data_7NZW
# 
_entry.id   7NZW 
# 
_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   7NZW         pdb_00007nzw 10.2210/pdb7nzw/pdb 
WWPDB D_1292114760 ?            ?                   
# 
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                        7NZW 
_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 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB 'PDB entry for the same citation' 7NZR unspecified 
PDB 'PDB entry for the same citation' 7NZS unspecified 
PDB 'PDB entry for the same citation' 7NZT unspecified 
PDB 'PDB entry for the same citation' 7NZU 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 '4-[(4,6-dimethylpyrimidin-2-yl)thio]-2,3,5,6-tetrafluorobenzenesulfonamide' 367.342   1   ?       ? ? ? 
4 non-polymer syn 'SODIUM ION'                                                                 22.990    1   ?       ? ? ? 
5 non-polymer syn 'DIMETHYL SULFOXIDE'                                                         78.133    1   ?       ? ? ? 
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 '4-[(4,6-dimethylpyrimidin-2-yl)thio]-2,3,5,6-tetrafluorobenzenesulfonamide' V50 
4 'SODIUM ION'                                                                 NA  
5 'DIMETHYL SULFOXIDE'                                                         DMS 
6 water                                                                        HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   SER n 
1 3   HIS n 
1 4   HIS n 
1 5   TRP n 
1 6   GLY n 
1 7   TYR n 
1 8   GLY n 
1 9   LYS n 
1 10  HIS n 
1 11  ASN n 
1 12  GLY n 
1 13  PRO n 
1 14  GLU n 
1 15  HIS n 
1 16  TRP n 
1 17  HIS n 
1 18  LYS n 
1 19  ASP n 
1 20  PHE n 
1 21  PRO n 
1 22  ILE n 
1 23  ALA n 
1 24  LYS n 
1 25  GLY n 
1 26  GLU n 
1 27  ARG n 
1 28  GLN n 
1 29  SER n 
1 30  PRO n 
1 31  VAL n 
1 32  ASP n 
1 33  ILE n 
1 34  ASP n 
1 35  THR n 
1 36  HIS n 
1 37  THR n 
1 38  ALA n 
1 39  LYS n 
1 40  TYR n 
1 41  ASP n 
1 42  PRO n 
1 43  SER n 
1 44  LEU n 
1 45  LYS n 
1 46  PRO n 
1 47  LEU n 
1 48  SER n 
1 49  VAL n 
1 50  SER n 
1 51  TYR n 
1 52  ASP n 
1 53  GLN n 
1 54  ALA n 
1 55  THR n 
1 56  SER n 
1 57  LEU n 
1 58  ARG n 
1 59  ILE n 
1 60  LEU n 
1 61  ASN n 
1 62  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 
ALA 'L-peptide linking' y ALANINE                                                                      ? 'C3 H7 N O2'         
89.093  
ARG 'L-peptide linking' y ARGININE                                                                     ? 'C6 H15 N4 O2 1'     
175.209 
ASN 'L-peptide linking' y ASPARAGINE                                                                   ? 'C4 H8 N2 O3'        
132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                                              ? 'C4 H7 N O4'         
133.103 
CYS 'L-peptide linking' y CYSTEINE                                                                     ? 'C3 H7 N O2 S'       
121.158 
DMS non-polymer         . 'DIMETHYL SULFOXIDE'                                                         ? 'C2 H6 O S'          
78.133  
GLN 'L-peptide linking' y GLUTAMINE                                                                    ? 'C5 H10 N2 O3'       
146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                                              ? 'C5 H9 N O4'         
147.129 
GLY 'peptide linking'   y GLYCINE                                                                      ? 'C2 H5 N O2'         
75.067  
HIS 'L-peptide linking' y HISTIDINE                                                                    ? 'C6 H10 N3 O2 1'     
156.162 
HOH non-polymer         . WATER                                                                        ? 'H2 O'               
18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                                                   ? 'C6 H13 N O2'        
131.173 
LEU 'L-peptide linking' y LEUCINE                                                                      ? 'C6 H13 N O2'        
131.173 
LYS 'L-peptide linking' y LYSINE                                                                       ? 'C6 H15 N2 O2 1'     
147.195 
MET 'L-peptide linking' y METHIONINE                                                                   ? 'C5 H11 N O2 S'      
149.211 
NA  non-polymer         . 'SODIUM ION'                                                                 ? 'Na 1'               
22.990  
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 
V50 non-polymer         . '4-[(4,6-dimethylpyrimidin-2-yl)thio]-2,3,5,6-tetrafluorobenzenesulfonamide' ? 'C12 H9 F4 N3 O2 S2' 
367.342 
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 V50 1   302 1   V50 V50 A . 
D 4 NA  1   303 1   NA  NA  A . 
E 5 DMS 1   304 1   DMS DMS A . 
F 6 HOH 1   401 259 HOH HOH A . 
F 6 HOH 2   402 217 HOH HOH A . 
F 6 HOH 3   403 232 HOH HOH A . 
F 6 HOH 4   404 140 HOH HOH A . 
F 6 HOH 5   405 220 HOH HOH A . 
F 6 HOH 6   406 68  HOH HOH A . 
F 6 HOH 7   407 39  HOH HOH A . 
F 6 HOH 8   408 71  HOH HOH A . 
F 6 HOH 9   409 133 HOH HOH A . 
F 6 HOH 10  410 237 HOH HOH A . 
F 6 HOH 11  411 226 HOH HOH A . 
F 6 HOH 12  412 146 HOH HOH A . 
F 6 HOH 13  413 116 HOH HOH A . 
F 6 HOH 14  414 59  HOH HOH A . 
F 6 HOH 15  415 252 HOH HOH A . 
F 6 HOH 16  416 224 HOH HOH A . 
F 6 HOH 17  417 172 HOH HOH A . 
F 6 HOH 18  418 160 HOH HOH A . 
F 6 HOH 19  419 125 HOH HOH A . 
F 6 HOH 20  420 152 HOH HOH A . 
F 6 HOH 21  421 31  HOH HOH A . 
F 6 HOH 22  422 102 HOH HOH A . 
F 6 HOH 23  423 170 HOH HOH A . 
F 6 HOH 24  424 111 HOH HOH A . 
F 6 HOH 25  425 93  HOH HOH A . 
F 6 HOH 26  426 85  HOH HOH A . 
F 6 HOH 27  427 205 HOH HOH A . 
F 6 HOH 28  428 153 HOH HOH A . 
F 6 HOH 29  429 255 HOH HOH A . 
F 6 HOH 30  430 80  HOH HOH A . 
F 6 HOH 31  431 200 HOH HOH A . 
F 6 HOH 32  432 44  HOH HOH A . 
F 6 HOH 33  433 47  HOH HOH A . 
F 6 HOH 34  434 221 HOH HOH A . 
F 6 HOH 35  435 135 HOH HOH A . 
F 6 HOH 36  436 6   HOH HOH A . 
F 6 HOH 37  437 1   HOH HOH A . 
F 6 HOH 38  438 18  HOH HOH A . 
F 6 HOH 39  439 38  HOH HOH A . 
F 6 HOH 40  440 26  HOH HOH A . 
F 6 HOH 41  441 113 HOH HOH A . 
F 6 HOH 42  442 243 HOH HOH A . 
F 6 HOH 43  443 183 HOH HOH A . 
F 6 HOH 44  444 132 HOH HOH A . 
F 6 HOH 45  445 163 HOH HOH A . 
F 6 HOH 46  446 194 HOH HOH A . 
F 6 HOH 47  447 69  HOH HOH A . 
F 6 HOH 48  448 228 HOH HOH A . 
F 6 HOH 49  449 35  HOH HOH A . 
F 6 HOH 50  450 127 HOH HOH A . 
F 6 HOH 51  451 9   HOH HOH A . 
F 6 HOH 52  452 37  HOH HOH A . 
F 6 HOH 53  453 10  HOH HOH A . 
F 6 HOH 54  454 55  HOH HOH A . 
F 6 HOH 55  455 136 HOH HOH A . 
F 6 HOH 56  456 117 HOH HOH A . 
F 6 HOH 57  457 33  HOH HOH A . 
F 6 HOH 58  458 84  HOH HOH A . 
F 6 HOH 59  459 12  HOH HOH A . 
F 6 HOH 60  460 90  HOH HOH A . 
F 6 HOH 61  461 147 HOH HOH A . 
F 6 HOH 62  462 202 HOH HOH A . 
F 6 HOH 63  463 175 HOH HOH A . 
F 6 HOH 64  464 138 HOH HOH A . 
F 6 HOH 65  465 81  HOH HOH A . 
F 6 HOH 66  466 45  HOH HOH A . 
F 6 HOH 67  467 130 HOH HOH A . 
F 6 HOH 68  468 149 HOH HOH A . 
F 6 HOH 69  469 253 HOH HOH A . 
F 6 HOH 70  470 51  HOH HOH A . 
F 6 HOH 71  471 14  HOH HOH A . 
F 6 HOH 72  472 193 HOH HOH A . 
F 6 HOH 73  473 141 HOH HOH A . 
F 6 HOH 74  474 67  HOH HOH A . 
F 6 HOH 75  475 7   HOH HOH A . 
F 6 HOH 76  476 2   HOH HOH A . 
F 6 HOH 77  477 161 HOH HOH A . 
F 6 HOH 78  478 124 HOH HOH A . 
F 6 HOH 79  479 43  HOH HOH A . 
F 6 HOH 80  480 78  HOH HOH A . 
F 6 HOH 81  481 142 HOH HOH A . 
F 6 HOH 82  482 27  HOH HOH A . 
F 6 HOH 83  483 96  HOH HOH A . 
F 6 HOH 84  484 145 HOH HOH A . 
F 6 HOH 85  485 61  HOH HOH A . 
F 6 HOH 86  486 56  HOH HOH A . 
F 6 HOH 87  487 88  HOH HOH A . 
F 6 HOH 88  488 17  HOH HOH A . 
F 6 HOH 89  489 52  HOH HOH A . 
F 6 HOH 90  490 20  HOH HOH A . 
F 6 HOH 91  491 32  HOH HOH A . 
F 6 HOH 92  492 19  HOH HOH A . 
F 6 HOH 93  493 57  HOH HOH A . 
F 6 HOH 94  494 107 HOH HOH A . 
F 6 HOH 95  495 70  HOH HOH A . 
F 6 HOH 96  496 62  HOH HOH A . 
F 6 HOH 97  497 5   HOH HOH A . 
F 6 HOH 98  498 29  HOH HOH A . 
F 6 HOH 99  499 63  HOH HOH A . 
F 6 HOH 100 500 219 HOH HOH A . 
F 6 HOH 101 501 76  HOH HOH A . 
F 6 HOH 102 502 95  HOH HOH A . 
F 6 HOH 103 503 112 HOH HOH A . 
F 6 HOH 104 504 4   HOH HOH A . 
F 6 HOH 105 505 106 HOH HOH A . 
F 6 HOH 106 506 23  HOH HOH A . 
F 6 HOH 107 507 210 HOH HOH A . 
F 6 HOH 108 508 22  HOH HOH A . 
F 6 HOH 109 509 8   HOH HOH A . 
F 6 HOH 110 510 28  HOH HOH A . 
F 6 HOH 111 511 231 HOH HOH A . 
F 6 HOH 112 512 179 HOH HOH A . 
F 6 HOH 113 513 159 HOH HOH A . 
F 6 HOH 114 514 15  HOH HOH A . 
F 6 HOH 115 515 190 HOH HOH A . 
F 6 HOH 116 516 206 HOH HOH A . 
F 6 HOH 117 517 36  HOH HOH A . 
F 6 HOH 118 518 240 HOH HOH A . 
F 6 HOH 119 519 192 HOH HOH A . 
F 6 HOH 120 520 208 HOH HOH A . 
F 6 HOH 121 521 164 HOH HOH A . 
F 6 HOH 122 522 245 HOH HOH A . 
F 6 HOH 123 523 58  HOH HOH A . 
F 6 HOH 124 524 236 HOH HOH A . 
F 6 HOH 125 525 66  HOH HOH A . 
F 6 HOH 126 526 72  HOH HOH A . 
F 6 HOH 127 527 187 HOH HOH A . 
F 6 HOH 128 528 75  HOH HOH A . 
F 6 HOH 129 529 64  HOH HOH A . 
F 6 HOH 130 530 103 HOH HOH A . 
F 6 HOH 131 531 122 HOH HOH A . 
F 6 HOH 132 532 188 HOH HOH A . 
F 6 HOH 133 533 30  HOH HOH A . 
F 6 HOH 134 534 13  HOH HOH A . 
F 6 HOH 135 535 24  HOH HOH A . 
F 6 HOH 136 536 214 HOH HOH A . 
F 6 HOH 137 537 16  HOH HOH A . 
F 6 HOH 138 538 25  HOH HOH A . 
F 6 HOH 139 539 173 HOH HOH A . 
F 6 HOH 140 540 92  HOH HOH A . 
F 6 HOH 141 541 79  HOH HOH A . 
F 6 HOH 142 542 143 HOH HOH A . 
F 6 HOH 143 543 53  HOH HOH A . 
F 6 HOH 144 544 21  HOH HOH A . 
F 6 HOH 145 545 195 HOH HOH A . 
F 6 HOH 146 546 218 HOH HOH A . 
F 6 HOH 147 547 77  HOH HOH A . 
F 6 HOH 148 548 258 HOH HOH A . 
F 6 HOH 149 549 182 HOH HOH A . 
F 6 HOH 150 550 65  HOH HOH A . 
F 6 HOH 151 551 126 HOH HOH A . 
F 6 HOH 152 552 201 HOH HOH A . 
F 6 HOH 153 553 87  HOH HOH A . 
F 6 HOH 154 554 50  HOH HOH A . 
F 6 HOH 155 555 40  HOH HOH A . 
F 6 HOH 156 556 151 HOH HOH A . 
F 6 HOH 157 557 189 HOH HOH A . 
F 6 HOH 158 558 131 HOH HOH A . 
F 6 HOH 159 559 119 HOH HOH A . 
F 6 HOH 160 560 251 HOH HOH A . 
F 6 HOH 161 561 3   HOH HOH A . 
F 6 HOH 162 562 48  HOH HOH A . 
F 6 HOH 163 563 115 HOH HOH A . 
F 6 HOH 164 564 120 HOH HOH A . 
F 6 HOH 165 565 105 HOH HOH A . 
F 6 HOH 166 566 177 HOH HOH A . 
F 6 HOH 167 567 94  HOH HOH A . 
F 6 HOH 168 568 86  HOH HOH A . 
F 6 HOH 169 569 108 HOH HOH A . 
F 6 HOH 170 570 129 HOH HOH A . 
F 6 HOH 171 571 222 HOH HOH A . 
F 6 HOH 172 572 109 HOH HOH A . 
F 6 HOH 173 573 91  HOH HOH A . 
F 6 HOH 174 574 11  HOH HOH A . 
F 6 HOH 175 575 233 HOH HOH A . 
F 6 HOH 176 576 242 HOH HOH A . 
F 6 HOH 177 577 215 HOH HOH A . 
F 6 HOH 178 578 60  HOH HOH A . 
F 6 HOH 179 579 54  HOH HOH A . 
F 6 HOH 180 580 157 HOH HOH A . 
F 6 HOH 181 581 254 HOH HOH A . 
F 6 HOH 182 582 42  HOH HOH A . 
F 6 HOH 183 583 110 HOH HOH A . 
F 6 HOH 184 584 118 HOH HOH A . 
F 6 HOH 185 585 246 HOH HOH A . 
F 6 HOH 186 586 121 HOH HOH A . 
F 6 HOH 187 587 123 HOH HOH A . 
F 6 HOH 188 588 97  HOH HOH A . 
F 6 HOH 189 589 197 HOH HOH A . 
F 6 HOH 190 590 241 HOH HOH A . 
F 6 HOH 191 591 134 HOH HOH A . 
F 6 HOH 192 592 203 HOH HOH A . 
F 6 HOH 193 593 74  HOH HOH A . 
F 6 HOH 194 594 34  HOH HOH A . 
F 6 HOH 195 595 104 HOH HOH A . 
F 6 HOH 196 596 167 HOH HOH A . 
F 6 HOH 197 597 148 HOH HOH A . 
F 6 HOH 198 598 247 HOH HOH A . 
F 6 HOH 199 599 155 HOH HOH A . 
F 6 HOH 200 600 209 HOH HOH A . 
F 6 HOH 201 601 150 HOH HOH A . 
F 6 HOH 202 602 198 HOH HOH A . 
F 6 HOH 203 603 128 HOH HOH A . 
F 6 HOH 204 604 230 HOH HOH A . 
F 6 HOH 205 605 234 HOH HOH A . 
F 6 HOH 206 606 98  HOH HOH A . 
F 6 HOH 207 607 49  HOH HOH A . 
F 6 HOH 208 608 137 HOH HOH A . 
F 6 HOH 209 609 101 HOH HOH A . 
F 6 HOH 210 610 213 HOH HOH A . 
F 6 HOH 211 611 162 HOH HOH A . 
F 6 HOH 212 612 89  HOH HOH A . 
F 6 HOH 213 613 238 HOH HOH A . 
F 6 HOH 214 614 83  HOH HOH A . 
F 6 HOH 215 615 239 HOH HOH A . 
F 6 HOH 216 616 244 HOH HOH A . 
F 6 HOH 217 617 100 HOH HOH A . 
F 6 HOH 218 618 165 HOH HOH A . 
F 6 HOH 219 619 196 HOH HOH A . 
F 6 HOH 220 620 82  HOH HOH A . 
F 6 HOH 221 621 139 HOH HOH A . 
F 6 HOH 222 622 46  HOH HOH A . 
F 6 HOH 223 623 114 HOH HOH A . 
F 6 HOH 224 624 171 HOH HOH A . 
F 6 HOH 225 625 227 HOH HOH A . 
F 6 HOH 226 626 223 HOH HOH A . 
F 6 HOH 227 627 207 HOH HOH A . 
F 6 HOH 228 628 261 HOH HOH A . 
F 6 HOH 229 629 184 HOH HOH A . 
F 6 HOH 230 630 260 HOH HOH A . 
F 6 HOH 231 631 181 HOH HOH A . 
F 6 HOH 232 632 174 HOH HOH A . 
F 6 HOH 233 633 73  HOH HOH A . 
F 6 HOH 234 634 256 HOH HOH A . 
F 6 HOH 235 635 158 HOH HOH A . 
F 6 HOH 236 636 257 HOH HOH A . 
F 6 HOH 237 637 99  HOH HOH A . 
F 6 HOH 238 638 169 HOH HOH A . 
F 6 HOH 239 639 144 HOH HOH A . 
F 6 HOH 240 640 180 HOH HOH A . 
F 6 HOH 241 641 186 HOH HOH A . 
F 6 HOH 242 642 216 HOH HOH A . 
F 6 HOH 243 643 176 HOH HOH A . 
F 6 HOH 244 644 178 HOH HOH A . 
F 6 HOH 245 645 204 HOH HOH A . 
F 6 HOH 246 646 249 HOH HOH A . 
F 6 HOH 247 647 248 HOH HOH A . 
F 6 HOH 248 648 154 HOH HOH A . 
F 6 HOH 249 649 212 HOH HOH A . 
F 6 HOH 250 650 41  HOH HOH A . 
F 6 HOH 251 651 225 HOH HOH A . 
F 6 HOH 252 652 166 HOH HOH A . 
F 6 HOH 253 653 199 HOH HOH A . 
F 6 HOH 254 654 168 HOH HOH A . 
F 6 HOH 255 655 250 HOH HOH A . 
F 6 HOH 256 656 156 HOH HOH A . 
F 6 HOH 257 657 191 HOH HOH A . 
F 6 HOH 258 658 211 HOH HOH A . 
F 6 HOH 259 659 229 HOH HOH A . 
F 6 HOH 260 660 235 HOH HOH A . 
F 6 HOH 261 661 185 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  ? NZ  ? A LYS 45  NZ  
6  1 Y 1 A LYS 80  ? NZ  ? A LYS 80  NZ  
7  1 Y 1 A LYS 148 ? NZ  ? A LYS 148 NZ  
8  1 Y 1 A LYS 158 ? CD  ? A LYS 158 CD  
9  1 Y 1 A LYS 158 ? CE  ? A LYS 158 CE  
10 1 Y 1 A LYS 158 ? NZ  ? A LYS 158 NZ  
11 1 Y 1 A GLN 254 ? CD  ? A GLN 254 CD  
12 1 Y 1 A GLN 254 ? OE1 ? A GLN 254 OE1 
13 1 Y 1 A GLN 254 ? NE2 ? A GLN 254 NE2 
14 1 Y 1 A LYS 256 ? CE  ? A LYS 256 CE  
15 1 Y 1 A LYS 256 ? NZ  ? A LYS 256 NZ  
16 1 Y 1 A LYS 260 ? CG  ? A LYS 260 CG  
17 1 Y 1 A LYS 260 ? CD  ? A LYS 260 CD  
18 1 Y 1 A LYS 260 ? CE  ? A LYS 260 CE  
19 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                   104.200 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     7NZW 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     42.222 
_cell.length_a_esd                 ? 
_cell.length_b                     41.289 
_cell.length_b_esd                 ? 
_cell.length_c                     71.468 
_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                         7NZW 
_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                   7NZW 
_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            2.06 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         40.17 
_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                         7NZW 
_reflns.data_reduction_details           ? 
_reflns.data_reduction_method            ? 
_reflns.d_resolution_high                1.450 
_reflns.d_resolution_low                 69.285 
_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                       42212 
_reflns.number_obs                       42212 
_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             99.200 
_reflns.R_free_details                   ? 
_reflns.Rmerge_F_all                     ? 
_reflns.Rmerge_F_obs                     ? 
_reflns.Friedel_coverage                 ? 
_reflns.number_gt                        ? 
_reflns.threshold_expression             ? 
_reflns.pdbx_redundancy                  6.800 
_reflns.pdbx_Rmerge_I_obs                ? 
_reflns.pdbx_Rmerge_I_all                ? 
_reflns.pdbx_Rsym_value                  0.053 
_reflns.pdbx_netI_over_av_sigmaI         8.100 
_reflns.pdbx_netI_over_sigmaI            16.000 
_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                  0.062 
_reflns.pdbx_Rpim_I_all                  0.023 
_reflns.pdbx_d_opt                       ? 
_reflns.pdbx_number_measured_all         285097 
_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 
1.450 1.530  ? 2.500  40590 ? ? ? 6128 99.100 ? ? ? ? 0.296 ? ? ? ? ? ? ? ? 6.600 0.296 ? ? 5.100  0.351 0.135 ? 1  1 ? ? ? 
1.530 1.620  ? 3.800  38388 ? ? ? 5740 98.300 ? ? ? ? 0.198 ? ? ? ? ? ? ? ? 6.700 0.198 ? ? 6.800  0.236 0.090 ? 2  1 ? ? ? 
1.620 1.730  ? 5.200  37340 ? ? ? 5475 99.700 ? ? ? ? 0.143 ? ? ? ? ? ? ? ? 6.800 0.143 ? ? 9.100  0.169 0.064 ? 3  1 ? ? ? 
1.730 1.870  ? 7.400  33057 ? ? ? 5039 98.300 ? ? ? ? 0.099 ? ? ? ? ? ? ? ? 6.600 0.099 ? ? 11.900 0.118 0.045 ? 4  1 ? ? ? 
1.870 2.050  ? 9.800  32838 ? ? ? 4725 99.900 ? ? ? ? 0.071 ? ? ? ? ? ? ? ? 6.900 0.071 ? ? 16.900 0.085 0.032 ? 5  1 ? ? ? 
2.050 2.290  ? 12.100 28836 ? ? ? 4259 99.700 ? ? ? ? 0.056 ? ? ? ? ? ? ? ? 6.800 0.056 ? ? 21.400 0.067 0.025 ? 6  1 ? ? ? 
2.290 2.650  ? 13.400 25921 ? ? ? 3747 99.000 ? ? ? ? 0.050 ? ? ? ? ? ? ? ? 6.900 0.050 ? ? 24.800 0.059 0.022 ? 7  1 ? ? ? 
2.650 3.240  ? 14.400 21982 ? ? ? 3212 99.600 ? ? ? ? 0.045 ? ? ? ? ? ? ? ? 6.800 0.045 ? ? 29.900 0.053 0.020 ? 8  1 ? ? ? 
3.240 4.590  ? 15.400 16959 ? ? ? 2489 99.400 ? ? ? ? 0.041 ? ? ? ? ? ? ? ? 6.800 0.041 ? ? 35.600 0.046 0.017 ? 9  1 ? ? ? 
4.590 69.285 ? 16.600 9186  ? ? ? 1398 99.300 ? ? ? ? 0.037 ? ? ? ? ? ? ? ? 6.600 0.037 ? ? 34.300 0.042 0.016 ? 10 1 ? ? ? 
# 
_refine.aniso_B[1][1]                            -0.2900 
_refine.aniso_B[1][2]                            -0.0000 
_refine.aniso_B[1][3]                            0.1000 
_refine.aniso_B[2][2]                            -0.4400 
_refine.aniso_B[2][3]                            -0.0000 
_refine.aniso_B[3][3]                            0.6000 
_refine.B_iso_max                                60.910 
_refine.B_iso_mean                               18.7530 
_refine.B_iso_min                                8.050 
_refine.correlation_coeff_Fo_to_Fc               0.9680 
_refine.correlation_coeff_Fo_to_Fc_free          0.9540 
_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                                 7NZW 
_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                            1.4500 
_refine.ls_d_res_low                             69.2800 
_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                     37979 
_refine.ls_number_reflns_R_free                  4219 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.0800 
_refine.ls_percent_reflns_R_free                 10.0000 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1756 
_refine.ls_R_factor_R_free                       0.2062 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1722 
_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                       0.0760 
_refine.pdbx_overall_ESU_R_Free                  0.0780 
_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                       1.4500 
_refine_hist.d_res_low                        69.2800 
_refine_hist.number_atoms_solvent             261 
_refine_hist.number_atoms_total               2349 
_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           19.30 
_refine_hist.pdbx_B_iso_mean_solvent          30.00 
_refine_hist.pdbx_number_atoms_protein        2036 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         52 
_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  2231 ? r_bond_refined_d       ? ? 
'X-RAY DIFFRACTION' ? 1.999  1.671  3053 ? r_angle_refined_deg    ? ? 
'X-RAY DIFFRACTION' ? 7.292  5.000  273  ? r_dihedral_angle_1_deg ? ? 
'X-RAY DIFFRACTION' ? 35.727 23.211 109  ? r_dihedral_angle_2_deg ? ? 
'X-RAY DIFFRACTION' ? 13.381 15.000 355  ? r_dihedral_angle_3_deg ? ? 
'X-RAY DIFFRACTION' ? 19.606 15.000 9    ? r_dihedral_angle_4_deg ? ? 
'X-RAY DIFFRACTION' ? 0.133  0.200  268  ? r_chiral_restr         ? ? 
'X-RAY DIFFRACTION' ? 0.014  0.020  1767 ? r_gen_planes_refined   ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.4500 
_refine_ls_shell.d_res_low                        1.4880 
_refine_ls_shell.number_reflns_all                3100 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             307 
_refine_ls_shell.number_reflns_R_work             2793 
_refine_ls_shell.percent_reflns_obs               99.5200 
_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                  0.2490 
_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                     7NZW 
_struct.title                        
'Crystal structure of chimeric carbonic anhydrase VA with 4-[(4,6-dimethylpyrimidin-2-yl)thio]-2,3,5,6-tetrafluorobenzenesulfonamide' 
_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        7NZW 
_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 5 ? 
F N N 6 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CAH2_HUMAN 
_struct_ref.pdbx_db_accession          P00918 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              7NZW 
_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 7NZW THR A 62  ? UNP P00918 ASN 62  'engineered mutation' 62  1 
1 7NZW TYR A 64  ? UNP P00918 HIS 64  'engineered mutation' 64  2 
1 7NZW LEU A 65  ? UNP P00918 ALA 65  'engineered mutation' 65  3 
1 7NZW GLN A 67  ? UNP P00918 ASN 67  'engineered mutation' 67  4 
1 7NZW LYS A 91  ? UNP P00918 ILE 91  'engineered mutation' 91  5 
1 7NZW TYR A 130 ? UNP P00918 PHE 130 'engineered mutation' 130 6 
1 7NZW 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)' 330   ? 
1 MORE         -4    ? 
1 'SSA (A^2)'  11280 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 GLY A 12  ? ASP A 19  ? GLY A 12  ASP A 19  5 ? 8 
HELX_P HELX_P2 AA2 PHE A 20  ? GLY A 25  ? PHE A 20  GLY A 25  5 ? 6 
HELX_P HELX_P3 AA3 LYS A 126 ? GLY A 128 ? LYS A 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 SER 73  OG  ? ? ? 1_555 D NA  . NA  ? ? A SER 73  A NA  303 1_555 ? ? ? ? ? ? ? 2.275 ? ? 
metalc2  metalc ? ? A HIS 94  NE2 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 94  A ZN  301 1_555 ? ? ? ? ? ? ? 2.025 ? ? 
metalc3  metalc ? ? A HIS 96  NE2 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 96  A ZN  301 1_555 ? ? ? ? ? ? ? 2.031 ? ? 
metalc4  metalc ? ? A HIS 119 ND1 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 119 A ZN  301 1_555 ? ? ? ? ? ? ? 2.049 ? ? 
metalc5  metalc ? ? A SER 219 OG  ? ? ? 1_555 D NA  . NA  ? ? A SER 219 A NA  303 1_545 ? ? ? ? ? ? ? 2.517 ? ? 
metalc6  metalc ? ? B ZN  .   ZN  ? ? ? 1_555 C V50 . N23 A ? A ZN  301 A V50 302 1_555 ? ? ? ? ? ? ? 1.985 ? ? 
metalc7  metalc ? ? B ZN  .   ZN  ? ? ? 1_555 C V50 . N23 C ? A ZN  301 A V50 302 1_555 ? ? ? ? ? ? ? 1.927 ? ? 
metalc8  metalc ? ? D NA  .   NA  ? ? ? 1_555 F HOH . O   ? ? A NA  303 A HOH 411 1_555 ? ? ? ? ? ? ? 2.451 ? ? 
metalc9  metalc ? ? D NA  .   NA  ? ? ? 1_555 F HOH . O   ? ? A NA  303 A HOH 445 1_565 ? ? ? ? ? ? ? 2.085 ? ? 
metalc10 metalc ? ? D NA  .   NA  ? ? ? 1_555 F HOH . O   ? ? A NA  303 A HOH 473 1_565 ? ? ? ? ? ? ? 2.096 ? ? 
metalc11 metalc ? ? D NA  .   NA  ? ? ? 1_555 F HOH . O   ? ? A NA  303 A HOH 517 1_565 ? ? ? ? ? ? ? 2.479 ? ? 
# 
_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  OG  ? A SER 73  ? A SER 73  ? 1_555 NA ? D NA . ? A NA 303 ? 1_555 OG  ? A SER 219 ? A SER 219 ? 1_555 36.5  ? 
2  OG  ? A SER 73  ? A SER 73  ? 1_555 NA ? D NA . ? A NA 303 ? 1_555 O   ? F HOH .   ? A HOH 411 ? 1_555 70.9  ? 
3  OG  ? A SER 219 ? A SER 219 ? 1_555 NA ? D NA . ? A NA 303 ? 1_555 O   ? F HOH .   ? A HOH 411 ? 1_555 43.4  ? 
4  OG  ? A SER 73  ? A SER 73  ? 1_555 NA ? D NA . ? A NA 303 ? 1_555 O   ? F HOH .   ? A HOH 445 ? 1_565 161.0 ? 
5  OG  ? A SER 219 ? A SER 219 ? 1_555 NA ? D NA . ? A NA 303 ? 1_555 O   ? F HOH .   ? A HOH 445 ? 1_565 128.9 ? 
6  O   ? F HOH .   ? A HOH 411 ? 1_555 NA ? D NA . ? A NA 303 ? 1_555 O   ? F HOH .   ? A HOH 445 ? 1_565 90.5  ? 
7  OG  ? A SER 73  ? A SER 73  ? 1_555 NA ? D NA . ? A NA 303 ? 1_555 O   ? F HOH .   ? A HOH 473 ? 1_565 86.3  ? 
8  OG  ? A SER 219 ? A SER 219 ? 1_555 NA ? D NA . ? A NA 303 ? 1_555 O   ? F HOH .   ? A HOH 473 ? 1_565 63.8  ? 
9  O   ? F HOH .   ? A HOH 411 ? 1_555 NA ? D NA . ? A NA 303 ? 1_555 O   ? F HOH .   ? A HOH 473 ? 1_565 82.4  ? 
10 O   ? F HOH .   ? A HOH 445 ? 1_565 NA ? D NA . ? A NA 303 ? 1_555 O   ? F HOH .   ? A HOH 473 ? 1_565 95.3  ? 
11 OG  ? A SER 73  ? A SER 73  ? 1_555 NA ? D NA . ? A NA 303 ? 1_555 O   ? F HOH .   ? A HOH 517 ? 1_565 99.1  ? 
12 OG  ? A SER 219 ? A SER 219 ? 1_555 NA ? D NA . ? A NA 303 ? 1_555 O   ? F HOH .   ? A HOH 517 ? 1_565 129.5 ? 
13 O   ? F HOH .   ? A HOH 411 ? 1_555 NA ? D NA . ? A NA 303 ? 1_555 O   ? F HOH .   ? A HOH 517 ? 1_565 117.1 ? 
14 O   ? F HOH .   ? A HOH 445 ? 1_565 NA ? D NA . ? A NA 303 ? 1_555 O   ? F HOH .   ? A HOH 517 ? 1_565 85.6  ? 
15 O   ? F HOH .   ? A HOH 473 ? 1_565 NA ? D NA . ? A NA 303 ? 1_555 O   ? F HOH .   ? A HOH 517 ? 1_565 160.5 ? 
16 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_555 101.6 ? 
17 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 ? 
18 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_555 100.9 ? 
19 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N23 A C V50 .   ? A V50 302 ? 1_555 119.1 ? 
20 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N23 A C V50 .   ? A V50 302 ? 1_555 116.7 ? 
21 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N23 A C V50 .   ? A V50 302 ? 1_555 107.8 ? 
22 NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N23 C C V50 .   ? A V50 302 ? 1_555 107.1 ? 
23 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N23 C C V50 .   ? A V50 302 ? 1_555 111.7 ? 
24 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N23 C C V50 .   ? A V50 302 ? 1_555 124.2 ? 
25 N23 A C V50 .   ? A V50 302 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N23 C C V50 .   ? A V50 302 ? 1_555 16.6  ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 SER 29  A . ? SER 29  A PRO 30  A ? PRO 30  A 1 -0.72 
2 PRO 200 A . ? PRO 200 A PRO 201 A ? PRO 201 A 1 4.98  
# 
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 HIS A 119 ? O HIS A 119 N HIS A 94  ? N HIS A 94  
AA2 7 8  O PHE A 93  ? O PHE A 93  N VAL A 68  ? N VAL A 68  
AA2 8 9  O GLU A 69  ? O GLU A 69  N 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 HIS A 94  ? N HIS A 94  O HIS A 119 ? O HIS A 119 
AA3 4 5  N LEU A 118 ? N LEU A 118 O ILE A 145 ? O ILE A 145 
AA3 5 6  N PHE A 146 ? N PHE A 146 O ILE A 215 ? O ILE A 215 
# 
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  ? ? -144.75 19.30   
2 1 LYS A 76  ? ? -101.26 -85.97  
3 1 ASN A 243 ? ? -96.92  53.42   
4 1 LYS A 251 ? ? 60.16   -145.59 
5 1 LYS A 251 ? ? 60.16   -136.63 
# 
_pdbx_validate_main_chain_plane.id                       1 
_pdbx_validate_main_chain_plane.PDB_model_num            1 
_pdbx_validate_main_chain_plane.auth_comp_id             LYS 
_pdbx_validate_main_chain_plane.auth_asym_id             A 
_pdbx_validate_main_chain_plane.auth_seq_id              251 
_pdbx_validate_main_chain_plane.PDB_ins_code             ? 
_pdbx_validate_main_chain_plane.label_alt_id             ? 
_pdbx_validate_main_chain_plane.improper_torsion_angle   -12.86 
# 
_pdbx_entry_details.entry_id                 7NZW 
_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         ? 
