data_7NZS
# 
_entry.id   7NZS 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.384 
_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   7NZS         pdb_00007nzs 10.2210/pdb7nzs/pdb 
WWPDB D_1292114717 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2022-04-13 
2 'Structure model' 1 1 2024-01-31 
# 
_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             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Data collection'        
2 2 'Structure model' 'Refinement description' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' chem_comp_atom                
2 2 'Structure model' chem_comp_bond                
3 2 'Structure model' pdbx_initial_refinement_model 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        7NZS 
_pdbx_database_status.recvd_initial_deposition_date   2021-03-24 
_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           Y 
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.details        'PDB entry for the same citation' 
_pdbx_database_related.db_id          7NZR 
_pdbx_database_related.content_type   unspecified 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Smirnov, A.'  1 0000-0001-5080-9367 
'Manakova, E.' 2 0000-0002-6027-2265 
'Grazulis, S.' 3 0000-0002-7928-5218 
# 
_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 chimeric carbonic anhydrase VA' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
_citation_author.citation_id        primary 
_citation_author.name               'Smirnov, A.' 
_citation_author.ordinal            1 
_citation_author.identifier_ORCID   0000-0001-5080-9367 
# 
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'                                     29377.160 1   4.2.1.1 
'N62T, H64Y, A65L, N67Q, I91K, F130Y, L203T' ? ? 
2 non-polymer syn 'ZINC ION'                                                 65.409    1   ?       ? ? ? 
3 non-polymer syn 'DIMETHYL SULFOXIDE'                                       78.133    1   ?       ? ? ? 
4 non-polymer syn BICINE                                                     163.172   2   ?       ? ? ? 
5 non-polymer syn '2,3,5,6-tetrafluoro-4-(propylsulfanyl)benzenesulfonamide' 303.297   2   ?       ? ? ? 
6 water       nat water                                                      18.015    261 ?       ? ? ? 
# 
_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       
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNTGYLFQVEFDDSQDKAVLK
GGPLDGTYRLKQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDYGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLTECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNTGYLFQVEFDDSQDKAVLK
GGPLDGTYRLKQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDYGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLTECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
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 'DIMETHYL SULFOXIDE'                                       DMS 
4 BICINE                                                     BCN 
5 '2,3,5,6-tetrafluoro-4-(propylsulfanyl)benzenesulfonamide' 3TV 
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  THR n 
1 63  GLY n 
1 64  TYR n 
1 65  LEU n 
1 66  PHE n 
1 67  GLN 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  LYS 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 TYR 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 THR 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 
3TV non-polymer         . '2,3,5,6-tetrafluoro-4-(propylsulfanyl)benzenesulfonamide' ? 'C9 H9 F4 N O2 S2' 303.297 
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   ?   ?   ?   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  THR 62  62  62  THR THR A . n 
A 1 63  GLY 63  63  63  GLY GLY A . n 
A 1 64  TYR 64  64  64  TYR TYR A . n 
A 1 65  LEU 65  65  65  LEU LEU A . n 
A 1 66  PHE 66  66  66  PHE PHE A . n 
A 1 67  GLN 67  67  67  GLN GLN 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  LYS 91  91  91  LYS LYS 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 126 126 126 LYS LYS A . n 
A 1 127 TYR 127 127 127 TYR TYR A . n 
A 1 128 GLY 128 128 128 GLY GLY A . n 
A 1 129 ASP 129 129 129 ASP ASP A . n 
A 1 130 TYR 130 130 130 TYR TYR A . n 
A 1 131 GLY 131 131 131 GLY GLY A . n 
A 1 132 LYS 132 132 132 LYS LYS A . n 
A 1 133 ALA 133 133 133 ALA ALA A . n 
A 1 134 VAL 134 134 134 VAL VAL A . n 
A 1 135 GLN 135 135 135 GLN GLN A . n 
A 1 136 GLN 136 136 136 GLN GLN A . n 
A 1 137 PRO 137 137 137 PRO PRO A . n 
A 1 138 ASP 138 138 138 ASP ASP A . n 
A 1 139 GLY 139 139 139 GLY GLY A . n 
A 1 140 LEU 140 140 140 LEU LEU A . n 
A 1 141 ALA 141 141 141 ALA ALA A . n 
A 1 142 VAL 142 142 142 VAL VAL A . n 
A 1 143 LEU 143 143 143 LEU LEU A . n 
A 1 144 GLY 144 144 144 GLY GLY A . n 
A 1 145 ILE 145 145 145 ILE ILE A . n 
A 1 146 PHE 146 146 146 PHE PHE A . n 
A 1 147 LEU 147 147 147 LEU LEU A . n 
A 1 148 LYS 148 148 148 LYS LYS A . n 
A 1 149 VAL 149 149 149 VAL VAL A . n 
A 1 150 GLY 150 150 150 GLY GLY A . n 
A 1 151 SER 151 151 151 SER SER A . n 
A 1 152 ALA 152 152 152 ALA ALA A . n 
A 1 153 LYS 153 153 153 LYS LYS A . n 
A 1 154 PRO 154 154 154 PRO PRO A . n 
A 1 155 GLY 155 155 155 GLY GLY A . n 
A 1 156 LEU 156 156 156 LEU LEU A . n 
A 1 157 GLN 157 157 157 GLN GLN A . n 
A 1 158 LYS 158 158 158 LYS LYS A . n 
A 1 159 VAL 159 159 159 VAL VAL A . n 
A 1 160 VAL 160 160 160 VAL VAL A . n 
A 1 161 ASP 161 161 161 ASP ASP A . n 
A 1 162 VAL 162 162 162 VAL VAL A . n 
A 1 163 LEU 163 163 163 LEU LEU A . n 
A 1 164 ASP 164 164 164 ASP ASP A . n 
A 1 165 SER 165 165 165 SER SER A . n 
A 1 166 ILE 166 166 166 ILE ILE A . n 
A 1 167 LYS 167 167 167 LYS LYS A . n 
A 1 168 THR 168 168 168 THR THR A . n 
A 1 169 LYS 169 169 169 LYS LYS A . n 
A 1 170 GLY 170 170 170 GLY GLY A . n 
A 1 171 LYS 171 171 171 LYS LYS A . n 
A 1 172 SER 172 172 172 SER SER A . n 
A 1 173 ALA 173 173 173 ALA ALA A . n 
A 1 174 ASP 174 174 174 ASP ASP A . n 
A 1 175 PHE 175 175 175 PHE PHE A . n 
A 1 176 THR 176 176 176 THR THR A . n 
A 1 177 ASN 177 177 177 ASN ASN A . n 
A 1 178 PHE 178 178 178 PHE PHE A . n 
A 1 179 ASP 179 179 179 ASP ASP A . n 
A 1 180 PRO 180 180 180 PRO PRO A . n 
A 1 181 ARG 181 181 181 ARG ARG A . n 
A 1 182 GLY 182 182 182 GLY GLY A . n 
A 1 183 LEU 183 183 183 LEU LEU A . n 
A 1 184 LEU 184 184 184 LEU LEU A . n 
A 1 185 PRO 185 185 185 PRO PRO A . n 
A 1 186 GLU 186 186 186 GLU GLU A . n 
A 1 187 SER 187 187 187 SER SER A . n 
A 1 188 LEU 188 188 188 LEU LEU A . n 
A 1 189 ASP 189 189 189 ASP ASP A . n 
A 1 190 TYR 190 190 190 TYR TYR A . n 
A 1 191 TRP 191 191 191 TRP TRP A . n 
A 1 192 THR 192 192 192 THR THR A . n 
A 1 193 TYR 193 193 193 TYR TYR A . n 
A 1 194 PRO 194 194 194 PRO PRO A . n 
A 1 195 GLY 195 195 195 GLY GLY A . n 
A 1 196 SER 196 196 196 SER SER A . n 
A 1 197 LEU 197 197 197 LEU LEU A . n 
A 1 198 THR 198 198 198 THR THR A . n 
A 1 199 THR 199 199 199 THR THR A . n 
A 1 200 PRO 200 200 200 PRO PRO A . n 
A 1 201 PRO 201 201 201 PRO PRO A . n 
A 1 202 LEU 202 202 202 LEU LEU A . n 
A 1 203 THR 203 203 203 THR THR A . n 
A 1 204 GLU 204 204 204 GLU GLU A . n 
A 1 205 CYS 205 205 205 CYS CYS A . n 
A 1 206 VAL 206 206 206 VAL VAL A . n 
A 1 207 THR 207 207 207 THR THR A . n 
A 1 208 TRP 208 208 208 TRP TRP A . n 
A 1 209 ILE 209 209 209 ILE ILE A . n 
A 1 210 VAL 210 210 210 VAL VAL A . n 
A 1 211 LEU 211 211 211 LEU LEU A . n 
A 1 212 LYS 212 212 212 LYS LYS A . n 
A 1 213 GLU 213 213 213 GLU GLU A . n 
A 1 214 PRO 214 214 214 PRO PRO A . n 
A 1 215 ILE 215 215 215 ILE ILE A . n 
A 1 216 SER 216 216 216 SER SER A . n 
A 1 217 VAL 217 217 217 VAL VAL A . n 
A 1 218 SER 218 218 218 SER SER A . n 
A 1 219 SER 219 219 219 SER SER A . n 
A 1 220 GLU 220 220 220 GLU GLU A . n 
A 1 221 GLN 221 221 221 GLN GLN A . n 
A 1 222 VAL 222 222 222 VAL VAL A . n 
A 1 223 LEU 223 223 223 LEU LEU A . n 
A 1 224 LYS 224 224 224 LYS LYS A . n 
A 1 225 PHE 225 225 225 PHE PHE A . n 
A 1 226 ARG 226 226 226 ARG ARG A . n 
A 1 227 LYS 227 227 227 LYS LYS A . n 
A 1 228 LEU 228 228 228 LEU LEU A . n 
A 1 229 ASN 229 229 229 ASN ASN A . n 
A 1 230 PHE 230 230 230 PHE PHE A . n 
A 1 231 ASN 231 231 231 ASN ASN A . n 
A 1 232 GLY 232 232 232 GLY GLY A . n 
A 1 233 GLU 233 233 233 GLU GLU A . n 
A 1 234 GLY 234 234 234 GLY GLY A . n 
A 1 235 GLU 235 235 235 GLU GLU A . n 
A 1 236 PRO 236 236 236 PRO PRO A . n 
A 1 237 GLU 237 237 237 GLU GLU A . n 
A 1 238 GLU 238 238 238 GLU GLU A . n 
A 1 239 LEU 239 239 239 LEU LEU A . n 
A 1 240 MET 240 240 240 MET MET A . n 
A 1 241 VAL 241 241 241 VAL VAL A . n 
A 1 242 ASP 242 242 242 ASP ASP A . n 
A 1 243 ASN 243 243 243 ASN ASN A . n 
A 1 244 TRP 244 244 244 TRP TRP A . n 
A 1 245 ARG 245 245 245 ARG ARG A . n 
A 1 246 PRO 246 246 246 PRO PRO A . n 
A 1 247 ALA 247 247 247 ALA ALA A . n 
A 1 248 GLN 248 248 248 GLN GLN A . n 
A 1 249 PRO 249 249 249 PRO PRO A . n 
A 1 250 LEU 250 250 250 LEU LEU A . n 
A 1 251 LYS 251 251 251 LYS LYS A . n 
A 1 252 ASN 252 252 252 ASN ASN A . n 
A 1 253 ARG 253 253 253 ARG ARG A . n 
A 1 254 GLN 254 254 254 GLN GLN A . n 
A 1 255 ILE 255 255 255 ILE ILE A . n 
A 1 256 LYS 256 256 256 LYS LYS A . n 
A 1 257 ALA 257 257 257 ALA ALA A . n 
A 1 258 SER 258 258 258 SER SER A . n 
A 1 259 PHE 259 259 259 PHE PHE A . n 
A 1 260 LYS 260 260 260 LYS LYS A . n 
# 
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 DMS 1   302 1   DMS DMS A . 
D 4 BCN 1   303 2   BCN BCN A . 
E 4 BCN 1   304 3   BCN BCN A . 
F 5 3TV 1   305 1   3TV V05 A . 
G 5 3TV 1   306 2   3TV V05 A . 
H 6 HOH 1   401 153 HOH HOH A . 
H 6 HOH 2   402 112 HOH HOH A . 
H 6 HOH 3   403 192 HOH HOH A . 
H 6 HOH 4   404 143 HOH HOH A . 
H 6 HOH 5   405 224 HOH HOH A . 
H 6 HOH 6   406 207 HOH HOH A . 
H 6 HOH 7   407 121 HOH HOH A . 
H 6 HOH 8   408 226 HOH HOH A . 
H 6 HOH 9   409 34  HOH HOH A . 
H 6 HOH 10  410 173 HOH HOH A . 
H 6 HOH 11  411 238 HOH HOH A . 
H 6 HOH 12  412 94  HOH HOH A . 
H 6 HOH 13  413 218 HOH HOH A . 
H 6 HOH 14  414 162 HOH HOH A . 
H 6 HOH 15  415 114 HOH HOH A . 
H 6 HOH 16  416 20  HOH HOH A . 
H 6 HOH 17  417 155 HOH HOH A . 
H 6 HOH 18  418 52  HOH HOH A . 
H 6 HOH 19  419 37  HOH HOH A . 
H 6 HOH 20  420 124 HOH HOH A . 
H 6 HOH 21  421 39  HOH HOH A . 
H 6 HOH 22  422 158 HOH HOH A . 
H 6 HOH 23  423 223 HOH HOH A . 
H 6 HOH 24  424 252 HOH HOH A . 
H 6 HOH 25  425 179 HOH HOH A . 
H 6 HOH 26  426 149 HOH HOH A . 
H 6 HOH 27  427 139 HOH HOH A . 
H 6 HOH 28  428 181 HOH HOH A . 
H 6 HOH 29  429 118 HOH HOH A . 
H 6 HOH 30  430 232 HOH HOH A . 
H 6 HOH 31  431 237 HOH HOH A . 
H 6 HOH 32  432 251 HOH HOH A . 
H 6 HOH 33  433 47  HOH HOH A . 
H 6 HOH 34  434 51  HOH HOH A . 
H 6 HOH 35  435 113 HOH HOH A . 
H 6 HOH 36  436 5   HOH HOH A . 
H 6 HOH 37  437 132 HOH HOH A . 
H 6 HOH 38  438 26  HOH HOH A . 
H 6 HOH 39  439 200 HOH HOH A . 
H 6 HOH 40  440 165 HOH HOH A . 
H 6 HOH 41  441 98  HOH HOH A . 
H 6 HOH 42  442 14  HOH HOH A . 
H 6 HOH 43  443 111 HOH HOH A . 
H 6 HOH 44  444 96  HOH HOH A . 
H 6 HOH 45  445 79  HOH HOH A . 
H 6 HOH 46  446 59  HOH HOH A . 
H 6 HOH 47  447 74  HOH HOH A . 
H 6 HOH 48  448 160 HOH HOH A . 
H 6 HOH 49  449 183 HOH HOH A . 
H 6 HOH 50  450 73  HOH HOH A . 
H 6 HOH 51  451 101 HOH HOH A . 
H 6 HOH 52  452 33  HOH HOH A . 
H 6 HOH 53  453 233 HOH HOH A . 
H 6 HOH 54  454 76  HOH HOH A . 
H 6 HOH 55  455 235 HOH HOH A . 
H 6 HOH 56  456 156 HOH HOH A . 
H 6 HOH 57  457 58  HOH HOH A . 
H 6 HOH 58  458 57  HOH HOH A . 
H 6 HOH 59  459 131 HOH HOH A . 
H 6 HOH 60  460 119 HOH HOH A . 
H 6 HOH 61  461 142 HOH HOH A . 
H 6 HOH 62  462 126 HOH HOH A . 
H 6 HOH 63  463 176 HOH HOH A . 
H 6 HOH 64  464 13  HOH HOH A . 
H 6 HOH 65  465 66  HOH HOH A . 
H 6 HOH 66  466 240 HOH HOH A . 
H 6 HOH 67  467 41  HOH HOH A . 
H 6 HOH 68  468 256 HOH HOH A . 
H 6 HOH 69  469 63  HOH HOH A . 
H 6 HOH 70  470 21  HOH HOH A . 
H 6 HOH 71  471 62  HOH HOH A . 
H 6 HOH 72  472 260 HOH HOH A . 
H 6 HOH 73  473 244 HOH HOH A . 
H 6 HOH 74  474 197 HOH HOH A . 
H 6 HOH 75  475 106 HOH HOH A . 
H 6 HOH 76  476 16  HOH HOH A . 
H 6 HOH 77  477 64  HOH HOH A . 
H 6 HOH 78  478 4   HOH HOH A . 
H 6 HOH 79  479 103 HOH HOH A . 
H 6 HOH 80  480 15  HOH HOH A . 
H 6 HOH 81  481 164 HOH HOH A . 
H 6 HOH 82  482 7   HOH HOH A . 
H 6 HOH 83  483 2   HOH HOH A . 
H 6 HOH 84  484 140 HOH HOH A . 
H 6 HOH 85  485 8   HOH HOH A . 
H 6 HOH 86  486 31  HOH HOH A . 
H 6 HOH 87  487 130 HOH HOH A . 
H 6 HOH 88  488 82  HOH HOH A . 
H 6 HOH 89  489 72  HOH HOH A . 
H 6 HOH 90  490 6   HOH HOH A . 
H 6 HOH 91  491 17  HOH HOH A . 
H 6 HOH 92  492 247 HOH HOH A . 
H 6 HOH 93  493 169 HOH HOH A . 
H 6 HOH 94  494 110 HOH HOH A . 
H 6 HOH 95  495 144 HOH HOH A . 
H 6 HOH 96  496 49  HOH HOH A . 
H 6 HOH 97  497 217 HOH HOH A . 
H 6 HOH 98  498 88  HOH HOH A . 
H 6 HOH 99  499 241 HOH HOH A . 
H 6 HOH 100 500 145 HOH HOH A . 
H 6 HOH 101 501 246 HOH HOH A . 
H 6 HOH 102 502 201 HOH HOH A . 
H 6 HOH 103 503 18  HOH HOH A . 
H 6 HOH 104 504 69  HOH HOH A . 
H 6 HOH 105 505 25  HOH HOH A . 
H 6 HOH 106 506 178 HOH HOH A . 
H 6 HOH 107 507 30  HOH HOH A . 
H 6 HOH 108 508 40  HOH HOH A . 
H 6 HOH 109 509 208 HOH HOH A . 
H 6 HOH 110 510 75  HOH HOH A . 
H 6 HOH 111 511 135 HOH HOH A . 
H 6 HOH 112 512 10  HOH HOH A . 
H 6 HOH 113 513 221 HOH HOH A . 
H 6 HOH 114 514 159 HOH HOH A . 
H 6 HOH 115 515 67  HOH HOH A . 
H 6 HOH 116 516 32  HOH HOH A . 
H 6 HOH 117 517 128 HOH HOH A . 
H 6 HOH 118 518 1   HOH HOH A . 
H 6 HOH 119 519 89  HOH HOH A . 
H 6 HOH 120 520 46  HOH HOH A . 
H 6 HOH 121 521 24  HOH HOH A . 
H 6 HOH 122 522 50  HOH HOH A . 
H 6 HOH 123 523 53  HOH HOH A . 
H 6 HOH 124 524 23  HOH HOH A . 
H 6 HOH 125 525 175 HOH HOH A . 
H 6 HOH 126 526 108 HOH HOH A . 
H 6 HOH 127 527 48  HOH HOH A . 
H 6 HOH 128 528 29  HOH HOH A . 
H 6 HOH 129 529 55  HOH HOH A . 
H 6 HOH 130 530 12  HOH HOH A . 
H 6 HOH 131 531 180 HOH HOH A . 
H 6 HOH 132 532 215 HOH HOH A . 
H 6 HOH 133 533 95  HOH HOH A . 
H 6 HOH 134 534 97  HOH HOH A . 
H 6 HOH 135 535 19  HOH HOH A . 
H 6 HOH 136 536 35  HOH HOH A . 
H 6 HOH 137 537 86  HOH HOH A . 
H 6 HOH 138 538 154 HOH HOH A . 
H 6 HOH 139 539 141 HOH HOH A . 
H 6 HOH 140 540 27  HOH HOH A . 
H 6 HOH 141 541 28  HOH HOH A . 
H 6 HOH 142 542 54  HOH HOH A . 
H 6 HOH 143 543 189 HOH HOH A . 
H 6 HOH 144 544 203 HOH HOH A . 
H 6 HOH 145 545 65  HOH HOH A . 
H 6 HOH 146 546 80  HOH HOH A . 
H 6 HOH 147 547 38  HOH HOH A . 
H 6 HOH 148 548 137 HOH HOH A . 
H 6 HOH 149 549 3   HOH HOH A . 
H 6 HOH 150 550 68  HOH HOH A . 
H 6 HOH 151 551 44  HOH HOH A . 
H 6 HOH 152 552 234 HOH HOH A . 
H 6 HOH 153 553 172 HOH HOH A . 
H 6 HOH 154 554 115 HOH HOH A . 
H 6 HOH 155 555 61  HOH HOH A . 
H 6 HOH 156 556 236 HOH HOH A . 
H 6 HOH 157 557 250 HOH HOH A . 
H 6 HOH 158 558 198 HOH HOH A . 
H 6 HOH 159 559 146 HOH HOH A . 
H 6 HOH 160 560 117 HOH HOH A . 
H 6 HOH 161 561 116 HOH HOH A . 
H 6 HOH 162 562 71  HOH HOH A . 
H 6 HOH 163 563 102 HOH HOH A . 
H 6 HOH 164 564 107 HOH HOH A . 
H 6 HOH 165 565 22  HOH HOH A . 
H 6 HOH 166 566 255 HOH HOH A . 
H 6 HOH 167 567 239 HOH HOH A . 
H 6 HOH 168 568 222 HOH HOH A . 
H 6 HOH 169 569 91  HOH HOH A . 
H 6 HOH 170 570 70  HOH HOH A . 
H 6 HOH 171 571 36  HOH HOH A . 
H 6 HOH 172 572 11  HOH HOH A . 
H 6 HOH 173 573 219 HOH HOH A . 
H 6 HOH 174 574 182 HOH HOH A . 
H 6 HOH 175 575 187 HOH HOH A . 
H 6 HOH 176 576 9   HOH HOH A . 
H 6 HOH 177 577 212 HOH HOH A . 
H 6 HOH 178 578 43  HOH HOH A . 
H 6 HOH 179 579 174 HOH HOH A . 
H 6 HOH 180 580 167 HOH HOH A . 
H 6 HOH 181 581 253 HOH HOH A . 
H 6 HOH 182 582 120 HOH HOH A . 
H 6 HOH 183 583 228 HOH HOH A . 
H 6 HOH 184 584 87  HOH HOH A . 
H 6 HOH 185 585 161 HOH HOH A . 
H 6 HOH 186 586 60  HOH HOH A . 
H 6 HOH 187 587 185 HOH HOH A . 
H 6 HOH 188 588 125 HOH HOH A . 
H 6 HOH 189 589 261 HOH HOH A . 
H 6 HOH 190 590 42  HOH HOH A . 
H 6 HOH 191 591 104 HOH HOH A . 
H 6 HOH 192 592 213 HOH HOH A . 
H 6 HOH 193 593 93  HOH HOH A . 
H 6 HOH 194 594 184 HOH HOH A . 
H 6 HOH 195 595 188 HOH HOH A . 
H 6 HOH 196 596 190 HOH HOH A . 
H 6 HOH 197 597 109 HOH HOH A . 
H 6 HOH 198 598 84  HOH HOH A . 
H 6 HOH 199 599 83  HOH HOH A . 
H 6 HOH 200 600 136 HOH HOH A . 
H 6 HOH 201 601 77  HOH HOH A . 
H 6 HOH 202 602 196 HOH HOH A . 
H 6 HOH 203 603 259 HOH HOH A . 
H 6 HOH 204 604 194 HOH HOH A . 
H 6 HOH 205 605 147 HOH HOH A . 
H 6 HOH 206 606 163 HOH HOH A . 
H 6 HOH 207 607 105 HOH HOH A . 
H 6 HOH 208 608 210 HOH HOH A . 
H 6 HOH 209 609 202 HOH HOH A . 
H 6 HOH 210 610 123 HOH HOH A . 
H 6 HOH 211 611 209 HOH HOH A . 
H 6 HOH 212 612 220 HOH HOH A . 
H 6 HOH 213 613 90  HOH HOH A . 
H 6 HOH 214 614 133 HOH HOH A . 
H 6 HOH 215 615 258 HOH HOH A . 
H 6 HOH 216 616 193 HOH HOH A . 
H 6 HOH 217 617 92  HOH HOH A . 
H 6 HOH 218 618 168 HOH HOH A . 
H 6 HOH 219 619 227 HOH HOH A . 
H 6 HOH 220 620 214 HOH HOH A . 
H 6 HOH 221 621 229 HOH HOH A . 
H 6 HOH 222 622 127 HOH HOH A . 
H 6 HOH 223 623 248 HOH HOH A . 
H 6 HOH 224 624 148 HOH HOH A . 
H 6 HOH 225 625 216 HOH HOH A . 
H 6 HOH 226 626 85  HOH HOH A . 
H 6 HOH 227 627 191 HOH HOH A . 
H 6 HOH 228 628 195 HOH HOH A . 
H 6 HOH 229 629 78  HOH HOH A . 
H 6 HOH 230 630 205 HOH HOH A . 
H 6 HOH 231 631 206 HOH HOH A . 
H 6 HOH 232 632 152 HOH HOH A . 
H 6 HOH 233 633 242 HOH HOH A . 
H 6 HOH 234 634 129 HOH HOH A . 
H 6 HOH 235 635 166 HOH HOH A . 
H 6 HOH 236 636 81  HOH HOH A . 
H 6 HOH 237 637 249 HOH HOH A . 
H 6 HOH 238 638 199 HOH HOH A . 
H 6 HOH 239 639 231 HOH HOH A . 
H 6 HOH 240 640 243 HOH HOH A . 
H 6 HOH 241 641 230 HOH HOH A . 
H 6 HOH 242 642 257 HOH HOH A . 
H 6 HOH 243 643 157 HOH HOH A . 
H 6 HOH 244 644 204 HOH HOH A . 
H 6 HOH 245 645 122 HOH HOH A . 
H 6 HOH 246 646 211 HOH HOH A . 
H 6 HOH 247 647 177 HOH HOH A . 
H 6 HOH 248 648 99  HOH HOH A . 
H 6 HOH 249 649 45  HOH HOH A . 
H 6 HOH 250 650 170 HOH HOH A . 
H 6 HOH 251 651 134 HOH HOH A . 
H 6 HOH 252 652 225 HOH HOH A . 
H 6 HOH 253 653 138 HOH HOH A . 
H 6 HOH 254 654 186 HOH HOH A . 
H 6 HOH 255 655 150 HOH HOH A . 
H 6 HOH 256 656 56  HOH HOH A . 
H 6 HOH 257 657 100 HOH HOH A . 
H 6 HOH 258 658 245 HOH HOH A . 
H 6 HOH 259 659 254 HOH HOH A . 
H 6 HOH 260 660 171 HOH HOH A . 
H 6 HOH 261 661 151 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 9   ? CG  ? A LYS 9   CG  
2  1 Y 1 A LYS 9   ? CD  ? A LYS 9   CD  
3  1 Y 1 A LYS 9   ? CE  ? A LYS 9   CE  
4  1 Y 1 A LYS 9   ? NZ  ? A LYS 9   NZ  
5  1 Y 1 A LYS 45  ? CE  ? A LYS 45  CE  
6  1 Y 1 A LYS 45  ? NZ  ? A LYS 45  NZ  
7  1 Y 1 A LYS 80  ? NZ  ? A LYS 80  NZ  
8  1 Y 1 A LYS 158 ? CG  ? A LYS 158 CG  
9  1 Y 1 A LYS 158 ? CD  ? A LYS 158 CD  
10 1 Y 1 A LYS 158 ? CE  ? A LYS 158 CE  
11 1 Y 1 A LYS 158 ? NZ  ? A LYS 158 NZ  
12 1 Y 1 A GLU 238 ? CG  ? A GLU 238 CG  
13 1 Y 1 A GLU 238 ? CD  ? A GLU 238 CD  
14 1 Y 1 A GLU 238 ? OE1 ? A GLU 238 OE1 
15 1 Y 1 A GLU 238 ? OE2 ? A GLU 238 OE2 
16 1 Y 1 A LYS 256 ? CE  ? A LYS 256 CE  
17 1 Y 1 A LYS 256 ? NZ  ? A LYS 256 NZ  
18 1 Y 1 A LYS 260 ? CG  ? A LYS 260 CG  
19 1 Y 1 A LYS 260 ? CD  ? A LYS 260 CD  
20 1 Y 1 A LYS 260 ? CE  ? A LYS 260 CE  
21 1 Y 1 A LYS 260 ? NZ  ? A LYS 260 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       ? ? ? 3.3.20   1 
? refinement        ? ? ? ? ? ? ? ? ? ? ? REFMAC      ? ? ? 5.8.0232 2 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.27     3 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? XDS         ? ? ? .        4 
? phasing           ? ? ? ? ? ? ? ? ? ? ? MOLREP      ? ? ? .        5 
? 'model building'  ? ? ? ? ? ? ? ? ? ? ? Coot        ? ? ? .        6 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   104.180 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     7NZS 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     42.130 
_cell.length_a_esd                 ? 
_cell.length_b                     41.304 
_cell.length_b_esd                 ? 
_cell.length_c                     71.250 
_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             ? 
# 
_symmetry.entry_id                         7NZS 
_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                   7NZS 
_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            2.05 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         39.88 
_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_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            291 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;Crystallization buffer was 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   ? 
# 
_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         2013-05-21 
_diffrn_detector.pdbx_frequency               ? 
# 
_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   0.97630 
_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        0.97630 
_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                         7NZS 
_reflns.data_reduction_details           ? 
_reflns.data_reduction_method            ? 
_reflns.d_resolution_high                1.500 
_reflns.d_resolution_low                 69.078 
_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                       38049 
_reflns.number_obs                       38049 
_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             99.400 
_reflns.R_free_details                   ? 
_reflns.Rmerge_F_all                     ? 
_reflns.Rmerge_F_obs                     ? 
_reflns.Friedel_coverage                 ? 
_reflns.number_gt                        ? 
_reflns.threshold_expression             ? 
_reflns.pdbx_redundancy                  6.700 
_reflns.pdbx_Rmerge_I_obs                ? 
_reflns.pdbx_Rmerge_I_all                ? 
_reflns.pdbx_Rsym_value                  0.047 
_reflns.pdbx_netI_over_av_sigmaI         9.100 
_reflns.pdbx_netI_over_sigmaI            17.500 
_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                  0.056 
_reflns.pdbx_Rpim_I_all                  0.021 
_reflns.pdbx_d_opt                       ? 
_reflns.pdbx_number_measured_all         254707 
_reflns.pdbx_diffrn_id                   1 
_reflns.pdbx_ordinal                     1 
_reflns.pdbx_CC_half                     ? 
_reflns.pdbx_CC_star                     ? 
_reflns.pdbx_R_split                     ? 
# 
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_all 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_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_Rsym_value 
_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 
1.500 1.580  ? 3.100  36997 ? ? ? 5516 99.400 ? ? ? ? 0.234 ? ? ? ? ? ? ? ? 6.700 0.234 ? ? 6.000  0.276 0.105 ? 1  1 ? ? ? 
1.580 1.680  ? 4.300  32741 ? ? ? 5191 99.000 ? ? ? ? 0.169 ? ? ? ? ? ? ? ? 6.300 0.169 ? ? 7.400  0.201 0.079 ? 2  1 ? ? ? 
1.680 1.790  ? 5.700  33652 ? ? ? 4943 99.600 ? ? ? ? 0.123 ? ? ? ? ? ? ? ? 6.800 0.123 ? ? 10.000 0.145 0.055 ? 3  1 ? ? ? 
1.790 1.940  ? 7.400  31198 ? ? ? 4565 99.600 ? ? ? ? 0.089 ? ? ? ? ? ? ? ? 6.800 0.089 ? ? 13.700 0.105 0.040 ? 4  1 ? ? ? 
1.940 2.120  ? 9.600  27084 ? ? ? 4216 99.100 ? ? ? ? 0.068 ? ? ? ? ? ? ? ? 6.400 0.068 ? ? 18.000 0.080 0.031 ? 5  1 ? ? ? 
2.120 2.370  ? 11.700 27069 ? ? ? 3838 99.600 ? ? ? ? 0.055 ? ? ? ? ? ? ? ? 7.100 0.055 ? ? 22.900 0.065 0.024 ? 6  1 ? ? ? 
2.370 2.740  ? 13.000 23417 ? ? ? 3384 99.600 ? ? ? ? 0.048 ? ? ? ? ? ? ? ? 6.900 0.048 ? ? 26.600 0.057 0.022 ? 7  1 ? ? ? 
2.740 3.350  ? 14.400 18684 ? ? ? 2878 99.500 ? ? ? ? 0.041 ? ? ? ? ? ? ? ? 6.500 0.041 ? ? 31.900 0.049 0.019 ? 8  1 ? ? ? 
3.350 4.740  ? 17.600 15606 ? ? ? 2249 99.600 ? ? ? ? 0.033 ? ? ? ? ? ? ? ? 6.900 0.033 ? ? 40.500 0.039 0.015 ? 9  1 ? ? ? 
4.740 69.078 ? 19.200 8259  ? ? ? 1269 99.100 ? ? ? ? 0.027 ? ? ? ? ? ? ? ? 6.500 0.027 ? ? 37.400 0.034 0.013 ? 10 1 ? ? ? 
# 
_refine.aniso_B[1][1]                            -0.0200 
_refine.aniso_B[1][2]                            -0.0000 
_refine.aniso_B[1][3]                            0.3300 
_refine.aniso_B[2][2]                            -0.6300 
_refine.aniso_B[2][3]                            0.0000 
_refine.aniso_B[3][3]                            0.4200 
_refine.B_iso_max                                70.360 
_refine.B_iso_mean                               19.4080 
_refine.B_iso_min                                6.960 
_refine.correlation_coeff_Fo_to_Fc               0.9670 
_refine.correlation_coeff_Fo_to_Fc_free          0.9530 
_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                                 7NZS 
_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                             40.8500 
_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                     34218 
_refine.ls_number_reflns_R_free                  3806 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.2600 
_refine.ls_percent_reflns_R_free                 10.0000 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1725 
_refine.ls_R_factor_R_free                       0.2018 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1692 
_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                      4HT0 
_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                       0.0830 
_refine.pdbx_overall_ESU_R_Free                  0.0840 
_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                        40.8500 
_refine_hist.number_atoms_solvent             261 
_refine_hist.number_atoms_total               2358 
_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       257 
_refine_hist.pdbx_B_iso_mean_ligand           35.21 
_refine_hist.pdbx_B_iso_mean_solvent          30.43 
_refine_hist.pdbx_number_atoms_protein        2034 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         63 
_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  2237 ? r_bond_refined_d       ? ? 
'X-RAY DIFFRACTION' ? 1.970  1.665  3056 ? r_angle_refined_deg    ? ? 
'X-RAY DIFFRACTION' ? 7.337  5.000  274  ? r_dihedral_angle_1_deg ? ? 
'X-RAY DIFFRACTION' ? 34.735 23.364 107  ? r_dihedral_angle_2_deg ? ? 
'X-RAY DIFFRACTION' ? 14.463 15.000 350  ? r_dihedral_angle_3_deg ? ? 
'X-RAY DIFFRACTION' ? 21.807 15.000 8    ? r_dihedral_angle_4_deg ? ? 
'X-RAY DIFFRACTION' ? 0.129  0.200  269  ? r_chiral_restr         ? ? 
'X-RAY DIFFRACTION' ? 0.012  0.020  1759 ? 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                2789 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             282 
_refine_ls_shell.number_reflns_R_work             2507 
_refine_ls_shell.percent_reflns_obs               99.2200 
_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                  0.2550 
_refine_ls_shell.R_factor_R_free_error            0.0000 
_refine_ls_shell.R_factor_R_work                  0.2140 
_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                    ? 
# 
_struct.entry_id                     7NZS 
_struct.title                        
'Crystal structure of chimeric carbonic anhydrase VA with 2,3,5,6-tetrafluoro-4-(propylsulfanyl)benzenesulfonamide' 
_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        7NZS 
_struct_keywords.text            
'drug design, carbonic anhydrase, benzenesulfonamide, metal-binding, 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 4 ? 
F N N 5 ? 
G N N 5 ? 
H 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              7NZS 
_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       260 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 7NZS THR A 62  ? UNP P00918 ASN 62  'engineered mutation' 62  1 
1 7NZS TYR A 64  ? UNP P00918 HIS 64  'engineered mutation' 64  2 
1 7NZS LEU A 65  ? UNP P00918 ALA 65  'engineered mutation' 65  3 
1 7NZS GLN A 67  ? UNP P00918 ASN 67  'engineered mutation' 67  4 
1 7NZS LYS A 91  ? UNP P00918 ILE 91  'engineered mutation' 91  5 
1 7NZS TYR A 130 ? UNP P00918 PHE 130 'engineered mutation' 130 6 
1 7NZS THR A 203 ? UNP P00918 LEU 203 'engineered mutation' 203 7 
# 
_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)' 710   ? 
1 MORE         4     ? 
1 'SSA (A^2)'  11300 ? 
# 
_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,G,H 
# 
_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 126 GLY A 128 5 ? 3 
HELX_P HELX_P4 AA4 ASP A 129 ? VAL A 134 ? ASP A 129 VAL A 134 1 ? 6 
HELX_P HELX_P5 AA5 LYS A 153 ? GLY A 155 ? LYS A 153 GLY A 155 5 ? 3 
HELX_P HELX_P6 AA6 LEU A 156 ? LEU A 163 ? LEU A 156 LEU A 163 1 ? 8 
HELX_P HELX_P7 AA7 ASP A 164 ? LYS A 167 ? ASP A 164 LYS A 167 5 ? 4 
HELX_P HELX_P8 AA8 ASP A 179 ? LEU A 184 ? ASP A 179 LEU A 184 5 ? 6 
HELX_P HELX_P9 AA9 SER A 218 ? ARG A 226 ? SER A 218 ARG A 226 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 ? ? ? ? ? ? ? 2.041 ? ? 
metalc2 metalc ? ? A HIS 96  NE2 ? ? ? 1_555 B ZN  . ZN ? ? A HIS 96  A ZN  301 1_555 ? ? ? ? ? ? ? 2.027 ? ? 
metalc3 metalc ? ? A HIS 119 ND1 ? ? ? 1_555 B ZN  . ZN ? ? A HIS 119 A ZN  301 1_555 ? ? ? ? ? ? ? 2.060 ? ? 
metalc4 metalc ? ? B ZN  .   ZN  ? ? ? 1_555 F 3TV . N2 ? ? A ZN  301 A 3TV 305 1_555 ? ? ? ? ? ? ? 1.898 ? ? 
# 
_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_555 102.1 ? 
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_555 109.0 ? 
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_555 100.4 ? 
4 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N2  ? F 3TV .   ? A 3TV 305 ? 1_555 117.3 ? 
5 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N2  ? F 3TV .   ? A 3TV 305 ? 1_555 114.9 ? 
6 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N2  ? F 3TV .   ? A 3TV 305 ? 1_555 111.4 ? 
