 
ATOM   1400 C  CG  . PHE   A 1 175 ? -16.176 1.270   0.683   1.00 21.28 ? 176 PHE   A CG  1 
ATOM   1401 C  CD1 . PHE   A 1 175 ? -16.485 0.224   -0.164  1.00 21.98 ? 176 PHE   A CD1 1 
ATOM   1402 C  CD2 . PHE   A 1 175 ? -16.467 1.117   2.037   1.00 20.61 ? 176 PHE   A CD2 1 
ATOM   1403 C  CE1 . PHE   A 1 175 ? -17.056 -0.947  0.329   1.00 23.59 ? 176 PHE   A CE1 1 
ATOM   1404 C  CE2 . PHE   A 1 175 ? -17.025 -0.043  2.537   1.00 20.66 ? 176 PHE   A CE2 1 
ATOM   1405 C  CZ  . PHE   A 1 175 ? -17.324 -1.079  1.675   1.00 22.81 ? 176 PHE   A CZ  1 
ATOM   1406 N  N   . THR   A 1 176 ? -18.664 4.484   -0.739  1.00 20.78 ? 177 THR   A N   1 
ATOM   1407 C  CA  . THR   A 1 176 ? -19.689 5.350   -0.214  1.00 20.96 ? 177 THR   A CA  1 
ATOM   1408 C  C   . THR   A 1 176 ? -20.855 4.486   0.228   1.00 18.49 ? 177 THR   A C   1 
ATOM   1409 O  O   . THR   A 1 176 ? -21.004 3.344   -0.215  1.00 21.49 ? 177 THR   A O   1 
ATOM   1410 C  CB  . THR   A 1 176 ? -20.074 6.443   -1.230  1.00 24.48 ? 177 THR   A CB  1 
ATOM   1411 O  OG1 . THR   A 1 176 ? -20.418 5.773   -2.438  1.00 27.41 ? 177 THR   A OG1 1 
ATOM   1412 C  CG2 . THR   A 1 176 ? -18.954 7.413   -1.505  1.00 28.82 ? 177 THR   A CG2 1 
ATOM   1413 N  N   . ASN   A 1 177 ? -21.640 5.056   1.151   1.00 18.45 ? 178 ASN   A N   1 
ATOM   1414 C  CA  . ASN   A 1 177 ? -22.929 4.560   1.577   1.00 19.31 ? 178 ASN   A CA  1 
ATOM   1415 C  C   . ASN   A 1 177 ? -22.798 3.238   2.345   1.00 20.44 ? 178 ASN   A C   1 
ATOM   1416 O  O   . ASN   A 1 177 ? -23.758 2.503   2.420   1.00 22.78 ? 178 ASN   A O   1 
ATOM   1417 C  CB  . ASN   A 1 177 ? -23.905 4.472   0.396   1.00 19.94 ? 178 ASN   A CB  1 
ATOM   1418 C  CG  . ASN   A 1 177 ? -24.121 5.851   -0.197  1.00 22.60 ? 178 ASN   A CG  1 
ATOM   1419 O  OD1 . ASN   A 1 177 ? -24.767 6.677   0.419   1.00 24.43 ? 178 ASN   A OD1 1 
ATOM   1420 N  ND2 . ASN   A 1 177 ? -23.573 6.096   -1.377  1.00 19.98 ? 178 ASN   A ND2 1 
ATOM   1421 N  N   . PHE   A 1 178 ? -21.638 2.978   2.949   1.00 18.72 ? 179 PHE   A N   1 
ATOM   1422 C  CA  . PHE   A 1 178 ? -21.497 1.755   3.747   1.00 19.30 ? 179 PHE   A CA  1 
ATOM   1423 C  C   . PHE   A 1 178 ? -21.995 2.033   5.158   1.00 17.30 ? 179 PHE   A C   1 
ATOM   1424 O  O   . PHE   A 1 178 ? -21.558 3.009   5.759   1.00 20.22 ? 179 PHE   A O   1 
ATOM   1425 C  CB  . PHE   A 1 178 ? -20.041 1.303   3.849   1.00 18.59 ? 179 PHE   A CB  1 
ATOM   1426 C  CG  . PHE   A 1 178 ? -19.901 0.037   4.674   1.00 18.79 ? 179 PHE   A CG  1 
ATOM   1427 C  CD1 . PHE   A 1 178 ? -20.381 -1.176  4.189   1.00 19.73 ? 179 PHE   A CD1 1 
ATOM   1428 C  CD2 . PHE   A 1 178 ? -19.495 0.108   6.008   1.00 17.33 ? 179 PHE   A CD2 1 
ATOM   1429 C  CE1 . PHE   A 1 178 ? -20.297 -2.331  4.959   1.00 19.71 ? 179 PHE   A CE1 1 
ATOM   1430 C  CE2 . PHE   A 1 178 ? -19.479 -1.039  6.794   1.00 18.12 ? 179 PHE   A CE2 1 
ATOM   1431 C  CZ  . PHE   A 1 178 ? -19.875 -2.247  6.282   1.00 19.06 ? 179 PHE   A CZ  1 
ATOM   1432 N  N   . ASP   A 1 179 ? -22.820 1.141   5.712   1.00 18.93 ? 180 ASP   A N   1 
ATOM   1433 C  CA  . ASP   A 1 179 ? -23.473 1.387   6.984   1.00 17.99 ? 180 ASP   A CA  1 
ATOM   1434 C  C   . ASP   A 1 179 ? -22.826 0.548   8.063   1.00 17.95 ? 180 ASP   A C   1 
ATOM   1435 O  O   . ASP   A 1 179 ? -23.013 -0.684  8.074   1.00 18.31 ? 180 ASP   A O   1 
ATOM   1436 C  CB  . ASP   A 1 179 ? -24.950 1.019   6.885   1.00 20.19 ? 180 ASP   A CB  1 
ATOM   1437 C  CG  . ASP   A 1 179 ? -25.760 1.486   8.081   1.00 24.72 ? 180 ASP   A CG  1 
ATOM   1438 O  OD1 . ASP   A 1 179 ? -25.177 1.693   9.162   1.00 21.37 ? 180 ASP   A OD1 1 
ATOM   1439 O  OD2 . ASP   A 1 179 ? -26.970 1.692   7.903   1.00 29.40 ? 180 ASP   A OD2 1 
ATOM   1440 N  N   . PRO   A 1 180 ? -22.036 1.146   9.003   1.00 16.12 ? 181 PRO   A N   1 
ATOM   1441 C  CA  . PRO   A 1 180 ? -21.311 0.315   9.974   1.00 17.24 ? 181 PRO   A CA  1 
ATOM   1442 C  C   . PRO   A 1 180 ? -22.221 -0.318  11.037  1.00 19.08 ? 181 PRO   A C   1 
ATOM   1443 O  O   . PRO   A 1 180 ? -21.799 -1.234  11.728  1.00 16.13 ? 181 PRO   A O   1 
ATOM   1444 C  CB  . PRO   A 1 180 ? -20.292 1.310   10.588  1.00 19.61 ? 181 PRO   A CB  1 
ATOM   1445 C  CG  . PRO   A 1 180 ? -20.970 2.670   10.467  1.00 16.86 ? 181 PRO   A CG  1 
ATOM   1446 C  CD  . PRO   A 1 180 ? -21.681 2.562   9.118   1.00 16.57 ? 181 PRO   A CD  1 
ATOM   1447 N  N   . ARG   A 1 181 ? -23.510 0.051   11.057  1.00 17.10 ? 182 ARG   A N   1 
ATOM   1448 C  CA  . ARG   A 1 181 ? -24.443 -0.586  12.009  1.00 15.68 ? 182 ARG   A CA  1 
ATOM   1449 C  C   . ARG   A 1 181 ? -24.599 -2.072  11.686  1.00 17.65 ? 182 ARG   A C   1 
ATOM   1450 O  O   . ARG   A 1 181 ? -24.965 -2.867  12.541  1.00 18.53 ? 182 ARG   A O   1 
ATOM   1451 C  CB  . ARG   A 1 181 ? -25.827 0.066   11.960  1.00 17.38 ? 182 ARG   A CB  1 
ATOM   1452 C  CG  . ARG   A 1 181 ? -25.815 1.518   12.439  1.00 18.96 ? 182 ARG   A CG  1 
ATOM   1453 C  CD  . ARG   A 1 181 ? -27.149 2.250   12.376  1.00 19.55 ? 182 ARG   A CD  1 
ATOM   1454 N  NE  . ARG   A 1 181 ? -27.496 2.333   10.964  1.00 22.28 ? 182 ARG   A NE  1 
ATOM   1455 C  CZ  . ARG   A 1 181 ? -28.585 2.979   10.566  1.00 29.35 ? 182 ARG   A CZ  1 
ATOM   1456 N  NH1 . ARG   A 1 181 ? -29.341 3.569   11.475  1.00 29.12 ? 182 ARG   A NH1 1 
ATOM   1457 N  NH2 . ARG   A 1 181 ? -28.908 3.029   9.287   1.00 26.37 ? 182 ARG   A NH2 1 
ATOM   1458 N  N   . GLY   A 1 182 ? -24.340 -2.467  10.439  1.00 16.53 ? 183 GLY   A N   1 
ATOM   1459 C  CA  . GLY   A 1 182 ? -24.444 -3.877  10.078  1.00 17.84 ? 183 GLY   A CA  1 
ATOM   1460 C  C   . GLY   A 1 182 ? -23.297 -4.749  10.578  1.00 19.81 ? 183 GLY   A C   1 
ATOM   1461 O  O   . GLY   A 1 182 ? -23.318 -5.944  10.286  1.00 22.33 ? 183 GLY   A O   1 
ATOM   1462 N  N   . LEU   A 1 183 ? -22.308 -4.141  11.261  1.00 16.92 ? 184 LEU   A N   1 
ATOM   1463 C  CA  . LEU   A 1 183 ? -21.174 -4.889  11.814  1.00 17.27 ? 184 LEU   A CA  1 
ATOM   1464 C  C   . LEU   A 1 183 ? -21.313 -5.073  13.330  1.00 17.26 ? 184 LEU   A C   1 
ATOM   1465 O  O   . LEU   A 1 183 ? -20.413 -5.627  13.946  1.00 18.51 ? 184 LEU   A O   1 
ATOM   1466 C  CB  . LEU   A 1 183 ? -19.870 -4.149  11.494  1.00 18.64 ? 184 LEU   A CB  1 
ATOM   1467 C  CG  . LEU   A 1 183 ? -19.566 -3.993  9.996   1.00 19.09 ? 184 LEU   A CG  1 
ATOM   1468 C  CD1 . LEU   A 1 183 ? -18.290 -3.250  9.763   1.00 21.11 ? 184 LEU   A CD1 1 
ATOM   1469 C  CD2 . LEU   A 1 183 ? -19.536 -5.335  9.276   1.00 23.18 ? 184 LEU   A CD2 1 
ATOM   1470 N  N   . LEU   A 1 184 ? -22.392 -4.597  13.945  1.00 15.97 ? 185 LEU   A N   1 
ATOM   1471 C  CA  . LEU   A 1 184 ? -22.587 -4.593  15.411  1.00 15.46 ? 185 LEU   A CA  1 
ATOM   1472 C  C   . LEU   A 1 184 ? -23.275 -5.896  15.838  1.00 18.76 ? 185 LEU   A C   1 
ATOM   1473 O  O   . LEU   A 1 184 ? -24.183 -6.401  15.151  1.00 22.82 ? 185 LEU   A O   1 
ATOM   1474 C  CB  . LEU   A 1 184 ? -23.408 -3.395  15.915  1.00 17.01 ? 185 LEU   A CB  1 
ATOM   1475 C  CG  . LEU   A 1 184 ? -22.801 -2.038  15.609  1.00 15.68 ? 185 LEU   A CG  1 
ATOM   1476 C  CD1 . LEU   A 1 184 ? -23.644 -0.846  16.007  1.00 17.51 ? 185 LEU   A CD1 1 
ATOM   1477 C  CD2 . LEU   A 1 184 ? -21.358 -1.901  16.085  1.00 16.67 ? 185 LEU   A CD2 1 
ATOM   1478 N  N   . PRO   A 1 185 ? -22.920 -6.459  17.002  1.00 17.05 ? 186 PRO   A N   1 
ATOM   1479 C  CA  . PRO   A 1 185 ? -23.671 -7.583  17.543  1.00 17.94 ? 186 PRO   A CA  1 
ATOM   1480 C  C   . PRO   A 1 185 ? -24.978 -7.060  18.139  1.00 17.89 ? 186 PRO   A C   1 
ATOM   1481 O  O   . PRO   A 1 185 ? -25.190 -5.863  18.264  1.00 17.62 ? 186 PRO   A O   1 
ATOM   1482 C  CB  . PRO   A 1 185 ? -22.670 -8.134  18.589  1.00 16.82 ? 186 PRO   A CB  1 
ATOM   1483 C  CG  . PRO   A 1 185 ? -21.983 -6.888  19.081  1.00 15.26 ? 186 PRO   A CG  1 
ATOM   1484 C  CD  . PRO   A 1 185 ? -21.747 -6.054  17.808  1.00 15.01 ? 186 PRO   A CD  1 
ATOM   1485 N  N   . GLU   A 1 186 ? -25.794 -7.959  18.661  1.00 19.63 ? 187 GLU   A N   1 
ATOM   1486 C  CA  . GLU   A 1 186 ? -27.052 -7.579  19.257  1.00 18.56 ? 187 GLU   A CA  1 
ATOM   1487 C  C   . GLU   A 1 186 ? -26.833 -6.819  20.569  1.00 19.14 ? 187 GLU   A C   1 
ATOM   1488 O  O   . GLU   A 1 186 ? -27.497 -5.827  20.824  1.00 20.43 ? 187 GLU   A O   1 
ATOM   1489 C  CB  . GLU   A 1 186 ? -27.819 -8.896  19.455  1.00 23.05 ? 187 GLU   A CB  1 
ATOM   1490 C  CG  . GLU   A 1 186 ? -28.989 -8.790  20.390  1.00 28.50 ? 187 GLU   A CG  1 
ATOM   1491 C  CD  . GLU   A 1 186 ? -29.650 -10.148 20.657  1.00 30.47 ? 187 GLU   A CD  1 
ATOM   1492 O  OE1 . GLU   A 1 186 ? -29.461 -11.075 19.839  1.00 30.21 ? 187 GLU   A OE1 1 
ATOM   1493 O  OE2 . GLU   A 1 186 ? -30.373 -10.250 21.683  1.00 38.70 ? 187 GLU   A OE2 1 
ATOM   1494 N  N   . SER   A 1 187 ? -25.916 -7.293  21.427  1.00 17.90 ? 188 SER   A N   1 
ATOM   1495 C  CA  . SER   A 1 187 ? -25.740 -6.721  22.758  1.00 18.80 ? 188 SER   A CA  1 
ATOM   1496 C  C   . SER   A 1 187 ? -24.599 -5.700  22.743  1.00 17.49 ? 188 SER   A C   1 
ATOM   1497 O  O   . SER   A 1 187 ? -23.584 -5.973  22.100  1.00 17.72 ? 188 SER   A O   1 
ATOM   1498 C  CB  . SER   A 1 187 ? -25.385 -7.798  23.735  1.00 19.59 ? 188 SER   A CB  1 
ATOM   1499 O  OG  . SER   A 1 187 ? -25.134 -7.224  25.013  1.00 20.71 ? 188 SER   A OG  1 
ATOM   1500 N  N   . LEU   A 1 188 ? -24.744 -4.603  23.481  1.00 16.18 ? 189 LEU   A N   1 
ATOM   1501 C  CA  . LEU   A 1 188 ? -23.667 -3.625  23.680  1.00 16.96 ? 189 LEU   A CA  1 
ATOM   1502 C  C   . LEU   A 1 188 ? -23.022 -3.734  25.073  1.00 16.19 ? 189 LEU   A C   1 
ATOM   1503 O  O   . LEU   A 1 188 ? -22.346 -2.774  25.480  1.00 18.22 ? 189 LEU   A O   1 
ATOM   1504 C  CB  . LEU   A 1 188 ? -24.178 -2.197  23.438  1.00 18.02 ? 189 LEU   A CB  1 
ATOM   1505 C  CG  . LEU   A 1 188 ? -24.693 -1.939  22.035  1.00 19.87 ? 189 LEU   A CG  1 
ATOM   1506 C  CD1 . LEU   A 1 188 ? -25.203 -0.507  21.911  1.00 22.16 ? 189 LEU   A CD1 1 
ATOM   1507 C  CD2 . LEU   A 1 188 ? -23.630 -2.253  20.965  1.00 22.43 ? 189 LEU   A CD2 1 
ATOM   1508 N  N   . ASP   A 1 189 ? -23.155 -4.876  25.771  1.00 16.87 ? 190 ASP   A N   1 
ATOM   1509 C  CA  . ASP   A 1 189 ? -22.391 -5.129  26.992  1.00 17.53 ? 190 ASP   A CA  1 
ATOM   1510 C  C   . ASP   A 1 189 ? -20.890 -5.078  26.662  1.00 15.47 ? 190 ASP   A C   1 
ATOM   1511 O  O   . ASP   A 1 189 ? -20.468 -5.548  25.588  1.00 15.52 ? 190 ASP   A O   1 
ATOM   1512 C  CB  . ASP   A 1 189 ? -22.781 -6.445  27.683  1.00 18.20 ? 190 ASP   A CB  1 
ATOM   1513 C  CG  . ASP   A 1 189 ? -24.179 -6.503  28.307  1.00 22.03 ? 190 ASP   A CG  1 
ATOM   1514 O  OD1 . ASP   A 1 189 ? -24.789 -5.440  28.483  1.00 26.89 ? 190 ASP   A OD1 1 
ATOM   1515 O  OD2 . ASP   A 1 189 ? -24.615 -7.626  28.600  1.00 29.35 ? 190 ASP   A OD2 1 
ATOM   1516 N  N   . TYR   A 1 190 ? -20.105 -4.438  27.553  1.00 14.81 ? 191 TYR   A N   1 
ATOM   1517 C  CA  . TYR   A 1 190 ? -18.702 -4.191  27.226  1.00 13.46 ? 191 TYR   A CA  1 
ATOM   1518 C  C   . TYR   A 1 190 ? -17.784 -4.255  28.446  1.00 14.61 ? 191 TYR   A C   1 
ATOM   1519 O  O   . TYR   A 1 190 ? -18.216 -4.121  29.592  1.00 14.97 ? 191 TYR   A O   1 
ATOM   1520 C  CB  . TYR   A 1 190 ? -18.585 -2.811  26.562  1.00 15.05 ? 191 TYR   A CB  1 
ATOM   1521 C  CG  . TYR   A 1 190 ? -18.980 -1.667  27.461  1.00 14.32 ? 191 TYR   A CG  1 
ATOM   1522 C  CD1 . TYR   A 1 190 ? -18.050 -1.045  28.307  1.00 15.25 ? 191 TYR   A CD1 1 
ATOM   1523 C  CD2 . TYR   A 1 190 ? -20.258 -1.123  27.398  1.00 14.93 ? 191 TYR   A CD2 1 
ATOM   1524 C  CE1 . TYR   A 1 190 ? -18.409 -0.007  29.155  1.00 15.58 ? 191 TYR   A CE1 1 
ATOM   1525 C  CE2 . TYR   A 1 190 ? -20.615 -0.046  28.209  1.00 16.79 ? 191 TYR   A CE2 1 
ATOM   1526 C  CZ  . TYR   A 1 190 ? -19.692 0.523   29.080  1.00 17.21 ? 191 TYR   A CZ  1 