# 
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 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CYS N    N  N N 74  
CYS CA   C  N R 75  
CYS C    C  N N 76  
CYS O    O  N N 77  
CYS CB   C  N N 78  
CYS SG   S  N N 79  
CYS OXT  O  N N 80  
CYS H    H  N N 81  
CYS H2   H  N N 82  
CYS HA   H  N N 83  
CYS HB2  H  N N 84  
CYS HB3  H  N N 85  
CYS HG   H  N N 86  
CYS HXT  H  N N 87  
DMS S    S  N N 88  
DMS O    O  N N 89  
DMS C1   C  N N 90  
DMS C2   C  N N 91  
DMS H11  H  N N 92  
DMS H12  H  N N 93  
DMS H13  H  N N 94  
DMS H21  H  N N 95  
DMS H22  H  N N 96  
DMS H23  H  N N 97  
GLN N    N  N N 98  
GLN CA   C  N S 99  
GLN C    C  N N 100 
GLN O    O  N N 101 
GLN CB   C  N N 102 
GLN CG   C  N N 103 
GLN CD   C  N N 104 
GLN OE1  O  N N 105 
GLN NE2  N  N N 106 
GLN OXT  O  N N 107 
GLN H    H  N N 108 
GLN H2   H  N N 109 
GLN HA   H  N N 110 
GLN HB2  H  N N 111 
GLN HB3  H  N N 112 
GLN HG2  H  N N 113 
GLN HG3  H  N N 114 
GLN HE21 H  N N 115 
GLN HE22 H  N N 116 
GLN HXT  H  N N 117 
GLU N    N  N N 118 
GLU CA   C  N S 119 
GLU C    C  N N 120 
GLU O    O  N N 121 
GLU CB   C  N N 122 
GLU CG   C  N N 123 
GLU CD   C  N N 124 
GLU OE1  O  N N 125 
GLU OE2  O  N N 126 
GLU OXT  O  N N 127 
GLU H    H  N N 128 
GLU H2   H  N N 129 
GLU HA   H  N N 130 
GLU HB2  H  N N 131 
GLU HB3  H  N N 132 
GLU HG2  H  N N 133 
GLU HG3  H  N N 134 
GLU HE2  H  N N 135 
GLU HXT  H  N N 136 
GLY N    N  N N 137 
GLY CA   C  N N 138 
GLY C    C  N N 139 
GLY O    O  N N 140 
GLY OXT  O  N N 141 
GLY H    H  N N 142 
GLY H2   H  N N 143 
GLY HA2  H  N N 144 
GLY HA3  H  N N 145 
GLY HXT  H  N N 146 
HIS N    N  N N 147 
HIS CA   C  N S 148 
HIS C    C  N N 149 
HIS O    O  N N 150 
HIS CB   C  N N 151 
HIS CG   C  Y N 152 
HIS ND1  N  Y N 153 
HIS CD2  C  Y N 154 
HIS CE1  C  Y N 155 
HIS NE2  N  Y N 156 
HIS OXT  O  N N 157 
HIS H    H  N N 158 
HIS H2   H  N N 159 
HIS HA   H  N N 160 
HIS HB2  H  N N 161 
HIS HB3  H  N N 162 
HIS HD1  H  N N 163 
HIS HD2  H  N N 164 
HIS HE1  H  N N 165 
HIS HE2  H  N N 166 
HIS HXT  H  N N 167 
HOH O    O  N N 168 
HOH H1   H  N N 169 
HOH H2   H  N N 170 
ILE N    N  N N 171 
ILE CA   C  N S 172 
ILE C    C  N N 173 
ILE O    O  N N 174 
ILE CB   C  N S 175 
ILE CG1  C  N N 176 
ILE CG2  C  N N 177 
ILE CD1  C  N N 178 
ILE OXT  O  N N 179 
ILE H    H  N N 180 
ILE H2   H  N N 181 
ILE HA   H  N N 182 
ILE HB   H  N N 183 
ILE HG12 H  N N 184 
ILE HG13 H  N N 185 
ILE HG21 H  N N 186 
ILE HG22 H  N N 187 
ILE HG23 H  N N 188 
ILE HD11 H  N N 189 
ILE HD12 H  N N 190 
ILE HD13 H  N N 191 
ILE HXT  H  N N 192 
LEU N    N  N N 193 
LEU CA   C  N S 194 
LEU C    C  N N 195 
LEU O    O  N N 196 
LEU CB   C  N N 197 
LEU CG   C  N N 198 
LEU CD1  C  N N 199 
LEU CD2  C  N N 200 
LEU OXT  O  N N 201 
LEU H    H  N N 202 
LEU H2   H  N N 203 
LEU HA   H  N N 204 
LEU HB2  H  N N 205 
LEU HB3  H  N N 206 
LEU HG   H  N N 207 
LEU HD11 H  N N 208 
LEU HD12 H  N N 209 
LEU HD13 H  N N 210 
LEU HD21 H  N N 211 
LEU HD22 H  N N 212 
LEU HD23 H  N N 213 
LEU HXT  H  N N 214 
LYS N    N  N N 215 
LYS CA   C  N S 216 
LYS C    C  N N 217 
LYS O    O  N N 218 
LYS CB   C  N N 219 
LYS CG   C  N N 220 
LYS CD   C  N N 221 
LYS CE   C  N N 222 
LYS NZ   N  N N 223 
LYS OXT  O  N N 224 
LYS H    H  N N 225 
LYS H2   H  N N 226 
LYS HA   H  N N 227 
LYS HB2  H  N N 228 
LYS HB3  H  N N 229 
LYS HG2  H  N N 230 
LYS HG3  H  N N 231 
LYS HD2  H  N N 232 
LYS HD3  H  N N 233 
LYS HE2  H  N N 234 
LYS HE3  H  N N 235 
LYS HZ1  H  N N 236 
LYS HZ2  H  N N 237 
LYS HZ3  H  N N 238 
LYS HXT  H  N N 239 
MET N    N  N N 240 
MET CA   C  N S 241 
MET C    C  N N 242 
MET O    O  N N 243 
MET CB   C  N N 244 
MET CG   C  N N 245 
MET SD   S  N N 246 
MET CE   C  N N 247 
MET OXT  O  N N 248 
MET H    H  N N 249 
MET H2   H  N N 250 
MET HA   H  N N 251 
MET HB2  H  N N 252 
MET HB3  H  N N 253 
MET HG2  H  N N 254 
MET HG3  H  N N 255 
MET HE1  H  N N 256 
MET HE2  H  N N 257 
MET HE3  H  N N 258 
MET HXT  H  N N 259 
NA  NA   NA N N 260 
PHE N    N  N N 261 
PHE CA   C  N S 262 
PHE C    C  N N 263 
PHE O    O  N N 264 
PHE CB   C  N N 265 
PHE CG   C  Y N 266 
PHE CD1  C  Y N 267 
PHE CD2  C  Y N 268 
PHE CE1  C  Y N 269 
PHE CE2  C  Y N 270 
PHE CZ   C  Y N 271 
PHE OXT  O  N N 272 
PHE H    H  N N 273 
PHE H2   H  N N 274 
PHE HA   H  N N 275 
PHE HB2  H  N N 276 
PHE HB3  H  N N 277 
PHE HD1  H  N N 278 
PHE HD2  H  N N 279 
PHE HE1  H  N N 280 
PHE HE2  H  N N 281 
PHE HZ   H  N N 282 
PHE HXT  H  N N 283 
PRO N    N  N N 284 
PRO CA   C  N S 285 
PRO C    C  N N 286 
PRO O    O  N N 287 
PRO CB   C  N N 288 
PRO CG   C  N N 289 
PRO CD   C  N N 290 
PRO OXT  O  N N 291 
PRO H    H  N N 292 
PRO HA   H  N N 293 
PRO HB2  H  N N 294 
PRO HB3  H  N N 295 
PRO HG2  H  N N 296 
PRO HG3  H  N N 297 
PRO HD2  H  N N 298 
PRO HD3  H  N N 299 
PRO HXT  H  N N 300 
SER N    N  N N 301 
SER CA   C  N S 302 
SER C    C  N N 303 
SER O    O  N N 304 
SER CB   C  N N 305 
SER OG   O  N N 306 
SER OXT  O  N N 307 
SER H    H  N N 308 
SER H2   H  N N 309 
SER HA   H  N N 310 
SER HB2  H  N N 311 
SER HB3  H  N N 312 
SER HG   H  N N 313 
SER HXT  H  N N 314 
THR N    N  N N 315 
THR CA   C  N S 316 
THR C    C  N N 317 
THR O    O  N N 318 
THR CB   C  N R 319 
THR OG1  O  N N 320 
THR CG2  C  N N 321 
THR OXT  O  N N 322 
THR H    H  N N 323 
THR H2   H  N N 324 
THR HA   H  N N 325 
THR HB   H  N N 326 
THR HG1  H  N N 327 
THR HG21 H  N N 328 
THR HG22 H  N N 329 
THR HG23 H  N N 330 
THR HXT  H  N N 331 
TRP N    N  N N 332 
TRP CA   C  N S 333 
TRP C    C  N N 334 
TRP O    O  N N 335 
TRP CB   C  N N 336 
TRP CG   C  Y N 337 
TRP CD1  C  Y N 338 
TRP CD2  C  Y N 339 
TRP NE1  N  Y N 340 
TRP CE2  C  Y N 341 
TRP CE3  C  Y N 342 
TRP CZ2  C  Y N 343 
TRP CZ3  C  Y N 344 
TRP CH2  C  Y N 345 
TRP OXT  O  N N 346 
TRP H    H  N N 347 
TRP H2   H  N N 348 
TRP HA   H  N N 349 
TRP HB2  H  N N 350 
TRP HB3  H  N N 351 
TRP HD1  H  N N 352 
TRP HE1  H  N N 353 
TRP HE3  H  N N 354 
TRP HZ2  H  N N 355 
TRP HZ3  H  N N 356 
TRP HH2  H  N N 357 
TRP HXT  H  N N 358 
TYR N    N  N N 359 
TYR CA   C  N S 360 
TYR C    C  N N 361 
TYR O    O  N N 362 
TYR CB   C  N N 363 
TYR CG   C  Y N 364 
TYR CD1  C  Y N 365 
TYR CD2  C  Y N 366 
TYR CE1  C  Y N 367 
TYR CE2  C  Y N 368 
TYR CZ   C  Y N 369 
TYR OH   O  N N 370 
TYR OXT  O  N N 371 
TYR H    H  N N 372 
TYR H2   H  N N 373 
TYR HA   H  N N 374 
TYR HB2  H  N N 375 
TYR HB3  H  N N 376 
TYR HD1  H  N N 377 
TYR HD2  H  N N 378 
TYR HE1  H  N N 379 
TYR HE2  H  N N 380 
TYR HH   H  N N 381 
TYR HXT  H  N N 382 
V50 F13  F  N N 383 
V50 C4   C  Y N 384 
V50 C5   C  Y N 385 
V50 S7   S  N N 386 
V50 O9   O  N N 387 
V50 N23  N  N N 388 
V50 O8   O  N N 389 
V50 C6   C  Y N 390 
V50 F11  F  N N 391 
V50 C1   C  Y N 392 
V50 F10  F  N N 393 
V50 C3   C  Y N 394 
V50 F12  F  N N 395 
V50 C2   C  Y N 396 
V50 S14  S  N N 397 
V50 C15  C  Y N 398 
V50 N20  N  Y N 399 
V50 C19  C  Y N 400 
V50 C21  C  N N 401 
V50 C18  C  Y N 402 
V50 C17  C  Y N 403 
V50 N16  N  Y N 404 
V50 C22  C  N N 405 
V50 H1   H  N N 406 
V50 H2   H  N N 407 
V50 H3   H  N N 408 
V50 H4   H  N N 409 
V50 H5   H  N N 410 
V50 H6   H  N N 411 
V50 H7   H  N N 412 
V50 H8   H  N N 413 
V50 H9   H  N N 414 
VAL N    N  N N 415 
VAL CA   C  N S 416 
VAL C    C  N N 417 
VAL O    O  N N 418 
VAL CB   C  N N 419 
VAL CG1  C  N N 420 
VAL CG2  C  N N 421 
VAL OXT  O  N N 422 
VAL H    H  N N 423 
VAL H2   H  N N 424 
VAL HA   H  N N 425 
VAL HB   H  N N 426 
VAL HG11 H  N N 427 
VAL HG12 H  N N 428 
VAL HG13 H  N N 429 
VAL HG21 H  N N 430 
VAL HG22 H  N N 431 
VAL HG23 H  N N 432 
VAL HXT  H  N N 433 
ZN  ZN   ZN N N 434 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
DMS S   O    doub N N 83  
DMS S   C1   sing N N 84  
DMS S   C2   sing N N 85  
DMS C1  H11  sing N N 86  
DMS C1  H12  sing N N 87  
DMS C1  H13  sing N N 88  
DMS C2  H21  sing N N 89  
DMS C2  H22  sing N N 90  
DMS C2  H23  sing N N 91  
GLN N   CA   sing N N 92  
GLN N   H    sing N N 93  
GLN N   H2   sing N N 94  
GLN CA  C    sing N N 95  
GLN CA  CB   sing N N 96  
GLN CA  HA   sing N N 97  
GLN C   O    doub N N 98  
GLN C   OXT  sing N N 99  
GLN CB  CG   sing N N 100 
GLN CB  HB2  sing N N 101 
GLN CB  HB3  sing N N 102 
GLN CG  CD   sing N N 103 
GLN CG  HG2  sing N N 104 
GLN CG  HG3  sing N N 105 
GLN CD  OE1  doub N N 106 
GLN CD  NE2  sing N N 107 
GLN NE2 HE21 sing N N 108 
GLN NE2 HE22 sing N N 109 
GLN OXT HXT  sing N N 110 
GLU N   CA   sing N N 111 
GLU N   H    sing N N 112 
GLU N   H2   sing N N 113 
GLU CA  C    sing N N 114 
GLU CA  CB   sing N N 115 
GLU CA  HA   sing N N 116 
GLU C   O    doub N N 117 
GLU C   OXT  sing N N 118 
GLU CB  CG   sing N N 119 
GLU CB  HB2  sing N N 120 
GLU CB  HB3  sing N N 121 
GLU CG  CD   sing N N 122 
GLU CG  HG2  sing N N 123 
GLU CG  HG3  sing N N 124 
GLU CD  OE1  doub N N 125 
GLU CD  OE2  sing N N 126 
GLU OE2 HE2  sing N N 127 
GLU OXT HXT  sing N N 128 
GLY N   CA   sing N N 129 
GLY N   H    sing N N 130 
GLY N   H2   sing N N 131 
GLY CA  C    sing N N 132 
GLY CA  HA2  sing N N 133 
GLY CA  HA3  sing N N 134 
GLY C   O    doub N N 135 
GLY C   OXT  sing N N 136 
GLY OXT HXT  sing N N 137 
HIS N   CA   sing N N 138 
HIS N   H    sing N N 139 
HIS N   H2   sing N N 140 
HIS CA  C    sing N N 141 
HIS CA  CB   sing N N 142 
HIS CA  HA   sing N N 143 
HIS C   O    doub N N 144 
HIS C   OXT  sing N N 145 
HIS CB  CG   sing N N 146 
HIS CB  HB2  sing N N 147 
HIS CB  HB3  sing N N 148 
HIS CG  ND1  sing Y N 149 
HIS CG  CD2  doub Y N 150 
HIS ND1 CE1  doub Y N 151 
HIS ND1 HD1  sing N N 152 
HIS CD2 NE2  sing Y N 153 
HIS CD2 HD2  sing N N 154 
HIS CE1 NE2  sing Y N 155 
HIS CE1 HE1  sing N N 156 
HIS NE2 HE2  sing N N 157 
HIS OXT HXT  sing N N 158 
HOH O   H1   sing N N 159 
HOH O   H2   sing N N 160 
ILE N   CA   sing N N 161 
ILE N   H    sing N N 162 
ILE N   H2   sing N N 163 
ILE CA  C    sing N N 164 
ILE CA  CB   sing N N 165 
ILE CA  HA   sing N N 166 
ILE C   O    doub N N 167 
ILE C   OXT  sing N N 168 
ILE CB  CG1  sing N N 169 
ILE CB  CG2  sing N N 170 
ILE CB  HB   sing N N 171 
ILE CG1 CD1  sing N N 172 
ILE CG1 HG12 sing N N 173 
ILE CG1 HG13 sing N N 174 
ILE CG2 HG21 sing N N 175 
ILE CG2 HG22 sing N N 176 
ILE CG2 HG23 sing N N 177 
ILE CD1 HD11 sing N N 178 
ILE CD1 HD12 sing N N 179 
ILE CD1 HD13 sing N N 180 
ILE OXT HXT  sing N N 181 
LEU N   CA   sing N N 182 
LEU N   H    sing N N 183 
LEU N   H2   sing N N 184 
LEU CA  C    sing N N 185 
LEU CA  CB   sing N N 186 
LEU CA  HA   sing N N 187 
LEU C   O    doub N N 188 
LEU C   OXT  sing N N 189 
LEU CB  CG   sing N N 190 
LEU CB  HB2  sing N N 191 
LEU CB  HB3  sing N N 192 
LEU CG  CD1  sing N N 193 
LEU CG  CD2  sing N N 194 
LEU CG  HG   sing N N 195 
LEU CD1 HD11 sing N N 196 
LEU CD1 HD12 sing N N 197 
LEU CD1 HD13 sing N N 198 
LEU CD2 HD21 sing N N 199 
LEU CD2 HD22 sing N N 200 
LEU CD2 HD23 sing N N 201 
LEU OXT HXT  sing N N 202 
LYS N   CA   sing N N 203 
LYS N   H    sing N N 204 
LYS N   H2   sing N N 205 
LYS CA  C    sing N N 206 
LYS CA  CB   sing N N 207 
LYS CA  HA   sing N N 208 
LYS C   O    doub N N 209 
LYS C   OXT  sing N N 210 
LYS CB  CG   sing N N 211 
LYS CB  HB2  sing N N 212 
LYS CB  HB3  sing N N 213 
LYS CG  CD   sing N N 214 
LYS CG  HG2  sing N N 215 
LYS CG  HG3  sing N N 216 
LYS CD  CE   sing N N 217 
LYS CD  HD2  sing N N 218 
LYS CD  HD3  sing N N 219 
LYS CE  NZ   sing N N 220 
LYS CE  HE2  sing N N 221 
LYS CE  HE3  sing N N 222 
LYS NZ  HZ1  sing N N 223 
LYS NZ  HZ2  sing N N 224 
LYS NZ  HZ3  sing N N 225 
LYS OXT HXT  sing N N 226 
MET N   CA   sing N N 227 
MET N   H    sing N N 228 
MET N   H2   sing N N 229 
MET CA  C    sing N N 230 
MET CA  CB   sing N N 231 
MET CA  HA   sing N N 232 
MET C   O    doub N N 233 
MET C   OXT  sing N N 234 
MET CB  CG   sing N N 235 
MET CB  HB2  sing N N 236 
MET CB  HB3  sing N N 237 
MET CG  SD   sing N N 238 
MET CG  HG2  sing N N 239 
MET CG  HG3  sing N N 240 
MET SD  CE   sing N N 241 
MET CE  HE1  sing N N 242 
MET CE  HE2  sing N N 243 
MET CE  HE3  sing N N 244 
MET OXT HXT  sing N N 245 
PHE N   CA   sing N N 246 
PHE N   H    sing N N 247 
PHE N   H2   sing N N 248 
PHE CA  C    sing N N 249 
PHE CA  CB   sing N N 250 
PHE CA  HA   sing N N 251 
PHE C   O    doub N N 252 
PHE C   OXT  sing N N 253 
PHE CB  CG   sing N N 254 
PHE CB  HB2  sing N N 255 
PHE CB  HB3  sing N N 256 
PHE CG  CD1  doub Y N 257 
PHE CG  CD2  sing Y N 258 
PHE CD1 CE1  sing Y N 259 
PHE CD1 HD1  sing N N 260 
PHE CD2 CE2  doub Y N 261 
PHE CD2 HD2  sing N N 262 
PHE CE1 CZ   doub Y N 263 
PHE CE1 HE1  sing N N 264 
PHE CE2 CZ   sing Y N 265 
PHE CE2 HE2  sing N N 266 
PHE CZ  HZ   sing N N 267 
PHE OXT HXT  sing N N 268 
PRO N   CA   sing N N 269 
PRO N   CD   sing N N 270 
PRO N   H    sing N N 271 
PRO CA  C    sing N N 272 
PRO CA  CB   sing N N 273 
PRO CA  HA   sing N N 274 
PRO C   O    doub N N 275 
PRO C   OXT  sing N N 276 
PRO CB  CG   sing N N 277 
PRO CB  HB2  sing N N 278 
PRO CB  HB3  sing N N 279 
PRO CG  CD   sing N N 280 
PRO CG  HG2  sing N N 281 
PRO CG  HG3  sing N N 282 
PRO CD  HD2  sing N N 283 
PRO CD  HD3  sing N N 284 
PRO OXT HXT  sing N N 285 
SER N   CA   sing N N 286 
SER N   H    sing N N 287 
SER N   H2   sing N N 288 
SER CA  C    sing N N 289 
SER CA  CB   sing N N 290 
SER CA  HA   sing N N 291 
SER C   O    doub N N 292 
SER C   OXT  sing N N 293 
SER CB  OG   sing N N 294 
SER CB  HB2  sing N N 295 
SER CB  HB3  sing N N 296 
SER OG  HG   sing N N 297 
SER OXT HXT  sing N N 298 
THR N   CA   sing N N 299 
THR N   H    sing N N 300 
THR N   H2   sing N N 301 
THR CA  C    sing N N 302 
THR CA  CB   sing N N 303 
THR CA  HA   sing N N 304 
THR C   O    doub N N 305 
THR C   OXT  sing N N 306 
THR CB  OG1  sing N N 307 
THR CB  CG2  sing N N 308 
THR CB  HB   sing N N 309 
THR OG1 HG1  sing N N 310 
THR CG2 HG21 sing N N 311 
THR CG2 HG22 sing N N 312 
THR CG2 HG23 sing N N 313 
THR OXT HXT  sing N N 314 
TRP N   CA   sing N N 315 
TRP N   H    sing N N 316 
TRP N   H2   sing N N 317 
TRP CA  C    sing N N 318 
TRP CA  CB   sing N N 319 
TRP CA  HA   sing N N 320 
TRP C   O    doub N N 321 
TRP C   OXT  sing N N 322 
TRP CB  CG   sing N N 323 
TRP CB  HB2  sing N N 324 
TRP CB  HB3  sing N N 325 
TRP CG  CD1  doub Y N 326 
TRP CG  CD2  sing Y N 327 
TRP CD1 NE1  sing Y N 328 
TRP CD1 HD1  sing N N 329 
TRP CD2 CE2  doub Y N 330 
TRP CD2 CE3  sing Y N 331 
TRP NE1 CE2  sing Y N 332 
TRP NE1 HE1  sing N N 333 
TRP CE2 CZ2  sing Y N 334 
TRP CE3 CZ3  doub Y N 335 
TRP CE3 HE3  sing N N 336 
TRP CZ2 CH2  doub Y N 337 
TRP CZ2 HZ2  sing N N 338 
TRP CZ3 CH2  sing Y N 339 
TRP CZ3 HZ3  sing N N 340 
TRP CH2 HH2  sing N N 341 
TRP OXT HXT  sing N N 342 
TYR N   CA   sing N N 343 
TYR N   H    sing N N 344 
TYR N   H2   sing N N 345 
TYR CA  C    sing N N 346 
TYR CA  CB   sing N N 347 
TYR CA  HA   sing N N 348 
TYR C   O    doub N N 349 
TYR C   OXT  sing N N 350 
TYR CB  CG   sing N N 351 
TYR CB  HB2  sing N N 352 
TYR CB  HB3  sing N N 353 
TYR CG  CD1  doub Y N 354 
TYR CG  CD2  sing Y N 355 
TYR CD1 CE1  sing Y N 356 
TYR CD1 HD1  sing N N 357 
TYR CD2 CE2  doub Y N 358 
TYR CD2 HD2  sing N N 359 
TYR CE1 CZ   doub Y N 360 
TYR CE1 HE1  sing N N 361 
TYR CE2 CZ   sing Y N 362 
TYR CE2 HE2  sing N N 363 
TYR CZ  OH   sing N N 364 
TYR OH  HH   sing N N 365 
TYR OXT HXT  sing N N 366 
V50 C21 C19  sing N N 367 
V50 C19 N20  doub Y N 368 
V50 C19 C18  sing Y N 369 
V50 N20 C15  sing Y N 370 
V50 C18 C17  doub Y N 371 
V50 S14 C15  sing N N 372 
V50 S14 C2   sing N N 373 
V50 C15 N16  doub Y N 374 
V50 F10 C1   sing N N 375 
V50 C17 N16  sing Y N 376 
V50 C17 C22  sing N N 377 
V50 C1  C2   doub Y N 378 
V50 C1  C6   sing Y N 379 
V50 C2  C3   sing Y N 380 
V50 F12 C3   sing N N 381 
V50 C3  C4   doub Y N 382 
V50 C6  F11  sing N N 383 
V50 C6  C5   doub Y N 384 
V50 C4  C5   sing Y N 385 
V50 C4  F13  sing N N 386 
V50 C5  S7   sing N N 387 
V50 N23 S7   sing N N 388 
V50 O8  S7   doub N N 389 
V50 S7  O9   doub N N 390 
V50 N23 H1   sing N N 391 
V50 N23 H2   sing N N 392 
V50 C21 H3   sing N N 393 
V50 C21 H4   sing N N 394 
V50 C21 H5   sing N N 395 
V50 C18 H6   sing N N 396 
V50 C22 H7   sing N N 397 
V50 C22 H8   sing N N 398 
V50 C22 H9   sing N N 399 
VAL N   CA   sing N N 400 
VAL N   H    sing N N 401 
VAL N   H2   sing N N 402 
VAL CA  C    sing N N 403 
VAL CA  CB   sing N N 404 
VAL CA  HA   sing N N 405 
VAL C   O    doub N N 406 
VAL C   OXT  sing N N 407 
VAL CB  CG1  sing N N 408 
VAL CB  CG2  sing N N 409 
VAL CB  HB   sing N N 410 
VAL CG1 HG11 sing N N 411 
VAL CG1 HG12 sing N N 412 
VAL CG1 HG13 sing N N 413 
VAL CG2 HG21 sing N N 414 
VAL CG2 HG22 sing N N 415 
VAL CG2 HG23 sing N N 416 
VAL OXT HXT  sing N N 417 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        V50 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   V50 
_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                    7NZW 
_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]   0.023684 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.005992 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.024220 
_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]   0.014433 
_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  
NA 
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   ? 32.628  1.446   8.455   1.00 34.41 ? 4   HIS A N   1 
ATOM   2    C  CA  . HIS A 1 4   ? 31.374  1.953   9.070   1.00 32.40 ? 4   HIS A CA  1 
ATOM   3    C  C   . HIS A 1 4   ? 30.647  0.817   9.773   1.00 28.99 ? 4   HIS A C   1 
ATOM   4    O  O   . HIS A 1 4   ? 30.906  -0.347  9.493   1.00 31.98 ? 4   HIS A O   1 
ATOM   5    C  CB  . HIS A 1 4   ? 30.462  2.568   8.006   1.00 32.90 ? 4   HIS A CB  1 
ATOM   6    C  CG  . HIS A 1 4   ? 29.899  3.817   8.548   1.00 36.95 ? 4   HIS A CG  1 
ATOM   7    N  ND1 . HIS A 1 4   ? 28.872  4.498   7.939   1.00 42.33 ? 4   HIS A ND1 1 
ATOM   8    C  CD2 . HIS A 1 4   ? 30.215  4.485   9.685   1.00 41.17 ? 4   HIS A CD2 1 
ATOM   9    C  CE1 . HIS A 1 4   ? 28.579  5.570   8.667   1.00 49.37 ? 4   HIS A CE1 1 
ATOM   10   N  NE2 . HIS A 1 4   ? 29.389  5.578   9.761   1.00 47.29 ? 4   HIS A NE2 1 
ATOM   11   N  N   . TRP A 1 5   ? 29.661  1.181   10.595  1.00 23.17 ? 5   TRP A N   1 
ATOM   12   C  CA  . TRP A 1 5   ? 28.959  0.210   11.423  1.00 19.96 ? 5   TRP A CA  1 
ATOM   13   C  C   . TRP A 1 5   ? 28.007  -0.595  10.551  1.00 20.92 ? 5   TRP A C   1 
ATOM   14   O  O   . TRP A 1 5   ? 27.553  -0.133  9.496   1.00 22.06 ? 5   TRP A O   1 
ATOM   15   C  CB  . TRP A 1 5   ? 28.242  0.898   12.605  1.00 17.95 ? 5   TRP A CB  1 
ATOM   16   C  CG  . TRP A 1 5   ? 27.079  1.754   12.186  1.00 18.27 ? 5   TRP A CG  1 
ATOM   17   C  CD1 . TRP A 1 5   ? 27.057  3.078   11.825  1.00 19.00 ? 5   TRP A CD1 1 
ATOM   18   C  CD2 . TRP A 1 5   ? 25.721  1.298   12.075  1.00 18.69 ? 5   TRP A CD2 1 
ATOM   19   N  NE1 . TRP A 1 5   ? 25.781  3.482   11.503  1.00 19.82 ? 5   TRP A NE1 1 
ATOM   20   C  CE2 . TRP A 1 5   ? 24.944  2.397   11.651  1.00 18.40 ? 5   TRP A CE2 1 
ATOM   21   C  CE3 . TRP A 1 5   ? 25.109  0.067   12.336  1.00 17.10 ? 5   TRP A CE3 1 
ATOM   22   C  CZ2 . TRP A 1 5   ? 23.565  2.304   11.503  1.00 19.34 ? 5   TRP A CZ2 1 
ATOM   23   C  CZ3 . TRP A 1 5   ? 23.732  -0.033  12.176  1.00 17.40 ? 5   TRP A CZ3 1 
ATOM   24   C  CH2 . TRP A 1 5   ? 23.000  1.078   11.753  1.00 17.14 ? 5   TRP A CH2 1 
ATOM   25   N  N   . GLY A 1 6   ? 27.672  -1.782  11.064  1.00 18.40 ? 6   GLY A N   1 
ATOM   26   C  CA  . GLY A 1 6   ? 26.679  -2.608  10.418  1.00 19.24 ? 6   GLY A CA  1 
ATOM   27   C  C   . GLY A 1 6   ? 26.287  -3.747  11.349  1.00 19.24 ? 6   GLY A C   1 
ATOM   28   O  O   . GLY A 1 6   ? 26.353  -3.618  12.572  1.00 20.37 ? 6   GLY A O   1 
ATOM   29   N  N   . TYR A 1 7   ? 25.992  -4.889  10.763  1.00 19.98 ? 7   TYR A N   1 
ATOM   30   C  CA  . TYR A 1 7   ? 25.573  -6.010  11.580  1.00 22.15 ? 7   TYR A CA  1 
ATOM   31   C  C   . TYR A 1 7   ? 26.508  -7.222  11.512  1.00 27.89 ? 7   TYR A C   1 
ATOM   32   O  O   . TYR A 1 7   ? 26.319  -8.184  12.275  1.00 27.93 ? 7   TYR A O   1 
ATOM   33   C  CB  . TYR A 1 7   ? 24.095  -6.293  11.291  1.00 18.51 ? 7   TYR A CB  1 
ATOM   34   C  CG  . TYR A 1 7   ? 23.177  -5.210  11.812  1.00 15.88 ? 7   TYR A CG  1 
ATOM   35   C  CD1 . TYR A 1 7   ? 22.788  -5.226  13.154  1.00 14.47 ? 7   TYR A CD1 1 
ATOM   36   C  CD2 . TYR A 1 7   ? 22.701  -4.192  10.993  1.00 16.49 ? 7   TYR A CD2 1 
ATOM   37   C  CE1 . TYR A 1 7   ? 21.954  -4.222  13.649  1.00 13.43 ? 7   TYR A CE1 1 
ATOM   38   C  CE2 . TYR A 1 7   ? 21.855  -3.202  11.475  1.00 13.75 ? 7   TYR A CE2 1 
ATOM   39   C  CZ  . TYR A 1 7   ? 21.458  -3.239  12.813  1.00 14.42 ? 7   TYR A CZ  1 
ATOM   40   O  OH  . TYR A 1 7   ? 20.625  -2.239  13.206  1.00 14.62 ? 7   TYR A OH  1 
ATOM   41   N  N   . GLY A 1 8   ? 27.561  -7.149  10.677  1.00 29.23 ? 8   GLY A N   1 
ATOM   42   C  CA  . GLY A 1 8   ? 28.437  -8.314  10.481  1.00 29.35 ? 8   GLY A CA  1 
ATOM   43   C  C   . GLY A 1 8   ? 29.431  -8.567  11.618  1.00 29.01 ? 8   GLY A C   1 
ATOM   44   O  O   . GLY A 1 8   ? 29.506  -7.819  12.603  1.00 34.74 ? 8   GLY A O   1 
ATOM   45   N  N   . LYS A 1 9   ? 30.291  -9.600  11.445  1.00 35.11 ? 9   LYS A N   1 
ATOM   46   C  CA  . LYS A 1 9   ? 31.293  -9.977  12.441  1.00 35.93 ? 9   LYS A CA  1 
ATOM   47   C  C   . LYS A 1 9   ? 32.309  -8.853  12.579  1.00 33.16 ? 9   LYS A C   1 
ATOM   48   O  O   . LYS A 1 9   ? 32.830  -8.642  13.673  1.00 32.92 ? 9   LYS A O   1 
ATOM   49   C  CB  . LYS A 1 9   ? 32.102  -11.218 12.037  1.00 35.00 ? 9   LYS A CB  1 
ATOM   50   N  N   . HIS A 1 10  ? 32.485  -8.100  11.479  1.00 30.15 ? 10  HIS A N   1 
ATOM   51   C  CA  . HIS A 1 10  ? 33.541  -7.108  11.414  1.00 28.19 ? 10  HIS A CA  1 
ATOM   52   C  C   . HIS A 1 10  ? 33.077  -5.755  11.947  1.00 24.95 ? 10  HIS A C   1 
ATOM   53   O  O   . HIS A 1 10  ? 33.898  -5.005  12.466  1.00 24.25 ? 10  HIS A O   1 
ATOM   54   C  CB  . HIS A 1 10  ? 34.259  -7.146  10.049  1.00 25.67 ? 10  HIS A CB  1 
ATOM   55   C  CG  . HIS A 1 10  ? 34.836  -8.504  9.808   1.00 31.32 ? 10  HIS A CG  1 
ATOM   56   N  ND1 . HIS A 1 10  ? 35.754  -9.048  10.682  1.00 33.07 ? 10  HIS A ND1 1 
ATOM   57   C  CD2 . HIS A 1 10  ? 34.567  -9.456  8.880   1.00 35.29 ? 10  HIS A CD2 1 
ATOM   58   C  CE1 . HIS A 1 10  ? 36.061  -10.274 10.294  1.00 32.46 ? 10  HIS A CE1 1 
ATOM   59   N  NE2 . HIS A 1 10  ? 35.350  -10.548 9.182   1.00 34.02 ? 10  HIS A NE2 1 
ATOM   60   N  N   . ASN A 1 11  ? 31.754  -5.490  11.918  1.00 21.97 ? 11  ASN A N   1 
ATOM   61   C  CA  . ASN A 1 11  ? 31.328  -4.125  12.184  1.00 20.29 ? 11  ASN A CA  1 
ATOM   62   C  C   . ASN A 1 11  ? 29.999  -4.114  12.949  1.00 20.81 ? 11  ASN A C   1 
ATOM   63   O  O   . ASN A 1 11  ? 29.344  -3.068  12.995  1.00 20.13 ? 11  ASN A O   1 
ATOM   64   C  CB  . ASN A 1 11  ? 31.178  -3.331  10.893  1.00 19.34 ? 11  ASN A CB  1 
ATOM   65   C  CG  . ASN A 1 11  ? 30.120  -3.893  9.977   1.00 21.97 ? 11  ASN A CG  1 
ATOM   66   O  OD1 . ASN A 1 11  ? 29.555  -4.944  10.284  1.00 22.99 ? 11  ASN A OD1 1 
ATOM   67   N  ND2 . ASN A 1 11  ? 29.828  -3.190  8.881   1.00 22.98 ? 11  ASN A ND2 1 
ATOM   68   N  N   . GLY A 1 12  ? 29.670  -5.256  13.582  1.00 19.61 ? 12  GLY A N   1 
ATOM   69   C  CA  . GLY A 1 12  ? 28.396  -5.503  14.256  1.00 18.49 ? 12  GLY A CA  1 
ATOM   70   C  C   . GLY A 1 12  ? 28.336  -4.882  15.643  1.00 19.48 ? 12  GLY A C   1 
ATOM   71   O  O   . GLY A 1 12  ? 29.206  -4.138  16.073  1.00 18.14 ? 12  GLY A O   1 
ATOM   72   N  N   . PRO A 1 13  ? 27.231  -5.171  16.366  1.00 16.18 ? 13  PRO A N   1 
ATOM   73   C  CA  . PRO A 1 13  ? 26.964  -4.538  17.654  1.00 17.04 ? 13  PRO A CA  1 
ATOM   74   C  C   . PRO A 1 13  ? 28.108  -4.539  18.648  1.00 17.16 ? 13  PRO A C   1 
ATOM   75   O  O   . PRO A 1 13  ? 28.273  -3.565  19.376  1.00 17.40 ? 13  PRO A O   1 
ATOM   76   C  CB  . PRO A 1 13  ? 25.760  -5.367  18.117  1.00 17.62 ? 13  PRO A CB  1 
ATOM   77   C  CG  . PRO A 1 13  ? 25.027  -5.627  16.860  1.00 16.70 ? 13  PRO A CG  1 
ATOM   78   C  CD  . PRO A 1 13  ? 26.116  -5.974  15.837  1.00 16.50 ? 13  PRO A CD  1 
ATOM   79   N  N   . GLU A 1 14  ? 28.958  -5.560  18.619  1.00 18.46 ? 14  GLU A N   1 
ATOM   80   C  CA  . GLU A 1 14  ? 30.017  -5.610  19.600  1.00 19.18 ? 14  GLU A CA  1 
ATOM   81   C  C   . GLU A 1 14  ? 31.185  -4.683  19.246  1.00 17.52 ? 14  GLU A C   1 
ATOM   82   O  O   . GLU A 1 14  ? 32.039  -4.464  20.081  1.00 18.15 ? 14  GLU A O   1 
ATOM   83   C  CB  . GLU A 1 14  ? 30.567  -7.023  19.771  1.00 24.27 ? 14  GLU A CB  1 
ATOM   84   C  CG  . GLU A 1 14  ? 29.528  -8.068  20.189  1.00 31.74 ? 14  GLU A CG  1 
ATOM   85   C  CD  . GLU A 1 14  ? 28.642  -7.863  21.424  1.00 40.24 ? 14  GLU A CD  1 
ATOM   86   O  OE1 . GLU A 1 14  ? 29.182  -7.805  22.550  1.00 40.45 ? 14  GLU A OE1 1 
ATOM   87   O  OE2 . GLU A 1 14  ? 27.375  -7.818  21.259  1.00 44.82 ? 14  GLU A OE2 1 
ATOM   88   N  N   . HIS A 1 15  ? 31.138  -4.073  18.058  1.00 17.99 ? 15  HIS A N   1 
ATOM   89   C  CA  . HIS A 1 15  ? 32.146  -3.100  17.638  1.00 17.99 ? 15  HIS A CA  1 
ATOM   90   C  C   . HIS A 1 15  ? 31.713  -1.645  17.842  1.00 17.34 ? 15  HIS A C   1 
ATOM   91   O  O   . HIS A 1 15  ? 32.531  -0.736  17.852  1.00 17.20 ? 15  HIS A O   1 
ATOM   92   C  CB  . HIS A 1 15  ? 32.493  -3.315  16.168  1.00 17.67 ? 15  HIS A CB  1 
ATOM   93   C  CG  . HIS A 1 15  ? 33.231  -4.600  15.921  1.00 19.65 ? 15  HIS A CG  1 
ATOM   94   N  ND1 . HIS A 1 15  ? 34.594  -4.663  16.089  1.00 23.99 ? 15  HIS A ND1 1 
ATOM   95   C  CD2 . HIS A 1 15  ? 32.820  -5.821  15.535  1.00 22.23 ? 15  HIS A CD2 1 
ATOM   96   C  CE1 . HIS A 1 15  ? 35.010  -5.880  15.819  1.00 23.05 ? 15  HIS A CE1 1 
ATOM   97   N  NE2 . HIS A 1 15  ? 33.974  -6.613  15.502  1.00 24.46 ? 15  HIS A NE2 1 
ATOM   98   N  N   . TRP A 1 16  ? 30.401  -1.401  18.006  1.00 16.24 ? 16  TRP A N   1 
ATOM   99   C  CA  . TRP A 1 16  ? 29.892  -0.033  17.913  1.00 15.85 ? 16  TRP A CA  1 
ATOM   100  C  C   . TRP A 1 16  ? 30.486  0.932   18.935  1.00 14.00 ? 16  TRP A C   1 
ATOM   101  O  O   . TRP A 1 16  ? 30.574  2.137   18.670  1.00 14.60 ? 16  TRP A O   1 
ATOM   102  C  CB  . TRP A 1 16  ? 28.352  -0.076  18.001  1.00 13.51 ? 16  TRP A CB  1 
ATOM   103  C  CG  . TRP A 1 16  ? 27.702  -0.841  16.893  1.00 15.97 ? 16  TRP A CG  1 
ATOM   104  C  CD1 . TRP A 1 16  ? 28.199  -1.224  15.682  1.00 14.56 ? 16  TRP A CD1 1 
ATOM   105  C  CD2 . TRP A 1 16  ? 26.297  -1.154  16.831  1.00 13.66 ? 16  TRP A CD2 1 
ATOM   106  N  NE1 . TRP A 1 16  ? 27.271  -1.856  14.932  1.00 15.51 ? 16  TRP A NE1 1 
ATOM   107  C  CE2 . TRP A 1 16  ? 26.067  -1.792  15.600  1.00 15.40 ? 16  TRP A CE2 1 
ATOM   108  C  CE3 . TRP A 1 16  ? 25.227  -0.928  17.721  1.00 15.05 ? 16  TRP A CE3 1 
ATOM   109  C  CZ2 . TRP A 1 16  ? 24.804  -2.244  15.221  1.00 15.94 ? 16  TRP A CZ2 1 
ATOM   110  C  CZ3 . TRP A 1 16  ? 23.996  -1.387  17.347  1.00 14.12 ? 16  TRP A CZ3 1 