# 
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 -2.03 
2 PRO 200 A . ? PRO 200 A PRO 201 A ? PRO 201 A 1 7.00  
# 
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 256 ALA A 257 
AA2 3  TYR A 190 ? GLY A 195 ? TYR A 190 GLY A 195 
AA2 4  VAL A 206 ? LEU A 211 ? VAL A 206 LEU A 211 
AA2 5  LEU A 140 ? VAL A 149 ? LEU A 140 VAL A 149 
AA2 6  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
AA2 7  THR A 87  ? TRP A 97  ? THR A 87  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 172 ASP A 174 
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  THR A 87  ? TRP A 97  ? THR A 87  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 140 VAL A 149 
AA3 6  ILE A 215 ? VAL A 217 ? ILE A 215 VAL A 217 
# 
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 257 
AA2 2 3  O LYS A 256 ? O LYS A 256 N THR A 192 ? N THR A 192 
AA2 3 4  N GLY A 195 ? N GLY A 195 O VAL A 206 ? O VAL A 206 
AA2 4 5  O ILE A 209 ? O ILE A 209 N GLY A 144 ? N GLY A 144 
AA2 5 6  O ILE A 145 ? O ILE A 145 N LEU A 118 ? N LEU A 118 
AA2 6 7  O TRP A 123 ? O TRP A 123 N ARG A 89  ? N ARG A 89  
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 LEU A 57  ? N LEU A 57  
AA2 9 10 N ILE A 59  ? N ILE A 59  O ALA A 173 ? O ALA A 173 
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 ARG A 89  ? N ARG A 89  O TRP A 123 ? O TRP A 123 
AA3 4 5  N LEU A 118 ? N LEU A 118 O ILE A 145 ? O ILE A 145 
AA3 5 6  N LYS A 148 ? N LYS A 148 O VAL A 217 ? O VAL A 217 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 11  ? ? -144.28 20.53   
2 1 LEU A 65  ? ? -175.11 -175.79 
3 1 LYS A 76  ? ? -112.81 -84.40  
4 1 LYS A 111 ? ? 73.79   -2.00   
5 1 PHE A 175 ? ? -151.51 67.96   
6 1 ASN A 243 ? ? -96.46  50.24   
7 1 LYS A 251 ? ? 61.35   -132.77 
# 
_pdbx_entry_details.entry_id                 7NZS 
_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_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       661 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   6.02 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A MET 1 ? A MET 1 
2 1 Y 1 A SER 2 ? A SER 2 
3 1 Y 1 A HIS 3 ? A HIS 3 
# 
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 
3TV F18  F  N N 1   
3TV C7   C  Y N 2   
3TV C6   C  Y N 3   
3TV F17  F  N N 4   
3TV C8   C  Y N 5   
3TV S11  S  N N 6   
3TV C12  C  N N 7   
3TV C13  C  N N 8   
3TV C14  C  N N 9   
3TV C9   C  Y N 10  
3TV F15  F  N N 11  
3TV C10  C  Y N 12  
3TV F16  F  N N 13  
3TV C5   C  Y N 14  
3TV S1   S  N N 15  
3TV O3   O  N N 16  
3TV O4   O  N N 17  
3TV N2   N  N N 18  
3TV H1   H  N N 19  
3TV H2   H  N N 20  
3TV H3   H  N N 21  
3TV H4   H  N N 22  
3TV H5   H  N N 23  
3TV H6   H  N N 24  
3TV H7   H  N N 25  
3TV H8   H  N N 26  
3TV H9   H  N N 27  
ALA N    N  N N 28  
ALA CA   C  N S 29  
ALA C    C  N N 30  
ALA O    O  N N 31  
ALA CB   C  N N 32  
ALA OXT  O  N N 33  
ALA H    H  N N 34  
ALA H2   H  N N 35  
ALA HA   H  N N 36  
ALA HB1  H  N N 37  
ALA HB2  H  N N 38  
ALA HB3  H  N N 39  
ALA HXT  H  N N 40  
ARG N    N  N N 41  
ARG CA   C  N S 42  
ARG C    C  N N 43  
ARG O    O  N N 44  
ARG CB   C  N N 45  
ARG CG   C  N N 46  
ARG CD   C  N N 47  
ARG NE   N  N N 48  
ARG CZ   C  N N 49  
ARG NH1  N  N N 50  
ARG NH2  N  N N 51  
ARG OXT  O  N N 52  
ARG H    H  N N 53  
ARG H2   H  N N 54  
ARG HA   H  N N 55  
ARG HB2  H  N N 56  
ARG HB3  H  N N 57  
ARG HG2  H  N N 58  
ARG HG3  H  N N 59  
ARG HD2  H  N N 60  
ARG HD3  H  N N 61  
ARG HE   H  N N 62  
ARG HH11 H  N N 63  
ARG HH12 H  N N 64  
ARG HH21 H  N N 65  
ARG HH22 H  N N 66  
ARG HXT  H  N N 67  
ASN N    N  N N 68  
ASN CA   C  N S 69  
ASN C    C  N N 70  
ASN O    O  N N 71  
ASN CB   C  N N 72  
ASN CG   C  N N 73  
ASN OD1  O  N N 74  
ASN ND2  N  N N 75  
ASN OXT  O  N N 76  
ASN H    H  N N 77  
ASN H2   H  N N 78  
ASN HA   H  N N 79  
ASN HB2  H  N N 80  
ASN HB3  H  N N 81  
ASN HD21 H  N N 82  
ASN HD22 H  N N 83  
ASN HXT  H  N N 84  
ASP N    N  N N 85  
ASP CA   C  N S 86  
ASP C    C  N N 87  
ASP O    O  N N 88  
ASP CB   C  N N 89  
ASP CG   C  N N 90  
ASP OD1  O  N N 91  
ASP OD2  O  N N 92  
ASP OXT  O  N N 93  
ASP H    H  N N 94  
ASP H2   H  N N 95  
ASP HA   H  N N 96  
ASP HB2  H  N N 97  
ASP HB3  H  N N 98  
ASP HD2  H  N N 99  
ASP HXT  H  N N 100 
BCN N1   N  N N 101 
BCN C1   C  N N 102 
BCN C2   C  N N 103 
BCN O21  O  N N 104 
BCN O22  O  N N 105 
BCN C3   C  N N 106 
BCN C4   C  N N 107 
BCN O4   O  N N 108 
BCN C5   C  N N 109 
BCN C6   C  N N 110 
BCN O6   O  N N 111 
BCN H11  H  N N 112 
BCN H12  H  N N 113 
BCN HO2  H  N N 114 
BCN H31  H  N N 115 
BCN H32  H  N N 116 
BCN H41  H  N N 117 
BCN H42  H  N N 118 
BCN HO4  H  N N 119 
BCN H51  H  N N 120 
BCN H52  H  N N 121 
BCN H61  H  N N 122 
BCN H62  H  N N 123 
BCN HO6  H  N N 124 
CYS N    N  N N 125 
CYS CA   C  N R 126 
CYS C    C  N N 127 
CYS O    O  N N 128 
CYS CB   C  N N 129 
CYS SG   S  N N 130 
CYS OXT  O  N N 131 
CYS H    H  N N 132 
CYS H2   H  N N 133 
CYS HA   H  N N 134 
CYS HB2  H  N N 135 
CYS HB3  H  N N 136 
CYS HG   H  N N 137 
CYS HXT  H  N N 138 
DMS S    S  N N 139 
DMS O    O  N N 140 
DMS C1   C  N N 141 
DMS C2   C  N N 142 
DMS H11  H  N N 143 
DMS H12  H  N N 144 
DMS H13  H  N N 145 
DMS H21  H  N N 146 
DMS H22  H  N N 147 
DMS H23  H  N N 148 
GLN N    N  N N 149 
GLN CA   C  N S 150 
GLN C    C  N N 151 
GLN O    O  N N 152 
GLN CB   C  N N 153 
GLN CG   C  N N 154 
GLN CD   C  N N 155 
GLN OE1  O  N N 156 
GLN NE2  N  N N 157 
GLN OXT  O  N N 158 
GLN H    H  N N 159 
GLN H2   H  N N 160 
GLN HA   H  N N 161 
GLN HB2  H  N N 162 
GLN HB3  H  N N 163 
GLN HG2  H  N N 164 
GLN HG3  H  N N 165 
GLN HE21 H  N N 166 
GLN HE22 H  N N 167 
GLN HXT  H  N N 168 
GLU N    N  N N 169 
GLU CA   C  N S 170 
GLU C    C  N N 171 
GLU O    O  N N 172 
GLU CB   C  N N 173 
GLU CG   C  N N 174 
GLU CD   C  N N 175 
GLU OE1  O  N N 176 
GLU OE2  O  N N 177 
GLU OXT  O  N N 178 
GLU H    H  N N 179 
GLU H2   H  N N 180 
GLU HA   H  N N 181 
GLU HB2  H  N N 182 
GLU HB3  H  N N 183 
GLU HG2  H  N N 184 
GLU HG3  H  N N 185 
GLU HE2  H  N N 186 
GLU HXT  H  N N 187 
GLY N    N  N N 188 
GLY CA   C  N N 189 
GLY C    C  N N 190 
GLY O    O  N N 191 
GLY OXT  O  N N 192 
GLY H    H  N N 193 
GLY H2   H  N N 194 
GLY HA2  H  N N 195 
GLY HA3  H  N N 196 
GLY HXT  H  N N 197 
HIS N    N  N N 198 
HIS CA   C  N S 199 
HIS C    C  N N 200 
HIS O    O  N N 201 
HIS CB   C  N N 202 
HIS CG   C  Y N 203 
HIS ND1  N  Y N 204 
HIS CD2  C  Y N 205 
HIS CE1  C  Y N 206 
HIS NE2  N  Y N 207 
HIS OXT  O  N N 208 
HIS H    H  N N 209 
HIS H2   H  N N 210 
HIS HA   H  N N 211 
HIS HB2  H  N N 212 
HIS HB3  H  N N 213 
HIS HD1  H  N N 214 
HIS HD2  H  N N 215 
HIS HE1  H  N N 216 
HIS HE2  H  N N 217 
HIS HXT  H  N N 218 
HOH O    O  N N 219 
HOH H1   H  N N 220 
HOH H2   H  N N 221 
ILE N    N  N N 222 
ILE CA   C  N S 223 
ILE C    C  N N 224 
ILE O    O  N N 225 
ILE CB   C  N S 226 
ILE CG1  C  N N 227 
ILE CG2  C  N N 228 
ILE CD1  C  N N 229 
ILE OXT  O  N N 230 
ILE H    H  N N 231 
ILE H2   H  N N 232 
ILE HA   H  N N 233 
ILE HB   H  N N 234 
ILE HG12 H  N N 235 
ILE HG13 H  N N 236 
ILE HG21 H  N N 237 
ILE HG22 H  N N 238 
ILE HG23 H  N N 239 
ILE HD11 H  N N 240 
ILE HD12 H  N N 241 
ILE HD13 H  N N 242 
ILE HXT  H  N N 243 
LEU N    N  N N 244 
LEU CA   C  N S 245 
LEU C    C  N N 246 
LEU O    O  N N 247 
LEU CB   C  N N 248 
LEU CG   C  N N 249 
LEU CD1  C  N N 250 
LEU CD2  C  N N 251 
LEU OXT  O  N N 252 
LEU H    H  N N 253 
LEU H2   H  N N 254 
LEU HA   H  N N 255 
LEU HB2  H  N N 256 
LEU HB3  H  N N 257 
LEU HG   H  N N 258 
LEU HD11 H  N N 259 
LEU HD12 H  N N 260 
LEU HD13 H  N N 261 
LEU HD21 H  N N 262 
LEU HD22 H  N N 263 
LEU HD23 H  N N 264 
LEU HXT  H  N N 265 
LYS N    N  N N 266 
LYS CA   C  N S 267 
LYS C    C  N N 268 
LYS O    O  N N 269 
LYS CB   C  N N 270 
LYS CG   C  N N 271 
LYS CD   C  N N 272 
LYS CE   C  N N 273 
LYS NZ   N  N N 274 
LYS OXT  O  N N 275 
LYS H    H  N N 276 
LYS H2   H  N N 277 
LYS HA   H  N N 278 
LYS HB2  H  N N 279 
LYS HB3  H  N N 280 
LYS HG2  H  N N 281 
LYS HG3  H  N N 282 
LYS HD2  H  N N 283 
LYS HD3  H  N N 284 
LYS HE2  H  N N 285 
LYS HE3  H  N N 286 
LYS HZ1  H  N N 287 
LYS HZ2  H  N N 288 
LYS HZ3  H  N N 289 
LYS HXT  H  N N 290 
MET N    N  N N 291 
MET CA   C  N S 292 
MET C    C  N N 293 
MET O    O  N N 294 
MET CB   C  N N 295 
MET CG   C  N N 296 
MET SD   S  N N 297 
MET CE   C  N N 298 
MET OXT  O  N N 299 
MET H    H  N N 300 
MET H2   H  N N 301 
MET HA   H  N N 302 
MET HB2  H  N N 303 
MET HB3  H  N N 304 
MET HG2  H  N N 305 
MET HG3  H  N N 306 
MET HE1  H  N N 307 
MET HE2  H  N N 308 
MET HE3  H  N N 309 
MET HXT  H  N N 310 
PHE N    N  N N 311 
PHE CA   C  N S 312 
PHE C    C  N N 313 
PHE O    O  N N 314 
PHE CB   C  N N 315 
PHE CG   C  Y N 316 
PHE CD1  C  Y N 317 
PHE CD2  C  Y N 318 
PHE CE1  C  Y N 319 
PHE CE2  C  Y N 320 
PHE CZ   C  Y N 321 
PHE OXT  O  N N 322 
PHE H    H  N N 323 
PHE H2   H  N N 324 
PHE HA   H  N N 325 
PHE HB2  H  N N 326 
PHE HB3  H  N N 327 
PHE HD1  H  N N 328 
PHE HD2  H  N N 329 
PHE HE1  H  N N 330 
PHE HE2  H  N N 331 
PHE HZ   H  N N 332 
PHE HXT  H  N N 333 
PRO N    N  N N 334 
PRO CA   C  N S 335 
PRO C    C  N N 336 
PRO O    O  N N 337 
PRO CB   C  N N 338 
PRO CG   C  N N 339 
PRO CD   C  N N 340 
PRO OXT  O  N N 341 
PRO H    H  N N 342 
PRO HA   H  N N 343 
PRO HB2  H  N N 344 
PRO HB3  H  N N 345 
PRO HG2  H  N N 346 
PRO HG3  H  N N 347 
PRO HD2  H  N N 348 
PRO HD3  H  N N 349 
PRO HXT  H  N N 350 
SER N    N  N N 351 
SER CA   C  N S 352 
SER C    C  N N 353 
SER O    O  N N 354 
SER CB   C  N N 355 
SER OG   O  N N 356 
SER OXT  O  N N 357 
SER H    H  N N 358 
SER H2   H  N N 359 
SER HA   H  N N 360 
SER HB2  H  N N 361 
SER HB3  H  N N 362 
SER HG   H  N N 363 
SER HXT  H  N N 364 
THR N    N  N N 365 
THR CA   C  N S 366 
THR C    C  N N 367 
THR O    O  N N 368 
THR CB   C  N R 369 
THR OG1  O  N N 370 
THR CG2  C  N N 371 
THR OXT  O  N N 372 
THR H    H  N N 373 
THR H2   H  N N 374 
THR HA   H  N N 375 
THR HB   H  N N 376 
THR HG1  H  N N 377 
THR HG21 H  N N 378 
THR HG22 H  N N 379 
THR HG23 H  N N 380 
THR HXT  H  N N 381 
TRP N    N  N N 382 
TRP CA   C  N S 383 
TRP C    C  N N 384 
TRP O    O  N N 385 
TRP CB   C  N N 386 
TRP CG   C  Y N 387 
TRP CD1  C  Y N 388 
TRP CD2  C  Y N 389 
TRP NE1  N  Y N 390 
TRP CE2  C  Y N 391 
TRP CE3  C  Y N 392 
TRP CZ2  C  Y N 393 
TRP CZ3  C  Y N 394 
TRP CH2  C  Y N 395 
TRP OXT  O  N N 396 
TRP H    H  N N 397 
TRP H2   H  N N 398 
TRP HA   H  N N 399 
TRP HB2  H  N N 400 
TRP HB3  H  N N 401 
TRP HD1  H  N N 402 
TRP HE1  H  N N 403 
TRP HE3  H  N N 404 
TRP HZ2  H  N N 405 
TRP HZ3  H  N N 406 
TRP HH2  H  N N 407 
TRP HXT  H  N N 408 
TYR N    N  N N 409 
TYR CA   C  N S 410 
TYR C    C  N N 411 
TYR O    O  N N 412 
TYR CB   C  N N 413 
TYR CG   C  Y N 414 
TYR CD1  C  Y N 415 
TYR CD2  C  Y N 416 
TYR CE1  C  Y N 417 
TYR CE2  C  Y N 418 
TYR CZ   C  Y N 419 
TYR OH   O  N N 420 
TYR OXT  O  N N 421 
TYR H    H  N N 422 
TYR H2   H  N N 423 
TYR HA   H  N N 424 
TYR HB2  H  N N 425 
TYR HB3  H  N N 426 
TYR HD1  H  N N 427 
TYR HD2  H  N N 428 
TYR HE1  H  N N 429 
TYR HE2  H  N N 430 
TYR HH   H  N N 431 
TYR HXT  H  N N 432 
VAL N    N  N N 433 
VAL CA   C  N S 434 
VAL C    C  N N 435 
VAL O    O  N N 436 
VAL CB   C  N N 437 
VAL CG1  C  N N 438 
VAL CG2  C  N N 439 
VAL OXT  O  N N 440 
VAL H    H  N N 441 
VAL H2   H  N N 442 
VAL HA   H  N N 443 
VAL HB   H  N N 444 
VAL HG11 H  N N 445 
VAL HG12 H  N N 446 
VAL HG13 H  N N 447 
VAL HG21 H  N N 448 
VAL HG22 H  N N 449 
VAL HG23 H  N N 450 
VAL HXT  H  N N 451 
ZN  ZN   ZN N N 452 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
3TV C14 C13  sing N N 1   
3TV C13 C12  sing N N 2   
3TV S11 C12  sing N N 3   
3TV S11 C8   sing N N 4   
3TV F18 C7   sing N N 5   
3TV C8  C7   doub Y N 6   
3TV C8  C9   sing Y N 7   
3TV C7  C6   sing Y N 8   
3TV F15 C9   sing N N 9   
3TV C9  C10  doub Y N 10  
3TV C6  F17  sing N N 11  
3TV C6  C5   doub Y N 12  
3TV C10 C5   sing Y N 13  
3TV C10 F16  sing N N 14  
3TV C5  S1   sing N N 15  
3TV N2  S1   sing N N 16  
3TV S1  O4   doub N N 17  
3TV S1  O3   doub N N 18  
3TV C12 H1   sing N N 19  
3TV C12 H2   sing N N 20  
3TV C13 H3   sing N N 21  
3TV C13 H4   sing N N 22  
3TV C14 H5   sing N N 23  
3TV C14 H6   sing N N 24  
3TV C14 H7   sing N N 25  
3TV N2  H8   sing N N 26  
3TV N2  H9   sing N N 27  
ALA N   CA   sing N N 28  
ALA N   H    sing N N 29  
ALA N   H2   sing N N 30  
ALA CA  C    sing N N 31  
ALA CA  CB   sing N N 32  
ALA CA  HA   sing N N 33  
ALA C   O    doub N N 34  
ALA C   OXT  sing N N 35  
ALA CB  HB1  sing N N 36  
ALA CB  HB2  sing N N 37  
ALA CB  HB3  sing N N 38  
ALA OXT HXT  sing N N 39  
ARG N   CA   sing N N 40  
ARG N   H    sing N N 41  
ARG N   H2   sing N N 42  
ARG CA  C    sing N N 43  
ARG CA  CB   sing N N 44  
ARG CA  HA   sing N N 45  
ARG C   O    doub N N 46  
ARG C   OXT  sing N N 47  
ARG CB  CG   sing N N 48  
ARG CB  HB2  sing N N 49  
ARG CB  HB3  sing N N 50  
ARG CG  CD   sing N N 51  
ARG CG  HG2  sing N N 52  
ARG CG  HG3  sing N N 53  
ARG CD  NE   sing N N 54  
ARG CD  HD2  sing N N 55  
ARG CD  HD3  sing N N 56  
ARG NE  CZ   sing N N 57  
ARG NE  HE   sing N N 58  
ARG CZ  NH1  sing N N 59  
ARG CZ  NH2  doub N N 60  
ARG NH1 HH11 sing N N 61  
ARG NH1 HH12 sing N N 62  
ARG NH2 HH21 sing N N 63  
ARG NH2 HH22 sing N N 64  
ARG OXT HXT  sing N N 65  
ASN N   CA   sing N N 66  
ASN N   H    sing N N 67  
ASN N   H2   sing N N 68  
ASN CA  C    sing N N 69  
ASN CA  CB   sing N N 70  
ASN CA  HA   sing N N 71  
ASN C   O    doub N N 72  
ASN C   OXT  sing N N 73  
ASN CB  CG   sing N N 74  
ASN CB  HB2  sing N N 75  
ASN CB  HB3  sing N N 76  
ASN CG  OD1  doub N N 77  
ASN CG  ND2  sing N N 78  
ASN ND2 HD21 sing N N 79  
ASN ND2 HD22 sing N N 80  
ASN OXT HXT  sing N N 81  
ASP N   CA   sing N N 82  
ASP N   H    sing N N 83  
ASP N   H2   sing N N 84  
ASP CA  C    sing N N 85  
ASP CA  CB   sing N N 86  
ASP CA  HA   sing N N 87  
ASP C   O    doub N N 88  
ASP C   OXT  sing N N 89  
ASP CB  CG   sing N N 90  
ASP CB  HB2  sing N N 91  
ASP CB  HB3  sing N N 92  
ASP CG  OD1  doub N N 93  
ASP CG  OD2  sing N N 94  
ASP OD2 HD2  sing N N 95  
ASP OXT HXT  sing N N 96  
BCN N1  C1   sing N N 97  
BCN N1  C3   sing N N 98  
BCN N1  C5   sing N N 99  
BCN C1  C2   sing N N 100 
BCN C1  H11  sing N N 101 
BCN C1  H12  sing N N 102 
BCN C2  O21  doub N N 103 
BCN C2  O22  sing N N 104 
BCN O22 HO2  sing N N 105 
BCN C3  C4   sing N N 106 
BCN C3  H31  sing N N 107 
BCN C3  H32  sing N N 108 
BCN C4  O4   sing N N 109 
BCN C4  H41  sing N N 110 
BCN C4  H42  sing N N 111 
BCN O4  HO4  sing N N 112 
BCN C5  C6   sing N N 113 
BCN C5  H51  sing N N 114 
BCN C5  H52  sing N N 115 
BCN C6  O6   sing N N 116 
BCN C6  H61  sing N N 117 
BCN C6  H62  sing N N 118 
BCN O6  HO6  sing N N 119 
CYS N   CA   sing N N 120 
CYS N   H    sing N N 121 
CYS N   H2   sing N N 122 
CYS CA  C    sing N N 123 
CYS CA  CB   sing N N 124 
CYS CA  HA   sing N N 125 
CYS C   O    doub N N 126 
CYS C   OXT  sing N N 127 
CYS CB  SG   sing N N 128 
CYS CB  HB2  sing N N 129 
CYS CB  HB3  sing N N 130 
CYS SG  HG   sing N N 131 
CYS OXT HXT  sing N N 132 
DMS S   O    doub N N 133 
DMS S   C1   sing N N 134 
DMS S   C2   sing N N 135 
DMS C1  H11  sing N N 136 
DMS C1  H12  sing N N 137 
DMS C1  H13  sing N N 138 
DMS C2  H21  sing N N 139 
DMS C2  H22  sing N N 140 
DMS C2  H23  sing N N 141 
GLN N   CA   sing N N 142 
GLN N   H    sing N N 143 
GLN N   H2   sing N N 144 
GLN CA  C    sing N N 145 
GLN CA  CB   sing N N 146 
GLN CA  HA   sing N N 147 
GLN C   O    doub N N 148 
GLN C   OXT  sing N N 149 
GLN CB  CG   sing N N 150 
GLN CB  HB2  sing N N 151 
GLN CB  HB3  sing N N 152 
GLN CG  CD   sing N N 153 
GLN CG  HG2  sing N N 154 
GLN CG  HG3  sing N N 155 
GLN CD  OE1  doub N N 156 
GLN CD  NE2  sing N N 157 
GLN NE2 HE21 sing N N 158 
GLN NE2 HE22 sing N N 159 
GLN OXT HXT  sing N N 160 
GLU N   CA   sing N N 161 
GLU N   H    sing N N 162 
GLU N   H2   sing N N 163 
GLU CA  C    sing N N 164 
GLU CA  CB   sing N N 165 
GLU CA  HA   sing N N 166 
GLU C   O    doub N N 167 
GLU C   OXT  sing N N 168 
GLU CB  CG   sing N N 169 
GLU CB  HB2  sing N N 170 
GLU CB  HB3  sing N N 171 
GLU CG  CD   sing N N 172 
GLU CG  HG2  sing N N 173 
GLU CG  HG3  sing N N 174 
GLU CD  OE1  doub N N 175 
GLU CD  OE2  sing N N 176 
GLU OE2 HE2  sing N N 177 
GLU OXT HXT  sing N N 178 
GLY N   CA   sing N N 179 
GLY N   H    sing N N 180 
GLY N   H2   sing N N 181 
GLY CA  C    sing N N 182 
GLY CA  HA2  sing N N 183 
GLY CA  HA3  sing N N 184 
GLY C   O    doub N N 185 
GLY C   OXT  sing N N 186 
GLY OXT HXT  sing N N 187 
HIS N   CA   sing N N 188 
HIS N   H    sing N N 189 
HIS N   H2   sing N N 190 
HIS CA  C    sing N N 191 
HIS CA  CB   sing N N 192 
HIS CA  HA   sing N N 193 
HIS C   O    doub N N 194 
HIS C   OXT  sing N N 195 
HIS CB  CG   sing N N 196 
HIS CB  HB2  sing N N 197 
HIS CB  HB3  sing N N 198 
HIS CG  ND1  sing Y N 199 
HIS CG  CD2  doub Y N 200 
HIS ND1 CE1  doub Y N 201 
HIS ND1 HD1  sing N N 202 
HIS CD2 NE2  sing Y N 203 
HIS CD2 HD2  sing N N 204 
HIS CE1 NE2  sing Y N 205 
HIS CE1 HE1  sing N N 206 
HIS NE2 HE2  sing N N 207 
HIS OXT HXT  sing N N 208 
HOH O   H1   sing N N 209 
HOH O   H2   sing N N 210 
ILE N   CA   sing N N 211 
ILE N   H    sing N N 212 
ILE N   H2   sing N N 213 
ILE CA  C    sing N N 214 
ILE CA  CB   sing N N 215 
ILE CA  HA   sing N N 216 
ILE C   O    doub N N 217 
ILE C   OXT  sing N N 218 
ILE CB  CG1  sing N N 219 
ILE CB  CG2  sing N N 220 
ILE CB  HB   sing N N 221 
ILE CG1 CD1  sing N N 222 
ILE CG1 HG12 sing N N 223 
ILE CG1 HG13 sing N N 224 
ILE CG2 HG21 sing N N 225 
ILE CG2 HG22 sing N N 226 
ILE CG2 HG23 sing N N 227 
ILE CD1 HD11 sing N N 228 
ILE CD1 HD12 sing N N 229 
ILE CD1 HD13 sing N N 230 
ILE OXT HXT  sing N N 231 
LEU N   CA   sing N N 232 
LEU N   H    sing N N 233 
LEU N   H2   sing N N 234 
LEU CA  C    sing N N 235 
LEU CA  CB   sing N N 236 
LEU CA  HA   sing N N 237 
LEU C   O    doub N N 238 
LEU C   OXT  sing N N 239 
LEU CB  CG   sing N N 240 
LEU CB  HB2  sing N N 241 
LEU CB  HB3  sing N N 242 
LEU CG  CD1  sing N N 243 
LEU CG  CD2  sing N N 244 
LEU CG  HG   sing N N 245 
LEU CD1 HD11 sing N N 246 
LEU CD1 HD12 sing N N 247 
LEU CD1 HD13 sing N N 248 
LEU CD2 HD21 sing N N 249 
LEU CD2 HD22 sing N N 250 
LEU CD2 HD23 sing N N 251 
LEU OXT HXT  sing N N 252 
LYS N   CA   sing N N 253 
LYS N   H    sing N N 254 
LYS N   H2   sing N N 255 
LYS CA  C    sing N N 256 
LYS CA  CB   sing N N 257 
LYS CA  HA   sing N N 258 
LYS C   O    doub N N 259 
LYS C   OXT  sing N N 260 
LYS CB  CG   sing N N 261 
LYS CB  HB2  sing N N 262 
LYS CB  HB3  sing N N 263 
LYS CG  CD   sing N N 264 
LYS CG  HG2  sing N N 265 
LYS CG  HG3  sing N N 266 
LYS CD  CE   sing N N 267 
LYS CD  HD2  sing N N 268 
LYS CD  HD3  sing N N 269 
LYS CE  NZ   sing N N 270 
LYS CE  HE2  sing N N 271 
LYS CE  HE3  sing N N 272 
LYS NZ  HZ1  sing N N 273 
LYS NZ  HZ2  sing N N 274 
LYS NZ  HZ3  sing N N 275 
LYS OXT HXT  sing N N 276 
MET N   CA   sing N N 277 
MET N   H    sing N N 278 
MET N   H2   sing N N 279 
MET CA  C    sing N N 280 
MET CA  CB   sing N N 281 
MET CA  HA   sing N N 282 
MET C   O    doub N N 283 
MET C   OXT  sing N N 284 
MET CB  CG   sing N N 285 
MET CB  HB2  sing N N 286 
MET CB  HB3  sing N N 287 
MET CG  SD   sing N N 288 
MET CG  HG2  sing N N 289 
MET CG  HG3  sing N N 290 
MET SD  CE   sing N N 291 
MET CE  HE1  sing N N 292 
MET CE  HE2  sing N N 293 
MET CE  HE3  sing N N 294 
MET OXT HXT  sing N N 295 
PHE N   CA   sing N N 296 
PHE N   H    sing N N 297 
PHE N   H2   sing N N 298 
PHE CA  C    sing N N 299 
PHE CA  CB   sing N N 300 
PHE CA  HA   sing N N 301 
PHE C   O    doub N N 302 
PHE C   OXT  sing N N 303 
PHE CB  CG   sing N N 304 
PHE CB  HB2  sing N N 305 
PHE CB  HB3  sing N N 306 
PHE CG  CD1  doub Y N 307 
PHE CG  CD2  sing Y N 308 
PHE CD1 CE1  sing Y N 309 
PHE CD1 HD1  sing N N 310 
PHE CD2 CE2  doub Y N 311 
PHE CD2 HD2  sing N N 312 
PHE CE1 CZ   doub Y N 313 
PHE CE1 HE1  sing N N 314 
PHE CE2 CZ   sing Y N 315 
PHE CE2 HE2  sing N N 316 
PHE CZ  HZ   sing N N 317 
PHE OXT HXT  sing N N 318 
PRO N   CA   sing N N 319 
PRO N   CD   sing N N 320 
PRO N   H    sing N N 321 
PRO CA  C    sing N N 322 
PRO CA  CB   sing N N 323 
PRO CA  HA   sing N N 324 
PRO C   O    doub N N 325 
PRO C   OXT  sing N N 326 
PRO CB  CG   sing N N 327 
PRO CB  HB2  sing N N 328 
PRO CB  HB3  sing N N 329 
PRO CG  CD   sing N N 330 
PRO CG  HG2  sing N N 331 
PRO CG  HG3  sing N N 332 
PRO CD  HD2  sing N N 333 
PRO CD  HD3  sing N N 334 
PRO OXT HXT  sing N N 335 
SER N   CA   sing N N 336 
SER N   H    sing N N 337 
SER N   H2   sing N N 338 
SER CA  C    sing N N 339 
SER CA  CB   sing N N 340 
SER CA  HA   sing N N 341 
SER C   O    doub N N 342 
SER C   OXT  sing N N 343 
SER CB  OG   sing N N 344 
SER CB  HB2  sing N N 345 
SER CB  HB3  sing N N 346 
SER OG  HG   sing N N 347 
SER OXT HXT  sing N N 348 
THR N   CA   sing N N 349 
THR N   H    sing N N 350 
THR N   H2   sing N N 351 
THR CA  C    sing N N 352 
THR CA  CB   sing N N 353 
THR CA  HA   sing N N 354 
THR C   O    doub N N 355 
THR C   OXT  sing N N 356 
THR CB  OG1  sing N N 357 
THR CB  CG2  sing N N 358 
THR CB  HB   sing N N 359 
THR OG1 HG1  sing N N 360 
THR CG2 HG21 sing N N 361 
THR CG2 HG22 sing N N 362 
THR CG2 HG23 sing N N 363 
THR OXT HXT  sing N N 364 
TRP N   CA   sing N N 365 
TRP N   H    sing N N 366 
TRP N   H2   sing N N 367 
TRP CA  C    sing N N 368 
TRP CA  CB   sing N N 369 
TRP CA  HA   sing N N 370 
TRP C   O    doub N N 371 
TRP C   OXT  sing N N 372 
TRP CB  CG   sing N N 373 
TRP CB  HB2  sing N N 374 
TRP CB  HB3  sing N N 375 
TRP CG  CD1  doub Y N 376 
TRP CG  CD2  sing Y N 377 
TRP CD1 NE1  sing Y N 378 
TRP CD1 HD1  sing N N 379 
TRP CD2 CE2  doub Y N 380 
TRP CD2 CE3  sing Y N 381 
TRP NE1 CE2  sing Y N 382 
TRP NE1 HE1  sing N N 383 
TRP CE2 CZ2  sing Y N 384 
TRP CE3 CZ3  doub Y N 385 
TRP CE3 HE3  sing N N 386 
TRP CZ2 CH2  doub Y N 387 
TRP CZ2 HZ2  sing N N 388 
TRP CZ3 CH2  sing Y N 389 
TRP CZ3 HZ3  sing N N 390 
TRP CH2 HH2  sing N N 391 
TRP OXT HXT  sing N N 392 
TYR N   CA   sing N N 393 
TYR N   H    sing N N 394 
TYR N   H2   sing N N 395 
TYR CA  C    sing N N 396 
TYR CA  CB   sing N N 397 
TYR CA  HA   sing N N 398 
TYR C   O    doub N N 399 
TYR C   OXT  sing N N 400 
TYR CB  CG   sing N N 401 
TYR CB  HB2  sing N N 402 
TYR CB  HB3  sing N N 403 
TYR CG  CD1  doub Y N 404 
TYR CG  CD2  sing Y N 405 
TYR CD1 CE1  sing Y N 406 
TYR CD1 HD1  sing N N 407 
TYR CD2 CE2  doub Y N 408 
TYR CD2 HD2  sing N N 409 
TYR CE1 CZ   doub Y N 410 
TYR CE1 HE1  sing N N 411 
TYR CE2 CZ   sing Y N 412 
TYR CE2 HE2  sing N N 413 
TYR CZ  OH   sing N N 414 
TYR OH  HH   sing N N 415 
TYR OXT HXT  sing N N 416 
VAL N   CA   sing N N 417 
VAL N   H    sing N N 418 
VAL N   H2   sing N N 419 
VAL CA  C    sing N N 420 
VAL CA  CB   sing N N 421 
VAL CA  HA   sing N N 422 
VAL C   O    doub N N 423 
VAL C   OXT  sing N N 424 
VAL CB  CG1  sing N N 425 
VAL CB  CG2  sing N N 426 
VAL CB  HB   sing N N 427 
VAL CG1 HG11 sing N N 428 
VAL CG1 HG12 sing N N 429 
VAL CG1 HG13 sing N N 430 
VAL CG2 HG21 sing N N 431 
VAL CG2 HG22 sing N N 432 
VAL CG2 HG23 sing N N 433 
VAL OXT HXT  sing N N 434 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        3TV 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   3TV 
_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        ? 
# 
_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                    7NZS 
_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.fract_transf_matrix[1][1]   0.023736 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.005999 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.024211 
_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]   0.014476 
_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  
F  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . HIS A 1 4   ? 32.286  1.391   7.868   1.00 39.58 ? 4   HIS A N   1 
ATOM   2    C  CA  . HIS A 1 4   ? 31.139  1.911   8.648   1.00 31.50 ? 4   HIS A CA  1 
ATOM   3    C  C   . HIS A 1 4   ? 30.509  0.819   9.510   1.00 26.56 ? 4   HIS A C   1 
ATOM   4    O  O   . HIS A 1 4   ? 30.860  -0.349  9.375   1.00 30.17 ? 4   HIS A O   1 
ATOM   5    C  CB  . HIS A 1 4   ? 30.171  2.627   7.728   1.00 28.72 ? 4   HIS A CB  1 
ATOM   6    C  CG  . HIS A 1 4   ? 29.816  3.856   8.438   1.00 31.02 ? 4   HIS A CG  1 
ATOM   7    N  ND1 . HIS A 1 4   ? 28.723  4.624   8.084   1.00 35.04 ? 4   HIS A ND1 1 
ATOM   8    C  CD2 . HIS A 1 4   ? 30.390  4.478   9.489   1.00 31.06 ? 4   HIS A CD2 1 
ATOM   9    C  CE1 . HIS A 1 4   ? 28.642  5.666   8.887   1.00 42.19 ? 4   HIS A CE1 1 
ATOM   10   N  NE2 . HIS A 1 4   ? 29.653  5.599   9.759   1.00 41.59 ? 4   HIS A NE2 1 
ATOM   11   N  N   . TRP A 1 5   ? 29.554  1.210   10.371  1.00 22.42 ? 5   TRP A N   1 
ATOM   12   C  CA  . TRP A 1 5   ? 28.946  0.246   11.282  1.00 19.34 ? 5   TRP A CA  1 
ATOM   13   C  C   . TRP A 1 5   ? 27.949  -0.559  10.460  1.00 20.93 ? 5   TRP A C   1 
ATOM   14   O  O   . TRP A 1 5   ? 27.497  -0.085  9.416   1.00 22.95 ? 5   TRP A O   1 
ATOM   15   C  CB  . TRP A 1 5   ? 28.242  0.952   12.464  1.00 18.10 ? 5   TRP A CB  1 
ATOM   16   C  CG  . TRP A 1 5   ? 27.043  1.771   12.068  1.00 18.54 ? 5   TRP A CG  1 
ATOM   17   C  CD1 . TRP A 1 5   ? 26.991  3.085   11.688  1.00 20.26 ? 5   TRP A CD1 1 
ATOM   18   C  CD2 . TRP A 1 5   ? 25.694  1.294   12.022  1.00 19.35 ? 5   TRP A CD2 1 
ATOM   19   N  NE1 . TRP A 1 5   ? 25.698  3.449   11.421  1.00 20.58 ? 5   TRP A NE1 1 
ATOM   20   C  CE2 . TRP A 1 5   ? 24.884  2.368   11.627  1.00 18.81 ? 5   TRP A CE2 1 
ATOM   21   C  CE3 . TRP A 1 5   ? 25.122  0.058   12.317  1.00 16.83 ? 5   TRP A CE3 1 
ATOM   22   C  CZ2 . TRP A 1 5   ? 23.510  2.233   11.478  1.00 17.27 ? 5   TRP A CZ2 1 
ATOM   23   C  CZ3 . TRP A 1 5   ? 23.751  -0.086  12.154  1.00 18.18 ? 5   TRP A CZ3 1 
ATOM   24   C  CH2 . TRP A 1 5   ? 22.992  1.001   11.753  1.00 18.00 ? 5   TRP A CH2 1 
ATOM   25   N  N   . GLY A 1 6   ? 27.611  -1.734  10.993  1.00 17.37 ? 6   GLY A N   1 
ATOM   26   C  CA  . GLY A 1 6   ? 26.631  -2.600  10.361  1.00 17.93 ? 6   GLY A CA  1 
ATOM   27   C  C   . GLY A 1 6   ? 26.246  -3.728  11.309  1.00 18.08 ? 6   GLY A C   1 
ATOM   28   O  O   . GLY A 1 6   ? 26.289  -3.580  12.535  1.00 18.52 ? 6   GLY A O   1 
ATOM   29   N  N   . TYR A 1 7   ? 25.933  -4.876  10.735  1.00 19.18 ? 7   TYR A N   1 
ATOM   30   C  CA  . TYR A 1 7   ? 25.537  -5.987  11.581  1.00 20.36 ? 7   TYR A CA  1 
ATOM   31   C  C   . TYR A 1 7   ? 26.492  -7.173  11.551  1.00 26.88 ? 7   TYR A C   1 
ATOM   32   O  O   . TYR A 1 7   ? 26.288  -8.133  12.305  1.00 26.75 ? 7   TYR A O   1 
ATOM   33   C  CB  . TYR A 1 7   ? 24.071  -6.305  11.304  1.00 18.39 ? 7   TYR A CB  1 
ATOM   34   C  CG  . TYR A 1 7   ? 23.163  -5.227  11.823  1.00 16.58 ? 7   TYR A CG  1 
ATOM   35   C  CD1 . TYR A 1 7   ? 22.784  -5.231  13.156  1.00 15.49 ? 7   TYR A CD1 1 
ATOM   36   C  CD2 . TYR A 1 7   ? 22.691  -4.194  11.011  1.00 15.53 ? 7   TYR A CD2 1 
ATOM   37   C  CE1 . TYR A 1 7   ? 21.945  -4.216  13.633  1.00 14.92 ? 7   TYR A CE1 1 
ATOM   38   C  CE2 . TYR A 1 7   ? 21.841  -3.192  11.461  1.00 14.45 ? 7   TYR A CE2 1 
ATOM   39   C  CZ  . TYR A 1 7   ? 21.454  -3.237  12.796  1.00 15.32 ? 7   TYR A CZ  1 
ATOM   40   O  OH  . TYR A 1 7   ? 20.605  -2.265  13.234  1.00 15.88 ? 7   TYR A OH  1 
ATOM   41   N  N   . GLY A 1 8   ? 27.571  -7.071  10.757  1.00 26.94 ? 8   GLY A N   1 
ATOM   42   C  CA  . GLY A 1 8   ? 28.480  -8.218  10.606  1.00 28.40 ? 8   GLY A CA  1 
ATOM   43   C  C   . GLY A 1 8   ? 29.484  -8.450  11.738  1.00 27.78 ? 8   GLY A C   1 
ATOM   44   O  O   . GLY A 1 8   ? 29.616  -7.670  12.702  1.00 29.79 ? 8   GLY A O   1 
ATOM   45   N  N   . LYS A 1 9   ? 30.277  -9.535  11.583  1.00 31.16 ? 9   LYS A N   1 
ATOM   46   C  CA  . LYS A 1 9   ? 31.339  -9.922  12.513  1.00 32.35 ? 9   LYS A CA  1 
ATOM   47   C  C   . LYS A 1 9   ? 32.318  -8.763  12.674  1.00 30.16 ? 9   LYS A C   1 
ATOM   48   O  O   . LYS A 1 9   ? 32.821  -8.540  13.783  1.00 31.45 ? 9   LYS A O   1 
ATOM   49   C  CB  . LYS A 1 9   ? 32.130  -11.134 12.008  1.00 30.68 ? 9   LYS A CB  1 
ATOM   50   N  N   . HIS A 1 10  ? 32.460  -8.010  11.565  1.00 31.23 ? 10  HIS A N   1 
ATOM   51   C  CA  . HIS A 1 10  ? 33.506  -7.015  11.412  1.00 26.72 ? 10  HIS A CA  1 
ATOM   52   C  C   . HIS A 1 10  ? 33.040  -5.661  11.918  1.00 22.55 ? 10  HIS A C   1 
ATOM   53   O  O   . HIS A 1 10  ? 33.853  -4.899  12.415  1.00 24.48 ? 10  HIS A O   1 
ATOM   54   C  CB  . HIS A 1 10  ? 34.121  -7.036  10.000  1.00 25.30 ? 10  HIS A CB  1 
ATOM   55   C  CG  . HIS A 1 10  ? 34.673  -8.387  9.673   1.00 29.57 ? 10  HIS A CG  1 
ATOM   56   N  ND1 . HIS A 1 10  ? 35.606  -9.004  10.505  1.00 29.53 ? 10  HIS A ND1 1 
ATOM   57   C  CD2 . HIS A 1 10  ? 34.402  -9.268  8.678   1.00 33.14 ? 10  HIS A CD2 1 
ATOM   58   C  CE1 . HIS A 1 10  ? 35.878  -10.218 10.047  1.00 28.56 ? 10  HIS A CE1 1 
ATOM   59   N  NE2 . HIS A 1 10  ? 35.173  -10.395 8.902   1.00 33.50 ? 10  HIS A NE2 1 
ATOM   60   N  N   . ASN A 1 11  ? 31.720  -5.403  11.883  1.00 22.48 ? 11  ASN A N   1 
ATOM   61   C  CA  . ASN A 1 11  ? 31.302  -4.045  12.186  1.00 18.93 ? 11  ASN A CA  1 
ATOM   62   C  C   . ASN A 1 11  ? 29.973  -4.061  12.951  1.00 19.04 ? 11  ASN A C   1 
ATOM   63   O  O   . ASN A 1 11  ? 29.273  -3.051  12.970  1.00 19.27 ? 11  ASN A O   1 
ATOM   64   C  CB  . ASN A 1 11  ? 31.159  -3.254  10.895  1.00 19.37 ? 11  ASN A CB  1 
ATOM   65   C  CG  . ASN A 1 11  ? 30.077  -3.808  9.992   1.00 22.72 ? 11  ASN A CG  1 
ATOM   66   O  OD1 . ASN A 1 11  ? 29.507  -4.856  10.293  1.00 22.71 ? 11  ASN A OD1 1 
ATOM   67   N  ND2 . ASN A 1 11  ? 29.794  -3.122  8.889   1.00 24.53 ? 11  ASN A ND2 1 
ATOM   68   N  N   . GLY A 1 12  ? 29.668  -5.219  13.565  1.00 18.09 ? 12  GLY A N   1 
ATOM   69   C  CA  . GLY A 1 12  ? 28.383  -5.442  14.221  1.00 19.04 ? 12  GLY A CA  1 
ATOM   70   C  C   . GLY A 1 12  ? 28.305  -4.794  15.599  1.00 18.53 ? 12  GLY A C   1 
ATOM   71   O  O   . GLY A 1 12  ? 29.191  -4.092  16.072  1.00 18.61 ? 12  GLY A O   1 
ATOM   72   N  N   . PRO A 1 13  ? 27.188  -5.072  16.307  1.00 17.60 ? 13  PRO A N   1 
ATOM   73   C  CA  . PRO A 1 13  ? 26.956  -4.497  17.631  1.00 18.06 ? 13  PRO A CA  1 
ATOM   74   C  C   . PRO A 1 13  ? 28.103  -4.501  18.636  1.00 17.00 ? 13  PRO A C   1 
ATOM   75   O  O   . PRO A 1 13  ? 28.269  -3.558  19.405  1.00 18.13 ? 13  PRO A O   1 
ATOM   76   C  CB  . PRO A 1 13  ? 25.820  -5.448  18.069  1.00 17.53 ? 13  PRO A CB  1 
ATOM   77   C  CG  . PRO A 1 13  ? 24.992  -5.598  16.864  1.00 17.29 ? 13  PRO A CG  1 
ATOM   78   C  CD  . PRO A 1 13  ? 26.038  -5.818  15.767  1.00 16.42 ? 13  PRO A CD  1 
ATOM   79   N  N   . GLU A 1 14  ? 28.937  -5.543  18.635  1.00 17.10 ? 14  GLU A N   1 
ATOM   80   C  CA  . GLU A 1 14  ? 30.037  -5.627  19.569  1.00 19.62 ? 14  GLU A CA  1 
ATOM   81   C  C   . GLU A 1 14  ? 31.165  -4.633  19.231  1.00 18.50 ? 14  GLU A C   1 
ATOM   82   O  O   . GLU A 1 14  ? 32.031  -4.361  20.063  1.00 18.96 ? 14  GLU A O   1 
ATOM   83   C  CB  . GLU A 1 14  ? 30.498  -7.077  19.501  1.00 22.64 ? 14  GLU A CB  1 
ATOM   84   C  CG  . GLU A 1 14  ? 31.159  -7.422  18.158  1.00 29.38 ? 14  GLU A CG  1 
ATOM   85   C  CD  . GLU A 1 14  ? 30.482  -8.060  16.939  1.00 34.18 ? 14  GLU A CD  1 
ATOM   86   O  OE1 . GLU A 1 14  ? 29.318  -7.710  16.661  1.00 26.15 ? 14  GLU A OE1 1 
ATOM   87   O  OE2 . GLU A 1 14  ? 31.125  -8.901  16.280  1.00 28.12 ? 14  GLU A OE2 1 
ATOM   88   N  N   . HIS A 1 15  ? 31.105  -4.054  18.027  1.00 18.60 ? 15  HIS A N   1 
ATOM   89   C  CA  . HIS A 1 15  ? 32.113  -3.080  17.596  1.00 18.20 ? 15  HIS A CA  1 
ATOM   90   C  C   . HIS A 1 15  ? 31.670  -1.629  17.793  1.00 17.33 ? 15  HIS A C   1 
ATOM   91   O  O   . HIS A 1 15  ? 32.486  -0.700  17.727  1.00 16.77 ? 15  HIS A O   1 
ATOM   92   C  CB  . HIS A 1 15  ? 32.490  -3.253  16.127  1.00 18.52 ? 15  HIS A CB  1 
ATOM   93   C  CG  . HIS A 1 15  ? 33.175  -4.551  15.858  1.00 20.80 ? 15  HIS A CG  1 
ATOM   94   N  ND1 . HIS A 1 15  ? 34.536  -4.698  16.026  1.00 23.33 ? 15  HIS A ND1 1 
ATOM   95   C  CD2 . HIS A 1 15  ? 32.692  -5.734  15.432  1.00 21.23 ? 15  HIS A CD2 1 
ATOM   96   C  CE1 . HIS A 1 15  ? 34.867  -5.928  15.696  1.00 21.33 ? 15  HIS A CE1 1 
ATOM   97   N  NE2 . HIS A 1 15  ? 33.774  -6.591  15.369  1.00 24.86 ? 15  HIS A NE2 1 
ATOM   98   N  N   . TRP A 1 16  ? 30.363  -1.404  18.031  1.00 16.99 ? 16  TRP A N   1 
ATOM   99   C  CA  . TRP A 1 16  ? 29.865  -0.046  17.896  1.00 15.15 ? 16  TRP A CA  1 
ATOM   100  C  C   . TRP A 1 16  ? 30.457  0.916   18.905  1.00 14.59 ? 16  TRP A C   1 
ATOM   101  O  O   . TRP A 1 16  ? 30.528  2.110   18.636  1.00 14.43 ? 16  TRP A O   1 
ATOM   102  C  CB  . TRP A 1 16  ? 28.324  -0.051  17.999  1.00 13.68 ? 16  TRP A CB  1 
ATOM   103  C  CG  . TRP A 1 16  ? 27.653  -0.764  16.875  1.00 15.18 ? 16  TRP A CG  1 
ATOM   104  C  CD1 . TRP A 1 16  ? 28.163  -1.181  15.686  1.00 14.06 ? 16  TRP A CD1 1 
ATOM   105  C  CD2 . TRP A 1 16  ? 26.261  -1.127  16.825  1.00 12.95 ? 16  TRP A CD2 1 
ATOM   106  N  NE1 . TRP A 1 16  ? 27.219  -1.791  14.918  1.00 15.74 ? 16  TRP A NE1 1 
ATOM   107  C  CE2 . TRP A 1 16  ? 26.027  -1.759  15.595  1.00 14.48 ? 16  TRP A CE2 1 
ATOM   108  C  CE3 . TRP A 1 16  ? 25.195  -0.928  17.716  1.00 14.87 ? 16  TRP A CE3 1 
ATOM   109  C  CZ2 . TRP A 1 16  ? 24.764  -2.209  15.194  1.00 15.83 ? 16  TRP A CZ2 1 
ATOM   110  C  CZ3 . TRP A 1 16  ? 23.959  -1.393  17.332  1.00 14.04 ? 16  TRP A CZ3 1 
ATOM   111  C  CH2 . TRP A 1 16  ? 23.738  -2.012  16.098  1.00 15.68 ? 16  TRP A CH2 1 
ATOM   112  N  N   . HIS A 1 17  ? 30.871  0.431   20.068  1.00 15.26 ? 17  HIS A N   1 
ATOM   113  C  CA  . HIS A 1 17  ? 31.303  1.285   21.154  1.00 15.65 ? 17  HIS A CA  1 
ATOM   114  C  C   . HIS A 1 17  ? 32.540  2.104   20.741  1.00 15.72 ? 17  HIS A C   1 
ATOM   115  O  O   . HIS A 1 17  ? 32.808  3.125   21.376  1.00 16.85 ? 17  HIS A O   1 