ATOM   1527 O  OH  . TYR   A 1 190 ? -20.107 1.548   29.894  1.00 17.73 ? 191 TYR   A OH  1 
ATOM   1528 N  N   . TRP   A 1 191 ? -16.493 -4.437  28.177  1.00 14.32 ? 192 TRP   A N   1 
ATOM   1529 C  CA  . TRP   A 1 191 ? -15.411 -4.167  29.107  1.00 12.53 ? 192 TRP   A CA  1 
ATOM   1530 C  C   . TRP   A 1 191 ? -14.750 -2.862  28.693  1.00 12.13 ? 192 TRP   A C   1 
ATOM   1531 O  O   . TRP   A 1 191 ? -14.703 -2.523  27.509  1.00 13.45 ? 192 TRP   A O   1 
ATOM   1532 C  CB  . TRP   A 1 191 ? -14.376 -5.296  29.082  1.00 13.00 ? 192 TRP   A CB  1 
ATOM   1533 C  CG  . TRP   A 1 191 ? -14.910 -6.634  29.498  1.00 13.31 ? 192 TRP   A CG  1 
ATOM   1534 C  CD1 . TRP   A 1 191 ? -15.123 -7.071  30.779  1.00 14.80 ? 192 TRP   A CD1 1 
ATOM   1535 C  CD2 . TRP   A 1 191 ? -15.162 -7.767  28.654  1.00 13.57 ? 192 TRP   A CD2 1 
ATOM   1536 N  NE1 . TRP   A 1 191 ? -15.503 -8.389  30.779  1.00 16.50 ? 192 TRP   A NE1 1 
ATOM   1537 C  CE2 . TRP   A 1 191 ? -15.560 -8.833  29.492  1.00 15.46 ? 192 TRP   A CE2 1 
ATOM   1538 C  CE3 . TRP   A 1 191 ? -15.064 -7.981  27.262  1.00 13.83 ? 192 TRP   A CE3 1 
ATOM   1539 C  CZ2 . TRP   A 1 191 ? -15.879 -10.095 28.981  1.00 15.13 ? 192 TRP   A CZ2 1 
ATOM   1540 C  CZ3 . TRP   A 1 191 ? -15.399 -9.230  26.777  1.00 15.16 ? 192 TRP   A CZ3 1 
ATOM   1541 C  CH2 . TRP   A 1 191 ? -15.789 -10.257 27.625  1.00 14.81 ? 192 TRP   A CH2 1 
ATOM   1542 N  N   . THR   A 1 192 ? -14.121 -2.169  29.645  1.00 12.37 ? 193 THR   A N   1 
ATOM   1543 C  CA  . THR   A 1 192 ? -13.442 -0.920  29.311  1.00 12.44 ? 193 THR   A CA  1 
ATOM   1544 C  C   . THR   A 1 192 ? -12.194 -0.740  30.166  1.00 12.83 ? 193 THR   A C   1 
ATOM   1545 O  O   . THR   A 1 192 ? -12.157 -1.126  31.344  1.00 13.85 ? 193 THR   A O   1 
ATOM   1546 C  CB  . THR   A 1 192 ? -14.378 0.294   29.382  1.00 12.64 ? 193 THR   A CB  1 
ATOM   1547 O  OG1 . THR   A 1 192 ? -13.687 1.486   29.011  1.00 14.78 ? 193 THR   A OG1 1 
ATOM   1548 C  CG2 . THR   A 1 192 ? -14.924 0.594   30.775  1.00 14.10 ? 193 THR   A CG2 1 
ATOM   1549 N  N   . TYR   A 1 193 ? -11.163 -0.147  29.562  1.00 13.22 ? 194 TYR   A N   1 
ATOM   1550 C  CA  . TYR   A 1 193 ? -9.911  0.111   30.276  1.00 11.82 ? 194 TYR   A CA  1 
ATOM   1551 C  C   . TYR   A 1 193 ? -9.144  1.188   29.506  1.00 12.62 ? 194 TYR   A C   1 
ATOM   1552 O  O   . TYR   A 1 193 ? -9.388  1.373   28.314  1.00 13.60 ? 194 TYR   A O   1 
ATOM   1553 C  CB  . TYR   A 1 193 ? -9.065  -1.176  30.452  1.00 12.91 ? 194 TYR   A CB  1 
ATOM   1554 C  CG  . TYR   A 1 193 ? -8.374  -1.599  29.178  1.00 13.35 ? 194 TYR   A CG  1 
ATOM   1555 C  CD1 . TYR   A 1 193 ? -9.051  -2.323  28.202  1.00 12.52 ? 194 TYR   A CD1 1 
ATOM   1556 C  CD2 . TYR   A 1 193 ? -7.029  -1.294  28.978  1.00 12.83 ? 194 TYR   A CD2 1 
ATOM   1557 C  CE1 . TYR   A 1 193 ? -8.438  -2.658  27.011  1.00 12.04 ? 194 TYR   A CE1 1 
ATOM   1558 C  CE2 . TYR   A 1 193 ? -6.399  -1.590  27.774  1.00 13.59 ? 194 TYR   A CE2 1 
ATOM   1559 C  CZ  . TYR   A 1 193 ? -7.099  -2.338  26.846  1.00 12.01 ? 194 TYR   A CZ  1 
ATOM   1560 O  OH  . TYR   A 1 193 ? -6.497  -2.644  25.671  1.00 12.83 ? 194 TYR   A OH  1 
ATOM   1561 N  N   . PRO   A 1 194 ? -8.176  1.877   30.133  1.00 12.41 ? 195 PRO   A N   1 
ATOM   1562 C  CA  . PRO   A 1 194 ? -7.363  2.892   29.472  1.00 13.53 ? 195 PRO   A CA  1 
ATOM   1563 C  C   . PRO   A 1 194 ? -6.142  2.253   28.827  1.00 12.41 ? 195 PRO   A C   1 
ATOM   1564 O  O   . PRO   A 1 194 ? -5.453  1.481   29.499  1.00 13.74 ? 195 PRO   A O   1 
ATOM   1565 C  CB  . PRO   A 1 194 ? -6.875  3.823   30.632  1.00 13.44 ? 195 PRO   A CB  1 
ATOM   1566 C  CG  . PRO   A 1 194 ? -6.898  2.917   31.861  1.00 13.84 ? 195 PRO   A CG  1 
ATOM   1567 C  CD  . PRO   A 1 194 ? -7.960  1.850   31.603  1.00 12.34 ? 195 PRO   A CD  1 
ATOM   1568 N  N   . GLY   A 1 195 ? -5.931  2.562   27.532  1.00 11.85 ? 196 GLY   A N   1 
ATOM   1569 C  CA  . GLY   A 1 195 ? -4.791  1.948   26.856  1.00 13.84 ? 196 GLY   A CA  1 
ATOM   1570 C  C   . GLY   A 1 195 ? -4.285  2.799   25.707  1.00 12.46 ? 196 GLY   A C   1 
ATOM   1571 O  O   . GLY   A 1 195 ? -4.200  4.014   25.837  1.00 11.61 ? 196 GLY   A O   1 
ATOM   1572 N  N   . SER   A 1 196 ? -3.890  2.137   24.621  1.00 11.63 ? 197 SER   A N   1 
ATOM   1573 C  CA  . SER   A 1 196 ? -3.074  2.762   23.584  1.00 11.38 ? 197 SER   A CA  1 
ATOM   1574 C  C   . SER   A 1 196 ? -3.547  2.373   22.198  1.00 11.61 ? 197 SER   A C   1 
ATOM   1575 O  O   . SER   A 1 196 ? -4.279  1.380   22.047  1.00 12.46 ? 197 SER   A O   1 
ATOM   1576 C  CB  . SER   A 1 196 ? -1.608  2.380   23.733  1.00 12.14 ? 197 SER   A CB  1 
ATOM   1577 O  OG  . SER   A 1 196 ? -1.387  1.006   23.403  1.00 12.80 ? 197 SER   A OG  1 
ATOM   1578 N  N   . LEU   A 1 197 ? -3.003  3.063   21.187  1.00 12.07 ? 198 LEU   A N   1 
ATOM   1579 C  CA  . LEU   A 1 197 ? -3.018  2.515   19.833  1.00 12.10 ? 198 LEU   A CA  1 
ATOM   1580 C  C   . LEU   A 1 197 ? -2.269  1.181   19.869  1.00 12.59 ? 198 LEU   A C   1 
ATOM   1581 O  O   . LEU   A 1 197 ? -1.300  1.034   20.665  1.00 12.49 ? 198 LEU   A O   1 
ATOM   1582 C  CB  . LEU   A 1 197 ? -2.286  3.472   18.884  1.00 15.39 ? 198 LEU   A CB  1 
ATOM   1583 C  CG  . LEU   A 1 197 ? -2.822  4.890   18.778  1.00 15.93 ? 198 LEU   A CG  1 
ATOM   1584 C  CD1 . LEU   A 1 197 ? -1.998  5.748   17.798  1.00 18.58 ? 198 LEU   A CD1 1 
ATOM   1585 C  CD2 . LEU   A 1 197 ? -4.250  4.882   18.305  1.00 18.20 ? 198 LEU   A CD2 1 
ATOM   1586 N  N   . THR   A 1 198 ? -2.618  0.249   18.975  1.00 11.70 ? 199 THR   A N   1 
ATOM   1587 C  CA  . THR   A 1 198 ? -1.930  -1.024  18.938  1.00 13.45 ? 199 THR   A CA  1 
ATOM   1588 C  C   . THR   A 1 198 ? -0.925  -1.108  17.787  1.00 12.79 ? 199 THR   A C   1 
ATOM   1589 O  O   . THR   A 1 198 ? -0.346  -2.173  17.640  1.00 15.25 ? 199 THR   A O   1 
ATOM   1590 C  CB  . THR   A 1 198 ? -2.900  -2.210  18.882  1.00 13.32 ? 199 THR   A CB  1 
ATOM   1591 O  OG1 . THR   A 1 198 ? -3.545  -2.261  17.609  1.00 13.34 ? 199 THR   A OG1 1 
ATOM   1592 C  CG2 . THR   A 1 198 ? -3.940  -2.148  19.986  1.00 14.05 ? 199 THR   A CG2 1 
ATOM   1593 N  N   . THR   A 1 199 ? -0.763  -0.037  17.003  1.00 14.13 ? 200 THR   A N   1 
ATOM   1594 C  CA  . THR   A 1 199 ? 0.327   0.013   16.029  1.00 14.66 ? 200 THR   A CA  1 
ATOM   1595 C  C   . THR   A 1 199 ? 1.146   1.258   16.326  1.00 15.07 ? 200 THR   A C   1 
ATOM   1596 O  O   . THR   A 1 199 ? 0.677   2.186   16.969  1.00 15.38 ? 200 THR   A O   1 
ATOM   1597 C  CB  . THR   A 1 199 ? -0.169  0.195   14.589  1.00 17.45 ? 200 THR   A CB  1 
ATOM   1598 O  OG1 . THR   A 1 199 ? -0.934  1.408   14.436  1.00 21.22 ? 200 THR   A OG1 1 
ATOM   1599 C  CG2 . THR   A 1 199 ? -0.981  -0.978  14.095  1.00 17.40 ? 200 THR   A CG2 1 
ATOM   1600 N  N   . PRO   A 1 200 ? 2.439   1.288   15.934  1.00 15.56 ? 201 PRO   A N   1 
ATOM   1601 C  CA  . PRO   A 1 200 ? 3.169   2.540   16.055  1.00 16.23 ? 201 PRO   A CA  1 
ATOM   1602 C  C   . PRO   A 1 200 ? 2.311   3.687   15.507  1.00 16.03 ? 201 PRO   A C   1 
ATOM   1603 O  O   . PRO   A 1 200 ? 1.615   3.586   14.463  1.00 16.74 ? 201 PRO   A O   1 
ATOM   1604 C  CB  . PRO   A 1 200 ? 4.366   2.254   15.123  1.00 17.20 ? 201 PRO   A CB  1 
ATOM   1605 C  CG  . PRO   A 1 200 ? 4.584   0.782   15.254  1.00 16.00 ? 201 PRO   A CG  1 
ATOM   1606 C  CD  . PRO   A 1 200 ? 3.176   0.203   15.262  1.00 16.82 ? 201 PRO   A CD  1 
ATOM   1607 N  N   . PRO   A 1 201 ? 2.305   4.869   16.145  1.00 15.72 ? 202 PRO   A N   1 
ATOM   1608 C  CA  . PRO   A 1 201 ? 3.206   5.216   17.250  1.00 17.09 ? 202 PRO   A CA  1 
ATOM   1609 C  C   . PRO   A 1 201 ? 2.832   4.819   18.679  1.00 15.90 ? 202 PRO   A C   1 
ATOM   1610 O  O   . PRO   A 1 201 ? 3.494   5.242   19.634  1.00 15.63 ? 202 PRO   A O   1 
ATOM   1611 C  CB  . PRO   A 1 201 ? 3.244   6.761   17.113  1.00 18.19 ? 202 PRO   A CB  1 
ATOM   1612 C  CG  . PRO   A 1 201 ? 1.839   7.118   16.637  1.00 18.88 ? 202 PRO   A CG  1 
ATOM   1613 C  CD  . PRO   A 1 201 ? 1.543   6.025   15.646  1.00 16.86 ? 202 PRO   A CD  1 
ATOM   1614 N  N   . LEU   A 1 202 ? 1.827   3.932   18.843  1.00 13.61 ? 203 LEU   A N   1 
ATOM   1615 C  CA  . LEU   A 1 202 ? 1.578   3.337   20.156  1.00 13.77 ? 203 LEU   A CA  1 
ATOM   1616 C  C   . LEU   A 1 202 ? 1.189   4.360   21.226  1.00 13.68 ? 203 LEU   A C   1 
ATOM   1617 O  O   . LEU   A 1 202 ? 1.376   4.083   22.400  1.00 13.65 ? 203 LEU   A O   1 
ATOM   1618 C  CB  . LEU   A 1 202 ? 2.721   2.410   20.588  1.00 14.80 ? 203 LEU   A CB  1 
ATOM   1619 C  CG  . LEU   A 1 202 ? 3.020   1.252   19.636  1.00 13.36 ? 203 LEU   A CG  1 
ATOM   1620 C  CD1 . LEU   A 1 202 ? 4.340   0.621   20.094  1.00 15.38 ? 203 LEU   A CD1 1 
ATOM   1621 C  CD2 . LEU   A 1 202 ? 1.931   0.176   19.592  1.00 14.47 ? 203 LEU   A CD2 1 
ATOM   1622 N  N   . LEU   A 1 203 ? 0.558   5.453   20.808  1.00 14.18 ? 204 LEU   A N   1 
ATOM   1623 C  CA  . LEU   A 1 203 ? 0.270   6.551   21.720  1.00 13.87 ? 204 LEU   A CA  1 
ATOM   1624 C  C   . LEU   A 1 203 ? -0.757  6.133   22.764  1.00 14.48 ? 204 LEU   A C   1 
ATOM   1625 O  O   . LEU   A 1 203 ? -1.725  5.409   22.477  1.00 14.09 ? 204 LEU   A O   1 
ATOM   1626 C  CB  . LEU   A 1 203 ? -0.204  7.769   20.922  1.00 14.04 ? 204 LEU   A CB  1 
ATOM   1627 C  CG  . LEU   A 1 203 ? 0.853   8.325   19.949  1.00 16.69 ? 204 LEU   A CG  1 
ATOM   1628 C  CD1 . LEU   A 1 203 ? 0.220   9.400   19.080  1.00 18.86 ? 204 LEU   A CD1 1 
ATOM   1629 C  CD2 . LEU   A 1 203 ? 2.023   8.940   20.721  1.00 20.57 ? 204 LEU   A CD2 1 
ATOM   1630 N  N   . GLU   A 1 204 ? -0.556  6.584   24.010  1.00 15.17 ? 205 GLU   A N   1 
ATOM   1631 C  CA  . GLU   A 1 204 ? -1.406  6.229   25.138  1.00 14.09 ? 205 GLU   A CA  1 
ATOM   1632 C  C   . GLU   A 1 204 ? -2.587  7.188   25.275  1.00 15.33 ? 205 GLU   A C   1 
ATOM   1633 O  O   . GLU   A 1 204 ? -2.699  7.905   26.279  1.00 17.30 ? 205 GLU   A O   1 
ATOM   1634 C  CB  . GLU   A 1 204 ? -0.548  6.050   26.393  1.00 15.58 ? 205 GLU   A CB  1 
ATOM   1635 C  CG  . GLU   A 1 204 ? 0.357   4.849   26.268  1.00 16.40 ? 205 GLU   A CG  1 
ATOM   1636 C  CD  . GLU   A 1 204 ? 1.300   4.568   27.426  1.00 16.54 ? 205 GLU   A CD  1 
ATOM   1637 O  OE1 . GLU   A 1 204 ? 1.635   5.544   28.186  1.00 21.10 ? 205 GLU   A OE1 1 
ATOM   1638 O  OE2 . GLU   A 1 204 ? 1.748   3.413   27.520  1.00 16.72 ? 205 GLU   A OE2 1 
ATOM   1639 N  N   . CYS   A 1 205 ? -3.520  7.090   24.334  1.00 15.68 ? 206 CYS   A N   1 
ATOM   1640 C  CA  . CYS   A 1 205 ? -4.547  8.124   24.154  1.00 14.60 ? 206 CYS   A CA  1 
ATOM   1641 C  C   . CYS   A 1 205 ? -5.927  7.480   24.019  1.00 13.38 ? 206 CYS   A C   1 
ATOM   1642 O  O   . CYS   A 1 205 ? -6.845  8.199   23.608  1.00 14.96 ? 206 CYS   A O   1 
ATOM   1643 C  CB  . CYS   A 1 205 ? -4.295  8.942   22.885  1.00 15.13 ? 206 CYS   A CB  1 
ATOM   1644 S  SG  . CYS   A 1 205 ? -4.214  7.971   21.357  1.00 16.24 ? 206 CYS   A SG  1 
ATOM   1645 N  N   . VAL   A 1 206 ? -6.044  6.157   24.288  1.00 12.38 ? 207 VAL   A N   1 
ATOM   1646 C  CA  . VAL   A 1 206 ? -7.289  5.430   23.945  1.00 12.29 ? 207 VAL   A CA  1 
ATOM   1647 C  C   . VAL   A 1 206 ? -8.063  5.005   25.207  1.00 12.05 ? 207 VAL   A C   1 
ATOM   1648 O  O   . VAL   A 1 206 ? -7.513  4.350   26.084  1.00 14.58 ? 207 VAL   A O   1 
ATOM   1649 C  CB  . VAL   A 1 206 ? -7.001  4.173   23.080  1.00 13.09 ? 207 VAL   A CB  1 
ATOM   1650 C  CG1 . VAL   A 1 206 ? -8.327  3.496   22.715  1.00 12.21 ? 207 VAL   A CG1 1 
ATOM   1651 C  CG2 . VAL   A 1 206 ? -6.246  4.507   21.776  1.00 13.86 ? 207 VAL   A CG2 1 
ATOM   1652 N  N   . THR   A 1 207 ? -9.389  5.268   25.215  1.00 12.17 ? 208 THR   A N   1 
ATOM   1653 C  CA  . THR   A 1 207 ? -10.307 4.554   26.076  1.00 12.49 ? 208 THR   A CA  1 
ATOM   1654 C  C   . THR   A 1 207 ? -10.848 3.383   25.273  1.00 12.50 ? 208 THR   A C   1 