ATOM   111  C  CH2 . TRP A 1 16  ? 23.777  -2.033  16.128  1.00 15.06 ? 16  TRP A CH2 1 
ATOM   112  N  N   . HIS A 1 17  ? 30.883  0.429   20.103  1.00 14.98 ? 17  HIS A N   1 
ATOM   113  C  CA  . HIS A 1 17  ? 31.344  1.256   21.208  1.00 15.18 ? 17  HIS A CA  1 
ATOM   114  C  C   . HIS A 1 17  ? 32.600  2.063   20.832  1.00 16.28 ? 17  HIS A C   1 
ATOM   115  O  O   . HIS A 1 17  ? 32.821  3.130   21.398  1.00 16.62 ? 17  HIS A O   1 
ATOM   116  C  CB  . HIS A 1 17  ? 31.626  0.418   22.451  1.00 16.29 ? 17  HIS A CB  1 
ATOM   117  C  CG  . HIS A 1 17  ? 32.827  -0.459  22.312  1.00 18.32 ? 17  HIS A CG  1 
ATOM   118  N  ND1 . HIS A 1 17  ? 34.040  -0.089  22.839  1.00 22.63 ? 17  HIS A ND1 1 
ATOM   119  C  CD2 . HIS A 1 17  ? 33.007  -1.612  21.658  1.00 18.51 ? 17  HIS A CD2 1 
ATOM   120  C  CE1 . HIS A 1 17  ? 34.926  -1.017  22.505  1.00 20.20 ? 17  HIS A CE1 1 
ATOM   121  N  NE2 . HIS A 1 17  ? 34.330  -1.973  21.825  1.00 21.01 ? 17  HIS A NE2 1 
ATOM   122  N  N   . LYS A 1 18  ? 33.353  1.543   19.857  1.00 18.13 ? 18  LYS A N   1 
ATOM   123  C  CA  . LYS A 1 18  ? 34.595  2.241   19.524  1.00 18.10 ? 18  LYS A CA  1 
ATOM   124  C  C   . LYS A 1 18  ? 34.256  3.596   18.898  1.00 21.06 ? 18  LYS A C   1 
ATOM   125  O  O   . LYS A 1 18  ? 34.872  4.599   19.261  1.00 22.74 ? 18  LYS A O   1 
ATOM   126  C  CB  . LYS A 1 18  ? 35.452  1.390   18.591  1.00 19.24 ? 18  LYS A CB  1 
ATOM   127  C  CG  . LYS A 1 18  ? 36.080  0.164   19.259  1.00 22.20 ? 18  LYS A CG  1 
ATOM   128  C  CD  . LYS A 1 18  ? 36.735  -0.819  18.309  1.00 21.47 ? 18  LYS A CD  1 
ATOM   129  C  CE  . LYS A 1 18  ? 35.805  -1.796  17.624  1.00 21.97 ? 18  LYS A CE  1 
ATOM   130  N  NZ  . LYS A 1 18  ? 36.459  -2.527  16.518  1.00 23.35 ? 18  LYS A NZ  1 
ATOM   131  N  N   . ASP A 1 19  ? 33.228  3.658   18.014  1.00 19.70 ? 19  ASP A N   1 
ATOM   132  C  CA  . ASP A 1 19  ? 32.826  4.931   17.433  1.00 20.00 ? 19  ASP A CA  1 
ATOM   133  C  C   . ASP A 1 19  ? 31.766  5.645   18.266  1.00 20.85 ? 19  ASP A C   1 
ATOM   134  O  O   . ASP A 1 19  ? 31.634  6.854   18.177  1.00 21.12 ? 19  ASP A O   1 
ATOM   135  C  CB  . ASP A 1 19  ? 32.398  4.786   15.976  1.00 21.91 ? 19  ASP A CB  1 
ATOM   136  C  CG  . ASP A 1 19  ? 33.613  4.527   15.096  1.00 29.95 ? 19  ASP A CG  1 
ATOM   137  O  OD1 . ASP A 1 19  ? 34.281  5.511   14.737  1.00 28.36 ? 19  ASP A OD1 1 
ATOM   138  O  OD2 . ASP A 1 19  ? 33.958  3.336   14.918  1.00 33.91 ? 19  ASP A OD2 1 
ATOM   139  N  N   . PHE A 1 20  ? 31.069  4.916   19.139  1.00 17.79 ? 20  PHE A N   1 
ATOM   140  C  CA  . PHE A 1 20  ? 29.903  5.459   19.810  1.00 17.51 ? 20  PHE A CA  1 
ATOM   141  C  C   . PHE A 1 20  ? 29.970  4.959   21.236  1.00 17.34 ? 20  PHE A C   1 
ATOM   142  O  O   . PHE A 1 20  ? 29.382  3.940   21.587  1.00 16.37 ? 20  PHE A O   1 
ATOM   143  C  CB  . PHE A 1 20  ? 28.607  4.984   19.116  1.00 15.98 ? 20  PHE A CB  1 
ATOM   144  C  CG  . PHE A 1 20  ? 28.525  5.337   17.662  1.00 14.82 ? 20  PHE A CG  1 
ATOM   145  C  CD1 . PHE A 1 20  ? 28.224  6.638   17.280  1.00 16.13 ? 20  PHE A CD1 1 
ATOM   146  C  CD2 . PHE A 1 20  ? 28.866  4.413   16.689  1.00 16.03 ? 20  PHE A CD2 1 
ATOM   147  C  CE1 . PHE A 1 20  ? 28.215  6.951   15.923  1.00 15.13 ? 20  PHE A CE1 1 
ATOM   148  C  CE2 . PHE A 1 20  ? 28.866  4.723   15.329  1.00 15.37 ? 20  PHE A CE2 1 
ATOM   149  C  CZ  . PHE A 1 20  ? 28.533  6.016   14.959  1.00 17.62 ? 20  PHE A CZ  1 
ATOM   150  N  N   . PRO A 1 21  ? 30.828  5.556   22.091  1.00 19.03 ? 21  PRO A N   1 
ATOM   151  C  CA  . PRO A 1 21  ? 31.085  5.034   23.428  1.00 18.73 ? 21  PRO A CA  1 
ATOM   152  C  C   . PRO A 1 21  ? 29.858  4.865   24.331  1.00 18.03 ? 21  PRO A C   1 
ATOM   153  O  O   . PRO A 1 21  ? 29.865  4.095   25.289  1.00 18.24 ? 21  PRO A O   1 
ATOM   154  C  CB  . PRO A 1 21  ? 32.120  6.032   24.006  1.00 21.49 ? 21  PRO A CB  1 
ATOM   155  C  CG  . PRO A 1 21  ? 31.961  7.245   23.152  1.00 22.92 ? 21  PRO A CG  1 
ATOM   156  C  CD  . PRO A 1 21  ? 31.683  6.714   21.755  1.00 20.06 ? 21  PRO A CD  1 
ATOM   157  N  N   . ILE A 1 22  ? 28.781  5.603   23.990  1.00 15.77 ? 22  ILE A N   1 
ATOM   158  C  CA  . ILE A 1 22  ? 27.526  5.521   24.729  1.00 16.43 ? 22  ILE A CA  1 
ATOM   159  C  C   . ILE A 1 22  ? 26.910  4.145   24.547  1.00 13.68 ? 22  ILE A C   1 
ATOM   160  O  O   . ILE A 1 22  ? 26.082  3.809   25.358  1.00 14.38 ? 22  ILE A O   1 
ATOM   161  C  CB  . ILE A 1 22  ? 26.544  6.634   24.300  1.00 15.89 ? 22  ILE A CB  1 
ATOM   162  C  CG1 . ILE A 1 22  ? 25.461  6.967   25.336  1.00 18.42 ? 22  ILE A CG1 1 
ATOM   163  C  CG2 . ILE A 1 22  ? 25.881  6.311   22.960  1.00 14.47 ? 22  ILE A CG2 1 
ATOM   164  C  CD1 . ILE A 1 22  ? 25.932  7.299   26.732  1.00 21.53 ? 22  ILE A CD1 1 
ATOM   165  N  N   . ALA A 1 23  ? 27.454  3.340   23.624  1.00 14.58 ? 23  ALA A N   1 
ATOM   166  C  CA  . ALA A 1 23  ? 27.063  1.943   23.550  1.00 13.98 ? 23  ALA A CA  1 
ATOM   167  C  C   . ALA A 1 23  ? 27.161  1.215   24.884  1.00 14.60 ? 23  ALA A C   1 
ATOM   168  O  O   . ALA A 1 23  ? 26.487  0.210   25.059  1.00 14.07 ? 23  ALA A O   1 
ATOM   169  C  CB  . ALA A 1 23  ? 27.902  1.240   22.486  1.00 13.85 ? 23  ALA A CB  1 
ATOM   170  N  N   . LYS A 1 24  ? 28.051  1.643   25.810  1.00 15.57 ? 24  LYS A N   1 
ATOM   171  C  CA  . LYS A 1 24  ? 28.229  1.009   27.108  1.00 15.26 ? 24  LYS A CA  1 
ATOM   172  C  C   . LYS A 1 24  ? 27.613  1.882   28.204  1.00 17.49 ? 24  LYS A C   1 
ATOM   173  O  O   . LYS A 1 24  ? 28.028  1.826   29.368  1.00 18.33 ? 24  LYS A O   1 
ATOM   174  C  CB  . LYS A 1 24  ? 29.737  0.854   27.350  1.00 15.91 ? 24  LYS A CB  1 
ATOM   175  C  CG  . LYS A 1 24  ? 30.355  -0.182  26.448  1.00 20.16 ? 24  LYS A CG  1 
ATOM   176  C  CD  . LYS A 1 24  ? 31.823  -0.356  26.835  1.00 21.61 ? 24  LYS A CD  1 
ATOM   177  C  CE  . LYS A 1 24  ? 32.565  -1.155  25.789  1.00 24.20 ? 24  LYS A CE  1 
ATOM   178  N  NZ  . LYS A 1 24  ? 32.309  -2.611  25.917  1.00 29.35 ? 24  LYS A NZ  1 
ATOM   179  N  N   . GLY A 1 25  ? 26.587  2.660   27.830  1.00 16.43 ? 25  GLY A N   1 
ATOM   180  C  CA  . GLY A 1 25  ? 25.977  3.633   28.737  1.00 16.76 ? 25  GLY A CA  1 
ATOM   181  C  C   . GLY A 1 25  ? 24.988  2.997   29.708  1.00 14.51 ? 25  GLY A C   1 
ATOM   182  O  O   . GLY A 1 25  ? 24.796  1.771   29.747  1.00 16.09 ? 25  GLY A O   1 
ATOM   183  N  N   . GLU A 1 26  ? 24.304  3.878   30.452  1.00 16.23 ? 26  GLU A N   1 
ATOM   184  C  CA  . GLU A 1 26  ? 23.455  3.389   31.521  1.00 16.29 ? 26  GLU A CA  1 
ATOM   185  C  C   . GLU A 1 26  ? 22.002  3.168   31.106  1.00 15.04 ? 26  GLU A C   1 
ATOM   186  O  O   . GLU A 1 26  ? 21.262  2.649   31.911  1.00 16.85 ? 26  GLU A O   1 
ATOM   187  C  CB  . GLU A 1 26  ? 23.410  4.366   32.702  1.00 22.11 ? 26  GLU A CB  1 
ATOM   188  C  CG  . GLU A 1 26  ? 24.782  4.693   33.301  1.00 29.78 ? 26  GLU A CG  1 
ATOM   189  C  CD  . GLU A 1 26  ? 25.484  3.469   33.846  1.00 29.21 ? 26  GLU A CD  1 
ATOM   190  O  OE1 . GLU A 1 26  ? 24.866  2.703   34.627  1.00 33.26 ? 26  GLU A OE1 1 
ATOM   191  O  OE2 . GLU A 1 26  ? 26.657  3.273   33.474  1.00 35.21 ? 26  GLU A OE2 1 
ATOM   192  N  N   A ARG A 1 27  ? 21.616  3.612   29.890  0.50 13.95 ? 27  ARG A N   1 
ATOM   193  N  N   B ARG A 1 27  ? 21.646  3.507   29.863  0.50 14.36 ? 27  ARG A N   1 
ATOM   194  C  CA  A ARG A 1 27  ? 20.230  3.477   29.413  0.50 11.73 ? 27  ARG A CA  1 
ATOM   195  C  CA  B ARG A 1 27  ? 20.239  3.426   29.474  0.50 12.65 ? 27  ARG A CA  1 
ATOM   196  C  C   A ARG A 1 27  ? 20.200  2.992   27.953  0.50 11.06 ? 27  ARG A C   1 
ATOM   197  C  C   B ARG A 1 27  ? 20.111  2.877   28.049  0.50 11.75 ? 27  ARG A C   1 
ATOM   198  O  O   A ARG A 1 27  ? 19.619  3.659   27.078  0.50 9.77  ? 27  ARG A O   1 
ATOM   199  O  O   B ARG A 1 27  ? 19.347  3.391   27.272  0.50 11.65 ? 27  ARG A O   1 
ATOM   200  C  CB  A ARG A 1 27  ? 19.377  4.727   29.718  0.50 11.90 ? 27  ARG A CB  1 
ATOM   201  C  CB  B ARG A 1 27  ? 19.584  4.809   29.628  0.50 13.22 ? 27  ARG A CB  1 
ATOM   202  C  CG  A ARG A 1 27  ? 19.735  5.990   28.950  0.50 12.40 ? 27  ARG A CG  1 
ATOM   203  C  CG  B ARG A 1 27  ? 19.999  5.586   30.871  0.50 14.72 ? 27  ARG A CG  1 
ATOM   204  C  CD  A ARG A 1 27  ? 18.840  7.217   29.186  0.50 13.58 ? 27  ARG A CD  1 
ATOM   205  C  CD  B ARG A 1 27  ? 19.405  6.986   30.791  0.50 15.86 ? 27  ARG A CD  1 
ATOM   206  N  NE  A ARG A 1 27  ? 17.578  7.100   28.486  0.50 12.91 ? 27  ARG A NE  1 
ATOM   207  N  NE  B ARG A 1 27  ? 19.813  7.818   31.922  0.50 17.80 ? 27  ARG A NE  1 
ATOM   208  C  CZ  A ARG A 1 27  ? 16.730  8.103   28.290  0.50 10.41 ? 27  ARG A CZ  1 
ATOM   209  C  CZ  B ARG A 1 27  ? 20.819  8.684   31.894  0.50 17.99 ? 27  ARG A CZ  1 
ATOM   210  N  NH1 A ARG A 1 27  ? 17.016  9.310   28.748  0.50 8.10  ? 27  ARG A NH1 1 
ATOM   211  N  NH1 B ARG A 1 27  ? 21.530  8.839   30.790  0.50 20.58 ? 27  ARG A NH1 1 
ATOM   212  N  NH2 A ARG A 1 27  ? 15.600  7.897   27.638  0.50 10.65 ? 27  ARG A NH2 1 
ATOM   213  N  NH2 B ARG A 1 27  ? 21.112  9.393   32.970  0.50 23.33 ? 27  ARG A NH2 1 
ATOM   214  N  N   . GLN A 1 28  ? 20.897  1.852   27.696  1.00 11.52 ? 28  GLN A N   1 
ATOM   215  C  CA  . GLN A 1 28  ? 20.955  1.340   26.341  1.00 11.40 ? 28  GLN A CA  1 
ATOM   216  C  C   . GLN A 1 28  ? 19.779  0.418   26.051  1.00 11.77 ? 28  GLN A C   1 
ATOM   217  O  O   . GLN A 1 28  ? 19.283  -0.281  26.920  1.00 11.80 ? 28  GLN A O   1 
ATOM   218  C  CB  . GLN A 1 28  ? 22.302  0.653   26.062  1.00 11.07 ? 28  GLN A CB  1 
ATOM   219  C  CG  . GLN A 1 28  ? 23.447  1.675   26.029  1.00 12.11 ? 28  GLN A CG  1 
ATOM   220  C  CD  . GLN A 1 28  ? 23.342  2.491   24.764  1.00 10.79 ? 28  GLN A CD  1 
ATOM   221  O  OE1 . GLN A 1 28  ? 23.531  2.000   23.662  1.00 11.71 ? 28  GLN A OE1 1 
ATOM   222  N  NE2 . GLN A 1 28  ? 22.982  3.759   24.878  1.00 11.49 ? 28  GLN A NE2 1 
ATOM   223  N  N   . SER A 1 29  ? 19.412  0.404   24.776  1.00 10.58 ? 29  SER A N   1 
ATOM   224  C  CA  . SER A 1 29  ? 18.344  -0.473  24.318  1.00 9.58  ? 29  SER A CA  1 
ATOM   225  C  C   . SER A 1 29  ? 18.843  -1.340  23.170  1.00 10.04 ? 29  SER A C   1 
ATOM   226  O  O   . SER A 1 29  ? 19.819  -1.009  22.476  1.00 9.67  ? 29  SER A O   1 
ATOM   227  C  CB  . SER A 1 29  ? 17.207  0.363   23.758  1.00 10.43 ? 29  SER A CB  1 
ATOM   228  O  OG  . SER A 1 29  ? 16.580  1.107   24.815  1.00 10.56 ? 29  SER A OG  1 
ATOM   229  N  N   . PRO A 1 30  ? 18.201  -2.478  22.871  1.00 9.21  ? 30  PRO A N   1 
ATOM   230  C  CA  . PRO A 1 30  ? 17.016  -2.979  23.604  1.00 9.07  ? 30  PRO A CA  1 
ATOM   231  C  C   . PRO A 1 30  ? 17.413  -3.681  24.896  1.00 9.32  ? 30  PRO A C   1 
ATOM   232  O  O   . PRO A 1 30  ? 18.597  -3.768  25.244  1.00 10.24 ? 30  PRO A O   1 
ATOM   233  C  CB  . PRO A 1 30  ? 16.464  -4.021  22.618  1.00 9.20  ? 30  PRO A CB  1 
ATOM   234  C  CG  . PRO A 1 30  ? 17.728  -4.626  21.948  1.00 8.90  ? 30  PRO A CG  1 
ATOM   235  C  CD  . PRO A 1 30  ? 18.667  -3.431  21.835  1.00 10.06 ? 30  PRO A CD  1 
ATOM   236  N  N   . VAL A 1 31  ? 16.418  -4.231  25.579  1.00 9.82  ? 31  VAL A N   1 
ATOM   237  C  CA  . VAL A 1 31  ? 16.615  -4.995  26.794  1.00 9.72  ? 31  VAL A CA  1 
ATOM   238  C  C   . VAL A 1 31  ? 15.743  -6.233  26.733  1.00 9.96  ? 31  VAL A C   1 
ATOM   239  O  O   . VAL A 1 31  ? 14.751  -6.291  26.008  1.00 10.66 ? 31  VAL A O   1 
ATOM   240  C  CB  . VAL A 1 31  ? 16.320  -4.169  28.070  1.00 10.47 ? 31  VAL A CB  1 
ATOM   241  C  CG1 . VAL A 1 31  ? 17.202  -2.941  28.186  1.00 11.89 ? 31  VAL A CG1 1 
ATOM   242  C  CG2 . VAL A 1 31  ? 14.844  -3.736  28.144  1.00 11.80 ? 31  VAL A CG2 1 
ATOM   243  N  N   . ASP A 1 32  ? 16.060  -7.205  27.589  1.00 10.52 ? 32  ASP A N   1 
ATOM   244  C  CA  . ASP A 1 32  ? 15.165  -8.287  27.918  1.00 10.55 ? 32  ASP A CA  1 
ATOM   245  C  C   . ASP A 1 32  ? 14.083  -7.760  28.871  1.00 10.60 ? 32  ASP A C   1 
ATOM   246  O  O   . ASP A 1 32  ? 14.396  -7.142  29.900  1.00 12.70 ? 32  ASP A O   1 
ATOM   247  C  CB  . ASP A 1 32  ? 15.922  -9.478  28.493  1.00 11.44 ? 32  ASP A CB  1 
ATOM   248  C  CG  . ASP A 1 32  ? 14.989  -10.635 28.782  1.00 12.95 ? 32  ASP A CG  1 
ATOM   249  O  OD1 . ASP A 1 32  ? 14.232  -11.086 27.878  1.00 12.14 ? 32  ASP A OD1 1 
ATOM   250  O  OD2 . ASP A 1 32  ? 14.963  -11.055 29.976  1.00 16.04 ? 32  ASP A OD2 1 
ATOM   251  N  N   . ILE A 1 33  ? 12.817  -8.030  28.513  1.00 10.89 ? 33  ILE A N   1 
ATOM   252  C  CA  . ILE A 1 33  ? 11.712  -7.700  29.398  1.00 12.76 ? 33  ILE A CA  1 
ATOM   253  C  C   . ILE A 1 33  ? 11.401  -8.918  30.264  1.00 12.66 ? 33  ILE A C   1 
ATOM   254  O  O   . ILE A 1 33  ? 10.901  -9.921  29.793  1.00 13.60 ? 33  ILE A O   1 
ATOM   255  C  CB  . ILE A 1 33  ? 10.502  -7.211  28.600  1.00 12.27 ? 33  ILE A CB  1 
ATOM   256  C  CG1 . ILE A 1 33  ? 10.832  -5.946  27.799  1.00 13.09 ? 33  ILE A CG1 1 
ATOM   257  C  CG2 . ILE A 1 33  ? 9.337   -6.933  29.544  1.00 13.59 ? 33  ILE A CG2 1 
ATOM   258  C  CD1 . ILE A 1 33  ? 9.856   -5.661  26.664  1.00 14.22 ? 33  ILE A CD1 1 
ATOM   259  N  N   . ASP A 1 34  ? 11.825  -8.836  31.534  1.00 14.52 ? 34  ASP A N   1 
ATOM   260  C  CA  . ASP A 1 34  ? 11.531  -9.879  32.512  1.00 15.44 ? 34  ASP A CA  1 
ATOM   261  C  C   . ASP A 1 34  ? 10.105  -9.625  33.041  1.00 16.73 ? 34  ASP A C   1 
ATOM   262  O  O   . ASP A 1 34  ? 9.886   -8.687  33.818  1.00 16.91 ? 34  ASP A O   1 
ATOM   263  C  CB  . ASP A 1 34  ? 12.586  -9.822  33.637  1.00 16.96 ? 34  ASP A CB  1 
ATOM   264  C  CG  . ASP A 1 34  ? 12.444  -10.901 34.711  1.00 21.27 ? 34  ASP A CG  1 
ATOM   265  O  OD1 . ASP A 1 34  ? 11.335  -11.346 34.928  1.00 20.32 ? 34  ASP A OD1 1 
ATOM   266  O  OD2 . ASP A 1 34  ? 13.488  -11.313 35.275  1.00 29.70 ? 34  ASP A OD2 1 
ATOM   267  N  N   . THR A 1 35  ? 9.137   -10.413 32.598  1.00 17.53 ? 35  THR A N   1 
ATOM   268  C  CA  . THR A 1 35  ? 7.734   -10.084 32.826  1.00 18.19 ? 35  THR A CA  1 
ATOM   269  C  C   . THR A 1 35  ? 7.384   -10.243 34.299  1.00 21.04 ? 35  THR A C   1 
ATOM   270  O  O   . THR A 1 35  ? 6.379   -9.667  34.764  1.00 23.72 ? 35  THR A O   1 
ATOM   271  C  CB  . THR A 1 35  ? 6.782   -10.960 32.009  1.00 20.25 ? 35  THR A CB  1 
ATOM   272  O  OG1 . THR A 1 35  ? 7.042   -12.275 32.511  1.00 18.91 ? 35  THR A OG1 1 
ATOM   273  C  CG2 . THR A 1 35  ? 6.996   -10.890 30.511  1.00 22.09 ? 35  THR A CG2 1 
ATOM   274  N  N   . HIS A 1 36  ? 8.225   -10.999 35.023  1.00 21.05 ? 36  HIS A N   1 
ATOM   275  C  CA  . HIS A 1 36  ? 8.058   -11.221 36.456  1.00 22.63 ? 36  HIS A CA  1 
ATOM   276  C  C   . HIS A 1 36  ? 8.580   -10.064 37.294  1.00 28.15 ? 36  HIS A C   1 
ATOM   277  O  O   . HIS A 1 36  ? 8.145   -9.901  38.429  1.00 40.56 ? 36  HIS A O   1 
ATOM   278  C  CB  . HIS A 1 36  ? 8.752   -12.535 36.852  1.00 22.55 ? 36  HIS A CB  1 
ATOM   279  C  CG  . HIS A 1 36  ? 8.122   -13.658 36.113  1.00 23.66 ? 36  HIS A CG  1 
ATOM   280  N  ND1 . HIS A 1 36  ? 8.791   -14.372 35.131  1.00 28.47 ? 36  HIS A ND1 1 
ATOM   281  C  CD2 . HIS A 1 36  ? 6.884   -14.169 36.159  1.00 22.84 ? 36  HIS A CD2 1 
ATOM   282  C  CE1 . HIS A 1 36  ? 7.991   -15.286 34.624  1.00 22.56 ? 36  HIS A CE1 1 
ATOM   283  N  NE2 . HIS A 1 36  ? 6.825   -15.189 35.242  1.00 23.63 ? 36  HIS A NE2 1 
ATOM   284  N  N   . THR A 1 37  ? 9.562   -9.313  36.808  1.00 23.72 ? 37  THR A N   1 
ATOM   285  C  CA  . THR A 1 37  ? 10.048  -8.218  37.623  1.00 23.64 ? 37  THR A CA  1 
ATOM   286  C  C   . THR A 1 37  ? 9.513   -6.871  37.125  1.00 20.20 ? 37  THR A C   1 
ATOM   287  O  O   . THR A 1 37  ? 9.701   -5.858  37.800  1.00 25.67 ? 37  THR A O   1 
ATOM   288  C  CB  . THR A 1 37  ? 11.538  -8.358  37.938  1.00 31.96 ? 37  THR A CB  1 
ATOM   289  O  OG1 . THR A 1 37  ? 12.303  -7.876  36.841  1.00 32.58 ? 37  THR A OG1 1 
ATOM   290  C  CG2 . THR A 1 37  ? 11.923  -9.792  38.216  1.00 29.75 ? 37  THR A CG2 1 
ATOM   291  N  N   . ALA A 1 38  ? 8.819   -6.844  35.979  1.00 20.48 ? 38  ALA A N   1 
ATOM   292  C  CA  . ALA A 1 38  ? 8.158   -5.609  35.561  1.00 19.97 ? 38  ALA A CA  1 
ATOM   293  C  C   . ALA A 1 38  ? 7.088   -5.240  36.594  1.00 22.70 ? 38  ALA A C   1 
ATOM   294  O  O   . ALA A 1 38  ? 6.381   -6.101  37.093  1.00 29.11 ? 38  ALA A O   1 
ATOM   295  C  CB  . ALA A 1 38  ? 7.567   -5.742  34.191  1.00 19.24 ? 38  ALA A CB  1 
ATOM   296  N  N   . LYS A 1 39  ? 7.014   -3.964  36.951  1.00 22.61 ? 39  LYS A N   1 
ATOM   297  C  CA  . LYS A 1 39  ? 6.071   -3.528  37.969  1.00 21.42 ? 39  LYS A CA  1 
ATOM   298  C  C   . LYS A 1 39  ? 4.790   -3.016  37.289  1.00 21.62 ? 39  LYS A C   1 
ATOM   299  O  O   . LYS A 1 39  ? 4.846   -2.030  36.543  1.00 17.04 ? 39  LYS A O   1 
ATOM   300  C  CB  . LYS A 1 39  ? 6.804   -2.388  38.682  1.00 27.34 ? 39  LYS A CB  1 
ATOM   301  C  CG  . LYS A 1 39  ? 5.985   -1.503  39.606  1.00 29.34 ? 39  LYS A CG  1 
ATOM   302  C  CD  . LYS A 1 39  ? 5.748   -2.096  40.984  1.00 27.85 ? 39  LYS A CD  1 
ATOM   303  C  CE  . LYS A 1 39  ? 5.279   -0.998  41.921  1.00 30.36 ? 39  LYS A CE  1 
ATOM   304  N  NZ  . LYS A 1 39  ? 4.793   -1.556  43.205  1.00 29.78 ? 39  LYS A NZ  1 
ATOM   305  N  N   . TYR A 1 40  ? 3.626   -3.565  37.642  1.00 22.32 ? 40  TYR A N   1 
ATOM   306  C  CA  . TYR A 1 40  ? 2.377   -2.949  37.232  1.00 21.63 ? 40  TYR A CA  1 
ATOM   307  C  C   . TYR A 1 40  ? 2.265   -1.551  37.840  1.00 21.07 ? 40  TYR A C   1 
ATOM   308  O  O   . TYR A 1 40  ? 2.482   -1.372  39.059  1.00 21.28 ? 40  TYR A O   1 
ATOM   309  C  CB  . TYR A 1 40  ? 1.157   -3.826  37.555  1.00 23.86 ? 40  TYR A CB  1 
ATOM   310  C  CG  . TYR A 1 40  ? -0.141  -3.084  37.446  1.00 27.76 ? 40  TYR A CG  1 
ATOM   311  C  CD1 . TYR A 1 40  ? -0.615  -2.640  36.226  1.00 27.89 ? 40  TYR A CD1 1 
ATOM   312  C  CD2 . TYR A 1 40  ? -0.887  -2.789  38.581  1.00 33.69 ? 40  TYR A CD2 1 
ATOM   313  C  CE1 . TYR A 1 40  ? -1.801  -1.946  36.104  1.00 31.02 ? 40  TYR A CE1 1 
ATOM   314  C  CE2 . TYR A 1 40  ? -2.085  -2.094  38.480  1.00 35.03 ? 40  TYR A CE2 1 
ATOM   315  C  CZ  . TYR A 1 40  ? -2.539  -1.672  37.241  1.00 34.90 ? 40  TYR A CZ  1 
ATOM   316  O  OH  . TYR A 1 40  ? -3.696  -0.961  37.115  1.00 37.10 ? 40  TYR A OH  1 
ATOM   317  N  N   . ASP A 1 41  ? 1.918   -0.559  37.012  1.00 19.56 ? 41  ASP A N   1 
ATOM   318  C  CA  . ASP A 1 41  ? 1.933   0.822   37.456  1.00 19.64 ? 41  ASP A CA  1 
ATOM   319  C  C   . ASP A 1 41  ? 0.533   1.373   37.236  1.00 27.37 ? 41  ASP A C   1 
ATOM   320  O  O   . ASP A 1 41  ? 0.228   1.816   36.133  1.00 25.02 ? 41  ASP A O   1 
ATOM   321  C  CB  . ASP A 1 41  ? 2.983   1.660   36.719  1.00 24.94 ? 41  ASP A CB  1 
ATOM   322  C  CG  . ASP A 1 41  ? 3.142   3.054   37.300  1.00 30.01 ? 41  ASP A CG  1 
ATOM   323  O  OD1 . ASP A 1 41  ? 2.239   3.472   38.067  1.00 28.56 ? 41  ASP A OD1 1 
ATOM   324  O  OD2 . ASP A 1 41  ? 4.200   3.685   37.021  1.00 31.82 ? 41  ASP A OD2 1 
ATOM   325  N  N   . PRO A 1 42  ? -0.356  1.379   38.261  1.00 29.26 ? 42  PRO A N   1 
ATOM   326  C  CA  . PRO A 1 42  ? -1.767  1.665   38.013  1.00 31.20 ? 42  PRO A CA  1 
ATOM   327  C  C   . PRO A 1 42  ? -1.933  3.152   37.705  1.00 32.20 ? 42  PRO A C   1 
ATOM   328  O  O   . PRO A 1 42  ? -3.020  3.571   37.326  1.00 36.41 ? 42  PRO A O   1 
ATOM   329  C  CB  . PRO A 1 42  ? -2.438  1.233   39.331  1.00 32.17 ? 42  PRO A CB  1 
ATOM   330  C  CG  . PRO A 1 42  ? -1.373  1.505   40.379  1.00 31.23 ? 42  PRO A CG  1 
ATOM   331  C  CD  . PRO A 1 42  ? -0.055  1.166   39.690  1.00 29.55 ? 42  PRO A CD  1 
ATOM   332  N  N   . SER A 1 43  ? -0.840  3.923   37.807  1.00 34.83 ? 43  SER A N   1 
ATOM   333  C  CA  . SER A 1 43  ? -0.842  5.346   37.474  1.00 36.02 ? 43  SER A CA  1 
ATOM   334  C  C   . SER A 1 43  ? -0.515  5.638   35.998  1.00 34.49 ? 43  SER A C   1 
ATOM   335  O  O   . SER A 1 43  ? -0.663  6.773   35.544  1.00 36.15 ? 43  SER A O   1 
ATOM   336  C  CB  . SER A 1 43  ? 0.042   6.117   38.411  1.00 37.40 ? 43  SER A CB  1 
ATOM   337  O  OG  . SER A 1 43  ? 1.386   6.138   37.960  1.00 37.29 ? 43  SER A OG  1 
ATOM   338  N  N   . LEU A 1 44  ? -0.072  4.633   35.229  1.00 33.15 ? 44  LEU A N   1 
ATOM   339  C  CA  . LEU A 1 44  ? 0.150   4.821   33.794  1.00 29.53 ? 44  LEU A CA  1 
ATOM   340  C  C   . LEU A 1 44  ? -1.193  5.029   33.112  1.00 33.06 ? 44  LEU A C   1 
ATOM   341  O  O   . LEU A 1 44  ? -2.186  4.458   33.538  1.00 33.47 ? 44  LEU A O   1 
ATOM   342  C  CB  . LEU A 1 44  ? 0.780   3.563   33.195  1.00 26.37 ? 44  LEU A CB  1 
ATOM   343  C  CG  . LEU A 1 44  ? 2.272   3.378   33.451  1.00 22.95 ? 44  LEU A CG  1 
ATOM   344  C  CD1 . LEU A 1 44  ? 2.699   2.004   32.961  1.00 22.75 ? 44  LEU A CD1 1 
ATOM   345  C  CD2 . LEU A 1 44  ? 3.072   4.485   32.772  1.00 22.83 ? 44  LEU A CD2 1 
ATOM   346  N  N   . LYS A 1 45  ? -1.193  5.765   32.000  1.00 33.90 ? 45  LYS A N   1 
ATOM   347  C  CA  . LYS A 1 45  ? -2.427  5.946   31.250  1.00 31.05 ? 45  LYS A CA  1 
ATOM   348  C  C   . LYS A 1 45  ? -2.476  4.958   30.099  1.00 30.81 ? 45  LYS A C   1 
ATOM   349  O  O   . LYS A 1 45  ? -1.474  4.288   29.795  1.00 30.43 ? 45  LYS A O   1 
ATOM   350  C  CB  . LYS A 1 45  ? -2.605  7.411   30.869  1.00 30.16 ? 45  LYS A CB  1 
ATOM   351  C  CG  . LYS A 1 45  ? -2.579  8.343   32.071  1.00 31.82 ? 45  LYS A CG  1 
ATOM   352  C  CD  . LYS A 1 45  ? -2.192  9.759   31.726  1.00 39.22 ? 45  LYS A CD  1 
ATOM   353  C  CE  . LYS A 1 45  ? -2.104  10.663  32.939  1.00 38.07 ? 45  LYS A CE  1 
ATOM   354  N  N   . PRO A 1 46  ? -3.689  4.750   29.525  1.00 28.83 ? 46  PRO A N   1 
ATOM   355  C  CA  . PRO A 1 46  ? -3.826  4.002   28.277  1.00 25.74 ? 46  PRO A CA  1 
ATOM   356  C  C   . PRO A 1 46  ? -3.054  4.847   27.283  1.00 22.71 ? 46  PRO A C   1 
ATOM   357  O  O   . PRO A 1 46  ? -3.040  6.069   27.395  1.00 23.78 ? 46  PRO A O   1 
ATOM   358  C  CB  . PRO A 1 46  ? -5.346  4.026   27.973  1.00 28.76 ? 46  PRO A CB  1 
ATOM   359  C  CG  . PRO A 1 46  ? -5.867  5.200   28.796  1.00 33.96 ? 46  PRO A CG  1 
ATOM   360  C  CD  . PRO A 1 46  ? -4.983  5.244   30.030  1.00 33.03 ? 46  PRO A CD  1 
ATOM   361  N  N   . LEU A 1 47  ? -2.433  4.147   26.338  1.00 26.53 ? 47  LEU A N   1 
ATOM   362  C  CA  . LEU A 1 47  ? -1.767  4.820   25.258  1.00 25.69 ? 47  LEU A CA  1 
ATOM   363  C  C   . LEU A 1 47  ? -2.867  5.451   24.411  1.00 27.59 ? 47  LEU A C   1 
ATOM   364  O  O   . LEU A 1 47  ? -3.967  4.907   24.309  1.00 25.02 ? 47  LEU A O   1 
ATOM   365  C  CB  . LEU A 1 47  ? -1.045  3.726   24.479  1.00 29.84 ? 47  LEU A CB  1 
ATOM   366  C  CG  . LEU A 1 47  ? 0.287   4.102   23.873  1.00 32.63 ? 47  LEU A CG  1 
ATOM   367  C  CD1 . LEU A 1 47  ? 1.153   4.795   24.915  1.00 29.56 ? 47  LEU A CD1 1 
ATOM   368  C  CD2 . LEU A 1 47  ? 0.954   2.846   23.330  1.00 32.01 ? 47  LEU A CD2 1 
ATOM   369  N  N   . SER A 1 48  ? -2.588  6.632   23.886  1.00 20.53 ? 48  SER A N   1 
ATOM   370  C  CA  . SER A 1 48  ? -3.427  7.262   22.894  1.00 19.70 ? 48  SER A CA  1 
ATOM   371  C  C   . SER A 1 48  ? -2.657  7.264   21.575  1.00 18.91 ? 48  SER A C   1 
ATOM   372  O  O   . SER A 1 48  ? -1.642  7.950   21.414  1.00 18.54 ? 48  SER A O   1 
ATOM   373  C  CB  . SER A 1 48  ? -3.804  8.659   23.366  1.00 20.03 ? 48  SER A CB  1 
ATOM   374  O  OG  . SER A 1 48  ? -4.469  9.372   22.330  1.00 20.62 ? 48  SER A OG  1 
ATOM   375  N  N   . VAL A 1 49  ? -3.087  6.447   20.645  1.00 17.72 ? 49  VAL A N   1 
ATOM   376  C  CA  . VAL A 1 49  ? -2.490  6.374   19.333  1.00 19.95 ? 49  VAL A CA  1 
ATOM   377  C  C   . VAL A 1 49  ? -3.490  6.958   18.353  1.00 22.87 ? 49  VAL A C   1 
ATOM   378  O  O   . VAL A 1 49  ? -4.527  6.356   18.108  1.00 23.69 ? 49  VAL A O   1 
ATOM   379  C  CB  . VAL A 1 49  ? -2.159  4.912   18.988  1.00 23.49 ? 49  VAL A CB  1 
ATOM   380  C  CG1 . VAL A 1 49  ? -1.483  4.795   17.628  1.00 26.80 ? 49  VAL A CG1 1 
ATOM   381  C  CG2 . VAL A 1 49  ? -1.361  4.220   20.070  1.00 21.19 ? 49  VAL A CG2 1 
ATOM   382  N  N   . SER A 1 50  ? -3.193  8.125   17.789  1.00 20.75 ? 50  SER A N   1 
ATOM   383  C  CA  . SER A 1 50  ? -4.134  8.789   16.910  1.00 20.94 ? 50  SER A CA  1 
ATOM   384  C  C   . SER A 1 50  ? -3.507  8.883   15.539  1.00 18.72 ? 50  SER A C   1 
ATOM   385  O  O   . SER A 1 50  ? -2.834  9.860   15.234  1.00 20.31 ? 50  SER A O   1 
ATOM   386  C  CB  . SER A 1 50  ? -4.536  10.148  17.409  1.00 23.70 ? 50  SER A CB  1 
ATOM   387  O  OG  . SER A 1 50  ? -5.071  10.044  18.714  1.00 30.05 ? 50  SER A OG  1 
ATOM   388  N  N   . TYR A 1 51  ? -3.718  7.858   14.726  1.00 18.42 ? 51  TYR A N   1 
ATOM   389  C  CA  . TYR A 1 51  ? -3.129  7.772   13.407  1.00 18.94 ? 51  TYR A CA  1 
ATOM   390  C  C   . TYR A 1 51  ? -4.119  8.010   12.262  1.00 21.28 ? 51  TYR A C   1 
ATOM   391  O  O   . TYR A 1 51  ? -3.776  7.736   11.125  1.00 20.10 ? 51  TYR A O   1 
ATOM   392  C  CB  . TYR A 1 51  ? -2.476  6.400   13.200  1.00 16.89 ? 51  TYR A CB  1 
ATOM   393  C  CG  . TYR A 1 51  ? -1.204  6.120   13.988  1.00 17.19 ? 51  TYR A CG  1 
ATOM   394  C  CD1 . TYR A 1 51  ? -0.524  7.102   14.707  1.00 17.39 ? 51  TYR A CD1 1 
ATOM   395  C  CD2 . TYR A 1 51  ? -0.694  4.827   14.004  1.00 16.22 ? 51  TYR A CD2 1 
ATOM   396  C  CE1 . TYR A 1 51  ? 0.659   6.782   15.362  1.00 16.21 ? 51  TYR A CE1 1 
ATOM   397  C  CE2 . TYR A 1 51  ? 0.477   4.492   14.668  1.00 15.88 ? 51  TYR A CE2 1 
ATOM   398  C  CZ  . TYR A 1 51  ? 1.159   5.490   15.346  1.00 14.70 ? 51  TYR A CZ  1 
ATOM   399  O  OH  . TYR A 1 51  ? 2.295   5.149   16.024  1.00 14.78 ? 51  TYR A OH  1 
ATOM   400  N  N   A ASP A 1 52  ? -5.305  8.558   12.572  0.50 23.63 ? 52  ASP A N   1 
ATOM   401  N  N   B ASP A 1 52  ? -5.336  8.491   12.560  0.50 23.68 ? 52  ASP A N   1 
ATOM   402  C  CA  A ASP A 1 52  ? -6.368  8.731   11.588  0.50 25.18 ? 52  ASP A CA  1 
ATOM   403  C  CA  B ASP A 1 52  ? -6.339  8.696   11.519  0.50 25.48 ? 52  ASP A CA  1 
ATOM   404  C  C   A ASP A 1 52  ? -5.965  9.666   10.441  0.50 25.76 ? 52  ASP A C   1 
ATOM   405  C  C   B ASP A 1 52  ? -5.782  9.545   10.374  0.50 26.73 ? 52  ASP A C   1 
ATOM   406  O  O   A ASP A 1 52  ? -6.438  9.505   9.314   0.50 24.58 ? 52  ASP A O   1 
ATOM   407  O  O   B ASP A 1 52  ? -5.973  9.207   9.198   0.50 27.56 ? 52  ASP A O   1 
ATOM   408  C  CB  A ASP A 1 52  ? -7.676  9.153   12.267  0.50 25.96 ? 52  ASP A CB  1 
ATOM   409  C  CB  B ASP A 1 52  ? -7.622  9.312   12.089  0.50 26.08 ? 52  ASP A CB  1 
ATOM   410  C  CG  A ASP A 1 52  ? -7.501  10.092  13.449  0.50 26.25 ? 52  ASP A CG  1 
ATOM   411  C  CG  B ASP A 1 52  ? -8.738  9.475   11.066  0.50 26.47 ? 52  ASP A CG  1 
ATOM   412  O  OD1 A ASP A 1 52  ? -6.811  9.701   14.438  0.50 28.75 ? 52  ASP A OD1 1 
ATOM   413  O  OD1 B ASP A 1 52  ? -9.162  8.452   10.473  0.50 27.28 ? 52  ASP A OD1 1 
ATOM   414  O  OD2 A ASP A 1 52  ? -8.059  11.201  13.389  0.50 31.22 ? 52  ASP A OD2 1 
ATOM   415  O  OD2 B ASP A 1 52  ? -9.165  10.625  10.855  0.50 30.62 ? 52  ASP A OD2 1 