ATOM   116  C  CB  . HIS A 1 17  ? 31.582  0.458   22.426  1.00 15.73 ? 17  HIS A CB  1 
ATOM   117  C  CG  . HIS A 1 17  ? 32.794  -0.411  22.313  1.00 18.10 ? 17  HIS A CG  1 
ATOM   118  N  ND1 . HIS A 1 17  ? 34.008  -0.039  22.868  1.00 21.43 ? 17  HIS A ND1 1 
ATOM   119  C  CD2 . HIS A 1 17  ? 33.008  -1.548  21.634  1.00 17.53 ? 17  HIS A CD2 1 
ATOM   120  C  CE1 . HIS A 1 17  ? 34.914  -0.942  22.503  1.00 18.88 ? 17  HIS A CE1 1 
ATOM   121  N  NE2 . HIS A 1 17  ? 34.332  -1.881  21.789  1.00 20.91 ? 17  HIS A NE2 1 
ATOM   122  N  N   . LYS A 1 18  ? 33.294  1.581   19.763  1.00 18.66 ? 18  LYS A N   1 
ATOM   123  C  CA  . LYS A 1 18  ? 34.540  2.274   19.451  1.00 19.33 ? 18  LYS A CA  1 
ATOM   124  C  C   . LYS A 1 18  ? 34.225  3.615   18.783  1.00 22.57 ? 18  LYS A C   1 
ATOM   125  O  O   . LYS A 1 18  ? 34.970  4.569   18.949  1.00 26.33 ? 18  LYS A O   1 
ATOM   126  C  CB  . LYS A 1 18  ? 35.406  1.384   18.559  1.00 20.91 ? 18  LYS A CB  1 
ATOM   127  C  CG  . LYS A 1 18  ? 36.092  0.206   19.258  1.00 20.78 ? 18  LYS A CG  1 
ATOM   128  C  CD  . LYS A 1 18  ? 36.705  -0.744  18.275  1.00 21.13 ? 18  LYS A CD  1 
ATOM   129  C  CE  . LYS A 1 18  ? 35.755  -1.707  17.603  1.00 22.15 ? 18  LYS A CE  1 
ATOM   130  N  NZ  . LYS A 1 18  ? 36.388  -2.425  16.484  1.00 21.27 ? 18  LYS A NZ  1 
ATOM   131  N  N   . ASP A 1 19  ? 33.121  3.715   18.031  1.00 19.74 ? 19  ASP A N   1 
ATOM   132  C  CA  . ASP A 1 19  ? 32.762  4.978   17.402  1.00 19.74 ? 19  ASP A CA  1 
ATOM   133  C  C   . ASP A 1 19  ? 31.703  5.696   18.240  1.00 21.77 ? 19  ASP A C   1 
ATOM   134  O  O   . ASP A 1 19  ? 31.601  6.916   18.207  1.00 21.85 ? 19  ASP A O   1 
ATOM   135  C  CB  . ASP A 1 19  ? 32.396  4.774   15.926  1.00 23.03 ? 19  ASP A CB  1 
ATOM   136  C  CG  . ASP A 1 19  ? 33.613  4.507   15.063  1.00 28.40 ? 19  ASP A CG  1 
ATOM   137  O  OD1 . ASP A 1 19  ? 34.251  5.498   14.692  1.00 28.91 ? 19  ASP A OD1 1 
ATOM   138  O  OD2 . ASP A 1 19  ? 33.991  3.308   14.900  1.00 28.21 ? 19  ASP A OD2 1 
ATOM   139  N  N   . PHE A 1 20  ? 30.973  4.933   19.062  1.00 18.79 ? 20  PHE A N   1 
ATOM   140  C  CA  . PHE A 1 20  ? 29.811  5.456   19.766  1.00 18.20 ? 20  PHE A CA  1 
ATOM   141  C  C   . PHE A 1 20  ? 29.916  4.959   21.199  1.00 19.41 ? 20  PHE A C   1 
ATOM   142  O  O   . PHE A 1 20  ? 29.322  3.944   21.556  1.00 17.59 ? 20  PHE A O   1 
ATOM   143  C  CB  . PHE A 1 20  ? 28.524  4.984   19.052  1.00 17.19 ? 20  PHE A CB  1 
ATOM   144  C  CG  . PHE A 1 20  ? 28.475  5.316   17.583  1.00 15.34 ? 20  PHE A CG  1 
ATOM   145  C  CD1 . PHE A 1 20  ? 28.168  6.611   17.169  1.00 16.40 ? 20  PHE A CD1 1 
ATOM   146  C  CD2 . PHE A 1 20  ? 28.853  4.406   16.608  1.00 15.46 ? 20  PHE A CD2 1 
ATOM   147  C  CE1 . PHE A 1 20  ? 28.155  6.944   15.822  1.00 17.10 ? 20  PHE A CE1 1 
ATOM   148  C  CE2 . PHE A 1 20  ? 28.858  4.735   15.258  1.00 14.58 ? 20  PHE A CE2 1 
ATOM   149  C  CZ  . PHE A 1 20  ? 28.505  6.017   14.866  1.00 16.34 ? 20  PHE A CZ  1 
ATOM   150  N  N   . PRO A 1 21  ? 30.785  5.568   22.049  1.00 19.49 ? 21  PRO A N   1 
ATOM   151  C  CA  . PRO A 1 21  ? 31.036  5.050   23.394  1.00 19.32 ? 21  PRO A CA  1 
ATOM   152  C  C   . PRO A 1 21  ? 29.827  4.872   24.318  1.00 19.06 ? 21  PRO A C   1 
ATOM   153  O  O   . PRO A 1 21  ? 29.874  4.099   25.267  1.00 20.03 ? 21  PRO A O   1 
ATOM   154  C  CB  . PRO A 1 21  ? 32.116  5.997   23.980  1.00 22.36 ? 21  PRO A CB  1 
ATOM   155  C  CG  . PRO A 1 21  ? 32.145  7.164   23.040  1.00 23.90 ? 21  PRO A CG  1 
ATOM   156  C  CD  . PRO A 1 21  ? 31.680  6.685   21.678  1.00 22.53 ? 21  PRO A CD  1 
ATOM   157  N  N   . ILE A 1 22  ? 28.751  5.611   24.005  1.00 16.99 ? 22  ILE A N   1 
ATOM   158  C  CA  . ILE A 1 22  ? 27.508  5.509   24.779  1.00 16.50 ? 22  ILE A CA  1 
ATOM   159  C  C   . ILE A 1 22  ? 26.913  4.123   24.570  1.00 14.13 ? 22  ILE A C   1 
ATOM   160  O  O   . ILE A 1 22  ? 26.075  3.758   25.357  1.00 15.20 ? 22  ILE A O   1 
ATOM   161  C  CB  . ILE A 1 22  ? 26.494  6.594   24.332  1.00 15.71 ? 22  ILE A CB  1 
ATOM   162  C  CG1 . ILE A 1 22  ? 25.403  6.905   25.373  1.00 18.74 ? 22  ILE A CG1 1 
ATOM   163  C  CG2 . ILE A 1 22  ? 25.878  6.307   22.956  1.00 15.35 ? 22  ILE A CG2 1 
ATOM   164  C  CD1 . ILE A 1 22  ? 25.865  7.409   26.722  1.00 20.93 ? 22  ILE A CD1 1 
ATOM   165  N  N   . ALA A 1 23  ? 27.424  3.352   23.597  1.00 14.80 ? 23  ALA A N   1 
ATOM   166  C  CA  . ALA A 1 23  ? 27.069  1.939   23.528  1.00 13.27 ? 23  ALA A CA  1 
ATOM   167  C  C   . ALA A 1 23  ? 27.163  1.213   24.866  1.00 14.74 ? 23  ALA A C   1 
ATOM   168  O  O   . ALA A 1 23  ? 26.485  0.213   25.055  1.00 14.87 ? 23  ALA A O   1 
ATOM   169  C  CB  . ALA A 1 23  ? 27.887  1.226   22.450  1.00 13.32 ? 23  ALA A CB  1 
ATOM   170  N  N   . LYS A 1 24  ? 28.037  1.660   25.777  1.00 15.65 ? 24  LYS A N   1 
ATOM   171  C  CA  . LYS A 1 24  ? 28.254  1.034   27.072  1.00 15.13 ? 24  LYS A CA  1 
ATOM   172  C  C   . LYS A 1 24  ? 27.627  1.864   28.191  1.00 18.27 ? 24  LYS A C   1 
ATOM   173  O  O   . LYS A 1 24  ? 28.031  1.718   29.342  1.00 19.05 ? 24  LYS A O   1 
ATOM   174  C  CB  . LYS A 1 24  ? 29.765  0.885   27.297  1.00 16.71 ? 24  LYS A CB  1 
ATOM   175  C  CG  . LYS A 1 24  ? 30.378  -0.171  26.404  1.00 21.30 ? 24  LYS A CG  1 
ATOM   176  C  CD  . LYS A 1 24  ? 31.869  -0.258  26.719  1.00 23.09 ? 24  LYS A CD  1 
ATOM   177  C  CE  . LYS A 1 24  ? 32.591  -1.152  25.738  1.00 23.72 ? 24  LYS A CE  1 
ATOM   178  N  NZ  . LYS A 1 24  ? 32.282  -2.564  26.062  1.00 31.35 ? 24  LYS A NZ  1 
ATOM   179  N  N   . GLY A 1 25  ? 26.618  2.689   27.834  1.00 18.00 ? 25  GLY A N   1 
ATOM   180  C  CA  . GLY A 1 25  ? 25.960  3.633   28.738  1.00 16.92 ? 25  GLY A CA  1 
ATOM   181  C  C   . GLY A 1 25  ? 24.974  2.962   29.678  1.00 15.43 ? 25  GLY A C   1 
ATOM   182  O  O   . GLY A 1 25  ? 24.860  1.729   29.721  1.00 17.11 ? 25  GLY A O   1 
ATOM   183  N  N   . GLU A 1 26  ? 24.274  3.816   30.451  1.00 15.67 ? 26  GLU A N   1 
ATOM   184  C  CA  . GLU A 1 26  ? 23.453  3.319   31.533  1.00 18.14 ? 26  GLU A CA  1 
ATOM   185  C  C   . GLU A 1 26  ? 22.002  3.121   31.106  1.00 15.01 ? 26  GLU A C   1 
ATOM   186  O  O   . GLU A 1 26  ? 21.213  2.569   31.877  1.00 16.20 ? 26  GLU A O   1 
ATOM   187  C  CB  . GLU A 1 26  ? 23.444  4.360   32.659  1.00 22.92 ? 26  GLU A CB  1 
ATOM   188  C  CG  . GLU A 1 26  ? 24.823  4.607   33.289  1.00 31.78 ? 26  GLU A CG  1 
ATOM   189  C  CD  . GLU A 1 26  ? 25.513  3.336   33.756  1.00 31.46 ? 26  GLU A CD  1 
ATOM   190  O  OE1 . GLU A 1 26  ? 24.927  2.575   34.575  1.00 36.16 ? 26  GLU A OE1 1 
ATOM   191  O  OE2 . GLU A 1 26  ? 26.630  3.100   33.289  1.00 36.21 ? 26  GLU A OE2 1 
ATOM   192  N  N   A ARG A 1 27  ? 21.632  3.606   29.903  0.50 15.02 ? 27  ARG A N   1 
ATOM   193  N  N   B ARG A 1 27  ? 21.683  3.508   29.862  0.50 14.16 ? 27  ARG A N   1 
ATOM   194  C  CA  A ARG A 1 27  ? 20.250  3.438   29.450  0.50 13.68 ? 27  ARG A CA  1 
ATOM   195  C  CA  B ARG A 1 27  ? 20.290  3.446   29.440  0.50 12.83 ? 27  ARG A CA  1 
ATOM   196  C  C   A ARG A 1 27  ? 20.200  2.936   27.999  0.50 12.19 ? 27  ARG A C   1 
ATOM   197  C  C   B ARG A 1 27  ? 20.195  2.926   28.001  0.50 11.69 ? 27  ARG A C   1 
ATOM   198  O  O   A ARG A 1 27  ? 19.508  3.566   27.175  0.50 12.29 ? 27  ARG A O   1 
ATOM   199  O  O   B ARG A 1 27  ? 19.504  3.507   27.154  0.50 11.89 ? 27  ARG A O   1 
ATOM   200  C  CB  A ARG A 1 27  ? 19.368  4.660   29.775  0.50 14.24 ? 27  ARG A CB  1 
ATOM   201  C  CB  B ARG A 1 27  ? 19.626  4.820   29.586  0.50 12.64 ? 27  ARG A CB  1 
ATOM   202  C  CG  A ARG A 1 27  ? 19.700  5.960   29.048  0.50 15.04 ? 27  ARG A CG  1 
ATOM   203  C  CG  B ARG A 1 27  ? 20.059  5.597   30.818  0.50 12.68 ? 27  ARG A CG  1 
ATOM   204  C  CD  A ARG A 1 27  ? 18.867  7.234   29.330  0.50 16.58 ? 27  ARG A CD  1 
ATOM   205  C  CD  B ARG A 1 27  ? 19.487  6.991   30.622  0.50 13.05 ? 27  ARG A CD  1 
ATOM   206  N  NE  A ARG A 1 27  ? 17.589  7.169   28.616  0.50 14.99 ? 27  ARG A NE  1 
ATOM   207  N  NE  B ARG A 1 27  ? 19.745  7.860   31.780  0.50 14.41 ? 27  ARG A NE  1 
ATOM   208  C  CZ  A ARG A 1 27  ? 16.721  8.146   28.266  0.50 11.82 ? 27  ARG A CZ  1 
ATOM   209  C  CZ  B ARG A 1 27  ? 20.749  8.725   31.863  0.50 15.28 ? 27  ARG A CZ  1 
ATOM   210  N  NH1 A ARG A 1 27  ? 16.981  9.405   28.575  0.50 6.96  ? 27  ARG A NH1 1 
ATOM   211  N  NH1 B ARG A 1 27  ? 21.601  8.849   30.859  0.50 16.80 ? 27  ARG A NH1 1 
ATOM   212  N  NH2 A ARG A 1 27  ? 15.612  7.844   27.615  0.50 10.72 ? 27  ARG A NH2 1 
ATOM   213  N  NH2 B ARG A 1 27  ? 20.899  9.464   32.948  0.50 18.79 ? 27  ARG A NH2 1 
ATOM   214  N  N   . GLN A 1 28  ? 20.914  1.839   27.720  1.00 12.59 ? 28  GLN A N   1 
ATOM   215  C  CA  . GLN A 1 28  ? 20.989  1.334   26.355  1.00 12.24 ? 28  GLN A CA  1 
ATOM   216  C  C   . GLN A 1 28  ? 19.798  0.426   26.047  1.00 11.28 ? 28  GLN A C   1 
ATOM   217  O  O   . GLN A 1 28  ? 19.288  -0.279  26.899  1.00 12.01 ? 28  GLN A O   1 
ATOM   218  C  CB  . GLN A 1 28  ? 22.327  0.629   26.078  1.00 12.52 ? 28  GLN A CB  1 
ATOM   219  C  CG  . GLN A 1 28  ? 23.451  1.661   26.005  1.00 13.32 ? 28  GLN A CG  1 
ATOM   220  C  CD  . GLN A 1 28  ? 23.316  2.482   24.745  1.00 11.41 ? 28  GLN A CD  1 
ATOM   221  O  OE1 . GLN A 1 28  ? 23.559  2.012   23.649  1.00 12.22 ? 28  GLN A OE1 1 
ATOM   222  N  NE2 . GLN A 1 28  ? 22.989  3.759   24.842  1.00 12.04 ? 28  GLN A NE2 1 
ATOM   223  N  N   . SER A 1 29  ? 19.435  0.387   24.765  1.00 11.27 ? 29  SER A N   1 
ATOM   224  C  CA  . SER A 1 29  ? 18.350  -0.485  24.297  1.00 9.33  ? 29  SER A CA  1 
ATOM   225  C  C   . SER A 1 29  ? 18.848  -1.365  23.171  1.00 10.91 ? 29  SER A C   1 
ATOM   226  O  O   . SER A 1 29  ? 19.791  -1.018  22.467  1.00 10.58 ? 29  SER A O   1 
ATOM   227  C  CB  . SER A 1 29  ? 17.207  0.365   23.749  1.00 9.69  ? 29  SER A CB  1 
ATOM   228  O  OG  . SER A 1 29  ? 16.587  1.061   24.841  1.00 9.30  ? 29  SER A OG  1 
ATOM   229  N  N   . PRO A 1 30  ? 18.197  -2.502  22.860  1.00 9.47  ? 30  PRO A N   1 
ATOM   230  C  CA  . PRO A 1 30  ? 17.011  -3.001  23.586  1.00 9.61  ? 30  PRO A CA  1 
ATOM   231  C  C   . PRO A 1 30  ? 17.436  -3.695  24.878  1.00 9.69  ? 30  PRO A C   1 
ATOM   232  O  O   . PRO A 1 30  ? 18.616  -3.768  25.197  1.00 10.46 ? 30  PRO A O   1 
ATOM   233  C  CB  . PRO A 1 30  ? 16.479  -4.001  22.553  1.00 9.87  ? 30  PRO A CB  1 
ATOM   234  C  CG  . PRO A 1 30  ? 17.758  -4.628  21.910  1.00 9.70  ? 30  PRO A CG  1 
ATOM   235  C  CD  . PRO A 1 30  ? 18.666  -3.425  21.797  1.00 9.64  ? 30  PRO A CD  1 
ATOM   236  N  N   . VAL A 1 31  ? 16.455  -4.273  25.576  1.00 9.82  ? 31  VAL A N   1 
ATOM   237  C  CA  . VAL A 1 31  ? 16.652  -5.026  26.801  1.00 10.36 ? 31  VAL A CA  1 
ATOM   238  C  C   . VAL A 1 31  ? 15.751  -6.252  26.720  1.00 10.11 ? 31  VAL A C   1 
ATOM   239  O  O   . VAL A 1 31  ? 14.724  -6.310  26.013  1.00 10.99 ? 31  VAL A O   1 
ATOM   240  C  CB  . VAL A 1 31  ? 16.321  -4.211  28.076  1.00 11.05 ? 31  VAL A CB  1 
ATOM   241  C  CG1 . VAL A 1 31  ? 17.217  -2.983  28.200  1.00 12.71 ? 31  VAL A CG1 1 
ATOM   242  C  CG2 . VAL A 1 31  ? 14.822  -3.807  28.143  1.00 11.39 ? 31  VAL A CG2 1 
ATOM   243  N  N   . ASP A 1 32  ? 16.103  -7.245  27.549  1.00 11.46 ? 32  ASP A N   1 
ATOM   244  C  CA  . ASP A 1 32  ? 15.162  -8.293  27.880  1.00 11.16 ? 32  ASP A CA  1 
ATOM   245  C  C   . ASP A 1 32  ? 14.088  -7.757  28.837  1.00 11.88 ? 32  ASP A C   1 
ATOM   246  O  O   . ASP A 1 32  ? 14.406  -7.113  29.832  1.00 12.97 ? 32  ASP A O   1 
ATOM   247  C  CB  . ASP A 1 32  ? 15.883  -9.493  28.504  1.00 13.12 ? 32  ASP A CB  1 
ATOM   248  C  CG  . ASP A 1 32  ? 14.935  -10.651 28.775  1.00 14.28 ? 32  ASP A CG  1 
ATOM   249  O  OD1 . ASP A 1 32  ? 14.222  -11.126 27.848  1.00 13.18 ? 32  ASP A OD1 1 
ATOM   250  O  OD2 . ASP A 1 32  ? 14.883  -11.083 29.973  1.00 17.75 ? 32  ASP A OD2 1 
ATOM   251  N  N   . ILE A 1 33  ? 12.823  -8.010  28.509  1.00 11.91 ? 33  ILE A N   1 
ATOM   252  C  CA  . ILE A 1 33  ? 11.704  -7.668  29.387  1.00 12.80 ? 33  ILE A CA  1 
ATOM   253  C  C   . ILE A 1 33  ? 11.383  -8.890  30.248  1.00 13.54 ? 33  ILE A C   1 
ATOM   254  O  O   . ILE A 1 33  ? 10.829  -9.865  29.757  1.00 14.38 ? 33  ILE A O   1 
ATOM   255  C  CB  . ILE A 1 33  ? 10.489  -7.190  28.587  1.00 13.02 ? 33  ILE A CB  1 
ATOM   256  C  CG1 . ILE A 1 33  ? 10.846  -5.967  27.737  1.00 13.68 ? 33  ILE A CG1 1 
ATOM   257  C  CG2 . ILE A 1 33  ? 9.315   -6.887  29.514  1.00 15.11 ? 33  ILE A CG2 1 
ATOM   258  C  CD1 . ILE A 1 33  ? 9.819   -5.689  26.670  1.00 15.06 ? 33  ILE A CD1 1 
ATOM   259  N  N   . ASP A 1 34  ? 11.844  -8.830  31.509  1.00 15.80 ? 34  ASP A N   1 
ATOM   260  C  CA  . ASP A 1 34  ? 11.532  -9.870  32.494  1.00 15.00 ? 34  ASP A CA  1 
ATOM   261  C  C   . ASP A 1 34  ? 10.137  -9.553  33.048  1.00 16.89 ? 34  ASP A C   1 
ATOM   262  O  O   . ASP A 1 34  ? 9.976   -8.572  33.794  1.00 16.38 ? 34  ASP A O   1 
ATOM   263  C  CB  . ASP A 1 34  ? 12.603  -9.811  33.604  1.00 17.28 ? 34  ASP A CB  1 
ATOM   264  C  CG  . ASP A 1 34  ? 12.429  -10.884 34.669  1.00 22.17 ? 34  ASP A CG  1 
ATOM   265  O  OD1 . ASP A 1 34  ? 11.298  -11.339 34.862  1.00 20.63 ? 34  ASP A OD1 1 
ATOM   266  O  OD2 . ASP A 1 34  ? 13.469  -11.327 35.228  1.00 28.49 ? 34  ASP A OD2 1 
ATOM   267  N  N   . THR A 1 35  ? 9.143   -10.317 32.611  1.00 16.71 ? 35  THR A N   1 
ATOM   268  C  CA  . THR A 1 35  ? 7.744   -10.024 32.877  1.00 17.94 ? 35  THR A CA  1 
ATOM   269  C  C   . THR A 1 35  ? 7.425   -10.192 34.359  1.00 19.01 ? 35  THR A C   1 
ATOM   270  O  O   . THR A 1 35  ? 6.419   -9.613  34.800  1.00 22.42 ? 35  THR A O   1 
ATOM   271  C  CB  . THR A 1 35  ? 6.827   -10.895 32.031  1.00 20.95 ? 35  THR A CB  1 
ATOM   272  O  OG1 . THR A 1 35  ? 7.021   -12.243 32.474  1.00 19.27 ? 35  THR A OG1 1 
ATOM   273  C  CG2 . THR A 1 35  ? 7.081   -10.746 30.547  1.00 23.06 ? 35  THR A CG2 1 
ATOM   274  N  N   . HIS A 1 36  ? 8.311   -10.873 35.129  1.00 21.21 ? 36  HIS A N   1 
ATOM   275  C  CA  . HIS A 1 36  ? 8.129   -11.124 36.567  1.00 19.71 ? 36  HIS A CA  1 
ATOM   276  C  C   . HIS A 1 36  ? 8.829   -10.100 37.472  1.00 23.68 ? 36  HIS A C   1 
ATOM   277  O  O   . HIS A 1 36  ? 8.735   -10.126 38.709  1.00 24.73 ? 36  HIS A O   1 
ATOM   278  C  CB  . HIS A 1 36  ? 8.731   -12.503 36.886  1.00 21.53 ? 36  HIS A CB  1 
ATOM   279  C  CG  . HIS A 1 36  ? 8.320   -13.546 35.900  1.00 21.55 ? 36  HIS A CG  1 
ATOM   280  N  ND1 . HIS A 1 36  ? 7.022   -14.045 35.823  1.00 23.35 ? 36  HIS A ND1 1 
ATOM   281  C  CD2 . HIS A 1 36  ? 9.034   -14.184 34.933  1.00 23.47 ? 36  HIS A CD2 1 
ATOM   282  C  CE1 . HIS A 1 36  ? 6.945   -14.952 34.864  1.00 22.30 ? 36  HIS A CE1 1 
ATOM   283  N  NE2 . HIS A 1 36  ? 8.183   -15.081 34.334  1.00 22.18 ? 36  HIS A NE2 1 
ATOM   284  N  N   . THR A 1 37  ? 9.610   -9.211  36.901  1.00 20.81 ? 37  THR A N   1 
ATOM   285  C  CA  . THR A 1 37  ? 10.175  -8.128  37.669  1.00 19.94 ? 37  THR A CA  1 
ATOM   286  C  C   . THR A 1 37  ? 9.580   -6.810  37.177  1.00 20.07 ? 37  THR A C   1 
ATOM   287  O  O   . THR A 1 37  ? 9.764   -5.783  37.845  1.00 25.08 ? 37  THR A O   1 
ATOM   288  C  CB  . THR A 1 37  ? 11.696  -8.254  37.833  1.00 25.47 ? 37  THR A CB  1 
ATOM   289  O  OG1 . THR A 1 37  ? 12.391  -8.002  36.625  1.00 28.17 ? 37  THR A OG1 1 
ATOM   290  C  CG2 . THR A 1 37  ? 12.120  -9.642  38.247  1.00 25.28 ? 37  THR A CG2 1 
ATOM   291  N  N   . ALA A 1 38  ? 8.875   -6.835  36.038  1.00 20.86 ? 38  ALA A N   1 
ATOM   292  C  CA  . ALA A 1 38  ? 8.229   -5.588  35.612  1.00 20.26 ? 38  ALA A CA  1 
ATOM   293  C  C   . ALA A 1 38  ? 7.130   -5.230  36.623  1.00 22.34 ? 38  ALA A C   1 
ATOM   294  O  O   . ALA A 1 38  ? 6.504   -6.106  37.200  1.00 26.80 ? 38  ALA A O   1 
ATOM   295  C  CB  . ALA A 1 38  ? 7.689   -5.693  34.219  1.00 18.54 ? 38  ALA A CB  1 
ATOM   296  N  N   . LYS A 1 39  ? 6.981   -3.938  36.905  1.00 21.62 ? 39  LYS A N   1 
ATOM   297  C  CA  . LYS A 1 39  ? 6.086   -3.451  37.938  1.00 21.20 ? 39  LYS A CA  1 
ATOM   298  C  C   . LYS A 1 39  ? 4.794   -2.962  37.272  1.00 20.51 ? 39  LYS A C   1 
ATOM   299  O  O   . LYS A 1 39  ? 4.813   -2.020  36.466  1.00 17.74 ? 39  LYS A O   1 
ATOM   300  C  CB  . LYS A 1 39  ? 6.867   -2.328  38.628  1.00 22.22 ? 39  LYS A CB  1 
ATOM   301  C  CG  . LYS A 1 39  ? 6.081   -1.399  39.540  1.00 25.13 ? 39  LYS A CG  1 
ATOM   302  C  CD  . LYS A 1 39  ? 5.825   -2.071  40.876  1.00 23.94 ? 39  LYS A CD  1 
ATOM   303  C  CE  . LYS A 1 39  ? 5.252   -1.061  41.853  1.00 28.33 ? 39  LYS A CE  1 
ATOM   304  N  NZ  . LYS A 1 39  ? 4.717   -1.771  43.042  1.00 29.09 ? 39  LYS A NZ  1 
ATOM   305  N  N   . TYR A 1 40  ? 3.649   -3.508  37.674  1.00 21.10 ? 40  TYR A N   1 
ATOM   306  C  CA  . TYR A 1 40  ? 2.413   -2.903  37.218  1.00 20.07 ? 40  TYR A CA  1 
ATOM   307  C  C   . TYR A 1 40  ? 2.263   -1.514  37.830  1.00 21.10 ? 40  TYR A C   1 
ATOM   308  O  O   . TYR A 1 40  ? 2.430   -1.359  39.049  1.00 20.65 ? 40  TYR A O   1 
ATOM   309  C  CB  . TYR A 1 40  ? 1.208   -3.788  37.567  1.00 24.79 ? 40  TYR A CB  1 
ATOM   310  C  CG  . TYR A 1 40  ? -0.101  -3.063  37.435  1.00 29.35 ? 40  TYR A CG  1 
ATOM   311  C  CD1 . TYR A 1 40  ? -0.590  -2.643  36.205  1.00 29.51 ? 40  TYR A CD1 1 
ATOM   312  C  CD2 . TYR A 1 40  ? -0.865  -2.790  38.562  1.00 36.80 ? 40  TYR A CD2 1 
ATOM   313  C  CE1 . TYR A 1 40  ? -1.799  -1.984  36.087  1.00 31.49 ? 40  TYR A CE1 1 
ATOM   314  C  CE2 . TYR A 1 40  ? -2.078  -2.126  38.460  1.00 37.86 ? 40  TYR A CE2 1 
ATOM   315  C  CZ  . TYR A 1 40  ? -2.547  -1.726  37.225  1.00 37.16 ? 40  TYR A CZ  1 
ATOM   316  O  OH  . TYR A 1 40  ? -3.731  -1.054  37.143  1.00 42.15 ? 40  TYR A OH  1 
ATOM   317  N  N   . ASP A 1 41  ? 1.933   -0.513  36.997  1.00 21.64 ? 41  ASP A N   1 
ATOM   318  C  CA  . ASP A 1 41  ? 1.900   0.876   37.417  1.00 22.30 ? 41  ASP A CA  1 
ATOM   319  C  C   . ASP A 1 41  ? 0.484   1.397   37.178  1.00 29.37 ? 41  ASP A C   1 
ATOM   320  O  O   . ASP A 1 41  ? 0.147   1.795   36.058  1.00 24.80 ? 41  ASP A O   1 
ATOM   321  C  CB  . ASP A 1 41  ? 2.975   1.717   36.727  1.00 26.67 ? 41  ASP A CB  1 
ATOM   322  C  CG  . ASP A 1 41  ? 3.113   3.121   37.295  1.00 32.60 ? 41  ASP A CG  1 
ATOM   323  O  OD1 . ASP A 1 41  ? 2.203   3.531   38.036  1.00 30.65 ? 41  ASP A OD1 1 
ATOM   324  O  OD2 . ASP A 1 41  ? 4.139   3.798   36.976  1.00 33.48 ? 41  ASP A OD2 1 
ATOM   325  N  N   . PRO A 1 42  ? -0.392  1.387   38.209  1.00 31.87 ? 42  PRO A N   1 
ATOM   326  C  CA  . PRO A 1 42  ? -1.793  1.769   38.020  1.00 32.89 ? 42  PRO A CA  1 
ATOM   327  C  C   . PRO A 1 42  ? -1.918  3.256   37.703  1.00 35.58 ? 42  PRO A C   1 
ATOM   328  O  O   . PRO A 1 42  ? -2.993  3.701   37.298  1.00 37.98 ? 42  PRO A O   1 
ATOM   329  C  CB  . PRO A 1 42  ? -2.448  1.416   39.365  1.00 36.64 ? 42  PRO A CB  1 
ATOM   330  C  CG  . PRO A 1 42  ? -1.308  1.475   40.367  1.00 34.50 ? 42  PRO A CG  1 
ATOM   331  C  CD  . PRO A 1 42  ? -0.096  0.981   39.597  1.00 31.46 ? 42  PRO A CD  1 
ATOM   332  N  N   . SER A 1 43  ? -0.810  4.006   37.833  1.00 34.18 ? 43  SER A N   1 
ATOM   333  C  CA  . SER A 1 43  ? -0.805  5.421   37.476  1.00 35.62 ? 43  SER A CA  1 
ATOM   334  C  C   . SER A 1 43  ? -0.524  5.700   35.987  1.00 35.69 ? 43  SER A C   1 
ATOM   335  O  O   . SER A 1 43  ? -0.741  6.824   35.533  1.00 38.16 ? 43  SER A O   1 
ATOM   336  C  CB  . SER A 1 43  ? 0.098   6.211   38.381  1.00 37.29 ? 43  SER A CB  1 
ATOM   337  O  OG  . SER A 1 43  ? 1.461   6.098   38.015  1.00 34.34 ? 43  SER A OG  1 
ATOM   338  N  N   . LEU A 1 44  ? -0.028  4.711   35.220  1.00 31.98 ? 44  LEU A N   1 
ATOM   339  C  CA  . LEU A 1 44  ? 0.142   4.871   33.777  1.00 31.52 ? 44  LEU A CA  1 
ATOM   340  C  C   . LEU A 1 44  ? -1.215  5.045   33.113  1.00 34.21 ? 44  LEU A C   1 
ATOM   341  O  O   . LEU A 1 44  ? -2.147  4.323   33.449  1.00 34.44 ? 44  LEU A O   1 
ATOM   342  C  CB  . LEU A 1 44  ? 0.798   3.617   33.191  1.00 28.35 ? 44  LEU A CB  1 
ATOM   343  C  CG  . LEU A 1 44  ? 2.287   3.456   33.482  1.00 26.32 ? 44  LEU A CG  1 
ATOM   344  C  CD1 . LEU A 1 44  ? 2.735   2.067   33.040  1.00 26.75 ? 44  LEU A CD1 1 
ATOM   345  C  CD2 . LEU A 1 44  ? 3.083   4.548   32.776  1.00 25.92 ? 44  LEU A CD2 1 
ATOM   346  N  N   . LYS A 1 45  ? -1.267  5.924   32.103  1.00 35.48 ? 45  LYS A N   1 
ATOM   347  C  CA  . LYS A 1 45  ? -2.462  6.129   31.294  1.00 33.08 ? 45  LYS A CA  1 
ATOM   348  C  C   . LYS A 1 45  ? -2.509  5.138   30.135  1.00 32.23 ? 45  LYS A C   1 
ATOM   349  O  O   . LYS A 1 45  ? -1.517  4.473   29.814  1.00 33.30 ? 45  LYS A O   1 
ATOM   350  C  CB  . LYS A 1 45  ? -2.546  7.591   30.875  1.00 32.10 ? 45  LYS A CB  1 
ATOM   351  C  CG  . LYS A 1 45  ? -2.170  8.546   32.004  1.00 31.85 ? 45  LYS A CG  1 
ATOM   352  C  CD  . LYS A 1 45  ? -2.856  9.883   31.979  1.00 40.61 ? 45  LYS A CD  1 
ATOM   353  N  N   . PRO A 1 46  ? -3.697  4.930   29.508  1.00 30.23 ? 46  PRO A N   1 
ATOM   354  C  CA  . PRO A 1 46  ? -3.781  4.115   28.296  1.00 28.65 ? 46  PRO A CA  1 
ATOM   355  C  C   . PRO A 1 46  ? -3.020  4.960   27.292  1.00 23.53 ? 46  PRO A C   1 
ATOM   356  O  O   . PRO A 1 46  ? -2.950  6.174   27.441  1.00 25.84 ? 46  PRO A O   1 
ATOM   357  C  CB  . PRO A 1 46  ? -5.289  4.088   27.947  1.00 30.25 ? 46  PRO A CB  1 
ATOM   358  C  CG  . PRO A 1 46  ? -5.962  4.466   29.268  1.00 31.38 ? 46  PRO A CG  1 
ATOM   359  C  CD  . PRO A 1 46  ? -5.010  5.478   29.890  1.00 33.12 ? 46  PRO A CD  1 
ATOM   360  N  N   . LEU A 1 47  ? -2.408  4.274   26.339  1.00 28.08 ? 47  LEU A N   1 
ATOM   361  C  CA  . LEU A 1 47  ? -1.762  4.956   25.257  1.00 25.69 ? 47  LEU A CA  1 
ATOM   362  C  C   . LEU A 1 47  ? -2.877  5.589   24.435  1.00 24.77 ? 47  LEU A C   1 
ATOM   363  O  O   . LEU A 1 47  ? -3.996  5.084   24.404  1.00 23.23 ? 47  LEU A O   1 
ATOM   364  C  CB  . LEU A 1 47  ? -1.029  3.882   24.457  1.00 28.79 ? 47  LEU A CB  1 
ATOM   365  C  CG  . LEU A 1 47  ? 0.297   4.253   23.831  1.00 34.40 ? 47  LEU A CG  1 
ATOM   366  C  CD1 . LEU A 1 47  ? 1.202   4.913   24.858  1.00 29.83 ? 47  LEU A CD1 1 
ATOM   367  C  CD2 . LEU A 1 47  ? 0.931   2.986   23.252  1.00 34.87 ? 47  LEU A CD2 1 
ATOM   368  N  N   . SER A 1 48  ? -2.565  6.711   23.815  1.00 18.75 ? 48  SER A N   1 
ATOM   369  C  CA  . SER A 1 48  ? -3.412  7.331   22.819  1.00 18.32 ? 48  SER A CA  1 
ATOM   370  C  C   . SER A 1 48  ? -2.626  7.329   21.524  1.00 19.87 ? 48  SER A C   1 
ATOM   371  O  O   . SER A 1 48  ? -1.578  7.978   21.398  1.00 17.85 ? 48  SER A O   1 
ATOM   372  C  CB  . SER A 1 48  ? -3.754  8.737   23.260  1.00 18.39 ? 48  SER A CB  1 
ATOM   373  O  OG  . SER A 1 48  ? -4.424  9.418   22.223  1.00 20.19 ? 48  SER A OG  1 
ATOM   374  N  N   . VAL A 1 49  ? -3.070  6.505   20.613  1.00 18.66 ? 49  VAL A N   1 
ATOM   375  C  CA  . VAL A 1 49  ? -2.431  6.390   19.329  1.00 19.08 ? 49  VAL A CA  1 
ATOM   376  C  C   . VAL A 1 49  ? -3.405  6.988   18.336  1.00 21.67 ? 49  VAL A C   1 
ATOM   377  O  O   . VAL A 1 49  ? -4.456  6.387   18.101  1.00 24.86 ? 49  VAL A O   1 
ATOM   378  C  CB  . VAL A 1 49  ? -2.153  4.916   19.013  1.00 21.78 ? 49  VAL A CB  1 
ATOM   379  C  CG1 . VAL A 1 49  ? -1.457  4.778   17.669  1.00 27.85 ? 49  VAL A CG1 1 
ATOM   380  C  CG2 . VAL A 1 49  ? -1.373  4.241   20.119  1.00 20.38 ? 49  VAL A CG2 1 
ATOM   381  N  N   . SER A 1 50  ? -3.123  8.184   17.829  1.00 19.07 ? 50  SER A N   1 
ATOM   382  C  CA  . SER A 1 50  ? -4.045  8.850   16.919  1.00 19.33 ? 50  SER A CA  1 
ATOM   383  C  C   . SER A 1 50  ? -3.448  8.896   15.526  1.00 18.58 ? 50  SER A C   1 
ATOM   384  O  O   . SER A 1 50  ? -2.771  9.851   15.206  1.00 19.55 ? 50  SER A O   1 
ATOM   385  C  CB  . SER A 1 50  ? -4.417  10.232  17.410  1.00 21.75 ? 50  SER A CB  1 
ATOM   386  O  OG  . SER A 1 50  ? -5.008  10.127  18.697  1.00 27.25 ? 50  SER A OG  1 
ATOM   387  N  N   . TYR A 1 51  ? -3.697  7.880   14.692  1.00 18.07 ? 51  TYR A N   1 
ATOM   388  C  CA  . TYR A 1 51  ? -3.102  7.827   13.373  1.00 17.67 ? 51  TYR A CA  1 
ATOM   389  C  C   . TYR A 1 51  ? -4.092  8.080   12.235  1.00 21.42 ? 51  TYR A C   1 
ATOM   390  O  O   . TYR A 1 51  ? -3.742  7.813   11.089  1.00 19.40 ? 51  TYR A O   1 
ATOM   391  C  CB  . TYR A 1 51  ? -2.454  6.450   13.181  1.00 16.69 ? 51  TYR A CB  1 
ATOM   392  C  CG  . TYR A 1 51  ? -1.196  6.180   13.990  1.00 15.90 ? 51  TYR A CG  1 
ATOM   393  C  CD1 . TYR A 1 51  ? -0.482  7.175   14.669  1.00 16.23 ? 51  TYR A CD1 1 
ATOM   394  C  CD2 . TYR A 1 51  ? -0.711  4.888   14.026  1.00 13.93 ? 51  TYR A CD2 1 
ATOM   395  C  CE1 . TYR A 1 51  ? 0.716   6.853   15.316  1.00 15.35 ? 51  TYR A CE1 1 
ATOM   396  C  CE2 . TYR A 1 51  ? 0.474   4.559   14.648  1.00 15.61 ? 51  TYR A CE2 1 
ATOM   397  C  CZ  . TYR A 1 51  ? 1.177   5.544   15.333  1.00 15.51 ? 51  TYR A CZ  1 
ATOM   398  O  OH  . TYR A 1 51  ? 2.335   5.152   15.963  1.00 15.72 ? 51  TYR A OH  1 
ATOM   399  N  N   A ASP A 1 52  ? -5.294  8.583   12.569  0.50 22.62 ? 52  ASP A N   1 
ATOM   400  N  N   B ASP A 1 52  ? -5.315  8.550   12.545  0.50 21.97 ? 52  ASP A N   1 
ATOM   401  C  CA  A ASP A 1 52  ? -6.363  8.800   11.598  0.50 25.92 ? 52  ASP A CA  1 
ATOM   402  C  CA  B ASP A 1 52  ? -6.339  8.759   11.520  0.50 24.80 ? 52  ASP A CA  1 
ATOM   403  C  C   A ASP A 1 52  ? -5.947  9.701   10.427  0.50 25.77 ? 52  ASP A C   1 
ATOM   404  C  C   B ASP A 1 52  ? -5.850  9.638   10.364  0.50 25.41 ? 52  ASP A C   1 
ATOM   405  O  O   A ASP A 1 52  ? -6.400  9.494   9.297   0.50 25.49 ? 52  ASP A O   1 
ATOM   406  O  O   B ASP A 1 52  ? -6.180  9.376   9.201   0.50 24.79 ? 52  ASP A O   1 
ATOM   407  C  CB  A ASP A 1 52  ? -7.673  9.217   12.283  0.50 27.66 ? 52  ASP A CB  1 
ATOM   408  C  CB  B ASP A 1 52  ? -7.646  9.311   12.103  0.50 25.57 ? 52  ASP A CB  1 
ATOM   409  C  CG  A ASP A 1 52  ? -7.513  10.136  13.482  0.50 27.96 ? 52  ASP A CG  1 
ATOM   410  C  CG  B ASP A 1 52  ? -8.714  9.540   11.041  0.50 25.68 ? 52  ASP A CG  1 
ATOM   411  O  OD1 A ASP A 1 52  ? -6.925  9.700   14.505  0.50 31.92 ? 52  ASP A OD1 1 
ATOM   412  O  OD1 B ASP A 1 52  ? -9.115  8.561   10.381  0.50 24.64 ? 52  ASP A OD1 1 
ATOM   413  O  OD2 A ASP A 1 52  ? -7.978  11.284  13.398  0.50 33.58 ? 52  ASP A OD2 1 
ATOM   414  O  OD2 B ASP A 1 52  ? -9.106  10.705  10.853  0.50 29.42 ? 52  ASP A OD2 1 
ATOM   415  N  N   . GLN A 1 53  ? -5.074  10.682  10.667  1.00 24.51 ? 53  GLN A N   1 
ATOM   416  C  CA  . GLN A 1 53  ? -4.687  11.604  9.602   1.00 26.94 ? 53  GLN A CA  1 
ATOM   417  C  C   . GLN A 1 53  ? -3.242  11.406  9.146   1.00 24.26 ? 53  GLN A C   1 
ATOM   418  O  O   . GLN A 1 53  ? -2.663  12.302  8.544   1.00 23.66 ? 53  GLN A O   1 
ATOM   419  C  CB  . GLN A 1 53  ? -4.966  13.053  10.012  1.00 30.12 ? 53  GLN A CB  1 
ATOM   420  C  CG  . GLN A 1 53  ? -6.446  13.346  10.231  1.00 37.45 ? 53  GLN A CG  1 
ATOM   421  C  CD  . GLN A 1 53  ? -7.252  13.151  8.970   1.00 42.59 ? 53  GLN A CD  1 
ATOM   422  O  OE1 . GLN A 1 53  ? -6.798  13.436  7.855   1.00 50.78 ? 53  GLN A OE1 1 
ATOM   423  N  NE2 . GLN A 1 53  ? -8.461  12.640  9.135   1.00 45.92 ? 53  GLN A NE2 1 
ATOM   424  N  N   . ALA A 1 54  ? -2.666  10.239  9.450   1.00 21.82 ? 54  ALA A N   1 
ATOM   425  C  CA  . ALA A 1 54  ? -1.317  9.911   9.014   1.00 18.07 ? 54  ALA A CA  1 
ATOM   426  C  C   . ALA A 1 54  ? -1.141  10.067  7.503   1.00 21.38 ? 54  ALA A C   1 
ATOM   427  O  O   . ALA A 1 54  ? -1.997  9.601   6.750   1.00 22.61 ? 54  ALA A O   1 
ATOM   428  C  CB  . ALA A 1 54  ? -0.926  8.516   9.516   1.00 18.69 ? 54  ALA A CB  1 
ATOM   429  N  N   . THR A 1 55  ? -0.056  10.718  7.058   1.00 18.36 ? 55  THR A N   1 
ATOM   430  C  CA  . THR A 1 55  ? 0.273   10.852  5.647   1.00 18.76 ? 55  THR A CA  1 
ATOM   431  C  C   . THR A 1 55  ? 1.635   10.251  5.386   1.00 18.70 ? 55  THR A C   1 
ATOM   432  O  O   . THR A 1 55  ? 2.641   10.892  5.619   1.00 16.24 ? 55  THR A O   1 
ATOM   433  C  CB  . THR A 1 55  ? 0.396   12.333  5.250   1.00 22.53 ? 55  THR A CB  1 
ATOM   434  O  OG1 . THR A 1 55  ? -0.809  12.973  5.636   1.00 30.80 ? 55  THR A OG1 1 
ATOM   435  C  CG2 . THR A 1 55  ? 0.618   12.449  3.759   1.00 27.02 ? 55  THR A CG2 1 
ATOM   436  N  N   . SER A 1 56  ? 1.664   9.038   4.844   1.00 18.88 ? 56  SER A N   1 
ATOM   437  C  CA  . SER A 1 56  ? 2.916   8.435   4.424   1.00 17.02 ? 56  SER A CA  1 
ATOM   438  C  C   . SER A 1 56  ? 3.434   9.125   3.167   1.00 18.29 ? 56  SER A C   1 
ATOM   439  O  O   . SER A 1 56  ? 2.621   9.606   2.344   1.00 19.89 ? 56  SER A O   1 
ATOM   440  C  CB  . SER A 1 56  ? 2.818   6.917   4.232   1.00 18.43 ? 56  SER A CB  1 
ATOM   441  O  OG  . SER A 1 56  ? 1.820   6.600   3.241   1.00 18.68 ? 56  SER A OG  1 
ATOM   442  N  N   . LEU A 1 57  ? 4.749   9.128   2.995   1.00 18.29 ? 57  LEU A N   1 
ATOM   443  C  CA  . LEU A 1 57  ? 5.295   9.746   1.794   1.00 21.22 ? 57  LEU A CA  1 
ATOM   444  C  C   . LEU A 1 57  ? 6.113   8.775   0.955   1.00 22.76 ? 57  LEU A C   1 
ATOM   445  O  O   . LEU A 1 57  ? 6.080   8.790   -0.284  1.00 20.14 ? 57  LEU A O   1 
ATOM   446  C  CB  . LEU A 1 57  ? 6.154   10.919  2.233   1.00 23.92 ? 57  LEU A CB  1 
ATOM   447  C  CG  . LEU A 1 57  ? 5.389   12.063  2.892   1.00 29.01 ? 57  LEU A CG  1 
ATOM   448  C  CD1 . LEU A 1 57  ? 6.345   13.166  3.298   1.00 28.54 ? 57  LEU A CD1 1 
ATOM   449  C  CD2 . LEU A 1 57  ? 4.215   12.603  2.062   1.00 33.52 ? 57  LEU A CD2 1 
ATOM   450  N  N   . ARG A 1 58  ? 6.950   7.987   1.621   1.00 17.91 ? 58  ARG A N   1 
ATOM   451  C  CA  . ARG A 1 58  ? 8.037   7.363   0.910   1.00 17.73 ? 58  ARG A CA  1 
ATOM   452  C  C   . ARG A 1 58  ? 8.481   6.171   1.725   1.00 18.28 ? 58  ARG A C   1 
ATOM   453  O  O   . ARG A 1 58  ? 8.335   6.180   2.941   1.00 18.11 ? 58  ARG A O   1 
ATOM   454  C  CB  . ARG A 1 58  ? 9.223   8.317   0.780   1.00 20.99 ? 58  ARG A CB  1 
ATOM   455  C  CG  . ARG A 1 58  ? 10.254  7.899   -0.240  1.00 24.35 ? 58  ARG A CG  1 
ATOM   456  C  CD  . ARG A 1 58  ? 11.099  9.149   -0.372  1.00 25.40 ? 58  ARG A CD  1 
ATOM   457  N  NE  . ARG A 1 58  ? 11.893  9.237   0.843   1.00 21.30 ? 58  ARG A NE  1 
ATOM   458  C  CZ  . ARG A 1 58  ? 13.213  9.446   0.878   1.00 21.57 ? 58  ARG A CZ  1 
ATOM   459  N  NH1 . ARG A 1 58  ? 13.894  9.612   -0.247  1.00 22.37 ? 58  ARG A NH1 1 
ATOM   460  N  NH2 . ARG A 1 58  ? 13.834  9.495   2.047   1.00 20.64 ? 58  ARG A NH2 1 
ATOM   461  N  N   . ILE A 1 59  ? 8.997   5.190   1.014   1.00 15.64 ? 59  ILE A N   1 
ATOM   462  C  CA  . ILE A 1 59  ? 9.659   4.061   1.647   1.00 15.19 ? 59  ILE A CA  1 
ATOM   463  C  C   . ILE A 1 59  ? 11.096  4.063   1.157   1.00 14.75 ? 59  ILE A C   1 
ATOM   464  O  O   . ILE A 1 59  ? 11.358  4.290   -0.033  1.00 16.65 ? 59  ILE A O   1 
ATOM   465  C  CB  . ILE A 1 59  ? 8.940   2.742   1.336   1.00 13.19 ? 59  ILE A CB  1 
ATOM   466  C  CG1 . ILE A 1 59  ? 9.523   1.598   2.191   1.00 15.86 ? 59  ILE A CG1 1 
ATOM   467  C  CG2 . ILE A 1 59  ? 9.066   2.393   -0.166  1.00 15.45 ? 59  ILE A CG2 1 
ATOM   468  C  CD1 . ILE A 1 59  ? 8.672   0.329   2.098   1.00 16.56 ? 59  ILE A CD1 1 
ATOM   469  N  N   . LEU A 1 60  ? 12.060  3.706   2.027   1.00 15.46 ? 60  LEU A N   1 
ATOM   470  C  CA  . LEU A 1 60  ? 13.471  3.856   1.769   1.00 14.59 ? 60  LEU A CA  1 
ATOM   471  C  C   . LEU A 1 60  ? 14.237  2.669   2.347   1.00 15.77 ? 60  LEU A C   1 
ATOM   472  O  O   . LEU A 1 60  ? 14.023  2.271   3.502   1.00 15.91 ? 60  LEU A O   1 
ATOM   473  C  CB  . LEU A 1 60  ? 13.896  5.175   2.455   1.00 16.40 ? 60  LEU A CB  1 
ATOM   474  C  CG  . LEU A 1 60  ? 15.406  5.384   2.493   1.00 15.23 ? 60  LEU A CG  1 
ATOM   475  C  CD1 . LEU A 1 60  ? 15.992  5.576   1.092   1.00 16.24 ? 60  LEU A CD1 1 
ATOM   476  C  CD2 . LEU A 1 60  ? 15.852  6.542   3.410   1.00 15.05 ? 60  LEU A CD2 1 
ATOM   477  N  N   . ASN A 1 61  ? 15.176  2.145   1.568   1.00 12.90 ? 61  ASN A N   1 
ATOM   478  C  CA  . ASN A 1 61  ? 16.188  1.203   2.017   1.00 13.21 ? 61  ASN A CA  1 
ATOM   479  C  C   . ASN A 1 61  ? 17.397  2.020   2.474   1.00 17.49 ? 61  ASN A C   1 
ATOM   480  O  O   . ASN A 1 61  ? 18.100  2.618   1.656   1.00 17.10 ? 61  ASN A O   1 
ATOM   481  C  CB  . ASN A 1 61  ? 16.583  0.224   0.890   1.00 14.50 ? 61  ASN A CB  1 
ATOM   482  C  CG  . ASN A 1 61  ? 17.603  -0.801  1.299   1.00 15.77 ? 61  ASN A CG  1 
ATOM   483  O  OD1 . ASN A 1 61  ? 18.463  -0.565  2.164   1.00 16.06 ? 61  ASN A OD1 1 
ATOM   484  N  ND2 . ASN A 1 61  ? 17.584  -1.978  0.650   1.00 15.73 ? 61  ASN A ND2 1 
ATOM   485  N  N   . THR A 1 62  ? 17.716  1.993   3.773   1.00 13.67 ? 62  THR A N   1 
ATOM   486  C  CA  . THR A 1 62  ? 18.739  2.890   4.321   1.00 13.82 ? 62  THR A CA  1 
ATOM   487  C  C   . THR A 1 62  ? 20.118  2.213   4.298   1.00 14.52 ? 62  THR A C   1 
ATOM   488  O  O   . THR A 1 62  ? 21.159  2.837   4.614   1.00 17.18 ? 62  THR A O   1 
ATOM   489  C  CB  . THR A 1 62  ? 18.385  3.245   5.780   1.00 13.58 ? 62  THR A CB  1 
ATOM   490  O  OG1 . THR A 1 62  ? 18.565  2.008   6.510   1.00 15.04 ? 62  THR A OG1 1 
ATOM   491  C  CG2 . THR A 1 62  ? 17.023  3.863   5.983   1.00 15.83 ? 62  THR A CG2 1 
ATOM   492  N  N   . GLY A 1 63  ? 20.185  0.936   3.873   1.00 14.43 ? 63  GLY A N   1 
ATOM   493  C  CA  . GLY A 1 63  ? 21.378  0.114   3.961   1.00 14.65 ? 63  GLY A CA  1 
ATOM   494  C  C   . GLY A 1 63  ? 21.472  -0.720  5.253   1.00 14.70 ? 63  GLY A C   1 
ATOM   495  O  O   . GLY A 1 63  ? 22.316  -1.619  5.349   1.00 14.89 ? 63  GLY A O   1 
ATOM   496  N  N   A TYR A 1 64  ? 20.580  -0.412  6.201   0.50 14.16 ? 64  TYR A N   1 
ATOM   497  N  N   B TYR A 1 64  ? 20.606  -0.434  6.245   0.50 14.28 ? 64  TYR A N   1 
ATOM   498  C  CA  A TYR A 1 64  ? 20.540  -1.124  7.471   0.50 15.07 ? 64  TYR A CA  1 
ATOM   499  C  CA  B TYR A 1 64  ? 20.572  -1.239  7.471   0.50 15.04 ? 64  TYR A CA  1 
ATOM   500  C  C   A TYR A 1 64  ? 19.179  -1.781  7.697   0.50 14.33 ? 64  TYR A C   1 
ATOM   501  C  C   B TYR A 1 64  ? 19.143  -1.622  7.888   0.50 14.19 ? 64  TYR A C   1 