ATOM   1655 O  O   . THR   A 1 207 ? -11.485 3.593   24.221  1.00 12.64 ? 208 THR   A O   1 
ATOM   1656 C  CB  . THR   A 1 207 ? -11.482 5.437   26.507  1.00 14.24 ? 208 THR   A CB  1 
ATOM   1657 O  OG1 . THR   A 1 207 ? -10.938 6.534   27.258  1.00 14.06 ? 208 THR   A OG1 1 
ATOM   1658 C  CG2 . THR   A 1 207 ? -12.442 4.694   27.412  1.00 14.91 ? 208 THR   A CG2 1 
ATOM   1659 N  N   . TRP   A 1 208 ? -10.450 2.177   25.655  1.00 12.48 ? 209 TRP   A N   1 
ATOM   1660 C  CA  . TRP   A 1 208 ? -10.903 0.977   24.952  1.00 11.75 ? 209 TRP   A CA  1 
ATOM   1661 C  C   . TRP   A 1 208 ? -12.285 0.569   25.450  1.00 12.55 ? 209 TRP   A C   1 
ATOM   1662 O  O   . TRP   A 1 208 ? -12.490 0.489   26.654  1.00 11.91 ? 209 TRP   A O   1 
ATOM   1663 C  CB  . TRP   A 1 208 ? -9.898  -0.199  25.131  1.00 12.57 ? 209 TRP   A CB  1 
ATOM   1664 C  CG  . TRP   A 1 208 ? -8.756  -0.059  24.175  1.00 11.42 ? 209 TRP   A CG  1 
ATOM   1665 C  CD1 . TRP   A 1 208 ? -7.531  0.529   24.398  1.00 11.49 ? 209 TRP   A CD1 1 
ATOM   1666 C  CD2 . TRP   A 1 208 ? -8.799  -0.443  22.802  1.00 12.58 ? 209 TRP   A CD2 1 
ATOM   1667 N  NE1 . TRP   A 1 208 ? -6.852  0.535   23.223  1.00 12.72 ? 209 TRP   A NE1 1 
ATOM   1668 C  CE2 . TRP   A 1 208 ? -7.541  -0.140  22.240  1.00 12.36 ? 209 TRP   A CE2 1 
ATOM   1669 C  CE3 . TRP   A 1 208 ? -9.768  -1.101  22.007  1.00 12.81 ? 209 TRP   A CE3 1 
ATOM   1670 C  CZ2 . TRP   A 1 208 ? -7.260  -0.327  20.877  1.00 14.14 ? 209 TRP   A CZ2 1 
ATOM   1671 C  CZ3 . TRP   A 1 208 ? -9.460  -1.353  20.688  1.00 14.60 ? 209 TRP   A CZ3 1 
ATOM   1672 C  CH2 . TRP   A 1 208 ? -8.224  -0.998  20.139  1.00 12.59 ? 209 TRP   A CH2 1 
ATOM   1673 N  N   . ILE   A 1 209 ? -13.171 0.197   24.532  1.00 11.67 ? 210 ILE   A N   1 
ATOM   1674 C  CA  . ILE   A 1 209 ? -14.487 -0.335  24.838  1.00 13.44 ? 210 ILE   A CA  1 
ATOM   1675 C  C   . ILE   A 1 209 ? -14.620 -1.607  24.025  1.00 12.38 ? 210 ILE   A C   1 
ATOM   1676 O  O   . ILE   A 1 209 ? -14.621 -1.539  22.789  1.00 13.91 ? 210 ILE   A O   1 
ATOM   1677 C  CB  . ILE   A 1 209 ? -15.544 0.707   24.459  1.00 13.24 ? 210 ILE   A CB  1 
ATOM   1678 C  CG1 . ILE   A 1 209 ? -15.373 1.991   25.307  1.00 15.08 ? 210 ILE   A CG1 1 
ATOM   1679 C  CG2 . ILE   A 1 209 ? -16.954 0.107   24.687  1.00 14.81 ? 210 ILE   A CG2 1 
ATOM   1680 C  CD1 . ILE   A 1 209 ? -16.232 3.155   24.827  1.00 16.41 ? 210 ILE   A CD1 1 
ATOM   1681 N  N   . VAL   A 1 210 ? -14.543 -2.771  24.653  1.00 13.03 ? 211 VAL   A N   1 
ATOM   1682 C  CA  . VAL   A 1 210 ? -14.519 -4.065  23.965  1.00 12.08 ? 211 VAL   A CA  1 
ATOM   1683 C  C   . VAL   A 1 210 ? -15.840 -4.809  24.208  1.00 12.14 ? 211 VAL   A C   1 
ATOM   1684 O  O   . VAL   A 1 210 ? -16.188 -5.042  25.372  1.00 13.02 ? 211 VAL   A O   1 
ATOM   1685 C  CB  . VAL   A 1 210 ? -13.308 -4.899  24.408  1.00 12.56 ? 211 VAL   A CB  1 
ATOM   1686 C  CG1 . VAL   A 1 210 ? -13.307 -6.266  23.734  1.00 13.30 ? 211 VAL   A CG1 1 
ATOM   1687 C  CG2 . VAL   A 1 210 ? -12.006 -4.149  24.109  1.00 13.45 ? 211 VAL   A CG2 1 
ATOM   1688 N  N   . LEU   A 1 211 ? -16.638 -5.021  23.172  1.00 12.44 ? 212 LEU   A N   1 
ATOM   1689 C  CA  . LEU   A 1 211 ? -17.922 -5.695  23.355  1.00 12.43 ? 212 LEU   A CA  1 
ATOM   1690 C  C   . LEU   A 1 211 ? -17.706 -7.150  23.729  1.00 12.82 ? 212 LEU   A C   1 
ATOM   1691 O  O   . LEU   A 1 211 ? -16.860 -7.838  23.154  1.00 13.99 ? 212 LEU   A O   1 
ATOM   1692 C  CB  . LEU   A 1 211 ? -18.757 -5.586  22.086  1.00 13.74 ? 212 LEU   A CB  1 
ATOM   1693 C  CG  . LEU   A 1 211 ? -19.100 -4.192  21.635  1.00 14.85 ? 212 LEU   A CG  1 
ATOM   1694 C  CD1 . LEU   A 1 211 ? -20.159 -4.260  20.504  1.00 17.10 ? 212 LEU   A CD1 1 
ATOM   1695 C  CD2 . LEU   A 1 211 ? -19.559 -3.307  22.783  1.00 15.23 ? 212 LEU   A CD2 1 
ATOM   1696 N  N   . LYS   A 1 212 ? -18.566 -7.645  24.638  1.00 13.57 ? 213 LYS   A N   1 
ATOM   1697 C  CA  . LYS   A 1 212 ? -18.507 -9.043  25.033  1.00 14.13 ? 213 LYS   A CA  1 
ATOM   1698 C  C   . LYS   A 1 212 ? -18.957 -9.988  23.924  1.00 15.14 ? 213 LYS   A C   1 
ATOM   1699 O  O   . LYS   A 1 212 ? -18.440 -11.093 23.791  1.00 16.92 ? 213 LYS   A O   1 
ATOM   1700 C  CB  . LYS   A 1 212 ? -19.201 -9.254  26.380  1.00 16.90 ? 213 LYS   A CB  1 
ATOM   1701 C  CG  . LYS   A 1 212 ? -19.389 -10.716 26.766  1.00 21.86 ? 213 LYS   A CG  1 
ATOM   1702 C  CD  . LYS   A 1 212 ? -20.319 -10.887 27.945  1.00 29.17 ? 213 LYS   A CD  1 
ATOM   1703 C  CE  . LYS   A 1 212 ? -20.376 -12.282 28.522  1.00 35.85 ? 213 LYS   A CE  1 
ATOM   1704 N  NZ  . LYS   A 1 212 ? -21.428 -12.348 29.575  1.00 43.34 ? 213 LYS   A NZ  1 
ATOM   1705 N  N   . GLU   A 1 213 ? -20.002 -9.612  23.197  1.00 13.50 ? 214 GLU   A N   1 
ATOM   1706 C  CA  . GLU   A 1 213 ? -20.587 -10.534 22.239  1.00 14.85 ? 214 GLU   A CA  1 
ATOM   1707 C  C   . GLU   A 1 213 ? -19.875 -10.397 20.897  1.00 13.82 ? 214 GLU   A C   1 
ATOM   1708 O  O   . GLU   A 1 213 ? -19.833 -9.316  20.310  1.00 13.26 ? 214 GLU   A O   1 
ATOM   1709 C  CB  . GLU   A 1 213 ? -22.057 -10.168 22.027  1.00 15.70 ? 214 GLU   A CB  1 
ATOM   1710 C  CG  . GLU   A 1 213 ? -22.750 -11.088 21.012  1.00 17.98 ? 214 GLU   A CG  1 
ATOM   1711 C  CD  . GLU   A 1 213 ? -24.253 -10.956 20.807  1.00 25.66 ? 214 GLU   A CD  1 
ATOM   1712 O  OE1 . GLU   A 1 213 ? -24.869 -10.080 21.417  1.00 22.43 ? 214 GLU   A OE1 1 
ATOM   1713 O  OE2 . GLU   A 1 213 ? -24.811 -11.839 20.087  1.00 32.87 ? 214 GLU   A OE2 1 
ATOM   1714 N  N   A PRO   A 1 214 ? -19.321 -11.490 20.334  0.50 13.47 ? 215 PRO   A N   1 
ATOM   1715 N  N   B PRO   A 1 214 ? -19.286 -11.494 20.393  0.50 14.30 ? 215 PRO   A N   1 
ATOM   1716 C  CA  A PRO   A 1 214 ? -18.654 -11.398 19.038  0.50 13.11 ? 215 PRO   A CA  1 
ATOM   1717 C  CA  B PRO   A 1 214 ? -18.659 -11.505 19.067  0.50 14.02 ? 215 PRO   A CA  1 
ATOM   1718 C  C   A PRO   A 1 214 ? -19.724 -11.357 17.962  0.50 14.91 ? 215 PRO   A C   1 
ATOM   1719 C  C   B PRO   A 1 214 ? -19.665 -11.578 17.926  0.50 15.49 ? 215 PRO   A C   1 
ATOM   1720 O  O   A PRO   A 1 214 ? -20.909 -11.593 18.213  0.50 16.36 ? 215 PRO   A O   1 
ATOM   1721 O  O   B PRO   A 1 214 ? -20.758 -12.140 18.103  0.50 16.24 ? 215 PRO   A O   1 
ATOM   1722 C  CB  A PRO   A 1 214 ? -17.907 -12.739 18.916  0.50 13.45 ? 215 PRO   A CB  1 
ATOM   1723 C  CB  B PRO   A 1 214 ? -17.911 -12.854 19.023  0.50 14.87 ? 215 PRO   A CB  1 
ATOM   1724 C  CG  A PRO   A 1 214 ? -18.782 -13.689 19.702  0.50 13.58 ? 215 PRO   A CG  1 
ATOM   1725 C  CG  B PRO   A 1 214 ? -17.918 -13.370 20.460  0.50 16.01 ? 215 PRO   A CG  1 
ATOM   1726 C  CD  A PRO   A 1 214 ? -19.313 -12.874 20.868  0.50 13.83 ? 215 PRO   A CD  1 
ATOM   1727 C  CD  B PRO   A 1 214 ? -19.140 -12.774 21.118  0.50 15.05 ? 215 PRO   A CD  1 
ATOM   1728 N  N   . ILE   A 1 215 ? -19.275 -11.049 16.753  1.00 14.82 ? 216 ILE   A N   1 
ATOM   1729 C  CA  . ILE   A 1 215 ? -20.089 -11.249 15.568  1.00 16.25 ? 216 ILE   A CA  1 
ATOM   1730 C  C   . ILE   A 1 215 ? -19.548 -12.468 14.854  1.00 14.69 ? 216 ILE   A C   1 
ATOM   1731 O  O   . ILE   A 1 215 ? -18.372 -12.812 14.992  1.00 15.25 ? 216 ILE   A O   1 
ATOM   1732 C  CB  . ILE   A 1 215 ? -20.109 -10.048 14.615  1.00 15.72 ? 216 ILE   A CB  1 
ATOM   1733 C  CG1 . ILE   A 1 215 ? -18.701 -9.614  14.151  1.00 15.62 ? 216 ILE   A CG1 1 
ATOM   1734 C  CG2 . ILE   A 1 215 ? -20.895 -8.879  15.240  1.00 17.68 ? 216 ILE   A CG2 1 
ATOM   1735 C  CD1 . ILE   A 1 215 ? -18.714 -8.667  12.908  1.00 18.13 ? 216 ILE   A CD1 1 
ATOM   1736 N  N   A SER   A 1 216 ? -20.437 -13.100 14.082  0.50 15.79 ? 217 SER   A N   1 
ATOM   1737 N  N   B SER   A 1 216 ? -20.421 -13.166 14.131  0.50 16.83 ? 217 SER   A N   1 
ATOM   1738 C  CA  A SER   A 1 216 ? -20.116 -14.254 13.267  0.50 15.40 ? 217 SER   A CA  1 
ATOM   1739 C  CA  B SER   A 1 216 ? -19.972 -14.301 13.349  0.50 17.41 ? 217 SER   A CA  1 
ATOM   1740 C  C   A SER   A 1 216 ? -19.859 -13.815 11.832  0.50 15.84 ? 217 SER   A C   1 
ATOM   1741 C  C   B SER   A 1 216 ? -19.866 -13.894 11.887  0.50 16.99 ? 217 SER   A C   1 
ATOM   1742 O  O   A SER   A 1 216 ? -20.643 -13.061 11.250  0.50 17.66 ? 217 SER   A O   1 
ATOM   1743 O  O   B SER   A 1 216 ? -20.766 -13.240 11.352  0.50 19.00 ? 217 SER   A O   1 
ATOM   1744 C  CB  A SER   A 1 216 ? -21.246 -15.277 13.367  0.50 14.93 ? 217 SER   A CB  1 
ATOM   1745 C  CB  B SER   A 1 216 ? -20.888 -15.479 13.550  0.50 18.80 ? 217 SER   A CB  1 
ATOM   1746 O  OG  A SER   A 1 216 ? -21.153 -15.944 14.627  0.50 15.66 ? 217 SER   A OG  1 
ATOM   1747 O  OG  B SER   A 1 216 ? -20.706 -16.471 12.550  0.50 24.64 ? 217 SER   A OG  1 
ATOM   1748 N  N   . VAL   A 1 217 ? -18.755 -14.295 11.272  1.00 15.16 ? 218 VAL   A N   1 
ATOM   1749 C  CA  . VAL   A 1 217 ? -18.496 -14.137 9.853   1.00 16.15 ? 218 VAL   A CA  1 
ATOM   1750 C  C   . VAL   A 1 217 ? -18.216 -15.516 9.248   1.00 16.58 ? 218 VAL   A C   1 
ATOM   1751 O  O   . VAL   A 1 217 ? -17.838 -16.466 9.956   1.00 16.24 ? 218 VAL   A O   1 
ATOM   1752 C  CB  . VAL   A 1 217 ? -17.308 -13.178 9.610   1.00 16.80 ? 218 VAL   A CB  1 
ATOM   1753 C  CG1 . VAL   A 1 217 ? -17.565 -11.789 10.201  1.00 18.85 ? 218 VAL   A CG1 1 
ATOM   1754 C  CG2 . VAL   A 1 217 ? -15.975 -13.740 10.081  1.00 17.73 ? 218 VAL   A CG2 1 
ATOM   1755 N  N   . SER   A 1 218 ? -18.328 -15.637 7.916   1.00 16.30 ? 219 SER   A N   1 
ATOM   1756 C  CA  . SER   A 1 218 ? -18.144 -16.961 7.345   1.00 17.43 ? 219 SER   A CA  1 
ATOM   1757 C  C   . SER   A 1 218 ? -16.669 -17.211 7.058   1.00 16.83 ? 219 SER   A C   1 
ATOM   1758 O  O   . SER   A 1 218 ? -15.830 -16.300 6.966   1.00 16.08 ? 219 SER   A O   1 
ATOM   1759 C  CB  . SER   A 1 218 ? -18.964 -17.163 6.088   1.00 17.13 ? 219 SER   A CB  1 
ATOM   1760 O  OG  . SER   A 1 218 ? -18.461 -16.329 5.052   1.00 20.72 ? 219 SER   A OG  1 
ATOM   1761 N  N   A SER   A 1 219 ? -16.330 -18.493 6.919   0.50 16.88 ? 220 SER   A N   1 
ATOM   1762 N  N   B SER   A 1 219 ? -16.335 -18.490 6.915   0.50 16.95 ? 220 SER   A N   1 
ATOM   1763 C  CA  A SER   A 1 219 ? -14.982 -18.878 6.542   0.50 18.75 ? 220 SER   A CA  1 
ATOM   1764 C  CA  B SER   A 1 219 ? -14.979 -18.860 6.559   0.50 18.86 ? 220 SER   A CA  1 
ATOM   1765 C  C   A SER   A 1 219 ? -14.605 -18.207 5.220   0.50 19.16 ? 220 SER   A C   1 
ATOM   1766 C  C   B SER   A 1 219 ? -14.602 -18.221 5.220   0.50 19.21 ? 220 SER   A C   1 
ATOM   1767 O  O   A SER   A 1 219 ? -13.492 -17.701 5.068   0.50 20.50 ? 220 SER   A O   1 
ATOM   1768 O  O   B SER   A 1 219 ? -13.484 -17.730 5.059   0.50 20.60 ? 220 SER   A O   1 
ATOM   1769 C  CB  A SER   A 1 219 ? -14.836 -20.390 6.504   0.50 18.79 ? 220 SER   A CB  1 
ATOM   1770 C  CB  B SER   A 1 219 ? -14.816 -20.368 6.598   0.50 18.88 ? 220 SER   A CB  1 
ATOM   1771 O  OG  A SER   A 1 219 ? -15.834 -20.977 5.670   0.50 18.91 ? 220 SER   A OG  1 
ATOM   1772 O  OG  B SER   A 1 219 ? -13.531 -20.752 6.156   0.50 20.03 ? 220 SER   A OG  1 
ATOM   1773 N  N   . GLU   A 1 220 ? -15.564 -18.125 4.286   1.00 19.78 ? 221 GLU   A N   1 
ATOM   1774 C  CA  . GLU   A 1 220 ? -15.278 -17.498 3.003   1.00 21.48 ? 221 GLU   A CA  1 
ATOM   1775 C  C   . GLU   A 1 220 ? -14.956 -16.006 3.172   1.00 21.20 ? 221 GLU   A C   1 
ATOM   1776 O  O   . GLU   A 1 220 ? -14.067 -15.501 2.495   1.00 20.25 ? 221 GLU   A O   1 
ATOM   1777 C  CB  . GLU   A 1 220 ? -16.390 -17.693 1.989   1.00 25.79 ? 221 GLU   A CB  1 
ATOM   1778 C  CG  . GLU   A 1 220 ? -16.583 -19.170 1.628   1.00 29.46 ? 221 GLU   A CG  1 
ATOM   1779 C  CD  . GLU   A 1 220 ? -17.689 -19.840 2.427   1.00 37.29 ? 221 GLU   A CD  1 
ATOM   1780 O  OE1 . GLU   A 1 220 ? -17.840 -19.552 3.649   1.00 31.39 ? 221 GLU   A OE1 1 
ATOM   1781 O  OE2 . GLU   A 1 220 ? -18.417 -20.665 1.828   1.00 49.60 ? 221 GLU   A OE2 1 