ATOM   416  N  N   . GLN A 1 53  ? -5.100  10.645  10.719  1.00 24.64 ? 53  GLN A N   1 
ATOM   417  C  CA  . GLN A 1 53  ? -4.683  11.607  9.694   1.00 27.84 ? 53  GLN A CA  1 
ATOM   418  C  C   . GLN A 1 53  ? -3.252  11.372  9.200   1.00 25.18 ? 53  GLN A C   1 
ATOM   419  O  O   . GLN A 1 53  ? -2.673  12.231  8.535   1.00 24.44 ? 53  GLN A O   1 
ATOM   420  C  CB  . GLN A 1 53  ? -4.941  13.053  10.130  1.00 34.29 ? 53  GLN A CB  1 
ATOM   421  C  CG  . GLN A 1 53  ? -6.415  13.458  10.103  1.00 38.72 ? 53  GLN A CG  1 
ATOM   422  C  CD  . GLN A 1 53  ? -7.020  13.243  8.736   1.00 44.96 ? 53  GLN A CD  1 
ATOM   423  O  OE1 . GLN A 1 53  ? -6.488  13.692  7.715   1.00 45.50 ? 53  GLN A OE1 1 
ATOM   424  N  NE2 . GLN A 1 53  ? -8.130  12.526  8.704   1.00 45.46 ? 53  GLN A NE2 1 
ATOM   425  N  N   . ALA A 1 54  ? -2.692  10.195  9.490   1.00 22.70 ? 54  ALA A N   1 
ATOM   426  C  CA  . ALA A 1 54  ? -1.340  9.907   9.040   1.00 17.93 ? 54  ALA A CA  1 
ATOM   427  C  C   . ALA A 1 54  ? -1.188  10.068  7.528   1.00 22.43 ? 54  ALA A C   1 
ATOM   428  O  O   . ALA A 1 54  ? -2.065  9.663   6.757   1.00 23.70 ? 54  ALA A O   1 
ATOM   429  C  CB  . ALA A 1 54  ? -0.943  8.517   9.506   1.00 18.21 ? 54  ALA A CB  1 
ATOM   430  N  N   . THR A 1 55  ? -0.078  10.689  7.117   1.00 17.82 ? 55  THR A N   1 
ATOM   431  C  CA  . THR A 1 55  ? 0.263   10.915  5.720   1.00 19.24 ? 55  THR A CA  1 
ATOM   432  C  C   . THR A 1 55  ? 1.586   10.239  5.433   1.00 17.06 ? 55  THR A C   1 
ATOM   433  O  O   . THR A 1 55  ? 2.625   10.836  5.651   1.00 16.06 ? 55  THR A O   1 
ATOM   434  C  CB  . THR A 1 55  ? 0.410   12.414  5.394   1.00 22.51 ? 55  THR A CB  1 
ATOM   435  O  OG1 . THR A 1 55  ? -0.872  13.014  5.561   1.00 28.35 ? 55  THR A OG1 1 
ATOM   436  C  CG2 . THR A 1 55  ? 0.831   12.608  3.953   1.00 27.32 ? 55  THR A CG2 1 
ATOM   437  N  N   . SER A 1 56  ? 1.560   9.031   4.885   1.00 17.55 ? 56  SER A N   1 
ATOM   438  C  CA  . SER A 1 56  ? 2.819   8.415   4.494   1.00 16.27 ? 56  SER A CA  1 
ATOM   439  C  C   . SER A 1 56  ? 3.321   9.059   3.207   1.00 19.13 ? 56  SER A C   1 
ATOM   440  O  O   . SER A 1 56  ? 2.508   9.524   2.381   1.00 17.77 ? 56  SER A O   1 
ATOM   441  C  CB  . SER A 1 56  ? 2.697   6.903   4.313   1.00 18.56 ? 56  SER A CB  1 
ATOM   442  O  OG  . SER A 1 56  ? 1.721   6.614   3.302   1.00 17.90 ? 56  SER A OG  1 
ATOM   443  N  N   . LEU A 1 57  ? 4.631   9.050   3.017   1.00 17.43 ? 57  LEU A N   1 
ATOM   444  C  CA  . LEU A 1 57  ? 5.178   9.673   1.827   1.00 19.48 ? 57  LEU A CA  1 
ATOM   445  C  C   . LEU A 1 57  ? 6.033   8.721   1.002   1.00 20.21 ? 57  LEU A C   1 
ATOM   446  O  O   . LEU A 1 57  ? 5.946   8.684   -0.228  1.00 18.68 ? 57  LEU A O   1 
ATOM   447  C  CB  . LEU A 1 57  ? 6.015   10.860  2.278   1.00 21.27 ? 57  LEU A CB  1 
ATOM   448  C  CG  . LEU A 1 57  ? 5.236   12.028  2.884   1.00 24.39 ? 57  LEU A CG  1 
ATOM   449  C  CD1 . LEU A 1 57  ? 6.223   13.119  3.271   1.00 22.94 ? 57  LEU A CD1 1 
ATOM   450  C  CD2 . LEU A 1 57  ? 4.126   12.566  1.967   1.00 29.97 ? 57  LEU A CD2 1 
ATOM   451  N  N   . ARG A 1 58  ? 6.932   7.987   1.657   1.00 17.02 ? 58  ARG A N   1 
ATOM   452  C  CA  . ARG A 1 58  ? 8.025   7.372   0.949   1.00 16.53 ? 58  ARG A CA  1 
ATOM   453  C  C   . ARG A 1 58  ? 8.442   6.126   1.705   1.00 17.73 ? 58  ARG A C   1 
ATOM   454  O  O   . ARG A 1 58  ? 8.290   6.124   2.925   1.00 17.06 ? 58  ARG A O   1 
ATOM   455  C  CB  . ARG A 1 58  ? 9.208   8.339   0.832   1.00 19.44 ? 58  ARG A CB  1 
ATOM   456  C  CG  . ARG A 1 58  ? 10.257  7.929   -0.180  1.00 20.92 ? 58  ARG A CG  1 
ATOM   457  C  CD  . ARG A 1 58  ? 11.117  9.160   -0.366  1.00 21.25 ? 58  ARG A CD  1 
ATOM   458  N  NE  . ARG A 1 58  ? 11.950  9.201   0.828   1.00 18.86 ? 58  ARG A NE  1 
ATOM   459  C  CZ  . ARG A 1 58  ? 13.269  9.380   0.870   1.00 19.48 ? 58  ARG A CZ  1 
ATOM   460  N  NH1 . ARG A 1 58  ? 13.958  9.605   -0.242  1.00 21.54 ? 58  ARG A NH1 1 
ATOM   461  N  NH2 . ARG A 1 58  ? 13.869  9.378   2.053   1.00 18.65 ? 58  ARG A NH2 1 
ATOM   462  N  N   . ILE A 1 59  ? 9.007   5.155   0.995   1.00 15.50 ? 59  ILE A N   1 
ATOM   463  C  CA  . ILE A 1 59  ? 9.674   4.028   1.630   1.00 15.19 ? 59  ILE A CA  1 
ATOM   464  C  C   . ILE A 1 59  ? 11.113  4.032   1.133   1.00 14.78 ? 59  ILE A C   1 
ATOM   465  O  O   . ILE A 1 59  ? 11.390  4.247   -0.057  1.00 15.94 ? 59  ILE A O   1 
ATOM   466  C  CB  . ILE A 1 59  ? 8.904   2.724   1.358   1.00 13.99 ? 59  ILE A CB  1 
ATOM   467  C  CG1 . ILE A 1 59  ? 9.442   1.577   2.237   1.00 15.33 ? 59  ILE A CG1 1 
ATOM   468  C  CG2 . ILE A 1 59  ? 8.924   2.379   -0.139  1.00 15.77 ? 59  ILE A CG2 1 
ATOM   469  C  CD1 . ILE A 1 59  ? 8.604   0.316   2.077   1.00 16.79 ? 59  ILE A CD1 1 
ATOM   470  N  N   . LEU A 1 60  ? 12.085  3.706   1.997   1.00 13.80 ? 60  LEU A N   1 
ATOM   471  C  CA  . LEU A 1 60  ? 13.502  3.858   1.726   1.00 13.24 ? 60  LEU A CA  1 
ATOM   472  C  C   . LEU A 1 60  ? 14.263  2.648   2.279   1.00 13.93 ? 60  LEU A C   1 
ATOM   473  O  O   . LEU A 1 60  ? 14.074  2.274   3.457   1.00 13.48 ? 60  LEU A O   1 
ATOM   474  C  CB  . LEU A 1 60  ? 13.966  5.158   2.424   1.00 15.05 ? 60  LEU A CB  1 
ATOM   475  C  CG  . LEU A 1 60  ? 15.477  5.357   2.391   1.00 14.51 ? 60  LEU A CG  1 
ATOM   476  C  CD1 . LEU A 1 60  ? 15.998  5.607   0.994   1.00 16.30 ? 60  LEU A CD1 1 
ATOM   477  C  CD2 . LEU A 1 60  ? 15.896  6.492   3.362   1.00 14.56 ? 60  LEU A CD2 1 
ATOM   478  N  N   . ASN A 1 61  ? 15.181  2.096   1.493   1.00 12.10 ? 61  ASN A N   1 
ATOM   479  C  CA  . ASN A 1 61  ? 16.175  1.152   1.967   1.00 12.50 ? 61  ASN A CA  1 
ATOM   480  C  C   . ASN A 1 61  ? 17.359  1.979   2.436   1.00 13.95 ? 61  ASN A C   1 
ATOM   481  O  O   . ASN A 1 61  ? 18.026  2.602   1.598   1.00 15.72 ? 61  ASN A O   1 
ATOM   482  C  CB  . ASN A 1 61  ? 16.577  0.151   0.861   1.00 13.06 ? 61  ASN A CB  1 
ATOM   483  C  CG  . ASN A 1 61  ? 17.635  -0.838  1.265   1.00 14.03 ? 61  ASN A CG  1 
ATOM   484  O  OD1 . ASN A 1 61  ? 18.464  -0.588  2.143   1.00 15.63 ? 61  ASN A OD1 1 
ATOM   485  N  ND2 . ASN A 1 61  ? 17.657  -2.009  0.626   1.00 13.86 ? 61  ASN A ND2 1 
ATOM   486  N  N   . THR A 1 62  ? 17.680  1.990   3.733   1.00 13.34 ? 62  THR A N   1 
ATOM   487  C  CA  . THR A 1 62  ? 18.738  2.867   4.248   1.00 13.48 ? 62  THR A CA  1 
ATOM   488  C  C   . THR A 1 62  ? 20.109  2.201   4.164   1.00 14.15 ? 62  THR A C   1 
ATOM   489  O  O   . THR A 1 62  ? 21.154  2.818   4.482   1.00 16.10 ? 62  THR A O   1 
ATOM   490  C  CB  . THR A 1 62  ? 18.445  3.271   5.705   1.00 13.00 ? 62  THR A CB  1 
ATOM   491  O  OG1 . THR A 1 62  ? 18.617  2.013   6.416   1.00 14.27 ? 62  THR A OG1 1 
ATOM   492  C  CG2 . THR A 1 62  ? 17.072  3.864   5.924   1.00 15.27 ? 62  THR A CG2 1 
ATOM   493  N  N   . GLY A 1 63  ? 20.161  0.917   3.767   1.00 13.60 ? 63  GLY A N   1 
ATOM   494  C  CA  . GLY A 1 63  ? 21.361  0.126   3.895   1.00 13.36 ? 63  GLY A CA  1 
ATOM   495  C  C   . GLY A 1 63  ? 21.435  -0.676  5.196   1.00 14.04 ? 63  GLY A C   1 
ATOM   496  O  O   . GLY A 1 63  ? 22.306  -1.532  5.318   1.00 14.46 ? 63  GLY A O   1 
ATOM   497  N  N   . TYR A 1 64  ? 20.547  -0.348  6.157   1.00 13.64 ? 64  TYR A N   1 
ATOM   498  C  CA  . TYR A 1 64  ? 20.527  -1.093  7.428   1.00 14.07 ? 64  TYR A CA  1 
ATOM   499  C  C   . TYR A 1 64  ? 19.157  -1.683  7.745   1.00 14.35 ? 64  TYR A C   1 
ATOM   500  O  O   . TYR A 1 64  ? 19.039  -2.559  8.616   1.00 15.97 ? 64  TYR A O   1 
ATOM   501  C  CB  . TYR A 1 64  ? 20.870  -0.127  8.567   1.00 18.04 ? 64  TYR A CB  1 
ATOM   502  C  CG  . TYR A 1 64  ? 22.234  0.469   8.437   1.00 23.62 ? 64  TYR A CG  1 
ATOM   503  C  CD1 . TYR A 1 64  ? 23.321  -0.322  8.748   1.00 24.85 ? 64  TYR A CD1 1 
ATOM   504  C  CD2 . TYR A 1 64  ? 22.439  1.750   7.939   1.00 25.07 ? 64  TYR A CD2 1 
ATOM   505  C  CE1 . TYR A 1 64  ? 24.608  0.168   8.699   1.00 27.36 ? 64  TYR A CE1 1 
ATOM   506  C  CE2 . TYR A 1 64  ? 23.742  2.249   7.853   1.00 27.90 ? 64  TYR A CE2 1 
ATOM   507  C  CZ  . TYR A 1 64  ? 24.812  1.446   8.232   1.00 28.66 ? 64  TYR A CZ  1 
ATOM   508  O  OH  . TYR A 1 64  ? 26.113  1.857   8.160   1.00 34.61 ? 64  TYR A OH  1 
ATOM   509  N  N   . LEU A 1 65  ? 18.136  -1.164  7.104   1.00 12.88 ? 65  LEU A N   1 
ATOM   510  C  CA  . LEU A 1 65  ? 16.754  -1.567  7.299   1.00 11.94 ? 65  LEU A CA  1 
ATOM   511  C  C   . LEU A 1 65  ? 15.939  -0.922  6.169   1.00 11.82 ? 65  LEU A C   1 
ATOM   512  O  O   . LEU A 1 65  ? 16.538  -0.273  5.301   1.00 12.75 ? 65  LEU A O   1 
ATOM   513  C  CB  . LEU A 1 65  ? 16.238  -1.175  8.705   1.00 12.70 ? 65  LEU A CB  1 
ATOM   514  C  CG  . LEU A 1 65  ? 16.535  0.252   9.169   1.00 12.75 ? 65  LEU A CG  1 
ATOM   515  C  CD1 . LEU A 1 65  ? 15.640  1.227   8.442   1.00 14.31 ? 65  LEU A CD1 1 
ATOM   516  C  CD2 . LEU A 1 65  ? 16.277  0.430   10.670  1.00 15.03 ? 65  LEU A CD2 1 
ATOM   517  N  N   . PHE A 1 66  ? 14.617  -1.046  6.166   1.00 11.30 ? 66  PHE A N   1 
ATOM   518  C  CA  . PHE A 1 66  ? 13.798  -0.169  5.375   1.00 11.27 ? 66  PHE A CA  1 
ATOM   519  C  C   . PHE A 1 66  ? 12.864  0.607   6.292   1.00 12.24 ? 66  PHE A C   1 
ATOM   520  O  O   . PHE A 1 66  ? 12.502  0.130   7.375   1.00 12.12 ? 66  PHE A O   1 
ATOM   521  C  CB  . PHE A 1 66  ? 13.039  -0.967  4.301   1.00 12.75 ? 66  PHE A CB  1 
ATOM   522  C  CG  . PHE A 1 66  ? 11.908  -1.794  4.860   1.00 11.62 ? 66  PHE A CG  1 
ATOM   523  C  CD1 . PHE A 1 66  ? 10.634  -1.263  4.939   1.00 12.30 ? 66  PHE A CD1 1 
ATOM   524  C  CD2 . PHE A 1 66  ? 12.064  -3.152  5.166   1.00 13.36 ? 66  PHE A CD2 1 
ATOM   525  C  CE1 . PHE A 1 66  ? 9.569   -1.999  5.442   1.00 14.80 ? 66  PHE A CE1 1 
ATOM   526  C  CE2 . PHE A 1 66  ? 10.981  -3.897  5.652   1.00 12.05 ? 66  PHE A CE2 1 
ATOM   527  C  CZ  . PHE A 1 66  ? 9.735   -3.335  5.776   1.00 13.10 ? 66  PHE A CZ  1 
ATOM   528  N  N   . GLN A 1 67  ? 12.498  1.811   5.851   1.00 13.35 ? 67  GLN A N   1 
ATOM   529  C  CA  . GLN A 1 67  ? 11.645  2.649   6.649   1.00 14.98 ? 67  GLN A CA  1 
ATOM   530  C  C   . GLN A 1 67  ? 10.565  3.293   5.794   1.00 14.74 ? 67  GLN A C   1 
ATOM   531  O  O   . GLN A 1 67  ? 10.808  3.682   4.636   1.00 16.20 ? 67  GLN A O   1 
ATOM   532  C  CB  . GLN A 1 67  ? 12.451  3.720   7.410   1.00 16.35 ? 67  GLN A CB  1 
ATOM   533  C  CG  . GLN A 1 67  ? 13.227  4.651   6.493   1.00 17.26 ? 67  GLN A CG  1 
ATOM   534  C  CD  . GLN A 1 67  ? 14.124  5.546   7.312   1.00 19.41 ? 67  GLN A CD  1 
ATOM   535  O  OE1 . GLN A 1 67  ? 14.805  5.106   8.247   1.00 22.23 ? 67  GLN A OE1 1 
ATOM   536  N  NE2 . GLN A 1 67  ? 14.143  6.803   6.886   1.00 19.99 ? 67  GLN A NE2 1 
ATOM   537  N  N   . VAL A 1 68  ? 9.416   3.466   6.398   1.00 14.73 ? 68  VAL A N   1 
ATOM   538  C  CA  . VAL A 1 68  ? 8.324   4.210   5.798   1.00 13.53 ? 68  VAL A CA  1 
ATOM   539  C  C   . VAL A 1 68  ? 8.252   5.560   6.487   1.00 16.26 ? 68  VAL A C   1 
ATOM   540  O  O   . VAL A 1 68  ? 8.052   5.630   7.698   1.00 15.51 ? 68  VAL A O   1 
ATOM   541  C  CB  . VAL A 1 68  ? 6.988   3.457   5.863   1.00 14.52 ? 68  VAL A CB  1 
ATOM   542  C  CG1 . VAL A 1 68  ? 5.799   4.328   5.447   1.00 15.09 ? 68  VAL A CG1 1 
ATOM   543  C  CG2 . VAL A 1 68  ? 7.011   2.179   5.009   1.00 14.36 ? 68  VAL A CG2 1 
ATOM   544  N  N   . GLU A 1 69  ? 8.290   6.648   5.713   1.00 16.64 ? 69  GLU A N   1 
ATOM   545  C  CA  . GLU A 1 69  ? 8.381   7.980   6.281   1.00 15.90 ? 69  GLU A CA  1 
ATOM   546  C  C   . GLU A 1 69  ? 7.041   8.669   6.107   1.00 16.39 ? 69  GLU A C   1 
ATOM   547  O  O   . GLU A 1 69  ? 6.294   8.431   5.118   1.00 16.92 ? 69  GLU A O   1 
ATOM   548  C  CB  . GLU A 1 69  ? 9.408   8.785   5.499   1.00 15.89 ? 69  GLU A CB  1 
ATOM   549  C  CG  . GLU A 1 69  ? 10.797  8.180   5.580   1.00 17.11 ? 69  GLU A CG  1 
ATOM   550  C  CD  . GLU A 1 69  ? 11.730  8.684   4.524   1.00 19.98 ? 69  GLU A CD  1 
ATOM   551  O  OE1 . GLU A 1 69  ? 12.933  8.406   4.678   1.00 25.27 ? 69  GLU A OE1 1 
ATOM   552  O  OE2 . GLU A 1 69  ? 11.223  9.344   3.574   1.00 21.50 ? 69  GLU A OE2 1 
ATOM   553  N  N   . PHE A 1 70  ? 6.762   9.529   7.074   1.00 14.08 ? 70  PHE A N   1 
ATOM   554  C  CA  . PHE A 1 70  ? 5.503   10.260  7.141   1.00 13.72 ? 70  PHE A CA  1 
ATOM   555  C  C   . PHE A 1 70  ? 5.780   11.756  7.054   1.00 15.25 ? 70  PHE A C   1 
ATOM   556  O  O   . PHE A 1 70  ? 6.843   12.219  7.395   1.00 16.04 ? 70  PHE A O   1 
ATOM   557  C  CB  . PHE A 1 70  ? 4.771   9.913   8.443   1.00 15.78 ? 70  PHE A CB  1 
ATOM   558  C  CG  . PHE A 1 70  ? 4.172   8.527   8.395   1.00 16.97 ? 70  PHE A CG  1 
ATOM   559  C  CD1 . PHE A 1 70  ? 4.961   7.406   8.600   1.00 17.21 ? 70  PHE A CD1 1 
ATOM   560  C  CD2 . PHE A 1 70  ? 2.830   8.325   8.123   1.00 17.15 ? 70  PHE A CD2 1 
ATOM   561  C  CE1 . PHE A 1 70  ? 4.437   6.121   8.498   1.00 19.55 ? 70  PHE A CE1 1 
ATOM   562  C  CE2 . PHE A 1 70  ? 2.284   7.041   8.037   1.00 17.23 ? 70  PHE A CE2 1 
ATOM   563  C  CZ  . PHE A 1 70  ? 3.104   5.935   8.211   1.00 19.05 ? 70  PHE A CZ  1 
ATOM   564  N  N   . ASP A 1 71  ? 4.788   12.512  6.577   1.00 16.27 ? 71  ASP A N   1 
ATOM   565  C  CA  . ASP A 1 71  ? 4.806   13.963  6.683   1.00 16.66 ? 71  ASP A CA  1 
ATOM   566  C  C   . ASP A 1 71  ? 4.547   14.338  8.131   1.00 16.20 ? 71  ASP A C   1 
ATOM   567  O  O   . ASP A 1 71  ? 3.443   14.205  8.651   1.00 21.74 ? 71  ASP A O   1 
ATOM   568  C  CB  . ASP A 1 71  ? 3.695   14.547  5.812   1.00 20.31 ? 71  ASP A CB  1 
ATOM   569  C  CG  . ASP A 1 71  ? 3.496   16.043  6.032   1.00 21.42 ? 71  ASP A CG  1 
ATOM   570  O  OD1 . ASP A 1 71  ? 4.355   16.681  6.609   1.00 21.43 ? 71  ASP A OD1 1 
ATOM   571  O  OD2 . ASP A 1 71  ? 2.414   16.541  5.707   1.00 27.27 ? 71  ASP A OD2 1 
ATOM   572  N  N   . ASP A 1 72  ? 5.579   14.811  8.802   1.00 16.24 ? 72  ASP A N   1 
ATOM   573  C  CA  . ASP A 1 72  ? 5.506   15.233  10.188  1.00 16.99 ? 72  ASP A CA  1 
ATOM   574  C  C   . ASP A 1 72  ? 5.668   16.751  10.276  1.00 18.34 ? 72  ASP A C   1 
ATOM   575  O  O   . ASP A 1 72  ? 6.142   17.243  11.296  1.00 19.82 ? 72  ASP A O   1 
ATOM   576  C  CB  . ASP A 1 72  ? 6.563   14.512  11.033  1.00 17.15 ? 72  ASP A CB  1 
ATOM   577  C  CG  . ASP A 1 72  ? 7.991   14.838  10.599  1.00 17.82 ? 72  ASP A CG  1 
ATOM   578  O  OD1 . ASP A 1 72  ? 8.165   15.497  9.525   1.00 19.28 ? 72  ASP A OD1 1 
ATOM   579  O  OD2 . ASP A 1 72  ? 8.952   14.430  11.260  1.00 20.07 ? 72  ASP A OD2 1 
ATOM   580  N  N   . SER A 1 73  ? 5.205   17.459  9.242   1.00 18.23 ? 73  SER A N   1 
ATOM   581  C  CA  . SER A 1 73  ? 5.289   18.935  9.259   1.00 18.73 ? 73  SER A CA  1 
ATOM   582  C  C   . SER A 1 73  ? 4.060   19.556  9.929   1.00 25.37 ? 73  SER A C   1 
ATOM   583  O  O   . SER A 1 73  ? 3.922   20.787  10.037  1.00 22.02 ? 73  SER A O   1 
ATOM   584  C  CB  . SER A 1 73  ? 5.463   19.491  7.854   1.00 20.13 ? 73  SER A CB  1 
ATOM   585  O  OG  . SER A 1 73  ? 4.257   19.299  7.113   1.00 20.06 ? 73  SER A OG  1 
ATOM   586  N  N   . GLN A 1 74  ? 3.120   18.724  10.360  1.00 25.30 ? 74  GLN A N   1 
ATOM   587  C  CA  . GLN A 1 74  ? 1.933   19.208  11.050  1.00 26.53 ? 74  GLN A CA  1 
ATOM   588  C  C   . GLN A 1 74  ? 1.547   18.106  12.018  1.00 26.53 ? 74  GLN A C   1 
ATOM   589  O  O   . GLN A 1 74  ? 2.034   17.001  11.833  1.00 22.51 ? 74  GLN A O   1 
ATOM   590  C  CB  . GLN A 1 74  ? 0.747   19.326  10.088  1.00 31.67 ? 74  GLN A CB  1 
ATOM   591  C  CG  . GLN A 1 74  ? 0.828   20.461  9.087   1.00 37.15 ? 74  GLN A CG  1 
ATOM   592  C  CD  . GLN A 1 74  ? -0.459  20.483  8.303   1.00 40.05 ? 74  GLN A CD  1 
ATOM   593  O  OE1 . GLN A 1 74  ? -1.465  21.015  8.771   1.00 47.61 ? 74  GLN A OE1 1 
ATOM   594  N  NE2 . GLN A 1 74  ? -0.449  19.876  7.124   1.00 36.18 ? 74  GLN A NE2 1 
ATOM   595  N  N   . ASP A 1 75  ? 0.677   18.424  12.985  1.00 30.17 ? 75  ASP A N   1 
ATOM   596  C  CA  . ASP A 1 75  ? 0.241   17.487  14.009  1.00 31.48 ? 75  ASP A CA  1 
ATOM   597  C  C   . ASP A 1 75  ? -0.844  16.599  13.407  1.00 32.63 ? 75  ASP A C   1 
ATOM   598  O  O   . ASP A 1 75  ? -2.036  16.885  13.507  1.00 38.82 ? 75  ASP A O   1 
ATOM   599  C  CB  . ASP A 1 75  ? -0.232  18.190  15.285  1.00 38.74 ? 75  ASP A CB  1 
ATOM   600  C  CG  . ASP A 1 75  ? 0.677   18.044  16.498  1.00 41.57 ? 75  ASP A CG  1 
ATOM   601  O  OD1 . ASP A 1 75  ? 1.672   17.279  16.441  1.00 38.45 ? 75  ASP A OD1 1 
ATOM   602  O  OD2 . ASP A 1 75  ? 0.379   18.699  17.508  1.00 44.42 ? 75  ASP A OD2 1 
ATOM   603  N  N   . LYS A 1 76  ? -0.398  15.547  12.733  1.00 27.45 ? 76  LYS A N   1 
ATOM   604  C  CA  . LYS A 1 76  ? -1.310  14.623  12.092  1.00 29.90 ? 76  LYS A CA  1 
ATOM   605  C  C   . LYS A 1 76  ? -1.410  13.402  13.003  1.00 31.38 ? 76  LYS A C   1 
ATOM   606  O  O   . LYS A 1 76  ? -2.219  13.342  13.929  1.00 35.90 ? 76  LYS A O   1 
ATOM   607  C  CB  . LYS A 1 76  ? -0.809  14.359  10.668  1.00 26.78 ? 76  LYS A CB  1 
ATOM   608  C  CG  . LYS A 1 76  ? -1.108  15.492  9.685   1.00 30.97 ? 76  LYS A CG  1 
ATOM   609  C  CD  . LYS A 1 76  ? -0.449  15.296  8.337   1.00 31.55 ? 76  LYS A CD  1 
ATOM   610  C  CE  . LYS A 1 76  ? -0.944  16.290  7.304   1.00 30.97 ? 76  LYS A CE  1 
ATOM   611  N  NZ  . LYS A 1 76  ? -0.394  16.011  5.958   1.00 31.26 ? 76  LYS A NZ  1 
ATOM   612  N  N   . ALA A 1 77  ? -0.480  12.491  12.814  1.00 26.23 ? 77  ALA A N   1 
ATOM   613  C  CA  . ALA A 1 77  ? -0.453  11.246  13.559  1.00 24.44 ? 77  ALA A CA  1 
ATOM   614  C  C   . ALA A 1 77  ? 0.337   11.484  14.841  1.00 23.78 ? 77  ALA A C   1 
ATOM   615  O  O   . ALA A 1 77  ? 1.475   11.948  14.790  1.00 26.57 ? 77  ALA A O   1 
ATOM   616  C  CB  . ALA A 1 77  ? 0.264   10.261  12.684  1.00 24.35 ? 77  ALA A CB  1 
ATOM   617  N  N   . VAL A 1 78  ? -0.261  11.215  15.991  1.00 18.97 ? 78  VAL A N   1 
ATOM   618  C  CA  . VAL A 1 78  ? 0.433   11.481  17.240  1.00 18.97 ? 78  VAL A CA  1 
ATOM   619  C  C   . VAL A 1 78  ? 0.196   10.348  18.223  1.00 18.02 ? 78  VAL A C   1 
ATOM   620  O  O   . VAL A 1 78  ? -0.847  9.676   18.214  1.00 18.46 ? 78  VAL A O   1 
ATOM   621  C  CB  . VAL A 1 78  ? 0.035   12.835  17.853  1.00 22.70 ? 78  VAL A CB  1 
ATOM   622  C  CG1 . VAL A 1 78  ? 0.211   13.985  16.874  1.00 24.38 ? 78  VAL A CG1 1 
ATOM   623  C  CG2 . VAL A 1 78  ? -1.370  12.800  18.373  1.00 24.61 ? 78  VAL A CG2 1 
ATOM   624  N  N   . LEU A 1 79  ? 1.173   10.195  19.112  1.00 16.19 ? 79  LEU A N   1 
ATOM   625  C  CA  . LEU A 1 79  ? 1.172   9.328   20.261  1.00 14.96 ? 79  LEU A CA  1 
ATOM   626  C  C   . LEU A 1 79  ? 1.213   10.203  21.480  1.00 15.85 ? 79  LEU A C   1 
ATOM   627  O  O   . LEU A 1 79  ? 2.047   11.092  21.583  1.00 15.21 ? 79  LEU A O   1 
ATOM   628  C  CB  . LEU A 1 79  ? 2.426   8.459   20.190  1.00 14.35 ? 79  LEU A CB  1 
ATOM   629  C  CG  . LEU A 1 79  ? 2.535   7.380   21.252  1.00 14.25 ? 79  LEU A CG  1 
ATOM   630  C  CD1 . LEU A 1 79  ? 1.432   6.343   21.155  1.00 18.00 ? 79  LEU A CD1 1 
ATOM   631  C  CD2 . LEU A 1 79  ? 3.904   6.699   21.114  1.00 14.75 ? 79  LEU A CD2 1 
ATOM   632  N  N   . LYS A 1 80  ? 0.346   9.908   22.425  1.00 16.07 ? 80  LYS A N   1 
ATOM   633  C  CA  . LYS A 1 80  ? 0.365   10.573  23.709  1.00 16.98 ? 80  LYS A CA  1 
ATOM   634  C  C   . LYS A 1 80  ? -0.198  9.629   24.761  1.00 17.37 ? 80  LYS A C   1 
ATOM   635  O  O   . LYS A 1 80  ? -0.522  8.471   24.461  1.00 16.86 ? 80  LYS A O   1 
ATOM   636  C  CB  . LYS A 1 80  ? -0.404  11.906  23.740  1.00 22.02 ? 80  LYS A CB  1 
ATOM   637  C  CG  . LYS A 1 80  ? -1.910  11.792  23.582  1.00 27.44 ? 80  LYS A CG  1 
ATOM   638  C  CD  . LYS A 1 80  ? -2.594  13.164  23.531  1.00 26.64 ? 80  LYS A CD  1 
ATOM   639  C  CE  . LYS A 1 80  ? -2.085  14.056  22.416  1.00 34.58 ? 80  LYS A CE  1 
ATOM   640  N  N   . GLY A 1 81  ? -0.200  10.141  25.987  1.00 17.29 ? 81  GLY A N   1 
ATOM   641  C  CA  . GLY A 1 81  ? -0.657  9.404   27.156  1.00 20.50 ? 81  GLY A CA  1 
ATOM   642  C  C   . GLY A 1 81  ? 0.329   8.311   27.531  1.00 20.20 ? 81  GLY A C   1 
ATOM   643  O  O   . GLY A 1 81  ? 1.517   8.446   27.288  1.00 19.37 ? 81  GLY A O   1 
ATOM   644  N  N   . GLY A 1 82  ? -0.138  7.257   28.201  1.00 23.85 ? 82  GLY A N   1 
ATOM   645  C  CA  . GLY A 1 82  ? 0.818   6.280   28.692  1.00 24.61 ? 82  GLY A CA  1 
ATOM   646  C  C   . GLY A 1 82  ? 1.824   6.911   29.660  1.00 25.40 ? 82  GLY A C   1 
ATOM   647  O  O   . GLY A 1 82  ? 1.440   7.641   30.590  1.00 22.97 ? 82  GLY A O   1 
ATOM   648  N  N   . PRO A 1 83  ? 3.157   6.678   29.502  1.00 18.66 ? 83  PRO A N   1 
ATOM   649  C  CA  . PRO A 1 83  ? 4.129   7.309   30.365  1.00 19.52 ? 83  PRO A CA  1 
ATOM   650  C  C   . PRO A 1 83  ? 4.488   8.707   29.903  1.00 16.90 ? 83  PRO A C   1 
ATOM   651  O  O   . PRO A 1 83  ? 5.273   9.371   30.572  1.00 21.17 ? 83  PRO A O   1 
ATOM   652  C  CB  . PRO A 1 83  ? 5.360   6.389   30.214  1.00 18.22 ? 83  PRO A CB  1 
ATOM   653  C  CG  . PRO A 1 83  ? 5.262   5.929   28.759  1.00 17.78 ? 83  PRO A CG  1 
ATOM   654  C  CD  . PRO A 1 83  ? 3.771   5.824   28.455  1.00 18.20 ? 83  PRO A CD  1 
ATOM   655  N  N   . LEU A 1 84  ? 3.899   9.128   28.768  1.00 16.35 ? 84  LEU A N   1 
ATOM   656  C  CA  . LEU A 1 84  ? 4.437   10.305  28.091  1.00 17.84 ? 84  LEU A CA  1 
ATOM   657  C  C   . LEU A 1 84  ? 3.816   11.574  28.655  1.00 20.00 ? 84  LEU A C   1 
ATOM   658  O  O   . LEU A 1 84  ? 2.611   11.566  28.950  1.00 20.06 ? 84  LEU A O   1 
ATOM   659  C  CB  . LEU A 1 84  ? 4.227   10.221  26.586  1.00 15.62 ? 84  LEU A CB  1 
ATOM   660  C  CG  . LEU A 1 84  ? 4.697   8.931   25.918  1.00 13.80 ? 84  LEU A CG  1 
ATOM   661  C  CD1 . LEU A 1 84  ? 4.216   8.946   24.499  1.00 13.79 ? 84  LEU A CD1 1 
ATOM   662  C  CD2 . LEU A 1 84  ? 6.231   8.883   25.926  1.00 15.75 ? 84  LEU A CD2 1 
ATOM   663  N  N   . ASP A 1 85  ? 4.667   12.607  28.728  1.00 20.29 ? 85  ASP A N   1 
ATOM   664  C  CA  . ASP A 1 85  ? 4.244   13.976  28.981  1.00 20.94 ? 85  ASP A CA  1 
ATOM   665  C  C   . ASP A 1 85  ? 4.187   14.650  27.620  1.00 23.10 ? 85  ASP A C   1 
ATOM   666  O  O   . ASP A 1 85  ? 5.145   14.588  26.847  1.00 26.14 ? 85  ASP A O   1 
ATOM   667  C  CB  . ASP A 1 85  ? 5.200   14.687  29.939  1.00 24.11 ? 85  ASP A CB  1 
ATOM   668  C  CG  . ASP A 1 85  ? 5.117   14.183  31.370  1.00 30.86 ? 85  ASP A CG  1 
ATOM   669  O  OD1 . ASP A 1 85  ? 4.046   13.656  31.757  1.00 31.50 ? 85  ASP A OD1 1 
ATOM   670  O  OD2 . ASP A 1 85  ? 6.127   14.296  32.085  1.00 31.10 ? 85  ASP A OD2 1 
ATOM   671  N  N   . GLY A 1 86  ? 3.055   15.280  27.301  1.00 24.89 ? 86  GLY A N   1 
ATOM   672  C  CA  . GLY A 1 86  ? 2.931   15.999  26.043  1.00 24.98 ? 86  GLY A CA  1 
ATOM   673  C  C   . GLY A 1 86  ? 2.613   15.096  24.838  1.00 26.11 ? 86  GLY A C   1 
ATOM   674  O  O   . GLY A 1 86  ? 2.016   14.027  24.976  1.00 28.72 ? 86  GLY A O   1 
ATOM   675  N  N   . THR A 1 87  ? 3.019   15.544  23.637  1.00 23.74 ? 87  THR A N   1 
ATOM   676  C  CA  . THR A 1 87  ? 2.562   15.000  22.372  1.00 21.52 ? 87  THR A CA  1 
ATOM   677  C  C   . THR A 1 87  ? 3.776   14.621  21.539  1.00 18.73 ? 87  THR A C   1 
ATOM   678  O  O   . THR A 1 87  ? 4.762   15.363  21.475  1.00 18.00 ? 87  THR A O   1 
ATOM   679  C  CB  . THR A 1 87  ? 1.685   16.040  21.643  1.00 27.10 ? 87  THR A CB  1 
ATOM   680  O  OG1 . THR A 1 87  ? 0.464   16.025  22.386  1.00 33.71 ? 87  THR A OG1 1 
ATOM   681  C  CG2 . THR A 1 87  ? 1.379   15.712  20.195  1.00 30.14 ? 87  THR A CG2 1 
ATOM   682  N  N   . TYR A 1 88  ? 3.742   13.417  20.953  1.00 14.79 ? 88  TYR A N   1 
ATOM   683  C  CA  . TYR A 1 88  ? 4.865   12.956  20.138  1.00 13.88 ? 88  TYR A CA  1 
ATOM   684  C  C   . TYR A 1 88  ? 4.333   12.660  18.750  1.00 13.43 ? 88  TYR A C   1 
ATOM   685  O  O   . TYR A 1 88  ? 3.309   11.990  18.610  1.00 18.86 ? 88  TYR A O   1 
ATOM   686  C  CB  . TYR A 1 88  ? 5.541   11.710  20.711  1.00 13.40 ? 88  TYR A CB  1 
ATOM   687  C  CG  . TYR A 1 88  ? 6.312   11.888  21.989  1.00 12.63 ? 88  TYR A CG  1 
ATOM   688  C  CD1 . TYR A 1 88  ? 5.694   12.298  23.176  1.00 13.34 ? 88  TYR A CD1 1 
ATOM   689  C  CD2 . TYR A 1 88  ? 7.685   11.698  22.006  1.00 13.27 ? 88  TYR A CD2 1 
ATOM   690  C  CE1 . TYR A 1 88  ? 6.433   12.451  24.348  1.00 12.80 ? 88  TYR A CE1 1 
ATOM   691  C  CE2 . TYR A 1 88  ? 8.429   11.848  23.155  1.00 11.74 ? 88  TYR A CE2 1 
ATOM   692  C  CZ  . TYR A 1 88  ? 7.809   12.209  24.337  1.00 12.17 ? 88  TYR A CZ  1 
ATOM   693  O  OH  . TYR A 1 88  ? 8.598   12.295  25.439  1.00 14.44 ? 88  TYR A OH  1 
ATOM   694  N  N   . ARG A 1 89  ? 4.985   13.175  17.738  1.00 12.08 ? 89  ARG A N   1 
ATOM   695  C  CA  . ARG A 1 89  ? 4.535   13.092  16.367  1.00 12.23 ? 89  ARG A CA  1 
ATOM   696  C  C   . ARG A 1 89  ? 5.174   11.933  15.598  1.00 11.44 ? 89  ARG A C   1 
ATOM   697  O  O   . ARG A 1 89  ? 6.407   11.779  15.603  1.00 12.43 ? 89  ARG A O   1 
ATOM   698  C  CB  . ARG A 1 89  ? 4.776   14.475  15.757  1.00 15.37 ? 89  ARG A CB  1 
ATOM   699  C  CG  . ARG A 1 89  ? 4.288   14.563  14.324  1.00 18.00 ? 89  ARG A CG  1 
ATOM   700  C  CD  . ARG A 1 89  ? 4.495   15.977  13.793  1.00 19.11 ? 89  ARG A CD  1 
ATOM   701  N  NE  . ARG A 1 89  ? 3.802   17.011  14.571  1.00 20.59 ? 89  ARG A NE  1 
ATOM   702  C  CZ  . ARG A 1 89  ? 3.988   18.320  14.424  1.00 21.13 ? 89  ARG A CZ  1 
ATOM   703  N  NH1 . ARG A 1 89  ? 4.862   18.776  13.542  1.00 21.10 ? 89  ARG A NH1 1 
ATOM   704  N  NH2 . ARG A 1 89  ? 3.312   19.170  15.191  1.00 21.01 ? 89  ARG A NH2 1 
ATOM   705  N  N   . LEU A 1 90  ? 4.364   11.165  14.838  1.00 12.92 ? 90  LEU A N   1 
ATOM   706  C  CA  . LEU A 1 90  ? 4.921   10.042  14.119  1.00 12.01 ? 90  LEU A CA  1 
ATOM   707  C  C   . LEU A 1 90  ? 5.753   10.561  12.958  1.00 12.34 ? 90  LEU A C   1 
ATOM   708  O  O   . LEU A 1 90  ? 5.293   11.400  12.153  1.00 15.47 ? 90  LEU A O   1 
ATOM   709  C  CB  . LEU A 1 90  ? 3.799   9.157   13.563  1.00 13.90 ? 90  LEU A CB  1 
ATOM   710  C  CG  . LEU A 1 90  ? 4.269   8.036   12.625  1.00 13.80 ? 90  LEU A CG  1 
ATOM   711  C  CD1 . LEU A 1 90  ? 4.944   6.899   13.403  1.00 13.72 ? 90  LEU A CD1 1 
ATOM   712  C  CD2 . LEU A 1 90  ? 3.002   7.446   11.985  1.00 16.77 ? 90  LEU A CD2 1 
ATOM   713  N  N   . LYS A 1 91  ? 6.999   10.087  12.871  1.00 12.53 ? 91  LYS A N   1 
ATOM   714  C  CA  . LYS A 1 91  ? 7.903   10.462  11.803  1.00 13.23 ? 91  LYS A CA  1 
ATOM   715  C  C   . LYS A 1 91  ? 8.096   9.325   10.815  1.00 13.21 ? 91  LYS A C   1 
ATOM   716  O  O   . LYS A 1 91  ? 8.184   9.549   9.602   1.00 12.37 ? 91  LYS A O   1 
ATOM   717  C  CB  . LYS A 1 91  ? 9.283   10.801  12.393  1.00 15.07 ? 91  LYS A CB  1 
ATOM   718  C  CG  . LYS A 1 91  ? 10.369  11.088  11.361  1.00 17.22 ? 91  LYS A CG  1 
ATOM   719  C  CD  . LYS A 1 91  ? 11.600  11.771  11.889  1.00 24.33 ? 91  LYS A CD  1 
ATOM   720  C  CE  . LYS A 1 91  ? 12.364  12.305  10.690  1.00 25.47 ? 91  LYS A CE  1 