ATOM   502  O  O   A TYR A 1 64  ? 19.096  -2.805  8.380   0.50 13.82 ? 64  TYR A O   1 
ATOM   503  O  O   B TYR A 1 64  ? 18.957  -2.319  8.894   0.50 13.03 ? 64  TYR A O   1 
ATOM   504  C  CB  A TYR A 1 64  ? 20.893  -0.144  8.588   0.50 16.06 ? 64  TYR A CB  1 
ATOM   505  C  CB  B TYR A 1 64  ? 21.282  -0.513  8.618   0.50 16.64 ? 64  TYR A CB  1 
ATOM   506  C  CG  A TYR A 1 64  ? 22.304  0.367   8.472   0.50 17.11 ? 64  TYR A CG  1 
ATOM   507  C  CG  B TYR A 1 64  ? 20.841  0.921   8.758   0.50 17.80 ? 64  TYR A CG  1 
ATOM   508  C  CD1 A TYR A 1 64  ? 23.379  -0.461  8.742   0.50 17.90 ? 64  TYR A CD1 1 
ATOM   509  C  CD1 B TYR A 1 64  ? 19.711  1.272   9.482   0.50 18.80 ? 64  TYR A CD1 1 
ATOM   510  C  CD2 A TYR A 1 64  ? 22.561  1.662   8.068   0.50 20.35 ? 64  TYR A CD2 1 
ATOM   511  C  CD2 B TYR A 1 64  ? 21.523  1.938   8.120   0.50 16.32 ? 64  TYR A CD2 1 
ATOM   512  C  CE1 A TYR A 1 64  ? 24.678  0.001   8.679   0.50 20.43 ? 64  TYR A CE1 1 
ATOM   513  C  CE1 B TYR A 1 64  ? 19.270  2.587   9.552   0.50 18.68 ? 64  TYR A CE1 1 
ATOM   514  C  CE2 A TYR A 1 64  ? 23.862  2.137   7.975   0.50 20.53 ? 64  TYR A CE2 1 
ATOM   515  C  CE2 B TYR A 1 64  ? 21.106  3.257   8.196   0.50 18.40 ? 64  TYR A CE2 1 
ATOM   516  C  CZ  A TYR A 1 64  ? 24.919  1.299   8.279   0.50 21.28 ? 64  TYR A CZ  1 
ATOM   517  C  CZ  B TYR A 1 64  ? 19.967  3.584   8.915   0.50 18.84 ? 64  TYR A CZ  1 
ATOM   518  O  OH  A TYR A 1 64  ? 26.209  1.742   8.184   0.50 27.23 ? 64  TYR A OH  1 
ATOM   519  O  OH  B TYR A 1 64  ? 19.555  4.885   9.021   0.50 19.77 ? 64  TYR A OH  1 
ATOM   520  N  N   . LEU A 1 65  ? 18.137  -1.175  7.138   1.00 13.25 ? 65  LEU A N   1 
ATOM   521  C  CA  . LEU A 1 65  ? 16.747  -1.564  7.346   1.00 12.70 ? 65  LEU A CA  1 
ATOM   522  C  C   . LEU A 1 65  ? 15.940  -0.928  6.200   1.00 12.89 ? 65  LEU A C   1 
ATOM   523  O  O   . LEU A 1 65  ? 16.511  -0.246  5.341   1.00 13.81 ? 65  LEU A O   1 
ATOM   524  C  CB  . LEU A 1 65  ? 16.268  -1.158  8.754   1.00 13.65 ? 65  LEU A CB  1 
ATOM   525  C  CG  . LEU A 1 65  ? 16.573  0.273   9.186   1.00 12.74 ? 65  LEU A CG  1 
ATOM   526  C  CD1 . LEU A 1 65  ? 15.709  1.276   8.443   1.00 13.82 ? 65  LEU A CD1 1 
ATOM   527  C  CD2 . LEU A 1 65  ? 16.342  0.426   10.694  1.00 15.41 ? 65  LEU A CD2 1 
ATOM   528  N  N   . PHE A 1 66  ? 14.618  -1.060  6.202   1.00 13.29 ? 66  PHE A N   1 
ATOM   529  C  CA  . PHE A 1 66  ? 13.807  -0.157  5.429   1.00 12.62 ? 66  PHE A CA  1 
ATOM   530  C  C   . PHE A 1 66  ? 12.861  0.631   6.322   1.00 12.36 ? 66  PHE A C   1 
ATOM   531  O  O   . PHE A 1 66  ? 12.468  0.155   7.406   1.00 12.29 ? 66  PHE A O   1 
ATOM   532  C  CB  . PHE A 1 66  ? 13.050  -0.912  4.317   1.00 13.45 ? 66  PHE A CB  1 
ATOM   533  C  CG  . PHE A 1 66  ? 11.943  -1.776  4.851   1.00 11.70 ? 66  PHE A CG  1 
ATOM   534  C  CD1 . PHE A 1 66  ? 10.673  -1.233  4.942   1.00 12.64 ? 66  PHE A CD1 1 
ATOM   535  C  CD2 . PHE A 1 66  ? 12.122  -3.122  5.150   1.00 13.64 ? 66  PHE A CD2 1 
ATOM   536  C  CE1 . PHE A 1 66  ? 9.614   -1.974  5.434   1.00 14.31 ? 66  PHE A CE1 1 
ATOM   537  C  CE2 . PHE A 1 66  ? 11.050  -3.878  5.614   1.00 12.90 ? 66  PHE A CE2 1 
ATOM   538  C  CZ  . PHE A 1 66  ? 9.793   -3.305  5.761   1.00 13.45 ? 66  PHE A CZ  1 
ATOM   539  N  N   . GLN A 1 67  ? 12.517  1.838   5.892   1.00 13.81 ? 67  GLN A N   1 
ATOM   540  C  CA  . GLN A 1 67  ? 11.653  2.683   6.691   1.00 14.80 ? 67  GLN A CA  1 
ATOM   541  C  C   . GLN A 1 67  ? 10.602  3.344   5.824   1.00 14.54 ? 67  GLN A C   1 
ATOM   542  O  O   . GLN A 1 67  ? 10.875  3.698   4.674   1.00 16.19 ? 67  GLN A O   1 
ATOM   543  C  CB  . GLN A 1 67  ? 12.417  3.706   7.553   1.00 16.95 ? 67  GLN A CB  1 
ATOM   544  C  CG  . GLN A 1 67  ? 13.246  4.666   6.740   1.00 17.89 ? 67  GLN A CG  1 
ATOM   545  C  CD  . GLN A 1 67  ? 14.138  5.498   7.633   1.00 20.55 ? 67  GLN A CD  1 
ATOM   546  O  OE1 . GLN A 1 67  ? 14.854  4.998   8.499   1.00 20.98 ? 67  GLN A OE1 1 
ATOM   547  N  NE2 . GLN A 1 67  ? 14.111  6.782   7.349   1.00 22.15 ? 67  GLN A NE2 1 
ATOM   548  N  N   . VAL A 1 68  ? 9.436   3.516   6.385   1.00 13.66 ? 68  VAL A N   1 
ATOM   549  C  CA  . VAL A 1 68  ? 8.313   4.219   5.783   1.00 13.14 ? 68  VAL A CA  1 
ATOM   550  C  C   . VAL A 1 68  ? 8.255   5.569   6.484   1.00 15.61 ? 68  VAL A C   1 
ATOM   551  O  O   . VAL A 1 68  ? 8.150   5.616   7.708   1.00 14.78 ? 68  VAL A O   1 
ATOM   552  C  CB  . VAL A 1 68  ? 6.993   3.440   5.877   1.00 14.74 ? 68  VAL A CB  1 
ATOM   553  C  CG1 . VAL A 1 68  ? 5.804   4.316   5.518   1.00 15.94 ? 68  VAL A CG1 1 
ATOM   554  C  CG2 . VAL A 1 68  ? 6.998   2.207   4.979   1.00 13.53 ? 68  VAL A CG2 1 
ATOM   555  N  N   . GLU A 1 69  ? 8.213   6.662   5.710   1.00 15.39 ? 69  GLU A N   1 
ATOM   556  C  CA  . GLU A 1 69  ? 8.378   7.998   6.247   1.00 16.17 ? 69  GLU A CA  1 
ATOM   557  C  C   . GLU A 1 69  ? 7.046   8.684   6.082   1.00 16.82 ? 69  GLU A C   1 
ATOM   558  O  O   . GLU A 1 69  ? 6.285   8.442   5.116   1.00 17.71 ? 69  GLU A O   1 
ATOM   559  C  CB  . GLU A 1 69  ? 9.360   8.785   5.415   1.00 17.28 ? 69  GLU A CB  1 
ATOM   560  C  CG  . GLU A 1 69  ? 10.739  8.222   5.611   1.00 17.80 ? 69  GLU A CG  1 
ATOM   561  C  CD  . GLU A 1 69  ? 11.755  8.730   4.649   1.00 20.62 ? 69  GLU A CD  1 
ATOM   562  O  OE1 . GLU A 1 69  ? 12.950  8.489   4.932   1.00 24.55 ? 69  GLU A OE1 1 
ATOM   563  O  OE2 . GLU A 1 69  ? 11.313  9.396   3.697   1.00 24.58 ? 69  GLU A OE2 1 
ATOM   564  N  N   . PHE A 1 70  ? 6.779   9.547   7.045   1.00 14.27 ? 70  PHE A N   1 
ATOM   565  C  CA  . PHE A 1 70  ? 5.539   10.295  7.109   1.00 14.30 ? 70  PHE A CA  1 
ATOM   566  C  C   . PHE A 1 70  ? 5.827   11.789  7.054   1.00 14.89 ? 70  PHE A C   1 
ATOM   567  O  O   . PHE A 1 70  ? 6.910   12.232  7.391   1.00 16.37 ? 70  PHE A O   1 
ATOM   568  C  CB  . PHE A 1 70  ? 4.803   9.978   8.411   1.00 15.46 ? 70  PHE A CB  1 
ATOM   569  C  CG  . PHE A 1 70  ? 4.217   8.582   8.353   1.00 16.50 ? 70  PHE A CG  1 
ATOM   570  C  CD1 . PHE A 1 70  ? 5.011   7.493   8.652   1.00 16.07 ? 70  PHE A CD1 1 
ATOM   571  C  CD2 . PHE A 1 70  ? 2.896   8.333   8.011   1.00 16.18 ? 70  PHE A CD2 1 
ATOM   572  C  CE1 . PHE A 1 70  ? 4.535   6.192   8.536   1.00 17.85 ? 70  PHE A CE1 1 
ATOM   573  C  CE2 . PHE A 1 70  ? 2.395   7.031   7.928   1.00 16.49 ? 70  PHE A CE2 1 
ATOM   574  C  CZ  . PHE A 1 70  ? 3.227   5.956   8.187   1.00 17.58 ? 70  PHE A CZ  1 
ATOM   575  N  N   . ASP A 1 71  ? 4.854   12.530  6.520   1.00 17.45 ? 71  ASP A N   1 
ATOM   576  C  CA  . ASP A 1 71  ? 4.911   13.977  6.592   1.00 17.15 ? 71  ASP A CA  1 
ATOM   577  C  C   . ASP A 1 71  ? 4.587   14.393  8.010   1.00 16.09 ? 71  ASP A C   1 
ATOM   578  O  O   . ASP A 1 71  ? 3.467   14.217  8.505   1.00 21.26 ? 71  ASP A O   1 
ATOM   579  C  CB  . ASP A 1 71  ? 3.909   14.570  5.603   1.00 21.42 ? 71  ASP A CB  1 
ATOM   580  C  CG  . ASP A 1 71  ? 3.587   16.036  5.875   1.00 25.93 ? 71  ASP A CG  1 
ATOM   581  O  OD1 . ASP A 1 71  ? 4.408   16.717  6.497   1.00 22.39 ? 71  ASP A OD1 1 
ATOM   582  O  OD2 . ASP A 1 71  ? 2.488   16.479  5.450   1.00 33.28 ? 71  ASP A OD2 1 
ATOM   583  N  N   . ASP A 1 72  ? 5.612   14.879  8.713   1.00 15.76 ? 72  ASP A N   1 
ATOM   584  C  CA  . ASP A 1 72  ? 5.491   15.284  10.101  1.00 15.22 ? 72  ASP A CA  1 
ATOM   585  C  C   . ASP A 1 72  ? 5.591   16.808  10.229  1.00 18.08 ? 72  ASP A C   1 
ATOM   586  O  O   . ASP A 1 72  ? 6.111   17.285  11.237  1.00 20.79 ? 72  ASP A O   1 
ATOM   587  C  CB  . ASP A 1 72  ? 6.537   14.579  10.974  1.00 17.81 ? 72  ASP A CB  1 
ATOM   588  C  CG  . ASP A 1 72  ? 7.965   14.915  10.538  1.00 19.69 ? 72  ASP A CG  1 
ATOM   589  O  OD1 . ASP A 1 72  ? 8.131   15.600  9.474   1.00 22.10 ? 72  ASP A OD1 1 
ATOM   590  O  OD2 . ASP A 1 72  ? 8.942   14.494  11.207  1.00 21.06 ? 72  ASP A OD2 1 
ATOM   591  N  N   . SER A 1 73  ? 5.148   17.523  9.175   1.00 18.73 ? 73  SER A N   1 
ATOM   592  C  CA  . SER A 1 73  ? 5.228   18.997  9.158   1.00 20.07 ? 73  SER A CA  1 
ATOM   593  C  C   . SER A 1 73  ? 3.981   19.625  9.786   1.00 24.36 ? 73  SER A C   1 
ATOM   594  O  O   . SER A 1 73  ? 3.881   20.853  9.948   1.00 22.33 ? 73  SER A O   1 
ATOM   595  C  CB  . SER A 1 73  ? 5.438   19.523  7.752   1.00 20.31 ? 73  SER A CB  1 
ATOM   596  O  OG  . SER A 1 73  ? 4.274   19.295  6.952   1.00 23.54 ? 73  SER A OG  1 
ATOM   597  N  N   . GLN A 1 74  ? 3.011   18.792  10.160  1.00 25.46 ? 74  GLN A N   1 
ATOM   598  C  CA  . GLN A 1 74  ? 1.833   19.279  10.873  1.00 27.91 ? 74  GLN A CA  1 
ATOM   599  C  C   . GLN A 1 74  ? 1.464   18.234  11.917  1.00 28.68 ? 74  GLN A C   1 
ATOM   600  O  O   . GLN A 1 74  ? 1.985   17.120  11.860  1.00 24.50 ? 74  GLN A O   1 
ATOM   601  C  CB  . GLN A 1 74  ? 0.621   19.387  9.945   1.00 32.26 ? 74  GLN A CB  1 
ATOM   602  C  CG  . GLN A 1 74  ? 0.653   20.545  8.966   1.00 35.24 ? 74  GLN A CG  1 
ATOM   603  C  CD  . GLN A 1 74  ? -0.628  20.596  8.171   1.00 39.97 ? 74  GLN A CD  1 
ATOM   604  O  OE1 . GLN A 1 74  ? -1.600  21.234  8.575   1.00 50.14 ? 74  GLN A OE1 1 
ATOM   605  N  NE2 . GLN A 1 74  ? -0.641  19.929  7.029   1.00 35.87 ? 74  GLN A NE2 1 
ATOM   606  N  N   . ASP A 1 75  ? 0.571   18.602  12.849  1.00 31.94 ? 75  ASP A N   1 
ATOM   607  C  CA  . ASP A 1 75  ? 0.163   17.680  13.899  1.00 35.59 ? 75  ASP A CA  1 
ATOM   608  C  C   . ASP A 1 75  ? -0.885  16.733  13.314  1.00 33.91 ? 75  ASP A C   1 
ATOM   609  O  O   . ASP A 1 75  ? -2.071  17.065  13.233  1.00 38.14 ? 75  ASP A O   1 
ATOM   610  C  CB  . ASP A 1 75  ? -0.298  18.397  15.175  1.00 44.94 ? 75  ASP A CB  1 
ATOM   611  C  CG  . ASP A 1 75  ? 0.665   18.304  16.362  1.00 48.36 ? 75  ASP A CG  1 
ATOM   612  O  OD1 . ASP A 1 75  ? 1.520   17.365  16.406  1.00 41.82 ? 75  ASP A OD1 1 
ATOM   613  O  OD2 . ASP A 1 75  ? 0.550   19.170  17.264  1.00 52.05 ? 75  ASP A OD2 1 
ATOM   614  N  N   . LYS A 1 76  ? -0.414  15.578  12.851  1.00 29.87 ? 76  LYS A N   1 
ATOM   615  C  CA  . LYS A 1 76  ? -1.281  14.634  12.171  1.00 29.48 ? 76  LYS A CA  1 
ATOM   616  C  C   . LYS A 1 76  ? -1.410  13.395  13.048  1.00 32.26 ? 76  LYS A C   1 
ATOM   617  O  O   . LYS A 1 76  ? -2.299  13.297  13.888  1.00 39.82 ? 76  LYS A O   1 
ATOM   618  C  CB  . LYS A 1 76  ? -0.776  14.383  10.746  1.00 29.42 ? 76  LYS A CB  1 
ATOM   619  C  CG  . LYS A 1 76  ? -1.044  15.555  9.799   1.00 33.05 ? 76  LYS A CG  1 
ATOM   620  C  CD  . LYS A 1 76  ? -0.355  15.406  8.453   1.00 33.70 ? 76  LYS A CD  1 
ATOM   621  C  CE  . LYS A 1 76  ? -0.936  16.355  7.422   1.00 35.86 ? 76  LYS A CE  1 
ATOM   622  N  NZ  . LYS A 1 76  ? -0.674  15.909  6.035   1.00 39.04 ? 76  LYS A NZ  1 
ATOM   623  N  N   . ALA A 1 77  ? -0.441  12.515  12.906  1.00 26.60 ? 77  ALA A N   1 
ATOM   624  C  CA  . ALA A 1 77  ? -0.380  11.237  13.598  1.00 23.78 ? 77  ALA A CA  1 
ATOM   625  C  C   . ALA A 1 77  ? 0.443   11.443  14.864  1.00 23.33 ? 77  ALA A C   1 
ATOM   626  O  O   . ALA A 1 77  ? 1.614   11.772  14.763  1.00 27.41 ? 77  ALA A O   1 
ATOM   627  C  CB  . ALA A 1 77  ? 0.332   10.278  12.683  1.00 22.97 ? 77  ALA A CB  1 
ATOM   628  N  N   . VAL A 1 78  ? -0.175  11.261  16.023  1.00 18.77 ? 78  VAL A N   1 
ATOM   629  C  CA  . VAL A 1 78  ? 0.442   11.572  17.291  1.00 19.68 ? 78  VAL A CA  1 
ATOM   630  C  C   . VAL A 1 78  ? 0.261   10.416  18.260  1.00 16.98 ? 78  VAL A C   1 
ATOM   631  O  O   . VAL A 1 78  ? -0.760  9.732   18.260  1.00 18.62 ? 78  VAL A O   1 
ATOM   632  C  CB  . VAL A 1 78  ? -0.123  12.893  17.853  1.00 21.96 ? 78  VAL A CB  1 
ATOM   633  C  CG1 . VAL A 1 78  ? 0.154   14.050  16.887  1.00 23.92 ? 78  VAL A CG1 1 
ATOM   634  C  CG2 . VAL A 1 78  ? -1.591  12.782  18.126  1.00 26.13 ? 78  VAL A CG2 1 
ATOM   635  N  N   . LEU A 1 79  ? 1.270   10.234  19.110  1.00 15.88 ? 79  LEU A N   1 
ATOM   636  C  CA  . LEU A 1 79  ? 1.214   9.355   20.252  1.00 13.94 ? 79  LEU A CA  1 
ATOM   637  C  C   . LEU A 1 79  ? 1.262   10.232  21.474  1.00 15.40 ? 79  LEU A C   1 
ATOM   638  O  O   . LEU A 1 79  ? 2.090   11.126  21.558  1.00 16.37 ? 79  LEU A O   1 
ATOM   639  C  CB  . LEU A 1 79  ? 2.457   8.469   20.153  1.00 14.40 ? 79  LEU A CB  1 
ATOM   640  C  CG  . LEU A 1 79  ? 2.614   7.409   21.231  1.00 15.29 ? 79  LEU A CG  1 
ATOM   641  C  CD1 . LEU A 1 79  ? 1.501   6.395   21.137  1.00 18.14 ? 79  LEU A CD1 1 
ATOM   642  C  CD2 . LEU A 1 79  ? 3.934   6.687   21.029  1.00 15.58 ? 79  LEU A CD2 1 
ATOM   643  N  N   . LYS A 1 80  ? 0.418   9.926   22.436  1.00 15.28 ? 80  LYS A N   1 
ATOM   644  C  CA  . LYS A 1 80  ? 0.456   10.627  23.703  1.00 16.75 ? 80  LYS A CA  1 
ATOM   645  C  C   . LYS A 1 80  ? -0.093  9.704   24.781  1.00 17.55 ? 80  LYS A C   1 
ATOM   646  O  O   . LYS A 1 80  ? -0.457  8.580   24.477  1.00 16.97 ? 80  LYS A O   1 
ATOM   647  C  CB  . LYS A 1 80  ? -0.272  11.978  23.647  1.00 20.58 ? 80  LYS A CB  1 
ATOM   648  C  CG  . LYS A 1 80  ? -1.772  11.875  23.425  1.00 26.15 ? 80  LYS A CG  1 
ATOM   649  C  CD  . LYS A 1 80  ? -2.451  13.259  23.432  1.00 25.23 ? 80  LYS A CD  1 
ATOM   650  C  CE  . LYS A 1 80  ? -2.062  14.153  22.270  1.00 32.26 ? 80  LYS A CE  1 
ATOM   651  N  N   . GLY A 1 81  ? -0.096  10.199  26.010  1.00 17.99 ? 81  GLY A N   1 
ATOM   652  C  CA  . GLY A 1 81  ? -0.584  9.423   27.131  1.00 19.33 ? 81  GLY A CA  1 
ATOM   653  C  C   . GLY A 1 81  ? 0.427   8.368   27.548  1.00 19.25 ? 81  GLY A C   1 
ATOM   654  O  O   . GLY A 1 81  ? 1.633   8.498   27.322  1.00 18.92 ? 81  GLY A O   1 
ATOM   655  N  N   . GLY A 1 82  ? -0.059  7.349   28.252  1.00 23.60 ? 82  GLY A N   1 
ATOM   656  C  CA  . GLY A 1 82  ? 0.846   6.376   28.827  1.00 21.24 ? 82  GLY A CA  1 
ATOM   657  C  C   . GLY A 1 82  ? 1.875   7.015   29.750  1.00 24.29 ? 82  GLY A C   1 
ATOM   658  O  O   . GLY A 1 82  ? 1.532   7.768   30.671  1.00 22.86 ? 82  GLY A O   1 
ATOM   659  N  N   . PRO A 1 83  ? 3.188   6.759   29.539  1.00 17.76 ? 83  PRO A N   1 
ATOM   660  C  CA  . PRO A 1 83  ? 4.193   7.377   30.371  1.00 18.73 ? 83  PRO A CA  1 
ATOM   661  C  C   . PRO A 1 83  ? 4.607   8.747   29.871  1.00 17.46 ? 83  PRO A C   1 
ATOM   662  O  O   . PRO A 1 83  ? 5.478   9.373   30.464  1.00 23.54 ? 83  PRO A O   1 
ATOM   663  C  CB  . PRO A 1 83  ? 5.369   6.415   30.216  1.00 18.10 ? 83  PRO A CB  1 
ATOM   664  C  CG  . PRO A 1 83  ? 5.241   5.911   28.774  1.00 17.49 ? 83  PRO A CG  1 
ATOM   665  C  CD  . PRO A 1 83  ? 3.758   5.881   28.475  1.00 18.52 ? 83  PRO A CD  1 
ATOM   666  N  N   . LEU A 1 84  ? 3.993   9.202   28.776  1.00 16.42 ? 84  LEU A N   1 
ATOM   667  C  CA  . LEU A 1 84  ? 4.567   10.354  28.111  1.00 16.89 ? 84  LEU A CA  1 
ATOM   668  C  C   . LEU A 1 84  ? 3.963   11.638  28.678  1.00 20.15 ? 84  LEU A C   1 
ATOM   669  O  O   . LEU A 1 84  ? 2.779   11.679  28.982  1.00 20.18 ? 84  LEU A O   1 
ATOM   670  C  CB  . LEU A 1 84  ? 4.310   10.259  26.611  1.00 14.43 ? 84  LEU A CB  1 
ATOM   671  C  CG  . LEU A 1 84  ? 4.802   8.981   25.919  1.00 14.31 ? 84  LEU A CG  1 
ATOM   672  C  CD1 . LEU A 1 84  ? 4.241   8.913   24.496  1.00 14.96 ? 84  LEU A CD1 1 
ATOM   673  C  CD2 . LEU A 1 84  ? 6.363   8.939   25.911  1.00 14.44 ? 84  LEU A CD2 1 
ATOM   674  N  N   . ASP A 1 85  ? 4.803   12.669  28.701  1.00 20.03 ? 85  ASP A N   1 
ATOM   675  C  CA  . ASP A 1 85  ? 4.363   14.026  28.965  1.00 20.80 ? 85  ASP A CA  1 
ATOM   676  C  C   . ASP A 1 85  ? 4.303   14.706  27.614  1.00 23.21 ? 85  ASP A C   1 
ATOM   677  O  O   . ASP A 1 85  ? 5.249   14.615  26.826  1.00 24.93 ? 85  ASP A O   1 
ATOM   678  C  CB  . ASP A 1 85  ? 5.331   14.718  29.928  1.00 23.18 ? 85  ASP A CB  1 
ATOM   679  C  CG  . ASP A 1 85  ? 5.189   14.239  31.362  1.00 30.84 ? 85  ASP A CG  1 
ATOM   680  O  OD1 . ASP A 1 85  ? 4.083   13.761  31.733  1.00 33.51 ? 85  ASP A OD1 1 
ATOM   681  O  OD2 . ASP A 1 85  ? 6.171   14.329  32.090  1.00 29.71 ? 85  ASP A OD2 1 
ATOM   682  N  N   . GLY A 1 86  ? 3.185   15.358  27.314  1.00 22.94 ? 86  GLY A N   1 
ATOM   683  C  CA  . GLY A 1 86  ? 3.127   16.056  26.041  1.00 20.85 ? 86  GLY A CA  1 
ATOM   684  C  C   . GLY A 1 86  ? 2.728   15.152  24.867  1.00 23.95 ? 86  GLY A C   1 
ATOM   685  O  O   . GLY A 1 86  ? 2.026   14.147  25.019  1.00 27.18 ? 86  GLY A O   1 
ATOM   686  N  N   A THR A 1 87  ? 3.218   15.524  23.679  0.50 20.32 ? 87  THR A N   1 
ATOM   687  N  N   B THR A 1 87  ? 3.146   15.548  23.665  0.50 19.68 ? 87  THR A N   1 
ATOM   688  C  CA  A THR A 1 87  ? 2.712   15.023  22.414  0.50 19.24 ? 87  THR A CA  1 
ATOM   689  C  CA  B THR A 1 87  ? 2.683   14.870  22.473  0.50 18.25 ? 87  THR A CA  1 
ATOM   690  C  C   A THR A 1 87  ? 3.877   14.649  21.508  0.50 17.05 ? 87  THR A C   1 
ATOM   691  C  C   B THR A 1 87  ? 3.854   14.622  21.542  0.50 16.59 ? 87  THR A C   1 
ATOM   692  O  O   A THR A 1 87  ? 4.812   15.426  21.338  0.50 17.63 ? 87  THR A O   1 
ATOM   693  O  O   B THR A 1 87  ? 4.755   15.441  21.400  0.50 17.36 ? 87  THR A O   1 
ATOM   694  C  CB  A THR A 1 87  ? 1.926   16.114  21.666  0.50 21.83 ? 87  THR A CB  1 
ATOM   695  C  CB  B THR A 1 87  ? 1.630   15.678  21.702  0.50 19.64 ? 87  THR A CB  1 
ATOM   696  O  OG1 A THR A 1 87  ? 0.766   16.503  22.403  0.50 24.41 ? 87  THR A OG1 1 
ATOM   697  O  OG1 B THR A 1 87  ? 2.203   16.968  21.476  0.50 20.08 ? 87  THR A OG1 1 
ATOM   698  C  CG2 A THR A 1 87  ? 1.497   15.691  20.279  0.50 20.66 ? 87  THR A CG2 1 
ATOM   699  C  CG2 B THR A 1 87  ? 0.330   15.798  22.460  0.50 20.94 ? 87  THR A CG2 1 
ATOM   700  N  N   . TYR A 1 88  ? 3.833   13.435  20.946  1.00 15.43 ? 88  TYR A N   1 
ATOM   701  C  CA  . TYR A 1 88  ? 4.932   12.963  20.122  1.00 13.86 ? 88  TYR A CA  1 
ATOM   702  C  C   . TYR A 1 88  ? 4.409   12.655  18.730  1.00 14.31 ? 88  TYR A C   1 
ATOM   703  O  O   . TYR A 1 88  ? 3.373   12.018  18.599  1.00 17.84 ? 88  TYR A O   1 
ATOM   704  C  CB  . TYR A 1 88  ? 5.577   11.699  20.693  1.00 12.44 ? 88  TYR A CB  1 
ATOM   705  C  CG  . TYR A 1 88  ? 6.376   11.898  21.959  1.00 12.50 ? 88  TYR A CG  1 
ATOM   706  C  CD1 . TYR A 1 88  ? 5.778   12.322  23.160  1.00 13.58 ? 88  TYR A CD1 1 
ATOM   707  C  CD2 . TYR A 1 88  ? 7.752   11.685  21.962  1.00 12.77 ? 88  TYR A CD2 1 
ATOM   708  C  CE1 . TYR A 1 88  ? 6.523   12.437  24.337  1.00 13.67 ? 88  TYR A CE1 1 
ATOM   709  C  CE2 . TYR A 1 88  ? 8.512   11.824  23.112  1.00 11.04 ? 88  TYR A CE2 1 
ATOM   710  C  CZ  . TYR A 1 88  ? 7.900   12.195  24.295  1.00 12.69 ? 88  TYR A CZ  1 
ATOM   711  O  OH  . TYR A 1 88  ? 8.682   12.270  25.404  1.00 13.61 ? 88  TYR A OH  1 
ATOM   712  N  N   . ARG A 1 89  ? 5.064   13.164  17.693  1.00 13.01 ? 89  ARG A N   1 
ATOM   713  C  CA  . ARG A 1 89  ? 4.581   13.094  16.327  1.00 13.35 ? 89  ARG A CA  1 
ATOM   714  C  C   . ARG A 1 89  ? 5.227   11.948  15.547  1.00 11.51 ? 89  ARG A C   1 
ATOM   715  O  O   . ARG A 1 89  ? 6.463   11.808  15.553  1.00 11.25 ? 89  ARG A O   1 
ATOM   716  C  CB  . ARG A 1 89  ? 4.884   14.445  15.661  1.00 14.23 ? 89  ARG A CB  1 
ATOM   717  C  CG  . ARG A 1 89  ? 4.203   14.609  14.319  1.00 18.28 ? 89  ARG A CG  1 
ATOM   718  C  CD  . ARG A 1 89  ? 4.382   15.996  13.708  1.00 19.50 ? 89  ARG A CD  1 
ATOM   719  N  NE  . ARG A 1 89  ? 3.776   17.024  14.552  1.00 20.32 ? 89  ARG A NE  1 
ATOM   720  C  CZ  . ARG A 1 89  ? 4.026   18.330  14.446  1.00 20.59 ? 89  ARG A CZ  1 
ATOM   721  N  NH1 . ARG A 1 89  ? 4.866   18.808  13.537  1.00 20.64 ? 89  ARG A NH1 1 
ATOM   722  N  NH2 . ARG A 1 89  ? 3.389   19.173  15.237  1.00 21.42 ? 89  ARG A NH2 1 
ATOM   723  N  N   . LEU A 1 90  ? 4.432   11.153  14.813  1.00 12.48 ? 90  LEU A N   1 
ATOM   724  C  CA  . LEU A 1 90  ? 4.997   10.039  14.058  1.00 12.89 ? 90  LEU A CA  1 
ATOM   725  C  C   . LEU A 1 90  ? 5.829   10.543  12.898  1.00 12.06 ? 90  LEU A C   1 
ATOM   726  O  O   . LEU A 1 90  ? 5.378   11.397  12.117  1.00 15.78 ? 90  LEU A O   1 
ATOM   727  C  CB  . LEU A 1 90  ? 3.866   9.147   13.518  1.00 14.25 ? 90  LEU A CB  1 
ATOM   728  C  CG  . LEU A 1 90  ? 4.317   8.041   12.566  1.00 14.05 ? 90  LEU A CG  1 
ATOM   729  C  CD1 . LEU A 1 90  ? 5.047   6.932   13.336  1.00 14.87 ? 90  LEU A CD1 1 
ATOM   730  C  CD2 . LEU A 1 90  ? 3.066   7.425   11.935  1.00 16.27 ? 90  LEU A CD2 1 
ATOM   731  N  N   . LYS A 1 91  ? 7.077   10.073  12.831  1.00 12.24 ? 91  LYS A N   1 
ATOM   732  C  CA  . LYS A 1 91  ? 8.017   10.429  11.786  1.00 13.46 ? 91  LYS A CA  1 
ATOM   733  C  C   . LYS A 1 91  ? 8.195   9.278   10.814  1.00 13.88 ? 91  LYS A C   1 
ATOM   734  O  O   . LYS A 1 91  ? 8.251   9.484   9.595   1.00 12.15 ? 91  LYS A O   1 
ATOM   735  C  CB  . LYS A 1 91  ? 9.362   10.883  12.377  1.00 14.98 ? 91  LYS A CB  1 
ATOM   736  C  CG  . LYS A 1 91  ? 10.483  10.980  11.353  1.00 16.51 ? 91  LYS A CG  1 
ATOM   737  C  CD  . LYS A 1 91  ? 11.757  11.650  11.808  1.00 23.07 ? 91  LYS A CD  1 
ATOM   738  C  CE  . LYS A 1 91  ? 12.349  12.429  10.647  1.00 28.44 ? 91  LYS A CE  1 
ATOM   739  N  NZ  . LYS A 1 91  ? 11.297  13.284  10.024  1.00 30.49 ? 91  LYS A NZ  1 
ATOM   740  N  N   . GLN A 1 92  ? 8.348   8.047   11.312  1.00 13.08 ? 92  GLN A N   1 
ATOM   741  C  CA  . GLN A 1 92  ? 8.708   6.956   10.401  1.00 13.39 ? 92  GLN A CA  1 
ATOM   742  C  C   . GLN A 1 92  ? 8.494   5.637   11.149  1.00 13.15 ? 92  GLN A C   1 
ATOM   743  O  O   . GLN A 1 92  ? 8.352   5.689   12.378  1.00 12.85 ? 92  GLN A O   1 
ATOM   744  C  CB  . GLN A 1 92  ? 10.147  7.017   9.896   1.00 15.11 ? 92  GLN A CB  1 
ATOM   745  C  CG  . GLN A 1 92  ? 11.186  7.065   11.020  1.00 15.00 ? 92  GLN A CG  1 
ATOM   746  C  CD  . GLN A 1 92  ? 11.963  5.795   11.283  1.00 15.88 ? 92  GLN A CD  1 
ATOM   747  O  OE1 . GLN A 1 92  ? 11.424  4.699   11.222  1.00 13.86 ? 92  GLN A OE1 1 
ATOM   748  N  NE2 . GLN A 1 92  ? 13.239  5.959   11.603  1.00 19.77 ? 92  GLN A NE2 1 
ATOM   749  N  N   . PHE A 1 93  ? 8.194   4.548   10.418  1.00 11.99 ? 93  PHE A N   1 
ATOM   750  C  CA  . PHE A 1 93  ? 8.313   3.245   11.051  1.00 11.86 ? 93  PHE A CA  1 
ATOM   751  C  C   . PHE A 1 93  ? 9.310   2.406   10.275  1.00 10.64 ? 93  PHE A C   1 
ATOM   752  O  O   . PHE A 1 93  ? 9.585   2.624   9.103   1.00 11.93 ? 93  PHE A O   1 
ATOM   753  C  CB  . PHE A 1 93  ? 6.963   2.547   11.228  1.00 11.95 ? 93  PHE A CB  1 
ATOM   754  C  CG  . PHE A 1 93  ? 6.266   2.093   9.967   1.00 12.79 ? 93  PHE A CG  1 
ATOM   755  C  CD1 . PHE A 1 93  ? 6.703   1.002   9.226   1.00 13.19 ? 93  PHE A CD1 1 
ATOM   756  C  CD2 . PHE A 1 93  ? 5.132   2.778   9.541   1.00 13.45 ? 93  PHE A CD2 1 
ATOM   757  C  CE1 . PHE A 1 93  ? 6.008   0.619   8.083   1.00 14.33 ? 93  PHE A CE1 1 
ATOM   758  C  CE2 . PHE A 1 93  ? 4.427   2.376   8.420   1.00 15.19 ? 93  PHE A CE2 1 
ATOM   759  C  CZ  . PHE A 1 93  ? 4.888   1.330   7.673   1.00 15.39 ? 93  PHE A CZ  1 
ATOM   760  N  N   . HIS A 1 94  ? 9.862   1.398   10.935  1.00 9.88  ? 94  HIS A N   1 
ATOM   761  C  CA  . HIS A 1 94  ? 10.798  0.470   10.317  1.00 10.21 ? 94  HIS A CA  1 
ATOM   762  C  C   . HIS A 1 94  ? 10.743  -0.849  11.045  1.00 10.16 ? 94  HIS A C   1 
ATOM   763  O  O   . HIS A 1 94  ? 10.022  -0.975  12.048  1.00 10.65 ? 94  HIS A O   1 
ATOM   764  C  CB  . HIS A 1 94  ? 12.231  1.008   10.320  1.00 11.30 ? 94  HIS A CB  1 
ATOM   765  C  CG  . HIS A 1 94  ? 12.734  1.233   11.718  1.00 10.23 ? 94  HIS A CG  1 
ATOM   766  N  ND1 . HIS A 1 94  ? 12.541  2.445   12.377  1.00 10.29 ? 94  HIS A ND1 1 
ATOM   767  C  CD2 . HIS A 1 94  ? 13.325  0.373   12.593  1.00 10.19 ? 94  HIS A CD2 1 
ATOM   768  C  CE1 . HIS A 1 94  ? 13.054  2.328   13.598  1.00 9.40  ? 94  HIS A CE1 1 
ATOM   769  N  NE2 . HIS A 1 94  ? 13.536  1.082   13.753  1.00 8.12  ? 94  HIS A NE2 1 
ATOM   770  N  N   . PHE A 1 95  ? 11.495  -1.799  10.514  1.00 9.94  ? 95  PHE A N   1 
ATOM   771  C  CA  . PHE A 1 95  ? 11.541  -3.117  11.131  1.00 8.84  ? 95  PHE A CA  1 
ATOM   772  C  C   . PHE A 1 95  ? 12.982  -3.595  11.263  1.00 10.51 ? 95  PHE A C   1 
ATOM   773  O  O   . PHE A 1 95  ? 13.903  -3.131  10.604  1.00 11.33 ? 95  PHE A O   1 
ATOM   774  C  CB  . PHE A 1 95  ? 10.848  -4.171  10.254  1.00 9.70  ? 95  PHE A CB  1 
ATOM   775  C  CG  . PHE A 1 95  ? 9.392   -3.910  9.959   1.00 10.09 ? 95  PHE A CG  1 
ATOM   776  C  CD1 . PHE A 1 95  ? 9.017   -3.008  8.963   1.00 10.57 ? 95  PHE A CD1 1 
ATOM   777  C  CD2 . PHE A 1 95  ? 8.399   -4.603  10.618  1.00 10.95 ? 95  PHE A CD2 1 
ATOM   778  C  CE1 . PHE A 1 95  ? 7.676   -2.815  8.652   1.00 11.36 ? 95  PHE A CE1 1 
ATOM   779  C  CE2 . PHE A 1 95  ? 7.062   -4.401  10.331  1.00 10.64 ? 95  PHE A CE2 1 
ATOM   780  C  CZ  . PHE A 1 95  ? 6.694   -3.491  9.345   1.00 11.20 ? 95  PHE A CZ  1 
ATOM   781  N  N   . HIS A 1 96  ? 13.139  -4.517  12.233  1.00 9.78  ? 96  HIS A N   1 
ATOM   782  C  CA  . HIS A 1 96  ? 14.340  -5.333  12.375  1.00 10.46 ? 96  HIS A CA  1 
ATOM   783  C  C   . HIS A 1 96  ? 13.896  -6.787  12.259  1.00 11.22 ? 96  HIS A C   1 
ATOM   784  O  O   . HIS A 1 96  ? 12.821  -7.113  12.774  1.00 11.40 ? 96  HIS A O   1 
ATOM   785  C  CB  . HIS A 1 96  ? 15.065  -5.119  13.728  1.00 10.41 ? 96  HIS A CB  1 
ATOM   786  C  CG  . HIS A 1 96  ? 15.284  -3.672  14.026  1.00 10.73 ? 96  HIS A CG  1 
ATOM   787  N  ND1 . HIS A 1 96  ? 16.530  -3.042  13.829  1.00 10.58 ? 96  HIS A ND1 1 
ATOM   788  C  CD2 . HIS A 1 96  ? 14.436  -2.731  14.454  1.00 10.05 ? 96  HIS A CD2 1 
ATOM   789  C  CE1 . HIS A 1 96  ? 16.415  -1.762  14.217  1.00 10.64 ? 96  HIS A CE1 1 
ATOM   790  N  NE2 . HIS A 1 96  ? 15.115  -1.548  14.525  1.00 10.07 ? 96  HIS A NE2 1 
ATOM   791  N  N   . TRP A 1 97  ? 14.707  -7.647  11.638  1.00 9.58  ? 97  TRP A N   1 
ATOM   792  C  CA  . TRP A 1 97  ? 14.265  -9.032  11.464  1.00 9.75  ? 97  TRP A CA  1 
ATOM   793  C  C   . TRP A 1 97  ? 15.463  -9.982  11.349  1.00 9.73  ? 97  TRP A C   1 
ATOM   794  O  O   . TRP A 1 97  ? 16.606  -9.555  11.248  1.00 10.98 ? 97  TRP A O   1 
ATOM   795  C  CB  . TRP A 1 97  ? 13.365  -9.170  10.233  1.00 10.53 ? 97  TRP A CB  1 
ATOM   796  C  CG  . TRP A 1 97  ? 14.062  -8.773  8.964   1.00 10.77 ? 97  TRP A CG  1 
ATOM   797  C  CD1 . TRP A 1 97  ? 14.796  -9.585  8.160   1.00 11.45 ? 97  TRP A CD1 1 
ATOM   798  C  CD2 . TRP A 1 97  ? 14.126  -7.454  8.407   1.00 11.18 ? 97  TRP A CD2 1 
ATOM   799  N  NE1 . TRP A 1 97  ? 15.233  -8.889  7.068   1.00 12.71 ? 97  TRP A NE1 1 
ATOM   800  C  CE2 . TRP A 1 97  ? 14.854  -7.576  7.209   1.00 11.75 ? 97  TRP A CE2 1 
ATOM   801  C  CE3 . TRP A 1 97  ? 13.605  -6.201  8.766   1.00 12.11 ? 97  TRP A CE3 1 
ATOM   802  C  CZ2 . TRP A 1 97  ? 15.115  -6.480  6.387   1.00 12.89 ? 97  TRP A CZ2 1 
ATOM   803  C  CZ3 . TRP A 1 97  ? 13.879  -5.114  7.953   1.00 12.83 ? 97  TRP A CZ3 1 
ATOM   804  C  CH2 . TRP A 1 97  ? 14.651  -5.246  6.788   1.00 11.95 ? 97  TRP A CH2 1 
ATOM   805  N  N   . GLY A 1 98  ? 15.137  -11.285 11.358  1.00 11.36 ? 98  GLY A N   1 
ATOM   806  C  CA  . GLY A 1 98  ? 16.129  -12.348 11.430  1.00 10.45 ? 98  GLY A CA  1 
ATOM   807  C  C   . GLY A 1 98  ? 16.400  -13.056 10.088  1.00 12.00 ? 98  GLY A C   1 
ATOM   808  O  O   . GLY A 1 98  ? 15.699  -12.816 9.126   1.00 13.16 ? 98  GLY A O   1 
ATOM   809  N  N   . SER A 1 99  ? 17.452  -13.862 10.081  1.00 13.08 ? 99  SER A N   1 
ATOM   810  C  CA  . SER A 1 99  ? 17.677  -14.782 8.960   1.00 13.72 ? 99  SER A CA  1 
ATOM   811  C  C   . SER A 1 99  ? 16.771  -16.020 9.085   1.00 14.68 ? 99  SER A C   1 
ATOM   812  O  O   . SER A 1 99  ? 16.644  -16.776 8.104   1.00 18.28 ? 99  SER A O   1 
ATOM   813  C  CB  . SER A 1 99  ? 19.146  -15.143 8.943   1.00 14.31 ? 99  SER A CB  1 
ATOM   814  O  OG  . SER A 1 99  ? 19.512  -15.712 10.196  1.00 15.84 ? 99  SER A OG  1 
ATOM   815  N  N   . LEU A 1 100 ? 16.175  -16.260 10.270  1.00 13.99 ? 100 LEU A N   1 
ATOM   816  C  CA  . LEU A 1 100 ? 15.369  -17.413 10.633  1.00 16.21 ? 100 LEU A CA  1 
ATOM   817  C  C   . LEU A 1 100 ? 14.194  -16.906 11.460  1.00 14.68 ? 100 LEU A C   1 
ATOM   818  O  O   . LEU A 1 100 ? 14.311  -15.898 12.161  1.00 15.24 ? 100 LEU A O   1 
ATOM   819  C  CB  . LEU A 1 100 ? 16.173  -18.344 11.544  1.00 20.23 ? 100 LEU A CB  1 
ATOM   820  C  CG  . LEU A 1 100 ? 17.539  -18.759 11.012  1.00 22.65 ? 100 LEU A CG  1 
ATOM   821  C  CD1 . LEU A 1 100 ? 18.480  -19.110 12.152  1.00 25.33 ? 100 LEU A CD1 1 
ATOM   822  C  CD2 . LEU A 1 100 ? 17.366  -19.925 10.039  1.00 23.16 ? 100 LEU A CD2 1 
ATOM   823  N  N   . ASP A 1 101 ? 13.091  -17.670 11.467  1.00 14.50 ? 101 ASP A N   1 
ATOM   824  C  CA  . ASP A 1 101 ? 11.913  -17.207 12.188  1.00 13.95 ? 101 ASP A CA  1 
ATOM   825  C  C   . ASP A 1 101 ? 12.200  -17.123 13.699  1.00 14.09 ? 101 ASP A C   1 
ATOM   826  O  O   . ASP A 1 101 ? 11.529  -16.373 14.381  1.00 18.55 ? 101 ASP A O   1 
ATOM   827  C  CB  . ASP A 1 101 ? 10.712  -18.114 11.924  1.00 14.58 ? 101 ASP A CB  1 
ATOM   828  C  CG  . ASP A 1 101 ? 10.214  -18.129 10.493  1.00 16.83 ? 101 ASP A CG  1 
ATOM   829  O  OD1 . ASP A 1 101 ? 10.606  -17.274 9.667   1.00 15.59 ? 101 ASP A OD1 1 
ATOM   830  O  OD2 . ASP A 1 101 ? 9.380   -18.995 10.203  1.00 18.83 ? 101 ASP A OD2 1 
ATOM   831  N  N   . GLY A 1 102 ? 13.187  -17.907 14.196  1.00 17.16 ? 102 GLY A N   1 
ATOM   832  C  CA  . GLY A 1 102 ? 13.584  -17.986 15.606  1.00 15.91 ? 102 GLY A CA  1 
ATOM   833  C  C   . GLY A 1 102 ? 14.288  -16.762 16.189  1.00 15.35 ? 102 GLY A C   1 
ATOM   834  O  O   . GLY A 1 102 ? 14.617  -16.730 17.388  1.00 17.57 ? 102 GLY A O   1 
ATOM   835  N  N   . GLN A 1 103 ? 14.521  -15.734 15.370  1.00 12.63 ? 103 GLN A N   1 
ATOM   836  C  CA  . GLN A 1 103 ? 15.275  -14.593 15.877  1.00 11.25 ? 103 GLN A CA  1 
ATOM   837  C  C   . GLN A 1 103 ? 14.961  -13.415 14.980  1.00 10.40 ? 103 GLN A C   1 
ATOM   838  O  O   . GLN A 1 103 ? 14.403  -13.556 13.901  1.00 11.57 ? 103 GLN A O   1 
ATOM   839  C  CB  . GLN A 1 103 ? 16.774  -14.915 15.881  1.00 13.60 ? 103 GLN A CB  1 
ATOM   840  C  CG  . GLN A 1 103 ? 17.339  -15.073 14.460  1.00 15.18 ? 103 GLN A CG  1 
ATOM   841  C  CD  . GLN A 1 103 ? 18.741  -15.641 14.516  1.00 18.71 ? 103 GLN A CD  1 
ATOM   842  O  OE1 . GLN A 1 103 ? 18.989  -16.658 15.164  1.00 23.84 ? 103 GLN A OE1 1 
ATOM   843  N  NE2 . GLN A 1 103 ? 19.667  -15.027 13.802  1.00 16.82 ? 103 GLN A NE2 1 
ATOM   844  N  N   . GLY A 1 104 ? 15.288  -12.204 15.454  1.00 10.47 ? 104 GLY A N   1 
ATOM   845  C  CA  . GLY A 1 104 ? 15.003  -11.015 14.666  1.00 10.11 ? 104 GLY A CA  1 
ATOM   846  C  C   . GLY A 1 104 ? 14.573  -9.818  15.491  1.00 9.93  ? 104 GLY A C   1 
ATOM   847  O  O   . GLY A 1 104 ? 14.791  -8.665  15.109  1.00 11.26 ? 104 GLY A O   1 
ATOM   848  N  N   . SER A 1 105 ? 13.867  -10.084 16.583  1.00 9.05  ? 105 SER A N   1 
ATOM   849  C  CA  . SER A 1 105 ? 13.476  -8.961  17.434  1.00 9.30  ? 105 SER A CA  1 
ATOM   850  C  C   . SER A 1 105 ? 14.681  -8.422  18.206  1.00 9.23  ? 105 SER A C   1 
ATOM   851  O  O   . SER A 1 105 ? 15.683  -9.105  18.418  1.00 9.32  ? 105 SER A O   1 
ATOM   852  C  CB  . SER A 1 105 ? 12.342  -9.333  18.356  1.00 8.62  ? 105 SER A CB  1 
ATOM   853  O  OG  . SER A 1 105 ? 12.721  -10.298 19.311  1.00 10.27 ? 105 SER A OG  1 
ATOM   854  N  N   . GLU A 1 106 ? 14.542  -7.172  18.626  1.00 9.80  ? 106 GLU A N   1 
ATOM   855  C  CA  . GLU A 1 106 ? 15.576  -6.494  19.427  1.00 9.63  ? 106 GLU A CA  1 
ATOM   856  C  C   . GLU A 1 106 ? 15.214  -6.674  20.905  1.00 10.15 ? 106 GLU A C   1 
ATOM   857  O  O   . GLU A 1 106 ? 15.982  -7.246  21.664  1.00 10.75 ? 106 GLU A O   1 
ATOM   858  C  CB  . GLU A 1 106 ? 15.601  -5.016  19.004  1.00 9.93  ? 106 GLU A CB  1 
ATOM   859  C  CG  . GLU A 1 106 ? 15.987  -4.856  17.531  1.00 8.91  ? 106 GLU A CG  1 
ATOM   860  C  CD  . GLU A 1 106 ? 16.708  -3.569  17.243  1.00 9.94  ? 106 GLU A CD  1 
ATOM   861  O  OE1 . GLU A 1 106 ? 16.143  -2.478  17.501  1.00 10.55 ? 106 GLU A OE1 1 
ATOM   862  O  OE2 . GLU A 1 106 ? 17.899  -3.648  16.864  1.00 11.31 ? 106 GLU A OE2 1 
ATOM   863  N  N   . HIS A 1 107 ? 14.018  -6.255  21.320  1.00 9.18  ? 107 HIS A N   1 
ATOM   864  C  CA  . HIS A 1 107 ? 13.633  -6.626  22.662  1.00 9.10  ? 107 HIS A CA  1 
ATOM   865  C  C   . HIS A 1 107 ? 13.326  -8.111  22.662  1.00 9.35  ? 107 HIS A C   1 
ATOM   866  O  O   . HIS A 1 107 ? 12.981  -8.708  21.630  1.00 9.75  ? 107 HIS A O   1 
ATOM   867  C  CB  . HIS A 1 107 ? 12.376  -5.832  23.040  1.00 9.06  ? 107 HIS A CB  1 
ATOM   868  C  CG  . HIS A 1 107 ? 12.712  -4.403  23.202  1.00 9.00  ? 107 HIS A CG  1 
ATOM   869  N  ND1 . HIS A 1 107 ? 12.638  -3.499  22.151  1.00 9.83  ? 107 HIS A ND1 1 
ATOM   870  C  CD2 . HIS A 1 107 ? 13.133  -3.690  24.272  1.00 8.74  ? 107 HIS A CD2 1 
ATOM   871  C  CE1 . HIS A 1 107 ? 13.062  -2.293  22.559  1.00 9.32  ? 107 HIS A CE1 1 
ATOM   872  N  NE2 . HIS A 1 107 ? 13.368  -2.375  23.859  1.00 9.15  ? 107 HIS A NE2 1 
ATOM   873  N  N   . THR A 1 108 ? 13.399  -8.667  23.888  1.00 10.30 ? 108 THR A N   1 
ATOM   874  C  CA  . THR A 1 108 ? 13.008  -10.062 24.120  1.00 10.49 ? 108 THR A CA  1 
ATOM   875  C  C   . THR A 1 108 ? 12.048  -10.078 25.315  1.00 10.35 ? 108 THR A C   1 
ATOM   876  O  O   . THR A 1 108 ? 12.055  -9.141  26.104  1.00 10.84 ? 108 THR A O   1 
ATOM   877  C  CB  . THR A 1 108 ? 14.207  -11.010 24.322  1.00 10.78 ? 108 THR A CB  1 
ATOM   878  O  OG1 . THR A 1 108 ? 15.059  -10.521 25.364  1.00 11.20 ? 108 THR A OG1 1 
ATOM   879  C  CG2 . THR A 1 108 ? 15.071  -11.115 23.080  1.00 10.74 ? 108 THR A CG2 1 
ATOM   880  N  N   . VAL A 1 109 ? 11.242  -11.146 25.411  1.00 12.15 ? 109 VAL A N   1 
ATOM   881  C  CA  . VAL A 1 109 ? 10.309  -11.240 26.536  1.00 13.03 ? 109 VAL A CA  1 
ATOM   882  C  C   . VAL A 1 109 ? 10.643  -12.513 27.319  1.00 13.35 ? 109 VAL A C   1 
ATOM   883  O  O   . VAL A 1 109 ? 10.496  -13.599 26.760  1.00 14.73 ? 109 VAL A O   1 
ATOM   884  C  CB  . VAL A 1 109 ? 8.866   -11.241 25.987  1.00 13.13 ? 109 VAL A CB  1 
ATOM   885  C  CG1 . VAL A 1 109 ? 7.880   -11.306 27.147  1.00 14.45 ? 109 VAL A CG1 1 
ATOM   886  C  CG2 . VAL A 1 109 ? 8.567   -9.983  25.170  1.00 13.61 ? 109 VAL A CG2 1 
ATOM   887  N  N   . ASP A 1 110 ? 11.090  -12.394 28.565  1.00 14.65 ? 110 ASP A N   1 