ATOM   1782 N  N   . GLN   A 1 221 ? -15.674 -15.307 4.067   1.00 17.53 ? 222 GLN   A N   1 
ATOM   1783 C  CA  . GLN   A 1 221 ? -15.425 -13.876 4.230   1.00 16.91 ? 222 GLN   A CA  1 
ATOM   1784 C  C   . GLN   A 1 221 ? -14.009 -13.659 4.776   1.00 18.50 ? 222 GLN   A C   1 
ATOM   1785 O  O   . GLN   A 1 221 ? -13.253 -12.815 4.262   1.00 17.65 ? 222 GLN   A O   1 
ATOM   1786 C  CB  . GLN   A 1 221 ? -16.480 -13.325 5.190   1.00 17.10 ? 222 GLN   A CB  1 
ATOM   1787 C  CG  . GLN   A 1 221 ? -17.836 -13.211 4.500   1.00 17.13 ? 222 GLN   A CG  1 
ATOM   1788 C  CD  . GLN   A 1 221 ? -18.963 -12.657 5.335   1.00 16.29 ? 222 GLN   A CD  1 
ATOM   1789 O  OE1 . GLN   A 1 221 ? -19.124 -13.008 6.517   1.00 16.53 ? 222 GLN   A OE1 1 
ATOM   1790 N  NE2 . GLN   A 1 221 ? -19.742 -11.731 4.773   1.00 17.18 ? 222 GLN   A NE2 1 
ATOM   1791 N  N   . VAL   A 1 222 ? -13.639 -14.434 5.805   1.00 17.99 ? 223 VAL   A N   1 
ATOM   1792 C  CA  . VAL   A 1 222 ? -12.316 -14.242 6.393   1.00 18.01 ? 223 VAL   A CA  1 
ATOM   1793 C  C   . VAL   A 1 222 ? -11.210 -14.664 5.401   1.00 18.77 ? 223 VAL   A C   1 
ATOM   1794 O  O   . VAL   A 1 222 ? -10.128 -14.077 5.344   1.00 17.79 ? 223 VAL   A O   1 
ATOM   1795 C  CB  . VAL   A 1 222 ? -12.164 -14.793 7.840   1.00 20.19 ? 223 VAL   A CB  1 
ATOM   1796 C  CG1 . VAL   A 1 222 ? -12.193 -16.307 7.877   1.00 22.31 ? 223 VAL   A CG1 1 
ATOM   1797 C  CG2 . VAL   A 1 222 ? -10.865 -14.297 8.483   1.00 22.44 ? 223 VAL   A CG2 1 
ATOM   1798 N  N   . LEU   A 1 223 ? -11.493 -15.702 4.591   1.00 19.48 ? 224 LEU   A N   1 
ATOM   1799 C  CA  . LEU   A 1 223 ? -10.517 -16.102 3.584   1.00 21.01 ? 224 LEU   A CA  1 
ATOM   1800 C  C   . LEU   A 1 223 ? -10.194 -14.971 2.617   1.00 21.96 ? 224 LEU   A C   1 
ATOM   1801 O  O   . LEU   A 1 223 ? -9.032  -14.824 2.221   1.00 21.21 ? 224 LEU   A O   1 
ATOM   1802 C  CB  . LEU   A 1 223 ? -10.979 -17.381 2.868   1.00 24.34 ? 224 LEU   A CB  1 
ATOM   1803 C  CG  . LEU   A 1 223 ? -10.814 -18.651 3.712   1.00 25.52 ? 224 LEU   A CG  1 
ATOM   1804 C  CD1 . LEU   A 1 223 ? -11.642 -19.814 3.147   1.00 29.77 ? 224 LEU   A CD1 1 
ATOM   1805 C  CD2 . LEU   A 1 223 ? -9.344  -19.043 3.865   1.00 26.98 ? 224 LEU   A CD2 1 
ATOM   1806 N  N   . LYS   A 1 224 ? -11.182 -14.135 2.294   1.00 19.08 ? 225 LYS   A N   1 
ATOM   1807 C  CA  . LYS   A 1 224 ? -10.944 -13.006 1.400   1.00 20.47 ? 225 LYS   A CA  1 
ATOM   1808 C  C   . LYS   A 1 224 ? -10.080 -11.927 2.060   1.00 19.82 ? 225 LYS   A C   1 
ATOM   1809 O  O   . LYS   A 1 224 ? -9.251  -11.334 1.368   1.00 20.90 ? 225 LYS   A O   1 
ATOM   1810 C  CB  . LYS   A 1 224 ? -12.236 -12.512 0.741   1.00 22.98 ? 225 LYS   A CB  1 
ATOM   1811 C  CG  . LYS   A 1 224 ? -12.776 -13.514 -0.299  1.00 27.15 ? 225 LYS   A CG  1 
ATOM   1812 C  CD  . LYS   A 1 224 ? -14.073 -13.155 -1.015  1.00 37.21 ? 225 LYS   A CD  1 
ATOM   1813 C  CE  . LYS   A 1 224 ? -14.584 -14.306 -1.865  1.00 37.22 ? 225 LYS   A CE  1 
ATOM   1814 N  NZ  . LYS   A 1 224 ? -15.911 -14.025 -2.478  1.00 40.33 ? 225 LYS   A NZ  1 
ATOM   1815 N  N   . PHE   A 1 225 ? -10.176 -11.723 3.398   1.00 17.84 ? 226 PHE   A N   1 
ATOM   1816 C  CA  . PHE   A 1 225 ? -9.221  -10.851 4.076   1.00 15.51 ? 226 PHE   A CA  1 
ATOM   1817 C  C   . PHE   A 1 225 ? -7.791  -11.335 3.870   1.00 16.41 ? 226 PHE   A C   1 
ATOM   1818 O  O   . PHE   A 1 225 ? -6.885  -10.531 3.670   1.00 16.03 ? 226 PHE   A O   1 
ATOM   1819 C  CB  . PHE   A 1 225 ? -9.431  -10.853 5.604   1.00 15.83 ? 226 PHE   A CB  1 
ATOM   1820 C  CG  . PHE   A 1 225 ? -10.611 -10.056 6.128   1.00 17.50 ? 226 PHE   A CG  1 
ATOM   1821 C  CD1 . PHE   A 1 225 ? -11.667 -9.650  5.331   1.00 20.49 ? 226 PHE   A CD1 1 
ATOM   1822 C  CD2 . PHE   A 1 225 ? -10.696 -9.795  7.492   1.00 21.72 ? 226 PHE   A CD2 1 
ATOM   1823 C  CE1 . PHE   A 1 225 ? -12.720 -8.913  5.845   1.00 22.17 ? 226 PHE   A CE1 1 
ATOM   1824 C  CE2 . PHE   A 1 225 ? -11.758 -9.068  8.021   1.00 22.75 ? 226 PHE   A CE2 1 
ATOM   1825 C  CZ  . PHE   A 1 225 ? -12.756 -8.605  7.186   1.00 21.67 ? 226 PHE   A CZ  1 
ATOM   1826 N  N   . ARG   A 1 226 ? -7.592  -12.656 3.966   1.00 15.50 ? 227 ARG   A N   1 
ATOM   1827 C  CA  . ARG   A 1 226 ? -6.260  -13.238 3.898   1.00 16.94 ? 227 ARG   A CA  1 
ATOM   1828 C  C   . ARG   A 1 226 ? -5.667  -13.270 2.479   1.00 16.52 ? 227 ARG   A C   1 
ATOM   1829 O  O   . ARG   A 1 226 ? -4.532  -13.706 2.339   1.00 19.01 ? 227 ARG   A O   1 
ATOM   1830 C  CB  . ARG   A 1 226 ? -6.296  -14.670 4.459   1.00 16.10 ? 227 ARG   A CB  1 
ATOM   1831 C  CG  . ARG   A 1 226 ? -6.695  -14.783 5.922   1.00 16.38 ? 227 ARG   A CG  1 
ATOM   1832 C  CD  . ARG   A 1 226 ? -6.685  -16.248 6.416   1.00 16.58 ? 227 ARG   A CD  1 
ATOM   1833 N  NE  . ARG   A 1 226 ? -7.285  -16.375 7.754   1.00 16.92 ? 227 ARG   A NE  1 
ATOM   1834 C  CZ  . ARG   A 1 226 ? -8.232  -17.228 8.095   1.00 18.37 ? 227 ARG   A CZ  1 
ATOM   1835 N  NH1 . ARG   A 1 226 ? -8.632  -18.162 7.231   1.00 21.25 ? 227 ARG   A NH1 1 
ATOM   1836 N  NH2 . ARG   A 1 226 ? -8.716  -17.191 9.320   1.00 19.66 ? 227 ARG   A NH2 1 
ATOM   1837 N  N   . LYS   A 1 227 ? -6.406  -12.775 1.468   1.00 18.54 ? 228 LYS   A N   1 
ATOM   1838 C  CA  . LYS   A 1 227 ? -5.919  -12.661 0.100   1.00 18.44 ? 228 LYS   A CA  1 
ATOM   1839 C  C   . LYS   A 1 227 ? -5.308  -11.287 -0.160  1.00 18.17 ? 228 LYS   A C   1 
ATOM   1840 O  O   . LYS   A 1 227 ? -4.626  -11.069 -1.158  1.00 18.80 ? 228 LYS   A O   1 
ATOM   1841 C  CB  . LYS   A 1 227 ? -7.075  -12.878 -0.884  1.00 19.27 ? 228 LYS   A CB  1 
ATOM   1842 C  CG  . LYS   A 1 227 ? -7.488  -14.342 -0.967  1.00 24.03 ? 228 LYS   A CG  1 
ATOM   1843 C  CD  . LYS   A 1 227 ? -8.634  -14.602 -1.943  1.00 27.77 ? 228 LYS   A CD  1 
ATOM   1844 C  CE  . LYS   A 1 227 ? -8.239  -14.581 -3.407  1.00 34.70 ? 228 LYS   A CE  1 
ATOM   1845 N  NZ  . LYS   A 1 227 ? -9.409  -14.794 -4.303  1.00 39.09 ? 228 LYS   A NZ  1 
ATOM   1846 N  N   . LEU   A 1 228 ? -5.523  -10.352 0.755   1.00 16.42 ? 229 LEU   A N   1 
ATOM   1847 C  CA  . LEU   A 1 228 ? -4.859  -9.071  0.650   1.00 16.77 ? 229 LEU   A CA  1 
ATOM   1848 C  C   . LEU   A 1 228 ? -3.351  -9.241  0.792   1.00 16.74 ? 229 LEU   A C   1 
ATOM   1849 O  O   . LEU   A 1 228 ? -2.800  -10.249 1.244   1.00 17.49 ? 229 LEU   A O   1 
ATOM   1850 C  CB  . LEU   A 1 228 ? -5.364  -8.153  1.777   1.00 16.47 ? 229 LEU   A CB  1 
ATOM   1851 C  CG  . LEU   A 1 228 ? -6.804  -7.687  1.566   1.00 17.54 ? 229 LEU   A CG  1 
ATOM   1852 C  CD1 . LEU   A 1 228 ? -7.358  -7.080  2.845   1.00 17.52 ? 229 LEU   A CD1 1 
ATOM   1853 C  CD2 . LEU   A 1 228 ? -6.858  -6.661  0.440   1.00 19.34 ? 229 LEU   A CD2 1 
ATOM   1854 N  N   . ASN   A 1 229 ? -2.655  -8.172  0.406   1.00 18.04 ? 230 ASN   A N   1 
ATOM   1855 C  CA  . ASN   A 1 229 ? -1.199  -8.194  0.394   1.00 16.90 ? 230 ASN   A CA  1 
ATOM   1856 C  C   . ASN   A 1 229 ? -0.609  -7.047  1.234   1.00 18.46 ? 230 ASN   A C   1 
ATOM   1857 O  O   . ASN   A 1 229 ? -1.091  -5.918  1.153   1.00 18.28 ? 230 ASN   A O   1 
ATOM   1858 C  CB  . ASN   A 1 229 ? -0.690  -7.964  -1.045  1.00 19.14 ? 230 ASN   A CB  1 
ATOM   1859 C  CG  . ASN   A 1 229 ? -0.694  -9.172  -1.975  1.00 22.49 ? 230 ASN   A CG  1 
ATOM   1860 O  OD1 . ASN   A 1 229 ? -0.155  -9.082  -3.098  1.00 23.98 ? 230 ASN   A OD1 1 
ATOM   1861 N  ND2 . ASN   A 1 229 ? -1.313  -10.274 -1.586  1.00 21.16 ? 230 ASN   A ND2 1 
ATOM   1862 N  N   . PHE   A 1 230 ? 0.468   -7.320  2.002   1.00 17.49 ? 231 PHE   A N   1 
ATOM   1863 C  CA  . PHE   A 1 230 ? 1.246   -6.272  2.666   1.00 16.75 ? 231 PHE   A CA  1 
ATOM   1864 C  C   . PHE   A 1 230 ? 2.131   -5.493  1.678   1.00 18.54 ? 231 PHE   A C   1 
ATOM   1865 O  O   . PHE   A 1 230 ? 2.451   -4.314  1.927   1.00 18.35 ? 231 PHE   A O   1 
ATOM   1866 C  CB  . PHE   A 1 230 ? 2.188   -6.877  3.707   1.00 17.84 ? 231 PHE   A CB  1 
ATOM   1867 C  CG  . PHE   A 1 230 ? 1.625   -7.437  4.997   1.00 18.07 ? 231 PHE   A CG  1 
ATOM   1868 C  CD1 . PHE   A 1 230 ? 0.802   -6.661  5.811   1.00 18.28 ? 231 PHE   A CD1 1 
ATOM   1869 C  CD2 . PHE   A 1 230 ? 1.970   -8.730  5.415   1.00 18.18 ? 231 PHE   A CD2 1 
ATOM   1870 C  CE1 . PHE   A 1 230 ? 0.336   -7.167  7.033   1.00 17.01 ? 231 PHE   A CE1 1 
ATOM   1871 C  CE2 . PHE   A 1 230 ? 1.529   -9.234  6.641   1.00 16.98 ? 231 PHE   A CE2 1 
ATOM   1872 C  CZ  . PHE   A 1 230 ? 0.712   -8.450  7.436   1.00 16.89 ? 231 PHE   A CZ  1 
ATOM   1873 N  N   . ASN   A 1 231 ? 2.567   -6.171  0.608   1.00 19.28 ? 232 ASN   A N   1 
ATOM   1874 C  CA  . ASN   A 1 231 ? 3.456   -5.592  -0.394  1.00 20.05 ? 232 ASN   A CA  1 
ATOM   1875 C  C   . ASN   A 1 231 ? 2.693   -4.652  -1.338  1.00 18.77 ? 232 ASN   A C   1 
ATOM   1876 O  O   . ASN   A 1 231 ? 1.449   -4.739  -1.502  1.00 18.54 ? 232 ASN   A O   1 
ATOM   1877 C  CB  . ASN   A 1 231 ? 4.112   -6.720  -1.194  1.00 20.75 ? 232 ASN   A CB  1 
ATOM   1878 C  CG  . ASN   A 1 231 ? 3.054   -7.601  -1.819  1.00 21.86 ? 232 ASN   A CG  1 
ATOM   1879 O  OD1 . ASN   A 1 231 ? 2.487   -8.449  -1.137  1.00 23.27 ? 232 ASN   A OD1 1 
ATOM   1880 N  ND2 . ASN   A 1 231 ? 2.674   -7.383  -3.073  1.00 22.65 ? 232 ASN   A ND2 1 
ATOM   1881 N  N   . GLY   A 1 232 ? 3.497   -3.765  -1.970  1.00 21.91 ? 233 GLY   A N   1 
ATOM   1882 C  CA  . GLY   A 1 232 ? 3.010   -2.951  -3.091  1.00 23.17 ? 233 GLY   A CA  1 
ATOM   1883 C  C   . GLY   A 1 232 ? 2.832   -3.746  -4.386  1.00 23.11 ? 233 GLY   A C   1 
ATOM   1884 O  O   . GLY   A 1 232 ? 3.357   -4.849  -4.508  1.00 23.81 ? 233 GLY   A O   1 
ATOM   1885 N  N   . GLU   A 1 233 ? 2.030   -3.221  -5.327  1.00 23.62 ? 234 GLU   A N   1 
ATOM   1886 C  CA  . GLU   A 1 233 ? 1.965   -3.735  -6.697  1.00 24.47 ? 234 GLU   A CA  1 
ATOM   1887 C  C   . GLU   A 1 233 ? 3.363   -3.869  -7.302  1.00 24.49 ? 234 GLU   A C   1 
ATOM   1888 O  O   . GLU   A 1 233 ? 4.243   -3.035  -7.133  1.00 25.76 ? 234 GLU   A O   1 
ATOM   1889 C  CB  . GLU   A 1 233 ? 1.117   -2.822  -7.593  1.00 23.70 ? 234 GLU   A CB  1 
ATOM   1890 C  CG  . GLU   A 1 233 ? 0.867   -3.357  -9.011  1.00 27.12 ? 234 GLU   A CG  1 
ATOM   1891 C  CD  . GLU   A 1 233 ? -0.000  -2.429  -9.855  1.00 35.35 ? 234 GLU   A CD  1 
ATOM   1892 O  OE1 . GLU   A 1 233 ? -0.279  -1.269  -9.396  1.00 35.39 ? 234 GLU   A OE1 1 
ATOM   1893 O  OE2 . GLU   A 1 233 ? -0.403  -2.847  -10.991 1.00 39.67 ? 234 GLU   A OE2 1 
ATOM   1894 N  N   . GLY   A 1 234 ? 3.547   -5.011  -7.972  1.00 24.86 ? 235 GLY   A N   1 
ATOM   1895 C  CA  . GLY   A 1 234 ? 4.799   -5.277  -8.659  1.00 28.56 ? 235 GLY   A CA  1 
ATOM   1896 C  C   . GLY   A 1 234 ? 5.921   -5.677  -7.701  1.00 31.38 ? 235 GLY   A C   1 
ATOM   1897 O  O   . GLY   A 1 234 ? 7.095   -5.621  -8.085  1.00 32.48 ? 235 GLY   A O   1 
ATOM   1898 N  N   . GLU   A 1 235 ? 5.566   -6.040  -6.452  1.00 24.87 ? 236 GLU   A N   1 
ATOM   1899 C  CA  . GLU   A 1 235 ? 6.515   -6.664  -5.542  1.00 23.18 ? 236 GLU   A CA  1 
ATOM   1900 C  C   . GLU   A 1 235 ? 6.086   -8.113  -5.278  1.00 24.97 ? 236 GLU   A C   1 
ATOM   1901 O  O   . GLU   A 1 235 ? 4.927   -8.471  -5.502  1.00 25.03 ? 236 GLU   A O   1 
ATOM   1902 C  CB  . GLU   A 1 235 ? 6.624   -5.911  -4.211  1.00 27.32 ? 236 GLU   A CB  1 
ATOM   1903 C  CG  . GLU   A 1 235 ? 7.002   -4.444  -4.394  1.00 29.87 ? 236 GLU   A CG  1 
ATOM   1904 C  CD  . GLU   A 1 235 ? 6.923   -3.578  -3.144  1.00 38.54 ? 236 GLU   A CD  1 
ATOM   1905 O  OE1 . GLU   A 1 235 ? 6.243   -3.978  -2.154  1.00 34.91 ? 236 GLU   A OE1 1 
ATOM   1906 O  OE2 . GLU   A 1 235 ? 7.550   -2.493  -3.149  1.00 42.33 ? 236 GLU   A OE2 1 
ATOM   1907 N  N   . PRO   A 1 236 ? 6.978   -8.977  -4.763  1.00 23.50 ? 237 PRO   A N   1 
ATOM   1908 C  CA  . PRO   A 1 236 ? 6.618   -10.365 -4.472  1.00 24.28 ? 237 PRO   A CA  1 
ATOM   1909 C  C   . PRO   A 1 236 ? 5.608   -10.418 -3.325  1.00 23.38 ? 237 PRO   A C   1 