ATOM   721  N  NZ  . LYS A 1 91  ? 11.623  13.449  10.094  1.00 31.71 ? 91  LYS A NZ  1 
ATOM   722  N  N   . GLN A 1 92  ? 8.233   8.085   11.302  1.00 12.80 ? 92  GLN A N   1 
ATOM   723  C  CA  . GLN A 1 92  ? 8.558   6.974   10.402  1.00 12.93 ? 92  GLN A CA  1 
ATOM   724  C  C   . GLN A 1 92  ? 8.310   5.656   11.141  1.00 13.49 ? 92  GLN A C   1 
ATOM   725  O  O   . GLN A 1 92  ? 8.185   5.693   12.370  1.00 13.36 ? 92  GLN A O   1 
ATOM   726  C  CB  . GLN A 1 92  ? 10.020  6.986   9.941   1.00 14.40 ? 92  GLN A CB  1 
ATOM   727  C  CG  . GLN A 1 92  ? 11.086  6.993   11.059  1.00 15.80 ? 92  GLN A CG  1 
ATOM   728  C  CD  . GLN A 1 92  ? 11.980  5.775   11.109  1.00 18.20 ? 92  GLN A CD  1 
ATOM   729  O  OE1 . GLN A 1 92  ? 11.501  4.680   11.213  1.00 17.74 ? 92  GLN A OE1 1 
ATOM   730  N  NE2 . GLN A 1 92  ? 13.281  5.964   11.065  1.00 30.53 ? 92  GLN A NE2 1 
ATOM   731  N  N   . PHE A 1 93  ? 8.141   4.552   10.391  1.00 11.90 ? 93  PHE A N   1 
ATOM   732  C  CA  . PHE A 1 93  ? 8.276   3.243   11.016  1.00 12.21 ? 93  PHE A CA  1 
ATOM   733  C  C   . PHE A 1 93  ? 9.290   2.430   10.235  1.00 11.06 ? 93  PHE A C   1 
ATOM   734  O  O   . PHE A 1 93  ? 9.552   2.670   9.075   1.00 13.11 ? 93  PHE A O   1 
ATOM   735  C  CB  . PHE A 1 93  ? 6.946   2.516   11.222  1.00 12.50 ? 93  PHE A CB  1 
ATOM   736  C  CG  . PHE A 1 93  ? 6.232   2.074   9.975   1.00 13.20 ? 93  PHE A CG  1 
ATOM   737  C  CD1 . PHE A 1 93  ? 6.646   0.971   9.265   1.00 13.44 ? 93  PHE A CD1 1 
ATOM   738  C  CD2 . PHE A 1 93  ? 5.130   2.794   9.535   1.00 12.71 ? 93  PHE A CD2 1 
ATOM   739  C  CE1 . PHE A 1 93  ? 5.986   0.594   8.098   1.00 14.26 ? 93  PHE A CE1 1 
ATOM   740  C  CE2 . PHE A 1 93  ? 4.444   2.402   8.401   1.00 14.60 ? 93  PHE A CE2 1 
ATOM   741  C  CZ  . PHE A 1 93  ? 4.884   1.309   7.696   1.00 15.54 ? 93  PHE A CZ  1 
ATOM   742  N  N   . HIS A 1 94  ? 9.856   1.418   10.909  1.00 10.19 ? 94  HIS A N   1 
ATOM   743  C  CA  . HIS A 1 94  ? 10.791  0.498   10.293  1.00 10.04 ? 94  HIS A CA  1 
ATOM   744  C  C   . HIS A 1 94  ? 10.751  -0.811  11.062  1.00 10.63 ? 94  HIS A C   1 
ATOM   745  O  O   . HIS A 1 94  ? 10.045  -0.924  12.071  1.00 10.32 ? 94  HIS A O   1 
ATOM   746  C  CB  . HIS A 1 94  ? 12.223  1.064   10.286  1.00 10.74 ? 94  HIS A CB  1 
ATOM   747  C  CG  . HIS A 1 94  ? 12.773  1.300   11.661  1.00 10.01 ? 94  HIS A CG  1 
ATOM   748  N  ND1 . HIS A 1 94  ? 12.616  2.529   12.315  1.00 9.90  ? 94  HIS A ND1 1 
ATOM   749  C  CD2 . HIS A 1 94  ? 13.311  0.413   12.552  1.00 9.92  ? 94  HIS A CD2 1 
ATOM   750  C  CE1 . HIS A 1 94  ? 13.115  2.417   13.533  1.00 9.88  ? 94  HIS A CE1 1 
ATOM   751  N  NE2 . HIS A 1 94  ? 13.577  1.132   13.701  1.00 9.20  ? 94  HIS A NE2 1 
ATOM   752  N  N   . PHE A 1 95  ? 11.481  -1.769  10.548  1.00 9.97  ? 95  PHE A N   1 
ATOM   753  C  CA  . PHE A 1 95  ? 11.525  -3.100  11.133  1.00 9.29  ? 95  PHE A CA  1 
ATOM   754  C  C   . PHE A 1 95  ? 12.976  -3.555  11.271  1.00 10.26 ? 95  PHE A C   1 
ATOM   755  O  O   . PHE A 1 95  ? 13.896  -3.081  10.601  1.00 11.40 ? 95  PHE A O   1 
ATOM   756  C  CB  . PHE A 1 95  ? 10.841  -4.145  10.228  1.00 10.55 ? 95  PHE A CB  1 
ATOM   757  C  CG  . PHE A 1 95  ? 9.380   -3.891  9.940   1.00 9.84  ? 95  PHE A CG  1 
ATOM   758  C  CD1 . PHE A 1 95  ? 8.977   -2.995  8.957   1.00 10.94 ? 95  PHE A CD1 1 
ATOM   759  C  CD2 . PHE A 1 95  ? 8.414   -4.585  10.640  1.00 10.82 ? 95  PHE A CD2 1 
ATOM   760  C  CE1 . PHE A 1 95  ? 7.639   -2.800  8.680   1.00 11.85 ? 95  PHE A CE1 1 
ATOM   761  C  CE2 . PHE A 1 95  ? 7.070   -4.359  10.406  1.00 11.45 ? 95  PHE A CE2 1 
ATOM   762  C  CZ  . PHE A 1 95  ? 6.696   -3.476  9.408   1.00 11.97 ? 95  PHE A CZ  1 
ATOM   763  N  N   . HIS A 1 96  ? 13.177  -4.485  12.227  1.00 10.15 ? 96  HIS A N   1 
ATOM   764  C  CA  . HIS A 1 96  ? 14.384  -5.295  12.388  1.00 9.99  ? 96  HIS A CA  1 
ATOM   765  C  C   . HIS A 1 96  ? 13.919  -6.738  12.278  1.00 10.25 ? 96  HIS A C   1 
ATOM   766  O  O   . HIS A 1 96  ? 12.848  -7.061  12.768  1.00 10.94 ? 96  HIS A O   1 
ATOM   767  C  CB  . HIS A 1 96  ? 15.105  -5.060  13.746  1.00 10.14 ? 96  HIS A CB  1 
ATOM   768  C  CG  . HIS A 1 96  ? 15.310  -3.619  14.045  1.00 10.04 ? 96  HIS A CG  1 
ATOM   769  N  ND1 . HIS A 1 96  ? 16.535  -3.012  13.821  1.00 9.97  ? 96  HIS A ND1 1 
ATOM   770  C  CD2 . HIS A 1 96  ? 14.461  -2.658  14.463  1.00 9.55  ? 96  HIS A CD2 1 
ATOM   771  C  CE1 . HIS A 1 96  ? 16.421  -1.714  14.187  1.00 10.03 ? 96  HIS A CE1 1 
ATOM   772  N  NE2 . HIS A 1 96  ? 15.154  -1.469  14.497  1.00 9.76  ? 96  HIS A NE2 1 
ATOM   773  N  N   . TRP A 1 97  ? 14.704  -7.610  11.659  1.00 9.70  ? 97  TRP A N   1 
ATOM   774  C  CA  . TRP A 1 97  ? 14.280  -8.992  11.474  1.00 9.93  ? 97  TRP A CA  1 
ATOM   775  C  C   . TRP A 1 97  ? 15.494  -9.925  11.380  1.00 9.37  ? 97  TRP A C   1 
ATOM   776  O  O   . TRP A 1 97  ? 16.652  -9.537  11.286  1.00 10.76 ? 97  TRP A O   1 
ATOM   777  C  CB  . TRP A 1 97  ? 13.371  -9.111  10.228  1.00 9.98  ? 97  TRP A CB  1 
ATOM   778  C  CG  . TRP A 1 97  ? 14.061  -8.747  8.950   1.00 10.03 ? 97  TRP A CG  1 
ATOM   779  C  CD1 . TRP A 1 97  ? 14.810  -9.568  8.166   1.00 11.46 ? 97  TRP A CD1 1 
ATOM   780  C  CD2 . TRP A 1 97  ? 14.153  -7.420  8.415   1.00 10.09 ? 97  TRP A CD2 1 
ATOM   781  N  NE1 . TRP A 1 97  ? 15.259  -8.873  7.091   1.00 12.93 ? 97  TRP A NE1 1 
ATOM   782  C  CE2 . TRP A 1 97  ? 14.885  -7.560  7.215   1.00 10.04 ? 97  TRP A CE2 1 
ATOM   783  C  CE3 . TRP A 1 97  ? 13.611  -6.167  8.755   1.00 11.38 ? 97  TRP A CE3 1 
ATOM   784  C  CZ2 . TRP A 1 97  ? 15.139  -6.469  6.392   1.00 11.19 ? 97  TRP A CZ2 1 
ATOM   785  C  CZ3 . TRP A 1 97  ? 13.885  -5.074  7.945   1.00 12.20 ? 97  TRP A CZ3 1 
ATOM   786  C  CH2 . TRP A 1 97  ? 14.638  -5.234  6.764   1.00 11.99 ? 97  TRP A CH2 1 
ATOM   787  N  N   . GLY A 1 98  ? 15.173  -11.236 11.391  1.00 10.13 ? 98  GLY A N   1 
ATOM   788  C  CA  . GLY A 1 98  ? 16.133  -12.320 11.455  1.00 10.46 ? 98  GLY A CA  1 
ATOM   789  C  C   . GLY A 1 98  ? 16.397  -13.010 10.108  1.00 11.38 ? 98  GLY A C   1 
ATOM   790  O  O   . GLY A 1 98  ? 15.680  -12.778 9.150   1.00 12.40 ? 98  GLY A O   1 
ATOM   791  N  N   . SER A 1 99  ? 17.417  -13.869 10.116  1.00 12.53 ? 99  SER A N   1 
ATOM   792  C  CA  . SER A 1 99  ? 17.622  -14.819 9.011   1.00 12.45 ? 99  SER A CA  1 
ATOM   793  C  C   . SER A 1 99  ? 16.702  -16.036 9.169   1.00 13.51 ? 99  SER A C   1 
ATOM   794  O  O   . SER A 1 99  ? 16.594  -16.807 8.223   1.00 17.07 ? 99  SER A O   1 
ATOM   795  C  CB  . SER A 1 99  ? 19.087  -15.233 9.003   1.00 15.26 ? 99  SER A CB  1 
ATOM   796  O  OG  . SER A 1 99  ? 19.483  -15.692 10.292  1.00 15.32 ? 99  SER A OG  1 
ATOM   797  N  N   . LEU A 1 100 ? 16.158  -16.264 10.367  1.00 12.90 ? 100 LEU A N   1 
ATOM   798  C  CA  . LEU A 1 100 ? 15.357  -17.420 10.716  1.00 15.66 ? 100 LEU A CA  1 
ATOM   799  C  C   . LEU A 1 100 ? 14.189  -16.916 11.553  1.00 13.28 ? 100 LEU A C   1 
ATOM   800  O  O   . LEU A 1 100 ? 14.306  -15.888 12.249  1.00 12.99 ? 100 LEU A O   1 
ATOM   801  C  CB  . LEU A 1 100 ? 16.170  -18.354 11.609  1.00 18.18 ? 100 LEU A CB  1 
ATOM   802  C  CG  . LEU A 1 100 ? 17.479  -18.831 10.994  1.00 22.88 ? 100 LEU A CG  1 
ATOM   803  C  CD1 . LEU A 1 100 ? 18.437  -19.337 12.066  1.00 24.30 ? 100 LEU A CD1 1 
ATOM   804  C  CD2 . LEU A 1 100 ? 17.165  -19.923 9.975   1.00 23.14 ? 100 LEU A CD2 1 
ATOM   805  N  N   . ASP A 1 101 ? 13.070  -17.652 11.511  1.00 14.00 ? 101 ASP A N   1 
ATOM   806  C  CA  . ASP A 1 101 ? 11.882  -17.205 12.236  1.00 13.04 ? 101 ASP A CA  1 
ATOM   807  C  C   . ASP A 1 101 ? 12.136  -17.118 13.752  1.00 13.33 ? 101 ASP A C   1 
ATOM   808  O  O   . ASP A 1 101 ? 11.433  -16.363 14.435  1.00 16.50 ? 101 ASP A O   1 
ATOM   809  C  CB  . ASP A 1 101 ? 10.725  -18.154 11.940  1.00 13.91 ? 101 ASP A CB  1 
ATOM   810  C  CG  . ASP A 1 101 ? 10.234  -18.164 10.505  1.00 15.62 ? 101 ASP A CG  1 
ATOM   811  O  OD1 . ASP A 1 101 ? 10.604  -17.290 9.699   1.00 14.97 ? 101 ASP A OD1 1 
ATOM   812  O  OD2 . ASP A 1 101 ? 9.405   -19.019 10.244  1.00 19.32 ? 101 ASP A OD2 1 
ATOM   813  N  N   . GLY A 1 102 ? 13.145  -17.850 14.256  1.00 15.02 ? 102 GLY A N   1 
ATOM   814  C  CA  . GLY A 1 102 ? 13.486  -17.921 15.680  1.00 15.51 ? 102 GLY A CA  1 
ATOM   815  C  C   . GLY A 1 102 ? 14.234  -16.715 16.243  1.00 15.50 ? 102 GLY A C   1 
ATOM   816  O  O   . GLY A 1 102 ? 14.587  -16.700 17.433  1.00 15.77 ? 102 GLY A O   1 
ATOM   817  N  N   . GLN A 1 103 ? 14.511  -15.703 15.396  1.00 12.91 ? 103 GLN A N   1 
ATOM   818  C  CA  . GLN A 1 103 ? 15.303  -14.577 15.884  1.00 12.13 ? 103 GLN A CA  1 
ATOM   819  C  C   . GLN A 1 103 ? 14.968  -13.385 15.002  1.00 11.22 ? 103 GLN A C   1 
ATOM   820  O  O   . GLN A 1 103 ? 14.405  -13.534 13.931  1.00 12.07 ? 103 GLN A O   1 
ATOM   821  C  CB  . GLN A 1 103 ? 16.793  -14.878 15.881  1.00 13.59 ? 103 GLN A CB  1 
ATOM   822  C  CG  . GLN A 1 103 ? 17.327  -15.042 14.460  1.00 14.37 ? 103 GLN A CG  1 
ATOM   823  C  CD  . GLN A 1 103 ? 18.696  -15.663 14.473  1.00 17.70 ? 103 GLN A CD  1 
ATOM   824  O  OE1 . GLN A 1 103 ? 18.859  -16.724 15.090  1.00 20.46 ? 103 GLN A OE1 1 
ATOM   825  N  NE2 . GLN A 1 103 ? 19.662  -15.066 13.781  1.00 16.87 ? 103 GLN A NE2 1 
ATOM   826  N  N   . GLY A 1 104 ? 15.292  -12.174 15.468  1.00 10.87 ? 104 GLY A N   1 
ATOM   827  C  CA  . GLY A 1 104 ? 15.044  -10.992 14.669  1.00 10.77 ? 104 GLY A CA  1 
ATOM   828  C  C   . GLY A 1 104 ? 14.613  -9.805  15.509  1.00 9.66  ? 104 GLY A C   1 
ATOM   829  O  O   . GLY A 1 104 ? 14.843  -8.666  15.141  1.00 11.41 ? 104 GLY A O   1 
ATOM   830  N  N   . SER A 1 105 ? 13.904  -10.072 16.619  1.00 8.58  ? 105 SER A N   1 
ATOM   831  C  CA  . SER A 1 105 ? 13.505  -8.949  17.476  1.00 9.19  ? 105 SER A CA  1 
ATOM   832  C  C   . SER A 1 105 ? 14.706  -8.415  18.236  1.00 9.24  ? 105 SER A C   1 
ATOM   833  O  O   . SER A 1 105 ? 15.720  -9.075  18.432  1.00 9.77  ? 105 SER A O   1 
ATOM   834  C  CB  . SER A 1 105 ? 12.392  -9.272  18.418  1.00 8.69  ? 105 SER A CB  1 
ATOM   835  O  OG  . SER A 1 105 ? 12.763  -10.278 19.341  1.00 9.22  ? 105 SER A OG  1 
ATOM   836  N  N   . GLU A 1 106 ? 14.569  -7.134  18.593  1.00 9.37  ? 106 GLU A N   1 
ATOM   837  C  CA  . GLU A 1 106 ? 15.576  -6.472  19.430  1.00 8.91  ? 106 GLU A CA  1 
ATOM   838  C  C   . GLU A 1 106 ? 15.212  -6.658  20.905  1.00 9.29  ? 106 GLU A C   1 
ATOM   839  O  O   . GLU A 1 106 ? 16.008  -7.221  21.639  1.00 9.32  ? 106 GLU A O   1 
ATOM   840  C  CB  . GLU A 1 106 ? 15.630  -4.982  19.038  1.00 9.08  ? 106 GLU A CB  1 
ATOM   841  C  CG  . GLU A 1 106 ? 15.969  -4.819  17.564  1.00 9.08  ? 106 GLU A CG  1 
ATOM   842  C  CD  . GLU A 1 106 ? 16.701  -3.556  17.265  1.00 9.46  ? 106 GLU A CD  1 
ATOM   843  O  OE1 . GLU A 1 106 ? 16.151  -2.499  17.442  1.00 9.97  ? 106 GLU A OE1 1 
ATOM   844  O  OE2 . GLU A 1 106 ? 17.888  -3.661  16.883  1.00 10.48 ? 106 GLU A OE2 1 
ATOM   845  N  N   . HIS A 1 107 ? 14.024  -6.245  21.342  1.00 8.89  ? 107 HIS A N   1 
ATOM   846  C  CA  . HIS A 1 107 ? 13.646  -6.616  22.684  1.00 8.40  ? 107 HIS A CA  1 
ATOM   847  C  C   . HIS A 1 107 ? 13.315  -8.093  22.668  1.00 9.01  ? 107 HIS A C   1 
ATOM   848  O  O   . HIS A 1 107 ? 12.958  -8.686  21.640  1.00 9.38  ? 107 HIS A O   1 
ATOM   849  C  CB  . HIS A 1 107 ? 12.391  -5.811  23.076  1.00 8.20  ? 107 HIS A CB  1 
ATOM   850  C  CG  . HIS A 1 107 ? 12.712  -4.359  23.223  1.00 8.05  ? 107 HIS A CG  1 
ATOM   851  N  ND1 . HIS A 1 107 ? 12.665  -3.467  22.178  1.00 8.48  ? 107 HIS A ND1 1 
ATOM   852  C  CD2 . HIS A 1 107 ? 13.142  -3.636  24.286  1.00 8.49  ? 107 HIS A CD2 1 
ATOM   853  C  CE1 . HIS A 1 107 ? 13.097  -2.262  22.580  1.00 9.40  ? 107 HIS A CE1 1 
ATOM   854  N  NE2 . HIS A 1 107 ? 13.396  -2.325  23.883  1.00 9.58  ? 107 HIS A NE2 1 
ATOM   855  N  N   . THR A 1 108 ? 13.391  -8.643  23.877  1.00 9.12  ? 108 THR A N   1 
ATOM   856  C  CA  . THR A 1 108 ? 12.987  -10.026 24.130  1.00 9.70  ? 108 THR A CA  1 
ATOM   857  C  C   . THR A 1 108 ? 12.050  -10.061 25.327  1.00 9.62  ? 108 THR A C   1 
ATOM   858  O  O   . THR A 1 108 ? 12.021  -9.124  26.113  1.00 10.09 ? 108 THR A O   1 
ATOM   859  C  CB  . THR A 1 108 ? 14.207  -10.929 24.330  1.00 10.30 ? 108 THR A CB  1 
ATOM   860  O  OG1 . THR A 1 108 ? 15.059  -10.466 25.391  1.00 10.79 ? 108 THR A OG1 1 
ATOM   861  C  CG2 . THR A 1 108 ? 15.032  -11.062 23.060  1.00 11.15 ? 108 THR A CG2 1 
ATOM   862  N  N   . VAL A 1 109 ? 11.271  -11.142 25.426  1.00 10.86 ? 109 VAL A N   1 
ATOM   863  C  CA  . VAL A 1 109 ? 10.329  -11.231 26.552  1.00 13.05 ? 109 VAL A CA  1 
ATOM   864  C  C   . VAL A 1 109 ? 10.661  -12.526 27.304  1.00 13.36 ? 109 VAL A C   1 
ATOM   865  O  O   . VAL A 1 109 ? 10.481  -13.607 26.742  1.00 13.88 ? 109 VAL A O   1 
ATOM   866  C  CB  . VAL A 1 109 ? 8.882   -11.200 26.039  1.00 13.05 ? 109 VAL A CB  1 
ATOM   867  C  CG1 . VAL A 1 109 ? 7.918   -11.408 27.215  1.00 15.02 ? 109 VAL A CG1 1 
ATOM   868  C  CG2 . VAL A 1 109 ? 8.571   -9.896  25.313  1.00 13.56 ? 109 VAL A CG2 1 
ATOM   869  N  N   . ASP A 1 110 ? 11.115  -12.398 28.544  1.00 14.68 ? 110 ASP A N   1 
ATOM   870  C  CA  . ASP A 1 110 ? 11.583  -13.585 29.266  1.00 14.97 ? 110 ASP A CA  1 
ATOM   871  C  C   . ASP A 1 110 ? 12.514  -14.399 28.355  1.00 14.24 ? 110 ASP A C   1 
ATOM   872  O  O   . ASP A 1 110 ? 12.432  -15.621 28.266  1.00 15.14 ? 110 ASP A O   1 
ATOM   873  C  CB  . ASP A 1 110 ? 10.376  -14.391 29.754  1.00 17.27 ? 110 ASP A CB  1 
ATOM   874  C  CG  . ASP A 1 110 ? 9.536   -13.596 30.758  1.00 16.09 ? 110 ASP A CG  1 
ATOM   875  O  OD1 . ASP A 1 110 ? 10.135  -12.795 31.491  1.00 18.37 ? 110 ASP A OD1 1 
ATOM   876  O  OD2 . ASP A 1 110 ? 8.289   -13.844 30.774  1.00 21.49 ? 110 ASP A OD2 1 
ATOM   877  N  N   . LYS A 1 111 ? 13.434  -13.705 27.689  1.00 13.56 ? 111 LYS A N   1 
ATOM   878  C  CA  . LYS A 1 111 ? 14.466  -14.197 26.761  1.00 13.64 ? 111 LYS A CA  1 
ATOM   879  C  C   . LYS A 1 111 ? 13.924  -14.721 25.421  1.00 14.52 ? 111 LYS A C   1 
ATOM   880  O  O   . LYS A 1 111 ? 14.705  -15.122 24.560  1.00 14.88 ? 111 LYS A O   1 
ATOM   881  C  CB  . LYS A 1 111 ? 15.388  -15.235 27.427  1.00 16.79 ? 111 LYS A CB  1 
ATOM   882  C  CG  . LYS A 1 111 ? 16.095  -14.720 28.684  1.00 18.76 ? 111 LYS A CG  1 
ATOM   883  C  CD  . LYS A 1 111 ? 17.086  -13.633 28.355  1.00 21.79 ? 111 LYS A CD  1 
ATOM   884  C  CE  . LYS A 1 111 ? 17.747  -13.055 29.587  1.00 27.37 ? 111 LYS A CE  1 
ATOM   885  N  NZ  . LYS A 1 111 ? 18.999  -13.802 29.816  1.00 33.83 ? 111 LYS A NZ  1 
ATOM   886  N  N   . LYS A 1 112 ? 12.604  -14.674 25.221  1.00 13.48 ? 112 LYS A N   1 
ATOM   887  C  CA  . LYS A 1 112 ? 12.002  -15.086 23.967  1.00 13.43 ? 112 LYS A CA  1 
ATOM   888  C  C   . LYS A 1 112 ? 12.310  -14.039 22.889  1.00 12.63 ? 112 LYS A C   1 
ATOM   889  O  O   . LYS A 1 112 ? 12.066  -12.835 23.081  1.00 12.74 ? 112 LYS A O   1 
ATOM   890  C  CB  . LYS A 1 112 ? 10.478  -15.200 24.053  1.00 14.74 ? 112 LYS A CB  1 
ATOM   891  C  CG  . LYS A 1 112 ? 9.841   -15.694 22.768  1.00 15.57 ? 112 LYS A CG  1 
ATOM   892  C  CD  . LYS A 1 112 ? 8.338   -15.633 22.923  1.00 18.25 ? 112 LYS A CD  1 
ATOM   893  C  CE  . LYS A 1 112 ? 7.631   -15.784 21.595  1.00 22.82 ? 112 LYS A CE  1 
ATOM   894  N  NZ  . LYS A 1 112 ? 7.888   -17.103 20.984  1.00 21.20 ? 112 LYS A NZ  1 
ATOM   895  N  N   A LYS A 1 113 ? 12.839  -14.525 21.754  0.50 11.90 ? 113 LYS A N   1 
ATOM   896  N  N   B LYS A 1 113 ? 12.841  -14.513 21.745  0.50 12.01 ? 113 LYS A N   1 
ATOM   897  C  CA  A LYS A 1 113 ? 13.038  -13.732 20.550  0.50 11.81 ? 113 LYS A CA  1 
ATOM   898  C  CA  B LYS A 1 113 ? 13.077  -13.698 20.558  0.50 12.05 ? 113 LYS A CA  1 
ATOM   899  C  C   A LYS A 1 113 ? 11.864  -13.948 19.616  0.50 11.54 ? 113 LYS A C   1 
ATOM   900  C  C   B LYS A 1 113 ? 11.981  -13.943 19.534  0.50 11.72 ? 113 LYS A C   1 
ATOM   901  O  O   A LYS A 1 113 ? 11.344  -15.055 19.468  0.50 11.72 ? 113 LYS A O   1 
ATOM   902  O  O   B LYS A 1 113 ? 11.661  -15.080 19.186  0.50 12.36 ? 113 LYS A O   1 
ATOM   903  C  CB  A LYS A 1 113 ? 14.334  -14.164 19.865  0.50 12.56 ? 113 LYS A CB  1 
ATOM   904  C  CB  B LYS A 1 113 ? 14.404  -14.086 19.902  0.50 12.90 ? 113 LYS A CB  1 
ATOM   905  C  CG  A LYS A 1 113 ? 15.572  -13.848 20.669  0.50 12.85 ? 113 LYS A CG  1 
ATOM   906  C  CG  B LYS A 1 113 ? 15.650  -13.667 20.651  0.50 13.41 ? 113 LYS A CG  1 
ATOM   907  C  CD  A LYS A 1 113 ? 16.811  -14.542 20.141  0.50 14.14 ? 113 LYS A CD  1 
ATOM   908  C  CD  B LYS A 1 113 ? 16.904  -14.210 19.971  0.50 15.30 ? 113 LYS A CD  1 
ATOM   909  C  CE  A LYS A 1 113 ? 18.005  -13.726 20.568  0.50 14.35 ? 113 LYS A CE  1 
ATOM   910  C  CE  B LYS A 1 113 ? 18.149  -13.744 20.682  0.50 15.95 ? 113 LYS A CE  1 
ATOM   911  N  NZ  A LYS A 1 113 ? 19.242  -14.532 20.652  0.50 16.13 ? 113 LYS A NZ  1 
ATOM   912  N  NZ  B LYS A 1 113 ? 18.428  -14.563 21.884  0.50 17.29 ? 113 LYS A NZ  1 
ATOM   913  N  N   . TYR A 1 114 ? 11.413  -12.851 19.020  1.00 11.45 ? 114 TYR A N   1 
ATOM   914  C  CA  . TYR A 1 114 ? 10.434  -12.917 17.960  1.00 9.78  ? 114 TYR A CA  1 
ATOM   915  C  C   . TYR A 1 114 ? 11.077  -12.841 16.578  1.00 10.44 ? 114 TYR A C   1 
ATOM   916  O  O   . TYR A 1 114 ? 12.270  -12.583 16.457  1.00 11.42 ? 114 TYR A O   1 
ATOM   917  C  CB  . TYR A 1 114 ? 9.365   -11.824 18.129  1.00 10.78 ? 114 TYR A CB  1 
ATOM   918  C  CG  . TYR A 1 114 ? 8.445   -12.049 19.292  1.00 11.40 ? 114 TYR A CG  1 
ATOM   919  C  CD1 . TYR A 1 114 ? 8.743   -11.628 20.583  1.00 12.26 ? 114 TYR A CD1 1 
ATOM   920  C  CD2 . TYR A 1 114 ? 7.257   -12.711 19.083  1.00 12.90 ? 114 TYR A CD2 1 
ATOM   921  C  CE1 . TYR A 1 114 ? 7.881   -11.805 21.643  1.00 12.93 ? 114 TYR A CE1 1 
ATOM   922  C  CE2 . TYR A 1 114 ? 6.378   -12.919 20.155  1.00 13.84 ? 114 TYR A CE2 1 
ATOM   923  C  CZ  . TYR A 1 114 ? 6.691   -12.453 21.421  1.00 14.20 ? 114 TYR A CZ  1 
ATOM   924  O  OH  . TYR A 1 114 ? 5.840   -12.578 22.514  1.00 18.82 ? 114 TYR A OH  1 
ATOM   925  N  N   . ALA A 1 115 ? 10.309  -13.079 15.513  1.00 11.12 ? 115 ALA A N   1 
ATOM   926  C  CA  . ALA A 1 115 ? 10.866  -13.077 14.157  1.00 10.61 ? 115 ALA A CA  1 
ATOM   927  C  C   . ALA A 1 115 ? 11.289  -11.695 13.671  1.00 10.85 ? 115 ALA A C   1 
ATOM   928  O  O   . ALA A 1 115 ? 12.135  -11.574 12.770  1.00 11.81 ? 115 ALA A O   1 
ATOM   929  C  CB  . ALA A 1 115 ? 9.885   -13.734 13.188  1.00 12.03 ? 115 ALA A CB  1 
ATOM   930  N  N   . ALA A 1 116 ? 10.625  -10.686 14.247  1.00 10.40 ? 116 ALA A N   1 
ATOM   931  C  CA  . ALA A 1 116 ? 10.877  -9.331  13.797  1.00 10.19 ? 116 ALA A CA  1 
ATOM   932  C  C   . ALA A 1 116 ? 10.333  -8.368  14.826  1.00 9.21  ? 116 ALA A C   1 
ATOM   933  O  O   . ALA A 1 116 ? 9.616   -8.779  15.722  1.00 9.82  ? 116 ALA A O   1 
ATOM   934  C  CB  . ALA A 1 116 ? 10.340  -9.037  12.403  1.00 11.94 ? 116 ALA A CB  1 
ATOM   935  N  N   . GLU A 1 117 ? 10.666  -7.084  14.675  1.00 8.91  ? 117 GLU A N   1 
ATOM   936  C  CA  . GLU A 1 117 ? 10.162  -6.041  15.548  1.00 9.31  ? 117 GLU A CA  1 
ATOM   937  C  C   . GLU A 1 117 ? 9.969   -4.782  14.711  1.00 9.57  ? 117 GLU A C   1 
ATOM   938  O  O   . GLU A 1 117 ? 10.853  -4.368  13.968  1.00 10.89 ? 117 GLU A O   1 
ATOM   939  C  CB  . GLU A 1 117 ? 11.120  -5.790  16.703  1.00 10.27 ? 117 GLU A CB  1 
ATOM   940  C  CG  . GLU A 1 117 ? 10.546  -4.939  17.842  1.00 10.40 ? 117 GLU A CG  1 
ATOM   941  C  CD  . GLU A 1 117 ? 11.470  -4.874  19.053  1.00 10.31 ? 117 GLU A CD  1 
ATOM   942  O  OE1 . GLU A 1 117 ? 12.115  -5.917  19.319  1.00 9.98  ? 117 GLU A OE1 1 
ATOM   943  O  OE2 . GLU A 1 117 ? 11.506  -3.809  19.719  1.00 10.21 ? 117 GLU A OE2 1 
ATOM   944  N  N   . LEU A 1 118 ? 8.760   -4.258  14.862  1.00 10.01 ? 118 LEU A N   1 
ATOM   945  C  CA  . LEU A 1 118 ? 8.333   -3.009  14.247  1.00 9.53  ? 118 LEU A CA  1 
ATOM   946  C  C   . LEU A 1 118 ? 8.541   -1.891  15.259  1.00 9.52  ? 118 LEU A C   1 
ATOM   947  O  O   . LEU A 1 118 ? 8.098   -1.965  16.397  1.00 9.73  ? 118 LEU A O   1 
ATOM   948  C  CB  . LEU A 1 118 ? 6.837   -3.160  13.886  1.00 9.53  ? 118 LEU A CB  1 
ATOM   949  C  CG  . LEU A 1 118 ? 6.022   -1.886  13.576  1.00 9.85  ? 118 LEU A CG  1 
ATOM   950  C  CD1 . LEU A 1 118 ? 6.540   -1.169  12.334  1.00 10.91 ? 118 LEU A CD1 1 
ATOM   951  C  CD2 . LEU A 1 118 ? 4.565   -2.303  13.323  1.00 11.30 ? 118 LEU A CD2 1 
ATOM   952  N  N   . HIS A 1 119 ? 9.125   -0.794  14.766  1.00 8.87  ? 119 HIS A N   1 
ATOM   953  C  CA  . HIS A 1 119 ? 9.365   0.421   15.539  1.00 9.12  ? 119 HIS A CA  1 
ATOM   954  C  C   . HIS A 1 119 ? 8.661   1.574   14.858  1.00 9.13  ? 119 HIS A C   1 
ATOM   955  O  O   . HIS A 1 119 ? 9.011   1.893   13.719  1.00 11.13 ? 119 HIS A O   1 
ATOM   956  C  CB  . HIS A 1 119 ? 10.877  0.687   15.629  1.00 8.67  ? 119 HIS A CB  1 
ATOM   957  C  CG  . HIS A 1 119 ? 11.525  -0.316  16.525  1.00 8.75  ? 119 HIS A CG  1 
ATOM   958  N  ND1 . HIS A 1 119 ? 12.882  -0.556  16.471  1.00 10.04 ? 119 HIS A ND1 1 
ATOM   959  C  CD2 . HIS A 1 119 ? 11.010  -1.139  17.465  1.00 9.31  ? 119 HIS A CD2 1 
ATOM   960  C  CE1 . HIS A 1 119 ? 13.183  -1.507  17.378  1.00 8.56  ? 119 HIS A CE1 1 
ATOM   961  N  NE2 . HIS A 1 119 ? 12.064  -1.850  17.989  1.00 9.00  ? 119 HIS A NE2 1 
ATOM   962  N  N   . LEU A 1 120 ? 7.688   2.190   15.590  1.00 9.37  ? 120 LEU A N   1 
ATOM   963  C  CA  . LEU A 1 120 ? 7.036   3.417   15.127  1.00 9.02  ? 120 LEU A CA  1 
ATOM   964  C  C   . LEU A 1 120 ? 7.670   4.558   15.915  1.00 9.72  ? 120 LEU A C   1 
ATOM   965  O  O   . LEU A 1 120 ? 7.576   4.595   17.128  1.00 8.75  ? 120 LEU A O   1 
ATOM   966  C  CB  . LEU A 1 120 ? 5.524   3.317   15.351  1.00 10.60 ? 120 LEU A CB  1 
ATOM   967  C  CG  . LEU A 1 120 ? 4.866   2.242   14.467  1.00 10.49 ? 120 LEU A CG  1 
ATOM   968  C  CD1 . LEU A 1 120 ? 4.136   1.250   15.355  1.00 13.03 ? 120 LEU A CD1 1 
ATOM   969  C  CD2 . LEU A 1 120 ? 3.893   2.896   13.465  1.00 13.45 ? 120 LEU A CD2 1 
ATOM   970  N  N   . VAL A 1 121 ? 8.364   5.442   15.202  1.00 10.00 ? 121 VAL A N   1 
ATOM   971  C  CA  . VAL A 1 121 ? 9.230   6.432   15.840  1.00 10.42 ? 121 VAL A CA  1 
ATOM   972  C  C   . VAL A 1 121 ? 8.514   7.764   15.864  1.00 10.59 ? 121 VAL A C   1 
ATOM   973  O  O   . VAL A 1 121 ? 8.124   8.248   14.792  1.00 11.20 ? 121 VAL A O   1 
ATOM   974  C  CB  . VAL A 1 121 ? 10.546  6.539   15.050  1.00 11.35 ? 121 VAL A CB  1 
ATOM   975  C  CG1 . VAL A 1 121 ? 11.479  7.612   15.641  1.00 11.85 ? 121 VAL A CG1 1 
ATOM   976  C  CG2 . VAL A 1 121 ? 11.221  5.185   14.832  1.00 11.55 ? 121 VAL A CG2 1 
ATOM   977  N  N   . HIS A 1 122 ? 8.453   8.381   17.052  1.00 9.14  ? 122 HIS A N   1 
ATOM   978  C  CA  . HIS A 1 122 ? 7.777   9.650   17.243  1.00 9.67  ? 122 HIS A CA  1 
ATOM   979  C  C   . HIS A 1 122 ? 8.672   10.608  18.013  1.00 10.01 ? 122 HIS A C   1 
ATOM   980  O  O   . HIS A 1 122 ? 9.425   10.206  18.875  1.00 11.03 ? 122 HIS A O   1 
ATOM   981  C  CB  . HIS A 1 122 ? 6.511   9.445   18.123  1.00 10.51 ? 122 HIS A CB  1 
ATOM   982  C  CG  . HIS A 1 122 ? 5.611   8.326   17.717  1.00 10.01 ? 122 HIS A CG  1 
ATOM   983  N  ND1 . HIS A 1 122 ? 5.926   6.996   18.013  1.00 10.99 ? 122 HIS A ND1 1 
ATOM   984  C  CD2 . HIS A 1 122 ? 4.384   8.306   17.115  1.00 10.46 ? 122 HIS A CD2 1 
ATOM   985  C  CE1 . HIS A 1 122 ? 4.938   6.206   17.588  1.00 11.26 ? 122 HIS A CE1 1 
ATOM   986  N  NE2 . HIS A 1 122 ? 3.971   6.990   16.995  1.00 11.58 ? 122 HIS A NE2 1 
ATOM   987  N  N   . TRP A 1 123 ? 8.561   11.894  17.680  1.00 10.11 ? 123 TRP A N   1 
ATOM   988  C  CA  . TRP A 1 123 ? 9.371   12.907  18.374  1.00 10.31 ? 123 TRP A CA  1 
ATOM   989  C  C   . TRP A 1 123 ? 8.489   13.873  19.152  1.00 11.59 ? 123 TRP A C   1 
ATOM   990  O  O   . TRP A 1 123 ? 7.375   14.213  18.714  1.00 11.47 ? 123 TRP A O   1 
ATOM   991  C  CB  . TRP A 1 123 ? 10.335  13.632  17.404  1.00 12.06 ? 123 TRP A CB  1 
ATOM   992  C  CG  . TRP A 1 123 ? 9.669   14.262  16.220  1.00 12.90 ? 123 TRP A CG  1 
ATOM   993  C  CD1 . TRP A 1 123 ? 9.444   13.647  15.028  1.00 12.78 ? 123 TRP A CD1 1 
ATOM   994  C  CD2 . TRP A 1 123 ? 9.191   15.609  16.068  1.00 14.31 ? 123 TRP A CD2 1 
ATOM   995  N  NE1 . TRP A 1 123 ? 8.877   14.500  14.139  1.00 14.93 ? 123 TRP A NE1 1 
ATOM   996  C  CE2 . TRP A 1 123 ? 8.677   15.710  14.751  1.00 15.89 ? 123 TRP A CE2 1 
ATOM   997  C  CE3 . TRP A 1 123 ? 9.165   16.724  16.915  1.00 15.01 ? 123 TRP A CE3 1 
ATOM   998  C  CZ2 . TRP A 1 123 ? 8.099   16.883  14.265  1.00 17.27 ? 123 TRP A CZ2 1 
ATOM   999  C  CZ3 . TRP A 1 123 ? 8.596   17.879  16.423  1.00 17.01 ? 123 TRP A CZ3 1 
ATOM   1000 C  CH2 . TRP A 1 123 ? 8.098   17.970  15.119  1.00 18.78 ? 123 TRP A CH2 1 
ATOM   1001 N  N   . ASN A 1 124 ? 9.047   14.301  20.290  1.00 11.44 ? 124 ASN A N   1 
ATOM   1002 C  CA  . ASN A 1 124 ? 8.381   15.216  21.211  1.00 12.67 ? 124 ASN A CA  1 
ATOM   1003 C  C   . ASN A 1 124 ? 8.221   16.590  20.541  1.00 13.54 ? 124 ASN A C   1 
ATOM   1004 O  O   . ASN A 1 124 ? 9.225   17.283  20.250  1.00 13.77 ? 124 ASN A O   1 
ATOM   1005 C  CB  . ASN A 1 124 ? 9.208   15.237  22.492  1.00 12.12 ? 124 ASN A CB  1 
ATOM   1006 C  CG  . ASN A 1 124 ? 8.477   15.887  23.645  1.00 15.56 ? 124 ASN A CG  1 
ATOM   1007 O  OD1 . ASN A 1 124 ? 7.637   16.758  23.412  1.00 16.48 ? 124 ASN A OD1 1 
ATOM   1008 N  ND2 . ASN A 1 124 ? 8.811   15.456  24.857  1.00 16.01 ? 124 ASN A ND2 1 
ATOM   1009 N  N   . THR A 1 125 ? 6.965   17.038  20.341  1.00 16.17 ? 125 THR A N   1 
ATOM   1010 C  CA  . THR A 1 125 ? 6.755   18.257  19.540  1.00 15.53 ? 125 THR A CA  1 
ATOM   1011 C  C   . THR A 1 125 ? 7.257   19.440  20.387  1.00 17.45 ? 125 THR A C   1 
ATOM   1012 O  O   . THR A 1 125 ? 7.380   20.554  19.820  1.00 17.03 ? 125 THR A O   1 
ATOM   1013 C  CB  . THR A 1 125 ? 5.260   18.421  19.207  1.00 17.72 ? 125 THR A CB  1 
ATOM   1014 O  OG1 . THR A 1 125 ? 4.474   18.509  20.393  1.00 22.18 ? 125 THR A OG1 1 
ATOM   1015 C  CG2 . THR A 1 125 ? 4.763   17.344  18.262  1.00 20.39 ? 125 THR A CG2 1 
ATOM   1016 N  N   . LYS A 1 126 ? 7.509   19.342  21.759  1.00 15.17 ? 126 LYS A N   1 
ATOM   1017 C  CA  . LYS A 1 126 ? 8.041   20.535  22.450  1.00 15.06 ? 126 LYS A CA  1 
ATOM   1018 C  C   . LYS A 1 126 ? 9.413   20.943  21.923  1.00 15.95 ? 126 LYS A C   1 
ATOM   1019 O  O   . LYS A 1 126 ? 9.874   22.051  22.235  1.00 18.50 ? 126 LYS A O   1 
ATOM   1020 C  CB  . LYS A 1 126 ? 8.051   20.272  23.948  1.00 18.23 ? 126 LYS A CB  1 
ATOM   1021 C  CG  . LYS A 1 126 ? 9.086   19.327  24.513  1.00 20.80 ? 126 LYS A CG  1 
ATOM   1022 C  CD  . LYS A 1 126 ? 8.749   19.264  25.994  1.00 26.97 ? 126 LYS A CD  1 
ATOM   1023 C  CE  . LYS A 1 126 ? 9.785   18.569  26.826  1.00 33.45 ? 126 LYS A CE  1 
ATOM   1024 N  NZ  . LYS A 1 126 ? 10.045  19.350  28.063  1.00 41.95 ? 126 LYS A NZ  1 