ATOM   888  C  CA  . ASP A 1 110 ? 11.587  -13.582 29.274  1.00 15.31 ? 110 ASP A CA  1 
ATOM   889  C  C   . ASP A 1 110 ? 12.501  -14.396 28.349  1.00 13.87 ? 110 ASP A C   1 
ATOM   890  O  O   . ASP A 1 110 ? 12.425  -15.630 28.299  1.00 15.03 ? 110 ASP A O   1 
ATOM   891  C  CB  . ASP A 1 110 ? 10.402  -14.401 29.812  1.00 18.16 ? 110 ASP A CB  1 
ATOM   892  C  CG  . ASP A 1 110 ? 9.510   -13.582 30.746  1.00 15.80 ? 110 ASP A CG  1 
ATOM   893  O  OD1 . ASP A 1 110 ? 10.077  -12.789 31.508  1.00 19.84 ? 110 ASP A OD1 1 
ATOM   894  O  OD2 . ASP A 1 110 ? 8.258   -13.806 30.684  1.00 21.19 ? 110 ASP A OD2 1 
ATOM   895  N  N   . LYS A 1 111 ? 13.382  -13.696 27.656  1.00 13.52 ? 111 LYS A N   1 
ATOM   896  C  CA  . LYS A 1 111 ? 14.422  -14.209 26.754  1.00 14.17 ? 111 LYS A CA  1 
ATOM   897  C  C   . LYS A 1 111 ? 13.887  -14.729 25.413  1.00 15.14 ? 111 LYS A C   1 
ATOM   898  O  O   . LYS A 1 111 ? 14.709  -15.101 24.567  1.00 14.63 ? 111 LYS A O   1 
ATOM   899  C  CB  . LYS A 1 111 ? 15.305  -15.283 27.423  1.00 17.50 ? 111 LYS A CB  1 
ATOM   900  C  CG  . LYS A 1 111 ? 16.045  -14.783 28.664  1.00 19.30 ? 111 LYS A CG  1 
ATOM   901  C  CD  . LYS A 1 111 ? 17.121  -13.761 28.308  1.00 22.70 ? 111 LYS A CD  1 
ATOM   902  C  CE  . LYS A 1 111 ? 17.801  -13.124 29.507  1.00 26.30 ? 111 LYS A CE  1 
ATOM   903  N  NZ  . LYS A 1 111 ? 19.075  -13.833 29.758  1.00 34.42 ? 111 LYS A NZ  1 
ATOM   904  N  N   . LYS A 1 112 ? 12.564  -14.708 25.210  1.00 13.28 ? 112 LYS A N   1 
ATOM   905  C  CA  . LYS A 1 112 ? 11.959  -15.093 23.947  1.00 12.96 ? 112 LYS A CA  1 
ATOM   906  C  C   . LYS A 1 112 ? 12.289  -14.051 22.881  1.00 13.31 ? 112 LYS A C   1 
ATOM   907  O  O   . LYS A 1 112 ? 12.061  -12.852 23.081  1.00 11.90 ? 112 LYS A O   1 
ATOM   908  C  CB  . LYS A 1 112 ? 10.434  -15.197 24.050  1.00 14.67 ? 112 LYS A CB  1 
ATOM   909  C  CG  . LYS A 1 112 ? 9.790   -15.677 22.762  1.00 15.19 ? 112 LYS A CG  1 
ATOM   910  C  CD  . LYS A 1 112 ? 8.265   -15.681 22.823  1.00 16.74 ? 112 LYS A CD  1 
ATOM   911  C  CE  . LYS A 1 112 ? 7.656   -15.731 21.450  1.00 21.21 ? 112 LYS A CE  1 
ATOM   912  N  NZ  . LYS A 1 112 ? 7.841   -17.072 20.881  1.00 21.36 ? 112 LYS A NZ  1 
ATOM   913  N  N   . LYS A 1 113 ? 12.840  -14.539 21.760  1.00 12.04 ? 113 LYS A N   1 
ATOM   914  C  CA  . LYS A 1 113 ? 13.047  -13.743 20.555  1.00 11.71 ? 113 LYS A CA  1 
ATOM   915  C  C   . LYS A 1 113 ? 11.910  -13.977 19.575  1.00 12.42 ? 113 LYS A C   1 
ATOM   916  O  O   . LYS A 1 113 ? 11.574  -15.132 19.287  1.00 13.51 ? 113 LYS A O   1 
ATOM   917  C  CB  . LYS A 1 113 ? 14.353  -14.149 19.871  1.00 12.98 ? 113 LYS A CB  1 
ATOM   918  C  CG  . LYS A 1 113 ? 15.581  -13.783 20.659  1.00 13.76 ? 113 LYS A CG  1 
ATOM   919  C  CD  . LYS A 1 113 ? 16.876  -14.349 20.054  1.00 15.26 ? 113 LYS A CD  1 
ATOM   920  C  CE  . LYS A 1 113 ? 18.042  -13.651 20.716  1.00 18.10 ? 113 LYS A CE  1 
ATOM   921  N  NZ  . LYS A 1 113 ? 19.152  -14.598 20.864  1.00 25.48 ? 113 LYS A NZ  1 
ATOM   922  N  N   . TYR A 1 114 ? 11.370  -12.889 19.014  1.00 11.40 ? 114 TYR A N   1 
ATOM   923  C  CA  . TYR A 1 114 ? 10.412  -12.943 17.923  1.00 10.70 ? 114 TYR A CA  1 
ATOM   924  C  C   . TYR A 1 114 ? 11.096  -12.853 16.562  1.00 11.54 ? 114 TYR A C   1 
ATOM   925  O  O   . TYR A 1 114 ? 12.296  -12.626 16.493  1.00 12.57 ? 114 TYR A O   1 
ATOM   926  C  CB  . TYR A 1 114 ? 9.311   -11.871 18.094  1.00 10.75 ? 114 TYR A CB  1 
ATOM   927  C  CG  . TYR A 1 114 ? 8.401   -12.102 19.276  1.00 11.55 ? 114 TYR A CG  1 
ATOM   928  C  CD1 . TYR A 1 114 ? 8.712   -11.634 20.541  1.00 12.62 ? 114 TYR A CD1 1 
ATOM   929  C  CD2 . TYR A 1 114 ? 7.188   -12.744 19.096  1.00 13.29 ? 114 TYR A CD2 1 
ATOM   930  C  CE1 . TYR A 1 114 ? 7.851   -11.831 21.608  1.00 14.15 ? 114 TYR A CE1 1 
ATOM   931  C  CE2 . TYR A 1 114 ? 6.317   -12.949 20.149  1.00 13.73 ? 114 TYR A CE2 1 
ATOM   932  C  CZ  . TYR A 1 114 ? 6.652   -12.491 21.408  1.00 14.86 ? 114 TYR A CZ  1 
ATOM   933  O  OH  . TYR A 1 114 ? 5.785   -12.694 22.437  1.00 20.70 ? 114 TYR A OH  1 
ATOM   934  N  N   . ALA A 1 115 ? 10.318  -13.109 15.492  1.00 11.55 ? 115 ALA A N   1 
ATOM   935  C  CA  . ALA A 1 115 ? 10.861  -13.114 14.137  1.00 11.83 ? 115 ALA A CA  1 
ATOM   936  C  C   . ALA A 1 115 ? 11.256  -11.729 13.644  1.00 12.52 ? 115 ALA A C   1 
ATOM   937  O  O   . ALA A 1 115 ? 12.102  -11.594 12.757  1.00 12.57 ? 115 ALA A O   1 
ATOM   938  C  CB  . ALA A 1 115 ? 9.885   -13.761 13.199  1.00 13.03 ? 115 ALA A CB  1 
ATOM   939  N  N   . ALA A 1 116 ? 10.591  -10.705 14.209  1.00 11.72 ? 116 ALA A N   1 
ATOM   940  C  CA  . ALA A 1 116 ? 10.868  -9.359  13.744  1.00 10.18 ? 116 ALA A CA  1 
ATOM   941  C  C   . ALA A 1 116 ? 10.327  -8.397  14.789  1.00 9.70  ? 116 ALA A C   1 
ATOM   942  O  O   . ALA A 1 116 ? 9.617   -8.815  15.715  1.00 10.11 ? 116 ALA A O   1 
ATOM   943  C  CB  . ALA A 1 116 ? 10.300  -9.110  12.337  1.00 10.65 ? 116 ALA A CB  1 
ATOM   944  N  N   . GLU A 1 117 ? 10.649  -7.109  14.639  1.00 9.96  ? 117 GLU A N   1 
ATOM   945  C  CA  . GLU A 1 117 ? 10.140  -6.084  15.543  1.00 9.82  ? 117 GLU A CA  1 
ATOM   946  C  C   . GLU A 1 117 ? 9.938   -4.829  14.713  1.00 9.68  ? 117 GLU A C   1 
ATOM   947  O  O   . GLU A 1 117 ? 10.826  -4.427  13.938  1.00 11.33 ? 117 GLU A O   1 
ATOM   948  C  CB  . GLU A 1 117 ? 11.067  -5.839  16.733  1.00 10.17 ? 117 GLU A CB  1 
ATOM   949  C  CG  . GLU A 1 117 ? 10.466  -4.953  17.834  1.00 10.37 ? 117 GLU A CG  1 
ATOM   950  C  CD  . GLU A 1 117 ? 11.387  -4.932  19.060  1.00 10.80 ? 117 GLU A CD  1 
ATOM   951  O  OE1 . GLU A 1 117 ? 12.091  -5.958  19.331  1.00 10.33 ? 117 GLU A OE1 1 
ATOM   952  O  OE2 . GLU A 1 117 ? 11.422  -3.873  19.759  1.00 10.58 ? 117 GLU A OE2 1 
ATOM   953  N  N   . LEU A 1 118 ? 8.742   -4.298  14.869  1.00 9.98  ? 118 LEU A N   1 
ATOM   954  C  CA  . LEU A 1 118 ? 8.310   -3.052  14.237  1.00 9.50  ? 118 LEU A CA  1 
ATOM   955  C  C   . LEU A 1 118 ? 8.504   -1.913  15.231  1.00 9.39  ? 118 LEU A C   1 
ATOM   956  O  O   . LEU A 1 118 ? 8.052   -2.007  16.361  1.00 10.28 ? 118 LEU A O   1 
ATOM   957  C  CB  . LEU A 1 118 ? 6.817   -3.178  13.858  1.00 9.86  ? 118 LEU A CB  1 
ATOM   958  C  CG  . LEU A 1 118 ? 6.016   -1.900  13.552  1.00 10.14 ? 118 LEU A CG  1 
ATOM   959  C  CD1 . LEU A 1 118 ? 6.572   -1.188  12.327  1.00 11.00 ? 118 LEU A CD1 1 
ATOM   960  C  CD2 . LEU A 1 118 ? 4.549   -2.306  13.313  1.00 11.56 ? 118 LEU A CD2 1 
ATOM   961  N  N   . HIS A 1 119 ? 9.101   -0.809  14.760  1.00 8.67  ? 119 HIS A N   1 
ATOM   962  C  CA  . HIS A 1 119 ? 9.335   0.381   15.572  1.00 9.16  ? 119 HIS A CA  1 
ATOM   963  C  C   . HIS A 1 119 ? 8.660   1.535   14.881  1.00 9.19  ? 119 HIS A C   1 
ATOM   964  O  O   . HIS A 1 119 ? 8.997   1.828   13.736  1.00 10.20 ? 119 HIS A O   1 
ATOM   965  C  CB  . HIS A 1 119 ? 10.849  0.630   15.663  1.00 8.74  ? 119 HIS A CB  1 
ATOM   966  C  CG  . HIS A 1 119 ? 11.486  -0.397  16.539  1.00 8.87  ? 119 HIS A CG  1 
ATOM   967  N  ND1 . HIS A 1 119 ? 12.824  -0.688  16.493  1.00 9.65  ? 119 HIS A ND1 1 
ATOM   968  C  CD2 . HIS A 1 119 ? 10.951  -1.155  17.518  1.00 9.00  ? 119 HIS A CD2 1 
ATOM   969  C  CE1 . HIS A 1 119 ? 13.122  -1.591  17.433  1.00 9.03  ? 119 HIS A CE1 1 
ATOM   970  N  NE2 . HIS A 1 119 ? 11.962  -1.941  18.007  1.00 8.62  ? 119 HIS A NE2 1 
ATOM   971  N  N   . LEU A 1 120 ? 7.684   2.167   15.580  1.00 9.20  ? 120 LEU A N   1 
ATOM   972  C  CA  . LEU A 1 120 ? 7.110   3.418   15.111  1.00 9.01  ? 120 LEU A CA  1 
ATOM   973  C  C   . LEU A 1 120 ? 7.725   4.577   15.902  1.00 9.16  ? 120 LEU A C   1 
ATOM   974  O  O   . LEU A 1 120 ? 7.607   4.612   17.131  1.00 8.57  ? 120 LEU A O   1 
ATOM   975  C  CB  . LEU A 1 120 ? 5.592   3.341   15.232  1.00 10.05 ? 120 LEU A CB  1 
ATOM   976  C  CG  . LEU A 1 120 ? 4.939   2.265   14.364  1.00 10.94 ? 120 LEU A CG  1 
ATOM   977  C  CD1 . LEU A 1 120 ? 4.274   1.269   15.270  1.00 13.78 ? 120 LEU A CD1 1 
ATOM   978  C  CD2 . LEU A 1 120 ? 3.908   2.917   13.443  1.00 12.94 ? 120 LEU A CD2 1 
ATOM   979  N  N   . VAL A 1 121 ? 8.478   5.417   15.189  1.00 10.90 ? 121 VAL A N   1 
ATOM   980  C  CA  . VAL A 1 121 ? 9.332   6.424   15.819  1.00 10.44 ? 121 VAL A CA  1 
ATOM   981  C  C   . VAL A 1 121 ? 8.591   7.741   15.823  1.00 11.40 ? 121 VAL A C   1 
ATOM   982  O  O   . VAL A 1 121 ? 8.214   8.228   14.745  1.00 11.39 ? 121 VAL A O   1 
ATOM   983  C  CB  . VAL A 1 121 ? 10.665  6.523   15.049  1.00 10.80 ? 121 VAL A CB  1 
ATOM   984  C  CG1 . VAL A 1 121 ? 11.578  7.563   15.714  1.00 11.67 ? 121 VAL A CG1 1 
ATOM   985  C  CG2 . VAL A 1 121 ? 11.328  5.155   14.881  1.00 10.68 ? 121 VAL A CG2 1 
ATOM   986  N  N   . HIS A 1 122 ? 8.476   8.337   17.017  1.00 9.36  ? 122 HIS A N   1 
ATOM   987  C  CA  . HIS A 1 122 ? 7.815   9.615   17.211  1.00 10.82 ? 122 HIS A CA  1 
ATOM   988  C  C   . HIS A 1 122 ? 8.740   10.571  17.941  1.00 10.24 ? 122 HIS A C   1 
ATOM   989  O  O   . HIS A 1 122 ? 9.459   10.193  18.859  1.00 10.97 ? 122 HIS A O   1 
ATOM   990  C  CB  . HIS A 1 122 ? 6.517   9.464   18.067  1.00 11.26 ? 122 HIS A CB  1 
ATOM   991  C  CG  . HIS A 1 122 ? 5.641   8.334   17.686  1.00 10.22 ? 122 HIS A CG  1 
ATOM   992  N  ND1 . HIS A 1 122 ? 5.972   7.000   17.977  1.00 10.55 ? 122 HIS A ND1 1 
ATOM   993  C  CD2 . HIS A 1 122 ? 4.423   8.315   17.075  1.00 11.46 ? 122 HIS A CD2 1 
ATOM   994  C  CE1 . HIS A 1 122 ? 4.983   6.213   17.544  1.00 11.64 ? 122 HIS A CE1 1 
ATOM   995  N  NE2 . HIS A 1 122 ? 4.019   7.005   16.977  1.00 12.66 ? 122 HIS A NE2 1 
ATOM   996  N  N   . TRP A 1 123 ? 8.585   11.867  17.622  1.00 10.54 ? 123 TRP A N   1 
ATOM   997  C  CA  . TRP A 1 123 ? 9.394   12.874  18.312  1.00 11.35 ? 123 TRP A CA  1 
ATOM   998  C  C   . TRP A 1 123 ? 8.520   13.834  19.101  1.00 11.58 ? 123 TRP A C   1 
ATOM   999  O  O   . TRP A 1 123 ? 7.433   14.230  18.668  1.00 12.12 ? 123 TRP A O   1 
ATOM   1000 C  CB  . TRP A 1 123 ? 10.349  13.603  17.345  1.00 13.24 ? 123 TRP A CB  1 
ATOM   1001 C  CG  . TRP A 1 123 ? 9.683   14.255  16.157  1.00 12.92 ? 123 TRP A CG  1 
ATOM   1002 C  CD1 . TRP A 1 123 ? 9.444   13.664  14.942  1.00 12.82 ? 123 TRP A CD1 1 
ATOM   1003 C  CD2 . TRP A 1 123 ? 9.201   15.607  16.007  1.00 13.95 ? 123 TRP A CD2 1 
ATOM   1004 N  NE1 . TRP A 1 123 ? 8.842   14.520  14.079  1.00 15.08 ? 123 TRP A NE1 1 
ATOM   1005 C  CE2 . TRP A 1 123 ? 8.682   15.734  14.697  1.00 15.78 ? 123 TRP A CE2 1 
ATOM   1006 C  CE3 . TRP A 1 123 ? 9.197   16.729  16.845  1.00 14.75 ? 123 TRP A CE3 1 
ATOM   1007 C  CZ2 . TRP A 1 123 ? 8.088   16.908  14.225  1.00 17.39 ? 123 TRP A CZ2 1 
ATOM   1008 C  CZ3 . TRP A 1 123 ? 8.623   17.895  16.371  1.00 16.69 ? 123 TRP A CZ3 1 
ATOM   1009 C  CH2 . TRP A 1 123 ? 8.119   18.001  15.073  1.00 18.35 ? 123 TRP A CH2 1 
ATOM   1010 N  N   . ASN A 1 124 ? 9.113   14.323  20.186  1.00 11.35 ? 124 ASN A N   1 
ATOM   1011 C  CA  . ASN A 1 124 ? 8.477   15.217  21.150  1.00 12.78 ? 124 ASN A CA  1 
ATOM   1012 C  C   . ASN A 1 124 ? 8.307   16.610  20.539  1.00 13.11 ? 124 ASN A C   1 
ATOM   1013 O  O   . ASN A 1 124 ? 9.303   17.279  20.235  1.00 12.93 ? 124 ASN A O   1 
ATOM   1014 C  CB  . ASN A 1 124 ? 9.329   15.211  22.408  1.00 12.66 ? 124 ASN A CB  1 
ATOM   1015 C  CG  . ASN A 1 124 ? 8.651   15.843  23.613  1.00 14.32 ? 124 ASN A CG  1 
ATOM   1016 O  OD1 . ASN A 1 124 ? 7.806   16.720  23.451  1.00 15.38 ? 124 ASN A OD1 1 
ATOM   1017 N  ND2 . ASN A 1 124 ? 9.004   15.392  24.820  1.00 14.97 ? 124 ASN A ND2 1 
ATOM   1018 N  N   . THR A 1 125 ? 7.045   17.083  20.390  1.00 14.54 ? 125 THR A N   1 
ATOM   1019 C  CA  . THR A 1 125 ? 6.819   18.302  19.595  1.00 15.04 ? 125 THR A CA  1 
ATOM   1020 C  C   . THR A 1 125 ? 7.282   19.502  20.435  1.00 16.61 ? 125 THR A C   1 
ATOM   1021 O  O   . THR A 1 125 ? 7.485   20.576  19.801  1.00 16.58 ? 125 THR A O   1 
ATOM   1022 C  CB  . THR A 1 125 ? 5.336   18.425  19.209  1.00 19.26 ? 125 THR A CB  1 
ATOM   1023 O  OG1 . THR A 1 125 ? 4.561   18.497  20.404  1.00 21.92 ? 125 THR A OG1 1 
ATOM   1024 C  CG2 . THR A 1 125 ? 4.879   17.288  18.314  1.00 21.31 ? 125 THR A CG2 1 
ATOM   1025 N  N   . LYS A 1 126 ? 7.600   19.335  21.741  1.00 14.81 ? 126 LYS A N   1 
ATOM   1026 C  CA  . LYS A 1 126 ? 8.166   20.494  22.490  1.00 15.05 ? 126 LYS A CA  1 
ATOM   1027 C  C   . LYS A 1 126 ? 9.505   20.926  21.885  1.00 15.30 ? 126 LYS A C   1 
ATOM   1028 O  O   . LYS A 1 126 ? 9.956   22.054  22.125  1.00 16.70 ? 126 LYS A O   1 
ATOM   1029 C  CB  . LYS A 1 126 ? 8.299   20.215  23.989  1.00 17.29 ? 126 LYS A CB  1 
ATOM   1030 C  CG  . LYS A 1 126 ? 9.474   19.363  24.433  1.00 20.29 ? 126 LYS A CG  1 
ATOM   1031 C  CD  . LYS A 1 126 ? 9.418   18.896  25.915  1.00 22.43 ? 126 LYS A CD  1 
ATOM   1032 C  CE  . LYS A 1 126 ? 9.882   19.978  26.863  1.00 27.16 ? 126 LYS A CE  1 
ATOM   1033 N  NZ  . LYS A 1 126 ? 9.618   19.611  28.283  1.00 28.27 ? 126 LYS A NZ  1 
ATOM   1034 N  N   . TYR A 1 127 ? 10.162  20.062  21.098  1.00 14.16 ? 127 TYR A N   1 
ATOM   1035 C  CA  . TYR A 1 127 ? 11.505  20.344  20.579  1.00 14.48 ? 127 TYR A CA  1 
ATOM   1036 C  C   . TYR A 1 127 ? 11.491  20.798  19.121  1.00 15.22 ? 127 TYR A C   1 
ATOM   1037 O  O   . TYR A 1 127 ? 12.567  21.071  18.599  1.00 15.67 ? 127 TYR A O   1 
ATOM   1038 C  CB  . TYR A 1 127 ? 12.490  19.177  20.767  1.00 14.82 ? 127 TYR A CB  1 
ATOM   1039 C  CG  . TYR A 1 127 ? 12.649  18.841  22.214  1.00 16.65 ? 127 TYR A CG  1 
ATOM   1040 C  CD1 . TYR A 1 127 ? 13.075  19.819  23.117  1.00 17.94 ? 127 TYR A CD1 1 
ATOM   1041 C  CD2 . TYR A 1 127 ? 12.409  17.565  22.700  1.00 15.47 ? 127 TYR A CD2 1 
ATOM   1042 C  CE1 . TYR A 1 127 ? 13.230  19.519  24.463  1.00 18.97 ? 127 TYR A CE1 1 
ATOM   1043 C  CE2 . TYR A 1 127 ? 12.543  17.255  24.037  1.00 16.14 ? 127 TYR A CE2 1 
ATOM   1044 C  CZ  . TYR A 1 127 ? 12.942  18.258  24.928  1.00 18.35 ? 127 TYR A CZ  1 
ATOM   1045 O  OH  . TYR A 1 127 ? 13.118  17.964  26.249  1.00 18.34 ? 127 TYR A OH  1 
ATOM   1046 N  N   . GLY A 1 128 ? 10.298  20.940  18.528  1.00 14.52 ? 128 GLY A N   1 
ATOM   1047 C  CA  . GLY A 1 128 ? 10.153  21.686  17.276  1.00 15.16 ? 128 GLY A CA  1 
ATOM   1048 C  C   . GLY A 1 128 ? 10.420  20.854  16.025  1.00 15.69 ? 128 GLY A C   1 
ATOM   1049 O  O   . GLY A 1 128 ? 9.718   21.003  15.033  1.00 17.87 ? 128 GLY A O   1 
ATOM   1050 N  N   . ASP A 1 129 ? 11.471  20.018  16.060  1.00 15.88 ? 129 ASP A N   1 
ATOM   1051 C  CA  . ASP A 1 129 ? 11.592  19.053  14.980  1.00 17.30 ? 129 ASP A CA  1 
ATOM   1052 C  C   . ASP A 1 129 ? 12.402  17.863  15.457  1.00 17.95 ? 129 ASP A C   1 
ATOM   1053 O  O   . ASP A 1 129 ? 12.900  17.834  16.586  1.00 17.61 ? 129 ASP A O   1 
ATOM   1054 C  CB  . ASP A 1 129 ? 12.202  19.637  13.711  1.00 21.12 ? 129 ASP A CB  1 
ATOM   1055 C  CG  . ASP A 1 129 ? 13.609  20.154  13.884  1.00 20.76 ? 129 ASP A CG  1 
ATOM   1056 O  OD1 . ASP A 1 129 ? 14.280  19.837  14.888  1.00 22.52 ? 129 ASP A OD1 1 
ATOM   1057 O  OD2 . ASP A 1 129 ? 14.083  20.823  12.942  1.00 24.73 ? 129 ASP A OD2 1 
ATOM   1058 N  N   . TYR A 1 130 ? 12.474  16.870  14.559  1.00 16.48 ? 130 TYR A N   1 
ATOM   1059 C  CA  . TYR A 1 130 ? 13.114  15.613  14.893  1.00 17.08 ? 130 TYR A CA  1 
ATOM   1060 C  C   . TYR A 1 130 ? 14.597  15.818  15.210  1.00 16.78 ? 130 TYR A C   1 
ATOM   1061 O  O   . TYR A 1 130 ? 15.118  15.262  16.186  1.00 15.04 ? 130 TYR A O   1 
ATOM   1062 C  CB  . TYR A 1 130 ? 12.898  14.604  13.761  1.00 17.30 ? 130 TYR A CB  1 
ATOM   1063 C  CG  . TYR A 1 130 ? 13.770  13.381  13.837  1.00 18.58 ? 130 TYR A CG  1 
ATOM   1064 C  CD1 . TYR A 1 130 ? 13.424  12.289  14.614  1.00 18.66 ? 130 TYR A CD1 1 
ATOM   1065 C  CD2 . TYR A 1 130 ? 14.977  13.355  13.166  1.00 20.44 ? 130 TYR A CD2 1 
ATOM   1066 C  CE1 . TYR A 1 130 ? 14.272  11.197  14.734  1.00 19.39 ? 130 TYR A CE1 1 
ATOM   1067 C  CE2 . TYR A 1 130 ? 15.827  12.262  13.255  1.00 22.17 ? 130 TYR A CE2 1 
ATOM   1068 C  CZ  . TYR A 1 130 ? 15.460  11.168  14.013  1.00 20.51 ? 130 TYR A CZ  1 
ATOM   1069 O  OH  . TYR A 1 130 ? 16.356  10.124  14.050  1.00 26.82 ? 130 TYR A OH  1 
ATOM   1070 N  N   . GLY A 1 131 ? 15.312  16.577  14.356  1.00 15.87 ? 131 GLY A N   1 
ATOM   1071 C  CA  . GLY A 1 131 ? 16.736  16.699  14.563  1.00 18.91 ? 131 GLY A CA  1 
ATOM   1072 C  C   . GLY A 1 131 ? 17.115  17.277  15.919  1.00 16.74 ? 131 GLY A C   1 
ATOM   1073 O  O   . GLY A 1 131 ? 18.143  16.902  16.473  1.00 20.10 ? 131 GLY A O   1 
ATOM   1074 N  N   A LYS A 1 132 ? 16.292  18.196  16.442  0.50 16.23 ? 132 LYS A N   1 
ATOM   1075 N  N   B LYS A 1 132 ? 16.279  18.166  16.471  0.50 16.23 ? 132 LYS A N   1 
ATOM   1076 C  CA  A LYS A 1 132 ? 16.519  18.701  17.792  0.50 17.13 ? 132 LYS A CA  1 
ATOM   1077 C  CA  B LYS A 1 132 ? 16.544  18.699  17.806  0.50 17.09 ? 132 LYS A CA  1 
ATOM   1078 C  C   A LYS A 1 132 ? 16.137  17.615  18.809  0.50 16.93 ? 132 LYS A C   1 
ATOM   1079 C  C   B LYS A 1 132 ? 16.063  17.729  18.897  0.50 17.11 ? 132 LYS A C   1 
ATOM   1080 O  O   A LYS A 1 132 ? 16.933  17.270  19.669  0.50 16.91 ? 132 LYS A O   1 
ATOM   1081 O  O   B LYS A 1 132 ? 16.691  17.617  19.938  0.50 18.21 ? 132 LYS A O   1 
ATOM   1082 C  CB  A LYS A 1 132 ? 15.725  19.988  18.053  0.50 18.44 ? 132 LYS A CB  1 
ATOM   1083 C  CB  B LYS A 1 132 ? 15.859  20.055  18.000  0.50 18.20 ? 132 LYS A CB  1 
ATOM   1084 C  CG  A LYS A 1 132 ? 16.380  21.294  17.608  0.50 20.23 ? 132 LYS A CG  1 
ATOM   1085 C  CG  B LYS A 1 132 ? 15.759  20.532  19.443  0.50 18.79 ? 132 LYS A CG  1 
ATOM   1086 C  CD  A LYS A 1 132 ? 17.816  21.413  18.059  0.50 21.47 ? 132 LYS A CD  1 
ATOM   1087 C  CD  B LYS A 1 132 ? 16.775  21.585  19.863  0.50 23.04 ? 132 LYS A CD  1 
ATOM   1088 C  CE  A LYS A 1 132 ? 18.146  22.750  18.691  0.50 22.14 ? 132 LYS A CE  1 
ATOM   1089 C  CE  B LYS A 1 132 ? 16.625  22.067  21.296  0.50 22.68 ? 132 LYS A CE  1 
ATOM   1090 N  NZ  A LYS A 1 132 ? 17.045  23.705  18.445  0.50 22.69 ? 132 LYS A NZ  1 
ATOM   1091 N  NZ  B LYS A 1 132 ? 15.904  23.360  21.409  0.50 24.11 ? 132 LYS A NZ  1 
ATOM   1092 N  N   . ALA A 1 133 ? 14.928  17.062  18.665  1.00 14.58 ? 133 ALA A N   1 
ATOM   1093 C  CA  . ALA A 1 133 ? 14.388  16.095  19.607  1.00 13.44 ? 133 ALA A CA  1 
ATOM   1094 C  C   . ALA A 1 133 ? 15.382  14.952  19.825  1.00 13.42 ? 133 ALA A C   1 
ATOM   1095 O  O   . ALA A 1 133 ? 15.532  14.516  20.960  1.00 15.03 ? 133 ALA A O   1 
ATOM   1096 C  CB  . ALA A 1 133 ? 13.047  15.543  19.103  1.00 13.56 ? 133 ALA A CB  1 
ATOM   1097 N  N   . VAL A 1 134 ? 16.028  14.449  18.774  1.00 15.11 ? 134 VAL A N   1 
ATOM   1098 C  CA  . VAL A 1 134 ? 16.877  13.262  18.923  1.00 17.65 ? 134 VAL A CA  1 
ATOM   1099 C  C   . VAL A 1 134 ? 18.116  13.517  19.763  1.00 18.60 ? 134 VAL A C   1 
ATOM   1100 O  O   . VAL A 1 134 ? 18.795  12.531  20.072  1.00 22.35 ? 134 VAL A O   1 
ATOM   1101 C  CB  . VAL A 1 134 ? 17.280  12.584  17.597  1.00 18.15 ? 134 VAL A CB  1 
ATOM   1102 C  CG1 . VAL A 1 134 ? 16.073  12.188  16.817  1.00 25.21 ? 134 VAL A CG1 1 
ATOM   1103 C  CG2 . VAL A 1 134 ? 18.204  13.460  16.751  1.00 19.08 ? 134 VAL A CG2 1 
ATOM   1104 N  N   . GLN A 1 135 ? 18.339  14.787  20.157  1.00 18.82 ? 135 GLN A N   1 
ATOM   1105 C  CA  . GLN A 1 135 ? 19.461  15.205  20.976  1.00 23.38 ? 135 GLN A CA  1 
ATOM   1106 C  C   . GLN A 1 135 ? 19.046  15.278  22.449  1.00 21.21 ? 135 GLN A C   1 
ATOM   1107 O  O   . GLN A 1 135 ? 19.836  15.612  23.320  1.00 27.17 ? 135 GLN A O   1 
ATOM   1108 C  CB  . GLN A 1 135 ? 20.008  16.551  20.480  1.00 26.44 ? 135 GLN A CB  1 
ATOM   1109 C  CG  . GLN A 1 135 ? 20.498  16.484  19.036  1.00 28.83 ? 135 GLN A CG  1 
ATOM   1110 C  CD  . GLN A 1 135 ? 20.876  17.860  18.537  1.00 32.11 ? 135 GLN A CD  1 
ATOM   1111 O  OE1 . GLN A 1 135 ? 20.529  18.252  17.425  1.00 36.35 ? 135 GLN A OE1 1 
ATOM   1112 N  NE2 . GLN A 1 135 ? 21.551  18.631  19.382  1.00 35.30 ? 135 GLN A NE2 1 
ATOM   1113 N  N   . GLN A 1 136 ? 17.766  15.030  22.748  1.00 18.50 ? 136 GLN A N   1 
ATOM   1114 C  CA  . GLN A 1 136 ? 17.291  15.382  24.080  1.00 16.73 ? 136 GLN A CA  1 
ATOM   1115 C  C   . GLN A 1 136 ? 16.930  14.123  24.846  1.00 16.19 ? 136 GLN A C   1 
ATOM   1116 O  O   . GLN A 1 136 ? 16.542  13.116  24.270  1.00 14.21 ? 136 GLN A O   1 
ATOM   1117 C  CB  . GLN A 1 136 ? 15.964  16.147  24.046  1.00 16.59 ? 136 GLN A CB  1 
ATOM   1118 C  CG  . GLN A 1 136 ? 15.995  17.431  23.203  1.00 20.68 ? 136 GLN A CG  1 
ATOM   1119 C  CD  . GLN A 1 136 ? 17.092  18.366  23.655  1.00 22.73 ? 136 GLN A CD  1 
ATOM   1120 O  OE1 . GLN A 1 136 ? 17.281  18.548  24.865  1.00 22.84 ? 136 GLN A OE1 1 
ATOM   1121 N  NE2 . GLN A 1 136 ? 17.813  18.953  22.698  1.00 28.39 ? 136 GLN A NE2 1 
ATOM   1122 N  N   . PRO A 1 137 ? 16.982  14.083  26.185  1.00 16.44 ? 137 PRO A N   1 
ATOM   1123 C  CA  . PRO A 1 137 ? 16.755  12.831  26.903  1.00 15.38 ? 137 PRO A CA  1 
ATOM   1124 C  C   . PRO A 1 137 ? 15.357  12.237  26.800  1.00 14.20 ? 137 PRO A C   1 
ATOM   1125 O  O   . PRO A 1 137 ? 15.204  11.023  26.932  1.00 15.25 ? 137 PRO A O   1 
ATOM   1126 C  CB  . PRO A 1 137 ? 17.098  13.180  28.362  1.00 17.23 ? 137 PRO A CB  1 
ATOM   1127 C  CG  . PRO A 1 137 ? 16.923  14.661  28.425  1.00 22.59 ? 137 PRO A CG  1 
ATOM   1128 C  CD  . PRO A 1 137 ? 17.317  15.209  27.069  1.00 19.06 ? 137 PRO A CD  1 
ATOM   1129 N  N   . ASP A 1 138 ? 14.353  13.108  26.538  1.00 12.36 ? 138 ASP A N   1 
ATOM   1130 C  CA  . ASP A 1 138 ? 12.967  12.690  26.302  1.00 13.72 ? 138 ASP A CA  1 
ATOM   1131 C  C   . ASP A 1 138 ? 12.514  13.104  24.906  1.00 12.62 ? 138 ASP A C   1 
ATOM   1132 O  O   . ASP A 1 138 ? 11.377  13.486  24.671  1.00 14.70 ? 138 ASP A O   1 
ATOM   1133 C  CB  . ASP A 1 138 ? 12.030  13.346  27.330  1.00 15.53 ? 138 ASP A CB  1 
ATOM   1134 C  CG  . ASP A 1 138 ? 12.079  14.854  27.316  1.00 15.44 ? 138 ASP A CG  1 
ATOM   1135 O  OD1 . ASP A 1 138 ? 13.039  15.438  26.746  1.00 16.11 ? 138 ASP A OD1 1 
ATOM   1136 O  OD2 . ASP A 1 138 ? 11.171  15.422  27.974  1.00 18.19 ? 138 ASP A OD2 1 
ATOM   1137 N  N   . GLY A 1 139 ? 13.424  12.964  23.934  1.00 11.98 ? 139 GLY A N   1 
ATOM   1138 C  CA  . GLY A 1 139 ? 13.168  13.444  22.574  1.00 12.05 ? 139 GLY A CA  1 
ATOM   1139 C  C   . GLY A 1 139 ? 12.246  12.521  21.761  1.00 10.30 ? 139 GLY A C   1 
ATOM   1140 O  O   . GLY A 1 139 ? 11.546  13.016  20.890  1.00 10.62 ? 139 GLY A O   1 
ATOM   1141 N  N   . LEU A 1 140 ? 12.403  11.201  21.965  1.00 10.08 ? 140 LEU A N   1 
ATOM   1142 C  CA  . LEU A 1 140 ? 11.708  10.250  21.127  1.00 10.42 ? 140 LEU A CA  1 
ATOM   1143 C  C   . LEU A 1 140 ? 10.831  9.364   21.978  1.00 11.54 ? 140 LEU A C   1 
ATOM   1144 O  O   . LEU A 1 140 ? 11.130  9.086   23.133  1.00 11.15 ? 140 LEU A O   1 
ATOM   1145 C  CB  . LEU A 1 140 ? 12.685  9.385   20.316  1.00 11.62 ? 140 LEU A CB  1 
ATOM   1146 C  CG  . LEU A 1 140 ? 13.578  10.076  19.291  1.00 13.29 ? 140 LEU A CG  1 
ATOM   1147 C  CD1 . LEU A 1 140 ? 14.248  8.985   18.457  1.00 14.26 ? 140 LEU A CD1 1 
ATOM   1148 C  CD2 . LEU A 1 140 ? 12.881  11.106  18.369  1.00 13.97 ? 140 LEU A CD2 1 
ATOM   1149 N  N   . ALA A 1 141 ? 9.762   8.885   21.315  1.00 9.84  ? 141 ALA A N   1 
ATOM   1150 C  CA  . ALA A 1 141 ? 8.993   7.794   21.864  1.00 9.32  ? 141 ALA A CA  1 
ATOM   1151 C  C   . ALA A 1 141 ? 8.893   6.773   20.759  1.00 9.30  ? 141 ALA A C   1 
ATOM   1152 O  O   . ALA A 1 141 ? 8.444   7.109   19.671  1.00 9.77  ? 141 ALA A O   1 
ATOM   1153 C  CB  . ALA A 1 141 ? 7.639   8.248   22.383  1.00 10.69 ? 141 ALA A CB  1 
ATOM   1154 N  N   . VAL A 1 142 ? 9.362   5.558   21.050  1.00 8.88  ? 142 VAL A N   1 
ATOM   1155 C  CA  . VAL A 1 142 ? 9.296   4.522   20.037  1.00 8.76  ? 142 VAL A CA  1 
ATOM   1156 C  C   . VAL A 1 142 ? 8.315   3.458   20.508  1.00 8.77  ? 142 VAL A C   1 
ATOM   1157 O  O   . VAL A 1 142 ? 8.438   2.894   21.609  1.00 9.72  ? 142 VAL A O   1 
ATOM   1158 C  CB  . VAL A 1 142 ? 10.659  3.905   19.664  1.00 8.91  ? 142 VAL A CB  1 
ATOM   1159 C  CG1 . VAL A 1 142 ? 10.472  2.845   18.558  1.00 9.93  ? 142 VAL A CG1 1 
ATOM   1160 C  CG2 . VAL A 1 142 ? 11.614  4.987   19.211  1.00 10.08 ? 142 VAL A CG2 1 
ATOM   1161 N  N   . LEU A 1 143 ? 7.304   3.200   19.657  1.00 8.87  ? 143 LEU A N   1 
ATOM   1162 C  CA  . LEU A 1 143 ? 6.334   2.166   19.898  1.00 9.70  ? 143 LEU A CA  1 
ATOM   1163 C  C   . LEU A 1 143 ? 6.859   0.898   19.238  1.00 9.68  ? 143 LEU A C   1 
ATOM   1164 O  O   . LEU A 1 143 ? 7.007   0.874   18.038  1.00 10.98 ? 143 LEU A O   1 
ATOM   1165 C  CB  . LEU A 1 143 ? 4.975   2.597   19.343  1.00 11.45 ? 143 LEU A CB  1 
ATOM   1166 C  CG  . LEU A 1 143 ? 3.794   1.651   19.539  1.00 12.19 ? 143 LEU A CG  1 
ATOM   1167 C  CD1 . LEU A 1 143 ? 3.567   1.385   21.008  1.00 13.39 ? 143 LEU A CD1 1 
ATOM   1168 C  CD2 . LEU A 1 143 ? 2.534   2.293   18.915  1.00 13.69 ? 143 LEU A CD2 1 
ATOM   1169 N  N   . GLY A 1 144 ? 7.073   -0.165  20.031  1.00 9.17  ? 144 GLY A N   1 
ATOM   1170 C  CA  . GLY A 1 144 ? 7.635   -1.413  19.507  1.00 8.58  ? 144 GLY A CA  1 
ATOM   1171 C  C   . GLY A 1 144 ? 6.605   -2.524  19.510  1.00 9.04  ? 144 GLY A C   1 
ATOM   1172 O  O   . GLY A 1 144 ? 5.859   -2.635  20.475  1.00 11.11 ? 144 GLY A O   1 
ATOM   1173 N  N   . ILE A 1 145 ? 6.564   -3.268  18.409  1.00 9.18  ? 145 ILE A N   1 
ATOM   1174 C  CA  . ILE A 1 145 ? 5.546   -4.302  18.214  1.00 9.77  ? 145 ILE A CA  1 
ATOM   1175 C  C   . ILE A 1 145 ? 6.275   -5.534  17.699  1.00 10.24 ? 145 ILE A C   1 
ATOM   1176 O  O   . ILE A 1 145 ? 6.960   -5.503  16.692  1.00 11.03 ? 145 ILE A O   1 
ATOM   1177 C  CB  . ILE A 1 145 ? 4.427   -3.800  17.262  1.00 10.22 ? 145 ILE A CB  1 
ATOM   1178 C  CG1 . ILE A 1 145 ? 3.752   -2.540  17.795  1.00 13.55 ? 145 ILE A CG1 1 
ATOM   1179 C  CG2 . ILE A 1 145 ? 3.416   -4.920  16.985  1.00 11.97 ? 145 ILE A CG2 1 
ATOM   1180 C  CD1 . ILE A 1 145 ? 2.711   -1.908  16.846  1.00 12.68 ? 145 ILE A CD1 1 
ATOM   1181 N  N   . PHE A 1 146 ? 6.108   -6.647  18.401  1.00 10.34 ? 146 PHE A N   1 
ATOM   1182 C  CA  . PHE A 1 146 ? 6.732   -7.894  17.970  1.00 9.36  ? 146 PHE A CA  1 
ATOM   1183 C  C   . PHE A 1 146 ? 5.951   -8.502  16.803  1.00 10.33 ? 146 PHE A C   1 
ATOM   1184 O  O   . PHE A 1 146 ? 4.720   -8.418  16.748  1.00 11.95 ? 146 PHE A O   1 
ATOM   1185 C  CB  . PHE A 1 146 ? 6.732   -8.900  19.124  1.00 9.53  ? 146 PHE A CB  1 
ATOM   1186 C  CG  . PHE A 1 146 ? 7.559   -8.423  20.287  1.00 8.82  ? 146 PHE A CG  1 
ATOM   1187 C  CD1 . PHE A 1 146 ? 8.933   -8.277  20.117  1.00 9.66  ? 146 PHE A CD1 1 
ATOM   1188 C  CD2 . PHE A 1 146 ? 6.987   -8.138  21.518  1.00 10.36 ? 146 PHE A CD2 1 
ATOM   1189 C  CE1 . PHE A 1 146 ? 9.709   -7.848  21.189  1.00 8.86  ? 146 PHE A CE1 1 
ATOM   1190 C  CE2 . PHE A 1 146 ? 7.764   -7.698  22.588  1.00 9.51  ? 146 PHE A CE2 1 
ATOM   1191 C  CZ  . PHE A 1 146 ? 9.147   -7.583  22.427  1.00 9.96  ? 146 PHE A CZ  1 
ATOM   1192 N  N   . LEU A 1 147 ? 6.671   -9.183  15.930  1.00 9.91  ? 147 LEU A N   1 
ATOM   1193 C  CA  . LEU A 1 147 ? 6.052   -9.994  14.881  1.00 9.53  ? 147 LEU A CA  1 
ATOM   1194 C  C   . LEU A 1 147 ? 6.412   -11.455 15.105  1.00 10.67 ? 147 LEU A C   1 
ATOM   1195 O  O   . LEU A 1 147 ? 7.564   -11.831 15.206  1.00 11.13 ? 147 LEU A O   1 
ATOM   1196 C  CB  . LEU A 1 147 ? 6.625   -9.616  13.498  1.00 10.48 ? 147 LEU A CB  1 
ATOM   1197 C  CG  . LEU A 1 147 ? 6.093   -8.350  12.829  1.00 10.13 ? 147 LEU A CG  1 
ATOM   1198 C  CD1 . LEU A 1 147 ? 6.266   -7.098  13.737  1.00 11.77 ? 147 LEU A CD1 1 
ATOM   1199 C  CD2 . LEU A 1 147 ? 6.746   -8.146  11.469  1.00 11.53 ? 147 LEU A CD2 1 
ATOM   1200 N  N   . LYS A 1 148 ? 5.359   -12.278 15.056  1.00 12.09 ? 148 LYS A N   1 
ATOM   1201 C  CA  . LYS A 1 148 ? 5.551   -13.727 15.035  1.00 12.59 ? 148 LYS A CA  1 
ATOM   1202 C  C   . LYS A 1 148 ? 5.074   -14.243 13.690  1.00 13.68 ? 148 LYS A C   1 
ATOM   1203 O  O   . LYS A 1 148 ? 4.225   -13.617 13.049  1.00 13.19 ? 148 LYS A O   1 
ATOM   1204 C  CB  . LYS A 1 148 ? 4.805   -14.403 16.197  1.00 15.64 ? 148 LYS A CB  1 
ATOM   1205 C  CG  . LYS A 1 148 ? 3.290   -14.364 16.130  1.00 18.16 ? 148 LYS A CG  1 
ATOM   1206 C  CD  . LYS A 1 148 ? 2.756   -15.056 17.378  1.00 22.81 ? 148 LYS A CD  1 
ATOM   1207 C  CE  . LYS A 1 148 ? 1.332   -15.535 17.224  1.00 29.61 ? 148 LYS A CE  1 
ATOM   1208 N  NZ  . LYS A 1 148 ? 0.802   -15.927 18.559  1.00 33.66 ? 148 LYS A NZ  1 
ATOM   1209 N  N   . VAL A 1 149 ? 5.553   -15.409 13.280  1.00 12.98 ? 149 VAL A N   1 
ATOM   1210 C  CA  . VAL A 1 149 ? 5.176   -16.015 12.025  1.00 13.54 ? 149 VAL A CA  1 
ATOM   1211 C  C   . VAL A 1 149 ? 3.965   -16.917 12.254  1.00 13.56 ? 149 VAL A C   1 
ATOM   1212 O  O   . VAL A 1 149 ? 3.996   -17.844 13.071  1.00 15.74 ? 149 VAL A O   1 
ATOM   1213 C  CB  . VAL A 1 149 ? 6.358   -16.767 11.400  1.00 13.13 ? 149 VAL A CB  1 
ATOM   1214 C  CG1 . VAL A 1 149 ? 5.982   -17.588 10.172  1.00 14.92 ? 149 VAL A CG1 1 
ATOM   1215 C  CG2 . VAL A 1 149 ? 7.495   -15.832 11.061  1.00 14.22 ? 149 VAL A CG2 1 
ATOM   1216 N  N   . GLY A 1 150 ? 2.956   -16.668 11.440  1.00 13.60 ? 150 GLY A N   1 
ATOM   1217 C  CA  . GLY A 1 150 ? 1.686   -17.401 11.530  1.00 13.52 ? 150 GLY A CA  1 
ATOM   1218 C  C   . GLY A 1 150 ? 0.787   -16.976 10.388  1.00 14.40 ? 150 GLY A C   1 
ATOM   1219 O  O   . GLY A 1 150 ? 1.190   -17.130 9.252   1.00 15.54 ? 150 GLY A O   1 
ATOM   1220 N  N   A SER A 1 151 ? -0.431  -16.476 10.691  0.50 14.98 ? 151 SER A N   1 
ATOM   1221 N  N   B SER A 1 151 ? -0.398  -16.434 10.719  0.50 14.98 ? 151 SER A N   1 
ATOM   1222 C  CA  A SER A 1 151 ? -1.316  -15.938 9.658   0.50 15.63 ? 151 SER A CA  1 
ATOM   1223 C  CA  B SER A 1 151 ? -1.265  -15.837 9.712   0.50 15.46 ? 151 SER A CA  1 
ATOM   1224 C  C   A SER A 1 151 ? -0.770  -14.607 9.139   0.50 15.84 ? 151 SER A C   1 
ATOM   1225 C  C   B SER A 1 151 ? -0.620  -14.596 9.091   0.50 16.02 ? 151 SER A C   1 
ATOM   1226 O  O   A SER A 1 151 ? -0.090  -13.904 9.885   0.50 15.59 ? 151 SER A O   1 
ATOM   1227 O  O   B SER A 1 151 ? 0.264   -13.955 9.671   0.50 14.49 ? 151 SER A O   1 
ATOM   1228 C  CB  A SER A 1 151 ? -2.708  -15.760 10.162  0.50 18.38 ? 151 SER A CB  1 
ATOM   1229 C  CB  B SER A 1 151 ? -2.621  -15.547 10.257  0.50 17.78 ? 151 SER A CB  1 
ATOM   1230 O  OG  A SER A 1 151 ? -2.693  -14.914 11.299  0.50 19.21 ? 151 SER A OG  1 
ATOM   1231 O  OG  B SER A 1 151 ? -3.133  -16.731 10.845  0.50 19.23 ? 151 SER A OG  1 
ATOM   1232 N  N   . ALA A 1 152 ? -1.012  -14.308 7.849   1.00 15.58 ? 152 ALA A N   1 
ATOM   1233 C  CA  . ALA A 1 152 ? -0.596  -13.060 7.207   1.00 15.93 ? 152 ALA A CA  1 
ATOM   1234 C  C   . ALA A 1 152 ? -1.248  -11.874 7.895   1.00 14.07 ? 152 ALA A C   1 
ATOM   1235 O  O   . ALA A 1 152 ? -2.370  -11.948 8.401   1.00 16.57 ? 152 ALA A O   1 
ATOM   1236 C  CB  . ALA A 1 152 ? -0.931  -13.036 5.735   1.00 16.31 ? 152 ALA A CB  1 
ATOM   1237 N  N   . LYS A 1 153 ? -0.532  -10.743 7.838   1.00 16.32 ? 153 LYS A N   1 
ATOM   1238 C  CA  . LYS A 1 153 ? -1.076  -9.498  8.354   1.00 16.72 ? 153 LYS A CA  1 
ATOM   1239 C  C   . LYS A 1 153 ? -1.495  -8.706  7.123   1.00 15.67 ? 153 LYS A C   1 
ATOM   1240 O  O   . LYS A 1 153 ? -0.665  -8.238  6.351   1.00 15.38 ? 153 LYS A O   1 
ATOM   1241 C  CB  . LYS A 1 153 ? 0.003   -8.715  9.121   1.00 16.60 ? 153 LYS A CB  1 
ATOM   1242 C  CG  . LYS A 1 153 ? -0.508  -7.488  9.888   1.00 18.48 ? 153 LYS A CG  1 
ATOM   1243 C  CD  . LYS A 1 153 ? -1.344  -7.904  11.073  1.00 17.10 ? 153 LYS A CD  1 
ATOM   1244 C  CE  . LYS A 1 153 ? -1.737  -6.742  11.981  1.00 20.05 ? 153 LYS A CE  1 
ATOM   1245 N  NZ  . LYS A 1 153 ? -2.768  -7.109  12.973  1.00 22.26 ? 153 LYS A NZ  1 
ATOM   1246 N  N   . PRO A 1 154 ? -2.830  -8.585  6.868   1.00 15.46 ? 154 PRO A N   1 
ATOM   1247 C  CA  . PRO A 1 154 ? -3.260  -7.996  5.587   1.00 18.54 ? 154 PRO A CA  1 
ATOM   1248 C  C   . PRO A 1 154 ? -2.767  -6.572  5.407   1.00 17.34 ? 154 PRO A C   1 
ATOM   1249 O  O   . PRO A 1 154 ? -2.331  -6.220  4.326   1.00 19.75 ? 154 PRO A O   1 
ATOM   1250 C  CB  . PRO A 1 154 ? -4.796  -8.095  5.629   1.00 17.59 ? 154 PRO A CB  1 
ATOM   1251 C  CG  . PRO A 1 154 ? -5.082  -9.142  6.662   1.00 20.58 ? 154 PRO A CG  1 
ATOM   1252 C  CD  . PRO A 1 154 ? -3.934  -9.135  7.656   1.00 17.01 ? 154 PRO A CD  1 
ATOM   1253 N  N   . GLY A 1 155 ? -2.675  -5.839  6.520   1.00 16.54 ? 155 GLY A N   1 
ATOM   1254 C  CA  . GLY A 1 155 ? -2.243  -4.446  6.529   1.00 18.09 ? 155 GLY A CA  1 
ATOM   1255 C  C   . GLY A 1 155 ? -0.756  -4.251  6.235   1.00 18.35 ? 155 GLY A C   1 
ATOM   1256 O  O   . GLY A 1 155 ? -0.312  -3.131  6.013   1.00 22.27 ? 155 GLY A O   1 
ATOM   1257 N  N   . LEU A 1 156 ? 0.029   -5.334  6.250   1.00 15.31 ? 156 LEU A N   1 
ATOM   1258 C  CA  . LEU A 1 156 ? 1.452   -5.284  5.936   1.00 15.16 ? 156 LEU A CA  1 
ATOM   1259 C  C   . LEU A 1 156 ? 1.702   -5.536  4.453   1.00 14.54 ? 156 LEU A C   1 
ATOM   1260 O  O   . LEU A 1 156 ? 2.781   -5.297  3.933   1.00 14.70 ? 156 LEU A O   1 
ATOM   1261 C  CB  . LEU A 1 156 ? 2.184   -6.335  6.791   1.00 15.60 ? 156 LEU A CB  1 
ATOM   1262 C  CG  . LEU A 1 156 ? 3.695   -6.497  6.599   1.00 15.74 ? 156 LEU A CG  1 
ATOM   1263 C  CD1 . LEU A 1 156 ? 4.451   -5.195  6.953   1.00 15.05 ? 156 LEU A CD1 1 
ATOM   1264 C  CD2 . LEU A 1 156 ? 4.248   -7.648  7.431   1.00 14.98 ? 156 LEU A CD2 1 
ATOM   1265 N  N   . GLN A 1 157 ? 0.692   -6.068  3.741   1.00 14.81 ? 157 GLN A N   1 
ATOM   1266 C  CA  . GLN A 1 157 ? 1.012   -6.519  2.397   1.00 16.65 ? 157 GLN A CA  1 
ATOM   1267 C  C   . GLN A 1 157 ? 1.462   -5.423  1.427   1.00 15.10 ? 157 GLN A C   1 
ATOM   1268 O  O   . GLN A 1 157 ? 2.371   -5.651  0.643   1.00 15.35 ? 157 GLN A O   1 
ATOM   1269 C  CB  . GLN A 1 157 ? -0.096  -7.404  1.838   1.00 17.56 ? 157 GLN A CB  1 
ATOM   1270 C  CG  . GLN A 1 157 ? 0.328   -8.100  0.547   1.00 18.98 ? 157 GLN A CG  1 
ATOM   1271 C  CD  . GLN A 1 157 ? 1.382   -9.145  0.791   1.00 18.40 ? 157 GLN A CD  1 
ATOM   1272 O  OE1 . GLN A 1 157 ? 1.431   -9.743  1.889   1.00 18.40 ? 157 GLN A OE1 1 
ATOM   1273 N  NE2 . GLN A 1 157 ? 2.257   -9.365  -0.189  1.00 18.56 ? 157 GLN A NE2 1 