ATOM   1910 O  O   . PRO   A 1 236 ? 5.626   -9.550  -2.445  1.00 24.39 ? 237 PRO   A O   1 
ATOM   1911 C  CB  . PRO   A 1 236 ? 7.947   -10.992 -4.044  1.00 25.54 ? 237 PRO   A CB  1 
ATOM   1912 C  CG  . PRO   A 1 236 ? 8.967   -10.114 -4.683  1.00 25.14 ? 237 PRO   A CG  1 
ATOM   1913 C  CD  . PRO   A 1 236 ? 8.394   -8.719  -4.467  1.00 23.89 ? 237 PRO   A CD  1 
ATOM   1914 N  N   . GLU   A 1 237 ? 4.745   -11.433 -3.404  1.00 22.66 ? 238 GLU   A N   1 
ATOM   1915 C  CA  . GLU   A 1 237 ? 3.535   -11.439 -2.617  1.00 22.07 ? 238 GLU   A CA  1 
ATOM   1916 C  C   . GLU   A 1 237 ? 3.909   -11.748 -1.166  1.00 22.94 ? 238 GLU   A C   1 
ATOM   1917 O  O   . GLU   A 1 237 ? 4.563   -12.740 -0.871  1.00 22.25 ? 238 GLU   A O   1 
ATOM   1918 C  CB  . GLU   A 1 237 ? 2.517   -12.429 -3.183  1.00 22.06 ? 238 GLU   A CB  1 
ATOM   1919 C  CG  . GLU   A 1 237 ? 1.187   -12.341 -2.453  1.00 27.26 ? 238 GLU   A CG  1 
ATOM   1920 C  CD  . GLU   A 1 237 ? 0.076   -13.101 -3.146  1.00 29.31 ? 238 GLU   A CD  1 
ATOM   1921 O  OE1 . GLU   A 1 237 ? 0.335   -14.283 -3.490  1.00 38.12 ? 238 GLU   A OE1 1 
ATOM   1922 O  OE2 . GLU   A 1 237 ? -1.037  -12.539 -3.315  1.00 27.35 ? 238 GLU   A OE2 1 
ATOM   1923 N  N   . GLU   A 1 238 ? 3.368   -10.933 -0.266  1.00 19.77 ? 239 GLU   A N   1 
ATOM   1924 C  CA  . GLU   A 1 238 ? 3.427   -11.138 1.176   1.00 21.65 ? 239 GLU   A CA  1 
ATOM   1925 C  C   . GLU   A 1 238 ? 1.975   -11.077 1.643   1.00 19.53 ? 239 GLU   A C   1 
ATOM   1926 O  O   . GLU   A 1 238 ? 1.355   -10.010 1.669   1.00 19.47 ? 239 GLU   A O   1 
ATOM   1927 C  CB  . GLU   A 1 238 ? 4.174   -10.016 1.899   1.00 22.67 ? 239 GLU   A CB  1 
ATOM   1928 C  CG  . GLU   A 1 238 ? 5.640   -9.776  1.500   1.00 25.00 ? 239 GLU   A CG  1 
ATOM   1929 C  CD  . GLU   A 1 238 ? 6.147   -8.414  1.983   1.00 35.82 ? 239 GLU   A CD  1 
ATOM   1930 O  OE1 . GLU   A 1 238 ? 5.986   -8.106  3.195   1.00 35.97 ? 239 GLU   A OE1 1 
ATOM   1931 O  OE2 . GLU   A 1 238 ? 6.628   -7.609  1.140   1.00 38.82 ? 239 GLU   A OE2 1 
ATOM   1932 N  N   . LEU   A 1 239 ? 1.383   -12.244 1.948   1.00 18.93 ? 240 LEU   A N   1 
ATOM   1933 C  CA  . LEU   A 1 239 ? -0.030  -12.219 2.275   1.00 17.71 ? 240 LEU   A CA  1 
ATOM   1934 C  C   . LEU   A 1 239 ? -0.249  -11.411 3.562   1.00 14.76 ? 240 LEU   A C   1 
ATOM   1935 O  O   . LEU   A 1 239 ? 0.491   -11.575 4.546   1.00 18.17 ? 240 LEU   A O   1 
ATOM   1936 C  CB  . LEU   A 1 239 ? -0.541  -13.653 2.453   1.00 17.10 ? 240 LEU   A CB  1 
ATOM   1937 C  CG  . LEU   A 1 239 ? -0.603  -14.502 1.178   1.00 18.43 ? 240 LEU   A CG  1 
ATOM   1938 C  CD1 . LEU   A 1 239 ? -1.092  -15.904 1.533   1.00 22.75 ? 240 LEU   A CD1 1 
ATOM   1939 C  CD2 . LEU   A 1 239 ? -1.537  -13.875 0.152   1.00 19.41 ? 240 LEU   A CD2 1 
ATOM   1940 N  N   . MET   A 1 240 ? -1.336  -10.624 3.543   1.00 15.56 ? 241 MET   A N   1 
ATOM   1941 C  CA  . MET   A 1 240 ? -1.710  -9.816  4.706   1.00 16.90 ? 241 MET   A CA  1 
ATOM   1942 C  C   . MET   A 1 240 ? -2.465  -10.713 5.692   1.00 16.33 ? 241 MET   A C   1 
ATOM   1943 O  O   . MET   A 1 240 ? -3.672  -10.917 5.595   1.00 16.49 ? 241 MET   A O   1 
ATOM   1944 C  CB  . MET   A 1 240 ? -2.567  -8.639  4.255   1.00 18.37 ? 241 MET   A CB  1 
ATOM   1945 C  CG  . MET   A 1 240 ? -2.809  -7.626  5.381   1.00 18.04 ? 241 MET   A CG  1 
ATOM   1946 S  SD  . MET   A 1 240 ? -3.846  -6.261  4.846   1.00 18.08 ? 241 MET   A SD  1 
ATOM   1947 C  CE  . MET   A 1 240 ? -2.578  -5.140  4.238   1.00 17.19 ? 241 MET   A CE  1 
ATOM   1948 N  N   . VAL   A 1 241 ? -1.707  -11.299 6.633   1.00 15.65 ? 242 VAL   A N   1 
ATOM   1949 C  CA  . VAL   A 1 241 ? -2.230  -12.188 7.686   1.00 15.56 ? 242 VAL   A CA  1 
ATOM   1950 C  C   . VAL   A 1 241 ? -1.426  -11.912 8.962   1.00 15.41 ? 242 VAL   A C   1 
ATOM   1951 O  O   . VAL   A 1 241 ? -0.275  -11.462 8.896   1.00 16.29 ? 242 VAL   A O   1 
ATOM   1952 C  CB  . VAL   A 1 241 ? -2.122  -13.688 7.333   1.00 15.61 ? 242 VAL   A CB  1 
ATOM   1953 C  CG1 . VAL   A 1 241 ? -2.992  -14.036 6.119   1.00 18.20 ? 242 VAL   A CG1 1 
ATOM   1954 C  CG2 . VAL   A 1 241 ? -0.673  -14.120 7.167   1.00 17.84 ? 242 VAL   A CG2 1 
ATOM   1955 N  N   . ASP   A 1 242 ? -2.028  -12.192 10.129  1.00 13.41 ? 243 ASP   A N   1 
ATOM   1956 C  CA  . ASP   A 1 242 ? -1.359  -12.060 11.417  1.00 13.48 ? 243 ASP   A CA  1 
ATOM   1957 C  C   . ASP   A 1 242 ? -0.866  -10.625 11.632  1.00 13.87 ? 243 ASP   A C   1 
ATOM   1958 O  O   . ASP   A 1 242 ? 0.267   -10.393 12.069  1.00 15.93 ? 243 ASP   A O   1 
ATOM   1959 C  CB  . ASP   A 1 242 ? -0.279  -13.102 11.644  1.00 14.81 ? 243 ASP   A CB  1 
ATOM   1960 C  CG  . ASP   A 1 242 ? -0.853  -14.507 11.729  1.00 16.09 ? 243 ASP   A CG  1 
ATOM   1961 O  OD1 . ASP   A 1 242 ? -1.914  -14.695 12.389  1.00 15.47 ? 243 ASP   A OD1 1 
ATOM   1962 O  OD2 . ASP   A 1 242 ? -0.199  -15.410 11.163  1.00 17.32 ? 243 ASP   A OD2 1 
ATOM   1963 N  N   . ASN   A 1 243 ? -1.758  -9.672  11.381  1.00 12.85 ? 244 ASN   A N   1 
ATOM   1964 C  CA  . ASN   A 1 243 ? -1.449  -8.263  11.637  1.00 12.89 ? 244 ASN   A CA  1 
ATOM   1965 C  C   . ASN   A 1 243 ? -2.018  -7.809  12.988  1.00 13.46 ? 244 ASN   A C   1 
ATOM   1966 O  O   . ASN   A 1 243 ? -2.625  -6.732  13.076  1.00 13.57 ? 244 ASN   A O   1 
ATOM   1967 C  CB  . ASN   A 1 243 ? -2.020  -7.395  10.498  1.00 15.04 ? 244 ASN   A CB  1 
ATOM   1968 C  CG  . ASN   A 1 243 ? -3.496  -7.595  10.252  1.00 15.14 ? 244 ASN   A CG  1 
ATOM   1969 O  OD1 . ASN   A 1 243 ? -4.150  -8.387  10.966  1.00 14.24 ? 244 ASN   A OD1 1 
ATOM   1970 N  ND2 . ASN   A 1 243 ? -4.019  -6.868  9.252   1.00 16.21 ? 244 ASN   A ND2 1 
ATOM   1971 N  N   . TRP   A 1 244 ? -1.758  -8.607  14.025  1.00 13.68 ? 245 TRP   A N   1 
ATOM   1972 C  CA  . TRP   A 1 244 ? -2.240  -8.359  15.377  1.00 12.20 ? 245 TRP   A CA  1 
ATOM   1973 C  C   . TRP   A 1 244 ? -1.040  -8.243  16.296  1.00 14.97 ? 245 TRP   A C   1 
ATOM   1974 O  O   . TRP   A 1 244 ? -0.057  -8.974  16.165  1.00 15.40 ? 245 TRP   A O   1 
ATOM   1975 C  CB  . TRP   A 1 244 ? -3.206  -9.457  15.875  1.00 13.65 ? 245 TRP   A CB  1 
ATOM   1976 C  CG  . TRP   A 1 244 ? -2.710  -10.867 15.670  1.00 12.88 ? 245 TRP   A CG  1 
ATOM   1977 C  CD1 . TRP   A 1 244 ? -2.857  -11.604 14.509  1.00 12.68 ? 245 TRP   A CD1 1 
ATOM   1978 C  CD2 . TRP   A 1 244 ? -2.117  -11.736 16.643  1.00 14.11 ? 245 TRP   A CD2 1 
ATOM   1979 N  NE1 . TRP   A 1 244 ? -2.325  -12.869 14.709  1.00 12.97 ? 245 TRP   A NE1 1 
ATOM   1980 C  CE2 . TRP   A 1 244 ? -1.883  -12.972 16.009  1.00 13.90 ? 245 TRP   A CE2 1 
ATOM   1981 C  CE3 . TRP   A 1 244 ? -1.771  -11.586 18.004  1.00 14.66 ? 245 TRP   A CE3 1 
ATOM   1982 C  CZ2 . TRP   A 1 244 ? -1.236  -14.035 16.665  1.00 15.12 ? 245 TRP   A CZ2 1 
ATOM   1983 C  CZ3 . TRP   A 1 244 ? -1.188  -12.644 18.665  1.00 15.50 ? 245 TRP   A CZ3 1 
ATOM   1984 C  CH2 . TRP   A 1 244 ? -0.963  -13.866 18.013  1.00 16.68 ? 245 TRP   A CH2 1 
ATOM   1985 N  N   . ARG   A 1 245 ? -1.156  -7.289  17.236  1.00 14.02 ? 246 ARG   A N   1 
ATOM   1986 C  CA  . ARG   A 1 245 ? -0.181  -7.195  18.312  1.00 14.34 ? 246 ARG   A CA  1 
ATOM   1987 C  C   . ARG   A 1 245 ? -0.630  -8.087  19.464  1.00 13.72 ? 246 ARG   A C   1 
ATOM   1988 O  O   . ARG   A 1 245 ? -1.800  -8.118  19.802  1.00 14.70 ? 246 ARG   A O   1 
ATOM   1989 C  CB  . ARG   A 1 245 ? -0.091  -5.737  18.778  1.00 14.31 ? 246 ARG   A CB  1 
ATOM   1990 C  CG  . ARG   A 1 245 ? 0.982   -5.529  19.844  1.00 12.77 ? 246 ARG   A CG  1 
ATOM   1991 C  CD  . ARG   A 1 245 ? 0.879   -4.147  20.481  1.00 13.79 ? 246 ARG   A CD  1 
ATOM   1992 N  NE  . ARG   A 1 245 ? 2.161   -3.825  21.150  1.00 15.17 ? 246 ARG   A NE  1 
ATOM   1993 C  CZ  . ARG   A 1 245 ? 2.363   -2.814  22.001  1.00 15.91 ? 246 ARG   A CZ  1 
ATOM   1994 N  NH1 . ARG   A 1 245 ? 1.383   -1.991  22.364  1.00 14.74 ? 246 ARG   A NH1 1 
ATOM   1995 N  NH2 . ARG   A 1 245 ? 3.609   -2.612  22.459  1.00 16.51 ? 246 ARG   A NH2 1 
ATOM   1996 N  N   . PRO   A 1 246 ? 0.252   -8.925  20.066  1.00 14.96 ? 247 PRO   A N   1 
ATOM   1997 C  CA  . PRO   A 1 246 ? -0.129  -9.721  21.228  1.00 14.73 ? 247 PRO   A CA  1 
ATOM   1998 C  C   . PRO   A 1 246 ? -0.417  -8.913  22.494  1.00 14.36 ? 247 PRO   A C   1 
ATOM   1999 O  O   . PRO   A 1 246 ? -0.127  -7.708  22.587  1.00 13.84 ? 247 PRO   A O   1 
ATOM   2000 C  CB  . PRO   A 1 246 ? 1.131   -10.548 21.542  1.00 17.74 ? 247 PRO   A CB  1 
ATOM   2001 C  CG  . PRO   A 1 246 ? 2.060   -10.346 20.395  1.00 20.47 ? 247 PRO   A CG  1 
ATOM   2002 C  CD  . PRO   A 1 246 ? 1.683   -9.034  19.736  1.00 17.08 ? 247 PRO   A CD  1 
ATOM   2003 N  N   . ALA   A 1 247 ? -1.090  -9.591  23.444  1.00 15.08 ? 248 ALA   A N   1 
ATOM   2004 C  CA  . ALA   A 1 247 ? -1.424  -8.999  24.738  1.00 13.99 ? 248 ALA   A CA  1 
ATOM   2005 C  C   . ALA   A 1 247 ? -0.197  -8.434  25.471  1.00 15.63 ? 248 ALA   A C   1 
ATOM   2006 O  O   . ALA   A 1 247 ? 0.858   -9.057  25.507  1.00 17.27 ? 248 ALA   A O   1 
ATOM   2007 C  CB  . ALA   A 1 247 ? -2.200  -10.007 25.565  1.00 16.37 ? 248 ALA   A CB  1 
ATOM   2008 N  N   . GLN   A 1 248 ? -0.375  -7.240  26.045  1.00 14.68 ? 249 GLN   A N   1 
ATOM   2009 C  CA  . GLN   A 1 248 ? 0.684   -6.510  26.728  1.00 15.78 ? 249 GLN   A CA  1 
ATOM   2010 C  C   . GLN   A 1 248 ? 0.398   -6.517  28.230  1.00 17.74 ? 249 GLN   A C   1 
ATOM   2011 O  O   . GLN   A 1 248 ? -0.753  -6.731  28.663  1.00 17.42 ? 249 GLN   A O   1 
ATOM   2012 C  CB  . GLN   A 1 248 ? 0.718   -5.078  26.195  1.00 14.03 ? 249 GLN   A CB  1 
ATOM   2013 C  CG  . GLN   A 1 248 ? 1.038   -4.985  24.706  1.00 14.41 ? 249 GLN   A CG  1 
ATOM   2014 C  CD  . GLN   A 1 248 ? 2.360   -5.664  24.384  1.00 16.65 ? 249 GLN   A CD  1 
ATOM   2015 O  OE1 . GLN   A 1 248 ? 3.376   -5.370  25.023  1.00 18.57 ? 249 GLN   A OE1 1 
ATOM   2016 N  NE2 . GLN   A 1 248 ? 2.354   -6.609  23.456  1.00 15.73 ? 249 GLN   A NE2 1 
ATOM   2017 N  N   . PRO   A 1 249 ? 1.398   -6.242  29.100  1.00 16.29 ? 250 PRO   A N   1 
ATOM   2018 C  CA  . PRO   A 1 249 ? 1.139   -6.278  30.536  1.00 18.23 ? 250 PRO   A CA  1 
ATOM   2019 C  C   . PRO   A 1 249 ? 0.090   -5.259  30.973  1.00 17.21 ? 250 PRO   A C   1 
ATOM   2020 O  O   . PRO   A 1 249 ? 0.116   -4.079  30.584  1.00 18.32 ? 250 PRO   A O   1 
ATOM   2021 C  CB  . PRO   A 1 249 ? 2.523   -5.835  31.087  1.00 19.35 ? 250 PRO   A CB  1 
ATOM   2022 C  CG  . PRO   A 1 249 ? 3.508   -6.291  30.046  1.00 20.44 ? 250 PRO   A CG  1 
ATOM   2023 C  CD  . PRO   A 1 249 ? 2.799   -5.930  28.753  1.00 20.52 ? 250 PRO   A CD  1 
ATOM   2024 N  N   . LEU   A 1 250 ? -0.809  -5.721  31.863  1.00 18.33 ? 251 LEU   A N   1 
ATOM   2025 C  CA  . LEU   A 1 250 ? -1.883  -4.889  32.377  1.00 18.47 ? 251 LEU   A CA  1 
ATOM   2026 C  C   . LEU   A 1 250 ? -1.318  -3.819  33.309  1.00 17.32 ? 251 LEU   A C   1 
ATOM   2027 O  O   . LEU   A 1 250 ? -1.821  -2.692  33.344  1.00 15.47 ? 251 LEU   A O   1 
ATOM   2028 C  CB  . LEU   A 1 250 ? -2.911  -5.784  33.074  1.00 20.06 ? 251 LEU   A CB  1 
ATOM   2029 C  CG  . LEU   A 1 250 ? -4.179  -5.063  33.523  1.00 20.83 ? 251 LEU   A CG  1 
ATOM   2030 C  CD1 . LEU   A 1 250 ? -4.942  -4.489  32.342  1.00 19.75 ? 251 LEU   A CD1 1 
ATOM   2031 C  CD2 . LEU   A 1 250 ? -5.044  -6.071  34.272  1.00 24.05 ? 251 LEU   A CD2 1 
ATOM   2032 N  N   . LYS   A 1 251 ? -0.272  -4.156  34.077  1.00 19.01 ? 252 LYS   A N   1 
ATOM   2033 C  CA  . LYS   A 1 251 ? 0.355   -3.130  34.921  1.00 19.07 ? 252 LYS   A CA  1 
ATOM   2034 C  C   . LYS   A 1 251 ? -0.654  -2.580  35.927  1.00 20.12 ? 252 LYS   A C   1 
ATOM   2035 O  O   . LYS   A 1 251 ? -1.447  -3.351  36.489  1.00 23.30 ? 252 LYS   A O   1 
ATOM   2036 C  CB  . LYS   A 1 251 ? 1.134   -2.093  34.096  1.00 20.73 ? 252 LYS   A CB  1 