ATOM   1025 N  N   . TYR A 1 127 ? 10.091  20.074  21.161  1.00 14.40 ? 127 TYR A N   1 
ATOM   1026 C  CA  . TYR A 1 127 ? 11.432  20.356  20.670  1.00 15.15 ? 127 TYR A CA  1 
ATOM   1027 C  C   . TYR A 1 127 ? 11.422  20.795  19.213  1.00 14.79 ? 127 TYR A C   1 
ATOM   1028 O  O   . TYR A 1 127 ? 12.502  21.076  18.655  1.00 16.00 ? 127 TYR A O   1 
ATOM   1029 C  CB  . TYR A 1 127 ? 12.396  19.179  20.843  1.00 15.18 ? 127 TYR A CB  1 
ATOM   1030 C  CG  . TYR A 1 127 ? 12.535  18.845  22.297  1.00 16.66 ? 127 TYR A CG  1 
ATOM   1031 C  CD1 . TYR A 1 127 ? 12.937  19.804  23.220  1.00 17.66 ? 127 TYR A CD1 1 
ATOM   1032 C  CD2 . TYR A 1 127 ? 12.279  17.568  22.787  1.00 15.26 ? 127 TYR A CD2 1 
ATOM   1033 C  CE1 . TYR A 1 127 ? 13.060  19.498  24.567  1.00 17.35 ? 127 TYR A CE1 1 
ATOM   1034 C  CE2 . TYR A 1 127 ? 12.381  17.247  24.132  1.00 16.54 ? 127 TYR A CE2 1 
ATOM   1035 C  CZ  . TYR A 1 127 ? 12.774  18.234  25.035  1.00 18.14 ? 127 TYR A CZ  1 
ATOM   1036 O  OH  . TYR A 1 127 ? 12.942  17.965  26.355  1.00 19.01 ? 127 TYR A OH  1 
ATOM   1037 N  N   . GLY A 1 128 ? 10.229  20.941  18.627  1.00 15.27 ? 128 GLY A N   1 
ATOM   1038 C  CA  . GLY A 1 128 ? 10.181  21.666  17.353  1.00 15.01 ? 128 GLY A CA  1 
ATOM   1039 C  C   . GLY A 1 128 ? 10.437  20.823  16.109  1.00 17.99 ? 128 GLY A C   1 
ATOM   1040 O  O   . GLY A 1 128 ? 9.720   20.971  15.103  1.00 18.17 ? 128 GLY A O   1 
ATOM   1041 N  N   . ASP A 1 129 ? 11.519  20.030  16.126  1.00 17.71 ? 129 ASP A N   1 
ATOM   1042 C  CA  . ASP A 1 129 ? 11.620  19.030  15.083  1.00 18.88 ? 129 ASP A CA  1 
ATOM   1043 C  C   . ASP A 1 129 ? 12.419  17.850  15.584  1.00 18.02 ? 129 ASP A C   1 
ATOM   1044 O  O   . ASP A 1 129 ? 12.901  17.833  16.727  1.00 18.24 ? 129 ASP A O   1 
ATOM   1045 C  CB  . ASP A 1 129 ? 12.196  19.583  13.782  1.00 21.65 ? 129 ASP A CB  1 
ATOM   1046 C  CG  . ASP A 1 129 ? 13.589  20.134  13.966  1.00 19.14 ? 129 ASP A CG  1 
ATOM   1047 O  OD1 . ASP A 1 129 ? 14.237  19.871  15.014  1.00 22.61 ? 129 ASP A OD1 1 
ATOM   1048 O  OD2 . ASP A 1 129 ? 14.071  20.775  13.035  1.00 25.26 ? 129 ASP A OD2 1 
ATOM   1049 N  N   . TYR A 1 130 ? 12.553  16.884  14.676  1.00 17.43 ? 130 TYR A N   1 
ATOM   1050 C  CA  . TYR A 1 130 ? 13.174  15.627  15.042  1.00 18.26 ? 130 TYR A CA  1 
ATOM   1051 C  C   . TYR A 1 130 ? 14.653  15.830  15.398  1.00 15.83 ? 130 TYR A C   1 
ATOM   1052 O  O   . TYR A 1 130 ? 15.195  15.265  16.359  1.00 14.87 ? 130 TYR A O   1 
ATOM   1053 C  CB  . TYR A 1 130 ? 12.977  14.615  13.900  1.00 17.94 ? 130 TYR A CB  1 
ATOM   1054 C  CG  . TYR A 1 130 ? 13.884  13.418  14.030  1.00 20.06 ? 130 TYR A CG  1 
ATOM   1055 C  CD1 . TYR A 1 130 ? 13.516  12.291  14.752  1.00 18.60 ? 130 TYR A CD1 1 
ATOM   1056 C  CD2 . TYR A 1 130 ? 15.166  13.447  13.500  1.00 21.48 ? 130 TYR A CD2 1 
ATOM   1057 C  CE1 . TYR A 1 130 ? 14.396  11.230  14.891  1.00 18.70 ? 130 TYR A CE1 1 
ATOM   1058 C  CE2 . TYR A 1 130 ? 16.066  12.399  13.657  1.00 21.79 ? 130 TYR A CE2 1 
ATOM   1059 C  CZ  . TYR A 1 130 ? 15.648  11.248  14.304  1.00 21.14 ? 130 TYR A CZ  1 
ATOM   1060 O  OH  . TYR A 1 130 ? 16.568  10.251  14.490  1.00 24.76 ? 130 TYR A OH  1 
ATOM   1061 N  N   . GLY A 1 131 ? 15.364  16.657  14.612  1.00 16.18 ? 131 GLY A N   1 
ATOM   1062 C  CA  . GLY A 1 131 ? 16.784  16.787  14.861  1.00 17.96 ? 131 GLY A CA  1 
ATOM   1063 C  C   . GLY A 1 131 ? 17.131  17.407  16.212  1.00 15.92 ? 131 GLY A C   1 
ATOM   1064 O  O   . GLY A 1 131 ? 18.184  17.082  16.775  1.00 19.80 ? 131 GLY A O   1 
ATOM   1065 N  N   . LYS A 1 132 ? 16.287  18.308  16.712  1.00 15.72 ? 132 LYS A N   1 
ATOM   1066 C  CA  . LYS A 1 132 ? 16.451  18.849  18.057  1.00 17.05 ? 132 LYS A CA  1 
ATOM   1067 C  C   . LYS A 1 132 ? 16.010  17.796  19.092  1.00 15.51 ? 132 LYS A C   1 
ATOM   1068 O  O   . LYS A 1 132 ? 16.641  17.634  20.134  1.00 18.43 ? 132 LYS A O   1 
ATOM   1069 C  CB  . LYS A 1 132 ? 15.628  20.129  18.217  1.00 18.96 ? 132 LYS A CB  1 
ATOM   1070 C  CG  . LYS A 1 132 ? 16.233  21.475  17.822  1.00 24.70 ? 132 LYS A CG  1 
ATOM   1071 C  CD  . LYS A 1 132 ? 17.170  21.542  16.654  1.00 34.27 ? 132 LYS A CD  1 
ATOM   1072 C  CE  . LYS A 1 132 ? 17.948  22.842  16.768  1.00 33.52 ? 132 LYS A CE  1 
ATOM   1073 N  NZ  . LYS A 1 132 ? 17.875  23.369  18.161  1.00 38.31 ? 132 LYS A NZ  1 
ATOM   1074 N  N   . ALA A 1 133 ? 14.897  17.095  18.837  1.00 14.61 ? 133 ALA A N   1 
ATOM   1075 C  CA  . ALA A 1 133 ? 14.363  16.134  19.783  1.00 13.81 ? 133 ALA A CA  1 
ATOM   1076 C  C   . ALA A 1 133 ? 15.360  15.015  20.064  1.00 14.58 ? 133 ALA A C   1 
ATOM   1077 O  O   . ALA A 1 133 ? 15.469  14.593  21.210  1.00 14.23 ? 133 ALA A O   1 
ATOM   1078 C  CB  . ALA A 1 133 ? 13.072  15.562  19.209  1.00 14.05 ? 133 ALA A CB  1 
ATOM   1079 N  N   . VAL A 1 134 ? 16.152  14.598  19.068  1.00 15.60 ? 134 VAL A N   1 
ATOM   1080 C  CA  . VAL A 1 134 ? 17.056  13.464  19.296  1.00 17.99 ? 134 VAL A CA  1 
ATOM   1081 C  C   . VAL A 1 134 ? 18.233  13.877  20.174  1.00 19.49 ? 134 VAL A C   1 
ATOM   1082 O  O   . VAL A 1 134 ? 18.976  13.001  20.621  1.00 26.87 ? 134 VAL A O   1 
ATOM   1083 C  CB  . VAL A 1 134 ? 17.555  12.722  18.033  1.00 20.94 ? 134 VAL A CB  1 
ATOM   1084 C  CG1 . VAL A 1 134 ? 16.418  12.121  17.313  1.00 21.30 ? 134 VAL A CG1 1 
ATOM   1085 C  CG2 . VAL A 1 134 ? 18.418  13.588  17.105  1.00 21.36 ? 134 VAL A CG2 1 
ATOM   1086 N  N   . GLN A 1 135 ? 18.347  15.150  20.514  1.00 19.45 ? 135 GLN A N   1 
ATOM   1087 C  CA  . GLN A 1 135 ? 19.419  15.615  21.371  1.00 25.62 ? 135 GLN A CA  1 
ATOM   1088 C  C   . GLN A 1 135 ? 18.911  15.650  22.808  1.00 23.54 ? 135 GLN A C   1 
ATOM   1089 O  O   . GLN A 1 135 ? 19.549  16.194  23.713  1.00 27.94 ? 135 GLN A O   1 
ATOM   1090 C  CB  . GLN A 1 135 ? 19.889  16.982  20.863  1.00 28.92 ? 135 GLN A CB  1 
ATOM   1091 C  CG  . GLN A 1 135 ? 20.468  16.895  19.454  1.00 33.75 ? 135 GLN A CG  1 
ATOM   1092 C  CD  . GLN A 1 135 ? 20.831  18.259  18.919  1.00 34.10 ? 135 GLN A CD  1 
ATOM   1093 O  OE1 . GLN A 1 135 ? 20.437  18.634  17.818  1.00 35.89 ? 135 GLN A OE1 1 
ATOM   1094 N  NE2 . GLN A 1 135 ? 21.525  19.038  19.734  1.00 35.42 ? 135 GLN A NE2 1 
ATOM   1095 N  N   . GLN A 1 136 ? 17.671  15.173  23.027  1.00 18.20 ? 136 GLN A N   1 
ATOM   1096 C  CA  . GLN A 1 136 ? 17.133  15.440  24.341  1.00 16.73 ? 136 GLN A CA  1 
ATOM   1097 C  C   . GLN A 1 136 ? 16.828  14.130  25.033  1.00 16.46 ? 136 GLN A C   1 
ATOM   1098 O  O   . GLN A 1 136 ? 16.452  13.139  24.417  1.00 15.01 ? 136 GLN A O   1 
ATOM   1099 C  CB  . GLN A 1 136 ? 15.795  16.173  24.275  1.00 16.84 ? 136 GLN A CB  1 
ATOM   1100 C  CG  . GLN A 1 136 ? 15.830  17.459  23.439  1.00 19.95 ? 136 GLN A CG  1 
ATOM   1101 C  CD  . GLN A 1 136 ? 16.945  18.387  23.860  1.00 22.95 ? 136 GLN A CD  1 
ATOM   1102 O  OE1 . GLN A 1 136 ? 17.126  18.662  25.050  1.00 22.50 ? 136 GLN A OE1 1 
ATOM   1103 N  NE2 . GLN A 1 136 ? 17.664  18.911  22.881  1.00 30.24 ? 136 GLN A NE2 1 
ATOM   1104 N  N   . PRO A 1 137 ? 16.826  14.084  26.375  1.00 16.59 ? 137 PRO A N   1 
ATOM   1105 C  CA  . PRO A 1 137 ? 16.661  12.807  27.045  1.00 15.80 ? 137 PRO A CA  1 
ATOM   1106 C  C   . PRO A 1 137 ? 15.250  12.243  26.917  1.00 15.37 ? 137 PRO A C   1 
ATOM   1107 O  O   . PRO A 1 137 ? 15.094  11.018  27.027  1.00 16.16 ? 137 PRO A O   1 
ATOM   1108 C  CB  . PRO A 1 137 ? 17.050  13.121  28.504  1.00 18.26 ? 137 PRO A CB  1 
ATOM   1109 C  CG  . PRO A 1 137 ? 16.769  14.587  28.653  1.00 24.53 ? 137 PRO A CG  1 
ATOM   1110 C  CD  . PRO A 1 137 ? 17.070  15.212  27.311  1.00 19.40 ? 137 PRO A CD  1 
ATOM   1111 N  N   . ASP A 1 138 ? 14.255  13.122  26.638  1.00 13.51 ? 138 ASP A N   1 
ATOM   1112 C  CA  . ASP A 1 138 ? 12.878  12.682  26.390  1.00 13.61 ? 138 ASP A CA  1 
ATOM   1113 C  C   . ASP A 1 138 ? 12.411  13.085  24.995  1.00 12.15 ? 138 ASP A C   1 
ATOM   1114 O  O   . ASP A 1 138 ? 11.284  13.492  24.757  1.00 13.50 ? 138 ASP A O   1 
ATOM   1115 C  CB  . ASP A 1 138 ? 11.889  13.317  27.384  1.00 14.70 ? 138 ASP A CB  1 
ATOM   1116 C  CG  . ASP A 1 138 ? 11.949  14.830  27.423  1.00 14.80 ? 138 ASP A CG  1 
ATOM   1117 O  OD1 . ASP A 1 138 ? 12.911  15.406  26.889  1.00 16.79 ? 138 ASP A OD1 1 
ATOM   1118 O  OD2 . ASP A 1 138 ? 11.086  15.401  28.114  1.00 18.62 ? 138 ASP A OD2 1 
ATOM   1119 N  N   . GLY A 1 139 ? 13.327  12.990  24.044  1.00 11.88 ? 139 GLY A N   1 
ATOM   1120 C  CA  . GLY A 1 139 ? 13.058  13.440  22.685  1.00 11.91 ? 139 GLY A CA  1 
ATOM   1121 C  C   . GLY A 1 139 ? 12.178  12.517  21.843  1.00 10.24 ? 139 GLY A C   1 
ATOM   1122 O  O   . GLY A 1 139 ? 11.475  13.039  20.975  1.00 10.98 ? 139 GLY A O   1 
ATOM   1123 N  N   . LEU A 1 140 ? 12.333  11.198  22.018  1.00 9.65  ? 140 LEU A N   1 
ATOM   1124 C  CA  . LEU A 1 140 ? 11.626  10.266  21.157  1.00 10.42 ? 140 LEU A CA  1 
ATOM   1125 C  C   . LEU A 1 140 ? 10.760  9.373   22.020  1.00 10.82 ? 140 LEU A C   1 
ATOM   1126 O  O   . LEU A 1 140 ? 11.093  9.093   23.180  1.00 10.47 ? 140 LEU A O   1 
ATOM   1127 C  CB  . LEU A 1 140 ? 12.627  9.400   20.378  1.00 11.77 ? 140 LEU A CB  1 
ATOM   1128 C  CG  . LEU A 1 140 ? 13.544  10.133  19.402  1.00 13.18 ? 140 LEU A CG  1 
ATOM   1129 C  CD1 . LEU A 1 140 ? 14.282  9.115   18.511  1.00 15.51 ? 140 LEU A CD1 1 
ATOM   1130 C  CD2 . LEU A 1 140 ? 12.846  11.172  18.513  1.00 15.12 ? 140 LEU A CD2 1 
ATOM   1131 N  N   . ALA A 1 141 ? 9.681   8.900   21.378  1.00 10.23 ? 141 ALA A N   1 
ATOM   1132 C  CA  . ALA A 1 141 ? 8.948   7.774   21.908  1.00 9.52  ? 141 ALA A CA  1 
ATOM   1133 C  C   . ALA A 1 141 ? 8.847   6.768   20.782  1.00 8.85  ? 141 ALA A C   1 
ATOM   1134 O  O   . ALA A 1 141 ? 8.443   7.114   19.675  1.00 9.85  ? 141 ALA A O   1 
ATOM   1135 C  CB  . ALA A 1 141 ? 7.592   8.207   22.396  1.00 10.84 ? 141 ALA A CB  1 
ATOM   1136 N  N   . VAL A 1 142 ? 9.372   5.545   21.022  1.00 9.05  ? 142 VAL A N   1 
ATOM   1137 C  CA  . VAL A 1 142 ? 9.297   4.510   20.010  1.00 9.13  ? 142 VAL A CA  1 
ATOM   1138 C  C   . VAL A 1 142 ? 8.339   3.438   20.507  1.00 8.85  ? 142 VAL A C   1 
ATOM   1139 O  O   . VAL A 1 142 ? 8.451   2.901   21.623  1.00 9.53  ? 142 VAL A O   1 
ATOM   1140 C  CB  . VAL A 1 142 ? 10.675  3.918   19.643  1.00 8.71  ? 142 VAL A CB  1 
ATOM   1141 C  CG1 . VAL A 1 142 ? 10.525  2.887   18.509  1.00 10.58 ? 142 VAL A CG1 1 
ATOM   1142 C  CG2 . VAL A 1 142 ? 11.604  5.027   19.202  1.00 10.89 ? 142 VAL A CG2 1 
ATOM   1143 N  N   . LEU A 1 143 ? 7.314   3.196   19.673  1.00 8.79  ? 143 LEU A N   1 
ATOM   1144 C  CA  . LEU A 1 143 ? 6.349   2.152   19.917  1.00 9.45  ? 143 LEU A CA  1 
ATOM   1145 C  C   . LEU A 1 143 ? 6.877   0.890   19.228  1.00 9.83  ? 143 LEU A C   1 
ATOM   1146 O  O   . LEU A 1 143 ? 6.997   0.817   18.007  1.00 10.43 ? 143 LEU A O   1 
ATOM   1147 C  CB  . LEU A 1 143 ? 4.985   2.613   19.384  1.00 11.74 ? 143 LEU A CB  1 
ATOM   1148 C  CG  . LEU A 1 143 ? 3.800   1.657   19.551  1.00 13.09 ? 143 LEU A CG  1 
ATOM   1149 C  CD1 . LEU A 1 143 ? 3.581   1.298   20.998  1.00 13.31 ? 143 LEU A CD1 1 
ATOM   1150 C  CD2 . LEU A 1 143 ? 2.502   2.288   18.993  1.00 13.21 ? 143 LEU A CD2 1 
ATOM   1151 N  N   . GLY A 1 144 ? 7.089   -0.147  20.050  1.00 8.99  ? 144 GLY A N   1 
ATOM   1152 C  CA  . GLY A 1 144 ? 7.669   -1.394  19.568  1.00 9.21  ? 144 GLY A CA  1 
ATOM   1153 C  C   . GLY A 1 144 ? 6.640   -2.519  19.537  1.00 8.89  ? 144 GLY A C   1 
ATOM   1154 O  O   . GLY A 1 144 ? 5.890   -2.644  20.505  1.00 10.46 ? 144 GLY A O   1 
ATOM   1155 N  N   . ILE A 1 145 ? 6.580   -3.248  18.412  1.00 8.98  ? 145 ILE A N   1 
ATOM   1156 C  CA  . ILE A 1 145 ? 5.560   -4.287  18.266  1.00 9.32  ? 145 ILE A CA  1 
ATOM   1157 C  C   . ILE A 1 145 ? 6.288   -5.502  17.717  1.00 9.60  ? 145 ILE A C   1 
ATOM   1158 O  O   . ILE A 1 145 ? 6.962   -5.454  16.690  1.00 10.35 ? 145 ILE A O   1 
ATOM   1159 C  CB  . ILE A 1 145 ? 4.423   -3.793  17.326  1.00 9.42  ? 145 ILE A CB  1 
ATOM   1160 C  CG1 . ILE A 1 145 ? 3.754   -2.544  17.851  1.00 12.54 ? 145 ILE A CG1 1 
ATOM   1161 C  CG2 . ILE A 1 145 ? 3.411   -4.890  17.038  1.00 12.34 ? 145 ILE A CG2 1 
ATOM   1162 C  CD1 . ILE A 1 145 ? 2.741   -1.939  16.895  1.00 11.75 ? 145 ILE A CD1 1 
ATOM   1163 N  N   . PHE A 1 146 ? 6.090   -6.624  18.402  1.00 10.03 ? 146 PHE A N   1 
ATOM   1164 C  CA  . PHE A 1 146 ? 6.728   -7.860  17.977  1.00 10.17 ? 146 PHE A CA  1 
ATOM   1165 C  C   . PHE A 1 146 ? 5.965   -8.492  16.810  1.00 10.20 ? 146 PHE A C   1 
ATOM   1166 O  O   . PHE A 1 146 ? 4.731   -8.415  16.767  1.00 10.83 ? 146 PHE A O   1 
ATOM   1167 C  CB  . PHE A 1 146 ? 6.717   -8.822  19.149  1.00 10.21 ? 146 PHE A CB  1 
ATOM   1168 C  CG  . PHE A 1 146 ? 7.572   -8.374  20.298  1.00 8.77  ? 146 PHE A CG  1 
ATOM   1169 C  CD1 . PHE A 1 146 ? 8.936   -8.245  20.116  1.00 9.46  ? 146 PHE A CD1 1 
ATOM   1170 C  CD2 . PHE A 1 146 ? 7.034   -8.145  21.540  1.00 10.53 ? 146 PHE A CD2 1 
ATOM   1171 C  CE1 . PHE A 1 146 ? 9.732   -7.816  21.163  1.00 9.60  ? 146 PHE A CE1 1 
ATOM   1172 C  CE2 . PHE A 1 146 ? 7.819   -7.744  22.611  1.00 9.11  ? 146 PHE A CE2 1 
ATOM   1173 C  CZ  . PHE A 1 146 ? 9.195   -7.588  22.427  1.00 8.92  ? 146 PHE A CZ  1 
ATOM   1174 N  N   . LEU A 1 147 ? 6.675   -9.161  15.918  1.00 10.91 ? 147 LEU A N   1 
ATOM   1175 C  CA  . LEU A 1 147 ? 6.045   -9.969  14.862  1.00 10.12 ? 147 LEU A CA  1 
ATOM   1176 C  C   . LEU A 1 147 ? 6.390   -11.423 15.141  1.00 10.32 ? 147 LEU A C   1 
ATOM   1177 O  O   . LEU A 1 147 ? 7.553   -11.789 15.254  1.00 11.20 ? 147 LEU A O   1 
ATOM   1178 C  CB  . LEU A 1 147 ? 6.639   -9.562  13.494  1.00 10.98 ? 147 LEU A CB  1 
ATOM   1179 C  CG  . LEU A 1 147 ? 6.083   -8.303  12.849  1.00 9.73  ? 147 LEU A CG  1 
ATOM   1180 C  CD1 . LEU A 1 147 ? 6.321   -7.062  13.741  1.00 12.10 ? 147 LEU A CD1 1 
ATOM   1181 C  CD2 . LEU A 1 147 ? 6.707   -8.109  11.463  1.00 11.70 ? 147 LEU A CD2 1 
ATOM   1182 N  N   . LYS A 1 148 ? 5.353   -12.266 15.107  1.00 12.19 ? 148 LYS A N   1 
ATOM   1183 C  CA  . LYS A 1 148 ? 5.525   -13.713 15.090  1.00 11.92 ? 148 LYS A CA  1 
ATOM   1184 C  C   . LYS A 1 148 ? 5.061   -14.246 13.744  1.00 13.98 ? 148 LYS A C   1 
ATOM   1185 O  O   . LYS A 1 148 ? 4.237   -13.631 13.069  1.00 13.92 ? 148 LYS A O   1 
ATOM   1186 C  CB  . LYS A 1 148 ? 4.778   -14.354 16.268  1.00 14.26 ? 148 LYS A CB  1 
ATOM   1187 C  CG  . LYS A 1 148 ? 3.256   -14.338 16.217  1.00 16.33 ? 148 LYS A CG  1 
ATOM   1188 C  CD  . LYS A 1 148 ? 2.685   -15.017 17.477  1.00 22.13 ? 148 LYS A CD  1 
ATOM   1189 C  CE  . LYS A 1 148 ? 1.516   -15.937 17.202  1.00 30.40 ? 148 LYS A CE  1 
ATOM   1190 N  N   . VAL A 1 149 ? 5.590   -15.395 13.339  1.00 13.53 ? 149 VAL A N   1 
ATOM   1191 C  CA  . VAL A 1 149 ? 5.188   -16.030 12.100  1.00 13.86 ? 149 VAL A CA  1 
ATOM   1192 C  C   . VAL A 1 149 ? 3.966   -16.919 12.340  1.00 14.23 ? 149 VAL A C   1 
ATOM   1193 O  O   . VAL A 1 149 ? 3.993   -17.846 13.157  1.00 15.95 ? 149 VAL A O   1 
ATOM   1194 C  CB  . VAL A 1 149 ? 6.346   -16.780 11.432  1.00 14.18 ? 149 VAL A CB  1 
ATOM   1195 C  CG1 . VAL A 1 149 ? 5.912   -17.538 10.184  1.00 17.14 ? 149 VAL A CG1 1 
ATOM   1196 C  CG2 . VAL A 1 149 ? 7.442   -15.800 11.092  1.00 14.63 ? 149 VAL A CG2 1 
ATOM   1197 N  N   . GLY A 1 150 ? 2.935   -16.665 11.544  1.00 13.86 ? 150 GLY A N   1 
ATOM   1198 C  CA  . GLY A 1 150 ? 1.685   -17.420 11.606  1.00 13.71 ? 150 GLY A CA  1 
ATOM   1199 C  C   . GLY A 1 150 ? 0.794   -17.020 10.447  1.00 13.35 ? 150 GLY A C   1 
ATOM   1200 O  O   . GLY A 1 150 ? 1.214   -17.171 9.310   1.00 14.80 ? 150 GLY A O   1 
ATOM   1201 N  N   A SER A 1 151 ? -0.404  -16.482 10.756  0.50 14.64 ? 151 SER A N   1 
ATOM   1202 N  N   B SER A 1 151 ? -0.389  -16.469 10.764  0.50 15.22 ? 151 SER A N   1 
ATOM   1203 C  CA  A SER A 1 151 ? -1.296  -15.928 9.737   0.50 15.64 ? 151 SER A CA  1 
ATOM   1204 C  CA  B SER A 1 151 ? -1.270  -15.904 9.747   0.50 16.57 ? 151 SER A CA  1 
ATOM   1205 C  C   A SER A 1 151 ? -0.719  -14.631 9.164   0.50 16.89 ? 151 SER A C   1 
ATOM   1206 C  C   B SER A 1 151 ? -0.664  -14.635 9.142   0.50 17.56 ? 151 SER A C   1 
ATOM   1207 O  O   A SER A 1 151 ? 0.033   -13.928 9.846   0.50 16.64 ? 151 SER A O   1 
ATOM   1208 O  O   B SER A 1 151 ? 0.169   -13.965 9.761   0.50 16.99 ? 151 SER A O   1 
ATOM   1209 C  CB  A SER A 1 151 ? -2.669  -15.709 10.278  0.50 17.97 ? 151 SER A CB  1 
ATOM   1210 C  CB  B SER A 1 151 ? -2.633  -15.677 10.303  0.50 19.74 ? 151 SER A CB  1 
ATOM   1211 O  OG  A SER A 1 151 ? -2.660  -14.674 11.244  0.50 17.75 ? 151 SER A OG  1 
ATOM   1212 O  OG  B SER A 1 151 ? -3.132  -16.898 10.826  0.50 21.88 ? 151 SER A OG  1 
ATOM   1213 N  N   . ALA A 1 152 ? -1.023  -14.347 7.890   1.00 16.16 ? 152 ALA A N   1 
ATOM   1214 C  CA  . ALA A 1 152 ? -0.623  -13.086 7.253   1.00 14.70 ? 152 ALA A CA  1 
ATOM   1215 C  C   . ALA A 1 152 ? -1.285  -11.913 7.951   1.00 15.30 ? 152 ALA A C   1 
ATOM   1216 O  O   . ALA A 1 152 ? -2.411  -11.999 8.433   1.00 17.75 ? 152 ALA A O   1 
ATOM   1217 C  CB  . ALA A 1 152 ? -0.959  -13.064 5.766   1.00 17.29 ? 152 ALA A CB  1 
ATOM   1218 N  N   . LYS A 1 153 ? -0.564  -10.782 7.952   1.00 16.82 ? 153 LYS A N   1 
ATOM   1219 C  CA  . LYS A 1 153 ? -1.126  -9.537  8.430   1.00 15.94 ? 153 LYS A CA  1 
ATOM   1220 C  C   . LYS A 1 153 ? -1.544  -8.775  7.184   1.00 16.46 ? 153 LYS A C   1 
ATOM   1221 O  O   . LYS A 1 153 ? -0.692  -8.321  6.438   1.00 15.28 ? 153 LYS A O   1 
ATOM   1222 C  CB  . LYS A 1 153 ? -0.038  -8.748  9.168   1.00 16.45 ? 153 LYS A CB  1 
ATOM   1223 C  CG  . LYS A 1 153 ? -0.541  -7.562  9.995   1.00 18.11 ? 153 LYS A CG  1 
ATOM   1224 C  CD  . LYS A 1 153 ? -1.386  -7.914  11.165  1.00 18.61 ? 153 LYS A CD  1 
ATOM   1225 C  CE  . LYS A 1 153 ? -1.761  -6.731  12.040  1.00 21.02 ? 153 LYS A CE  1 
ATOM   1226 N  NZ  . LYS A 1 153 ? -2.814  -7.094  13.004  1.00 25.62 ? 153 LYS A NZ  1 
ATOM   1227 N  N   . PRO A 1 154 ? -2.869  -8.620  6.921   1.00 15.51 ? 154 PRO A N   1 
ATOM   1228 C  CA  . PRO A 1 154 ? -3.270  -8.022  5.639   1.00 18.35 ? 154 PRO A CA  1 
ATOM   1229 C  C   . PRO A 1 154 ? -2.741  -6.607  5.473   1.00 17.48 ? 154 PRO A C   1 
ATOM   1230 O  O   . PRO A 1 154 ? -2.289  -6.265  4.384   1.00 19.48 ? 154 PRO A O   1 
ATOM   1231 C  CB  . PRO A 1 154 ? -4.801  -8.036  5.691   1.00 20.03 ? 154 PRO A CB  1 
ATOM   1232 C  CG  . PRO A 1 154 ? -5.120  -9.103  6.697   1.00 18.59 ? 154 PRO A CG  1 
ATOM   1233 C  CD  . PRO A 1 154 ? -3.998  -9.124  7.714   1.00 19.11 ? 154 PRO A CD  1 
ATOM   1234 N  N   . GLY A 1 155 ? -2.683  -5.878  6.583   1.00 16.83 ? 155 GLY A N   1 
ATOM   1235 C  CA  . GLY A 1 155 ? -2.244  -4.492  6.641   1.00 17.85 ? 155 GLY A CA  1 
ATOM   1236 C  C   . GLY A 1 155 ? -0.759  -4.303  6.334   1.00 18.55 ? 155 GLY A C   1 
ATOM   1237 O  O   . GLY A 1 155 ? -0.316  -3.187  6.079   1.00 22.81 ? 155 GLY A O   1 
ATOM   1238 N  N   . LEU A 1 156 ? 0.027   -5.381  6.336   1.00 15.62 ? 156 LEU A N   1 
ATOM   1239 C  CA  . LEU A 1 156 ? 1.445   -5.362  6.003   1.00 15.14 ? 156 LEU A CA  1 
ATOM   1240 C  C   . LEU A 1 156 ? 1.694   -5.597  4.521   1.00 14.87 ? 156 LEU A C   1 
ATOM   1241 O  O   . LEU A 1 156 ? 2.769   -5.338  4.023   1.00 15.34 ? 156 LEU A O   1 
ATOM   1242 C  CB  . LEU A 1 156 ? 2.223   -6.406  6.839   1.00 14.50 ? 156 LEU A CB  1 
ATOM   1243 C  CG  . LEU A 1 156 ? 3.743   -6.516  6.631   1.00 14.64 ? 156 LEU A CG  1 
ATOM   1244 C  CD1 . LEU A 1 156 ? 4.489   -5.213  6.987   1.00 14.96 ? 156 LEU A CD1 1 
ATOM   1245 C  CD2 . LEU A 1 156 ? 4.334   -7.660  7.466   1.00 15.02 ? 156 LEU A CD2 1 
ATOM   1246 N  N   . GLN A 1 157 ? 0.698   -6.129  3.786   1.00 16.42 ? 157 GLN A N   1 
ATOM   1247 C  CA  . GLN A 1 157 ? 1.043   -6.601  2.447   1.00 17.71 ? 157 GLN A CA  1 
ATOM   1248 C  C   . GLN A 1 157 ? 1.463   -5.489  1.488   1.00 15.07 ? 157 GLN A C   1 
ATOM   1249 O  O   . GLN A 1 157 ? 2.352   -5.693  0.683   1.00 15.99 ? 157 GLN A O   1 
ATOM   1250 C  CB  . GLN A 1 157 ? -0.044  -7.503  1.848   1.00 18.38 ? 157 GLN A CB  1 
ATOM   1251 C  CG  . GLN A 1 157 ? 0.370   -8.203  0.546   1.00 20.36 ? 157 GLN A CG  1 
ATOM   1252 C  CD  . GLN A 1 157 ? 1.463   -9.200  0.815   1.00 18.20 ? 157 GLN A CD  1 
ATOM   1253 O  OE1 . GLN A 1 157 ? 1.519   -9.781  1.919   1.00 19.43 ? 157 GLN A OE1 1 
ATOM   1254 N  NE2 . GLN A 1 157 ? 2.325   -9.417  -0.164  1.00 17.79 ? 157 GLN A NE2 1 
ATOM   1255 N  N   . LYS A 1 158 ? 0.881   -4.296  1.632   1.00 17.91 ? 158 LYS A N   1 
ATOM   1256 C  CA  . LYS A 1 158 ? 1.280   -3.214  0.746   1.00 19.20 ? 158 LYS A CA  1 
ATOM   1257 C  C   . LYS A 1 158 ? 2.756   -2.877  0.919   1.00 18.79 ? 158 LYS A C   1 
ATOM   1258 O  O   . LYS A 1 158 ? 3.420   -2.463  -0.019  1.00 19.55 ? 158 LYS A O   1 
ATOM   1259 C  CB  . LYS A 1 158 ? 0.347   -2.011  0.935   1.00 21.25 ? 158 LYS A CB  1 
ATOM   1260 C  CG  . LYS A 1 158 ? -0.987  -2.123  0.202   1.00 25.14 ? 158 LYS A CG  1 
ATOM   1261 N  N   . VAL A 1 159 ? 3.258   -3.038  2.145   1.00 17.27 ? 159 VAL A N   1 
ATOM   1262 C  CA  . VAL A 1 159 ? 4.678   -2.811  2.380   1.00 16.21 ? 159 VAL A CA  1 
ATOM   1263 C  C   . VAL A 1 159 ? 5.524   -3.899  1.709   1.00 16.47 ? 159 VAL A C   1 
ATOM   1264 O  O   . VAL A 1 159 ? 6.522   -3.640  1.027   1.00 16.39 ? 159 VAL A O   1 
ATOM   1265 C  CB  . VAL A 1 159 ? 4.938   -2.804  3.897   1.00 16.69 ? 159 VAL A CB  1 
ATOM   1266 C  CG1 . VAL A 1 159 ? 6.432   -2.774  4.183   1.00 15.57 ? 159 VAL A CG1 1 
ATOM   1267 C  CG2 . VAL A 1 159 ? 4.215   -1.666  4.602   1.00 16.55 ? 159 VAL A CG2 1 
ATOM   1268 N  N   . VAL A 1 160 ? 5.125   -5.165  1.960   1.00 16.40 ? 160 VAL A N   1 
ATOM   1269 C  CA  . VAL A 1 160 ? 5.838   -6.310  1.412   1.00 18.29 ? 160 VAL A CA  1 
ATOM   1270 C  C   . VAL A 1 160 ? 5.920   -6.206  -0.118  1.00 16.40 ? 160 VAL A C   1 
ATOM   1271 O  O   . VAL A 1 160 ? 6.975   -6.452  -0.695  1.00 16.01 ? 160 VAL A O   1 
ATOM   1272 C  CB  . VAL A 1 160 ? 5.150   -7.617  1.888   1.00 18.36 ? 160 VAL A CB  1 
ATOM   1273 C  CG1 . VAL A 1 160 ? 5.534   -8.805  1.027   1.00 21.95 ? 160 VAL A CG1 1 
ATOM   1274 C  CG2 . VAL A 1 160 ? 5.405   -7.847  3.376   1.00 20.82 ? 160 VAL A CG2 1 
ATOM   1275 N  N   . ASP A 1 161 ? 4.818   -5.767  -0.752  1.00 17.85 ? 161 ASP A N   1 
ATOM   1276 C  CA  . ASP A 1 161 ? 4.797   -5.831  -2.210  1.00 19.61 ? 161 ASP A CA  1 
ATOM   1277 C  C   . ASP A 1 161 ? 5.686   -4.773  -2.861  1.00 20.94 ? 161 ASP A C   1 
ATOM   1278 O  O   . ASP A 1 161 ? 5.984   -4.857  -4.056  1.00 24.43 ? 161 ASP A O   1 
ATOM   1279 C  CB  . ASP A 1 161 ? 3.364   -5.764  -2.712  1.00 21.06 ? 161 ASP A CB  1 
ATOM   1280 C  CG  . ASP A 1 161 ? 2.684   -7.124  -2.621  1.00 23.95 ? 161 ASP A CG  1 
ATOM   1281 O  OD1 . ASP A 1 161 ? 3.404   -8.165  -2.712  1.00 27.90 ? 161 ASP A OD1 1 
ATOM   1282 O  OD2 . ASP A 1 161 ? 1.476   -7.128  -2.381  1.00 27.63 ? 161 ASP A OD2 1 
ATOM   1283 N  N   . VAL A 1 162 ? 6.109   -3.750  -2.115  1.00 20.35 ? 162 VAL A N   1 
ATOM   1284 C  CA  . VAL A 1 162 ? 6.867   -2.672  -2.729  1.00 19.37 ? 162 VAL A CA  1 
ATOM   1285 C  C   . VAL A 1 162 ? 8.371   -2.924  -2.526  1.00 16.94 ? 162 VAL A C   1 
ATOM   1286 O  O   . VAL A 1 162 ? 9.224   -2.216  -3.046  1.00 18.95 ? 162 VAL A O   1 
ATOM   1287 C  CB  . VAL A 1 162 ? 6.393   -1.308  -2.189  1.00 22.16 ? 162 VAL A CB  1 
ATOM   1288 C  CG1 . VAL A 1 162 ? 6.902   -1.035  -0.792  1.00 21.20 ? 162 VAL A CG1 1 
ATOM   1289 C  CG2 . VAL A 1 162 ? 6.729   -0.134  -3.090  1.00 22.71 ? 162 VAL A CG2 1 
ATOM   1290 N  N   . LEU A 1 163 ? 8.730   -3.954  -1.718  1.00 17.32 ? 163 LEU A N   1 
ATOM   1291 C  CA  . LEU A 1 163 ? 10.132  -4.130  -1.358  1.00 15.26 ? 163 LEU A CA  1 
ATOM   1292 C  C   . LEU A 1 163 ? 11.048  -4.487  -2.528  1.00 17.90 ? 163 LEU A C   1 
ATOM   1293 O  O   . LEU A 1 163 ? 12.225  -4.128  -2.539  1.00 16.99 ? 163 LEU A O   1 
ATOM   1294 C  CB  . LEU A 1 163 ? 10.337  -5.145  -0.225  1.00 15.69 ? 163 LEU A CB  1 
ATOM   1295 C  CG  . LEU A 1 163 ? 9.701   -4.795  1.118   1.00 15.74 ? 163 LEU A CG  1 
ATOM   1296 C  CD1 . LEU A 1 163 ? 9.959   -5.950  2.089   1.00 16.71 ? 163 LEU A CD1 1 
ATOM   1297 C  CD2 . LEU A 1 163 ? 10.269  -3.509  1.692   1.00 16.13 ? 163 LEU A CD2 1 
ATOM   1298 N  N   . ASP A 1 164 ? 10.459  -5.150  -3.536  1.00 21.00 ? 164 ASP A N   1 
ATOM   1299 C  CA  . ASP A 1 164 ? 11.271  -5.466  -4.700  1.00 22.56 ? 164 ASP A CA  1 
ATOM   1300 C  C   . ASP A 1 164 ? 11.713  -4.185  -5.438  1.00 21.94 ? 164 ASP A C   1 
ATOM   1301 O  O   . ASP A 1 164 ? 12.737  -4.238  -6.128  1.00 24.17 ? 164 ASP A O   1 
ATOM   1302 C  CB  . ASP A 1 164 ? 10.527  -6.431  -5.630  1.00 27.32 ? 164 ASP A CB  1 
ATOM   1303 C  CG  . ASP A 1 164 ? 9.565   -5.647  -6.488  1.00 32.31 ? 164 ASP A CG  1 
ATOM   1304 O  OD1 . ASP A 1 164 ? 8.578   -5.158  -5.932  1.00 32.63 ? 164 ASP A OD1 1 
ATOM   1305 O  OD2 . ASP A 1 164 ? 9.864   -5.450  -7.699  1.00 37.30 ? 164 ASP A OD2 1 
ATOM   1306 N  N   . SER A 1 165 ? 11.033  -3.036  -5.243  1.00 19.62 ? 165 SER A N   1 
ATOM   1307 C  CA  . SER A 1 165 ? 11.426  -1.779  -5.886  1.00 19.84 ? 165 SER A CA  1 
ATOM   1308 C  C   . SER A 1 165 ? 12.485  -1.012  -5.094  1.00 20.68 ? 165 SER A C   1 
ATOM   1309 O  O   . SER A 1 165 ? 13.017  0.009   -5.557  1.00 20.50 ? 165 SER A O   1 
ATOM   1310 C  CB  . SER A 1 165 ? 10.220  -0.920  -6.145  1.00 23.49 ? 165 SER A CB  1 
ATOM   1311 O  OG  . SER A 1 165 ? 9.724   -0.323  -4.956  1.00 23.20 ? 165 SER A OG  1 
ATOM   1312 N  N   . ILE A 1 166 ? 12.765  -1.460  -3.859  1.00 18.16 ? 166 ILE A N   1 
ATOM   1313 C  CA  . ILE A 1 166 ? 13.815  -0.831  -3.056  1.00 16.33 ? 166 ILE A CA  1 
ATOM   1314 C  C   . ILE A 1 166 ? 14.837  -1.861  -2.551  1.00 16.17 ? 166 ILE A C   1 
ATOM   1315 O  O   . ILE A 1 166 ? 15.262  -1.889  -1.396  1.00 16.02 ? 166 ILE A O   1 
ATOM   1316 C  CB  . ILE A 1 166 ? 13.218  0.013   -1.916  1.00 15.74 ? 166 ILE A CB  1 
ATOM   1317 C  CG1 . ILE A 1 166 ? 12.433  -0.879  -0.961  1.00 14.69 ? 166 ILE A CG1 1 
ATOM   1318 C  CG2 . ILE A 1 166 ? 12.385  1.177   -2.457  1.00 16.70 ? 166 ILE A CG2 1 
ATOM   1319 C  CD1 . ILE A 1 166 ? 12.328  -0.308  0.450   1.00 17.09 ? 166 ILE A CD1 1 
ATOM   1320 N  N   . LYS A 1 167 ? 15.289  -2.730  -3.453  1.00 16.20 ? 167 LYS A N   1 
ATOM   1321 C  CA  . LYS A 1 167 ? 16.063  -3.879  -3.045  1.00 15.95 ? 167 LYS A CA  1 
ATOM   1322 C  C   . LYS A 1 167 ? 17.365  -3.469  -2.380  1.00 17.03 ? 167 LYS A C   1 
ATOM   1323 O  O   . LYS A 1 167 ? 17.864  -4.151  -1.483  1.00 16.03 ? 167 LYS A O   1 
ATOM   1324 C  CB  . LYS A 1 167 ? 16.354  -4.784  -4.255  1.00 17.98 ? 167 LYS A CB  1 
ATOM   1325 C  CG  . LYS A 1 167 ? 17.043  -6.085  -3.871  1.00 19.12 ? 167 LYS A CG  1 
ATOM   1326 C  CD  . LYS A 1 167 ? 17.259  -7.053  -5.046  1.00 22.66 ? 167 LYS A CD  1 
ATOM   1327 C  CE  . LYS A 1 167 ? 18.074  -8.265  -4.648  1.00 27.74 ? 167 LYS A CE  1 
ATOM   1328 N  NZ  . LYS A 1 167 ? 18.300  -9.202  -5.782  1.00 33.49 ? 167 LYS A NZ  1 
ATOM   1329 N  N   . THR A 1 168 ? 17.943  -2.370  -2.877  1.00 14.43 ? 168 THR A N   1 