ATOM   1274 N  N   . LYS A 1 158 ? 0.917   -4.217  1.560   1.00 16.88 ? 158 LYS A N   1 
ATOM   1275 C  CA  . LYS A 1 158 ? 1.288   -3.128  0.675   1.00 17.66 ? 158 LYS A CA  1 
ATOM   1276 C  C   . LYS A 1 158 ? 2.778   -2.795  0.839   1.00 17.46 ? 158 LYS A C   1 
ATOM   1277 O  O   . LYS A 1 158 ? 3.434   -2.383  -0.105  1.00 18.96 ? 158 LYS A O   1 
ATOM   1278 C  CB  . LYS A 1 158 ? 0.314   -1.956  0.880   1.00 19.25 ? 158 LYS A CB  1 
ATOM   1279 N  N   . VAL A 1 159 ? 3.298   -2.953  2.070   1.00 17.02 ? 159 VAL A N   1 
ATOM   1280 C  CA  . VAL A 1 159 ? 4.711   -2.765  2.340   1.00 15.63 ? 159 VAL A CA  1 
ATOM   1281 C  C   . VAL A 1 159 ? 5.544   -3.859  1.663   1.00 15.33 ? 159 VAL A C   1 
ATOM   1282 O  O   . VAL A 1 159 ? 6.545   -3.601  0.995   1.00 15.87 ? 159 VAL A O   1 
ATOM   1283 C  CB  . VAL A 1 159 ? 4.959   -2.748  3.864   1.00 16.03 ? 159 VAL A CB  1 
ATOM   1284 C  CG1 . VAL A 1 159 ? 6.469   -2.686  4.164   1.00 15.59 ? 159 VAL A CG1 1 
ATOM   1285 C  CG2 . VAL A 1 159 ? 4.171   -1.610  4.532   1.00 17.56 ? 159 VAL A CG2 1 
ATOM   1286 N  N   . VAL A 1 160 ? 5.161   -5.125  1.912   1.00 16.07 ? 160 VAL A N   1 
ATOM   1287 C  CA  . VAL A 1 160 ? 5.860   -6.275  1.357   1.00 18.09 ? 160 VAL A CA  1 
ATOM   1288 C  C   . VAL A 1 160 ? 5.986   -6.145  -0.169  1.00 16.61 ? 160 VAL A C   1 
ATOM   1289 O  O   . VAL A 1 160 ? 7.047   -6.391  -0.752  1.00 18.71 ? 160 VAL A O   1 
ATOM   1290 C  CB  . VAL A 1 160 ? 5.124   -7.576  1.775   1.00 19.57 ? 160 VAL A CB  1 
ATOM   1291 C  CG1 . VAL A 1 160 ? 5.598   -8.798  0.999   1.00 22.93 ? 160 VAL A CG1 1 
ATOM   1292 C  CG2 . VAL A 1 160 ? 5.173   -7.807  3.279   1.00 21.34 ? 160 VAL A CG2 1 
ATOM   1293 N  N   . ASP A 1 161 ? 4.887   -5.716  -0.801  1.00 19.32 ? 161 ASP A N   1 
ATOM   1294 C  CA  . ASP A 1 161 ? 4.851   -5.781  -2.265  1.00 20.96 ? 161 ASP A CA  1 
ATOM   1295 C  C   . ASP A 1 161 ? 5.709   -4.692  -2.914  1.00 22.46 ? 161 ASP A C   1 
ATOM   1296 O  O   . ASP A 1 161 ? 6.060   -4.771  -4.095  1.00 25.80 ? 161 ASP A O   1 
ATOM   1297 C  CB  . ASP A 1 161 ? 3.399   -5.713  -2.721  1.00 22.65 ? 161 ASP A CB  1 
ATOM   1298 C  CG  . ASP A 1 161 ? 2.698   -7.067  -2.665  1.00 23.22 ? 161 ASP A CG  1 
ATOM   1299 O  OD1 . ASP A 1 161 ? 3.399   -8.140  -2.751  1.00 27.41 ? 161 ASP A OD1 1 
ATOM   1300 O  OD2 . ASP A 1 161 ? 1.475   -7.045  -2.494  1.00 26.76 ? 161 ASP A OD2 1 
ATOM   1301 N  N   . VAL A 1 162 ? 6.092   -3.653  -2.157  1.00 19.38 ? 162 VAL A N   1 
ATOM   1302 C  CA  . VAL A 1 162 ? 6.906   -2.602  -2.748  1.00 20.08 ? 162 VAL A CA  1 
ATOM   1303 C  C   . VAL A 1 162 ? 8.405   -2.882  -2.532  1.00 17.91 ? 162 VAL A C   1 
ATOM   1304 O  O   . VAL A 1 162 ? 9.260   -2.177  -3.051  1.00 18.51 ? 162 VAL A O   1 
ATOM   1305 C  CB  . VAL A 1 162 ? 6.436   -1.237  -2.198  1.00 21.81 ? 162 VAL A CB  1 
ATOM   1306 C  CG1 . VAL A 1 162 ? 6.811   -1.024  -0.742  1.00 22.71 ? 162 VAL A CG1 1 
ATOM   1307 C  CG2 . VAL A 1 162 ? 6.795   -0.020  -3.030  1.00 21.42 ? 162 VAL A CG2 1 
ATOM   1308 N  N   . LEU A 1 163 ? 8.779   -3.896  -1.708  1.00 18.28 ? 163 LEU A N   1 
ATOM   1309 C  CA  . LEU A 1 163 ? 10.179  -4.057  -1.347  1.00 16.01 ? 163 LEU A CA  1 
ATOM   1310 C  C   . LEU A 1 163 ? 11.056  -4.427  -2.534  1.00 18.63 ? 163 LEU A C   1 
ATOM   1311 O  O   . LEU A 1 163 ? 12.231  -4.078  -2.545  1.00 18.96 ? 163 LEU A O   1 
ATOM   1312 C  CB  . LEU A 1 163 ? 10.391  -5.094  -0.227  1.00 14.64 ? 163 LEU A CB  1 
ATOM   1313 C  CG  . LEU A 1 163 ? 9.713   -4.760  1.110   1.00 15.83 ? 163 LEU A CG  1 
ATOM   1314 C  CD1 . LEU A 1 163 ? 10.002  -5.871  2.105   1.00 15.56 ? 163 LEU A CD1 1 
ATOM   1315 C  CD2 . LEU A 1 163 ? 10.235  -3.427  1.679   1.00 16.67 ? 163 LEU A CD2 1 
ATOM   1316 N  N   . ASP A 1 164 ? 10.475  -5.110  -3.537  1.00 20.53 ? 164 ASP A N   1 
ATOM   1317 C  CA  . ASP A 1 164 ? 11.332  -5.358  -4.691  1.00 23.52 ? 164 ASP A CA  1 
ATOM   1318 C  C   . ASP A 1 164 ? 11.694  -4.063  -5.448  1.00 24.70 ? 164 ASP A C   1 
ATOM   1319 O  O   . ASP A 1 164 ? 12.655  -4.087  -6.215  1.00 26.59 ? 164 ASP A O   1 
ATOM   1320 C  CB  . ASP A 1 164 ? 10.728  -6.397  -5.640  1.00 31.41 ? 164 ASP A CB  1 
ATOM   1321 C  CG  . ASP A 1 164 ? 9.688   -5.730  -6.505  1.00 34.29 ? 164 ASP A CG  1 
ATOM   1322 O  OD1 . ASP A 1 164 ? 8.663   -5.325  -5.955  1.00 39.31 ? 164 ASP A OD1 1 
ATOM   1323 O  OD2 . ASP A 1 164 ? 9.950   -5.539  -7.722  1.00 45.04 ? 164 ASP A OD2 1 
ATOM   1324 N  N   . SER A 1 165 ? 11.001  -2.926  -5.231  1.00 21.91 ? 165 SER A N   1 
ATOM   1325 C  CA  . SER A 1 165 ? 11.431  -1.692  -5.884  1.00 20.74 ? 165 SER A CA  1 
ATOM   1326 C  C   . SER A 1 165 ? 12.509  -0.961  -5.080  1.00 21.82 ? 165 SER A C   1 
ATOM   1327 O  O   . SER A 1 165 ? 13.063  0.055   -5.532  1.00 22.67 ? 165 SER A O   1 
ATOM   1328 C  CB  . SER A 1 165 ? 10.254  -0.803  -6.127  1.00 22.31 ? 165 SER A CB  1 
ATOM   1329 O  OG  . SER A 1 165 ? 9.758   -0.327  -4.899  1.00 25.23 ? 165 SER A OG  1 
ATOM   1330 N  N   . ILE A 1 166 ? 12.820  -1.450  -3.856  1.00 19.36 ? 166 ILE A N   1 
ATOM   1331 C  CA  . ILE A 1 166 ? 13.854  -0.810  -3.033  1.00 17.21 ? 166 ILE A CA  1 
ATOM   1332 C  C   . ILE A 1 166 ? 14.862  -1.845  -2.517  1.00 18.51 ? 166 ILE A C   1 
ATOM   1333 O  O   . ILE A 1 166 ? 15.298  -1.866  -1.358  1.00 16.18 ? 166 ILE A O   1 
ATOM   1334 C  CB  . ILE A 1 166 ? 13.237  0.043   -1.896  1.00 17.05 ? 166 ILE A CB  1 
ATOM   1335 C  CG1 . ILE A 1 166 ? 12.458  -0.844  -0.935  1.00 16.27 ? 166 ILE A CG1 1 
ATOM   1336 C  CG2 . ILE A 1 166 ? 12.360  1.206   -2.407  1.00 17.95 ? 166 ILE A CG2 1 
ATOM   1337 C  CD1 . ILE A 1 166 ? 12.343  -0.223  0.458   1.00 18.40 ? 166 ILE A CD1 1 
ATOM   1338 N  N   . LYS A 1 167 ? 15.276  -2.743  -3.412  1.00 17.73 ? 167 LYS A N   1 
ATOM   1339 C  CA  . LYS A 1 167 ? 16.090  -3.871  -3.016  1.00 17.12 ? 167 LYS A CA  1 
ATOM   1340 C  C   . LYS A 1 167 ? 17.406  -3.437  -2.370  1.00 18.18 ? 167 LYS A C   1 
ATOM   1341 O  O   . LYS A 1 167 ? 17.907  -4.069  -1.429  1.00 17.50 ? 167 LYS A O   1 
ATOM   1342 C  CB  . LYS A 1 167 ? 16.348  -4.801  -4.214  1.00 17.26 ? 167 LYS A CB  1 
ATOM   1343 C  CG  . LYS A 1 167 ? 17.130  -6.048  -3.827  1.00 19.61 ? 167 LYS A CG  1 
ATOM   1344 C  CD  . LYS A 1 167 ? 17.433  -6.938  -5.051  1.00 25.43 ? 167 LYS A CD  1 
ATOM   1345 C  CE  . LYS A 1 167 ? 18.303  -8.121  -4.679  1.00 30.22 ? 167 LYS A CE  1 
ATOM   1346 N  NZ  . LYS A 1 167 ? 18.388  -9.125  -5.771  1.00 38.55 ? 167 LYS A NZ  1 
ATOM   1347 N  N   . THR A 1 168 ? 17.990  -2.326  -2.850  1.00 15.48 ? 168 THR A N   1 
ATOM   1348 C  CA  . THR A 1 168 ? 19.360  -2.006  -2.477  1.00 16.98 ? 168 THR A CA  1 
ATOM   1349 C  C   . THR A 1 168 ? 19.416  -0.649  -1.766  1.00 14.21 ? 168 THR A C   1 
ATOM   1350 O  O   . THR A 1 168 ? 18.502  0.179   -1.861  1.00 17.40 ? 168 THR A O   1 
ATOM   1351 C  CB  . THR A 1 168 ? 20.308  -2.074  -3.690  1.00 19.04 ? 168 THR A CB  1 
ATOM   1352 O  OG1 . THR A 1 168 ? 19.589  -1.289  -4.642  1.00 18.44 ? 168 THR A OG1 1 
ATOM   1353 C  CG2 . THR A 1 168 ? 20.486  -3.513  -4.136  1.00 19.55 ? 168 THR A CG2 1 
ATOM   1354 N  N   . LYS A 1 169 ? 20.490  -0.502  -0.998  1.00 18.04 ? 169 LYS A N   1 
ATOM   1355 C  CA  . LYS A 1 169 ? 20.794  0.665   -0.173  1.00 18.44 ? 169 LYS A CA  1 
ATOM   1356 C  C   . LYS A 1 169 ? 20.632  1.958   -0.966  1.00 21.48 ? 169 LYS A C   1 
ATOM   1357 O  O   . LYS A 1 169 ? 21.239  2.071   -2.041  1.00 23.38 ? 169 LYS A O   1 
ATOM   1358 C  CB  . LYS A 1 169 ? 22.216  0.561   0.370   1.00 20.07 ? 169 LYS A CB  1 
ATOM   1359 C  CG  . LYS A 1 169 ? 22.677  1.764   1.209   1.00 20.99 ? 169 LYS A CG  1 
ATOM   1360 C  CD  . LYS A 1 169 ? 24.015  1.526   1.781   1.00 21.58 ? 169 LYS A CD  1 
ATOM   1361 C  CE  . LYS A 1 169 ? 24.640  2.787   2.350   1.00 30.62 ? 169 LYS A CE  1 
ATOM   1362 N  NZ  . LYS A 1 169 ? 25.962  2.538   2.976   1.00 33.39 ? 169 LYS A NZ  1 
ATOM   1363 N  N   . GLY A 1 170 ? 19.810  2.894   -0.457  1.00 20.57 ? 170 GLY A N   1 
ATOM   1364 C  CA  . GLY A 1 170 ? 19.661  4.188   -1.115  1.00 19.16 ? 170 GLY A CA  1 
ATOM   1365 C  C   . GLY A 1 170 ? 18.451  4.296   -2.035  1.00 21.14 ? 170 GLY A C   1 
ATOM   1366 O  O   . GLY A 1 170 ? 18.101  5.394   -2.481  1.00 20.81 ? 170 GLY A O   1 
ATOM   1367 N  N   . LYS A 1 171 ? 17.841  3.157   -2.432  1.00 17.59 ? 171 LYS A N   1 
ATOM   1368 C  CA  . LYS A 1 171 ? 16.609  3.196   -3.209  1.00 19.77 ? 171 LYS A CA  1 
ATOM   1369 C  C   . LYS A 1 171 ? 15.431  3.666   -2.372  1.00 19.81 ? 171 LYS A C   1 
ATOM   1370 O  O   . LYS A 1 171 ? 15.276  3.191   -1.243  1.00 17.77 ? 171 LYS A O   1 
ATOM   1371 C  CB  . LYS A 1 171 ? 16.333  1.871   -3.930  1.00 20.90 ? 171 LYS A CB  1 
ATOM   1372 C  CG  . LYS A 1 171 ? 17.470  1.438   -4.860  1.00 24.13 ? 171 LYS A CG  1 
ATOM   1373 C  CD  . LYS A 1 171 ? 17.053  0.374   -5.897  1.00 29.70 ? 171 LYS A CD  1 
ATOM   1374 C  CE  . LYS A 1 171 ? 16.079  0.883   -6.960  1.00 37.40 ? 171 LYS A CE  1 
ATOM   1375 N  NZ  . LYS A 1 171 ? 15.468  -0.202  -7.782  1.00 35.44 ? 171 LYS A NZ  1 
ATOM   1376 N  N   . SER A 1 172 ? 14.571  4.502   -2.931  1.00 19.82 ? 172 SER A N   1 
ATOM   1377 C  CA  . SER A 1 172 ? 13.276  4.870   -2.380  1.00 19.39 ? 172 SER A CA  1 
ATOM   1378 C  C   . SER A 1 172 ? 12.147  4.708   -3.396  1.00 19.23 ? 172 SER A C   1 
ATOM   1379 O  O   . SER A 1 172 ? 12.358  4.656   -4.618  1.00 20.60 ? 172 SER A O   1 
ATOM   1380 C  CB  . SER A 1 172 ? 13.241  6.275   -1.783  1.00 19.11 ? 172 SER A CB  1 
ATOM   1381 O  OG  . SER A 1 172 ? 13.542  7.260   -2.774  1.00 21.73 ? 172 SER A OG  1 
ATOM   1382 N  N   . ALA A 1 173 ? 10.923  4.726   -2.897  1.00 20.26 ? 173 ALA A N   1 
ATOM   1383 C  CA  . ALA A 1 173 ? 9.744   4.676   -3.745  1.00 20.83 ? 173 ALA A CA  1 
ATOM   1384 C  C   . ALA A 1 173 ? 8.635   5.486   -3.076  1.00 24.85 ? 173 ALA A C   1 
ATOM   1385 O  O   . ALA A 1 173 ? 8.534   5.512   -1.855  1.00 19.44 ? 173 ALA A O   1 
ATOM   1386 C  CB  . ALA A 1 173 ? 9.306   3.264   -3.989  1.00 22.60 ? 173 ALA A CB  1 
ATOM   1387 N  N   . ASP A 1 174 ? 7.798   6.178   -3.849  1.00 23.55 ? 174 ASP A N   1 
ATOM   1388 C  CA  . ASP A 1 174 ? 6.644   6.854   -3.283  1.00 25.84 ? 174 ASP A CA  1 
ATOM   1389 C  C   . ASP A 1 174 ? 5.812   5.810   -2.538  1.00 24.23 ? 174 ASP A C   1 
ATOM   1390 O  O   . ASP A 1 174 ? 5.633   4.664   -2.977  1.00 25.13 ? 174 ASP A O   1 
ATOM   1391 C  CB  . ASP A 1 174 ? 5.849   7.618   -4.366  1.00 30.27 ? 174 ASP A CB  1 
ATOM   1392 C  CG  . ASP A 1 174 ? 6.699   8.569   -5.210  1.00 38.73 ? 174 ASP A CG  1 
ATOM   1393 O  OD1 . ASP A 1 174 ? 7.434   9.412   -4.624  1.00 39.84 ? 174 ASP A OD1 1 
ATOM   1394 O  OD2 . ASP A 1 174 ? 6.635   8.463   -6.472  1.00 39.32 ? 174 ASP A OD2 1 
ATOM   1395 N  N   . PHE A 1 175 ? 5.231   6.227   -1.425  1.00 19.32 ? 175 PHE A N   1 
ATOM   1396 C  CA  . PHE A 1 175 ? 4.527   5.285   -0.599  1.00 19.62 ? 175 PHE A CA  1 
ATOM   1397 C  C   . PHE A 1 175 ? 3.450   6.073   0.107   1.00 24.60 ? 175 PHE A C   1 
ATOM   1398 O  O   . PHE A 1 175 ? 3.522   6.321   1.301   1.00 24.51 ? 175 PHE A O   1 
ATOM   1399 C  CB  . PHE A 1 175 ? 5.512   4.470   0.257   1.00 19.20 ? 175 PHE A CB  1 
ATOM   1400 C  CG  . PHE A 1 175 ? 4.882   3.199   0.753   1.00 19.38 ? 175 PHE A CG  1 
ATOM   1401 C  CD1 . PHE A 1 175 ? 4.644   2.138   -0.101  1.00 20.06 ? 175 PHE A CD1 1 
ATOM   1402 C  CD2 . PHE A 1 175 ? 4.497   3.073   2.077   1.00 18.02 ? 175 PHE A CD2 1 
ATOM   1403 C  CE1 . PHE A 1 175 ? 4.009   1.003   0.380   1.00 20.19 ? 175 PHE A CE1 1 
ATOM   1404 C  CE2 . PHE A 1 175 ? 3.889   1.929   2.577   1.00 18.70 ? 175 PHE A CE2 1 
ATOM   1405 C  CZ  . PHE A 1 175 ? 3.648   0.881   1.707   1.00 17.71 ? 175 PHE A CZ  1 
ATOM   1406 N  N   . THR A 1 176 ? 2.482   6.534   -0.670  1.00 19.56 ? 176 THR A N   1 
ATOM   1407 C  CA  . THR A 1 176 ? 1.426   7.359   -0.124  1.00 18.69 ? 176 THR A CA  1 
ATOM   1408 C  C   . THR A 1 176 ? 0.236   6.525   0.309   1.00 16.86 ? 176 THR A C   1 
ATOM   1409 O  O   . THR A 1 176 ? 0.069   5.396   -0.139  1.00 18.92 ? 176 THR A O   1 
ATOM   1410 C  CB  . THR A 1 176 ? 1.047   8.433   -1.145  1.00 22.10 ? 176 THR A CB  1 
ATOM   1411 O  OG1 . THR A 1 176 ? 0.571   7.743   -2.300  1.00 24.65 ? 176 THR A OG1 1 
ATOM   1412 C  CG2 . THR A 1 176 ? 2.219   9.311   -1.495  1.00 23.78 ? 176 THR A CG2 1 
ATOM   1413 N  N   . ASN A 1 177 ? -0.593  7.089   1.185   1.00 16.55 ? 177 ASN A N   1 
ATOM   1414 C  CA  . ASN A 1 177 ? -1.883  6.554   1.567   1.00 17.46 ? 177 ASN A CA  1 
ATOM   1415 C  C   . ASN A 1 177 ? -1.743  5.216   2.302   1.00 17.13 ? 177 ASN A C   1 
ATOM   1416 O  O   . ASN A 1 177 ? -2.683  4.434   2.327   1.00 21.45 ? 177 ASN A O   1 
ATOM   1417 C  CB  . ASN A 1 177 ? -2.789  6.492   0.345   1.00 17.01 ? 177 ASN A CB  1 
ATOM   1418 C  CG  . ASN A 1 177 ? -2.952  7.886   -0.236  1.00 18.75 ? 177 ASN A CG  1 
ATOM   1419 O  OD1 . ASN A 1 177 ? -3.661  8.707   0.352   1.00 21.85 ? 177 ASN A OD1 1 
ATOM   1420 N  ND2 . ASN A 1 177 ? -2.295  8.120   -1.368  1.00 16.90 ? 177 ASN A ND2 1 
ATOM   1421 N  N   . PHE A 1 178 ? -0.590  4.987   2.918   1.00 17.09 ? 178 PHE A N   1 
ATOM   1422 C  CA  . PHE A 1 178 ? -0.463  3.777   3.732   1.00 18.29 ? 178 PHE A CA  1 
ATOM   1423 C  C   . PHE A 1 178 ? -0.897  4.054   5.162   1.00 15.59 ? 178 PHE A C   1 
ATOM   1424 O  O   . PHE A 1 178 ? -0.456  5.043   5.749   1.00 18.45 ? 178 PHE A O   1 
ATOM   1425 C  CB  . PHE A 1 178 ? 0.975   3.324   3.809   1.00 16.48 ? 178 PHE A CB  1 
ATOM   1426 C  CG  . PHE A 1 178 ? 1.060   2.068   4.633   1.00 18.34 ? 178 PHE A CG  1 
ATOM   1427 C  CD1 . PHE A 1 178 ? 0.640   0.851   4.107   1.00 17.65 ? 178 PHE A CD1 1 
ATOM   1428 C  CD2 . PHE A 1 178 ? 1.559   2.134   5.926   1.00 17.51 ? 178 PHE A CD2 1 
ATOM   1429 C  CE1 . PHE A 1 178 ? 0.713   -0.303  4.875   1.00 19.66 ? 178 PHE A CE1 1 
ATOM   1430 C  CE2 . PHE A 1 178 ? 1.617   0.977   6.695   1.00 18.19 ? 178 PHE A CE2 1 
ATOM   1431 C  CZ  . PHE A 1 178 ? 1.258   -0.238  6.152   1.00 18.69 ? 178 PHE A CZ  1 
ATOM   1432 N  N   . ASP A 1 179 ? -1.821  3.251   5.689   1.00 16.48 ? 179 ASP A N   1 
ATOM   1433 C  CA  . ASP A 1 179 ? -2.386  3.470   7.011   1.00 16.68 ? 179 ASP A CA  1 
ATOM   1434 C  C   . ASP A 1 179 ? -1.675  2.602   8.035   1.00 16.74 ? 179 ASP A C   1 
ATOM   1435 O  O   . ASP A 1 179 ? -1.818  1.394   8.029   1.00 17.63 ? 179 ASP A O   1 
ATOM   1436 C  CB  . ASP A 1 179 ? -3.869  3.093   7.026   1.00 18.61 ? 179 ASP A CB  1 
ATOM   1437 C  CG  . ASP A 1 179 ? -4.647  3.430   8.276   1.00 20.86 ? 179 ASP A CG  1 
ATOM   1438 O  OD1 . ASP A 1 179 ? -4.048  3.689   9.322   1.00 19.22 ? 179 ASP A OD1 1 
ATOM   1439 O  OD2 . ASP A 1 179 ? -5.891  3.506   8.175   1.00 25.63 ? 179 ASP A OD2 1 
ATOM   1440 N  N   . PRO A 1 180 ? -0.909  3.188   8.988   1.00 14.01 ? 180 PRO A N   1 
ATOM   1441 C  CA  . PRO A 1 180 ? -0.116  2.364   9.910   1.00 13.64 ? 180 PRO A CA  1 
ATOM   1442 C  C   . PRO A 1 180 ? -1.012  1.709   10.941  1.00 14.79 ? 180 PRO A C   1 
ATOM   1443 O  O   . PRO A 1 180 ? -0.541  0.796   11.642  1.00 14.16 ? 180 PRO A O   1 
ATOM   1444 C  CB  . PRO A 1 180 ? 0.878   3.392   10.489  1.00 16.51 ? 180 PRO A CB  1 
ATOM   1445 C  CG  . PRO A 1 180 ? 0.137   4.703   10.431  1.00 15.72 ? 180 PRO A CG  1 
ATOM   1446 C  CD  . PRO A 1 180 ? -0.706  4.622   9.164   1.00 14.13 ? 180 PRO A CD  1 
ATOM   1447 N  N   . ARG A 1 181 ? -2.320  2.056   10.971  1.00 14.05 ? 181 ARG A N   1 
ATOM   1448 C  CA  . ARG A 1 181 ? -3.213  1.421   11.938  1.00 15.48 ? 181 ARG A CA  1 
ATOM   1449 C  C   . ARG A 1 181 ? -3.368  -0.070  11.626  1.00 15.15 ? 181 ARG A C   1 
ATOM   1450 O  O   . ARG A 1 181 ? -3.744  -0.862  12.502  1.00 16.36 ? 181 ARG A O   1 
ATOM   1451 C  CB  . ARG A 1 181 ? -4.581  2.109   11.976  1.00 17.45 ? 181 ARG A CB  1 
ATOM   1452 C  CG  . ARG A 1 181 ? -4.466  3.517   12.553  1.00 18.01 ? 181 ARG A CG  1 
ATOM   1453 C  CD  . ARG A 1 181 ? -5.800  4.217   12.495  1.00 18.75 ? 181 ARG A CD  1 
ATOM   1454 N  NE  . ARG A 1 181 ? -6.199  4.420   11.128  1.00 18.14 ? 181 ARG A NE  1 
ATOM   1455 C  CZ  . ARG A 1 181 ? -7.272  5.146   10.808  1.00 21.13 ? 181 ARG A CZ  1 
ATOM   1456 N  NH1 . ARG A 1 181 ? -7.972  5.721   11.783  1.00 23.31 ? 181 ARG A NH1 1 
ATOM   1457 N  NH2 . ARG A 1 181 ? -7.599  5.287   9.534   1.00 20.93 ? 181 ARG A NH2 1 
ATOM   1458 N  N   . GLY A 1 182 ? -3.113  -0.404  10.369  1.00 16.15 ? 182 GLY A N   1 
ATOM   1459 C  CA  . GLY A 1 182 ? -3.212  -1.783  9.924   1.00 16.60 ? 182 GLY A CA  1 
ATOM   1460 C  C   . GLY A 1 182 ? -2.137  -2.688  10.512  1.00 18.93 ? 182 GLY A C   1 
ATOM   1461 O  O   . GLY A 1 182 ? -2.207  -3.908  10.305  1.00 18.93 ? 182 GLY A O   1 
ATOM   1462 N  N   . LEU A 1 183 ? -1.139  -2.089  11.201  1.00 15.64 ? 183 LEU A N   1 
ATOM   1463 C  CA  . LEU A 1 183 ? -0.008  -2.886  11.681  1.00 16.15 ? 183 LEU A CA  1 
ATOM   1464 C  C   . LEU A 1 183 ? -0.132  -3.106  13.190  1.00 15.80 ? 183 LEU A C   1 
ATOM   1465 O  O   . LEU A 1 183 ? 0.803   -3.666  13.789  1.00 17.58 ? 183 LEU A O   1 
ATOM   1466 C  CB  . LEU A 1 183 ? 1.316   -2.172  11.355  1.00 15.02 ? 183 LEU A CB  1 
ATOM   1467 C  CG  . LEU A 1 183 ? 1.672   -1.990  9.857   1.00 14.92 ? 183 LEU A CG  1 
ATOM   1468 C  CD1 . LEU A 1 183 ? 2.930   -1.175  9.664   1.00 15.50 ? 183 LEU A CD1 1 
ATOM   1469 C  CD2 . LEU A 1 183 ? 1.832   -3.315  9.095   1.00 18.89 ? 183 LEU A CD2 1 
ATOM   1470 N  N   . LEU A 1 184 ? -1.205  -2.623  13.817  1.00 15.08 ? 184 LEU A N   1 
ATOM   1471 C  CA  . LEU A 1 184 ? -1.323  -2.666  15.265  1.00 15.65 ? 184 LEU A CA  1 
ATOM   1472 C  C   . LEU A 1 184 ? -2.023  -3.942  15.698  1.00 18.26 ? 184 LEU A C   1 
ATOM   1473 O  O   . LEU A 1 184 ? -2.935  -4.434  15.022  1.00 24.26 ? 184 LEU A O   1 
ATOM   1474 C  CB  . LEU A 1 184 ? -2.089  -1.450  15.778  1.00 15.21 ? 184 LEU A CB  1 
ATOM   1475 C  CG  . LEU A 1 184 ? -1.487  -0.108  15.396  1.00 15.72 ? 184 LEU A CG  1 
ATOM   1476 C  CD1 . LEU A 1 184 ? -2.339  1.025   15.931  1.00 17.16 ? 184 LEU A CD1 1 
ATOM   1477 C  CD2 . LEU A 1 184 ? -0.047  0.028   15.912  1.00 16.84 ? 184 LEU A CD2 1 
ATOM   1478 N  N   . PRO A 1 185 ? -1.685  -4.505  16.871  1.00 15.54 ? 185 PRO A N   1 
ATOM   1479 C  CA  . PRO A 1 185 ? -2.444  -5.614  17.410  1.00 16.13 ? 185 PRO A CA  1 
ATOM   1480 C  C   . PRO A 1 185 ? -3.745  -5.104  18.011  1.00 17.16 ? 185 PRO A C   1 
ATOM   1481 O  O   . PRO A 1 185 ? -3.949  -3.898  18.171  1.00 17.35 ? 185 PRO A O   1 
ATOM   1482 C  CB  . PRO A 1 185 ? -1.489  -6.232  18.458  1.00 14.32 ? 185 PRO A CB  1 
ATOM   1483 C  CG  . PRO A 1 185 ? -0.690  -5.034  18.942  1.00 13.98 ? 185 PRO A CG  1 
ATOM   1484 C  CD  . PRO A 1 185 ? -0.535  -4.122  17.718  1.00 13.75 ? 185 PRO A CD  1 
ATOM   1485 N  N   . GLU A 1 186 ? -4.554  -6.043  18.493  1.00 18.16 ? 186 GLU A N   1 
ATOM   1486 C  CA  . GLU A 1 186 ? -5.819  -5.660  19.096  1.00 19.80 ? 186 GLU A CA  1 
ATOM   1487 C  C   . GLU A 1 186 ? -5.584  -4.858  20.360  1.00 17.37 ? 186 GLU A C   1 
ATOM   1488 O  O   . GLU A 1 186 ? -6.240  -3.853  20.546  1.00 21.20 ? 186 GLU A O   1 
ATOM   1489 C  CB  . GLU A 1 186 ? -6.612  -6.886  19.542  1.00 21.98 ? 186 GLU A CB  1 
ATOM   1490 C  CG  . GLU A 1 186 ? -7.294  -7.608  18.431  1.00 27.84 ? 186 GLU A CG  1 
ATOM   1491 C  CD  . GLU A 1 186 ? -8.094  -8.796  18.970  1.00 26.54 ? 186 GLU A CD  1 
ATOM   1492 O  OE1 . GLU A 1 186 ? -8.545  -9.604  18.153  1.00 35.08 ? 186 GLU A OE1 1 
ATOM   1493 O  OE2 . GLU A 1 186 ? -8.176  -8.935  20.207  1.00 24.65 ? 186 GLU A OE2 1 
ATOM   1494 N  N   . SER A 1 187 ? -4.679  -5.345  21.247  1.00 16.36 ? 187 SER A N   1 
ATOM   1495 C  CA  . SER A 1 187 ? -4.476  -4.798  22.583  1.00 17.03 ? 187 SER A CA  1 
ATOM   1496 C  C   . SER A 1 187 ? -3.360  -3.752  22.564  1.00 17.61 ? 187 SER A C   1 
ATOM   1497 O  O   . SER A 1 187 ? -2.382  -3.927  21.832  1.00 19.14 ? 187 SER A O   1 
ATOM   1498 C  CB  . SER A 1 187 ? -4.095  -5.884  23.572  1.00 18.86 ? 187 SER A CB  1 
ATOM   1499 O  OG  . SER A 1 187 ? -3.928  -5.305  24.862  1.00 17.70 ? 187 SER A OG  1 
ATOM   1500 N  N   . LEU A 1 188 ? -3.502  -2.688  23.374  1.00 15.98 ? 188 LEU A N   1 
ATOM   1501 C  CA  . LEU A 1 188 ? -2.447  -1.691  23.564  1.00 16.53 ? 188 LEU A CA  1 
ATOM   1502 C  C   . LEU A 1 188 ? -1.833  -1.828  24.955  1.00 16.26 ? 188 LEU A C   1 
ATOM   1503 O  O   . LEU A 1 188 ? -1.174  -0.899  25.426  1.00 18.05 ? 188 LEU A O   1 
ATOM   1504 C  CB  . LEU A 1 188 ? -2.987  -0.266  23.331  1.00 18.56 ? 188 LEU A CB  1 
ATOM   1505 C  CG  . LEU A 1 188 ? -3.459  0.082   21.919  1.00 21.19 ? 188 LEU A CG  1 
ATOM   1506 C  CD1 . LEU A 1 188 ? -3.983  1.515   21.819  1.00 22.94 ? 188 LEU A CD1 1 
ATOM   1507 C  CD2 . LEU A 1 188 ? -2.333  -0.131  20.892  1.00 19.12 ? 188 LEU A CD2 1 
ATOM   1508 N  N   . ASP A 1 189 ? -1.981  -2.993  25.603  1.00 16.81 ? 189 ASP A N   1 
ATOM   1509 C  CA  . ASP A 1 189 ? -1.242  -3.243  26.825  1.00 17.33 ? 189 ASP A CA  1 
ATOM   1510 C  C   . ASP A 1 189 ? 0.264   -3.188  26.510  1.00 14.45 ? 189 ASP A C   1 
ATOM   1511 O  O   . ASP A 1 189 ? 0.681   -3.657  25.446  1.00 14.95 ? 189 ASP A O   1 
ATOM   1512 C  CB  . ASP A 1 189 ? -1.596  -4.624  27.389  1.00 19.71 ? 189 ASP A CB  1 
ATOM   1513 C  CG  . ASP A 1 189 ? -2.976  -4.694  28.049  1.00 25.65 ? 189 ASP A CG  1 
ATOM   1514 O  OD1 . ASP A 1 189 ? -3.602  -3.628  28.197  1.00 27.24 ? 189 ASP A OD1 1 
ATOM   1515 O  OD2 . ASP A 1 189 ? -3.391  -5.824  28.348  1.00 26.91 ? 189 ASP A OD2 1 
ATOM   1516 N  N   . TYR A 1 190 ? 1.039   -2.548  27.387  1.00 14.68 ? 190 TYR A N   1 
ATOM   1517 C  CA  . TYR A 1 190 ? 2.438   -2.287  27.037  1.00 13.11 ? 190 TYR A CA  1 
ATOM   1518 C  C   . TYR A 1 190 ? 3.341   -2.364  28.262  1.00 13.04 ? 190 TYR A C   1 
ATOM   1519 O  O   . TYR A 1 190 ? 2.926   -2.273  29.427  1.00 13.92 ? 190 TYR A O   1 
ATOM   1520 C  CB  . TYR A 1 190 ? 2.574   -0.923  26.349  1.00 13.77 ? 190 TYR A CB  1 
ATOM   1521 C  CG  . TYR A 1 190 ? 2.225   0.224   27.259  1.00 13.52 ? 190 TYR A CG  1 
ATOM   1522 C  CD1 . TYR A 1 190 ? 3.156   0.833   28.086  1.00 12.60 ? 190 TYR A CD1 1 
ATOM   1523 C  CD2 . TYR A 1 190 ? 0.944   0.751   27.223  1.00 12.40 ? 190 TYR A CD2 1 
ATOM   1524 C  CE1 . TYR A 1 190 ? 2.797   1.869   28.953  1.00 14.26 ? 190 TYR A CE1 1 
ATOM   1525 C  CE2 . TYR A 1 190 ? 0.578   1.819   28.041  1.00 13.88 ? 190 TYR A CE2 1 
ATOM   1526 C  CZ  . TYR A 1 190 ? 1.513   2.409   28.883  1.00 14.98 ? 190 TYR A CZ  1 
ATOM   1527 O  OH  . TYR A 1 190 ? 1.087   3.426   29.685  1.00 15.86 ? 190 TYR A OH  1 
ATOM   1528 N  N   . TRP A 1 191 ? 4.627   -2.528  27.986  1.00 12.10 ? 191 TRP A N   1 
ATOM   1529 C  CA  . TRP A 1 191 ? 5.695   -2.252  28.921  1.00 10.93 ? 191 TRP A CA  1 
ATOM   1530 C  C   . TRP A 1 191 ? 6.413   -0.973  28.513  1.00 11.12 ? 191 TRP A C   1 
ATOM   1531 O  O   . TRP A 1 191 ? 6.454   -0.670  27.332  1.00 12.23 ? 191 TRP A O   1 
ATOM   1532 C  CB  . TRP A 1 191 ? 6.704   -3.391  28.891  1.00 11.68 ? 191 TRP A CB  1 
ATOM   1533 C  CG  . TRP A 1 191 ? 6.167   -4.711  29.314  1.00 11.09 ? 191 TRP A CG  1 
ATOM   1534 C  CD1 . TRP A 1 191 ? 5.996   -5.162  30.594  1.00 12.93 ? 191 TRP A CD1 1 
ATOM   1535 C  CD2 . TRP A 1 191 ? 5.914   -5.845  28.466  1.00 11.11 ? 191 TRP A CD2 1 
ATOM   1536 N  NE1 . TRP A 1 191 ? 5.576   -6.460  30.588  1.00 14.51 ? 191 TRP A NE1 1 
ATOM   1537 C  CE2 . TRP A 1 191 ? 5.542   -6.912  29.304  1.00 12.32 ? 191 TRP A CE2 1 
ATOM   1538 C  CE3 . TRP A 1 191 ? 6.049   -6.062  27.095  1.00 11.98 ? 191 TRP A CE3 1 
ATOM   1539 C  CZ2 . TRP A 1 191 ? 5.219   -8.147  28.772  1.00 12.79 ? 191 TRP A CZ2 1 
ATOM   1540 C  CZ3 . TRP A 1 191 ? 5.751   -7.294  26.574  1.00 12.48 ? 191 TRP A CZ3 1 
ATOM   1541 C  CH2 . TRP A 1 191 ? 5.342   -8.324  27.416  1.00 13.24 ? 191 TRP A CH2 1 
ATOM   1542 N  N   . THR A 1 192 ? 6.999   -0.265  29.471  1.00 10.61 ? 192 THR A N   1 
ATOM   1543 C  CA  . THR A 1 192 ? 7.698   0.983   29.184  1.00 11.13 ? 192 THR A CA  1 
ATOM   1544 C  C   . THR A 1 192 ? 8.949   1.126   30.042  1.00 11.73 ? 192 THR A C   1 
ATOM   1545 O  O   . THR A 1 192 ? 8.997   0.728   31.212  1.00 11.97 ? 192 THR A O   1 
ATOM   1546 C  CB  . THR A 1 192 ? 6.762   2.183   29.224  1.00 11.52 ? 192 THR A CB  1 
ATOM   1547 O  OG1 . THR A 1 192 ? 7.464   3.340   28.784  1.00 11.11 ? 192 THR A OG1 1 
ATOM   1548 C  CG2 . THR A 1 192 ? 6.188   2.455   30.607  1.00 13.58 ? 192 THR A CG2 1 
ATOM   1549 N  N   . TYR A 1 193 ? 9.994   1.664   29.440  1.00 10.52 ? 193 TYR A N   1 
ATOM   1550 C  CA  . TYR A 1 193 ? 11.233  1.897   30.171  1.00 10.64 ? 193 TYR A CA  1 
ATOM   1551 C  C   . TYR A 1 193 ? 12.015  2.955   29.412  1.00 11.15 ? 193 TYR A C   1 
ATOM   1552 O  O   . TYR A 1 193 ? 11.766  3.212   28.221  1.00 11.24 ? 193 TYR A O   1 
ATOM   1553 C  CB  . TYR A 1 193 ? 12.087  0.618   30.359  1.00 11.13 ? 193 TYR A CB  1 
ATOM   1554 C  CG  . TYR A 1 193 ? 12.758  0.154   29.083  1.00 10.40 ? 193 TYR A CG  1 
ATOM   1555 C  CD1 . TYR A 1 193 ? 12.075  -0.556  28.107  1.00 10.45 ? 193 TYR A CD1 1 
ATOM   1556 C  CD2 . TYR A 1 193 ? 14.082  0.481   28.873  1.00 9.51  ? 193 TYR A CD2 1 
ATOM   1557 C  CE1 . TYR A 1 193 ? 12.696  -0.886  26.907  1.00 11.33 ? 193 TYR A CE1 1 
ATOM   1558 C  CE2 . TYR A 1 193 ? 14.718  0.166   27.682  1.00 10.34 ? 193 TYR A CE2 1 
ATOM   1559 C  CZ  . TYR A 1 193 ? 14.025  -0.515  26.714  1.00 9.66  ? 193 TYR A CZ  1 
ATOM   1560 O  OH  . TYR A 1 193 ? 14.667  -0.787  25.537  1.00 9.82  ? 193 TYR A OH  1 
ATOM   1561 N  N   . PRO A 1 194 ? 12.989  3.615   30.067  1.00 11.63 ? 194 PRO A N   1 
ATOM   1562 C  CA  . PRO A 1 194 ? 13.805  4.625   29.425  1.00 11.89 ? 194 PRO A CA  1 
ATOM   1563 C  C   . PRO A 1 194 ? 15.029  4.008   28.766  1.00 11.31 ? 194 PRO A C   1 
ATOM   1564 O  O   . PRO A 1 194 ? 15.688  3.207   29.395  1.00 12.37 ? 194 PRO A O   1 
ATOM   1565 C  CB  . PRO A 1 194 ? 14.266  5.512   30.607  1.00 14.20 ? 194 PRO A CB  1 
ATOM   1566 C  CG  . PRO A 1 194 ? 14.275  4.589   31.774  1.00 14.57 ? 194 PRO A CG  1 
ATOM   1567 C  CD  . PRO A 1 194 ? 13.200  3.542   31.518  1.00 14.22 ? 194 PRO A CD  1 
ATOM   1568 N  N   . GLY A 1 195 ? 15.286  4.391   27.509  1.00 9.49  ? 195 GLY A N   1 
ATOM   1569 C  CA  . GLY A 1 195 ? 16.400  3.744   26.834  1.00 11.72 ? 195 GLY A CA  1 
ATOM   1570 C  C   . GLY A 1 195 ? 16.951  4.619   25.726  1.00 10.64 ? 195 GLY A C   1 
ATOM   1571 O  O   . GLY A 1 195 ? 16.997  5.827   25.858  1.00 10.33 ? 195 GLY A O   1 
ATOM   1572 N  N   . SER A 1 196 ? 17.318  3.957   24.626  1.00 10.32 ? 196 SER A N   1 
ATOM   1573 C  CA  . SER A 1 196 ? 18.154  4.560   23.595  1.00 10.36 ? 196 SER A CA  1 
ATOM   1574 C  C   . SER A 1 196 ? 17.704  4.142   22.202  1.00 10.98 ? 196 SER A C   1 
ATOM   1575 O  O   . SER A 1 196 ? 16.921  3.198   22.039  1.00 10.90 ? 196 SER A O   1 
ATOM   1576 C  CB  . SER A 1 196 ? 19.631  4.120   23.800  1.00 11.01 ? 196 SER A CB  1 
ATOM   1577 O  OG  . SER A 1 196 ? 19.863  2.797   23.337  1.00 9.94  ? 196 SER A OG  1 
ATOM   1578 N  N   . LEU A 1 197 ? 18.299  4.820   21.224  1.00 10.15 ? 197 LEU A N   1 
ATOM   1579 C  CA  . LEU A 1 197 ? 18.313  4.304   19.857  1.00 10.23 ? 197 LEU A CA  1 
ATOM   1580 C  C   . LEU A 1 197 ? 18.985  2.959   19.906  1.00 10.70 ? 197 LEU A C   1 
ATOM   1581 O  O   . LEU A 1 197 ? 19.988  2.804   20.602  1.00 9.93  ? 197 LEU A O   1 
ATOM   1582 C  CB  . LEU A 1 197 ? 19.132  5.247   18.969  1.00 11.85 ? 197 LEU A CB  1 
ATOM   1583 C  CG  . LEU A 1 197 ? 18.588  6.670   18.889  1.00 12.47 ? 197 LEU A CG  1 
ATOM   1584 C  CD1 . LEU A 1 197 ? 19.491  7.558   18.031  1.00 16.03 ? 197 LEU A CD1 1 
ATOM   1585 C  CD2 . LEU A 1 197 ? 17.201  6.716   18.289  1.00 14.84 ? 197 LEU A CD2 1 
ATOM   1586 N  N   . THR A 1 198 ? 18.541  2.027   19.047  1.00 9.61  ? 198 THR A N   1 
ATOM   1587 C  CA  . THR A 1 198 ? 19.165  0.724   19.012  1.00 11.21 ? 198 THR A CA  1 
ATOM   1588 C  C   . THR A 1 198 ? 20.185  0.614   17.878  1.00 10.97 ? 198 THR A C   1 
ATOM   1589 O  O   . THR A 1 198 ? 20.795  -0.451  17.764  1.00 11.67 ? 198 THR A O   1 
ATOM   1590 C  CB  . THR A 1 198 ? 18.135  -0.409  18.851  1.00 10.16 ? 198 THR A CB  1 
ATOM   1591 O  OG1 . THR A 1 198 ? 17.561  -0.366  17.538  1.00 10.26 ? 198 THR A OG1 1 
ATOM   1592 C  CG2 . THR A 1 198 ? 17.116  -0.469  19.963  1.00 11.51 ? 198 THR A CG2 1 
ATOM   1593 N  N   . THR A 1 199 ? 20.360  1.712   17.101  1.00 12.35 ? 199 THR A N   1 
ATOM   1594 C  CA  . THR A 1 199 ? 21.390  1.757   16.070  1.00 13.43 ? 199 THR A CA  1 
ATOM   1595 C  C   . THR A 1 199 ? 22.269  2.950   16.414  1.00 13.15 ? 199 THR A C   1 
ATOM   1596 O  O   . THR A 1 199 ? 21.833  3.899   17.081  1.00 13.37 ? 199 THR A O   1 
ATOM   1597 C  CB  . THR A 1 199 ? 20.782  2.051   14.691  1.00 14.52 ? 199 THR A CB  1 
ATOM   1598 O  OG1 . THR A 1 199 ? 20.034  3.272   14.701  1.00 16.08 ? 199 THR A OG1 1 
ATOM   1599 C  CG2 . THR A 1 199 ? 19.879  0.917   14.237  1.00 14.49 ? 199 THR A CG2 1 
ATOM   1600 N  N   . PRO A 1 200 ? 23.548  2.963   15.984  1.00 13.12 ? 200 PRO A N   1 
ATOM   1601 C  CA  . PRO A 1 200 ? 24.315  4.211   16.077  1.00 13.31 ? 200 PRO A CA  1 
ATOM   1602 C  C   . PRO A 1 200 ? 23.452  5.376   15.590  1.00 11.57 ? 200 PRO A C   1 
ATOM   1603 O  O   . PRO A 1 200 ? 22.718  5.278   14.585  1.00 14.02 ? 200 PRO A O   1 
ATOM   1604 C  CB  . PRO A 1 200 ? 25.437  3.887   15.053  1.00 12.85 ? 200 PRO A CB  1 
ATOM   1605 C  CG  . PRO A 1 200 ? 25.682  2.419   15.309  1.00 14.51 ? 200 PRO A CG  1 
ATOM   1606 C  CD  . PRO A 1 200 ? 24.287  1.812   15.412  1.00 14.60 ? 200 PRO A CD  1 
ATOM   1607 N  N   . PRO A 1 201 ? 23.516  6.558   16.241  1.00 12.83 ? 201 PRO A N   1 
ATOM   1608 C  CA  . PRO A 1 201 ? 24.488  6.841   17.315  1.00 13.14 ? 201 PRO A CA  1 
ATOM   1609 C  C   . PRO A 1 201 ? 24.171  6.427   18.754  1.00 13.80 ? 201 PRO A C   1 
ATOM   1610 O  O   . PRO A 1 201 ? 24.901  6.771   19.690  1.00 14.46 ? 201 PRO A O   1 
ATOM   1611 C  CB  . PRO A 1 201 ? 24.521  8.365   17.196  1.00 13.50 ? 201 PRO A CB  1 
ATOM   1612 C  CG  . PRO A 1 201 ? 23.122  8.768   16.889  1.00 15.06 ? 201 PRO A CG  1 
ATOM   1613 C  CD  . PRO A 1 201 ? 22.737  7.742   15.843  1.00 12.97 ? 201 PRO A CD  1 
ATOM   1614 N  N   . LEU A 1 202 ? 23.134  5.577   18.921  1.00 11.46 ? 202 LEU A N   1 
ATOM   1615 C  CA  . LEU A 1 202 ? 22.822  4.990   20.231  1.00 11.94 ? 202 LEU A CA  1 
ATOM   1616 C  C   . LEU A 1 202 ? 22.463  5.986   21.327  1.00 11.10 ? 202 LEU A C   1 
ATOM   1617 O  O   . LEU A 1 202 ? 22.470  5.615   22.502  1.00 12.91 ? 202 LEU A O   1 
ATOM   1618 C  CB  . LEU A 1 202 ? 23.960  4.083   20.723  1.00 11.75 ? 202 LEU A CB  1 
ATOM   1619 C  CG  . LEU A 1 202 ? 24.281  2.963   19.730  1.00 12.01 ? 202 LEU A CG  1 
ATOM   1620 C  CD1 . LEU A 1 202 ? 25.552  2.271   20.224  1.00 13.57 ? 202 LEU A CD1 1 
ATOM   1621 C  CD2 . LEU A 1 202 ? 23.112  1.938   19.570  1.00 13.53 ? 202 LEU A CD2 1 
ATOM   1622 N  N   . THR A 1 203 ? 21.989  7.163   20.908  1.00 12.10 ? 203 THR A N   1 
ATOM   1623 C  CA  . THR A 1 203 ? 21.675  8.233   21.835  1.00 12.15 ? 203 THR A CA  1 
ATOM   1624 C  C   . THR A 1 203 ? 20.612  7.785   22.845  1.00 12.85 ? 203 THR A C   1 
ATOM   1625 O  O   . THR A 1 203 ? 19.624  7.118   22.454  1.00 13.00 ? 203 THR A O   1 
ATOM   1626 C  CB  . THR A 1 203 ? 21.157  9.430   21.051  1.00 12.81 ? 203 THR A CB  1 
ATOM   1627 O  OG1 . THR A 1 203 ? 22.155  9.668   20.051  1.00 15.91 ? 203 THR A OG1 1 
ATOM   1628 C  CG2 . THR A 1 203 ? 20.964  10.623  21.963  1.00 14.75 ? 203 THR A CG2 1 
ATOM   1629 N  N   . GLU A 1 204 ? 20.736  8.228   24.092  1.00 13.39 ? 204 GLU A N   1 
ATOM   1630 C  CA  . GLU A 1 204 ? 19.798  7.862   25.145  1.00 14.23 ? 204 GLU A CA  1 
ATOM   1631 C  C   . GLU A 1 204 ? 18.602  8.811   25.230  1.00 15.63 ? 204 GLU A C   1 
ATOM   1632 O  O   . GLU A 1 204 ? 18.374  9.482   26.260  1.00 16.22 ? 204 GLU A O   1 
ATOM   1633 C  CB  . GLU A 1 204 ? 20.569  7.724   26.455  1.00 14.06 ? 204 GLU A CB  1 
ATOM   1634 C  CG  . GLU A 1 204 ? 21.504  6.523   26.356  1.00 13.52 ? 204 GLU A CG  1 
ATOM   1635 C  CD  . GLU A 1 204 ? 22.391  6.211   27.558  1.00 15.30 ? 204 GLU A CD  1 
ATOM   1636 O  OE1 . GLU A 1 204 ? 22.586  7.119   28.446  1.00 16.82 ? 204 GLU A OE1 1 
ATOM   1637 O  OE2 . GLU A 1 204 ? 22.830  5.068   27.667  1.00 13.67 ? 204 GLU A OE2 1 
ATOM   1638 N  N   . CYS A 1 205 ? 17.820  8.841   24.148  1.00 12.05 ? 205 CYS A N   1 
ATOM   1639 C  CA  . CYS A 1 205 ? 16.790  9.847   23.938  1.00 11.97 ? 205 CYS A CA  1 
ATOM   1640 C  C   . CYS A 1 205 ? 15.409  9.206   23.817  1.00 10.76 ? 205 CYS A C   1 
ATOM   1641 O  O   . CYS A 1 205 ? 14.499  9.910   23.429  1.00 10.57 ? 205 CYS A O   1 
ATOM   1642 C  CB  . CYS A 1 205 ? 17.104  10.652  22.669  1.00 12.44 ? 205 CYS A CB  1 
ATOM   1643 S  SG  . CYS A 1 205 ? 17.159  9.653   21.150  1.00 14.03 ? 205 CYS A SG  1 
ATOM   1644 N  N   . VAL A 1 206 ? 15.295  7.901   24.118  1.00 9.75  ? 206 VAL A N   1 
ATOM   1645 C  CA  . VAL A 1 206 ? 14.048  7.180   23.805  1.00 10.53 ? 206 VAL A CA  1 
ATOM   1646 C  C   . VAL A 1 206 ? 13.273  6.759   25.047  1.00 10.17 ? 206 VAL A C   1 
ATOM   1647 O  O   . VAL A 1 206 ? 13.782  6.061   25.913  1.00 11.68 ? 206 VAL A O   1 
ATOM   1648 C  CB  . VAL A 1 206 ? 14.338  5.941   22.957  1.00 10.07 ? 206 VAL A CB  1 
ATOM   1649 C  CG1 . VAL A 1 206 ? 13.004  5.298   22.544  1.00 10.14 ? 206 VAL A CG1 1 
ATOM   1650 C  CG2 . VAL A 1 206 ? 15.065  6.313   21.680  1.00 10.76 ? 206 VAL A CG2 1 
ATOM   1651 N  N   . THR A 1 207 ? 11.965  7.055   25.070  1.00 10.00 ? 207 THR A N   1 
ATOM   1652 C  CA  . THR A 1 207 ? 11.035  6.376   25.940  1.00 10.16 ? 207 THR A CA  1 
ATOM   1653 C  C   . THR A 1 207 ? 10.469  5.230   25.120  1.00 10.62 ? 207 THR A C   1 
ATOM   1654 O  O   . THR A 1 207 ? 9.808   5.478   24.105  1.00 10.02 ? 207 THR A O   1 
ATOM   1655 C  CB  . THR A 1 207 ? 9.857   7.279   26.368  1.00 10.38 ? 207 THR A CB  1 
ATOM   1656 O  OG1 . THR A 1 207 ? 10.385  8.372   27.134  1.00 11.42 ? 207 THR A OG1 1 
ATOM   1657 C  CG2 . THR A 1 207 ? 8.883   6.534   27.267  1.00 10.33 ? 207 THR A CG2 1 
ATOM   1658 N  N   . TRP A 1 208 ? 10.765  4.015   25.586  1.00 9.82  ? 208 TRP A N   1 