ATOM   2037 C  CG  . LYS   A 1 251 ? 2.373   -2.722  33.442  1.00 26.19 ? 252 LYS   A CG  1 
ATOM   2038 C  CD  . LYS   A 1 251 ? 3.263   -1.769  32.722  1.00 28.21 ? 252 LYS   A CD  1 
ATOM   2039 C  CE  . LYS   A 1 251 ? 4.590   -2.406  32.365  1.00 30.10 ? 252 LYS   A CE  1 
ATOM   2040 N  NZ  . LYS   A 1 251 ? 5.388   -1.473  31.530  1.00 32.37 ? 252 LYS   A NZ  1 
ATOM   2041 N  N   . ASN   A 1 252 ? -0.639  -1.261  36.103  1.00 18.94 ? 253 ASN   A N   1 
ATOM   2042 C  CA  . ASN   A 1 252 ? -1.473  -0.714  37.160  1.00 24.71 ? 253 ASN   A CA  1 
ATOM   2043 C  C   . ASN   A 1 252 ? -2.819  -0.281  36.581  1.00 25.42 ? 253 ASN   A C   1 
ATOM   2044 O  O   . ASN   A 1 252 ? -3.044  0.953   36.555  1.00 30.88 ? 253 ASN   A O   1 
ATOM   2045 C  CB  . ASN   A 1 252 ? -0.796  0.491   37.842  1.00 31.07 ? 253 ASN   A CB  1 
ATOM   2046 C  CG  . ASN   A 1 252 ? -1.512  0.936   39.105  1.00 38.72 ? 253 ASN   A CG  1 
ATOM   2047 O  OD1 . ASN   A 1 252 ? -1.956  0.109   39.899  1.00 44.52 ? 253 ASN   A OD1 1 
ATOM   2048 N  ND2 . ASN   A 1 252 ? -1.649  2.240   39.302  1.00 45.67 ? 253 ASN   A ND2 1 
ATOM   2049 N  N   . ARG   A 1 253 ? -3.598  -1.268  36.037  1.00 20.78 ? 254 ARG   A N   1 
ATOM   2050 C  CA  . ARG   A 1 253 ? -4.897  -0.950  35.456  1.00 16.85 ? 254 ARG   A CA  1 
ATOM   2051 C  C   . ARG   A 1 253 ? -5.952  -1.959  35.878  1.00 20.34 ? 254 ARG   A C   1 
ATOM   2052 O  O   . ARG   A 1 253 ? -5.659  -3.132  36.107  1.00 22.69 ? 254 ARG   A O   1 
ATOM   2053 C  CB  . ARG   A 1 253 ? -4.916  -0.868  33.915  1.00 15.97 ? 254 ARG   A CB  1 
ATOM   2054 C  CG  . ARG   A 1 253 ? -3.984  0.221   33.391  1.00 14.09 ? 254 ARG   A CG  1 
ATOM   2055 C  CD  . ARG   A 1 253 ? -3.860  0.228   31.859  1.00 15.34 ? 254 ARG   A CD  1 
ATOM   2056 N  NE  . ARG   A 1 253 ? -3.018  -0.905  31.417  1.00 14.45 ? 254 ARG   A NE  1 
ATOM   2057 C  CZ  . ARG   A 1 253 ? -2.729  -1.201  30.141  1.00 13.26 ? 254 ARG   A CZ  1 
ATOM   2058 N  NH1 . ARG   A 1 253 ? -3.370  -0.539  29.182  1.00 14.49 ? 254 ARG   A NH1 1 
ATOM   2059 N  NH2 . ARG   A 1 253 ? -1.911  -2.224  29.848  1.00 13.47 ? 254 ARG   A NH2 1 
ATOM   2060 N  N   . GLN   A 1 254 ? -7.195  -1.443  35.968  1.00 18.38 ? 255 GLN   A N   1 
ATOM   2061 C  CA  . GLN   A 1 254 ? -8.375  -2.232  36.246  1.00 20.93 ? 255 GLN   A CA  1 
ATOM   2062 C  C   . GLN   A 1 254 ? -9.242  -2.201  34.993  1.00 20.19 ? 255 GLN   A C   1 
ATOM   2063 O  O   . GLN   A 1 254 ? -9.463  -1.120  34.409  1.00 22.41 ? 255 GLN   A O   1 
ATOM   2064 C  CB  . GLN   A 1 254 ? -9.186  -1.561  37.358  1.00 26.12 ? 255 GLN   A CB  1 
ATOM   2065 C  CG  . GLN   A 1 254 ? -8.469  -1.473  38.702  1.00 41.19 ? 255 GLN   A CG  1 
ATOM   2066 C  CD  . GLN   A 1 254 ? -9.412  -1.834  39.829  1.00 53.58 ? 255 GLN   A CD  1 
ATOM   2067 O  OE1 . GLN   A 1 254 ? -10.432 -2.501  39.614  1.00 60.74 ? 255 GLN   A OE1 1 
ATOM   2068 N  NE2 . GLN   A 1 254 ? -9.075  -1.407  41.041  1.00 52.17 ? 255 GLN   A NE2 1 
ATOM   2069 N  N   . ILE   A 1 255 ? -9.685  -3.396  34.597  1.00 16.96 ? 256 ILE   A N   1 
ATOM   2070 C  CA  . ILE   A 1 255 ? -10.682 -3.530  33.544  1.00 16.19 ? 256 ILE   A CA  1 
ATOM   2071 C  C   . ILE   A 1 255 ? -12.061 -3.561  34.214  1.00 15.34 ? 256 ILE   A C   1 
ATOM   2072 O  O   . ILE   A 1 255 ? -12.271 -4.289  35.211  1.00 16.72 ? 256 ILE   A O   1 
ATOM   2073 C  CB  . ILE   A 1 255 ? -10.450 -4.815  32.726  1.00 16.39 ? 256 ILE   A CB  1 
ATOM   2074 C  CG1 . ILE   A 1 255 ? -9.039  -4.788  32.129  1.00 18.33 ? 256 ILE   A CG1 1 
ATOM   2075 C  CG2 . ILE   A 1 255 ? -11.550 -4.963  31.649  1.00 17.39 ? 256 ILE   A CG2 1 
ATOM   2076 C  CD1 . ILE   A 1 255 ? -8.700  -6.011  31.300  1.00 18.93 ? 256 ILE   A CD1 1 
ATOM   2077 N  N   . LYS   A 1 256 ? -12.951 -2.683  33.728  1.00 13.87 ? 257 LYS   A N   1 
ATOM   2078 C  CA  . LYS   A 1 256 ? -14.299 -2.578  34.297  1.00 14.22 ? 257 LYS   A CA  1 
ATOM   2079 C  C   . LYS   A 1 256 ? -15.323 -3.201  33.368  1.00 14.75 ? 257 LYS   A C   1 
ATOM   2080 O  O   . LYS   A 1 256 ? -15.162 -3.134  32.150  1.00 15.43 ? 257 LYS   A O   1 
ATOM   2081 C  CB  . LYS   A 1 256 ? -14.611 -1.097  34.535  1.00 15.61 ? 257 LYS   A CB  1 
ATOM   2082 C  CG  . LYS   A 1 256 ? -13.744 -0.431  35.620  1.00 19.37 ? 257 LYS   A CG  1 
ATOM   2083 C  CD  . LYS   A 1 256 ? -13.884 1.073   35.674  0.01 17.69 ? 257 LYS   A CD  1 
ATOM   2084 N  N   . ALA   A 1 257 ? -16.339 -3.881  33.891  1.00 16.90 ? 258 ALA   A N   1 
ATOM   2085 C  CA  . ALA   A 1 257 ? -17.426 -4.465  33.108  1.00 16.34 ? 258 ALA   A CA  1 
ATOM   2086 C  C   . ALA   A 1 257 ? -18.700 -3.644  33.270  1.00 17.78 ? 258 ALA   A C   1 
ATOM   2087 O  O   . ALA   A 1 257 ? -19.041 -3.218  34.392  1.00 17.99 ? 258 ALA   A O   1 
ATOM   2088 C  CB  . ALA   A 1 257 ? -17.655 -5.927  33.474  1.00 18.02 ? 258 ALA   A CB  1 
ATOM   2089 N  N   . SER   A 1 258 ? -19.468 -3.537  32.181  1.00 15.88 ? 259 SER   A N   1 
ATOM   2090 C  CA  . SER   A 1 258 ? -20.737 -2.831  32.171  1.00 18.03 ? 259 SER   A CA  1 
ATOM   2091 C  C   . SER   A 1 258 ? -21.861 -3.761  32.614  1.00 17.48 ? 259 SER   A C   1 
ATOM   2092 O  O   . SER   A 1 258 ? -22.974 -3.282  32.763  1.00 22.61 ? 259 SER   A O   1 
ATOM   2093 C  CB  . SER   A 1 258 ? -21.049 -2.261  30.792  1.00 16.77 ? 259 SER   A CB  1 
ATOM   2094 O  OG  . SER   A 1 258 ? -21.458 -3.290  29.897  1.00 17.95 ? 259 SER   A OG  1 
ATOM   2095 N  N   . PHE   A 1 259 ? -21.570 -5.024  32.882  1.00 18.87 ? 260 PHE   A N   1 
ATOM   2096 C  CA  . PHE   A 1 259 ? -22.593 -6.045  33.097  1.00 20.85 ? 260 PHE   A CA  1 
ATOM   2097 C  C   . PHE   A 1 259 ? -22.116 -6.966  34.215  1.00 27.13 ? 260 PHE   A C   1 
ATOM   2098 O  O   . PHE   A 1 259 ? -20.914 -7.135  34.443  1.00 24.08 ? 260 PHE   A O   1 
ATOM   2099 C  CB  . PHE   A 1 259 ? -22.791 -6.866  31.814  1.00 21.67 ? 260 PHE   A CB  1 
ATOM   2100 C  CG  . PHE   A 1 259 ? -21.517 -7.570  31.375  1.00 21.86 ? 260 PHE   A CG  1 
ATOM   2101 C  CD1 . PHE   A 1 259 ? -20.563 -6.925  30.594  1.00 20.58 ? 260 PHE   A CD1 1 
ATOM   2102 C  CD2 . PHE   A 1 259 ? -21.243 -8.857  31.808  1.00 24.29 ? 260 PHE   A CD2 1 
ATOM   2103 C  CE1 . PHE   A 1 259 ? -19.387 -7.572  30.223  1.00 21.42 ? 260 PHE   A CE1 1 
ATOM   2104 C  CE2 . PHE   A 1 259 ? -20.067 -9.495  31.445  1.00 25.44 ? 260 PHE   A CE2 1 
ATOM   2105 C  CZ  . PHE   A 1 259 ? -19.121 -8.847  30.674  1.00 23.98 ? 260 PHE   A CZ  1 
ATOM   2106 N  N   . LYS   A 1 260 ? -23.084 -7.599  34.893  1.00 38.24 ? 261 LYS   A N   1 
ATOM   2107 C  CA  . LYS   A 1 260 ? -22.740 -8.647  35.842  1.00 49.89 ? 261 LYS   A CA  1 
ATOM   2108 C  C   . LYS   A 1 260 ? -23.034 -10.027 35.230  1.00 59.91 ? 261 LYS   A C   1 
ATOM   2109 O  O   . LYS   A 1 260 ? -23.824 -10.252 34.283  1.00 60.26 ? 261 LYS   A O   1 
ATOM   2110 C  CB  . LYS   A 1 260 ? -23.325 -8.402  37.243  1.00 55.99 ? 261 LYS   A CB  1 
ATOM   2111 C  CG  . LYS   A 1 260 ? -24.692 -7.727  37.314  1.00 61.40 ? 261 LYS   A CG  1 
ATOM   2112 C  CD  . LYS   A 1 260 ? -25.394 -7.861  38.667  1.00 63.36 ? 261 LYS   A CD  1 
ATOM   2113 C  CE  . LYS   A 1 260 ? -24.471 -7.720  39.862  1.00 69.05 ? 261 LYS   A CE  1 
ATOM   2114 N  NZ  . LYS   A 1 260 ? -25.213 -7.361  41.097  1.00 69.49 ? 261 LYS   A NZ  1 
ATOM   2115 O  OXT . LYS   A 1 260 ? -22.422 -10.989 35.697  1.00 68.95 ? 261 LYS   A OXT 1 
HETATM 2116 ZN ZN  . ZN    B 2 .   ? -6.753  -1.809  15.418  1.00 12.65 ? 301 ZN    A ZN  1 
HETATM 2117 C  C1  . A1IEL C 3 .   ? -4.240  0.253   12.181  1.00 16.08 ? 302 A1IEL A C1  1 
HETATM 2118 C  C2  . A1IEL C 3 .   ? -4.475  0.105   13.555  1.00 15.05 ? 302 A1IEL A C2  1 
HETATM 2119 C  C3  . A1IEL C 3 .   ? -5.003  1.155   14.314  1.00 16.44 ? 302 A1IEL A C3  1 
HETATM 2120 C  C4  . A1IEL C 3 .   ? -5.225  2.415   13.689  1.00 18.16 ? 302 A1IEL A C4  1 
HETATM 2121 C  C5  . A1IEL C 3 .   ? -4.912  2.558   12.301  1.00 17.97 ? 302 A1IEL A C5  1 
HETATM 2122 C  C6  . A1IEL C 3 .   ? -4.423  1.477   11.553  1.00 18.21 ? 302 A1IEL A C6  1 
HETATM 2123 C  C9  . A1IEL C 3 .   ? -3.045  -3.149  11.430  1.00 19.87 ? 302 A1IEL A C9  1 
HETATM 2124 C  C16 . A1IEL C 3 .   ? -5.554  5.287   13.617  1.00 27.27 ? 302 A1IEL A C16 1 
HETATM 2125 C  C20 . A1IEL C 3 .   ? -3.728  6.720   12.623  1.00 34.84 ? 302 A1IEL A C20 1 
HETATM 2126 O  O14 . A1IEL C 3 .   ? -4.238  1.409   16.885  1.00 17.13 ? 302 A1IEL A O14 1 
HETATM 2127 S  S11 . A1IEL C 3 .   ? -5.369  0.903   16.038  1.00 16.01 ? 302 A1IEL A S11 1 
HETATM 2128 O  O12 . A1IEL C 3 .   ? -6.697  1.476   16.339  1.00 17.93 ? 302 A1IEL A O12 1 
HETATM 2129 N  N13 . A1IEL C 3 .   ? -5.383  -0.756  16.227  1.00 13.37 ? 302 A1IEL A N13 1 
HETATM 2130 C  C7  . A1IEL C 3 .   ? -3.733  -0.870  11.481  1.00 15.65 ? 302 A1IEL A C7  1 
HETATM 2131 O  O10 . A1IEL C 3 .   ? -3.470  -0.797  10.249  1.00 20.75 ? 302 A1IEL A O10 1 
HETATM 2132 O  O8  . A1IEL C 3 .   ? -3.571  -2.020  12.101  1.00 17.30 ? 302 A1IEL A O8  1 
HETATM 2133 S  S15 . A1IEL C 3 .   ? -5.888  3.799   14.653  1.00 18.94 ? 302 A1IEL A S15 1 
HETATM 2134 C  C17 . A1IEL C 3 .   ? -4.102  5.674   13.484  1.00 29.10 ? 302 A1IEL A C17 1 
HETATM 2135 C  C21 . A1IEL C 3 .   ? -2.354  7.052   12.522  1.00 34.12 ? 302 A1IEL A C21 1 
HETATM 2136 C  C22 . A1IEL C 3 .   ? -1.380  6.302   13.220  1.00 37.44 ? 302 A1IEL A C22 1 
HETATM 2137 C  C19 . A1IEL C 3 .   ? -1.741  5.202   14.062  1.00 32.10 ? 302 A1IEL A C19 1 
HETATM 2138 C  C18 . A1IEL C 3 .   ? -3.115  4.902   14.181  1.00 28.25 ? 302 A1IEL A C18 1 
HETATM 2139 N  N1  . BCN   D 4 .   ? -20.739 -14.826 23.615  1.00 49.00 ? 303 BCN   A N1  1 
HETATM 2140 C  C1  . BCN   D 4 .   ? -19.816 -14.315 24.636  1.00 44.00 ? 303 BCN   A C1  1 
HETATM 2141 C  C2  . BCN   D 4 .   ? -19.882 -15.313 25.789  1.00 47.36 ? 303 BCN   A C2  1 
HETATM 2142 O  O21 . BCN   D 4 .   ? -20.546 -16.358 25.590  1.00 51.47 ? 303 BCN   A O21 1 
HETATM 2143 O  O22 . BCN   D 4 .   ? -19.265 -15.035 26.836  1.00 48.82 ? 303 BCN   A O22 1 
HETATM 2144 C  C3  . BCN   D 4 .   ? -21.725 -13.826 23.163  1.00 40.16 ? 303 BCN   A C3  1 
HETATM 2145 C  C4  . BCN   D 4 .   ? -22.895 -13.504 24.081  1.00 51.01 ? 303 BCN   A C4  1 
HETATM 2146 O  O4  . BCN   D 4 .   ? -22.585 -12.518 25.068  1.00 47.10 ? 303 BCN   A O4  1 
HETATM 2147 C  C5  . BCN   D 4 .   ? -20.086 -15.711 22.631  1.00 39.41 ? 303 BCN   A C5  1 
HETATM 2148 C  C6  . BCN   D 4 .   ? -20.983 -16.751 21.991  1.00 57.72 ? 303 BCN   A C6  1 
HETATM 2149 O  O6  . BCN   D 4 .   ? -20.947 -16.688 20.565  1.00 53.04 ? 303 BCN   A O6  1 
HETATM 2150 S  S   . DMS   E 5 .   ? 1.422   -11.736 14.945  1.00 48.98 ? 304 DMS   A S   1 
HETATM 2151 O  O   . DMS   E 5 .   ? 1.764   -13.245 14.871  1.00 48.32 ? 304 DMS   A O   1 
HETATM 2152 C  C1  . DMS   E 5 .   ? 2.548   -10.965 13.773  1.00 38.58 ? 304 DMS   A C1  1 
HETATM 2153 C  C2  . DMS   E 5 .   ? 2.118   -11.178 16.472  1.00 39.67 ? 304 DMS   A C2  1 
HETATM 2154 O  O   . HOH   F 6 .   ? -1.016  -17.832 17.870  1.00 37.17 ? 401 HOH   A O   1 
HETATM 2155 O  O   . HOH   F 6 .   ? 12.288  -0.455  11.942  1.00 41.76 ? 402 HOH   A O   1 
HETATM 2156 O  O   . HOH   F 6 .   ? -19.269 14.008  9.074   1.00 38.75 ? 403 HOH   A O   1 
HETATM 2157 O  O   . HOH   F 6 .   ? 9.045   -9.987  13.475  1.00 24.81 ? 404 HOH   A O   1 
HETATM 2158 O  O   . HOH   F 6 .   ? -13.043 13.382  31.935  1.00 36.64 ? 405 HOH   A O   1 
HETATM 2159 O  O   . HOH   F 6 .   ? -2.373  22.128  21.717  1.00 43.28 ? 406 HOH   A O   1 
HETATM 2160 O  O   . HOH   F 6 .   ? -4.949  2.324   37.504  1.00 35.60 ? 407 HOH   A O   1 
HETATM 2161 O  O   . HOH   F 6 .   ? 6.496   -5.715  3.855   1.00 36.73 ? 408 HOH   A O   1 
HETATM 2162 O  O   . HOH   F 6 .   ? -20.615 8.387   30.206  1.00 30.79 ? 409 HOH   A O   1 
HETATM 2163 O  O   . HOH   F 6 .   ? -27.141 -12.835 20.319  1.00 36.39 ? 410 HOH   A O   1 
HETATM 2164 O  O   . HOH   F 6 .   ? -25.751 -10.707 17.997  1.00 29.59 ? 411 HOH   A O   1 