ATOM   1330 C  CA  . THR A 1 168 ? 19.305  -2.078  -2.505  1.00 16.09 ? 168 THR A CA  1 
ATOM   1331 C  C   . THR A 1 168 ? 19.367  -0.716  -1.826  1.00 13.39 ? 168 THR A C   1 
ATOM   1332 O  O   . THR A 1 168 ? 18.449  0.105   -1.893  1.00 17.06 ? 168 THR A O   1 
ATOM   1333 C  CB  . THR A 1 168 ? 20.257  -2.108  -3.713  1.00 17.22 ? 168 THR A CB  1 
ATOM   1334 O  OG1 . THR A 1 168 ? 19.622  -1.290  -4.683  1.00 18.48 ? 168 THR A OG1 1 
ATOM   1335 C  CG2 . THR A 1 168 ? 20.494  -3.523  -4.215  1.00 16.63 ? 168 THR A CG2 1 
ATOM   1336 N  N   . LYS A 1 169 ? 20.437  -0.570  -1.079  1.00 15.65 ? 169 LYS A N   1 
ATOM   1337 C  CA  . LYS A 1 169 ? 20.755  0.618   -0.285  1.00 16.88 ? 169 LYS A CA  1 
ATOM   1338 C  C   . LYS A 1 169 ? 20.595  1.928   -1.065  1.00 16.80 ? 169 LYS A C   1 
ATOM   1339 O  O   . LYS A 1 169 ? 21.124  2.063   -2.187  1.00 20.24 ? 169 LYS A O   1 
ATOM   1340 C  CB  . LYS A 1 169 ? 22.170  0.493   0.279   1.00 17.78 ? 169 LYS A CB  1 
ATOM   1341 C  CG  . LYS A 1 169 ? 22.656  1.737   1.026   1.00 19.86 ? 169 LYS A CG  1 
ATOM   1342 C  CD  . LYS A 1 169 ? 23.946  1.502   1.723   1.00 20.79 ? 169 LYS A CD  1 
ATOM   1343 C  CE  . LYS A 1 169 ? 24.562  2.740   2.331   1.00 28.95 ? 169 LYS A CE  1 
ATOM   1344 N  NZ  . LYS A 1 169 ? 25.917  2.477   2.884   1.00 35.82 ? 169 LYS A NZ  1 
ATOM   1345 N  N   . GLY A 1 170 ? 19.832  2.880   -0.510  1.00 19.69 ? 170 GLY A N   1 
ATOM   1346 C  CA  . GLY A 1 170 ? 19.644  4.185   -1.157  1.00 18.13 ? 170 GLY A CA  1 
ATOM   1347 C  C   . GLY A 1 170 ? 18.449  4.254   -2.105  1.00 21.73 ? 170 GLY A C   1 
ATOM   1348 O  O   . GLY A 1 170 ? 18.114  5.345   -2.578  1.00 19.19 ? 170 GLY A O   1 
ATOM   1349 N  N   . LYS A 1 171 ? 17.813  3.117   -2.429  1.00 17.16 ? 171 LYS A N   1 
ATOM   1350 C  CA  . LYS A 1 171 ? 16.592  3.135   -3.229  1.00 17.95 ? 171 LYS A CA  1 
ATOM   1351 C  C   . LYS A 1 171 ? 15.406  3.581   -2.402  1.00 18.40 ? 171 LYS A C   1 
ATOM   1352 O  O   . LYS A 1 171 ? 15.255  3.101   -1.273  1.00 16.87 ? 171 LYS A O   1 
ATOM   1353 C  CB  . LYS A 1 171 ? 16.342  1.780   -3.893  1.00 18.70 ? 171 LYS A CB  1 
ATOM   1354 C  CG  . LYS A 1 171 ? 17.434  1.396   -4.897  1.00 21.87 ? 171 LYS A CG  1 
ATOM   1355 C  CD  . LYS A 1 171 ? 17.005  0.348   -5.928  1.00 27.13 ? 171 LYS A CD  1 
ATOM   1356 C  CE  . LYS A 1 171 ? 15.908  0.833   -6.870  1.00 29.05 ? 171 LYS A CE  1 
ATOM   1357 N  NZ  . LYS A 1 171 ? 15.438  -0.250  -7.773  1.00 30.38 ? 171 LYS A NZ  1 
ATOM   1358 N  N   . SER A 1 172 ? 14.566  4.460   -2.949  1.00 16.99 ? 172 SER A N   1 
ATOM   1359 C  CA  . SER A 1 172 ? 13.272  4.855   -2.400  1.00 18.45 ? 172 SER A CA  1 
ATOM   1360 C  C   . SER A 1 172 ? 12.143  4.676   -3.412  1.00 17.66 ? 172 SER A C   1 
ATOM   1361 O  O   . SER A 1 172 ? 12.351  4.657   -4.638  1.00 19.38 ? 172 SER A O   1 
ATOM   1362 C  CB  . SER A 1 172 ? 13.268  6.254   -1.812  1.00 17.19 ? 172 SER A CB  1 
ATOM   1363 O  OG  . SER A 1 172 ? 13.545  7.234   -2.821  1.00 19.60 ? 172 SER A OG  1 
ATOM   1364 N  N   . ALA A 1 173 ? 10.920  4.653   -2.903  1.00 20.90 ? 173 ALA A N   1 
ATOM   1365 C  CA  . ALA A 1 173 ? 9.729   4.616   -3.743  1.00 20.36 ? 173 ALA A CA  1 
ATOM   1366 C  C   . ALA A 1 173 ? 8.627   5.434   -3.084  1.00 22.70 ? 173 ALA A C   1 
ATOM   1367 O  O   . ALA A 1 173 ? 8.566   5.528   -1.865  1.00 17.49 ? 173 ALA A O   1 
ATOM   1368 C  CB  . ALA A 1 173 ? 9.257   3.205   -3.954  1.00 22.46 ? 173 ALA A CB  1 
ATOM   1369 N  N   . ASP A 1 174 ? 7.756   6.053   -3.882  1.00 23.42 ? 174 ASP A N   1 
ATOM   1370 C  CA  . ASP A 1 174 ? 6.578   6.721   -3.359  1.00 25.88 ? 174 ASP A CA  1 
ATOM   1371 C  C   . ASP A 1 174 ? 5.763   5.706   -2.566  1.00 24.12 ? 174 ASP A C   1 
ATOM   1372 O  O   . ASP A 1 174 ? 5.586   4.544   -2.973  1.00 24.19 ? 174 ASP A O   1 
ATOM   1373 C  CB  . ASP A 1 174 ? 5.761   7.409   -4.472  1.00 28.90 ? 174 ASP A CB  1 
ATOM   1374 C  CG  . ASP A 1 174 ? 6.595   8.418   -5.253  1.00 37.53 ? 174 ASP A CG  1 
ATOM   1375 O  OD1 . ASP A 1 174 ? 7.117   9.376   -4.623  1.00 38.83 ? 174 ASP A OD1 1 
ATOM   1376 O  OD2 . ASP A 1 174 ? 6.750   8.232   -6.490  1.00 44.90 ? 174 ASP A OD2 1 
ATOM   1377 N  N   . PHE A 1 175 ? 5.273   6.155   -1.413  1.00 20.20 ? 175 PHE A N   1 
ATOM   1378 C  CA  . PHE A 1 175 ? 4.535   5.255   -0.563  1.00 17.97 ? 175 PHE A CA  1 
ATOM   1379 C  C   . PHE A 1 175 ? 3.439   6.034   0.130   1.00 20.66 ? 175 PHE A C   1 
ATOM   1380 O  O   . PHE A 1 175 ? 3.416   6.147   1.339   1.00 19.57 ? 175 PHE A O   1 
ATOM   1381 C  CB  . PHE A 1 175 ? 5.489   4.442   0.329   1.00 18.54 ? 175 PHE A CB  1 
ATOM   1382 C  CG  . PHE A 1 175 ? 4.887   3.153   0.812   1.00 18.64 ? 175 PHE A CG  1 
ATOM   1383 C  CD1 . PHE A 1 175 ? 4.666   2.097   -0.058  1.00 18.89 ? 175 PHE A CD1 1 
ATOM   1384 C  CD2 . PHE A 1 175 ? 4.483   3.028   2.129   1.00 18.72 ? 175 PHE A CD2 1 
ATOM   1385 C  CE1 . PHE A 1 175 ? 4.058   0.930   0.395   1.00 19.90 ? 175 PHE A CE1 1 
ATOM   1386 C  CE2 . PHE A 1 175 ? 3.886   1.856   2.600   1.00 17.59 ? 175 PHE A CE2 1 
ATOM   1387 C  CZ  . PHE A 1 175 ? 3.686   0.803   1.720   1.00 18.90 ? 175 PHE A CZ  1 
ATOM   1388 N  N   . THR A 1 176 ? 2.482   6.530   -0.644  1.00 18.41 ? 176 THR A N   1 
ATOM   1389 C  CA  . THR A 1 176 ? 1.404   7.326   -0.097  1.00 18.72 ? 176 THR A CA  1 
ATOM   1390 C  C   . THR A 1 176 ? 0.224   6.481   0.349   1.00 15.06 ? 176 THR A C   1 
ATOM   1391 O  O   . THR A 1 176 ? 0.095   5.351   -0.114  1.00 17.06 ? 176 THR A O   1 
ATOM   1392 C  CB  . THR A 1 176 ? 0.983   8.413   -1.094  1.00 19.40 ? 176 THR A CB  1 
ATOM   1393 O  OG1 . THR A 1 176 ? 0.574   7.748   -2.294  1.00 23.64 ? 176 THR A OG1 1 
ATOM   1394 C  CG2 . THR A 1 176 ? 2.106   9.372   -1.403  1.00 23.21 ? 176 THR A CG2 1 
ATOM   1395 N  N   . ASN A 1 177 ? -0.628  7.033   1.221   1.00 15.88 ? 177 ASN A N   1 
ATOM   1396 C  CA  . ASN A 1 177 ? -1.926  6.510   1.591   1.00 17.39 ? 177 ASN A CA  1 
ATOM   1397 C  C   . ASN A 1 177 ? -1.830  5.168   2.323   1.00 17.63 ? 177 ASN A C   1 
ATOM   1398 O  O   . ASN A 1 177 ? -2.773  4.389   2.342   1.00 21.13 ? 177 ASN A O   1 
ATOM   1399 C  CB  . ASN A 1 177 ? -2.837  6.462   0.360   1.00 17.42 ? 177 ASN A CB  1 
ATOM   1400 C  CG  . ASN A 1 177 ? -2.977  7.837   -0.259  1.00 19.37 ? 177 ASN A CG  1 
ATOM   1401 O  OD1 . ASN A 1 177 ? -3.633  8.696   0.312   1.00 23.46 ? 177 ASN A OD1 1 
ATOM   1402 N  ND2 . ASN A 1 177 ? -2.397  8.022   -1.436  1.00 17.03 ? 177 ASN A ND2 1 
ATOM   1403 N  N   . PHE A 1 178 ? -0.702  4.956   2.978   1.00 16.49 ? 178 PHE A N   1 
ATOM   1404 C  CA  . PHE A 1 178 ? -0.541  3.766   3.808   1.00 16.84 ? 178 PHE A CA  1 
ATOM   1405 C  C   . PHE A 1 178 ? -1.019  4.075   5.221   1.00 17.15 ? 178 PHE A C   1 
ATOM   1406 O  O   . PHE A 1 178 ? -0.575  5.056   5.815   1.00 19.54 ? 178 PHE A O   1 
ATOM   1407 C  CB  . PHE A 1 178 ? 0.912   3.327   3.881   1.00 16.70 ? 178 PHE A CB  1 
ATOM   1408 C  CG  . PHE A 1 178 ? 1.001   2.073   4.720   1.00 17.88 ? 178 PHE A CG  1 
ATOM   1409 C  CD1 . PHE A 1 178 ? 0.604   0.855   4.197   1.00 17.83 ? 178 PHE A CD1 1 
ATOM   1410 C  CD2 . PHE A 1 178 ? 1.486   2.128   6.025   1.00 16.64 ? 178 PHE A CD2 1 
ATOM   1411 C  CE1 . PHE A 1 178 ? 0.632   -0.302  4.968   1.00 19.56 ? 178 PHE A CE1 1 
ATOM   1412 C  CE2 . PHE A 1 178 ? 1.535   0.974   6.792   1.00 17.92 ? 178 PHE A CE2 1 
ATOM   1413 C  CZ  . PHE A 1 178 ? 1.132   -0.235  6.262   1.00 19.02 ? 178 PHE A CZ  1 
ATOM   1414 N  N   . ASP A 1 179 ? -1.893  3.246   5.773   1.00 16.91 ? 179 ASP A N   1 
ATOM   1415 C  CA  . ASP A 1 179 ? -2.464  3.458   7.080   1.00 16.64 ? 179 ASP A CA  1 
ATOM   1416 C  C   . ASP A 1 179 ? -1.739  2.569   8.075   1.00 15.60 ? 179 ASP A C   1 
ATOM   1417 O  O   . ASP A 1 179 ? -1.912  1.357   8.079   1.00 15.95 ? 179 ASP A O   1 
ATOM   1418 C  CB  . ASP A 1 179 ? -3.955  3.108   7.074   1.00 17.84 ? 179 ASP A CB  1 
ATOM   1419 C  CG  . ASP A 1 179 ? -4.708  3.484   8.328   1.00 21.53 ? 179 ASP A CG  1 
ATOM   1420 O  OD1 . ASP A 1 179 ? -4.090  3.671   9.383   1.00 19.56 ? 179 ASP A OD1 1 
ATOM   1421 O  OD2 . ASP A 1 179 ? -5.958  3.608   8.239   1.00 25.58 ? 179 ASP A OD2 1 
ATOM   1422 N  N   . PRO A 1 180 ? -0.936  3.152   8.996   1.00 14.28 ? 180 PRO A N   1 
ATOM   1423 C  CA  . PRO A 1 180 ? -0.201  2.315   9.956   1.00 14.26 ? 180 PRO A CA  1 
ATOM   1424 C  C   . PRO A 1 180 ? -1.084  1.659   11.003  1.00 15.26 ? 180 PRO A C   1 
ATOM   1425 O  O   . PRO A 1 180 ? -0.608  0.772   11.719  1.00 14.31 ? 180 PRO A O   1 
ATOM   1426 C  CB  . PRO A 1 180 ? 0.777   3.313   10.595  1.00 16.58 ? 180 PRO A CB  1 
ATOM   1427 C  CG  . PRO A 1 180 ? 0.135   4.676   10.455  1.00 16.22 ? 180 PRO A CG  1 
ATOM   1428 C  CD  . PRO A 1 180 ? -0.729  4.598   9.206   1.00 14.40 ? 180 PRO A CD  1 
ATOM   1429 N  N   . ARG A 1 181 ? -2.357  2.040   11.053  1.00 14.81 ? 181 ARG A N   1 
ATOM   1430 C  CA  . ARG A 1 181 ? -3.245  1.382   12.009  1.00 14.66 ? 181 ARG A CA  1 
ATOM   1431 C  C   . ARG A 1 181 ? -3.381  -0.099  11.685  1.00 16.31 ? 181 ARG A C   1 
ATOM   1432 O  O   . ARG A 1 181 ? -3.761  -0.881  12.543  1.00 17.26 ? 181 ARG A O   1 
ATOM   1433 C  CB  . ARG A 1 181 ? -4.646  2.024   12.057  1.00 15.12 ? 181 ARG A CB  1 
ATOM   1434 C  CG  . ARG A 1 181 ? -4.579  3.424   12.643  1.00 17.31 ? 181 ARG A CG  1 
ATOM   1435 C  CD  . ARG A 1 181 ? -5.844  4.229   12.559  1.00 18.16 ? 181 ARG A CD  1 
ATOM   1436 N  NE  . ARG A 1 181 ? -6.258  4.425   11.191  1.00 17.69 ? 181 ARG A NE  1 
ATOM   1437 C  CZ  . ARG A 1 181 ? -7.334  5.140   10.860  1.00 20.16 ? 181 ARG A CZ  1 
ATOM   1438 N  NH1 . ARG A 1 181 ? -8.075  5.695   11.816  1.00 22.65 ? 181 ARG A NH1 1 
ATOM   1439 N  NH2 . ARG A 1 181 ? -7.645  5.295   9.583   1.00 21.20 ? 181 ARG A NH2 1 
ATOM   1440 N  N   . GLY A 1 182 ? -3.159  -0.447  10.423  1.00 15.54 ? 182 GLY A N   1 
ATOM   1441 C  CA  . GLY A 1 182 ? -3.238  -1.841  9.991   1.00 16.64 ? 182 GLY A CA  1 
ATOM   1442 C  C   . GLY A 1 182 ? -2.157  -2.730  10.602  1.00 17.40 ? 182 GLY A C   1 
ATOM   1443 O  O   . GLY A 1 182 ? -2.171  -3.934  10.352  1.00 18.19 ? 182 GLY A O   1 
ATOM   1444 N  N   . LEU A 1 183 ? -1.146  -2.126  11.263  1.00 15.63 ? 183 LEU A N   1 
ATOM   1445 C  CA  . LEU A 1 183 ? -0.018  -2.898  11.776  1.00 15.47 ? 183 LEU A CA  1 
ATOM   1446 C  C   . LEU A 1 183 ? -0.136  -3.083  13.281  1.00 15.21 ? 183 LEU A C   1 
ATOM   1447 O  O   . LEU A 1 183 ? 0.793   -3.648  13.899  1.00 16.36 ? 183 LEU A O   1 
ATOM   1448 C  CB  . LEU A 1 183 ? 1.300   -2.177  11.457  1.00 13.85 ? 183 LEU A CB  1 
ATOM   1449 C  CG  . LEU A 1 183 ? 1.613   -2.011  9.961   1.00 14.82 ? 183 LEU A CG  1 
ATOM   1450 C  CD1 . LEU A 1 183 ? 2.815   -1.111  9.795   1.00 17.14 ? 183 LEU A CD1 1 
ATOM   1451 C  CD2 . LEU A 1 183 ? 1.781   -3.323  9.190   1.00 18.39 ? 183 LEU A CD2 1 
ATOM   1452 N  N   . LEU A 1 184 ? -1.220  -2.594  13.874  1.00 13.92 ? 184 LEU A N   1 
ATOM   1453 C  CA  . LEU A 1 184 ? -1.363  -2.640  15.332  1.00 14.87 ? 184 LEU A CA  1 
ATOM   1454 C  C   . LEU A 1 184 ? -2.048  -3.931  15.771  1.00 18.13 ? 184 LEU A C   1 
ATOM   1455 O  O   . LEU A 1 184 ? -2.952  -4.429  15.084  1.00 23.42 ? 184 LEU A O   1 
ATOM   1456 C  CB  . LEU A 1 184 ? -2.159  -1.448  15.862  1.00 14.68 ? 184 LEU A CB  1 
ATOM   1457 C  CG  . LEU A 1 184 ? -1.596  -0.086  15.461  1.00 13.20 ? 184 LEU A CG  1 
ATOM   1458 C  CD1 . LEU A 1 184 ? -2.436  1.070   15.940  1.00 16.65 ? 184 LEU A CD1 1 
ATOM   1459 C  CD2 . LEU A 1 184 ? -0.146  0.070   15.962  1.00 16.47 ? 184 LEU A CD2 1 
ATOM   1460 N  N   . PRO A 1 185 ? -1.705  -4.519  16.929  1.00 16.23 ? 185 PRO A N   1 
ATOM   1461 C  CA  . PRO A 1 185 ? -2.451  -5.650  17.451  1.00 15.50 ? 185 PRO A CA  1 
ATOM   1462 C  C   . PRO A 1 185 ? -3.751  -5.136  18.065  1.00 16.87 ? 185 PRO A C   1 
ATOM   1463 O  O   . PRO A 1 185 ? -3.959  -3.933  18.177  1.00 17.85 ? 185 PRO A O   1 
ATOM   1464 C  CB  . PRO A 1 185 ? -1.491  -6.234  18.506  1.00 15.13 ? 185 PRO A CB  1 
ATOM   1465 C  CG  . PRO A 1 185 ? -0.756  -5.003  19.007  1.00 13.49 ? 185 PRO A CG  1 
ATOM   1466 C  CD  . PRO A 1 185 ? -0.549  -4.135  17.769  1.00 12.79 ? 185 PRO A CD  1 
ATOM   1467 N  N   . GLU A 1 186 ? -4.584  -6.068  18.538  1.00 17.55 ? 186 GLU A N   1 
ATOM   1468 C  CA  . GLU A 1 186 ? -5.842  -5.677  19.162  1.00 18.47 ? 186 GLU A CA  1 
ATOM   1469 C  C   . GLU A 1 186 ? -5.600  -4.913  20.451  1.00 17.39 ? 186 GLU A C   1 
ATOM   1470 O  O   . GLU A 1 186 ? -6.243  -3.902  20.695  1.00 19.92 ? 186 GLU A O   1 
ATOM   1471 C  CB  . GLU A 1 186 ? -6.641  -6.913  19.590  1.00 24.44 ? 186 GLU A CB  1 
ATOM   1472 C  CG  . GLU A 1 186 ? -7.277  -7.695  18.481  1.00 28.81 ? 186 GLU A CG  1 
ATOM   1473 C  CD  . GLU A 1 186 ? -8.136  -8.828  19.039  1.00 26.98 ? 186 GLU A CD  1 
ATOM   1474 O  OE1 . GLU A 1 186 ? -8.581  -9.674  18.258  1.00 36.83 ? 186 GLU A OE1 1 
ATOM   1475 O  OE2 . GLU A 1 186 ? -8.297  -8.887  20.265  1.00 24.35 ? 186 GLU A OE2 1 
ATOM   1476 N  N   . SER A 1 187 ? -4.705  -5.422  21.330  1.00 15.67 ? 187 SER A N   1 
ATOM   1477 C  CA  . SER A 1 187 ? -4.499  -4.823  22.641  1.00 16.03 ? 187 SER A CA  1 
ATOM   1478 C  C   . SER A 1 187 ? -3.374  -3.792  22.608  1.00 15.55 ? 187 SER A C   1 
ATOM   1479 O  O   . SER A 1 187 ? -2.370  -4.002  21.915  1.00 18.84 ? 187 SER A O   1 
ATOM   1480 C  CB  . SER A 1 187 ? -4.125  -5.863  23.671  1.00 15.86 ? 187 SER A CB  1 
ATOM   1481 O  OG  . SER A 1 187 ? -3.921  -5.295  24.953  1.00 16.56 ? 187 SER A OG  1 
ATOM   1482 N  N   . LEU A 1 188 ? -3.559  -2.705  23.368  1.00 14.44 ? 188 LEU A N   1 
ATOM   1483 C  CA  . LEU A 1 188 ? -2.481  -1.731  23.578  1.00 16.20 ? 188 LEU A CA  1 
ATOM   1484 C  C   . LEU A 1 188 ? -1.850  -1.846  24.968  1.00 15.45 ? 188 LEU A C   1 
ATOM   1485 O  O   . LEU A 1 188 ? -1.200  -0.901  25.424  1.00 18.24 ? 188 LEU A O   1 
ATOM   1486 C  CB  . LEU A 1 188 ? -2.960  -0.296  23.304  1.00 18.41 ? 188 LEU A CB  1 
ATOM   1487 C  CG  . LEU A 1 188 ? -3.458  0.028   21.902  1.00 21.10 ? 188 LEU A CG  1 
ATOM   1488 C  CD1 . LEU A 1 188 ? -4.012  1.460   21.844  1.00 22.82 ? 188 LEU A CD1 1 
ATOM   1489 C  CD2 . LEU A 1 188 ? -2.344  -0.157  20.871  1.00 19.04 ? 188 LEU A CD2 1 
ATOM   1490 N  N   . ASP A 1 189 ? -1.966  -3.003  25.641  1.00 15.83 ? 189 ASP A N   1 
ATOM   1491 C  CA  . ASP A 1 189 ? -1.218  -3.281  26.847  1.00 16.26 ? 189 ASP A CA  1 
ATOM   1492 C  C   . ASP A 1 189 ? 0.277   -3.232  26.492  1.00 13.46 ? 189 ASP A C   1 
ATOM   1493 O  O   . ASP A 1 189 ? 0.676   -3.706  25.410  1.00 13.71 ? 189 ASP A O   1 
ATOM   1494 C  CB  . ASP A 1 189 ? -1.606  -4.664  27.376  1.00 17.41 ? 189 ASP A CB  1 
ATOM   1495 C  CG  . ASP A 1 189 ? -2.974  -4.763  28.048  1.00 23.15 ? 189 ASP A CG  1 
ATOM   1496 O  OD1 . ASP A 1 189 ? -3.560  -3.716  28.319  1.00 24.48 ? 189 ASP A OD1 1 
ATOM   1497 O  OD2 . ASP A 1 189 ? -3.371  -5.894  28.308  1.00 25.68 ? 189 ASP A OD2 1 
ATOM   1498 N  N   . TYR A 1 190 ? 1.062   -2.634  27.388  1.00 13.69 ? 190 TYR A N   1 
ATOM   1499 C  CA  . TYR A 1 190 ? 2.466   -2.363  27.055  1.00 11.97 ? 190 TYR A CA  1 
ATOM   1500 C  C   . TYR A 1 190 ? 3.347   -2.427  28.288  1.00 13.25 ? 190 TYR A C   1 
ATOM   1501 O  O   . TYR A 1 190 ? 2.914   -2.344  29.456  1.00 13.04 ? 190 TYR A O   1 
ATOM   1502 C  CB  . TYR A 1 190 ? 2.586   -0.979  26.402  1.00 12.33 ? 190 TYR A CB  1 
ATOM   1503 C  CG  . TYR A 1 190 ? 2.224   0.200   27.280  1.00 12.49 ? 190 TYR A CG  1 
ATOM   1504 C  CD1 . TYR A 1 190 ? 3.147   0.811   28.124  1.00 13.30 ? 190 TYR A CD1 1 
ATOM   1505 C  CD2 . TYR A 1 190 ? 0.926   0.707   27.269  1.00 11.93 ? 190 TYR A CD2 1 
ATOM   1506 C  CE1 . TYR A 1 190 ? 2.778   1.846   28.966  1.00 13.08 ? 190 TYR A CE1 1 
ATOM   1507 C  CE2 . TYR A 1 190 ? 0.572   1.781   28.063  1.00 13.91 ? 190 TYR A CE2 1 
ATOM   1508 C  CZ  . TYR A 1 190 ? 1.488   2.353   28.929  1.00 13.44 ? 190 TYR A CZ  1 
ATOM   1509 O  OH  . TYR A 1 190 ? 1.126   3.390   29.745  1.00 15.25 ? 190 TYR A OH  1 
ATOM   1510 N  N   . TRP A 1 191 ? 4.639   -2.526  28.015  1.00 12.14 ? 191 TRP A N   1 
ATOM   1511 C  CA  . TRP A 1 191 ? 5.729   -2.263  28.942  1.00 11.04 ? 191 TRP A CA  1 
ATOM   1512 C  C   . TRP A 1 191 ? 6.427   -0.972  28.560  1.00 11.31 ? 191 TRP A C   1 
ATOM   1513 O  O   . TRP A 1 191 ? 6.498   -0.668  27.381  1.00 12.21 ? 191 TRP A O   1 
ATOM   1514 C  CB  . TRP A 1 191 ? 6.744   -3.424  28.956  1.00 11.16 ? 191 TRP A CB  1 
ATOM   1515 C  CG  . TRP A 1 191 ? 6.187   -4.736  29.371  1.00 10.72 ? 191 TRP A CG  1 
ATOM   1516 C  CD1 . TRP A 1 191 ? 5.989   -5.191  30.641  1.00 12.91 ? 191 TRP A CD1 1 
ATOM   1517 C  CD2 . TRP A 1 191 ? 5.967   -5.874  28.512  1.00 11.14 ? 191 TRP A CD2 1 
ATOM   1518 N  NE1 . TRP A 1 191 ? 5.563   -6.499  30.601  1.00 14.09 ? 191 TRP A NE1 1 
ATOM   1519 C  CE2 . TRP A 1 191 ? 5.496   -6.940  29.308  1.00 12.34 ? 191 TRP A CE2 1 
ATOM   1520 C  CE3 . TRP A 1 191 ? 6.078   -6.067  27.123  1.00 11.51 ? 191 TRP A CE3 1 
ATOM   1521 C  CZ2 . TRP A 1 191 ? 5.218   -8.192  28.749  1.00 13.44 ? 191 TRP A CZ2 1 
ATOM   1522 C  CZ3 . TRP A 1 191 ? 5.757   -7.289  26.572  1.00 11.62 ? 191 TRP A CZ3 1 
ATOM   1523 C  CH2 . TRP A 1 191 ? 5.366   -8.345  27.395  1.00 13.07 ? 191 TRP A CH2 1 
ATOM   1524 N  N   . THR A 1 192 ? 7.007   -0.259  29.517  1.00 10.60 ? 192 THR A N   1 
ATOM   1525 C  CA  . THR A 1 192 ? 7.698   0.971   29.187  1.00 11.04 ? 192 THR A CA  1 
ATOM   1526 C  C   . THR A 1 192 ? 8.931   1.128   30.063  1.00 11.45 ? 192 THR A C   1 
ATOM   1527 O  O   . THR A 1 192 ? 8.968   0.708   31.217  1.00 12.79 ? 192 THR A O   1 
ATOM   1528 C  CB  . THR A 1 192 ? 6.765   2.176   29.250  1.00 10.07 ? 192 THR A CB  1 
ATOM   1529 O  OG1 . THR A 1 192 ? 7.471   3.332   28.851  1.00 11.61 ? 192 THR A OG1 1 
ATOM   1530 C  CG2 . THR A 1 192 ? 6.201   2.416   30.642  1.00 11.82 ? 192 THR A CG2 1 
ATOM   1531 N  N   . TYR A 1 193 ? 9.986   1.702   29.485  1.00 10.68 ? 193 TYR A N   1 
ATOM   1532 C  CA  . TYR A 1 193 ? 11.230  1.946   30.206  1.00 11.00 ? 193 TYR A CA  1 
ATOM   1533 C  C   . TYR A 1 193 ? 12.015  2.983   29.436  1.00 11.11 ? 193 TYR A C   1 
ATOM   1534 O  O   . TYR A 1 193 ? 11.796  3.197   28.237  1.00 10.57 ? 193 TYR A O   1 
ATOM   1535 C  CB  . TYR A 1 193 ? 12.069  0.657   30.377  1.00 11.09 ? 193 TYR A CB  1 
ATOM   1536 C  CG  . TYR A 1 193 ? 12.758  0.199   29.121  1.00 10.41 ? 193 TYR A CG  1 
ATOM   1537 C  CD1 . TYR A 1 193 ? 12.079  -0.527  28.150  1.00 10.05 ? 193 TYR A CD1 1 
ATOM   1538 C  CD2 . TYR A 1 193 ? 14.095  0.527   28.921  1.00 9.89  ? 193 TYR A CD2 1 
ATOM   1539 C  CE1 . TYR A 1 193 ? 12.710  -0.853  26.948  1.00 9.06  ? 193 TYR A CE1 1 
ATOM   1540 C  CE2 . TYR A 1 193 ? 14.716  0.250   27.707  1.00 9.89  ? 193 TYR A CE2 1 
ATOM   1541 C  CZ  . TYR A 1 193 ? 14.042  -0.476  26.753  1.00 8.77  ? 193 TYR A CZ  1 
ATOM   1542 O  OH  . TYR A 1 193 ? 14.686  -0.769  25.582  1.00 9.20  ? 193 TYR A OH  1 
ATOM   1543 N  N   . PRO A 1 194 ? 12.979  3.660   30.072  1.00 11.23 ? 194 PRO A N   1 
ATOM   1544 C  CA  . PRO A 1 194 ? 13.790  4.672   29.432  1.00 12.08 ? 194 PRO A CA  1 
ATOM   1545 C  C   . PRO A 1 194 ? 15.006  4.032   28.800  1.00 11.41 ? 194 PRO A C   1 
ATOM   1546 O  O   . PRO A 1 194 ? 15.690  3.242   29.441  1.00 12.68 ? 194 PRO A O   1 
ATOM   1547 C  CB  . PRO A 1 194 ? 14.255  5.572   30.599  1.00 13.01 ? 194 PRO A CB  1 
ATOM   1548 C  CG  . PRO A 1 194 ? 14.301  4.644   31.762  1.00 12.23 ? 194 PRO A CG  1 
ATOM   1549 C  CD  . PRO A 1 194 ? 13.176  3.631   31.534  1.00 13.20 ? 194 PRO A CD  1 
ATOM   1550 N  N   . GLY A 1 195 ? 15.240  4.409   27.542  1.00 10.23 ? 195 GLY A N   1 
ATOM   1551 C  CA  . GLY A 1 195 ? 16.332  3.759   26.830  1.00 11.26 ? 195 GLY A CA  1 
ATOM   1552 C  C   . GLY A 1 195 ? 16.931  4.616   25.742  1.00 8.95  ? 195 GLY A C   1 
ATOM   1553 O  O   . GLY A 1 195 ? 16.995  5.832   25.850  1.00 9.64  ? 195 GLY A O   1 
ATOM   1554 N  N   . SER A 1 196 ? 17.302  3.944   24.656  1.00 9.46  ? 196 SER A N   1 
ATOM   1555 C  CA  . SER A 1 196 ? 18.148  4.540   23.627  1.00 9.34  ? 196 SER A CA  1 
ATOM   1556 C  C   . SER A 1 196 ? 17.697  4.170   22.228  1.00 10.13 ? 196 SER A C   1 
ATOM   1557 O  O   . SER A 1 196 ? 16.928  3.223   22.062  1.00 10.35 ? 196 SER A O   1 
ATOM   1558 C  CB  . SER A 1 196 ? 19.641  4.155   23.801  1.00 10.69 ? 196 SER A CB  1 
ATOM   1559 O  OG  . SER A 1 196 ? 19.897  2.819   23.372  1.00 10.56 ? 196 SER A OG  1 
ATOM   1560 N  N   . LEU A 1 197 ? 18.298  4.826   21.244  1.00 9.72  ? 197 LEU A N   1 
ATOM   1561 C  CA  . LEU A 1 197 ? 18.311  4.306   19.878  1.00 9.32  ? 197 LEU A CA  1 
ATOM   1562 C  C   . LEU A 1 197 ? 19.011  2.969   19.897  1.00 9.51  ? 197 LEU A C   1 
ATOM   1563 O  O   . LEU A 1 197 ? 20.015  2.813   20.620  1.00 9.44  ? 197 LEU A O   1 
ATOM   1564 C  CB  . LEU A 1 197 ? 19.125  5.284   19.016  1.00 11.85 ? 197 LEU A CB  1 
ATOM   1565 C  CG  . LEU A 1 197 ? 18.624  6.730   19.020  1.00 13.30 ? 197 LEU A CG  1 
ATOM   1566 C  CD1 . LEU A 1 197 ? 19.445  7.620   18.076  1.00 16.45 ? 197 LEU A CD1 1 
ATOM   1567 C  CD2 . LEU A 1 197 ? 17.160  6.819   18.616  1.00 15.61 ? 197 LEU A CD2 1 
ATOM   1568 N  N   . THR A 1 198 ? 18.550  2.008   19.082  1.00 9.85  ? 198 THR A N   1 
ATOM   1569 C  CA  . THR A 1 198 ? 19.166  0.702   19.032  1.00 10.60 ? 198 THR A CA  1 
ATOM   1570 C  C   . THR A 1 198 ? 20.200  0.611   17.901  1.00 10.04 ? 198 THR A C   1 
ATOM   1571 O  O   . THR A 1 198 ? 20.780  -0.458  17.743  1.00 11.59 ? 198 THR A O   1 
ATOM   1572 C  CB  . THR A 1 198 ? 18.100  -0.385  18.854  1.00 10.37 ? 198 THR A CB  1 
ATOM   1573 O  OG1 . THR A 1 198 ? 17.544  -0.316  17.535  1.00 9.33  ? 198 THR A OG1 1 
ATOM   1574 C  CG2 . THR A 1 198 ? 17.092  -0.450  19.975  1.00 10.31 ? 198 THR A CG2 1 
ATOM   1575 N  N   . THR A 1 199 ? 20.398  1.726   17.164  1.00 12.37 ? 199 THR A N   1 
ATOM   1576 C  CA  . THR A 1 199 ? 21.505  1.707   16.209  1.00 13.03 ? 199 THR A CA  1 
ATOM   1577 C  C   . THR A 1 199 ? 22.349  2.935   16.487  1.00 14.02 ? 199 THR A C   1 
ATOM   1578 O  O   . THR A 1 199 ? 21.892  3.903   17.096  1.00 12.85 ? 199 THR A O   1 
ATOM   1579 C  CB  . THR A 1 199 ? 21.004  1.905   14.780  1.00 14.73 ? 199 THR A CB  1 
ATOM   1580 O  OG1 . THR A 1 199 ? 20.318  3.139   14.625  1.00 17.26 ? 199 THR A OG1 1 
ATOM   1581 C  CG2 . THR A 1 199 ? 20.063  0.794   14.355  1.00 17.16 ? 199 THR A CG2 1 
ATOM   1582 N  N   . PRO A 1 200 ? 23.607  2.957   15.991  1.00 14.21 ? 200 PRO A N   1 
ATOM   1583 C  CA  . PRO A 1 200 ? 24.351  4.214   16.081  1.00 13.60 ? 200 PRO A CA  1 
ATOM   1584 C  C   . PRO A 1 200 ? 23.473  5.372   15.594  1.00 12.91 ? 200 PRO A C   1 
ATOM   1585 O  O   . PRO A 1 200 ? 22.738  5.253   14.599  1.00 14.29 ? 200 PRO A O   1 
ATOM   1586 C  CB  . PRO A 1 200 ? 25.505  3.876   15.092  1.00 12.93 ? 200 PRO A CB  1 
ATOM   1587 C  CG  . PRO A 1 200 ? 25.767  2.421   15.357  1.00 13.83 ? 200 PRO A CG  1 
ATOM   1588 C  CD  . PRO A 1 200 ? 24.369  1.818   15.437  1.00 15.28 ? 200 PRO A CD  1 
ATOM   1589 N  N   . PRO A 1 201 ? 23.517  6.563   16.223  1.00 12.91 ? 201 PRO A N   1 
ATOM   1590 C  CA  . PRO A 1 201 ? 24.465  6.858   17.321  1.00 13.34 ? 201 PRO A CA  1 
ATOM   1591 C  C   . PRO A 1 201 ? 24.130  6.454   18.762  1.00 13.02 ? 201 PRO A C   1 
ATOM   1592 O  O   . PRO A 1 201 ? 24.855  6.826   19.686  1.00 14.09 ? 201 PRO A O   1 
ATOM   1593 C  CB  . PRO A 1 201 ? 24.475  8.382   17.225  1.00 13.12 ? 201 PRO A CB  1 
ATOM   1594 C  CG  . PRO A 1 201 ? 23.043  8.754   16.864  1.00 14.21 ? 201 PRO A CG  1 
ATOM   1595 C  CD  . PRO A 1 201 ? 22.709  7.735   15.800  1.00 15.11 ? 201 PRO A CD  1 
ATOM   1596 N  N   . LEU A 1 202 ? 23.098  5.606   18.943  1.00 11.78 ? 202 LEU A N   1 
ATOM   1597 C  CA  . LEU A 1 202 ? 22.813  4.990   20.237  1.00 11.88 ? 202 LEU A CA  1 
ATOM   1598 C  C   . LEU A 1 202 ? 22.465  6.005   21.322  1.00 12.00 ? 202 LEU A C   1 
ATOM   1599 O  O   . LEU A 1 202 ? 22.491  5.692   22.504  1.00 12.32 ? 202 LEU A O   1 
ATOM   1600 C  CB  . LEU A 1 202 ? 23.974  4.081   20.688  1.00 12.27 ? 202 LEU A CB  1 
ATOM   1601 C  CG  . LEU A 1 202 ? 24.311  2.948   19.716  1.00 11.13 ? 202 LEU A CG  1 
ATOM   1602 C  CD1 . LEU A 1 202 ? 25.589  2.268   20.197  1.00 14.34 ? 202 LEU A CD1 1 
ATOM   1603 C  CD2 . LEU A 1 202 ? 23.178  1.904   19.703  1.00 12.66 ? 202 LEU A CD2 1 
ATOM   1604 N  N   . THR A 1 203 ? 21.962  7.166   20.888  1.00 12.07 ? 203 THR A N   1 
ATOM   1605 C  CA  . THR A 1 203 ? 21.666  8.228   21.825  1.00 13.01 ? 203 THR A CA  1 
ATOM   1606 C  C   . THR A 1 203 ? 20.579  7.805   22.818  1.00 13.32 ? 203 THR A C   1 
ATOM   1607 O  O   . THR A 1 203 ? 19.552  7.150   22.478  1.00 13.00 ? 203 THR A O   1 
ATOM   1608 C  CB  . THR A 1 203 ? 21.140  9.421   21.051  1.00 14.72 ? 203 THR A CB  1 
ATOM   1609 O  OG1 . THR A 1 203 ? 22.099  9.636   20.021  1.00 16.91 ? 203 THR A OG1 1 
ATOM   1610 C  CG2 . THR A 1 203 ? 21.021  10.665  21.909  1.00 16.02 ? 203 THR A CG2 1 
ATOM   1611 N  N   . GLU A 1 204 ? 20.710  8.252   24.070  1.00 14.10 ? 204 GLU A N   1 
ATOM   1612 C  CA  . GLU A 1 204 ? 19.824  7.887   25.164  1.00 14.83 ? 204 GLU A CA  1 
ATOM   1613 C  C   . GLU A 1 204 ? 18.647  8.870   25.238  1.00 14.37 ? 204 GLU A C   1 
ATOM   1614 O  O   . GLU A 1 204 ? 18.485  9.637   26.202  1.00 15.89 ? 204 GLU A O   1 
ATOM   1615 C  CB  . GLU A 1 204 ? 20.653  7.781   26.457  1.00 15.27 ? 204 GLU A CB  1 
ATOM   1616 C  CG  . GLU A 1 204 ? 21.573  6.564   26.380  1.00 14.05 ? 204 GLU A CG  1 
ATOM   1617 C  CD  . GLU A 1 204 ? 22.429  6.246   27.596  1.00 15.08 ? 204 GLU A CD  1 
ATOM   1618 O  OE1 . GLU A 1 204 ? 22.598  7.152   28.493  1.00 17.53 ? 204 GLU A OE1 1 
ATOM   1619 O  OE2 . GLU A 1 204 ? 22.824  5.067   27.734  1.00 13.69 ? 204 GLU A OE2 1 
ATOM   1620 N  N   . CYS A 1 205 ? 17.832  8.886   24.174  1.00 11.46 ? 205 CYS A N   1 
ATOM   1621 C  CA  . CYS A 1 205 ? 16.764  9.864   23.994  1.00 11.64 ? 205 CYS A CA  1 
ATOM   1622 C  C   . CYS A 1 205 ? 15.374  9.244   23.859  1.00 10.39 ? 205 CYS A C   1 
ATOM   1623 O  O   . CYS A 1 205 ? 14.468  9.964   23.449  1.00 11.50 ? 205 CYS A O   1 
ATOM   1624 C  CB  . CYS A 1 205 ? 17.065  10.723  22.775  1.00 11.63 ? 205 CYS A CB  1 
ATOM   1625 S  SG  . CYS A 1 205 ? 17.171  9.768   21.225  1.00 14.02 ? 205 CYS A SG  1 
ATOM   1626 N  N   . VAL A 1 206 ? 15.262  7.943   24.158  1.00 9.65  ? 206 VAL A N   1 
ATOM   1627 C  CA  . VAL A 1 206 ? 14.040  7.201   23.823  1.00 10.37 ? 206 VAL A CA  1 
ATOM   1628 C  C   . VAL A 1 206 ? 13.279  6.817   25.086  1.00 9.98  ? 206 VAL A C   1 
ATOM   1629 O  O   . VAL A 1 206 ? 13.795  6.101   25.944  1.00 10.92 ? 206 VAL A O   1 
ATOM   1630 C  CB  . VAL A 1 206 ? 14.327  5.946   22.989  1.00 9.92  ? 206 VAL A CB  1 
ATOM   1631 C  CG1 . VAL A 1 206 ? 12.978  5.292   22.607  1.00 9.36  ? 206 VAL A CG1 1 
ATOM   1632 C  CG2 . VAL A 1 206 ? 15.040  6.310   21.694  1.00 10.91 ? 206 VAL A CG2 1 
ATOM   1633 N  N   . THR A 1 207 ? 11.951  7.095   25.094  1.00 9.78  ? 207 THR A N   1 
ATOM   1634 C  CA  . THR A 1 207 ? 11.017  6.413   25.959  1.00 10.60 ? 207 THR A CA  1 