ATOM   1659 C  CA  . TRP A 1 208 ? 10.340  2.803   24.880  1.00 9.35  ? 208 TRP A CA  1 
ATOM   1660 C  C   . TRP A 1 208 ? 8.956   2.394   25.350  1.00 9.65  ? 208 TRP A C   1 
ATOM   1661 O  O   . TRP A 1 208 ? 8.757   2.357   26.578  1.00 9.45  ? 208 TRP A O   1 
ATOM   1662 C  CB  . TRP A 1 208 ? 11.344  1.658   25.090  1.00 9.64  ? 208 TRP A CB  1 
ATOM   1663 C  CG  . TRP A 1 208 ? 12.448  1.760   24.080  1.00 8.66  ? 208 TRP A CG  1 
ATOM   1664 C  CD1 . TRP A 1 208 ? 13.706  2.288   24.284  1.00 9.72  ? 208 TRP A CD1 1 
ATOM   1665 C  CD2 . TRP A 1 208 ? 12.377  1.353   22.703  1.00 9.71  ? 208 TRP A CD2 1 
ATOM   1666 N  NE1 . TRP A 1 208 ? 14.387  2.305   23.092  1.00 9.39  ? 208 TRP A NE1 1 
ATOM   1667 C  CE2 . TRP A 1 208 ? 13.612  1.705   22.115  1.00 9.37  ? 208 TRP A CE2 1 
ATOM   1668 C  CE3 . TRP A 1 208 ? 11.379  0.762   21.904  1.00 9.97  ? 208 TRP A CE3 1 
ATOM   1669 C  CZ2 . TRP A 1 208 ? 13.882  1.483   20.760  1.00 9.36  ? 208 TRP A CZ2 1 
ATOM   1670 C  CZ3 . TRP A 1 208 ? 11.676  0.471   20.583  1.00 9.73  ? 208 TRP A CZ3 1 
ATOM   1671 C  CH2 . TRP A 1 208 ? 12.895  0.860   20.005  1.00 9.32  ? 208 TRP A CH2 1 
ATOM   1672 N  N   . ILE A 1 209 ? 8.050   2.098   24.411  1.00 9.27  ? 209 ILE A N   1 
ATOM   1673 C  CA  . ILE A 1 209 ? 6.739   1.561   24.717  1.00 9.47  ? 209 ILE A CA  1 
ATOM   1674 C  C   . ILE A 1 209 ? 6.598   0.302   23.897  1.00 9.45  ? 209 ILE A C   1 
ATOM   1675 O  O   . ILE A 1 209 ? 6.511   0.402   22.686  1.00 9.83  ? 209 ILE A O   1 
ATOM   1676 C  CB  . ILE A 1 209 ? 5.662   2.610   24.413  1.00 10.95 ? 209 ILE A CB  1 
ATOM   1677 C  CG1 . ILE A 1 209 ? 5.919   3.875   25.232  1.00 12.09 ? 209 ILE A CG1 1 
ATOM   1678 C  CG2 . ILE A 1 209 ? 4.250   2.084   24.684  1.00 12.41 ? 209 ILE A CG2 1 
ATOM   1679 C  CD1 . ILE A 1 209 ? 5.065   5.061   24.799  1.00 13.19 ? 209 ILE A CD1 1 
ATOM   1680 N  N   . VAL A 1 210 ? 6.621   -0.870  24.556  1.00 9.76  ? 210 VAL A N   1 
ATOM   1681 C  CA  . VAL A 1 210 ? 6.661   -2.138  23.838  1.00 9.76  ? 210 VAL A CA  1 
ATOM   1682 C  C   . VAL A 1 210 ? 5.332   -2.854  24.083  1.00 10.44 ? 210 VAL A C   1 
ATOM   1683 O  O   . VAL A 1 210 ? 5.034   -3.175  25.243  1.00 12.13 ? 210 VAL A O   1 
ATOM   1684 C  CB  . VAL A 1 210 ? 7.842   -3.002  24.294  1.00 9.61  ? 210 VAL A CB  1 
ATOM   1685 C  CG1 . VAL A 1 210 ? 7.818   -4.315  23.499  1.00 10.56 ? 210 VAL A CG1 1 
ATOM   1686 C  CG2 . VAL A 1 210 ? 9.160   -2.267  24.005  1.00 10.39 ? 210 VAL A CG2 1 
ATOM   1687 N  N   . LEU A 1 211 ? 4.559   -3.101  23.016  1.00 10.48 ? 211 LEU A N   1 
ATOM   1688 C  CA  . LEU A 1 211 ? 3.249   -3.751  23.199  1.00 10.99 ? 211 LEU A CA  1 
ATOM   1689 C  C   . LEU A 1 211 ? 3.463   -5.219  23.560  1.00 10.87 ? 211 LEU A C   1 
ATOM   1690 O  O   . LEU A 1 211 ? 4.316   -5.914  23.006  1.00 12.35 ? 211 LEU A O   1 
ATOM   1691 C  CB  . LEU A 1 211 ? 2.432   -3.603  21.917  1.00 11.02 ? 211 LEU A CB  1 
ATOM   1692 C  CG  . LEU A 1 211 ? 2.040   -2.176  21.516  1.00 11.66 ? 211 LEU A CG  1 
ATOM   1693 C  CD1 . LEU A 1 211 ? 0.971   -2.205  20.393  1.00 13.06 ? 211 LEU A CD1 1 
ATOM   1694 C  CD2 . LEU A 1 211 ? 1.632   -1.355  22.737  1.00 12.49 ? 211 LEU A CD2 1 
ATOM   1695 N  N   . LYS A 1 212 ? 2.589   -5.703  24.473  1.00 11.95 ? 212 LYS A N   1 
ATOM   1696 C  CA  . LYS A 1 212 ? 2.664   -7.100  24.890  1.00 13.18 ? 212 LYS A CA  1 
ATOM   1697 C  C   . LYS A 1 212 ? 2.181   -8.049  23.796  1.00 12.78 ? 212 LYS A C   1 
ATOM   1698 O  O   . LYS A 1 212 ? 2.700   -9.144  23.625  1.00 14.15 ? 212 LYS A O   1 
ATOM   1699 C  CB  . LYS A 1 212 ? 1.852   -7.267  26.176  1.00 16.32 ? 212 LYS A CB  1 
ATOM   1700 C  CG  . LYS A 1 212 ? 1.552   -8.713  26.585  1.00 23.12 ? 212 LYS A CG  1 
ATOM   1701 C  CD  . LYS A 1 212 ? 0.456   -8.810  27.657  1.00 31.83 ? 212 LYS A CD  1 
ATOM   1702 C  CE  . LYS A 1 212 ? -0.740  -7.881  27.453  1.00 34.24 ? 212 LYS A CE  1 
ATOM   1703 N  NZ  . LYS A 1 212 ? -1.495  -8.080  26.179  1.00 39.38 ? 212 LYS A NZ  1 
ATOM   1704 N  N   . GLU A 1 213 ? 1.200   -7.632  23.006  1.00 12.05 ? 213 GLU A N   1 
ATOM   1705 C  CA  . GLU A 1 213 ? 0.596   -8.554  22.054  1.00 14.02 ? 213 GLU A CA  1 
ATOM   1706 C  C   . GLU A 1 213 ? 1.348   -8.463  20.739  1.00 11.97 ? 213 GLU A C   1 
ATOM   1707 O  O   . GLU A 1 213 ? 1.392   -7.399  20.118  1.00 11.71 ? 213 GLU A O   1 
ATOM   1708 C  CB  . GLU A 1 213 ? -0.869  -8.142  21.798  1.00 14.73 ? 213 GLU A CB  1 
ATOM   1709 C  CG  . GLU A 1 213 ? -1.594  -9.144  20.909  1.00 18.80 ? 213 GLU A CG  1 
ATOM   1710 C  CD  . GLU A 1 213 ? -3.068  -8.812  20.632  1.00 21.03 ? 213 GLU A CD  1 
ATOM   1711 O  OE1 . GLU A 1 213 ? -3.651  -8.016  21.350  1.00 20.80 ? 213 GLU A OE1 1 
ATOM   1712 O  OE2 . GLU A 1 213 ? -3.634  -9.456  19.727  1.00 33.46 ? 213 GLU A OE2 1 
ATOM   1713 N  N   A PRO A 1 214 ? 1.908   -9.569  20.219  0.50 11.41 ? 214 PRO A N   1 
ATOM   1714 N  N   B PRO A 1 214 ? 1.982   -9.544  20.268  0.50 12.35 ? 214 PRO A N   1 
ATOM   1715 C  CA  A PRO A 1 214 ? 2.574   -9.510  18.925  0.50 11.37 ? 214 PRO A CA  1 
ATOM   1716 C  CA  B PRO A 1 214 ? 2.643   -9.528  18.961  0.50 12.29 ? 214 PRO A CA  1 
ATOM   1717 C  C   A PRO A 1 214 ? 1.484   -9.410  17.858  0.50 11.72 ? 214 PRO A C   1 
ATOM   1718 C  C   B PRO A 1 214 ? 1.607   -9.622  17.832  0.50 12.68 ? 214 PRO A C   1 
ATOM   1719 O  O   A PRO A 1 214 ? 0.278   -9.645  18.098  0.50 12.04 ? 214 PRO A O   1 
ATOM   1720 O  O   B PRO A 1 214 ? 0.521   -10.194 18.015  0.50 13.57 ? 214 PRO A O   1 
ATOM   1721 C  CB  A PRO A 1 214 ? 3.246   -10.881 18.765  0.50 11.82 ? 214 PRO A CB  1 
ATOM   1722 C  CB  B PRO A 1 214 ? 3.533   -10.783 18.989  0.50 12.98 ? 214 PRO A CB  1 
ATOM   1723 C  CG  A PRO A 1 214 ? 2.357   -11.791 19.593  0.50 10.94 ? 214 PRO A CG  1 
ATOM   1724 C  CG  B PRO A 1 214 ? 3.443   -11.293 20.423  0.50 14.04 ? 214 PRO A CG  1 
ATOM   1725 C  CD  A PRO A 1 214 ? 1.850   -10.949 20.755  0.50 11.34 ? 214 PRO A CD  1 
ATOM   1726 C  CD  B PRO A 1 214 ? 2.102   -10.843 20.957  0.50 13.02 ? 214 PRO A CD  1 
ATOM   1727 N  N   . ILE A 1 215 ? 1.941   -9.055  16.665  1.00 11.89 ? 215 ILE A N   1 
ATOM   1728 C  CA  . ILE A 1 215 ? 1.132   -9.280  15.462  1.00 12.28 ? 215 ILE A CA  1 
ATOM   1729 C  C   . ILE A 1 215 ? 1.672   -10.495 14.759  1.00 11.78 ? 215 ILE A C   1 
ATOM   1730 O  O   . ILE A 1 215 ? 2.860   -10.868 14.853  1.00 12.60 ? 215 ILE A O   1 
ATOM   1731 C  CB  . ILE A 1 215 ? 1.103   -8.073  14.507  1.00 13.15 ? 215 ILE A CB  1 
ATOM   1732 C  CG1 . ILE A 1 215 ? 2.499   -7.681  13.981  1.00 13.91 ? 215 ILE A CG1 1 
ATOM   1733 C  CG2 . ILE A 1 215 ? 0.381   -6.907  15.206  1.00 14.31 ? 215 ILE A CG2 1 
ATOM   1734 C  CD1 . ILE A 1 215 ? 2.432   -6.669  12.788  1.00 12.71 ? 215 ILE A CD1 1 
ATOM   1735 N  N   A SER A 1 216 ? 0.759   -11.113 14.006  0.50 13.13 ? 216 SER A N   1 
ATOM   1736 N  N   B SER A 1 216 ? 0.769   -11.218 14.111  0.50 14.08 ? 216 SER A N   1 
ATOM   1737 C  CA  A SER A 1 216 ? 1.050   -12.291 13.203  0.50 12.67 ? 216 SER A CA  1 
ATOM   1738 C  CA  B SER A 1 216 ? 1.307   -12.332 13.350  0.50 14.02 ? 216 SER A CA  1 
ATOM   1739 C  C   A SER A 1 216 ? 1.343   -11.859 11.776  0.50 12.91 ? 216 SER A C   1 
ATOM   1740 C  C   B SER A 1 216 ? 1.372   -11.925 11.890  0.50 13.56 ? 216 SER A C   1 
ATOM   1741 O  O   A SER A 1 216 ? 0.547   -11.143 11.148  0.50 14.10 ? 216 SER A O   1 
ATOM   1742 O  O   B SER A 1 216 ? 0.483   -11.214 11.404  0.50 15.37 ? 216 SER A O   1 
ATOM   1743 C  CB  A SER A 1 216 ? -0.126  -13.254 13.280  0.50 13.13 ? 216 SER A CB  1 
ATOM   1744 C  CB  B SER A 1 216 ? 0.573   -13.609 13.613  0.50 15.84 ? 216 SER A CB  1 
ATOM   1745 O  OG  A SER A 1 216 ? -0.066  -13.994 14.482  0.50 15.42 ? 216 SER A OG  1 
ATOM   1746 O  OG  B SER A 1 216 ? -0.180  -14.010 12.496  0.50 21.21 ? 216 SER A OG  1 
ATOM   1747 N  N   . VAL A 1 217 ? 2.472   -12.337 11.246  1.00 13.13 ? 217 VAL A N   1 
ATOM   1748 C  CA  . VAL A 1 217 ? 2.735   -12.154 9.824   1.00 12.38 ? 217 VAL A CA  1 
ATOM   1749 C  C   . VAL A 1 217 ? 2.996   -13.500 9.161   1.00 12.74 ? 217 VAL A C   1 
ATOM   1750 O  O   . VAL A 1 217 ? 3.330   -14.460 9.854   1.00 13.56 ? 217 VAL A O   1 
ATOM   1751 C  CB  . VAL A 1 217 ? 3.911   -11.172 9.542   1.00 13.22 ? 217 VAL A CB  1 
ATOM   1752 C  CG1 . VAL A 1 217 ? 3.665   -9.837  10.247  1.00 15.09 ? 217 VAL A CG1 1 
ATOM   1753 C  CG2 . VAL A 1 217 ? 5.221   -11.775 10.028  1.00 14.63 ? 217 VAL A CG2 1 
ATOM   1754 N  N   . SER A 1 218 ? 2.825   -13.624 7.847   1.00 12.83 ? 218 SER A N   1 
ATOM   1755 C  CA  . SER A 1 218 ? 3.055   -14.948 7.287   1.00 14.95 ? 218 SER A CA  1 
ATOM   1756 C  C   . SER A 1 218 ? 4.528   -15.200 7.029   1.00 14.26 ? 218 SER A C   1 
ATOM   1757 O  O   . SER A 1 218 ? 5.349   -14.280 6.918   1.00 13.23 ? 218 SER A O   1 
ATOM   1758 C  CB  . SER A 1 218 ? 2.250   -15.148 6.043   1.00 15.26 ? 218 SER A CB  1 
ATOM   1759 O  OG  . SER A 1 218 ? 2.671   -14.264 5.017   1.00 15.03 ? 218 SER A OG  1 
ATOM   1760 N  N   A SER A 1 219 ? 4.866   -16.478 6.847   0.50 13.67 ? 219 SER A N   1 
ATOM   1761 N  N   B SER A 1 219 ? 4.864   -16.482 6.854   0.50 14.59 ? 219 SER A N   1 
ATOM   1762 C  CA  A SER A 1 219 ? 6.216   -16.845 6.489   0.50 13.94 ? 219 SER A CA  1 
ATOM   1763 C  CA  B SER A 1 219 ? 6.205   -16.862 6.471   0.50 15.44 ? 219 SER A CA  1 
ATOM   1764 C  C   A SER A 1 219 ? 6.625   -16.153 5.179   0.50 14.78 ? 219 SER A C   1 
ATOM   1765 C  C   B SER A 1 219 ? 6.616   -16.132 5.186   0.50 15.74 ? 219 SER A C   1 
ATOM   1766 O  O   A SER A 1 219 ? 7.762   -15.682 5.040   0.50 14.97 ? 219 SER A O   1 
ATOM   1767 O  O   B SER A 1 219 ? 7.747   -15.643 5.066   0.50 15.78 ? 219 SER A O   1 
ATOM   1768 C  CB  A SER A 1 219 ? 6.319   -18.354 6.477   0.50 14.41 ? 219 SER A CB  1 
ATOM   1769 C  CB  B SER A 1 219 ? 6.286   -18.363 6.359   0.50 17.43 ? 219 SER A CB  1 
ATOM   1770 O  OG  A SER A 1 219 ? 5.378   -18.906 5.578   0.50 13.87 ? 219 SER A OG  1 
ATOM   1771 O  OG  B SER A 1 219 ? 7.622   -18.752 6.080   0.50 19.86 ? 219 SER A OG  1 
ATOM   1772 N  N   . GLU A 1 220 ? 5.672   -16.006 4.245   1.00 15.46 ? 220 GLU A N   1 
ATOM   1773 C  CA  . GLU A 1 220 ? 5.948   -15.404 2.954   1.00 16.46 ? 220 GLU A CA  1 
ATOM   1774 C  C   . GLU A 1 220 ? 6.236   -13.907 3.104   1.00 15.16 ? 220 GLU A C   1 
ATOM   1775 O  O   . GLU A 1 220 ? 7.095   -13.387 2.385   1.00 15.82 ? 220 GLU A O   1 
ATOM   1776 C  CB  . GLU A 1 220 ? 4.776   -15.551 1.987   1.00 17.20 ? 220 GLU A CB  1 
ATOM   1777 C  CG  . GLU A 1 220 ? 4.596   -16.999 1.518   1.00 20.83 ? 220 GLU A CG  1 
ATOM   1778 C  CD  . GLU A 1 220 ? 3.873   -17.884 2.521   1.00 23.83 ? 220 GLU A CD  1 
ATOM   1779 O  OE1 . GLU A 1 220 ? 3.249   -17.372 3.474   1.00 22.37 ? 220 GLU A OE1 1 
ATOM   1780 O  OE2 . GLU A 1 220 ? 3.971   -19.159 2.374   1.00 30.79 ? 220 GLU A OE2 1 
ATOM   1781 N  N   . GLN A 1 221 ? 5.520   -13.247 4.027   1.00 13.32 ? 221 GLN A N   1 
ATOM   1782 C  CA  . GLN A 1 221 ? 5.772   -11.816 4.199   1.00 11.86 ? 221 GLN A CA  1 
ATOM   1783 C  C   . GLN A 1 221 ? 7.181   -11.574 4.765   1.00 13.65 ? 221 GLN A C   1 
ATOM   1784 O  O   . GLN A 1 221 ? 7.894   -10.698 4.286   1.00 12.94 ? 221 GLN A O   1 
ATOM   1785 C  CB  . GLN A 1 221 ? 4.728   -11.263 5.155   1.00 13.74 ? 221 GLN A CB  1 
ATOM   1786 C  CG  . GLN A 1 221 ? 3.400   -11.115 4.422   1.00 13.25 ? 221 GLN A CG  1 
ATOM   1787 C  CD  . GLN A 1 221 ? 2.271   -10.620 5.307   1.00 13.51 ? 221 GLN A CD  1 
ATOM   1788 O  OE1 . GLN A 1 221 ? 2.118   -11.019 6.464   1.00 12.65 ? 221 GLN A OE1 1 
ATOM   1789 N  NE2 . GLN A 1 221 ? 1.416   -9.747  4.790   1.00 13.92 ? 221 GLN A NE2 1 
ATOM   1790 N  N   . VAL A 1 222 ? 7.606   -12.358 5.769   1.00 12.91 ? 222 VAL A N   1 
ATOM   1791 C  CA  . VAL A 1 222 ? 8.928   -12.102 6.350   1.00 14.33 ? 222 VAL A CA  1 
ATOM   1792 C  C   . VAL A 1 222 ? 10.033  -12.557 5.398   1.00 16.08 ? 222 VAL A C   1 
ATOM   1793 O  O   . VAL A 1 222 ? 11.120  -11.991 5.327   1.00 15.57 ? 222 VAL A O   1 
ATOM   1794 C  CB  . VAL A 1 222 ? 9.058   -12.695 7.781   1.00 14.67 ? 222 VAL A CB  1 
ATOM   1795 C  CG1 . VAL A 1 222 ? 8.978   -14.198 7.783   1.00 17.23 ? 222 VAL A CG1 1 
ATOM   1796 C  CG2 . VAL A 1 222 ? 10.344  -12.202 8.475   1.00 17.60 ? 222 VAL A CG2 1 
ATOM   1797 N  N   . LEU A 1 223 ? 9.727   -13.587 4.601   1.00 16.05 ? 223 LEU A N   1 
ATOM   1798 C  CA  . LEU A 1 223 ? 10.650  -14.031 3.586   1.00 16.45 ? 223 LEU A CA  1 
ATOM   1799 C  C   . LEU A 1 223 ? 10.991  -12.890 2.642   1.00 16.14 ? 223 LEU A C   1 
ATOM   1800 O  O   . LEU A 1 223 ? 12.154  -12.779 2.236   1.00 16.66 ? 223 LEU A O   1 
ATOM   1801 C  CB  . LEU A 1 223 ? 9.968   -15.159 2.809   1.00 20.43 ? 223 LEU A CB  1 
ATOM   1802 C  CG  . LEU A 1 223 ? 10.905  -16.055 2.027   1.00 29.95 ? 223 LEU A CG  1 
ATOM   1803 C  CD1 . LEU A 1 223 ? 11.836  -16.775 2.998   1.00 29.26 ? 223 LEU A CD1 1 
ATOM   1804 C  CD2 . LEU A 1 223 ? 10.065  -17.074 1.258   1.00 30.69 ? 223 LEU A CD2 1 
ATOM   1805 N  N   . LYS A 1 224 ? 10.000  -12.042 2.338   1.00 15.94 ? 224 LYS A N   1 
ATOM   1806 C  CA  . LYS A 1 224 ? 10.225  -10.915 1.450   1.00 15.92 ? 224 LYS A CA  1 
ATOM   1807 C  C   . LYS A 1 224 ? 11.121  -9.866  2.106   1.00 15.49 ? 224 LYS A C   1 
ATOM   1808 O  O   . LYS A 1 224 ? 11.915  -9.217  1.422   1.00 16.00 ? 224 LYS A O   1 
ATOM   1809 C  CB  . LYS A 1 224 ? 8.898   -10.432 0.852   1.00 18.65 ? 224 LYS A CB  1 
ATOM   1810 C  CG  . LYS A 1 224 ? 8.255   -11.476 -0.070  1.00 23.00 ? 224 LYS A CG  1 
ATOM   1811 C  CD  . LYS A 1 224 ? 7.357   -10.964 -1.187  1.00 32.16 ? 224 LYS A CD  1 
ATOM   1812 C  CE  . LYS A 1 224 ? 6.640   -12.112 -1.895  1.00 33.45 ? 224 LYS A CE  1 
ATOM   1813 N  NZ  . LYS A 1 224 ? 5.377   -11.695 -2.560  1.00 39.63 ? 224 LYS A NZ  1 
ATOM   1814 N  N   . PHE A 1 225 ? 11.036  -9.697  3.440   1.00 12.58 ? 225 PHE A N   1 
ATOM   1815 C  CA  . PHE A 1 225 ? 11.983  -8.794  4.087   1.00 13.28 ? 225 PHE A CA  1 
ATOM   1816 C  C   . PHE A 1 225 ? 13.419  -9.250  3.849   1.00 12.08 ? 225 PHE A C   1 
ATOM   1817 O  O   . PHE A 1 225 ? 14.327  -8.441  3.694   1.00 12.53 ? 225 PHE A O   1 
ATOM   1818 C  CB  . PHE A 1 225 ? 11.827  -8.772  5.626   1.00 12.78 ? 225 PHE A CB  1 
ATOM   1819 C  CG  . PHE A 1 225 ? 10.605  -8.086  6.214   1.00 13.85 ? 225 PHE A CG  1 
ATOM   1820 C  CD1 . PHE A 1 225 ? 9.530   -7.633  5.445   1.00 12.76 ? 225 PHE A CD1 1 
ATOM   1821 C  CD2 . PHE A 1 225 ? 10.532  -7.928  7.588   1.00 13.83 ? 225 PHE A CD2 1 
ATOM   1822 C  CE1 . PHE A 1 225 ? 8.444   -6.993  6.037   1.00 15.69 ? 225 PHE A CE1 1 
ATOM   1823 C  CE2 . PHE A 1 225 ? 9.463   -7.282  8.196   1.00 14.26 ? 225 PHE A CE2 1 
ATOM   1824 C  CZ  . PHE A 1 225 ? 8.420   -6.804  7.410   1.00 15.35 ? 225 PHE A CZ  1 
ATOM   1825 N  N   . ARG A 1 226 ? 13.633  -10.577 3.851   1.00 12.64 ? 226 ARG A N   1 
ATOM   1826 C  CA  . ARG A 1 226 ? 14.961  -11.178 3.795   1.00 13.25 ? 226 ARG A CA  1 
ATOM   1827 C  C   . ARG A 1 226 ? 15.550  -11.189 2.386   1.00 14.38 ? 226 ARG A C   1 
ATOM   1828 O  O   . ARG A 1 226 ? 16.704  -11.581 2.243   1.00 16.39 ? 226 ARG A O   1 
ATOM   1829 C  CB  . ARG A 1 226 ? 14.885  -12.618 4.332   1.00 14.00 ? 226 ARG A CB  1 
ATOM   1830 C  CG  . ARG A 1 226 ? 14.372  -12.731 5.763   1.00 14.62 ? 226 ARG A CG  1 
ATOM   1831 C  CD  . ARG A 1 226 ? 14.512  -14.191 6.189   1.00 15.36 ? 226 ARG A CD  1 
ATOM   1832 N  NE  . ARG A 1 226 ? 13.917  -14.362 7.525   1.00 15.69 ? 226 ARG A NE  1 
ATOM   1833 C  CZ  . ARG A 1 226 ? 12.947  -15.229 7.819   1.00 15.70 ? 226 ARG A CZ  1 
ATOM   1834 N  NH1 . ARG A 1 226 ? 12.507  -16.085 6.908   1.00 17.73 ? 226 ARG A NH1 1 
ATOM   1835 N  NH2 . ARG A 1 226 ? 12.469  -15.304 9.041   1.00 13.42 ? 226 ARG A NH2 1 
ATOM   1836 N  N   . LYS A 1 227 ? 14.794  -10.677 1.406   1.00 14.61 ? 227 LYS A N   1 
ATOM   1837 C  CA  . LYS A 1 227 ? 15.309  -10.594 0.050   1.00 15.95 ? 227 LYS A CA  1 
ATOM   1838 C  C   . LYS A 1 227 ? 15.898  -9.207  -0.159  1.00 16.48 ? 227 LYS A C   1 
ATOM   1839 O  O   . LYS A 1 227 ? 16.589  -8.986  -1.153  1.00 18.76 ? 227 LYS A O   1 
ATOM   1840 C  CB  . LYS A 1 227 ? 14.151  -10.796 -0.924  1.00 16.16 ? 227 LYS A CB  1 
ATOM   1841 C  CG  . LYS A 1 227 ? 13.637  -12.225 -0.974  1.00 21.41 ? 227 LYS A CG  1 
ATOM   1842 C  CD  . LYS A 1 227 ? 12.674  -12.391 -2.145  1.00 28.76 ? 227 LYS A CD  1 
ATOM   1843 C  CE  . LYS A 1 227 ? 12.855  -13.686 -2.911  1.00 36.70 ? 227 LYS A CE  1 
ATOM   1844 N  NZ  . LYS A 1 227 ? 12.762  -13.465 -4.377  1.00 41.19 ? 227 LYS A NZ  1 
ATOM   1845 N  N   . LEU A 1 228 ? 15.659  -8.267  0.773   1.00 15.79 ? 228 LEU A N   1 
ATOM   1846 C  CA  . LEU A 1 228 ? 16.363  -7.002  0.685   1.00 12.98 ? 228 LEU A CA  1 
ATOM   1847 C  C   . LEU A 1 228 ? 17.856  -7.196  0.832   1.00 13.55 ? 228 LEU A C   1 
ATOM   1848 O  O   . LEU A 1 228 ? 18.355  -8.236  1.254   1.00 13.68 ? 228 LEU A O   1 
ATOM   1849 C  CB  . LEU A 1 228 ? 15.868  -6.078  1.798   1.00 13.82 ? 228 LEU A CB  1 
ATOM   1850 C  CG  . LEU A 1 228 ? 14.457  -5.552  1.585   1.00 14.12 ? 228 LEU A CG  1 
ATOM   1851 C  CD1 . LEU A 1 228 ? 13.964  -4.909  2.883   1.00 14.46 ? 228 LEU A CD1 1 
ATOM   1852 C  CD2 . LEU A 1 228 ? 14.379  -4.532  0.446   1.00 13.12 ? 228 LEU A CD2 1 
ATOM   1853 N  N   . ASN A 1 229 ? 18.584  -6.108  0.502   1.00 16.44 ? 229 ASN A N   1 
ATOM   1854 C  CA  . ASN A 1 229 ? 20.027  -6.099  0.453   1.00 15.61 ? 229 ASN A CA  1 
ATOM   1855 C  C   . ASN A 1 229 ? 20.564  -4.930  1.288   1.00 16.19 ? 229 ASN A C   1 
ATOM   1856 O  O   . ASN A 1 229 ? 20.069  -3.813  1.174   1.00 17.77 ? 229 ASN A O   1 
ATOM   1857 C  CB  . ASN A 1 229 ? 20.542  -5.884  -0.983  1.00 18.07 ? 229 ASN A CB  1 
ATOM   1858 C  CG  . ASN A 1 229 ? 20.549  -7.107  -1.884  1.00 22.99 ? 229 ASN A CG  1 
ATOM   1859 O  OD1 . ASN A 1 229 ? 21.167  -7.034  -2.963  1.00 23.04 ? 229 ASN A OD1 1 
ATOM   1860 N  ND2 . ASN A 1 229 ? 19.893  -8.204  -1.504  1.00 19.21 ? 229 ASN A ND2 1 
ATOM   1861 N  N   . PHE A 1 230 ? 21.611  -5.252  2.027   1.00 15.74 ? 230 PHE A N   1 
ATOM   1862 C  CA  . PHE A 1 230 ? 22.366  -4.224  2.745   1.00 18.03 ? 230 PHE A CA  1 
ATOM   1863 C  C   . PHE A 1 230 ? 23.186  -3.362  1.792   1.00 20.00 ? 230 PHE A C   1 
ATOM   1864 O  O   . PHE A 1 230 ? 23.351  -2.155  2.021   1.00 17.85 ? 230 PHE A O   1 
ATOM   1865 C  CB  . PHE A 1 230 ? 23.355  -4.840  3.723   1.00 17.39 ? 230 PHE A CB  1 
ATOM   1866 C  CG  . PHE A 1 230 ? 22.870  -5.439  5.032   1.00 15.87 ? 230 PHE A CG  1 
ATOM   1867 C  CD1 . PHE A 1 230 ? 22.081  -4.728  5.925   1.00 17.10 ? 230 PHE A CD1 1 
ATOM   1868 C  CD2 . PHE A 1 230 ? 23.210  -6.738  5.375   1.00 17.13 ? 230 PHE A CD2 1 
ATOM   1869 C  CE1 . PHE A 1 230 ? 21.689  -5.286  7.144   1.00 17.32 ? 230 PHE A CE1 1 
ATOM   1870 C  CE2 . PHE A 1 230 ? 22.774  -7.323  6.565   1.00 15.90 ? 230 PHE A CE2 1 
ATOM   1871 C  CZ  . PHE A 1 230 ? 22.038  -6.577  7.461   1.00 16.31 ? 230 PHE A CZ  1 
ATOM   1872 N  N   . ASN A 1 231 ? 23.655  -3.995  0.717   1.00 19.68 ? 231 ASN A N   1 
ATOM   1873 C  CA  . ASN A 1 231 ? 24.537  -3.347  -0.246  1.00 19.32 ? 231 ASN A CA  1 
ATOM   1874 C  C   . ASN A 1 231 ? 23.760  -2.448  -1.205  1.00 18.50 ? 231 ASN A C   1 
ATOM   1875 O  O   . ASN A 1 231 ? 22.544  -2.543  -1.391  1.00 17.41 ? 231 ASN A O   1 
ATOM   1876 C  CB  . ASN A 1 231 ? 25.215  -4.437  -1.069  1.00 17.67 ? 231 ASN A CB  1 
ATOM   1877 C  CG  . ASN A 1 231 ? 24.207  -5.356  -1.724  1.00 18.68 ? 231 ASN A CG  1 
ATOM   1878 O  OD1 . ASN A 1 231 ? 23.667  -6.228  -1.055  1.00 22.92 ? 231 ASN A OD1 1 
ATOM   1879 N  ND2 . ASN A 1 231 ? 23.874  -5.171  -3.001  1.00 18.05 ? 231 ASN A ND2 1 
ATOM   1880 N  N   . GLY A 1 232 ? 24.514  -1.527  -1.849  1.00 18.66 ? 232 GLY A N   1 
ATOM   1881 C  CA  . GLY A 1 232 ? 23.931  -0.714  -2.911  1.00 18.71 ? 232 GLY A CA  1 
ATOM   1882 C  C   . GLY A 1 232 ? 23.955  -1.447  -4.247  1.00 19.26 ? 232 GLY A C   1 
ATOM   1883 O  O   . GLY A 1 232 ? 24.679  -2.436  -4.353  1.00 19.01 ? 232 GLY A O   1 
ATOM   1884 N  N   . GLU A 1 233 ? 23.121  -0.982  -5.198  1.00 19.62 ? 233 GLU A N   1 
ATOM   1885 C  CA  . GLU A 1 233 ? 23.119  -1.532  -6.546  1.00 21.26 ? 233 GLU A CA  1 
ATOM   1886 C  C   . GLU A 1 233 ? 24.546  -1.572  -7.080  1.00 20.66 ? 233 GLU A C   1 
ATOM   1887 O  O   . GLU A 1 233 ? 25.312  -0.613  -6.930  1.00 20.50 ? 233 GLU A O   1 
ATOM   1888 C  CB  . GLU A 1 233 ? 22.213  -0.719  -7.462  1.00 21.84 ? 233 GLU A CB  1 
ATOM   1889 C  CG  . GLU A 1 233 ? 22.004  -1.386  -8.813  1.00 24.90 ? 233 GLU A CG  1 
ATOM   1890 C  CD  . GLU A 1 233 ? 21.113  -0.606  -9.748  1.00 33.36 ? 233 GLU A CD  1 
ATOM   1891 O  OE1 . GLU A 1 233 ? 20.753  0.543   -9.385  1.00 34.02 ? 233 GLU A OE1 1 
ATOM   1892 O  OE2 . GLU A 1 233 ? 20.847  -1.118  -10.873 1.00 38.33 ? 233 GLU A OE2 1 
ATOM   1893 N  N   . GLY A 1 234 ? 24.864  -2.707  -7.707  1.00 20.31 ? 234 GLY A N   1 
ATOM   1894 C  CA  . GLY A 1 234 ? 26.122  -2.866  -8.410  1.00 25.70 ? 234 GLY A CA  1 
ATOM   1895 C  C   . GLY A 1 234 ? 27.269  -3.195  -7.466  1.00 27.69 ? 234 GLY A C   1 
ATOM   1896 O  O   . GLY A 1 234 ? 28.447  -3.104  -7.840  1.00 27.84 ? 234 GLY A O   1 
ATOM   1897 N  N   . GLU A 1 235 ? 26.921  -3.511  -6.210  1.00 25.87 ? 235 GLU A N   1 
ATOM   1898 C  CA  . GLU A 1 235 ? 27.917  -3.989  -5.265  1.00 24.41 ? 235 GLU A CA  1 
ATOM   1899 C  C   . GLU A 1 235 ? 27.513  -5.418  -4.956  1.00 23.79 ? 235 GLU A C   1 
ATOM   1900 O  O   . GLU A 1 235 ? 26.366  -5.792  -5.177  1.00 24.14 ? 235 GLU A O   1 
ATOM   1901 C  CB  . GLU A 1 235 ? 27.902  -3.211  -3.942  1.00 23.78 ? 235 GLU A CB  1 
ATOM   1902 C  CG  . GLU A 1 235 ? 28.329  -1.763  -4.030  1.00 26.69 ? 235 GLU A CG  1 
ATOM   1903 C  CD  . GLU A 1 235 ? 28.073  -0.972  -2.755  1.00 34.88 ? 235 GLU A CD  1 
ATOM   1904 O  OE1 . GLU A 1 235 ? 27.201  -1.404  -1.954  1.00 27.35 ? 235 GLU A OE1 1 
ATOM   1905 O  OE2 . GLU A 1 235 ? 28.783  0.043   -2.517  1.00 38.14 ? 235 GLU A OE2 1 
ATOM   1906 N  N   . PRO A 1 236 ? 28.410  -6.243  -4.378  1.00 23.64 ? 236 PRO A N   1 
ATOM   1907 C  CA  . PRO A 1 236 ? 28.106  -7.646  -4.133  1.00 22.08 ? 236 PRO A CA  1 
ATOM   1908 C  C   . PRO A 1 236 ? 26.933  -7.822  -3.166  1.00 22.57 ? 236 PRO A C   1 
ATOM   1909 O  O   . PRO A 1 236 ? 26.769  -7.003  -2.247  1.00 21.83 ? 236 PRO A O   1 
ATOM   1910 C  CB  . PRO A 1 236 ? 29.355  -8.197  -3.446  1.00 24.36 ? 236 PRO A CB  1 
ATOM   1911 C  CG  . PRO A 1 236 ? 30.463  -7.209  -3.794  1.00 23.65 ? 236 PRO A CG  1 
ATOM   1912 C  CD  . PRO A 1 236 ? 29.773  -5.866  -3.958  1.00 26.50 ? 236 PRO A CD  1 
ATOM   1913 N  N   . GLU A 1 237 ? 26.162  -8.896  -3.393  1.00 20.68 ? 237 GLU A N   1 
ATOM   1914 C  CA  . GLU A 1 237 ? 24.888  -9.086  -2.722  1.00 21.31 ? 237 GLU A CA  1 
ATOM   1915 C  C   . GLU A 1 237 ? 25.128  -9.547  -1.292  1.00 19.89 ? 237 GLU A C   1 
ATOM   1916 O  O   . GLU A 1 237 ? 25.662  -10.608 -1.044  1.00 18.14 ? 237 GLU A O   1 
ATOM   1917 C  CB  . GLU A 1 237 ? 23.947  -10.069 -3.434  1.00 21.83 ? 237 GLU A CB  1 
ATOM   1918 C  CG  . GLU A 1 237 ? 22.611  -10.206 -2.668  1.00 24.67 ? 237 GLU A CG  1 
ATOM   1919 C  CD  . GLU A 1 237 ? 21.444  -10.907 -3.368  1.00 27.32 ? 237 GLU A CD  1 
ATOM   1920 O  OE1 . GLU A 1 237 ? 21.682  -11.929 -4.011  1.00 33.95 ? 237 GLU A OE1 1 
ATOM   1921 O  OE2 . GLU A 1 237 ? 20.304  -10.419 -3.269  1.00 24.81 ? 237 GLU A OE2 1 
ATOM   1922 N  N   . GLU A 1 238 ? 24.587  -8.765  -0.357  1.00 19.60 ? 238 GLU A N   1 
ATOM   1923 C  CA  . GLU A 1 238 ? 24.559  -9.170  1.044   1.00 19.53 ? 238 GLU A CA  1 
ATOM   1924 C  C   . GLU A 1 238 ? 23.119  -9.060  1.553   1.00 14.73 ? 238 GLU A C   1 
ATOM   1925 O  O   . GLU A 1 238 ? 22.576  -7.959  1.595   1.00 18.23 ? 238 GLU A O   1 
ATOM   1926 C  CB  . GLU A 1 238 ? 25.444  -8.255  1.901   1.00 21.07 ? 238 GLU A CB  1 
ATOM   1927 N  N   . LEU A 1 239 ? 22.507  -10.225 1.815   1.00 15.15 ? 239 LEU A N   1 
ATOM   1928 C  CA  . LEU A 1 239 ? 21.089  -10.187 2.175   1.00 13.75 ? 239 LEU A CA  1 
ATOM   1929 C  C   . LEU A 1 239 ? 20.942  -9.400  3.488   1.00 13.19 ? 239 LEU A C   1 
ATOM   1930 O  O   . LEU A 1 239 ? 21.681  -9.665  4.447   1.00 14.75 ? 239 LEU A O   1 
ATOM   1931 C  CB  . LEU A 1 239 ? 20.553  -11.615 2.344   1.00 14.49 ? 239 LEU A CB  1 
ATOM   1932 C  CG  . LEU A 1 239 ? 20.481  -12.452 1.069   1.00 15.79 ? 239 LEU A CG  1 
ATOM   1933 C  CD1 . LEU A 1 239 ? 19.951  -13.828 1.438   1.00 16.99 ? 239 LEU A CD1 1 
ATOM   1934 C  CD2 . LEU A 1 239 ? 19.558  -11.793 0.054   1.00 15.95 ? 239 LEU A CD2 1 
ATOM   1935 N  N   . MET A 1 240 ? 19.900  -8.564  3.498   1.00 12.84 ? 240 MET A N   1 
ATOM   1936 C  CA  . MET A 1 240 ? 19.559  -7.795  4.700   1.00 13.69 ? 240 MET A CA  1 
ATOM   1937 C  C   . MET A 1 240 ? 18.775  -8.708  5.638   1.00 13.17 ? 240 MET A C   1 
ATOM   1938 O  O   . MET A 1 240 ? 17.563  -8.876  5.523   1.00 14.11 ? 240 MET A O   1 
ATOM   1939 C  CB  . MET A 1 240 ? 18.809  -6.506  4.354   1.00 14.34 ? 240 MET A CB  1 
ATOM   1940 C  CG  . MET A 1 240 ? 18.452  -5.607  5.575   1.00 14.08 ? 240 MET A CG  1 
ATOM   1941 S  SD  . MET A 1 240 ? 17.543  -4.178  5.103   1.00 15.73 ? 240 MET A SD  1 
ATOM   1942 C  CE  . MET A 1 240 ? 18.797  -3.170  4.282   1.00 13.85 ? 240 MET A CE  1 
ATOM   1943 N  N   . VAL A 1 241 ? 19.512  -9.308  6.569   1.00 11.13 ? 241 VAL A N   1 
ATOM   1944 C  CA  . VAL A 1 241 ? 18.996  -10.209 7.591   1.00 12.77 ? 241 VAL A CA  1 
ATOM   1945 C  C   . VAL A 1 241 ? 19.781  -9.967  8.870   1.00 13.37 ? 241 VAL A C   1 
ATOM   1946 O  O   . VAL A 1 241 ? 20.949  -9.569  8.856   1.00 13.07 ? 241 VAL A O   1 
ATOM   1947 C  CB  . VAL A 1 241 ? 19.039  -11.709 7.225   1.00 12.85 ? 241 VAL A CB  1 
ATOM   1948 C  CG1 . VAL A 1 241 ? 18.166  -11.947 6.010   1.00 12.61 ? 241 VAL A CG1 1 
ATOM   1949 C  CG2 . VAL A 1 241 ? 20.465  -12.201 7.005   1.00 13.16 ? 241 VAL A CG2 1 
ATOM   1950 N  N   . ASP A 1 242 ? 19.140  -10.245 10.009  1.00 11.84 ? 242 ASP A N   1 
ATOM   1951 C  CA  . ASP A 1 242 ? 19.809  -10.125 11.308  1.00 13.17 ? 242 ASP A CA  1 
ATOM   1952 C  C   . ASP A 1 242 ? 20.279  -8.713  11.581  1.00 12.59 ? 242 ASP A C   1 
ATOM   1953 O  O   . ASP A 1 242 ? 21.387  -8.494  12.049  1.00 14.20 ? 242 ASP A O   1 
ATOM   1954 C  CB  . ASP A 1 242 ? 20.880  -11.185 11.576  1.00 11.49 ? 242 ASP A CB  1 
ATOM   1955 C  CG  . ASP A 1 242 ? 20.274  -12.574 11.607  1.00 13.92 ? 242 ASP A CG  1 
ATOM   1956 O  OD1 . ASP A 1 242 ? 19.192  -12.746 12.231  1.00 13.10 ? 242 ASP A OD1 1 
ATOM   1957 O  OD2 . ASP A 1 242 ? 20.910  -13.515 10.993  1.00 14.34 ? 242 ASP A OD2 1 
ATOM   1958 N  N   . ASN A 1 243 ? 19.413  -7.753  11.282  1.00 11.61 ? 243 ASN A N   1 
ATOM   1959 C  CA  . ASN A 1 243 ? 19.746  -6.346  11.532  1.00 11.82 ? 243 ASN A CA  1 
ATOM   1960 C  C   . ASN A 1 243 ? 19.152  -5.918  12.872  1.00 11.41 ? 243 ASN A C   1 
ATOM   1961 O  O   . ASN A 1 243 ? 18.436  -4.915  12.954  1.00 11.60 ? 243 ASN A O   1 
ATOM   1962 C  CB  . ASN A 1 243 ? 19.220  -5.452  10.386  1.00 12.47 ? 243 ASN A CB  1 
ATOM   1963 C  CG  . ASN A 1 243 ? 17.738  -5.596  10.089  1.00 12.81 ? 243 ASN A CG  1 
ATOM   1964 O  OD1 . ASN A 1 243 ? 17.091  -6.521  10.611  1.00 13.78 ? 243 ASN A OD1 1 
ATOM   1965 N  ND2 . ASN A 1 243 ? 17.162  -4.699  9.294   1.00 14.35 ? 243 ASN A ND2 1 
ATOM   1966 N  N   . TRP A 1 244 ? 19.400  -6.703  13.916  1.00 10.51 ? 244 TRP A N   1 
ATOM   1967 C  CA  . TRP A 1 244 ? 18.925  -6.432  15.273  1.00 10.91 ? 244 TRP A CA  1 
ATOM   1968 C  C   . TRP A 1 244 ? 20.104  -6.328  16.208  1.00 11.55 ? 244 TRP A C   1 
ATOM   1969 O  O   . TRP A 1 244 ? 21.073  -7.055  16.044  1.00 11.93 ? 244 TRP A O   1 
ATOM   1970 C  CB  . TRP A 1 244 ? 17.936  -7.521  15.752  1.00 10.97 ? 244 TRP A CB  1 
ATOM   1971 C  CG  . TRP A 1 244 ? 18.417  -8.948  15.534  1.00 10.26 ? 244 TRP A CG  1 
ATOM   1972 C  CD1 . TRP A 1 244 ? 18.303  -9.686  14.393  1.00 10.64 ? 244 TRP A CD1 1 
ATOM   1973 C  CD2 . TRP A 1 244 ? 18.971  -9.831  16.529  1.00 10.72 ? 244 TRP A CD2 1 
ATOM   1974 N  NE1 . TRP A 1 244 ? 18.783  -10.941 14.608  1.00 9.93  ? 244 TRP A NE1 1 
ATOM   1975 C  CE2 . TRP A 1 244 ? 19.214  -11.066 15.896  1.00 11.23 ? 244 TRP A CE2 1 
ATOM   1976 C  CE3 . TRP A 1 244 ? 19.321  -9.690  17.880  1.00 11.55 ? 244 TRP A CE3 1 
ATOM   1977 C  CZ2 . TRP A 1 244 ? 19.800  -12.149 16.567  1.00 11.65 ? 244 TRP A CZ2 1 
ATOM   1978 C  CZ3 . TRP A 1 244 ? 19.849  -10.768 18.555  1.00 12.25 ? 244 TRP A CZ3 1 
ATOM   1979 C  CH2 . TRP A 1 244 ? 20.086  -11.982 17.899  1.00 12.08 ? 244 TRP A CH2 1 
ATOM   1980 N  N   . ARG A 1 245 ? 19.985  -5.435  17.194  1.00 10.65 ? 245 ARG A N   1 
ATOM   1981 C  CA  . ARG A 1 245 ? 20.967  -5.372  18.269  1.00 10.64 ? 245 ARG A CA  1 
ATOM   1982 C  C   . ARG A 1 245 ? 20.503  -6.299  19.397  1.00 11.11 ? 245 ARG A C   1 
ATOM   1983 O  O   . ARG A 1 245 ? 19.336  -6.327  19.760  1.00 11.91 ? 245 ARG A O   1 
ATOM   1984 C  CB  . ARG A 1 245 ? 21.038  -3.956  18.854  1.00 11.09 ? 245 ARG A CB  1 
ATOM   1985 C  CG  . ARG A 1 245 ? 22.192  -3.779  19.834  1.00 10.91 ? 245 ARG A CG  1 
ATOM   1986 C  CD  . ARG A 1 245 ? 22.101  -2.383  20.409  1.00 13.51 ? 245 ARG A CD  1 
ATOM   1987 N  NE  . ARG A 1 245 ? 23.337  -2.054  21.156  1.00 12.18 ? 245 ARG A NE  1 
ATOM   1988 C  CZ  . ARG A 1 245 ? 23.521  -1.050  22.016  1.00 13.28 ? 245 ARG A CZ  1 
ATOM   1989 N  NH1 . ARG A 1 245 ? 22.507  -0.264  22.392  1.00 12.81 ? 245 ARG A NH1 1 
ATOM   1990 N  NH2 . ARG A 1 245 ? 24.767  -0.792  22.447  1.00 13.42 ? 245 ARG A NH2 1 
ATOM   1991 N  N   . PRO A 1 246 ? 21.374  -7.078  20.038  1.00 11.56 ? 246 PRO A N   1 
ATOM   1992 C  CA  . PRO A 1 246 ? 20.961  -7.970  21.109  1.00 11.95 ? 246 PRO A CA  1 
ATOM   1993 C  C   . PRO A 1 246 ? 20.673  -7.159  22.367  1.00 11.43 ? 246 PRO A C   1 
ATOM   1994 O  O   . PRO A 1 246 ? 21.018  -5.981  22.485  1.00 12.63 ? 246 PRO A O   1 
ATOM   1995 C  CB  . PRO A 1 246 ? 22.252  -8.751  21.468  1.00 14.00 ? 246 PRO A CB  1 
ATOM   1996 C  CG  . PRO A 1 246 ? 23.140  -8.560  20.256  1.00 16.52 ? 246 PRO A CG  1 
ATOM   1997 C  CD  . PRO A 1 246 ? 22.794  -7.213  19.652  1.00 13.14 ? 246 PRO A CD  1 
ATOM   1998 N  N   . ALA A 1 247 ? 19.991  -7.788  23.325  1.00 12.27 ? 247 ALA A N   1 
ATOM   1999 C  CA  . ALA A 1 247 ? 19.646  -7.139  24.575  1.00 11.23 ? 247 ALA A CA  1 
ATOM   2000 C  C   . ALA A 1 247 ? 20.896  -6.633  25.307  1.00 11.65 ? 247 ALA A C   1 
ATOM   2001 O  O   . ALA A 1 247 ? 21.929  -7.331  25.414  1.00 13.86 ? 247 ALA A O   1 
ATOM   2002 C  CB  . ALA A 1 247 ? 18.858  -8.118  25.444  1.00 13.61 ? 247 ALA A CB  1 
ATOM   2003 N  N   . GLN A 1 248 ? 20.719  -5.463  25.890  1.00 12.08 ? 248 GLN A N   1 
ATOM   2004 C  CA  . GLN A 1 248 ? 21.759  -4.751  26.621  1.00 12.46 ? 248 GLN A CA  1 
ATOM   2005 C  C   . GLN A 1 248 ? 21.487  -4.782  28.114  1.00 14.20 ? 248 GLN A C   1 
ATOM   2006 O  O   . GLN A 1 248 ? 20.352  -4.998  28.520  1.00 13.12 ? 248 GLN A O   1 
ATOM   2007 C  CB  . GLN A 1 248 ? 21.855  -3.310  26.126  1.00 13.60 ? 248 GLN A CB  1 
ATOM   2008 C  CG  . GLN A 1 248 ? 22.152  -3.235  24.619  1.00 11.99 ? 248 GLN A CG  1 
ATOM   2009 C  CD  . GLN A 1 248 ? 23.474  -3.913  24.291  1.00 14.27 ? 248 GLN A CD  1 
ATOM   2010 O  OE1 . GLN A 1 248 ? 24.531  -3.598  24.881  1.00 16.35 ? 248 GLN A OE1 1 
ATOM   2011 N  NE2 . GLN A 1 248 ? 23.421  -4.893  23.388  1.00 14.80 ? 248 GLN A NE2 1 
ATOM   2012 N  N   . PRO A 1 249 ? 22.487  -4.491  28.989  1.00 15.48 ? 249 PRO A N   1 
ATOM   2013 C  CA  . PRO A 1 249 ? 22.247  -4.565  30.428  1.00 15.64 ? 249 PRO A CA  1 
ATOM   2014 C  C   . PRO A 1 249 ? 21.184  -3.570  30.916  1.00 15.91 ? 249 PRO A C   1 
ATOM   2015 O  O   . PRO A 1 249 ? 21.199  -2.408  30.518  1.00 15.85 ? 249 PRO A O   1 
ATOM   2016 C  CB  . PRO A 1 249 ? 23.644  -4.174  30.969  1.00 18.07 ? 249 PRO A CB  1 
ATOM   2017 C  CG  . PRO A 1 249 ? 24.575  -4.651  29.893  1.00 19.26 ? 249 PRO A CG  1 
ATOM   2018 C  CD  . PRO A 1 249 ? 23.884  -4.161  28.640  1.00 17.32 ? 249 PRO A CD  1 
ATOM   2019 N  N   . LEU A 1 250 ? 20.269  -4.075  31.753  1.00 15.43 ? 250 LEU A N   1 
ATOM   2020 C  CA  . LEU A 1 250 ? 19.204  -3.200  32.250  1.00 14.36 ? 250 LEU A CA  1 
ATOM   2021 C  C   . LEU A 1 250 ? 19.768  -2.115  33.172  1.00 17.22 ? 250 LEU A C   1 
ATOM   2022 O  O   . LEU A 1 250 ? 19.235  -1.000  33.267  1.00 14.95 ? 250 LEU A O   1 
ATOM   2023 C  CB  . LEU A 1 250 ? 18.120  -4.078  32.856  1.00 16.18 ? 250 LEU A CB  1 
ATOM   2024 C  CG  . LEU A 1 250 ? 16.871  -3.332  33.290  1.00 15.95 ? 250 LEU A CG  1 
ATOM   2025 C  CD1 . LEU A 1 250 ? 16.128  -2.714  32.092  1.00 15.81 ? 250 LEU A CD1 1 
ATOM   2026 C  CD2 . LEU A 1 250 ? 15.956  -4.249  34.073  1.00 18.97 ? 250 LEU A CD2 1 
ATOM   2027 N  N   . LYS A 1 251 ? 20.868  -2.440  33.857  1.00 18.63 ? 251 LYS A N   1 
ATOM   2028 C  CA  . LYS A 1 251 ? 21.495  -1.479  34.781  1.00 17.94 ? 251 LYS A CA  1 
ATOM   2029 C  C   . LYS A 1 251 ? 20.468  -1.151  35.874  1.00 19.34 ? 251 LYS A C   1 
ATOM   2030 O  O   . LYS A 1 251 ? 19.878  -2.076  36.420  1.00 25.75 ? 251 LYS A O   1 
ATOM   2031 C  CB  . LYS A 1 251 ? 22.196  -0.356  34.000  1.00 19.59 ? 251 LYS A CB  1 
ATOM   2032 C  CG  . LYS A 1 251 ? 23.133  -0.845  32.891  1.00 22.38 ? 251 LYS A CG  1 
ATOM   2033 C  CD  . LYS A 1 251 ? 24.520  -0.198  32.849  1.00 27.76 ? 251 LYS A CD  1 
ATOM   2034 C  CE  . LYS A 1 251 ? 25.592  -1.001  32.162  1.00 28.77 ? 251 LYS A CE  1 
ATOM   2035 N  NZ  . LYS A 1 251 ? 26.294  -0.122  31.198  1.00 30.76 ? 251 LYS A NZ  1 
ATOM   2036 N  N   . ASN A 1 252 ? 20.262  0.111   36.200  1.00 22.39 ? 252 ASN A N   1 
ATOM   2037 C  CA  . ASN A 1 252 ? 19.455  0.280   37.401  1.00 27.07 ? 252 ASN A CA  1 
ATOM   2038 C  C   . ASN A 1 252 ? 17.953  0.387   37.069  1.00 26.70 ? 252 ASN A C   1 
ATOM   2039 O  O   . ASN A 1 252 ? 17.140  0.630   37.951  1.00 29.20 ? 252 ASN A O   1 
ATOM   2040 C  CB  . ASN A 1 252 ? 20.031  1.369   38.313  1.00 33.79 ? 252 ASN A CB  1 
ATOM   2041 C  CG  . ASN A 1 252 ? 21.389  0.988   38.871  1.00 43.01 ? 252 ASN A CG  1 
ATOM   2042 O  OD1 . ASN A 1 252 ? 22.329  1.786   38.835  1.00 52.52 ? 252 ASN A OD1 1 
ATOM   2043 N  ND2 . ASN A 1 252 ? 21.516  -0.242  39.345  1.00 41.56 ? 252 ASN A ND2 1 
ATOM   2044 N  N   . ARG A 1 253 ? 17.580  0.226   35.791  1.00 17.76 ? 253 ARG A N   1 