HETATM 2165 O  O   . HOH   F 6 .   ? -6.134  -11.368 36.680  1.00 37.98 ? 412 HOH   A O   1 
HETATM 2166 O  O   . HOH   F 6 .   ? -24.275 8.589   20.233  1.00 27.90 ? 413 HOH   A O   1 
HETATM 2167 O  O   . HOH   F 6 .   ? -10.476 -18.337 17.143  1.00 19.83 ? 414 HOH   A O   1 
HETATM 2168 O  O   . HOH   F 6 .   ? -2.757  -19.323 6.428   1.00 35.68 ? 415 HOH   A O   1 
HETATM 2169 O  O   . HOH   F 6 .   ? -21.998 -14.294 18.803  1.00 31.27 ? 416 HOH   A O   1 
HETATM 2170 O  O   . HOH   F 6 .   ? -7.150  5.996   6.036   1.00 24.38 ? 417 HOH   A O   1 
HETATM 2171 O  O   . HOH   F 6 .   ? -4.799  -12.002 32.206  1.00 27.77 ? 418 HOH   A O   1 
HETATM 2172 O  O   . HOH   F 6 .   ? -13.266 -22.485 11.873  1.00 42.95 ? 419 HOH   A O   1 
HETATM 2173 O  O   . HOH   F 6 .   ? -8.791  -3.833  7.905   1.00 14.35 ? 420 HOH   A O   1 
HETATM 2174 O  O   . HOH   F 6 .   ? -6.724  -14.911 31.732  1.00 27.87 ? 421 HOH   A O   1 
HETATM 2175 O  O   . HOH   F 6 .   ? -14.259 -16.756 29.286  1.00 29.46 ? 422 HOH   A O   1 
HETATM 2176 O  O   . HOH   F 6 .   ? 7.547   -8.244  -1.257  1.00 32.55 ? 423 HOH   A O   1 
HETATM 2177 O  O   . HOH   F 6 .   ? -15.388 -10.504 37.333  1.00 42.97 ? 424 HOH   A O   1 
HETATM 2178 O  O   . HOH   F 6 .   ? -6.293  -4.763  -6.536  1.00 27.75 ? 425 HOH   A O   1 
HETATM 2179 O  O   . HOH   F 6 .   ? -12.371 12.580  29.545  1.00 37.08 ? 426 HOH   A O   1 
HETATM 2180 O  O   . HOH   F 6 .   ? 11.207  -6.994  22.639  1.00 34.22 ? 427 HOH   A O   1 
HETATM 2181 O  O   . HOH   F 6 .   ? -15.049 20.028  17.765  1.00 22.97 ? 428 HOH   A O   1 
HETATM 2182 O  O   . HOH   F 6 .   ? -9.178  6.711   -4.072  1.00 33.94 ? 429 HOH   A O   1 
HETATM 2183 O  O   . HOH   F 6 .   ? -16.851 -14.035 26.606  1.00 26.11 ? 430 HOH   A O   1 
HETATM 2184 O  O   . HOH   F 6 .   ? -1.319  -4.093  15.793  1.00 15.75 ? 431 HOH   A O   1 
HETATM 2185 O  O   . HOH   F 6 .   ? -14.202 14.292  27.264  1.00 27.05 ? 432 HOH   A O   1 
HETATM 2186 O  O   . HOH   F 6 .   ? -18.358 -12.385 -3.553  1.00 36.44 ? 433 HOH   A O   1 
HETATM 2187 O  O   . HOH   F 6 .   ? 3.572   5.096   29.905  1.00 24.65 ? 434 HOH   A O   1 
HETATM 2188 O  O   . HOH   F 6 .   ? -15.931 3.451   35.385  1.00 42.87 ? 435 HOH   A O   1 
HETATM 2189 O  O   . HOH   F 6 .   ? -13.095 -22.229 8.618   1.00 28.96 ? 436 HOH   A O   1 
HETATM 2190 O  O   . HOH   F 6 .   ? -0.518  14.150  16.281  1.00 33.92 ? 437 HOH   A O   1 
HETATM 2191 O  O   . HOH   F 6 .   ? -18.055 10.506  11.334  1.00 23.23 ? 438 HOH   A O   1 
HETATM 2192 O  O   . HOH   F 6 .   ? 11.559  -0.628  16.071  1.00 32.71 ? 439 HOH   A O   1 
HETATM 2193 O  O   . HOH   F 6 .   ? -11.117 -15.339 34.308  1.00 35.24 ? 440 HOH   A O   1 
HETATM 2194 O  O   . HOH   F 6 .   ? -15.819 8.804   -2.134  1.00 33.68 ? 441 HOH   A O   1 
HETATM 2195 O  O   . HOH   F 6 .   ? 2.552   1.067   -2.242  1.00 40.59 ? 442 HOH   A O   1 
HETATM 2196 O  O   . HOH   F 6 .   ? -20.037 -16.923 2.987   1.00 28.72 ? 443 HOH   A O   1 
HETATM 2197 O  O   . HOH   F 6 .   ? 2.466   -11.508 9.487   1.00 27.52 ? 444 HOH   A O   1 
HETATM 2198 O  O   . HOH   F 6 .   ? -10.475 13.364  8.951   1.00 44.67 ? 445 HOH   A O   1 
HETATM 2199 O  O   . HOH   F 6 .   ? -8.744  0.598   -6.557  1.00 31.15 ? 446 HOH   A O   1 
HETATM 2200 O  O   . HOH   F 6 .   ? -26.030 6.166   27.140  1.00 32.92 ? 447 HOH   A O   1 
HETATM 2201 O  O   . HOH   F 6 .   ? -8.051  -15.525 11.426  1.00 15.81 ? 448 HOH   A O   1 
HETATM 2202 O  O   . HOH   F 6 .   ? 6.246   -11.263 15.526  1.00 34.22 ? 449 HOH   A O   1 
HETATM 2203 O  O   . HOH   F 6 .   ? -0.076  1.235   34.609  1.00 35.61 ? 450 HOH   A O   1 
HETATM 2204 O  O   . HOH   F 6 .   ? -14.908 9.408   31.536  1.00 40.50 ? 451 HOH   A O   1 
HETATM 2205 O  O   . HOH   F 6 .   ? 4.267   -3.496  26.719  1.00 27.53 ? 452 HOH   A O   1 
HETATM 2206 O  O   . HOH   F 6 .   ? -6.900  -20.326 19.706  1.00 22.73 ? 453 HOH   A O   1 
HETATM 2207 O  O   . HOH   F 6 .   ? -25.438 9.504   13.060  1.00 36.42 ? 454 HOH   A O   1 
HETATM 2208 O  O   . HOH   F 6 .   ? -10.669 -19.518 20.003  1.00 28.27 ? 455 HOH   A O   1 
HETATM 2209 O  O   . HOH   F 6 .   ? -17.117 -8.444  20.549  1.00 14.67 ? 456 HOH   A O   1 
HETATM 2210 O  O   . HOH   F 6 .   ? -22.920 -5.979  2.847   1.00 27.09 ? 457 HOH   A O   1 
HETATM 2211 O  O   . HOH   F 6 .   ? -11.742 10.857  6.911   1.00 41.79 ? 458 HOH   A O   1 
HETATM 2212 O  O   . HOH   F 6 .   ? -21.282 7.731   1.937   1.00 25.13 ? 459 HOH   A O   1 
HETATM 2213 O  O   . HOH   F 6 .   ? 0.295   -19.577 10.933  1.00 37.83 ? 460 HOH   A O   1 
HETATM 2214 O  O   . HOH   F 6 .   ? 15.680  2.820   20.897  1.00 34.57 ? 461 HOH   A O   1 
HETATM 2215 O  O   . HOH   F 6 .   ? -27.713 2.859   23.784  1.00 35.98 ? 462 HOH   A O   1 
HETATM 2216 O  O   . HOH   F 6 .   ? -16.370 5.214   -8.268  1.00 33.87 ? 463 HOH   A O   1 
HETATM 2217 O  O   . HOH   F 6 .   ? -3.551  -11.164 20.975  1.00 16.42 ? 464 HOH   A O   1 
HETATM 2218 O  O   . HOH   F 6 .   ? -9.322  5.826   29.311  1.00 36.54 ? 465 HOH   A O   1 
HETATM 2219 O  O   . HOH   F 6 .   ? -16.225 15.830  23.792  1.00 23.69 ? 466 HOH   A O   1 
HETATM 2220 O  O   . HOH   F 6 .   ? -15.448 -21.921 13.150  1.00 27.37 ? 467 HOH   A O   1 
HETATM 2221 O  O   . HOH   F 6 .   ? 0.057   -1.176  -4.743  1.00 21.30 ? 468 HOH   A O   1 
HETATM 2222 O  O   . HOH   F 6 .   ? -4.607  -13.542 18.125  1.00 15.12 ? 469 HOH   A O   1 
HETATM 2223 O  O   . HOH   F 6 .   ? -10.641 8.697   25.639  1.00 16.22 ? 470 HOH   A O   1 
HETATM 2224 O  O   . HOH   F 6 .   ? 2.148   8.183   27.776  1.00 36.46 ? 471 HOH   A O   1 
HETATM 2225 O  O   . HOH   F 6 .   ? 4.778   -3.483  3.063   1.00 29.96 ? 472 HOH   A O   1 
HETATM 2226 O  O   . HOH   F 6 .   ? -18.700 -21.318 14.859  1.00 32.38 ? 473 HOH   A O   1 
HETATM 2227 O  O   . HOH   F 6 .   ? -0.415  -20.791 15.113  1.00 44.11 ? 474 HOH   A O   1 
HETATM 2228 O  O   . HOH   F 6 .   ? -0.536  10.896  23.526  1.00 25.83 ? 475 HOH   A O   1 
HETATM 2229 O  O   . HOH   F 6 .   ? -1.221  9.331   28.072  1.00 28.34 ? 476 HOH   A O   1 
HETATM 2230 O  O   . HOH   F 6 .   ? -14.689 -18.648 18.902  1.00 23.55 ? 477 HOH   A O   1 
HETATM 2231 O  O   . HOH   F 6 .   ? -11.026 0.998   33.695  1.00 33.03 ? 478 HOH   A O   1 
HETATM 2232 O  O   . HOH   F 6 .   ? -17.345 -16.324 22.109  1.00 29.25 ? 479 HOH   A O   1 
HETATM 2233 O  O   . HOH   F 6 .   ? -18.411 -3.783  -2.596  1.00 32.80 ? 480 HOH   A O   1 
HETATM 2234 O  O   . HOH   F 6 .   ? -9.626  15.667  30.074  1.00 43.71 ? 481 HOH   A O   1 
HETATM 2235 O  O   . HOH   F 6 .   ? -19.732 -4.436  41.468  1.00 38.03 ? 482 HOH   A O   1 
HETATM 2236 O  O   . HOH   F 6 .   ? -13.889 10.368  27.993  1.00 22.51 ? 483 HOH   A O   1 
HETATM 2237 O  O   . HOH   F 6 .   ? -3.798  -13.093 -2.803  1.00 24.60 ? 484 HOH   A O   1 
HETATM 2238 O  O   . HOH   F 6 .   ? 1.921   -15.805 9.477   1.00 33.71 ? 485 HOH   A O   1 
HETATM 2239 O  O   . HOH   F 6 .   ? 3.745   -2.892  5.192   1.00 43.36 ? 486 HOH   A O   1 
HETATM 2240 O  O   . HOH   F 6 .   ? 15.873  3.408   15.545  1.00 29.63 ? 487 HOH   A O   1 
HETATM 2241 O  O   . HOH   F 6 .   ? -26.089 -6.172  13.188  1.00 46.12 ? 488 HOH   A O   1 
HETATM 2242 O  O   . HOH   F 6 .   ? -21.978 5.549   4.803   1.00 19.53 ? 489 HOH   A O   1 
HETATM 2243 O  O   . HOH   F 6 .   ? -16.125 -12.402 24.487  1.00 19.69 ? 490 HOH   A O   1 
HETATM 2244 O  O   . HOH   F 6 .   ? 2.546   -13.241 5.296   1.00 28.98 ? 491 HOH   A O   1 
HETATM 2245 O  O   . HOH   F 6 .   ? -20.387 10.734  26.879  1.00 21.56 ? 492 HOH   A O   1 
HETATM 2246 O  O   . HOH   F 6 .   ? -2.032  -4.853  -7.137  1.00 40.42 ? 493 HOH   A O   1 
HETATM 2247 O  O   . HOH   F 6 .   ? -4.280  -8.535  31.305  1.00 27.83 ? 494 HOH   A O   1 
HETATM 2248 O  O   . HOH   F 6 .   ? -21.660 -7.255  23.783  1.00 16.70 ? 495 HOH   A O   1 
HETATM 2249 O  O   . HOH   F 6 .   ? 13.008  -5.854  24.604  1.00 30.65 ? 496 HOH   A O   1 
HETATM 2250 O  O   . HOH   F 6 .   ? -18.050 20.665  8.012   1.00 18.83 ? 497 HOH   A O   1 
HETATM 2251 O  O   . HOH   F 6 .   ? -3.382  -13.286 25.304  1.00 17.26 ? 498 HOH   A O   1 
HETATM 2252 O  O   . HOH   F 6 .   ? 2.370   1.300   4.568   1.00 39.51 ? 499 HOH   A O   1 
HETATM 2253 O  O   . HOH   F 6 .   ? -25.645 -3.261  32.053  1.00 40.92 ? 500 HOH   A O   1 
HETATM 2254 O  O   . HOH   F 6 .   ? -22.234 -18.454 13.728  1.00 28.17 ? 501 HOH   A O   1 
HETATM 2255 O  O   . HOH   F 6 .   ? -13.795 19.996  15.125  1.00 23.02 ? 502 HOH   A O   1 
HETATM 2256 O  O   . HOH   F 6 .   ? -23.541 -13.299 11.352  1.00 26.12 ? 503 HOH   A O   1 
HETATM 2257 O  O   . HOH   F 6 .   ? -26.396 -7.726  30.736  1.00 36.14 ? 504 HOH   A O   1 
HETATM 2258 O  O   . HOH   F 6 .   ? -23.353 -3.093  6.720   1.00 25.19 ? 505 HOH   A O   1 
HETATM 2259 O  O   . HOH   F 6 .   ? -2.524  -8.786  29.291  1.00 16.91 ? 506 HOH   A O   1 
HETATM 2260 O  O   . HOH   F 6 .   ? -10.578 20.666  24.992  1.00 25.79 ? 507 HOH   A O   1 
HETATM 2261 O  O   . HOH   F 6 .   ? 1.336   -11.778 25.072  1.00 28.69 ? 508 HOH   A O   1 
HETATM 2262 O  O   . HOH   F 6 .   ? -6.562  -5.263  37.679  1.00 30.21 ? 509 HOH   A O   1 
HETATM 2263 O  O   . HOH   F 6 .   ? -24.103 -2.660  29.233  1.00 32.85 ? 510 HOH   A O   1 
HETATM 2264 O  O   . HOH   F 6 .   ? 4.311   -6.707  7.855   1.00 29.30 ? 511 HOH   A O   1 
HETATM 2265 O  O   . HOH   F 6 .   ? -3.766  -15.940 24.494  1.00 19.70 ? 512 HOH   A O   1 
HETATM 2266 O  O   . HOH   F 6 .   ? -26.977 -2.641  14.479  1.00 26.84 ? 513 HOH   A O   1 
HETATM 2267 O  O   . HOH   F 6 .   ? -25.063 -7.891  9.041   1.00 25.28 ? 514 HOH   A O   1 
HETATM 2268 O  O   . HOH   F 6 .   ? 4.889   -4.914  21.022  1.00 18.97 ? 515 HOH   A O   1 
HETATM 2269 O  O   . HOH   F 6 .   ? 13.469  0.121   24.572  1.00 27.59 ? 516 HOH   A O   1 
HETATM 2270 O  O   . HOH   F 6 .   ? 9.638   7.401   19.050  1.00 46.67 ? 517 HOH   A O   1 
HETATM 2271 O  O   . HOH   F 6 .   ? -8.542  -15.442 36.952  1.00 31.57 ? 518 HOH   A O   1 
HETATM 2272 O  O   . HOH   F 6 .   ? -7.266  -8.698  32.763  1.00 23.60 ? 519 HOH   A O   1 
HETATM 2273 O  O   . HOH   F 6 .   ? 8.518   -3.942  21.237  1.00 18.96 ? 520 HOH   A O   1 
HETATM 2274 O  O   . HOH   F 6 .   ? -23.519 -11.319 17.184  1.00 38.52 ? 521 HOH   A O   1 
HETATM 2275 O  O   . HOH   F 6 .   ? 8.331   3.311   27.869  1.00 35.51 ? 522 HOH   A O   1 
HETATM 2276 O  O   . HOH   F 6 .   ? -24.200 -17.786 6.481   1.00 46.13 ? 523 HOH   A O   1 
HETATM 2277 O  O   . HOH   F 6 .   ? -10.771 8.547   7.715   1.00 24.77 ? 524 HOH   A O   1 
HETATM 2278 O  O   . HOH   F 6 .   ? -12.998 -16.998 26.833  1.00 21.20 ? 525 HOH   A O   1 
HETATM 2279 O  O   . HOH   F 6 .   ? -13.523 -1.010  -6.376  1.00 37.53 ? 526 HOH   A O   1 
HETATM 2280 O  O   . HOH   F 6 .   ? 11.232  1.295   26.098  1.00 32.00 ? 527 HOH   A O   1 
HETATM 2281 O  O   . HOH   F 6 .   ? 1.426   -6.360  34.597  1.00 26.99 ? 528 HOH   A O   1 
HETATM 2282 O  O   . HOH   F 6 .   ? -6.330  -19.787 24.009  1.00 28.28 ? 529 HOH   A O   1 
HETATM 2283 O  O   . HOH   F 6 .   ? -13.039 -9.018  -3.283  1.00 31.57 ? 530 HOH   A O   1 
HETATM 2284 O  O   . HOH   F 6 .   ? -11.116 -19.655 7.176   1.00 32.72 ? 531 HOH   A O   1 
HETATM 2285 O  O   . HOH   F 6 .   ? 5.435   7.198   20.292  1.00 20.91 ? 532 HOH   A O   1 
HETATM 2286 O  O   . HOH   F 6 .   ? -24.065 -0.854  26.659  1.00 24.64 ? 533 HOH   A O   1 
HETATM 2287 O  O   . HOH   F 6 .   ? -9.392  -10.126 -1.192  1.00 27.99 ? 534 HOH   A O   1 
HETATM 2288 O  O   . HOH   F 6 .   ? -22.763 -9.742  25.642  1.00 29.68 ? 535 HOH   A O   1 
HETATM 2289 O  O   . HOH   F 6 .   ? -16.360 -10.017 33.159  1.00 23.14 ? 536 HOH   A O   1 
HETATM 2290 O  O   . HOH   F 6 .   ? -27.528 -7.775  26.448  1.00 41.80 ? 537 HOH   A O   1 
HETATM 2291 O  O   . HOH   F 6 .   ? -19.441 9.959   8.951   1.00 19.61 ? 538 HOH   A O   1 