ATOM   2045 C  CA  . ARG A 1 253 ? 16.293  0.704   35.320  1.00 15.73 ? 253 ARG A CA  1 
ATOM   2046 C  C   . ARG A 1 253 ? 15.178  -0.248  35.735  1.00 16.22 ? 253 ARG A C   1 
ATOM   2047 O  O   . ARG A 1 253 ? 15.397  -1.433  35.949  1.00 18.81 ? 253 ARG A O   1 
ATOM   2048 C  CB  . ARG A 1 253 ? 16.332  0.824   33.783  1.00 14.48 ? 253 ARG A CB  1 
ATOM   2049 C  CG  . ARG A 1 253 ? 17.186  1.966   33.259  1.00 14.95 ? 253 ARG A CG  1 
ATOM   2050 C  CD  . ARG A 1 253 ? 17.242  1.847   31.748  1.00 16.23 ? 253 ARG A CD  1 
ATOM   2051 N  NE  . ARG A 1 253 ? 18.100  0.736   31.338  1.00 13.67 ? 253 ARG A NE  1 
ATOM   2052 C  CZ  . ARG A 1 253 ? 18.377  0.473   30.054  1.00 11.60 ? 253 ARG A CZ  1 
ATOM   2053 N  NH1 . ARG A 1 253 ? 17.765  1.182   29.104  1.00 11.33 ? 253 ARG A NH1 1 
ATOM   2054 N  NH2 . ARG A 1 253 ? 19.203  -0.524  29.724  1.00 11.56 ? 253 ARG A NH2 1 
ATOM   2055 N  N   . GLN A 1 254 ? 13.957  0.278   35.799  1.00 15.93 ? 254 GLN A N   1 
ATOM   2056 C  CA  . GLN A 1 254 ? 12.736  -0.457  36.060  1.00 17.40 ? 254 GLN A CA  1 
ATOM   2057 C  C   . GLN A 1 254 ? 11.917  -0.456  34.773  1.00 16.17 ? 254 GLN A C   1 
ATOM   2058 O  O   . GLN A 1 254 ? 11.837  0.587   34.126  1.00 19.35 ? 254 GLN A O   1 
ATOM   2059 C  CB  . GLN A 1 254 ? 11.956  0.350   37.101  1.00 23.22 ? 254 GLN A CB  1 
ATOM   2060 C  CG  . GLN A 1 254 ? 10.775  -0.377  37.724  1.00 34.43 ? 254 GLN A CG  1 
ATOM   2061 C  CD  . GLN A 1 254 ? 10.959  -0.538  39.216  1.00 45.55 ? 254 GLN A CD  1 
ATOM   2062 O  OE1 . GLN A 1 254 ? 11.502  0.334   39.904  1.00 52.59 ? 254 GLN A OE1 1 
ATOM   2063 N  NE2 . GLN A 1 254 ? 10.516  -1.675  39.725  1.00 40.51 ? 254 GLN A NE2 1 
ATOM   2064 N  N   . ILE A 1 255 ? 11.404  -1.618  34.394  1.00 14.90 ? 255 ILE A N   1 
ATOM   2065 C  CA  . ILE A 1 255 ? 10.382  -1.727  33.373  1.00 14.97 ? 255 ILE A CA  1 
ATOM   2066 C  C   . ILE A 1 255 ? 9.012   -1.709  34.042  1.00 15.41 ? 255 ILE A C   1 
ATOM   2067 O  O   . ILE A 1 255 ? 8.784   -2.419  35.026  1.00 16.02 ? 255 ILE A O   1 
ATOM   2068 C  CB  . ILE A 1 255 ? 10.585  -2.987  32.507  1.00 12.90 ? 255 ILE A CB  1 
ATOM   2069 C  CG1 . ILE A 1 255 ? 12.034  -3.029  31.965  1.00 14.68 ? 255 ILE A CG1 1 
ATOM   2070 C  CG2 . ILE A 1 255 ? 9.492   -3.066  31.418  1.00 14.43 ? 255 ILE A CG2 1 
ATOM   2071 C  CD1 . ILE A 1 255 ? 12.320  -4.231  31.056  1.00 14.38 ? 255 ILE A CD1 1 
ATOM   2072 N  N   . LYS A 1 256 ? 8.157   -0.805  33.572  1.00 14.26 ? 256 LYS A N   1 
ATOM   2073 C  CA  . LYS A 1 256 ? 6.789   -0.682  34.059  1.00 14.72 ? 256 LYS A CA  1 
ATOM   2074 C  C   . LYS A 1 256 ? 5.804   -1.350  33.115  1.00 15.81 ? 256 LYS A C   1 
ATOM   2075 O  O   . LYS A 1 256 ? 5.998   -1.310  31.896  1.00 16.72 ? 256 LYS A O   1 
ATOM   2076 C  CB  . LYS A 1 256 ? 6.465   0.796   34.291  1.00 16.35 ? 256 LYS A CB  1 
ATOM   2077 C  CG  . LYS A 1 256 ? 7.321   1.405   35.399  1.00 20.91 ? 256 LYS A CG  1 
ATOM   2078 C  CD  . LYS A 1 256 ? 7.015   2.860   35.701  1.00 28.96 ? 256 LYS A CD  1 
ATOM   2079 N  N   . ALA A 1 257 ? 4.785   -2.006  33.655  1.00 15.79 ? 257 ALA A N   1 
ATOM   2080 C  CA  . ALA A 1 257 ? 3.703   -2.586  32.875  1.00 15.56 ? 257 ALA A CA  1 
ATOM   2081 C  C   . ALA A 1 257 ? 2.414   -1.794  33.036  1.00 16.00 ? 257 ALA A C   1 
ATOM   2082 O  O   . ALA A 1 257 ? 2.071   -1.315  34.135  1.00 18.22 ? 257 ALA A O   1 
ATOM   2083 C  CB  . ALA A 1 257 ? 3.490   -4.049  33.234  1.00 16.33 ? 257 ALA A CB  1 
ATOM   2084 N  N   . SER A 1 258 ? 1.682   -1.688  31.940  1.00 14.81 ? 258 SER A N   1 
ATOM   2085 C  CA  . SER A 1 258 ? 0.417   -0.969  31.975  1.00 16.18 ? 258 SER A CA  1 
ATOM   2086 C  C   . SER A 1 258 ? -0.715  -1.866  32.442  1.00 18.87 ? 258 SER A C   1 
ATOM   2087 O  O   . SER A 1 258 ? -1.846  -1.376  32.509  1.00 22.65 ? 258 SER A O   1 
ATOM   2088 C  CB  . SER A 1 258 ? 0.112   -0.420  30.611  1.00 15.37 ? 258 SER A CB  1 
ATOM   2089 O  OG  . SER A 1 258 ? -0.331  -1.446  29.721  1.00 16.48 ? 258 SER A OG  1 
ATOM   2090 N  N   . PHE A 1 259 ? -0.420  -3.136  32.687  1.00 19.26 ? 259 PHE A N   1 
ATOM   2091 C  CA  . PHE A 1 259 ? -1.428  -4.174  32.837  1.00 21.92 ? 259 PHE A CA  1 
ATOM   2092 C  C   . PHE A 1 259 ? -1.005  -5.153  33.923  1.00 25.92 ? 259 PHE A C   1 
ATOM   2093 O  O   . PHE A 1 259 ? 0.186   -5.295  34.232  1.00 24.73 ? 259 PHE A O   1 
ATOM   2094 C  CB  . PHE A 1 259 ? -1.684  -4.943  31.536  1.00 21.26 ? 259 PHE A CB  1 
ATOM   2095 C  CG  . PHE A 1 259 ? -0.453  -5.679  31.058  1.00 21.40 ? 259 PHE A CG  1 
ATOM   2096 C  CD1 . PHE A 1 259 ? 0.542   -4.993  30.385  1.00 21.58 ? 259 PHE A CD1 1 
ATOM   2097 C  CD2 . PHE A 1 259 ? -0.208  -6.992  31.456  1.00 24.23 ? 259 PHE A CD2 1 
ATOM   2098 C  CE1 . PHE A 1 259 ? 1.698   -5.662  30.011  1.00 23.39 ? 259 PHE A CE1 1 
ATOM   2099 C  CE2 . PHE A 1 259 ? 0.964   -7.647  31.109  1.00 27.66 ? 259 PHE A CE2 1 
ATOM   2100 C  CZ  . PHE A 1 259 ? 1.909   -6.977  30.370  1.00 26.42 ? 259 PHE A CZ  1 
ATOM   2101 N  N   . LYS A 1 260 ? -2.071  -5.803  34.445  1.00 37.07 ? 260 LYS A N   1 
ATOM   2102 C  CA  . LYS A 1 260 ? -2.189  -7.093  35.112  1.00 45.93 ? 260 LYS A CA  1 
ATOM   2103 C  C   . LYS A 1 260 ? -1.352  -7.109  36.385  1.00 51.78 ? 260 LYS A C   1 
ATOM   2104 O  O   . LYS A 1 260 ? -0.121  -7.153  36.337  1.00 61.39 ? 260 LYS A O   1 
ATOM   2105 C  CB  . LYS A 1 260 ? -1.969  -8.283  34.164  1.00 43.98 ? 260 LYS A CB  1 
ATOM   2106 O  OXT . LYS A 1 260 ? -1.958  -7.070  37.458  1.00 59.36 ? 260 LYS A OXT 1 
HETATM 2107 ZN ZN  . ZN  B 2 .   ? 14.343  0.127   15.366  1.00 10.44 ? 301 ZN  A ZN  1 
HETATM 2108 S  S   . DMS C 3 .   ? 22.391  -9.767  14.947  1.00 29.92 ? 302 DMS A S   1 
HETATM 2109 O  O   . DMS C 3 .   ? 23.007  -11.088 14.465  1.00 33.80 ? 302 DMS A O   1 
HETATM 2110 C  C1  . DMS C 3 .   ? 22.717  -9.752  16.681  1.00 26.75 ? 302 DMS A C1  1 
HETATM 2111 C  C2  . DMS C 3 .   ? 23.583  -8.510  14.536  1.00 33.37 ? 302 DMS A C2  1 
HETATM 2112 N  N1  . BCN D 4 .   ? 0.498   -12.980 23.469  1.00 55.89 ? 303 BCN A N1  1 
HETATM 2113 C  C1  . BCN D 4 .   ? 1.378   -12.385 24.482  1.00 52.54 ? 303 BCN A C1  1 
HETATM 2114 C  C2  . BCN D 4 .   ? 1.046   -13.011 25.833  1.00 63.61 ? 303 BCN A C2  1 
HETATM 2115 O  O21 . BCN D 4 .   ? 0.093   -13.832 25.872  1.00 66.35 ? 303 BCN A O21 1 
HETATM 2116 O  O22 . BCN D 4 .   ? 1.740   -12.657 26.805  1.00 70.36 ? 303 BCN A O22 1 
HETATM 2117 C  C3  . BCN D 4 .   ? -0.475  -12.025 22.903  1.00 42.84 ? 303 BCN A C3  1 
HETATM 2118 C  C4  . BCN D 4 .   ? -1.639  -11.687 23.809  1.00 53.56 ? 303 BCN A C4  1 
HETATM 2119 O  O4  . BCN D 4 .   ? -1.327  -10.619 24.701  1.00 41.22 ? 303 BCN A O4  1 
HETATM 2120 C  C5  . BCN D 4 .   ? 1.249   -13.842 22.541  1.00 41.36 ? 303 BCN A C5  1 
HETATM 2121 C  C6  . BCN D 4 .   ? 0.420   -14.815 21.746  1.00 50.17 ? 303 BCN A C6  1 
HETATM 2122 O  O6  . BCN D 4 .   ? 0.692   -14.654 20.365  1.00 43.44 ? 303 BCN A O6  1 
HETATM 2123 N  N1  . BCN E 4 .   ? 12.719  19.635  10.553  1.00 40.86 ? 304 BCN A N1  1 
HETATM 2124 C  C1  . BCN E 4 .   ? 13.976  18.936  10.350  1.00 36.60 ? 304 BCN A C1  1 
HETATM 2125 C  C2  . BCN E 4 .   ? 14.588  18.211  11.553  1.00 35.65 ? 304 BCN A C2  1 
HETATM 2126 O  O21 . BCN E 4 .   ? 14.121  17.118  11.785  1.00 34.68 ? 304 BCN A O21 1 
HETATM 2127 O  O22 . BCN E 4 .   ? 15.574  18.740  12.158  1.00 37.52 ? 304 BCN A O22 1 
HETATM 2128 C  C3  . BCN E 4 .   ? 12.862  21.085  10.358  1.00 25.73 ? 304 BCN A C3  1 
HETATM 2129 C  C4  . BCN E 4 .   ? 13.434  21.557  9.068   1.00 29.59 ? 304 BCN A C4  1 
HETATM 2130 O  O4  . BCN E 4 .   ? 12.461  21.747  8.079   1.00 26.20 ? 304 BCN A O4  1 
HETATM 2131 C  C5  . BCN E 4 .   ? 11.541  19.085  9.840   1.00 38.18 ? 304 BCN A C5  1 
HETATM 2132 C  C6  . BCN E 4 .   ? 11.616  17.671  9.284   1.00 46.56 ? 304 BCN A C6  1 
HETATM 2133 O  O6  . BCN E 4 .   ? 12.495  16.853  10.052  1.00 32.82 ? 304 BCN A O6  1 
HETATM 2134 F  F18 . 3TV F 5 .   ? 15.131  7.238   14.777  1.00 19.92 ? 305 3TV A F18 1 
HETATM 2135 C  C7  . 3TV F 5 .   ? 15.585  5.997   14.655  1.00 19.32 ? 305 3TV A C7  1 
HETATM 2136 C  C6  . 3TV F 5 .   ? 15.244  5.098   15.610  1.00 15.21 ? 305 3TV A C6  1 
HETATM 2137 F  F17 . 3TV F 5 .   ? 14.521  5.496   16.645  1.00 15.19 ? 305 3TV A F17 1 
HETATM 2138 C  C8  . 3TV F 5 .   ? 16.285  5.501   13.620  1.00 18.48 ? 305 3TV A C8  1 
HETATM 2139 S  S11 . 3TV F 5 .   ? 16.786  6.632   12.302  1.00 24.33 ? 305 3TV A S11 1 
HETATM 2140 C  C12 . 3TV F 5 .   ? 17.998  7.909   12.776  1.00 31.85 ? 305 3TV A C12 1 
HETATM 2141 C  C13 . 3TV F 5 .   ? 18.538  7.535   14.108  1.00 22.06 ? 305 3TV A C13 1 
HETATM 2142 C  C14 . 3TV F 5 .   ? 19.488  6.472   13.663  1.00 25.54 ? 305 3TV A C14 1 
HETATM 2143 C  C9  . 3TV F 5 .   ? 16.673  4.229   13.519  1.00 20.93 ? 305 3TV A C9  1 
HETATM 2144 F  F15 . 3TV F 5 .   ? 17.377  3.761   12.507  1.00 20.63 ? 305 3TV A F15 1 
HETATM 2145 C  C10 . 3TV F 5 .   ? 16.333  3.344   14.487  1.00 16.50 ? 305 3TV A C10 1 
HETATM 2146 F  F16 . 3TV F 5 .   ? 16.779  2.092   14.319  1.00 20.83 ? 305 3TV A F16 1 
HETATM 2147 C  C5  . 3TV F 5 .   ? 15.627  3.780   15.624  1.00 13.79 ? 305 3TV A C5  1 
HETATM 2148 S  S1  . 3TV F 5 .   ? 15.119  2.636   16.906  1.00 11.61 ? 305 3TV A S1  1 
HETATM 2149 O  O3  . 3TV F 5 .   ? 13.688  2.787   16.848  1.00 11.02 ? 305 3TV A O3  1 
HETATM 2150 O  O4  . 3TV F 5 .   ? 15.813  2.975   18.142  1.00 11.57 ? 305 3TV A O4  1 
HETATM 2151 N  N2  . 3TV F 5 .   ? 15.555  1.112   16.445  1.00 13.35 ? 305 3TV A N2  1 
HETATM 2152 F  F18 . 3TV G 5 .   ? 34.404  1.644   9.417   1.00 46.26 ? 306 3TV A F18 1 
HETATM 2153 C  C7  . 3TV G 5 .   ? 34.223  0.865   10.471  1.00 46.13 ? 306 3TV A C7  1 
HETATM 2154 C  C6  . 3TV G 5 .   ? 33.339  1.257   11.477  1.00 39.48 ? 306 3TV A C6  1 
HETATM 2155 F  F17 . 3TV G 5 .   ? 32.712  2.434   11.297  1.00 42.06 ? 306 3TV A F17 1 
HETATM 2156 C  C8  . 3TV G 5 .   ? 34.902  -0.324  10.585  1.00 42.86 ? 306 3TV A C8  1 
HETATM 2157 S  S11 . 3TV G 5 .   ? 36.035  -0.798  9.310   1.00 49.06 ? 306 3TV A S11 1 
HETATM 2158 C  C12 . 3TV G 5 .   ? 35.067  -1.837  8.165   1.00 61.83 ? 306 3TV A C12 1 
HETATM 2159 C  C13 . 3TV G 5 .   ? 35.406  -1.449  6.715   1.00 66.59 ? 306 3TV A C13 1 
HETATM 2160 C  C14 . 3TV G 5 .   ? 36.862  -1.697  6.429   1.00 64.79 ? 306 3TV A C14 1 
HETATM 2161 C  C9  . 3TV G 5 .   ? 34.751  -1.153  11.625  1.00 42.19 ? 306 3TV A C9  1 
HETATM 2162 F  F15 . 3TV G 5 .   ? 35.413  -2.297  11.683  1.00 45.67 ? 306 3TV A F15 1 
HETATM 2163 C  C10 . 3TV G 5 .   ? 33.873  -0.819  12.629  1.00 39.20 ? 306 3TV A C10 1 
HETATM 2164 F  F16 . 3TV G 5 .   ? 33.810  -1.723  13.603  1.00 31.48 ? 306 3TV A F16 1 
HETATM 2165 C  C5  . 3TV G 5 .   ? 33.144  0.397   12.602  1.00 38.90 ? 306 3TV A C5  1 
HETATM 2166 S  S1  . 3TV G 5 .   ? 31.920  0.820   13.921  1.00 38.21 ? 306 3TV A S1  1 
HETATM 2167 O  O3  . 3TV G 5 .   ? 31.194  -0.503  13.940  1.00 26.92 ? 306 3TV A O3  1 
HETATM 2168 O  O4  . 3TV G 5 .   ? 31.196  2.093   13.625  1.00 34.40 ? 306 3TV A O4  1 
HETATM 2169 N  N2  . 3TV G 5 .   ? 32.579  1.246   15.494  1.00 30.05 ? 306 3TV A N2  1 
HETATM 2170 O  O   . HOH H 6 .   ? 3.215   21.083  6.110   1.00 24.01 ? 401 HOH A O   1 
HETATM 2171 O  O   . HOH H 6 .   ? 6.793   -14.644 29.180  1.00 31.86 ? 402 HOH A O   1 
HETATM 2172 O  O   . HOH H 6 .   ? -4.451  -8.857  17.657  1.00 38.34 ? 403 HOH A O   1 
HETATM 2173 O  O   . HOH H 6 .   ? 18.987  10.388  29.174  1.00 28.82 ? 404 HOH A O   1 
HETATM 2174 O  O   . HOH H 6 .   ? 1.444   18.102  19.123  1.00 33.44 ? 405 HOH A O   1 
HETATM 2175 O  O   . HOH H 6 .   ? 17.001  5.143   9.477   1.00 31.80 ? 406 HOH A O   1 
HETATM 2176 O  O   . HOH H 6 .   ? 0.205   -5.074  -2.074  1.00 33.71 ? 407 HOH A O   1 
HETATM 2177 O  O   . HOH H 6 .   ? 20.483  -2.371  39.750  1.00 42.10 ? 408 HOH A O   1 
HETATM 2178 O  O   . HOH H 6 .   ? 25.704  -0.866  28.962  1.00 22.87 ? 409 HOH A O   1 
HETATM 2179 O  O   . HOH H 6 .   ? 13.519  9.062   27.338  1.00 26.96 ? 410 HOH A O   1 
HETATM 2180 O  O   . HOH H 6 .   ? 36.062  2.028   15.160  1.00 40.62 ? 411 HOH A O   1 
HETATM 2181 O  O   . HOH H 6 .   ? 3.930   -14.315 22.129  1.00 28.39 ? 412 HOH A O   1 
HETATM 2182 O  O   . HOH H 6 .   ? -3.073  -1.537  29.495  1.00 35.05 ? 413 HOH A O   1 
HETATM 2183 O  O   . HOH H 6 .   ? 10.714  2.847   34.344  1.00 32.51 ? 414 HOH A O   1 
HETATM 2184 O  O   . HOH H 6 .   ? 9.150   14.302  29.049  1.00 23.59 ? 415 HOH A O   1 
HETATM 2185 O  O   . HOH H 6 .   ? 1.841   -18.833 5.020   1.00 25.57 ? 416 HOH A O   1 
HETATM 2186 O  O   . HOH H 6 .   ? 19.084  -1.226  11.459  1.00 30.82 ? 417 HOH A O   1 
HETATM 2187 O  O   . HOH H 6 .   ? 5.825   -8.560  37.458  1.00 26.62 ? 418 HOH A O   1 
HETATM 2188 O  O   . HOH H 6 .   ? 25.352  -1.827  26.549  1.00 22.64 ? 419 HOH A O   1 
HETATM 2189 O  O   . HOH H 6 .   ? 10.840  16.922  12.015  1.00 25.83 ? 420 HOH A O   1 
HETATM 2190 O  O   . HOH H 6 .   ? 14.324  -18.335 19.378  1.00 20.79 ? 421 HOH A O   1 
HETATM 2191 O  O   . HOH H 6 .   ? 17.709  -2.797  37.617  1.00 34.90 ? 422 HOH A O   1 
HETATM 2192 O  O   . HOH H 6 .   ? 8.312   -20.324 8.264   1.00 29.75 ? 423 HOH A O   1 
HETATM 2193 O  O   . HOH H 6 .   ? -4.188  -7.737  15.040  1.00 38.27 ? 424 HOH A O   1 
HETATM 2194 O  O   . HOH H 6 .   ? 1.618   19.220  5.982   1.00 30.16 ? 425 HOH A O   1 
HETATM 2195 O  O   . HOH H 6 .   ? 6.418   -16.885 18.725  1.00 23.51 ? 426 HOH A O   1 
HETATM 2196 O  O   . HOH H 6 .   ? -0.731  -12.264 18.952  1.00 34.53 ? 427 HOH A O   1 
HETATM 2197 O  O   . HOH H 6 .   ? 3.962   -21.143 4.047   1.00 34.05 ? 428 HOH A O   1 
HETATM 2198 O  O   . HOH H 6 .   ? -4.662  -4.019  13.125  1.00 42.19 ? 429 HOH A O   1 
HETATM 2199 O  O   . HOH H 6 .   ? 21.663  -7.908  -5.360  1.00 31.96 ? 430 HOH A O   1 
HETATM 2200 O  O   . HOH H 6 .   ? 32.321  -1.936  7.925   1.00 50.22 ? 431 HOH A O   1 
HETATM 2201 O  O   . HOH H 6 .   ? -6.687  13.279  5.260   1.00 45.52 ? 432 HOH A O   1 
HETATM 2202 O  O   . HOH H 6 .   ? 1.060   12.653  26.920  1.00 21.20 ? 433 HOH A O   1 
HETATM 2203 O  O   . HOH H 6 .   ? -3.038  10.660  20.402  1.00 24.36 ? 434 HOH A O   1 
HETATM 2204 O  O   . HOH H 6 .   ? 4.213   -12.135 26.171  1.00 27.58 ? 435 HOH A O   1 
HETATM 2205 O  O   . HOH H 6 .   ? 19.875  -2.313  15.804  1.00 11.98 ? 436 HOH A O   1 
HETATM 2206 O  O   . HOH H 6 .   ? 20.515  2.736   34.398  1.00 28.98 ? 437 HOH A O   1 
HETATM 2207 O  O   . HOH H 6 .   ? 14.244  -13.134 31.475  1.00 24.31 ? 438 HOH A O   1 
HETATM 2208 O  O   . HOH H 6 .   ? -0.848  21.376  17.520  1.00 34.11 ? 439 HOH A O   1 
HETATM 2209 O  O   . HOH H 6 .   ? -4.310  11.672  13.437  1.00 32.21 ? 440 HOH A O   1 
HETATM 2210 O  O   . HOH H 6 .   ? 24.429  10.699  20.861  1.00 27.47 ? 441 HOH A O   1 
HETATM 2211 O  O   . HOH H 6 .   ? 24.506  6.613   30.167  1.00 20.71 ? 442 HOH A O   1 
HETATM 2212 O  O   . HOH H 6 .   ? 28.102  4.820   31.955  1.00 36.84 ? 443 HOH A O   1 
HETATM 2213 O  O   . HOH H 6 .   ? 23.217  9.564   27.717  1.00 19.75 ? 444 HOH A O   1 
HETATM 2214 O  O   . HOH H 6 .   ? 20.604  -18.725 14.972  1.00 40.12 ? 445 HOH A O   1 
HETATM 2215 O  O   . HOH H 6 .   ? 34.528  1.999   24.452  1.00 24.96 ? 446 HOH A O   1 
HETATM 2216 O  O   . HOH H 6 .   ? 12.431  2.682   -6.361  1.00 28.73 ? 447 HOH A O   1 
HETATM 2217 O  O   . HOH H 6 .   ? 11.421  17.649  29.359  1.00 29.05 ? 448 HOH A O   1 
HETATM 2218 O  O   . HOH H 6 .   ? 32.706  -5.406  22.390  1.00 36.75 ? 449 HOH A O   1 
HETATM 2219 O  O   . HOH H 6 .   ? 15.231  9.714   5.485   1.00 25.47 ? 450 HOH A O   1 
HETATM 2220 O  O   . HOH H 6 .   ? 0.708   10.470  30.104  1.00 28.18 ? 451 HOH A O   1 
HETATM 2221 O  O   . HOH H 6 .   ? 3.111   12.563  11.399  1.00 20.16 ? 452 HOH A O   1 
HETATM 2222 O  O   . HOH H 6 .   ? 11.386  8.646   -3.452  1.00 53.41 ? 453 HOH A O   1 
HETATM 2223 O  O   . HOH H 6 .   ? 5.684   -19.882 13.263  1.00 22.61 ? 454 HOH A O   1 
HETATM 2224 O  O   . HOH H 6 .   ? 24.511  -6.998  25.964  1.00 36.53 ? 455 HOH A O   1 
HETATM 2225 O  O   . HOH H 6 .   ? 12.202  7.727   28.970  1.00 23.62 ? 456 HOH A O   1 
HETATM 2226 O  O   . HOH H 6 .   ? 1.177   -2.185  41.249  1.00 31.19 ? 457 HOH A O   1 
HETATM 2227 O  O   . HOH H 6 .   ? 10.485  -17.502 19.844  1.00 23.28 ? 458 HOH A O   1 
HETATM 2228 O  O   . HOH H 6 .   ? -2.222  -9.394  17.203  1.00 26.18 ? 459 HOH A O   1 
HETATM 2229 O  O   . HOH H 6 .   ? 10.641  -16.396 16.900  1.00 19.30 ? 460 HOH A O   1 
HETATM 2230 O  O   . HOH H 6 .   ? 13.115  -13.182 37.118  1.00 34.06 ? 461 HOH A O   1 
HETATM 2231 O  O   . HOH H 6 .   ? 23.030  -13.744 9.380   1.00 27.04 ? 462 HOH A O   1 
HETATM 2232 O  O   . HOH H 6 .   ? 7.005   -19.342 3.501   1.00 39.76 ? 463 HOH A O   1 
HETATM 2233 O  O   . HOH H 6 .   ? 7.633   12.288  27.865  1.00 17.60 ? 464 HOH A O   1 
HETATM 2234 O  O   . HOH H 6 .   ? 1.376   -15.224 2.880   1.00 27.77 ? 465 HOH A O   1 
HETATM 2235 O  O   . HOH H 6 .   ? 9.026   12.707  5.821   1.00 32.20 ? 466 HOH A O   1 
HETATM 2236 O  O   . HOH H 6 .   ? 8.173   -20.512 12.051  1.00 26.75 ? 467 HOH A O   1 
HETATM 2237 O  O   . HOH H 6 .   ? -6.170  -6.069  26.119  1.00 35.52 ? 468 HOH A O   1 
HETATM 2238 O  O   . HOH H 6 .   ? 8.786   14.776  31.699  1.00 25.76 ? 469 HOH A O   1 
HETATM 2239 O  O   . HOH H 6 .   ? 14.897  -2.619  -6.385  1.00 24.41 ? 470 HOH A O   1 
HETATM 2240 O  O   . HOH H 6 .   ? 16.287  -10.235 32.100  1.00 22.68 ? 471 HOH A O   1 
HETATM 2241 O  O   . HOH H 6 .   ? 9.017   -1.491  41.947  1.00 41.03 ? 472 HOH A O   1 
HETATM 2242 O  O   . HOH H 6 .   ? 5.762   -9.263  -3.645  1.00 43.73 ? 473 HOH A O   1 
HETATM 2243 O  O   . HOH H 6 .   ? -6.689  8.010   21.837  1.00 38.11 ? 474 HOH A O   1 
HETATM 2244 O  O   . HOH H 6 .   ? 7.240   22.051  15.220  1.00 24.41 ? 475 HOH A O   1 
HETATM 2245 O  O   . HOH H 6 .   ? 13.081  -13.570 11.203  1.00 12.57 ? 476 HOH A O   1 
HETATM 2246 O  O   . HOH H 6 .   ? 2.462   -19.313 14.736  1.00 26.34 ? 477 HOH A O   1 
HETATM 2247 O  O   . HOH H 6 .   ? 4.064   -6.538  20.391  1.00 12.08 ? 478 HOH A O   1 
HETATM 2248 O  O   . HOH H 6 .   ? 36.448  -0.590  14.500  1.00 22.18 ? 479 HOH A O   1 
HETATM 2249 O  O   . HOH H 6 .   ? 10.854  10.508  25.535  1.00 13.96 ? 480 HOH A O   1 
HETATM 2250 O  O   . HOH H 6 .   ? 8.123   -7.002  -3.163  1.00 31.09 ? 481 HOH A O   1 
HETATM 2251 O  O   . HOH H 6 .   ? -0.438  -5.278  23.583  1.00 15.79 ? 482 HOH A O   1 
HETATM 2252 O  O   . HOH H 6 .   ? 16.503  -11.648 17.952  1.00 10.52 ? 483 HOH A O   1 
HETATM 2253 O  O   . HOH H 6 .   ? 23.631  -11.421 5.153   1.00 25.87 ? 484 HOH A O   1 
HETATM 2254 O  O   . HOH H 6 .   ? 21.013  1.026   -4.593  1.00 19.00 ? 485 HOH A O   1 
HETATM 2255 O  O   . HOH H 6 .   ? -0.061  9.747   1.921   1.00 21.19 ? 486 HOH A O   1 
HETATM 2256 O  O   . HOH H 6 .   ? 7.072   16.857  5.972   1.00 38.29 ? 487 HOH A O   1 
HETATM 2257 O  O   . HOH H 6 .   ? 22.331  -10.003 25.099  1.00 25.49 ? 488 HOH A O   1 
HETATM 2258 O  O   . HOH H 6 .   ? 14.701  23.365  23.852  1.00 26.94 ? 489 HOH A O   1 
HETATM 2259 O  O   . HOH H 6 .   ? 17.238  -14.134 24.275  1.00 15.26 ? 490 HOH A O   1 
HETATM 2260 O  O   . HOH H 6 .   ? 17.533  -9.334  20.853  1.00 11.99 ? 491 HOH A O   1 
HETATM 2261 O  O   . HOH H 6 .   ? -5.898  -10.906 20.183  1.00 34.04 ? 492 HOH A O   1 
HETATM 2262 O  O   . HOH H 6 .   ? 19.532  6.373   -4.589  1.00 30.21 ? 493 HOH A O   1 
HETATM 2263 O  O   . HOH H 6 .   ? -4.729  8.228   27.176  1.00 34.34 ? 494 HOH A O   1 
HETATM 2264 O  O   . HOH H 6 .   ? 21.276  -17.727 10.735  1.00 30.70 ? 495 HOH A O   1 
HETATM 2265 O  O   . HOH H 6 .   ? 26.654  8.780   20.304  1.00 23.22 ? 496 HOH A O   1 
HETATM 2266 O  O   . HOH H 6 .   ? -4.654  0.109   34.839  1.00 39.70 ? 497 HOH A O   1 
HETATM 2267 O  O   . HOH H 6 .   ? 4.993   -10.475 24.335  1.00 19.77 ? 498 HOH A O   1 
HETATM 2268 O  O   . HOH H 6 .   ? 15.192  15.016  10.382  1.00 35.33 ? 499 HOH A O   1 
HETATM 2269 O  O   . HOH H 6 .   ? -4.591  -13.447 7.805   1.00 28.46 ? 500 HOH A O   1 
HETATM 2270 O  O   . HOH H 6 .   ? 23.144  -4.837  -7.909  1.00 40.44 ? 501 HOH A O   1 
HETATM 2271 O  O   . HOH H 6 .   ? 7.654   1.132   -5.914  1.00 33.65 ? 502 HOH A O   1 
HETATM 2272 O  O   . HOH H 6 .   ? 17.627  -11.477 25.075  1.00 13.92 ? 503 HOH A O   1 
HETATM 2273 O  O   . HOH H 6 .   ? 23.643  -9.566  9.442   1.00 21.97 ? 504 HOH A O   1 
HETATM 2274 O  O   . HOH H 6 .   ? 29.724  -2.037  21.186  1.00 16.30 ? 505 HOH A O   1 
HETATM 2275 O  O   . HOH H 6 .   ? -5.216  -5.866  30.415  1.00 37.62 ? 506 HOH A O   1 
HETATM 2276 O  O   . HOH H 6 .   ? 17.345  -10.920 -2.968  1.00 26.85 ? 507 HOH A O   1 
HETATM 2277 O  O   . HOH H 6 .   ? 5.493   10.765  -2.122  1.00 26.75 ? 508 HOH A O   1 
HETATM 2278 O  O   . HOH H 6 .   ? 23.142  6.738   12.276  1.00 34.08 ? 509 HOH A O   1 
HETATM 2279 O  O   . HOH H 6 .   ? -2.267  -11.454 11.251  1.00 29.54 ? 510 HOH A O   1 
HETATM 2280 O  O   . HOH H 6 .   ? -5.226  4.840   21.105  1.00 29.26 ? 511 HOH A O   1 
HETATM 2281 O  O   . HOH H 6 .   ? 18.547  -7.024  29.086  1.00 15.13 ? 512 HOH A O   1 
HETATM 2282 O  O   . HOH H 6 .   ? 24.996  -1.174  4.025   1.00 35.95 ? 513 HOH A O   1 
HETATM 2283 O  O   . HOH H 6 .   ? 7.207   11.266  31.526  1.00 36.00 ? 514 HOH A O   1 
HETATM 2284 O  O   . HOH H 6 .   ? 20.832  11.322  18.251  1.00 27.98 ? 515 HOH A O   1 
HETATM 2285 O  O   . HOH H 6 .   ? -2.086  -1.076  6.774   1.00 25.22 ? 516 HOH A O   1 
HETATM 2286 O  O   . HOH H 6 .   ? 13.985  -14.755 1.532   1.00 26.20 ? 517 HOH A O   1 
HETATM 2287 O  O   . HOH H 6 .   ? -0.866  7.655   4.862   1.00 21.81 ? 518 HOH A O   1 
HETATM 2288 O  O   . HOH H 6 .   ? 16.429  -14.059 0.984   1.00 30.53 ? 519 HOH A O   1 
HETATM 2289 O  O   . HOH H 6 .   ? 36.923  5.637   15.504  1.00 24.80 ? 520 HOH A O   1 
HETATM 2290 O  O   . HOH H 6 .   ? 32.343  3.044   26.052  1.00 28.02 ? 521 HOH A O   1 
HETATM 2291 O  O   . HOH H 6 .   ? 2.522   -1.927  -2.710  1.00 28.14 ? 522 HOH A O   1 
HETATM 2292 O  O   . HOH H 6 .   ? -0.990  -16.473 13.571  1.00 27.32 ? 523 HOH A O   1 
HETATM 2293 O  O   . HOH H 6 .   ? -1.657  -4.016  2.739   1.00 23.80 ? 524 HOH A O   1 
HETATM 2294 O  O   . HOH H 6 .   ? 22.593  -4.610  34.242  1.00 30.38 ? 525 HOH A O   1 
HETATM 2295 O  O   . HOH H 6 .   ? 6.190   13.151  34.629  1.00 33.39 ? 526 HOH A O   1 
HETATM 2296 O  O   . HOH H 6 .   ? 16.823  -6.958  31.238  1.00 24.36 ? 527 HOH A O   1 
HETATM 2297 O  O   . HOH H 6 .   ? 3.197   22.697  7.954   1.00 19.02 ? 528 HOH A O   1 
HETATM 2298 O  O   . HOH H 6 .   ? 19.031  -2.678  -7.014  1.00 31.03 ? 529 HOH A O   1 
HETATM 2299 O  O   . HOH H 6 .   ? 26.001  -3.089  20.998  1.00 15.67 ? 530 HOH A O   1 
HETATM 2300 O  O   . HOH H 6 .   ? 2.707   -10.730 -3.600  1.00 29.38 ? 531 HOH A O   1 
HETATM 2301 O  O   . HOH H 6 .   ? 3.918   -5.501  39.651  1.00 36.47 ? 532 HOH A O   1 
HETATM 2302 O  O   . HOH H 6 .   ? 28.634  -5.642  -0.626  1.00 28.37 ? 533 HOH A O   1 
HETATM 2303 O  O   . HOH H 6 .   ? 14.258  -3.624  37.313  1.00 22.76 ? 534 HOH A O   1 
HETATM 2304 O  O   . HOH H 6 .   ? 1.751   12.018  8.968   1.00 17.12 ? 535 HOH A O   1 
HETATM 2305 O  O   . HOH H 6 .   ? 10.013  -17.461 6.908   1.00 24.86 ? 536 HOH A O   1 
HETATM 2306 O  O   . HOH H 6 .   ? 7.599   -16.706 14.744  1.00 20.89 ? 537 HOH A O   1 
HETATM 2307 O  O   . HOH H 6 .   ? 12.369  -13.638 32.963  1.00 30.50 ? 538 HOH A O   1 
HETATM 2308 O  O   . HOH H 6 .   ? 22.889  9.869   24.970  1.00 20.67 ? 539 HOH A O   1 
HETATM 2309 O  O   . HOH H 6 .   ? 8.047   -15.080 26.595  1.00 20.82 ? 540 HOH A O   1 
HETATM 2310 O  O   . HOH H 6 .   ? 9.127   4.699   30.688  1.00 25.52 ? 541 HOH A O   1 
HETATM 2311 O  O   . HOH H 6 .   ? -3.873  -5.932  9.136   1.00 21.00 ? 542 HOH A O   1 
HETATM 2312 O  O   . HOH H 6 .   ? -2.173  1.293   34.439  1.00 43.14 ? 543 HOH A O   1 
HETATM 2313 O  O   . HOH H 6 .   ? 24.758  -10.560 12.129  1.00 43.41 ? 544 HOH A O   1 
HETATM 2314 O  O   . HOH H 6 .   ? 7.708   15.990  27.398  1.00 23.94 ? 545 HOH A O   1 
HETATM 2315 O  O   . HOH H 6 .   ? 5.198   17.917  23.661  1.00 24.54 ? 546 HOH A O   1 
HETATM 2316 O  O   . HOH H 6 .   ? 20.481  -6.817  32.618  1.00 24.34 ? 547 HOH A O   1 
HETATM 2317 O  O   . HOH H 6 .   ? 6.005   21.992  17.768  1.00 23.19 ? 548 HOH A O   1 
HETATM 2318 O  O   . HOH H 6 .   ? 22.401  0.097   29.479  1.00 16.04 ? 549 HOH A O   1 
HETATM 2319 O  O   . HOH H 6 .   ? -2.879  1.241   26.350  1.00 25.71 ? 550 HOH A O   1 
HETATM 2320 O  O   . HOH H 6 .   ? -3.024  1.183   4.067   1.00 25.57 ? 551 HOH A O   1 
HETATM 2321 O  O   . HOH H 6 .   ? 8.748   11.685  -5.838  1.00 35.91 ? 552 HOH A O   1 
HETATM 2322 O  O   . HOH H 6 .   ? 8.737   18.460  10.913  1.00 30.61 ? 553 HOH A O   1 
HETATM 2323 O  O   . HOH H 6 .   ? -0.069  -17.892 6.758   1.00 29.82 ? 554 HOH A O   1 
HETATM 2324 O  O   . HOH H 6 .   ? 13.716  -6.842  32.633  1.00 22.01 ? 555 HOH A O   1 
HETATM 2325 O  O   . HOH H 6 .   ? 26.322  -5.800  25.487  1.00 28.63 ? 556 HOH A O   1 
HETATM 2326 O  O   . HOH H 6 .   ? 9.072   11.187  3.245   1.00 33.84 ? 557 HOH A O   1 
HETATM 2327 O  O   . HOH H 6 .   ? 27.659  -9.317  14.577  1.00 45.20 ? 558 HOH A O   1 
HETATM 2328 O  O   . HOH H 6 .   ? -5.733  -2.061  25.129  1.00 24.37 ? 559 HOH A O   1 
HETATM 2329 O  O   . HOH H 6 .   ? 1.737   5.247   -3.228  1.00 33.28 ? 560 HOH A O   1 
HETATM 2330 O  O   . HOH H 6 .   ? 24.106  -12.602 1.246   1.00 26.98 ? 561 HOH A O   1 
HETATM 2331 O  O   . HOH H 6 .   ? -3.225  1.739   1.339   1.00 33.29 ? 562 HOH A O   1 
HETATM 2332 O  O   . HOH H 6 .   ? 11.900  -4.079  35.892  1.00 21.11 ? 563 HOH A O   1 
HETATM 2333 O  O   . HOH H 6 .   ? 8.446   9.674   28.896  1.00 23.70 ? 564 HOH A O   1 
HETATM 2334 O  O   . HOH H 6 .   ? 11.689  -8.144  -1.292  1.00 24.62 ? 565 HOH A O   1 
HETATM 2335 O  O   . HOH H 6 .   ? 24.737  6.087   10.561  1.00 46.22 ? 566 HOH A O   1 
HETATM 2336 O  O   . HOH H 6 .   ? -6.615  6.413   24.508  1.00 34.64 ? 567 HOH A O   1 
HETATM 2337 O  O   . HOH H 6 .   ? 9.755   11.580  7.735   1.00 37.00 ? 568 HOH A O   1 
HETATM 2338 O  O   . HOH H 6 .   ? 25.351  -4.910  7.844   1.00 27.22 ? 569 HOH A O   1 
HETATM 2339 O  O   . HOH H 6 .   ? -1.929  -9.890  13.979  1.00 20.31 ? 570 HOH A O   1 
HETATM 2340 O  O   . HOH H 6 .   ? 12.985  23.752  21.650  1.00 17.70 ? 571 HOH A O   1 
HETATM 2341 O  O   . HOH H 6 .   ? 4.652   -8.180  32.914  1.00 22.37 ? 572 HOH A O   1 
HETATM 2342 O  O   . HOH H 6 .   ? -2.534  1.707   32.068  1.00 31.45 ? 573 HOH A O   1 
HETATM 2343 O  O   . HOH H 6 .   ? 29.579  5.307   27.988  1.00 40.07 ? 574 HOH A O   1 
HETATM 2344 O  O   . HOH H 6 .   ? 13.536  -17.188 30.602  1.00 31.95 ? 575 HOH A O   1 
HETATM 2345 O  O   . HOH H 6 .   ? 18.966  -10.546 22.760  1.00 13.84 ? 576 HOH A O   1 
HETATM 2346 O  O   . HOH H 6 .   ? 12.612  -17.998 26.469  1.00 27.93 ? 577 HOH A O   1 
HETATM 2347 O  O   . HOH H 6 .   ? 11.666  -6.095  33.948  1.00 22.48 ? 578 HOH A O   1 
HETATM 2348 O  O   . HOH H 6 .   ? 12.508  10.229  7.346   1.00 39.86 ? 579 HOH A O   1 
HETATM 2349 O  O   . HOH H 6 .   ? -3.150  -16.062 6.662   1.00 34.63 ? 580 HOH A O   1 
HETATM 2350 O  O   . HOH H 6 .   ? -6.542  -9.616  15.905  1.00 44.31 ? 581 HOH A O   1 
HETATM 2351 O  O   . HOH H 6 .   ? 13.627  -6.760  -2.537  1.00 26.85 ? 582 HOH A O   1 
HETATM 2352 O  O   . HOH H 6 .   ? 5.784   -18.437 22.633  1.00 42.19 ? 583 HOH A O   1 
HETATM 2353 O  O   . HOH H 6 .   ? 14.500  8.715   11.776  1.00 32.30 ? 584 HOH A O   1 
HETATM 2354 O  O   . HOH H 6 .   ? 7.087   18.046  28.893  1.00 30.15 ? 585 HOH A O   1 
HETATM 2355 O  O   . HOH H 6 .   ? 34.292  -4.105  24.381  1.00 29.88 ? 586 HOH A O   1 
HETATM 2356 O  O   . HOH H 6 .   ? -0.196  17.733  3.648   1.00 34.87 ? 587 HOH A O   1 
HETATM 2357 O  O   . HOH H 6 .   ? 19.888  -15.804 17.947  1.00 33.90 ? 588 HOH A O   1 
HETATM 2358 O  O   . HOH H 6 .   ? -5.151  9.918   6.383   1.00 40.23 ? 589 HOH A O   1 
HETATM 2359 O  O   . HOH H 6 .   ? 8.147   -16.698 31.748  1.00 32.86 ? 590 HOH A O   1 
HETATM 2360 O  O   . HOH H 6 .   ? 14.154  3.291   35.365  1.00 31.54 ? 591 HOH A O   1 
HETATM 2361 O  O   . HOH H 6 .   ? 10.554  22.674  25.052  1.00 35.77 ? 592 HOH A O   1 
HETATM 2362 O  O   . HOH H 6 .   ? 26.244  -5.311  22.271  1.00 32.48 ? 593 HOH A O   1 
HETATM 2363 O  O   . HOH H 6 .   ? 23.610  7.887   32.964  1.00 35.41 ? 594 HOH A O   1 
HETATM 2364 O  O   . HOH H 6 .   ? -10.534 7.175   12.728  1.00 42.18 ? 595 HOH A O   1 
HETATM 2365 O  O   . HOH H 6 .   ? 8.224   5.518   -6.820  1.00 28.64 ? 596 HOH A O   1 
HETATM 2366 O  O   . HOH H 6 .   ? 20.893  -12.425 22.166  1.00 25.06 ? 597 HOH A O   1 
HETATM 2367 O  O   . HOH H 6 .   ? -3.583  -7.729  1.940   1.00 26.65 ? 598 HOH A O   1 
HETATM 2368 O  O   . HOH H 6 .   ? 24.123  3.154   -1.818  1.00 32.20 ? 599 HOH A O   1 
HETATM 2369 O  O   . HOH H 6 .   ? 35.250  4.119   23.037  1.00 31.35 ? 600 HOH A O   1 
HETATM 2370 O  O   . HOH H 6 .   ? 28.697  8.003   22.004  1.00 20.32 ? 601 HOH A O   1 
HETATM 2371 O  O   . HOH H 6 .   ? 14.097  -6.639  -7.302  1.00 38.80 ? 602 HOH A O   1 
HETATM 2372 O  O   . HOH H 6 .   ? 6.948   8.135   32.933  1.00 34.33 ? 603 HOH A O   1 
HETATM 2373 O  O   . HOH H 6 .   ? 35.107  7.645   19.630  1.00 38.55 ? 604 HOH A O   1 
HETATM 2374 O  O   . HOH H 6 .   ? 15.350  5.794   -5.740  1.00 35.73 ? 605 HOH A O   1 
HETATM 2375 O  O   . HOH H 6 .   ? 18.512  3.267   36.293  1.00 45.23 ? 606 HOH A O   1 
HETATM 2376 O  O   . HOH H 6 .   ? -0.265  -10.793 28.513  1.00 45.27 ? 607 HOH A O   1 
HETATM 2377 O  O   . HOH H 6 .   ? 30.065  4.069   30.212  1.00 48.01 ? 608 HOH A O   1 
HETATM 2378 O  O   . HOH H 6 .   ? 15.478  -10.603 -5.353  1.00 34.05 ? 609 HOH A O   1 
HETATM 2379 O  O   . HOH H 6 .   ? 2.891   -7.071  34.839  1.00 31.07 ? 610 HOH A O   1 
HETATM 2380 O  O   . HOH H 6 .   ? 31.565  8.568   15.340  1.00 38.78 ? 611 HOH A O   1 
HETATM 2381 O  O   . HOH H 6 .   ? -4.889  -4.375  33.427  1.00 38.86 ? 612 HOH A O   1 
HETATM 2382 O  O   . HOH H 6 .   ? 8.321   -15.414 16.820  1.00 21.47 ? 613 HOH A O   1 
HETATM 2383 O  O   . HOH H 6 .   ? -3.663  6.796   7.922   1.00 45.69 ? 614 HOH A O   1 
HETATM 2384 O  O   . HOH H 6 .   ? 25.703  -8.089  8.124   1.00 37.80 ? 615 HOH A O   1 
HETATM 2385 O  O   . HOH H 6 .   ? 1.960   16.331  30.951  1.00 39.19 ? 616 HOH A O   1 
HETATM 2386 O  O   . HOH H 6 .   ? 29.657  -2.745  23.851  1.00 31.38 ? 617 HOH A O   1 
HETATM 2387 O  O   . HOH H 6 .   ? -3.903  13.229  19.835  1.00 31.39 ? 618 HOH A O   1 
HETATM 2388 O  O   . HOH H 6 .   ? 8.636   7.896   30.863  1.00 30.73 ? 619 HOH A O   1 
HETATM 2389 O  O   . HOH H 6 .   ? 3.448   -7.835  37.423  1.00 43.51 ? 620 HOH A O   1 
HETATM 2390 O  O   . HOH H 6 .   ? 20.764  11.333  28.081  1.00 38.00 ? 621 HOH A O   1 
HETATM 2391 O  O   . HOH H 6 .   ? -2.643  -1.613  3.839   1.00 34.42 ? 622 HOH A O   1 
HETATM 2392 O  O   . HOH H 6 .   ? 19.709  10.424  15.114  1.00 42.91 ? 623 HOH A O   1 
HETATM 2393 O  O   . HOH H 6 .   ? 3.284   21.839  17.597  1.00 26.52 ? 624 HOH A O   1 
HETATM 2394 O  O   . HOH H 6 .   ? -4.300  7.026   35.623  1.00 44.81 ? 625 HOH A O   1 
HETATM 2395 O  O   . HOH H 6 .   ? 20.642  12.151  25.554  1.00 37.88 ? 626 HOH A O   1 
HETATM 2396 O  O   . HOH H 6 .   ? 5.561   -14.459 25.546  1.00 49.11 ? 627 HOH A O   1 
HETATM 2397 O  O   . HOH H 6 .   ? -5.929  -4.796  7.702   1.00 50.62 ? 628 HOH A O   1 
HETATM 2398 O  O   . HOH H 6 .   ? 21.408  2.750   -6.521  1.00 29.63 ? 629 HOH A O   1 
HETATM 2399 O  O   . HOH H 6 .   ? -3.132  12.032  27.196  1.00 43.06 ? 630 HOH A O   1 
HETATM 2400 O  O   . HOH H 6 .   ? 22.066  5.261   1.909   1.00 36.61 ? 631 HOH A O   1 
HETATM 2401 O  O   . HOH H 6 .   ? 17.388  8.252   6.234   1.00 28.30 ? 632 HOH A O   1 
HETATM 2402 O  O   . HOH H 6 .   ? 22.361  13.804  19.901  1.00 39.62 ? 633 HOH A O   1 
HETATM 2403 O  O   . HOH H 6 .   ? 4.172   -16.163 20.299  1.00 27.28 ? 634 HOH A O   1 
HETATM 2404 O  O   . HOH H 6 .   ? 23.943  -11.736 7.876   1.00 33.86 ? 635 HOH A O   1 
HETATM 2405 O  O   . HOH H 6 .   ? 19.641  -11.200 27.011  1.00 26.73 ? 636 HOH A O   1 
HETATM 2406 O  O   . HOH H 6 .   ? 18.973  -10.288 31.508  1.00 37.37 ? 637 HOH A O   1 
HETATM 2407 O  O   . HOH H 6 .   ? 1.056   -0.012  42.945  1.00 38.02 ? 638 HOH A O   1 
HETATM 2408 O  O   . HOH H 6 .   ? 9.999   -9.174  -2.798  1.00 37.83 ? 639 HOH A O   1 
HETATM 2409 O  O   . HOH H 6 .   ? -3.072  -5.121  0.375   1.00 33.61 ? 640 HOH A O   1 
HETATM 2410 O  O   . HOH H 6 .   ? 14.052  -8.214  -4.368  1.00 34.63 ? 641 HOH A O   1 
HETATM 2411 O  O   . HOH H 6 .   ? 36.625  0.574   26.092  1.00 30.92 ? 642 HOH A O   1 
HETATM 2412 O  O   . HOH H 6 .   ? 9.469   12.771  0.893   1.00 29.41 ? 643 HOH A O   1 
HETATM 2413 O  O   . HOH H 6 .   ? 3.214   -10.274 31.836  1.00 32.64 ? 644 HOH A O   1 
HETATM 2414 O  O   . HOH H 6 .   ? 16.108  -8.098  33.696  1.00 33.79 ? 645 HOH A O   1 
HETATM 2415 O  O   . HOH H 6 .   ? 11.938  4.893   34.743  1.00 29.66 ? 646 HOH A O   1 
HETATM 2416 O  O   . HOH H 6 .   ? 19.477  -15.414 5.024   1.00 47.98 ? 647 HOH A O   1 
HETATM 2417 O  O   . HOH H 6 .   ? 19.042  -15.568 25.290  1.00 27.90 ? 648 HOH A O   1 
HETATM 2418 O  O   . HOH H 6 .   ? 20.003  -9.422  28.931  1.00 22.25 ? 649 HOH A O   1 
HETATM 2419 O  O   . HOH H 6 .   ? 8.889   15.490  5.080   1.00 30.56 ? 650 HOH A O   1 
HETATM 2420 O  O   . HOH H 6 .   ? 27.145  7.177   29.869  1.00 35.02 ? 651 HOH A O   1 
HETATM 2421 O  O   . HOH H 6 .   ? 19.698  -1.284  43.285  1.00 38.43 ? 652 HOH A O   1 
HETATM 2422 O  O   . HOH H 6 .   ? 22.811  -15.758 7.171   1.00 34.18 ? 653 HOH A O   1 
HETATM 2423 O  O   . HOH H 6 .   ? 25.021  6.914   2.360   1.00 45.38 ? 654 HOH A O   1 
HETATM 2424 O  O   . HOH H 6 .   ? 23.132  -12.495 20.345  1.00 36.20 ? 655 HOH A O   1 
HETATM 2425 O  O   . HOH H 6 .   ? 8.204   23.527  26.293  1.00 30.93 ? 656 HOH A O   1 
HETATM 2426 O  O   . HOH H 6 .   ? 25.151  10.635  23.601  1.00 30.74 ? 657 HOH A O   1 
HETATM 2427 O  O   . HOH H 6 .   ? 20.561  -5.261  -7.500  1.00 41.31 ? 658 HOH A O   1 
HETATM 2428 O  O   . HOH H 6 .   ? 22.615  9.653   12.548  1.00 37.59 ? 659 HOH A O   1 
HETATM 2429 O  O   . HOH H 6 .   ? 33.112  -5.248  -2.189  1.00 30.78 ? 660 HOH A O   1 
HETATM 2430 O  O   . HOH H 6 .   ? 25.138  -11.462 21.723  1.00 37.70 ? 661 HOH A O   1 
# 