HETATM 2292 O  O   . HOH   F 6 .   ? -14.215 -21.656 3.423   1.00 44.78 ? 539 HOH   A O   1 
HETATM 2293 O  O   . HOH   F 6 .   ? 3.820   4.204   10.547  1.00 38.84 ? 540 HOH   A O   1 
HETATM 2294 O  O   . HOH   F 6 .   ? 3.443   -13.749 12.618  1.00 35.77 ? 541 HOH   A O   1 
HETATM 2295 O  O   . HOH   F 6 .   ? -17.914 6.338   38.668  1.00 42.18 ? 542 HOH   A O   1 
HETATM 2296 O  O   . HOH   F 6 .   ? -23.941 -0.832  3.975   1.00 26.20 ? 543 HOH   A O   1 
HETATM 2297 O  O   . HOH   F 6 .   ? 5.906   0.656   8.363   1.00 30.81 ? 544 HOH   A O   1 
HETATM 2298 O  O   . HOH   F 6 .   ? 1.207   -1.564  29.549  1.00 18.53 ? 545 HOH   A O   1 
HETATM 2299 O  O   . HOH   F 6 .   ? -13.778 -16.770 -0.053  1.00 39.28 ? 546 HOH   A O   1 
HETATM 2300 O  O   . HOH   F 6 .   ? -23.374 -5.467  42.207  1.00 47.01 ? 547 HOH   A O   1 
HETATM 2301 O  O   . HOH   F 6 .   ? -6.078  17.524  27.644  1.00 35.62 ? 548 HOH   A O   1 
HETATM 2302 O  O   . HOH   F 6 .   ? -18.846 -21.412 5.597   1.00 42.38 ? 549 HOH   A O   1 
HETATM 2303 O  O   . HOH   F 6 .   ? -13.394 -18.643 14.709  1.00 24.27 ? 550 HOH   A O   1 
HETATM 2304 O  O   . HOH   F 6 .   ? -19.279 12.077  12.586  1.00 48.45 ? 551 HOH   A O   1 
HETATM 2305 O  O   . HOH   F 6 .   ? -16.740 -16.045 -4.377  1.00 40.33 ? 552 HOH   A O   1 
HETATM 2306 O  O   . HOH   F 6 .   ? 10.356  -8.895  8.307   1.00 30.62 ? 553 HOH   A O   1 
HETATM 2307 O  O   . HOH   F 6 .   ? -24.804 11.950  6.351   1.00 35.20 ? 554 HOH   A O   1 
HETATM 2308 O  O   . HOH   F 6 .   ? -9.163  0.564   43.177  1.00 30.47 ? 555 HOH   A O   1 
HETATM 2309 O  O   . HOH   F 6 .   ? -2.992  5.957   -1.326  1.00 28.14 ? 556 HOH   A O   1 
HETATM 2310 O  O   . HOH   F 6 .   ? -27.001 -4.013  25.219  1.00 23.15 ? 557 HOH   A O   1 
HETATM 2311 O  O   . HOH   F 6 .   ? 4.418   -2.638  29.047  1.00 30.77 ? 558 HOH   A O   1 
HETATM 2312 O  O   . HOH   F 6 .   ? -12.062 2.890   30.975  1.00 28.24 ? 559 HOH   A O   1 
HETATM 2313 O  O   . HOH   F 6 .   ? -12.876 7.873   28.976  1.00 28.46 ? 560 HOH   A O   1 
HETATM 2314 O  O   . HOH   F 6 .   ? 8.742   1.923   30.625  1.00 49.76 ? 561 HOH   A O   1 
HETATM 2315 O  O   . HOH   F 6 .   ? -7.154  -16.975 1.514   1.00 28.29 ? 562 HOH   A O   1 
HETATM 2316 O  O   . HOH   F 6 .   ? -4.606  -16.117 0.655   1.00 32.89 ? 563 HOH   A O   1 
HETATM 2317 O  O   . HOH   F 6 .   ? 1.160   8.916   24.557  1.00 24.49 ? 564 HOH   A O   1 
HETATM 2318 O  O   . HOH   F 6 .   ? 11.194  -4.023  7.456   1.00 37.08 ? 565 HOH   A O   1 
HETATM 2319 O  O   . HOH   F 6 .   ? -6.836  6.347   10.019  1.00 29.38 ? 566 HOH   A O   1 
HETATM 2320 O  O   . HOH   F 6 .   ? 5.632   -12.863 11.252  1.00 42.23 ? 567 HOH   A O   1 
HETATM 2321 O  O   . HOH   F 6 .   ? -0.598  -8.573  32.649  1.00 26.28 ? 568 HOH   A O   1 
HETATM 2322 O  O   . HOH   F 6 .   ? -18.244 -21.002 -1.114  1.00 44.58 ? 569 HOH   A O   1 
HETATM 2323 O  O   . HOH   F 6 .   ? -8.097  -22.371 10.457  1.00 25.36 ? 570 HOH   A O   1 
HETATM 2324 O  O   . HOH   F 6 .   ? -17.022 0.354   -4.335  1.00 40.45 ? 571 HOH   A O   1 
HETATM 2325 O  O   . HOH   F 6 .   ? -7.578  -19.228 30.734  1.00 37.21 ? 572 HOH   A O   1 
HETATM 2326 O  O   . HOH   F 6 .   ? -17.135 -14.093 37.941  1.00 40.90 ? 573 HOH   A O   1 
HETATM 2327 O  O   . HOH   F 6 .   ? -9.008  -5.915  36.061  1.00 21.98 ? 574 HOH   A O   1 
HETATM 2328 O  O   . HOH   F 6 .   ? -3.626  3.984   8.914   1.00 34.79 ? 575 HOH   A O   1 
HETATM 2329 O  O   . HOH   F 6 .   ? -23.325 -0.658  34.537  1.00 33.19 ? 576 HOH   A O   1 
HETATM 2330 O  O   . HOH   F 6 .   ? -2.069  -12.383 22.921  1.00 18.22 ? 577 HOH   A O   1 
HETATM 2331 O  O   . HOH   F 6 .   ? -11.211 17.542  12.320  1.00 27.98 ? 578 HOH   A O   1 
HETATM 2332 O  O   . HOH   F 6 .   ? 7.686   6.110   21.790  1.00 20.18 ? 579 HOH   A O   1 
HETATM 2333 O  O   . HOH   F 6 .   ? -18.486 -8.831  35.008  1.00 37.58 ? 580 HOH   A O   1 
HETATM 2334 O  O   . HOH   F 6 .   ? 6.585   -5.973  6.698   1.00 37.83 ? 581 HOH   A O   1 
HETATM 2335 O  O   . HOH   F 6 .   ? 4.770   -13.370 -5.720  1.00 23.29 ? 582 HOH   A O   1 
HETATM 2336 O  O   . HOH   F 6 .   ? -23.195 -11.882 14.261  1.00 24.19 ? 583 HOH   A O   1 
HETATM 2337 O  O   . HOH   F 6 .   ? 5.107   -7.244  22.386  1.00 30.70 ? 584 HOH   A O   1 
HETATM 2338 O  O   . HOH   F 6 .   ? -24.853 -9.542  1.992   1.00 29.19 ? 585 HOH   A O   1 
HETATM 2339 O  O   . HOH   F 6 .   ? -8.342  -19.460 21.921  1.00 23.65 ? 586 HOH   A O   1 
HETATM 2340 O  O   . HOH   F 6 .   ? -5.518  3.426   -5.874  1.00 30.04 ? 587 HOH   A O   1 
HETATM 2341 O  O   . HOH   F 6 .   ? -21.495 -19.810 6.693   1.00 37.26 ? 588 HOH   A O   1 
HETATM 2342 O  O   . HOH   F 6 .   ? 6.979   -3.538  29.952  1.00 45.90 ? 589 HOH   A O   1 
HETATM 2343 O  O   . HOH   F 6 .   ? -9.549  -8.020  34.262  1.00 26.49 ? 590 HOH   A O   1 
HETATM 2344 O  O   . HOH   F 6 .   ? 2.863   -4.450  7.565   1.00 30.39 ? 591 HOH   A O   1 
HETATM 2345 O  O   . HOH   F 6 .   ? -0.195  -14.368 22.273  1.00 26.54 ? 592 HOH   A O   1 
HETATM 2346 O  O   . HOH   F 6 .   ? -10.027 14.897  12.240  1.00 27.50 ? 593 HOH   A O   1 
HETATM 2347 O  O   . HOH   F 6 .   ? -7.273  1.544   35.276  1.00 28.83 ? 594 HOH   A O   1 
HETATM 2348 O  O   . HOH   F 6 .   ? 14.345  -0.451  14.811  1.00 36.32 ? 595 HOH   A O   1 
HETATM 2349 O  O   . HOH   F 6 .   ? -7.520  -8.858  -2.489  1.00 34.29 ? 596 HOH   A O   1 
HETATM 2350 O  O   . HOH   F 6 .   ? 14.038  5.711   19.334  1.00 34.17 ? 597 HOH   A O   1 
HETATM 2351 O  O   . HOH   F 6 .   ? 8.912   -11.637 6.587   1.00 32.46 ? 598 HOH   A O   1 
HETATM 2352 O  O   . HOH   F 6 .   ? -18.161 3.959   -3.838  1.00 46.34 ? 599 HOH   A O   1 
HETATM 2353 O  O   . HOH   F 6 .   ? -31.709 5.010   12.936  1.00 42.55 ? 600 HOH   A O   1 
HETATM 2354 O  O   . HOH   F 6 .   ? -24.928 4.751   8.017   1.00 38.51 ? 601 HOH   A O   1 
HETATM 2355 O  O   . HOH   F 6 .   ? -25.389 11.059  19.552  1.00 36.59 ? 602 HOH   A O   1 
HETATM 2356 O  O   . HOH   F 6 .   ? 9.544   1.814   12.143  1.00 38.14 ? 603 HOH   A O   1 
HETATM 2357 O  O   . HOH   F 6 .   ? -12.911 -17.293 17.013  1.00 19.23 ? 604 HOH   A O   1 
HETATM 2358 O  O   . HOH   F 6 .   ? -15.096 11.518  35.077  1.00 45.69 ? 605 HOH   A O   1 
HETATM 2359 O  O   . HOH   F 6 .   ? -1.495  11.406  26.119  1.00 40.38 ? 606 HOH   A O   1 
HETATM 2360 O  O   . HOH   F 6 .   ? -21.869 19.482  12.224  1.00 42.89 ? 607 HOH   A O   1 
HETATM 2361 O  O   . HOH   F 6 .   ? 0.366   0.569   -6.801  1.00 30.15 ? 608 HOH   A O   1 
HETATM 2362 O  O   . HOH   F 6 .   ? 10.573  -2.775  13.498  1.00 36.84 ? 609 HOH   A O   1 
HETATM 2363 O  O   . HOH   F 6 .   ? 8.657   -4.831  23.813  1.00 31.34 ? 610 HOH   A O   1 
HETATM 2364 O  O   . HOH   F 6 .   ? 0.346   -2.783  39.324  1.00 38.76 ? 611 HOH   A O   1 
HETATM 2365 O  O   . HOH   F 6 .   ? 13.071  -3.994  13.569  1.00 33.85 ? 612 HOH   A O   1 
HETATM 2366 O  O   . HOH   F 6 .   ? 5.444   -10.936 19.084  1.00 37.41 ? 613 HOH   A O   1 
HETATM 2367 O  O   . HOH   F 6 .   ? 2.572   -14.948 -6.053  1.00 41.63 ? 614 HOH   A O   1 
HETATM 2368 O  O   . HOH   F 6 .   ? -16.439 -14.977 28.900  1.00 45.79 ? 615 HOH   A O   1 
HETATM 2369 O  O   . HOH   F 6 .   ? -15.417 -16.508 25.619  1.00 38.73 ? 616 HOH   A O   1 
HETATM 2370 O  O   . HOH   F 6 .   ? -15.407 -19.941 23.814  1.00 40.65 ? 617 HOH   A O   1 
HETATM 2371 O  O   . HOH   F 6 .   ? 12.051  -6.799  7.885   1.00 34.71 ? 618 HOH   A O   1 
HETATM 2372 O  O   . HOH   F 6 .   ? 14.366  -7.359  7.152   1.00 44.35 ? 619 HOH   A O   1 
HETATM 2373 O  O   . HOH   F 6 .   ? -23.823 -3.410  3.979   1.00 40.92 ? 620 HOH   A O   1 
HETATM 2374 O  O   . HOH   F 6 .   ? -1.059  3.065   11.289  1.00 46.90 ? 621 HOH   A O   1 
HETATM 2375 O  O   . HOH   F 6 .   ? -23.978 -15.067 22.106  1.00 54.96 ? 622 HOH   A O   1 
HETATM 2376 O  O   . HOH   F 6 .   ? 4.429   -0.064  5.382   1.00 44.02 ? 623 HOH   A O   1 
HETATM 2377 O  O   . HOH   F 6 .   ? -4.813  20.342  21.416  1.00 32.04 ? 624 HOH   A O   1 
HETATM 2378 O  O   . HOH   F 6 .   ? 3.392   2.516   8.268   1.00 34.03 ? 625 HOH   A O   1 
HETATM 2379 O  O   . HOH   F 6 .   ? -17.834 19.847  17.702  1.00 28.50 ? 626 HOH   A O   1 
HETATM 2380 O  O   . HOH   F 6 .   ? 5.862   -14.220 9.009   1.00 44.44 ? 627 HOH   A O   1 
HETATM 2381 O  O   . HOH   F 6 .   ? -25.116 9.074   26.227  1.00 41.12 ? 628 HOH   A O   1 
HETATM 2382 O  O   . HOH   F 6 .   ? -17.022 -18.077 20.248  1.00 30.18 ? 629 HOH   A O   1 
HETATM 2383 O  O   . HOH   F 6 .   ? -10.775 -10.959 -2.921  1.00 42.31 ? 630 HOH   A O   1 
HETATM 2384 O  O   . HOH   F 6 .   ? 2.832   -13.691 8.190   1.00 31.91 ? 631 HOH   A O   1 
HETATM 2385 O  O   . HOH   F 6 .   ? -19.922 -2.191  43.207  1.00 43.86 ? 632 HOH   A O   1 
HETATM 2386 O  O   . HOH   F 6 .   ? -5.722  20.268  26.285  1.00 39.91 ? 633 HOH   A O   1 
HETATM 2387 O  O   . HOH   F 6 .   ? -2.109  -11.997 31.648  1.00 33.72 ? 634 HOH   A O   1 
HETATM 2388 O  O   . HOH   F 6 .   ? -2.100  -17.464 25.660  1.00 35.19 ? 635 HOH   A O   1 
HETATM 2389 O  O   . HOH   F 6 .   ? 1.267   2.872   1.948   1.00 38.11 ? 636 HOH   A O   1 
HETATM 2390 O  O   . HOH   F 6 .   ? 6.411   -5.647  27.632  1.00 36.39 ? 637 HOH   A O   1 
HETATM 2391 O  O   . HOH   F 6 .   ? 1.683   12.584  22.800  1.00 32.39 ? 638 HOH   A O   1 
HETATM 2392 O  O   . HOH   F 6 .   ? -1.272  -13.107 27.142  1.00 28.04 ? 639 HOH   A O   1 
HETATM 2393 O  O   . HOH   F 6 .   ? -24.310 -6.970  0.457   1.00 33.99 ? 640 HOH   A O   1 
HETATM 2394 O  O   . HOH   F 6 .   ? -9.321  3.046   34.879  1.00 31.94 ? 641 HOH   A O   1 
HETATM 2395 O  O   . HOH   F 6 .   ? -17.905 -12.278 31.852  1.00 35.34 ? 642 HOH   A O   1 
HETATM 2396 O  O   . HOH   F 6 .   ? 1.956   -14.404 20.360  1.00 33.64 ? 643 HOH   A O   1 
HETATM 2397 O  O   . HOH   F 6 .   ? -12.930 21.675  26.449  1.00 27.69 ? 644 HOH   A O   1 
HETATM 2398 O  O   . HOH   F 6 .   ? 4.297   7.200   13.188  1.00 56.96 ? 645 HOH   A O   1 
HETATM 2399 O  O   . HOH   F 6 .   ? 15.523  -1.331  26.130  1.00 30.60 ? 646 HOH   A O   1 
HETATM 2400 O  O   . HOH   F 6 .   ? -8.192  7.707   7.908   1.00 30.99 ? 647 HOH   A O   1 
HETATM 2401 O  O   . HOH   F 6 .   ? -28.247 5.078   25.939  1.00 39.44 ? 648 HOH   A O   1 
HETATM 2402 O  O   . HOH   F 6 .   ? -11.381 1.061   -7.863  1.00 34.82 ? 649 HOH   A O   1 
HETATM 2403 O  O   . HOH   F 6 .   ? -21.445 20.490  14.484  1.00 45.83 ? 650 HOH   A O   1 
HETATM 2404 O  O   . HOH   F 6 .   ? -5.711  -12.598 -5.142  1.00 38.75 ? 651 HOH   A O   1 
HETATM 2405 O  O   . HOH   F 6 .   ? 12.764  -4.209  4.762   1.00 40.21 ? 652 HOH   A O   1 
HETATM 2406 O  O   . HOH   F 6 .   ? 1.606   3.106   -4.915  1.00 37.32 ? 653 HOH   A O   1 
HETATM 2407 O  O   . HOH   F 6 .   ? 1.541   -17.632 7.124   1.00 35.76 ? 654 HOH   A O   1 
HETATM 2408 O  O   . HOH   F 6 .   ? -7.420  -10.500 -4.612  1.00 42.09 ? 655 HOH   A O   1 
HETATM 2409 O  O   . HOH   F 6 .   ? -4.021  -15.755 -2.210  1.00 34.02 ? 656 HOH   A O   1 
HETATM 2410 O  O   . HOH   F 6 .   ? 1.569   -9.861  31.837  1.00 44.45 ? 657 HOH   A O   1 
HETATM 2411 O  O   . HOH   F 6 .   ? -1.174  -11.239 29.163  1.00 23.83 ? 658 HOH   A O   1 
HETATM 2412 O  O   . HOH   F 6 .   ? 6.420   5.399   29.220  1.00 35.74 ? 659 HOH   A O   1 
HETATM 2413 O  O   . HOH   F 6 .   ? -5.944  -18.610 3.488   1.00 36.55 ? 660 HOH   A O   1 
HETATM 2414 O  O   . HOH   F 6 .   ? 12.407  4.216   27.644  1.00 35.86 ? 661 HOH   A O   1 
HETATM 2415 O  O   . HOH   F 6 .   ? -0.743  -7.066  -7.887  1.00 39.57 ? 662 HOH   A O   1 
HETATM 2416 O  O   . HOH   F 6 .   ? 4.380   -11.510 23.370  1.00 40.41 ? 663 HOH   A O   1 
HETATM 2417 O  O   . HOH   F 6 .   ? 14.235  -1.445  28.565  1.00 37.65 ? 664 HOH   A O   1 
HETATM 2418 O  O   . HOH   F 6 .   ? 3.779   9.915   24.130  1.00 35.16 ? 665 HOH   A O   1 
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