ATOM   1635 C  C   . THR A 1 207 ? 10.466  5.252   25.151  1.00 9.65  ? 207 THR A C   1 
ATOM   1636 O  O   . THR A 1 207 ? 9.810   5.472   24.126  1.00 9.85  ? 207 THR A O   1 
ATOM   1637 C  CB  . THR A 1 207 ? 9.836   7.288   26.391  1.00 10.31 ? 207 THR A CB  1 
ATOM   1638 O  OG1 . THR A 1 207 ? 10.351  8.391   27.149  1.00 11.18 ? 207 THR A OG1 1 
ATOM   1639 C  CG2 . THR A 1 207 ? 8.918   6.481   27.287  1.00 11.27 ? 207 THR A CG2 1 
ATOM   1640 N  N   . TRP A 1 208 ? 10.769  4.044   25.610  1.00 10.21 ? 208 TRP A N   1 
ATOM   1641 C  CA  . TRP A 1 208 ? 10.350  2.835   24.902  1.00 9.09  ? 208 TRP A CA  1 
ATOM   1642 C  C   . TRP A 1 208 ? 8.956   2.438   25.372  1.00 9.30  ? 208 TRP A C   1 
ATOM   1643 O  O   . TRP A 1 208 ? 8.736   2.374   26.590  1.00 9.89  ? 208 TRP A O   1 
ATOM   1644 C  CB  . TRP A 1 208 ? 11.355  1.672   25.090  1.00 9.54  ? 208 TRP A CB  1 
ATOM   1645 C  CG  . TRP A 1 208 ? 12.448  1.783   24.082  1.00 8.52  ? 208 TRP A CG  1 
ATOM   1646 C  CD1 . TRP A 1 208 ? 13.686  2.348   24.298  1.00 9.07  ? 208 TRP A CD1 1 
ATOM   1647 C  CD2 . TRP A 1 208 ? 12.378  1.387   22.709  1.00 8.87  ? 208 TRP A CD2 1 
ATOM   1648 N  NE1 . TRP A 1 208 ? 14.389  2.329   23.120  1.00 9.36  ? 208 TRP A NE1 1 
ATOM   1649 C  CE2 . TRP A 1 208 ? 13.622  1.746   22.129  1.00 9.23  ? 208 TRP A CE2 1 
ATOM   1650 C  CE3 . TRP A 1 208 ? 11.374  0.795   21.911  1.00 9.36  ? 208 TRP A CE3 1 
ATOM   1651 C  CZ2 . TRP A 1 208 ? 13.893  1.524   20.785  1.00 9.62  ? 208 TRP A CZ2 1 
ATOM   1652 C  CZ3 . TRP A 1 208 ? 11.689  0.510   20.600  1.00 9.20  ? 208 TRP A CZ3 1 
ATOM   1653 C  CH2 . TRP A 1 208 ? 12.913  0.906   20.019  1.00 9.05  ? 208 TRP A CH2 1 
ATOM   1654 N  N   . ILE A 1 209 ? 8.085   2.074   24.418  1.00 8.93  ? 209 ILE A N   1 
ATOM   1655 C  CA  . ILE A 1 209 ? 6.760   1.548   24.759  1.00 9.73  ? 209 ILE A CA  1 
ATOM   1656 C  C   . ILE A 1 209 ? 6.624   0.294   23.925  1.00 9.70  ? 209 ILE A C   1 
ATOM   1657 O  O   . ILE A 1 209 ? 6.550   0.387   22.705  1.00 10.05 ? 209 ILE A O   1 
ATOM   1658 C  CB  . ILE A 1 209 ? 5.651   2.590   24.455  1.00 10.62 ? 209 ILE A CB  1 
ATOM   1659 C  CG1 . ILE A 1 209 ? 5.818   3.863   25.291  1.00 12.17 ? 209 ILE A CG1 1 
ATOM   1660 C  CG2 . ILE A 1 209 ? 4.256   2.004   24.688  1.00 11.68 ? 209 ILE A CG2 1 
ATOM   1661 C  CD1 . ILE A 1 209 ? 5.000   5.066   24.780  1.00 13.62 ? 209 ILE A CD1 1 
ATOM   1662 N  N   . VAL A 1 210 ? 6.624   -0.878  24.566  1.00 9.23  ? 210 VAL A N   1 
ATOM   1663 C  CA  . VAL A 1 210 ? 6.660   -2.148  23.848  1.00 9.59  ? 210 VAL A CA  1 
ATOM   1664 C  C   . VAL A 1 210 ? 5.326   -2.858  24.084  1.00 10.42 ? 210 VAL A C   1 
ATOM   1665 O  O   . VAL A 1 210 ? 5.008   -3.155  25.238  1.00 10.78 ? 210 VAL A O   1 
ATOM   1666 C  CB  . VAL A 1 210 ? 7.876   -2.996  24.277  1.00 9.45  ? 210 VAL A CB  1 
ATOM   1667 C  CG1 . VAL A 1 210 ? 7.840   -4.330  23.537  1.00 9.64  ? 210 VAL A CG1 1 
ATOM   1668 C  CG2 . VAL A 1 210 ? 9.191   -2.249  23.968  1.00 11.15 ? 210 VAL A CG2 1 
ATOM   1669 N  N   . LEU A 1 211 ? 4.571   -3.103  23.029  1.00 10.48 ? 211 LEU A N   1 
ATOM   1670 C  CA  . LEU A 1 211 ? 3.271   -3.768  23.205  1.00 11.00 ? 211 LEU A CA  1 
ATOM   1671 C  C   . LEU A 1 211 ? 3.486   -5.241  23.555  1.00 10.58 ? 211 LEU A C   1 
ATOM   1672 O  O   . LEU A 1 211 ? 4.318   -5.953  23.017  1.00 11.22 ? 211 LEU A O   1 
ATOM   1673 C  CB  . LEU A 1 211 ? 2.483   -3.634  21.899  1.00 11.45 ? 211 LEU A CB  1 
ATOM   1674 C  CG  . LEU A 1 211 ? 2.066   -2.195  21.518  1.00 12.49 ? 211 LEU A CG  1 
ATOM   1675 C  CD1 . LEU A 1 211 ? 1.006   -2.237  20.399  1.00 13.65 ? 211 LEU A CD1 1 
ATOM   1676 C  CD2 . LEU A 1 211 ? 1.609   -1.392  22.734  1.00 12.37 ? 211 LEU A CD2 1 
ATOM   1677 N  N   . LYS A 1 212 ? 2.627   -5.738  24.451  1.00 10.98 ? 212 LYS A N   1 
ATOM   1678 C  CA  . LYS A 1 212 ? 2.674   -7.129  24.896  1.00 12.50 ? 212 LYS A CA  1 
ATOM   1679 C  C   . LYS A 1 212 ? 2.172   -8.086  23.825  1.00 11.92 ? 212 LYS A C   1 
ATOM   1680 O  O   . LYS A 1 212 ? 2.728   -9.155  23.614  1.00 13.93 ? 212 LYS A O   1 
ATOM   1681 C  CB  . LYS A 1 212 ? 1.845   -7.291  26.174  1.00 16.26 ? 212 LYS A CB  1 
ATOM   1682 C  CG  . LYS A 1 212 ? 1.491   -8.714  26.619  1.00 21.71 ? 212 LYS A CG  1 
ATOM   1683 C  CD  . LYS A 1 212 ? 0.360   -8.673  27.676  1.00 29.45 ? 212 LYS A CD  1 
ATOM   1684 C  CE  . LYS A 1 212 ? -1.085  -8.381  27.238  1.00 29.04 ? 212 LYS A CE  1 
ATOM   1685 N  NZ  . LYS A 1 212 ? -1.374  -8.029  25.814  1.00 34.38 ? 212 LYS A NZ  1 
ATOM   1686 N  N   . GLU A 1 213 ? 1.174   -7.662  23.047  1.00 11.18 ? 213 GLU A N   1 
ATOM   1687 C  CA  . GLU A 1 213 ? 0.588   -8.563  22.068  1.00 12.35 ? 213 GLU A CA  1 
ATOM   1688 C  C   . GLU A 1 213 ? 1.351   -8.460  20.740  1.00 11.53 ? 213 GLU A C   1 
ATOM   1689 O  O   . GLU A 1 213 ? 1.395   -7.385  20.131  1.00 11.08 ? 213 GLU A O   1 
ATOM   1690 C  CB  . GLU A 1 213 ? -0.890  -8.188  21.859  1.00 12.97 ? 213 GLU A CB  1 
ATOM   1691 C  CG  . GLU A 1 213 ? -1.589  -9.158  20.942  1.00 15.62 ? 213 GLU A CG  1 
ATOM   1692 C  CD  . GLU A 1 213 ? -3.022  -8.728  20.591  1.00 17.61 ? 213 GLU A CD  1 
ATOM   1693 O  OE1 . GLU A 1 213 ? -3.663  -8.098  21.408  1.00 17.66 ? 213 GLU A OE1 1 
ATOM   1694 O  OE2 . GLU A 1 213 ? -3.394  -8.926  19.413  1.00 27.10 ? 213 GLU A OE2 1 
ATOM   1695 N  N   A PRO A 1 214 ? 1.933   -9.567  20.231  0.50 10.90 ? 214 PRO A N   1 
ATOM   1696 N  N   B PRO A 1 214 ? 2.010   -9.533  20.280  0.50 12.05 ? 214 PRO A N   1 
ATOM   1697 C  CA  A PRO A 1 214 ? 2.630   -9.517  18.952  0.50 11.48 ? 214 PRO A CA  1 
ATOM   1698 C  CA  B PRO A 1 214 ? 2.652   -9.504  18.966  0.50 12.69 ? 214 PRO A CA  1 
ATOM   1699 C  C   A PRO A 1 214 ? 1.559   -9.471  17.871  0.50 12.51 ? 214 PRO A C   1 
ATOM   1700 C  C   B PRO A 1 214 ? 1.593   -9.524  17.866  0.50 13.29 ? 214 PRO A C   1 
ATOM   1701 O  O   A PRO A 1 214 ? 0.402   -9.828  18.096  0.50 13.31 ? 214 PRO A O   1 
ATOM   1702 O  O   B PRO A 1 214 ? 0.473   -9.987  18.068  0.50 13.91 ? 214 PRO A O   1 
ATOM   1703 C  CB  A PRO A 1 214 ? 3.369   -10.868 18.846  0.50 10.51 ? 214 PRO A CB  1 
ATOM   1704 C  CB  B PRO A 1 214 ? 3.481   -10.800 18.894  0.50 12.27 ? 214 PRO A CB  1 
ATOM   1705 C  CG  A PRO A 1 214 ? 2.471   -11.815 19.645  0.50 10.16 ? 214 PRO A CG  1 
ATOM   1706 C  CG  B PRO A 1 214 ? 3.480   -11.316 20.329  0.50 13.92 ? 214 PRO A CG  1 
ATOM   1707 C  CD  A PRO A 1 214 ? 1.903   -10.957 20.772  0.50 10.34 ? 214 PRO A CD  1 
ATOM   1708 C  CD  B PRO A 1 214 ? 2.197   -10.830 20.976  0.50 12.38 ? 214 PRO A CD  1 
ATOM   1709 N  N   . ILE A 1 215 ? 1.961   -9.035  16.678  1.00 12.11 ? 215 ILE A N   1 
ATOM   1710 C  CA  . ILE A 1 215 ? 1.159   -9.261  15.477  1.00 12.20 ? 215 ILE A CA  1 
ATOM   1711 C  C   . ILE A 1 215 ? 1.700   -10.479 14.765  1.00 11.59 ? 215 ILE A C   1 
ATOM   1712 O  O   . ILE A 1 215 ? 2.881   -10.834 14.874  1.00 13.35 ? 215 ILE A O   1 
ATOM   1713 C  CB  . ILE A 1 215 ? 1.135   -8.044  14.545  1.00 13.29 ? 215 ILE A CB  1 
ATOM   1714 C  CG1 . ILE A 1 215 ? 2.532   -7.650  14.038  1.00 13.08 ? 215 ILE A CG1 1 
ATOM   1715 C  CG2 . ILE A 1 215 ? 0.416   -6.871  15.239  1.00 13.86 ? 215 ILE A CG2 1 
ATOM   1716 C  CD1 . ILE A 1 215 ? 2.432   -6.656  12.840  1.00 13.24 ? 215 ILE A CD1 1 
ATOM   1717 N  N   A SER A 1 216 ? 0.793   -11.100 14.016  0.50 13.48 ? 216 SER A N   1 
ATOM   1718 N  N   B SER A 1 216 ? 0.799   -11.252 14.158  0.50 14.16 ? 216 SER A N   1 
ATOM   1719 C  CA  A SER A 1 216 ? 1.060   -12.283 13.221  0.50 12.36 ? 216 SER A CA  1 
ATOM   1720 C  CA  B SER A 1 216 ? 1.244   -12.381 13.352  0.50 13.57 ? 216 SER A CA  1 
ATOM   1721 C  C   A SER A 1 216 ? 1.317   -11.884 11.773  0.50 12.60 ? 216 SER A C   1 
ATOM   1722 C  C   B SER A 1 216 ? 1.345   -11.942 11.894  0.50 13.23 ? 216 SER A C   1 
ATOM   1723 O  O   A SER A 1 216 ? 0.522   -11.176 11.153  0.50 14.09 ? 216 SER A O   1 
ATOM   1724 O  O   B SER A 1 216 ? 0.462   -11.237 11.407  0.50 14.61 ? 216 SER A O   1 
ATOM   1725 C  CB  A SER A 1 216 ? -0.097  -13.271 13.360  0.50 12.50 ? 216 SER A CB  1 
ATOM   1726 C  CB  B SER A 1 216 ? 0.336   -13.582 13.532  0.50 14.99 ? 216 SER A CB  1 
ATOM   1727 O  OG  A SER A 1 216 ? 0.049   -13.962 14.594  0.50 13.62 ? 216 SER A OG  1 
ATOM   1728 O  OG  B SER A 1 216 ? 0.459   -14.471 12.433  0.50 19.47 ? 216 SER A OG  1 
ATOM   1729 N  N   . VAL A 1 217 ? 2.444   -12.344 11.244  1.00 11.89 ? 217 VAL A N   1 
ATOM   1730 C  CA  . VAL A 1 217 ? 2.712   -12.160 9.827   1.00 12.71 ? 217 VAL A CA  1 
ATOM   1731 C  C   . VAL A 1 217 ? 2.959   -13.526 9.198   1.00 12.88 ? 217 VAL A C   1 
ATOM   1732 O  O   . VAL A 1 217 ? 3.317   -14.465 9.904   1.00 12.33 ? 217 VAL A O   1 
ATOM   1733 C  CB  . VAL A 1 217 ? 3.919   -11.205 9.606   1.00 13.30 ? 217 VAL A CB  1 
ATOM   1734 C  CG1 . VAL A 1 217 ? 3.650   -9.864  10.312  1.00 14.34 ? 217 VAL A CG1 1 
ATOM   1735 C  CG2 . VAL A 1 217 ? 5.187   -11.837 10.161  1.00 14.04 ? 217 VAL A CG2 1 
ATOM   1736 N  N   . SER A 1 218 ? 2.815   -13.644 7.884   1.00 13.07 ? 218 SER A N   1 
ATOM   1737 C  CA  . SER A 1 218 ? 3.061   -14.963 7.321   1.00 13.53 ? 218 SER A CA  1 
ATOM   1738 C  C   . SER A 1 218 ? 4.533   -15.222 7.064   1.00 13.52 ? 218 SER A C   1 
ATOM   1739 O  O   . SER A 1 218 ? 5.369   -14.299 6.948   1.00 12.74 ? 218 SER A O   1 
ATOM   1740 C  CB  . SER A 1 218 ? 2.249   -15.176 6.071   1.00 14.32 ? 218 SER A CB  1 
ATOM   1741 O  OG  . SER A 1 218 ? 2.734   -14.305 5.041   1.00 14.75 ? 218 SER A OG  1 
ATOM   1742 N  N   . SER A 1 219 ? 4.882   -16.511 6.912   1.00 13.24 ? 219 SER A N   1 
ATOM   1743 C  CA  . SER A 1 219 ? 6.234   -16.843 6.573   1.00 14.26 ? 219 SER A CA  1 
ATOM   1744 C  C   . SER A 1 219 ? 6.613   -16.133 5.274   1.00 15.84 ? 219 SER A C   1 
ATOM   1745 O  O   . SER A 1 219 ? 7.759   -15.699 5.114   1.00 17.04 ? 219 SER A O   1 
ATOM   1746 C  CB  . SER A 1 219 ? 6.396   -18.374 6.533   1.00 16.82 ? 219 SER A CB  1 
ATOM   1747 O  OG  . SER A 1 219 ? 5.451   -18.947 5.645   1.00 22.62 ? 219 SER A OG  1 
ATOM   1748 N  N   . GLU A 1 220 ? 5.649   -16.023 4.357   1.00 15.11 ? 220 GLU A N   1 
ATOM   1749 C  CA  . GLU A 1 220 ? 5.952   -15.445 3.062   1.00 16.61 ? 220 GLU A CA  1 
ATOM   1750 C  C   . GLU A 1 220 ? 6.224   -13.942 3.171   1.00 16.52 ? 220 GLU A C   1 
ATOM   1751 O  O   . GLU A 1 220 ? 7.104   -13.456 2.462   1.00 16.91 ? 220 GLU A O   1 
ATOM   1752 C  CB  . GLU A 1 220 ? 4.805   -15.611 2.072   1.00 17.32 ? 220 GLU A CB  1 
ATOM   1753 C  CG  . GLU A 1 220 ? 4.633   -17.059 1.610   1.00 21.49 ? 220 GLU A CG  1 
ATOM   1754 C  CD  . GLU A 1 220 ? 3.808   -17.893 2.574   1.00 23.70 ? 220 GLU A CD  1 
ATOM   1755 O  OE1 . GLU A 1 220 ? 3.159   -17.355 3.514   1.00 21.51 ? 220 GLU A OE1 1 
ATOM   1756 O  OE2 . GLU A 1 220 ? 3.825   -19.143 2.397   1.00 31.38 ? 220 GLU A OE2 1 
ATOM   1757 N  N   . GLN A 1 221 ? 5.509   -13.249 4.066   1.00 14.35 ? 221 GLN A N   1 
ATOM   1758 C  CA  . GLN A 1 221 ? 5.781   -11.823 4.254   1.00 14.01 ? 221 GLN A CA  1 
ATOM   1759 C  C   . GLN A 1 221 ? 7.183   -11.595 4.806   1.00 15.22 ? 221 GLN A C   1 
ATOM   1760 O  O   . GLN A 1 221 ? 7.900   -10.718 4.340   1.00 13.71 ? 221 GLN A O   1 
ATOM   1761 C  CB  . GLN A 1 221 ? 4.747   -11.264 5.197   1.00 14.45 ? 221 GLN A CB  1 
ATOM   1762 C  CG  . GLN A 1 221 ? 3.391   -11.174 4.489   1.00 14.12 ? 221 GLN A CG  1 
ATOM   1763 C  CD  . GLN A 1 221 ? 2.284   -10.620 5.350   1.00 13.92 ? 221 GLN A CD  1 
ATOM   1764 O  OE1 . GLN A 1 221 ? 2.150   -11.012 6.506   1.00 13.07 ? 221 GLN A OE1 1 
ATOM   1765 N  NE2 . GLN A 1 221 ? 1.434   -9.762  4.801   1.00 13.62 ? 221 GLN A NE2 1 
ATOM   1766 N  N   . VAL A 1 222 ? 7.577   -12.375 5.818   1.00 14.45 ? 222 VAL A N   1 
ATOM   1767 C  CA  . VAL A 1 222 ? 8.907   -12.124 6.376   1.00 14.21 ? 222 VAL A CA  1 
ATOM   1768 C  C   . VAL A 1 222 ? 10.020  -12.577 5.420   1.00 16.50 ? 222 VAL A C   1 
ATOM   1769 O  O   . VAL A 1 222 ? 11.109  -11.996 5.361   1.00 15.66 ? 222 VAL A O   1 
ATOM   1770 C  CB  . VAL A 1 222 ? 9.018   -12.680 7.816   1.00 15.62 ? 222 VAL A CB  1 
ATOM   1771 C  CG1 . VAL A 1 222 ? 8.897   -14.184 7.802   1.00 18.36 ? 222 VAL A CG1 1 
ATOM   1772 C  CG2 . VAL A 1 222 ? 10.325  -12.246 8.488   1.00 19.11 ? 222 VAL A CG2 1 
ATOM   1773 N  N   A LEU A 1 223 ? 9.732   -13.604 4.603   0.50 16.25 ? 223 LEU A N   1 
ATOM   1774 N  N   B LEU A 1 223 ? 9.725   -13.613 4.624   0.50 16.28 ? 223 LEU A N   1 
ATOM   1775 C  CA  A LEU A 1 223 ? 10.758  -14.035 3.671   0.50 16.10 ? 223 LEU A CA  1 
ATOM   1776 C  CA  B LEU A 1 223 ? 10.687  -14.052 3.635   0.50 16.26 ? 223 LEU A CA  1 
ATOM   1777 C  C   A LEU A 1 223 ? 11.045  -12.921 2.661   0.50 15.83 ? 223 LEU A C   1 
ATOM   1778 C  C   B LEU A 1 223 ? 11.045  -12.892 2.711   0.50 15.75 ? 223 LEU A C   1 
ATOM   1779 O  O   A LEU A 1 223 ? 12.187  -12.800 2.223   0.50 15.78 ? 223 LEU A O   1 
ATOM   1780 O  O   B LEU A 1 223 ? 12.210  -12.739 2.353   0.50 15.73 ? 223 LEU A O   1 
ATOM   1781 C  CB  A LEU A 1 223 ? 10.389  -15.391 3.041   0.50 19.00 ? 223 LEU A CB  1 
ATOM   1782 C  CB  B LEU A 1 223 ? 10.066  -15.218 2.860   0.50 18.62 ? 223 LEU A CB  1 
ATOM   1783 C  CG  A LEU A 1 223 ? 9.819   -15.403 1.623   0.50 20.85 ? 223 LEU A CG  1 
ATOM   1784 C  CG  B LEU A 1 223 ? 10.304  -16.591 3.489   0.50 21.00 ? 223 LEU A CG  1 
ATOM   1785 C  CD1 A LEU A 1 223 ? 10.735  -14.677 0.664   0.50 21.62 ? 223 LEU A CD1 1 
ATOM   1786 C  CD1 B LEU A 1 223 ? 9.486   -17.643 2.757   0.50 22.42 ? 223 LEU A CD1 1 
ATOM   1787 C  CD2 A LEU A 1 223 ? 9.620   -16.833 1.132   0.50 21.17 ? 223 LEU A CD2 1 
ATOM   1788 C  CD2 B LEU A 1 223 ? 11.780  -16.953 3.478   0.50 20.35 ? 223 LEU A CD2 1 
ATOM   1789 N  N   . LYS A 1 224 ? 10.047  -12.078 2.359   1.00 15.99 ? 224 LYS A N   1 
ATOM   1790 C  CA  . LYS A 1 224 ? 10.266  -10.949 1.467   1.00 16.01 ? 224 LYS A CA  1 
ATOM   1791 C  C   . LYS A 1 224 ? 11.135  -9.881  2.136   1.00 15.54 ? 224 LYS A C   1 
ATOM   1792 O  O   . LYS A 1 224 ? 11.920  -9.239  1.454   1.00 16.26 ? 224 LYS A O   1 
ATOM   1793 C  CB  . LYS A 1 224 ? 8.928   -10.465 0.886   1.00 18.92 ? 224 LYS A CB  1 
ATOM   1794 C  CG  . LYS A 1 224 ? 8.255   -11.537 0.007   1.00 22.75 ? 224 LYS A CG  1 
ATOM   1795 C  CD  . LYS A 1 224 ? 7.129   -11.054 -0.905  1.00 29.78 ? 224 LYS A CD  1 
ATOM   1796 C  CE  . LYS A 1 224 ? 6.540   -12.147 -1.789  1.00 30.74 ? 224 LYS A CE  1 
ATOM   1797 N  NZ  . LYS A 1 224 ? 5.273   -11.699 -2.428  1.00 35.84 ? 224 LYS A NZ  1 
ATOM   1798 N  N   . PHE A 1 225 ? 11.030  -9.679  3.464   1.00 13.30 ? 225 PHE A N   1 
ATOM   1799 C  CA  . PHE A 1 225 ? 11.977  -8.785  4.110   1.00 12.70 ? 225 PHE A CA  1 
ATOM   1800 C  C   . PHE A 1 225 ? 13.414  -9.255  3.900   1.00 12.13 ? 225 PHE A C   1 
ATOM   1801 O  O   . PHE A 1 225 ? 14.315  -8.447  3.682   1.00 12.51 ? 225 PHE A O   1 
ATOM   1802 C  CB  . PHE A 1 225 ? 11.813  -8.779  5.641   1.00 11.31 ? 225 PHE A CB  1 
ATOM   1803 C  CG  . PHE A 1 225 ? 10.587  -8.093  6.220   1.00 13.12 ? 225 PHE A CG  1 
ATOM   1804 C  CD1 . PHE A 1 225 ? 9.538   -7.610  5.452   1.00 13.29 ? 225 PHE A CD1 1 
ATOM   1805 C  CD2 . PHE A 1 225 ? 10.513  -7.908  7.605   1.00 13.44 ? 225 PHE A CD2 1 
ATOM   1806 C  CE1 . PHE A 1 225 ? 8.444   -7.006  6.068   1.00 15.32 ? 225 PHE A CE1 1 
ATOM   1807 C  CE2 . PHE A 1 225 ? 9.434   -7.293  8.232   1.00 15.88 ? 225 PHE A CE2 1 
ATOM   1808 C  CZ  . PHE A 1 225 ? 8.417   -6.792  7.438   1.00 13.43 ? 225 PHE A CZ  1 
ATOM   1809 N  N   . ARG A 1 226 ? 13.616  -10.581 3.943   1.00 11.88 ? 226 ARG A N   1 
ATOM   1810 C  CA  . ARG A 1 226 ? 14.939  -11.176 3.842   1.00 12.91 ? 226 ARG A CA  1 
ATOM   1811 C  C   . ARG A 1 226 ? 15.529  -11.174 2.434   1.00 15.16 ? 226 ARG A C   1 
ATOM   1812 O  O   . ARG A 1 226 ? 16.708  -11.522 2.295   1.00 15.53 ? 226 ARG A O   1 
ATOM   1813 C  CB  . ARG A 1 226 ? 14.896  -12.617 4.374   1.00 14.49 ? 226 ARG A CB  1 
ATOM   1814 C  CG  . ARG A 1 226 ? 14.373  -12.743 5.807   1.00 13.57 ? 226 ARG A CG  1 
ATOM   1815 C  CD  . ARG A 1 226 ? 14.541  -14.185 6.272   1.00 14.86 ? 226 ARG A CD  1 
ATOM   1816 N  NE  . ARG A 1 226 ? 13.890  -14.350 7.598   1.00 15.05 ? 226 ARG A NE  1 
ATOM   1817 C  CZ  . ARG A 1 226 ? 12.948  -15.239 7.890   1.00 14.83 ? 226 ARG A CZ  1 
ATOM   1818 N  NH1 . ARG A 1 226 ? 12.491  -16.052 6.942   1.00 17.69 ? 226 ARG A NH1 1 
ATOM   1819 N  NH2 . ARG A 1 226 ? 12.466  -15.300 9.116   1.00 13.65 ? 226 ARG A NH2 1 
ATOM   1820 N  N   . LYS A 1 227 ? 14.767  -10.708 1.441   1.00 13.99 ? 227 LYS A N   1 
ATOM   1821 C  CA  . LYS A 1 227 ? 15.321  -10.624 0.094   1.00 15.48 ? 227 LYS A CA  1 
ATOM   1822 C  C   . LYS A 1 227 ? 15.877  -9.231  -0.164  1.00 15.85 ? 227 LYS A C   1 
ATOM   1823 O  O   . LYS A 1 227 ? 16.583  -9.040  -1.154  1.00 17.06 ? 227 LYS A O   1 
ATOM   1824 C  CB  . LYS A 1 227 ? 14.197  -10.879 -0.910  1.00 16.63 ? 227 LYS A CB  1 
ATOM   1825 C  CG  . LYS A 1 227 ? 13.696  -12.322 -0.898  1.00 20.81 ? 227 LYS A CG  1 
ATOM   1826 C  CD  . LYS A 1 227 ? 12.661  -12.609 -1.971  1.00 28.63 ? 227 LYS A CD  1 
ATOM   1827 C  CE  . LYS A 1 227 ? 13.214  -13.366 -3.166  1.00 36.04 ? 227 LYS A CE  1 
ATOM   1828 N  NZ  . LYS A 1 227 ? 12.652  -12.884 -4.456  1.00 40.00 ? 227 LYS A NZ  1 
ATOM   1829 N  N   . LEU A 1 228 ? 15.629  -8.263  0.733   1.00 14.07 ? 228 LEU A N   1 
ATOM   1830 C  CA  . LEU A 1 228 ? 16.356  -7.006  0.656   1.00 13.76 ? 228 LEU A CA  1 
ATOM   1831 C  C   . LEU A 1 228 ? 17.858  -7.214  0.782   1.00 13.77 ? 228 LEU A C   1 
ATOM   1832 O  O   . LEU A 1 228 ? 18.391  -8.230  1.233   1.00 14.69 ? 228 LEU A O   1 
ATOM   1833 C  CB  . LEU A 1 228 ? 15.861  -6.053  1.750   1.00 13.96 ? 228 LEU A CB  1 
ATOM   1834 C  CG  . LEU A 1 228 ? 14.420  -5.623  1.568   1.00 14.63 ? 228 LEU A CG  1 
ATOM   1835 C  CD1 . LEU A 1 228 ? 13.909  -4.964  2.859   1.00 16.17 ? 228 LEU A CD1 1 
ATOM   1836 C  CD2 . LEU A 1 228 ? 14.369  -4.598  0.428   1.00 13.67 ? 228 LEU A CD2 1 
ATOM   1837 N  N   . ASN A 1 229 ? 18.577  -6.133  0.461   1.00 14.67 ? 229 ASN A N   1 
ATOM   1838 C  CA  . ASN A 1 229 ? 20.031  -6.141  0.444   1.00 14.31 ? 229 ASN A CA  1 
ATOM   1839 C  C   . ASN A 1 229 ? 20.573  -4.968  1.262   1.00 15.00 ? 229 ASN A C   1 
ATOM   1840 O  O   . ASN A 1 229 ? 20.066  -3.848  1.168   1.00 15.11 ? 229 ASN A O   1 
ATOM   1841 C  CB  . ASN A 1 229 ? 20.612  -5.940  -0.973  1.00 17.27 ? 229 ASN A CB  1 
ATOM   1842 C  CG  . ASN A 1 229 ? 20.529  -7.110  -1.942  1.00 21.61 ? 229 ASN A CG  1 
ATOM   1843 O  OD1 . ASN A 1 229 ? 21.077  -6.985  -3.049  1.00 22.56 ? 229 ASN A OD1 1 
ATOM   1844 N  ND2 . ASN A 1 229 ? 19.862  -8.211  -1.604  1.00 19.54 ? 229 ASN A ND2 1 
ATOM   1845 N  N   . PHE A 1 230 ? 21.617  -5.273  2.019   1.00 14.97 ? 230 PHE A N   1 
ATOM   1846 C  CA  . PHE A 1 230 ? 22.327  -4.221  2.722   1.00 15.94 ? 230 PHE A CA  1 
ATOM   1847 C  C   . PHE A 1 230 ? 23.132  -3.364  1.749   1.00 18.10 ? 230 PHE A C   1 
ATOM   1848 O  O   . PHE A 1 230 ? 23.310  -2.152  1.969   1.00 17.76 ? 230 PHE A O   1 
ATOM   1849 C  CB  . PHE A 1 230 ? 23.340  -4.851  3.671   1.00 15.29 ? 230 PHE A CB  1 
ATOM   1850 C  CG  . PHE A 1 230 ? 22.838  -5.431  4.988   1.00 15.07 ? 230 PHE A CG  1 
ATOM   1851 C  CD1 . PHE A 1 230 ? 22.063  -4.693  5.884   1.00 15.73 ? 230 PHE A CD1 1 
ATOM   1852 C  CD2 . PHE A 1 230 ? 23.142  -6.735  5.304   1.00 14.38 ? 230 PHE A CD2 1 
ATOM   1853 C  CE1 . PHE A 1 230 ? 21.669  -5.233  7.112   1.00 15.57 ? 230 PHE A CE1 1 
ATOM   1854 C  CE2 . PHE A 1 230 ? 22.706  -7.302  6.501   1.00 14.12 ? 230 PHE A CE2 1 
ATOM   1855 C  CZ  . PHE A 1 230 ? 22.012  -6.536  7.423   1.00 14.82 ? 230 PHE A CZ  1 
ATOM   1856 N  N   . ASN A 1 231 ? 23.635  -4.008  0.684   1.00 16.88 ? 231 ASN A N   1 
ATOM   1857 C  CA  . ASN A 1 231 ? 24.503  -3.337  -0.285  1.00 16.79 ? 231 ASN A CA  1 
ATOM   1858 C  C   . ASN A 1 231 ? 23.728  -2.444  -1.249  1.00 16.45 ? 231 ASN A C   1 
ATOM   1859 O  O   . ASN A 1 231 ? 22.509  -2.528  -1.420  1.00 16.84 ? 231 ASN A O   1 
ATOM   1860 C  CB  . ASN A 1 231 ? 25.224  -4.416  -1.074  1.00 16.89 ? 231 ASN A CB  1 
ATOM   1861 C  CG  . ASN A 1 231 ? 24.229  -5.339  -1.744  1.00 17.82 ? 231 ASN A CG  1 
ATOM   1862 O  OD1 . ASN A 1 231 ? 23.712  -6.256  -1.098  1.00 19.35 ? 231 ASN A OD1 1 
ATOM   1863 N  ND2 . ASN A 1 231 ? 23.942  -5.129  -3.034  1.00 16.47 ? 231 ASN A ND2 1 
ATOM   1864 N  N   . GLY A 1 232 ? 24.501  -1.514  -1.856  1.00 17.48 ? 232 GLY A N   1 
ATOM   1865 C  CA  . GLY A 1 232 ? 24.038  -0.704  -2.976  1.00 18.24 ? 232 GLY A CA  1 
ATOM   1866 C  C   . GLY A 1 232 ? 23.971  -1.501  -4.279  1.00 17.24 ? 232 GLY A C   1 
ATOM   1867 O  O   . GLY A 1 232 ? 24.642  -2.533  -4.387  1.00 17.52 ? 232 GLY A O   1 
ATOM   1868 N  N   . GLU A 1 233 ? 23.147  -1.034  -5.232  1.00 17.41 ? 233 GLU A N   1 
ATOM   1869 C  CA  . GLU A 1 233 ? 23.127  -1.630  -6.563  1.00 18.26 ? 233 GLU A CA  1 
ATOM   1870 C  C   . GLU A 1 233 ? 24.543  -1.659  -7.126  1.00 18.26 ? 233 GLU A C   1 
ATOM   1871 O  O   . GLU A 1 233 ? 25.322  -0.730  -6.982  1.00 18.80 ? 233 GLU A O   1 
ATOM   1872 C  CB  . GLU A 1 233 ? 22.123  -0.894  -7.456  1.00 19.92 ? 233 GLU A CB  1 
ATOM   1873 C  CG  . GLU A 1 233 ? 22.012  -1.436  -8.879  1.00 21.26 ? 233 GLU A CG  1 
ATOM   1874 C  CD  . GLU A 1 233 ? 21.139  -0.540  -9.734  1.00 28.97 ? 233 GLU A CD  1 
ATOM   1875 O  OE1 . GLU A 1 233 ? 20.840  0.602   -9.300  1.00 29.87 ? 233 GLU A OE1 1 
ATOM   1876 O  OE2 . GLU A 1 233 ? 20.801  -0.959  -10.855 1.00 34.21 ? 233 GLU A OE2 1 
ATOM   1877 N  N   . GLY A 1 234 ? 24.853  -2.764  -7.789  1.00 20.56 ? 234 GLY A N   1 
ATOM   1878 C  CA  . GLY A 1 234 ? 26.150  -2.872  -8.425  1.00 22.68 ? 234 GLY A CA  1 
ATOM   1879 C  C   . GLY A 1 234 ? 27.230  -3.367  -7.474  1.00 23.84 ? 234 GLY A C   1 
ATOM   1880 O  O   . GLY A 1 234 ? 28.384  -3.499  -7.883  1.00 25.71 ? 234 GLY A O   1 
ATOM   1881 N  N   . GLU A 1 235 ? 26.873  -3.626  -6.205  1.00 21.16 ? 235 GLU A N   1 
ATOM   1882 C  CA  . GLU A 1 235 ? 27.864  -4.139  -5.272  1.00 20.83 ? 235 GLU A CA  1 
ATOM   1883 C  C   . GLU A 1 235 ? 27.467  -5.565  -4.934  1.00 21.07 ? 235 GLU A C   1 
ATOM   1884 O  O   . GLU A 1 235 ? 26.312  -5.963  -5.158  1.00 21.64 ? 235 GLU A O   1 
ATOM   1885 C  CB  . GLU A 1 235 ? 27.909  -3.337  -3.967  1.00 21.95 ? 235 GLU A CB  1 
ATOM   1886 C  CG  . GLU A 1 235 ? 28.210  -1.864  -4.123  1.00 25.07 ? 235 GLU A CG  1 
ATOM   1887 C  CD  . GLU A 1 235 ? 28.052  -1.103  -2.818  1.00 31.75 ? 235 GLU A CD  1 
ATOM   1888 O  OE1 . GLU A 1 235 ? 27.173  -1.487  -2.001  1.00 25.18 ? 235 GLU A OE1 1 
ATOM   1889 O  OE2 . GLU A 1 235 ? 28.838  -0.165  -2.577  1.00 35.87 ? 235 GLU A OE2 1 
ATOM   1890 N  N   . PRO A 1 236 ? 28.421  -6.375  -4.433  1.00 19.81 ? 236 PRO A N   1 
ATOM   1891 C  CA  . PRO A 1 236 ? 28.174  -7.773  -4.116  1.00 19.80 ? 236 PRO A CA  1 
ATOM   1892 C  C   . PRO A 1 236 ? 26.988  -7.880  -3.163  1.00 18.61 ? 236 PRO A C   1 
ATOM   1893 O  O   . PRO A 1 236 ? 26.820  -7.048  -2.271  1.00 19.58 ? 236 PRO A O   1 
ATOM   1894 C  CB  . PRO A 1 236 ? 29.449  -8.178  -3.378  1.00 21.48 ? 236 PRO A CB  1 
ATOM   1895 C  CG  . PRO A 1 236 ? 30.497  -7.326  -4.029  1.00 23.01 ? 236 PRO A CG  1 
ATOM   1896 C  CD  . PRO A 1 236 ? 29.810  -5.979  -4.141  1.00 22.58 ? 236 PRO A CD  1 
ATOM   1897 N  N   . GLU A 1 237 ? 26.206  -8.923  -3.386  1.00 18.87 ? 237 GLU A N   1 
ATOM   1898 C  CA  . GLU A 1 237 ? 24.928  -9.083  -2.719  1.00 19.14 ? 237 GLU A CA  1 
ATOM   1899 C  C   . GLU A 1 237 ? 25.172  -9.540  -1.286  1.00 20.07 ? 237 GLU A C   1 
ATOM   1900 O  O   . GLU A 1 237 ? 25.727  -10.598 -1.046  1.00 16.61 ? 237 GLU A O   1 
ATOM   1901 C  CB  . GLU A 1 237 ? 24.048  -10.134 -3.397  1.00 19.07 ? 237 GLU A CB  1 
ATOM   1902 C  CG  . GLU A 1 237 ? 22.657  -10.136 -2.768  1.00 22.59 ? 237 GLU A CG  1 
ATOM   1903 C  CD  . GLU A 1 237 ? 21.553  -10.815 -3.562  1.00 27.08 ? 237 GLU A CD  1 
ATOM   1904 O  OE1 . GLU A 1 237 ? 21.869  -11.408 -4.618  1.00 33.84 ? 237 GLU A OE1 1 
ATOM   1905 O  OE2 . GLU A 1 237 ? 20.378  -10.690 -3.160  1.00 25.52 ? 237 GLU A OE2 1 
ATOM   1906 N  N   . GLU A 1 238 ? 24.612  -8.766  -0.351  1.00 18.15 ? 238 GLU A N   1 
ATOM   1907 C  CA  . GLU A 1 238 ? 24.605  -9.176  1.047   1.00 20.04 ? 238 GLU A CA  1 
ATOM   1908 C  C   . GLU A 1 238 ? 23.156  -9.086  1.517   1.00 15.22 ? 238 GLU A C   1 
ATOM   1909 O  O   . GLU A 1 238 ? 22.605  -7.975  1.550   1.00 16.78 ? 238 GLU A O   1 
ATOM   1910 C  CB  . GLU A 1 238 ? 25.433  -8.231  1.943   1.00 24.19 ? 238 GLU A CB  1 
ATOM   1911 C  CG  . GLU A 1 238 ? 26.844  -7.832  1.482   1.00 32.05 ? 238 GLU A CG  1 
ATOM   1912 C  CD  . GLU A 1 238 ? 27.565  -6.763  2.320   1.00 41.25 ? 238 GLU A CD  1 
ATOM   1913 O  OE1 . GLU A 1 238 ? 27.232  -5.542  2.201   1.00 43.90 ? 238 GLU A OE1 1 
ATOM   1914 O  OE2 . GLU A 1 238 ? 28.460  -7.140  3.101   1.00 47.97 ? 238 GLU A OE2 1 
ATOM   1915 N  N   . LEU A 1 239 ? 22.533  -10.248 1.824   1.00 14.86 ? 239 LEU A N   1 
ATOM   1916 C  CA  . LEU A 1 239 ? 21.128  -10.215 2.213   1.00 13.72 ? 239 LEU A CA  1 
ATOM   1917 C  C   . LEU A 1 239 ? 20.971  -9.421  3.519   1.00 12.28 ? 239 LEU A C   1 
ATOM   1918 O  O   . LEU A 1 239 ? 21.745  -9.614  4.477   1.00 14.23 ? 239 LEU A O   1 
ATOM   1919 C  CB  . LEU A 1 239 ? 20.626  -11.641 2.417   1.00 13.80 ? 239 LEU A CB  1 
ATOM   1920 C  CG  . LEU A 1 239 ? 20.600  -12.467 1.133   1.00 14.43 ? 239 LEU A CG  1 
ATOM   1921 C  CD1 . LEU A 1 239 ? 20.130  -13.875 1.452   1.00 17.98 ? 239 LEU A CD1 1 
ATOM   1922 C  CD2 . LEU A 1 239 ? 19.613  -11.884 0.152   1.00 15.84 ? 239 LEU A CD2 1 
ATOM   1923 N  N   . MET A 1 240 ? 19.936  -8.600  3.517   1.00 12.89 ? 240 MET A N   1 
ATOM   1924 C  CA  . MET A 1 240 ? 19.589  -7.831  4.710   1.00 12.91 ? 240 MET A CA  1 
ATOM   1925 C  C   . MET A 1 240 ? 18.788  -8.733  5.650   1.00 12.33 ? 240 MET A C   1 
ATOM   1926 O  O   . MET A 1 240 ? 17.587  -8.886  5.529   1.00 13.67 ? 240 MET A O   1 
ATOM   1927 C  CB  . MET A 1 240 ? 18.751  -6.619  4.298   1.00 12.99 ? 240 MET A CB  1 
ATOM   1928 C  CG  . MET A 1 240 ? 18.422  -5.636  5.495   1.00 12.68 ? 240 MET A CG  1 
ATOM   1929 S  SD  . MET A 1 240 ? 17.541  -4.201  5.058   1.00 15.19 ? 240 MET A SD  1 
ATOM   1930 C  CE  . MET A 1 240 ? 18.802  -3.198  4.266   1.00 13.93 ? 240 MET A CE  1 
ATOM   1931 N  N   . VAL A 1 241 ? 19.525  -9.326  6.572   1.00 11.53 ? 241 VAL A N   1 
ATOM   1932 C  CA  . VAL A 1 241 ? 18.986  -10.200 7.608   1.00 12.06 ? 241 VAL A CA  1 
ATOM   1933 C  C   . VAL A 1 241 ? 19.773  -9.941  8.879   1.00 12.31 ? 241 VAL A C   1 
ATOM   1934 O  O   . VAL A 1 241 ? 20.918  -9.536  8.848   1.00 11.93 ? 241 VAL A O   1 
ATOM   1935 C  CB  . VAL A 1 241 ? 19.072  -11.696 7.260   1.00 12.25 ? 241 VAL A CB  1 
ATOM   1936 C  CG1 . VAL A 1 241 ? 18.197  -12.009 6.041   1.00 13.27 ? 241 VAL A CG1 1 
ATOM   1937 C  CG2 . VAL A 1 241 ? 20.501  -12.181 7.086   1.00 13.38 ? 241 VAL A CG2 1 
ATOM   1938 N  N   . ASP A 1 242 ? 19.118  -10.215 10.022  1.00 11.10 ? 242 ASP A N   1 
ATOM   1939 C  CA  . ASP A 1 242 ? 19.821  -10.097 11.307  1.00 11.39 ? 242 ASP A CA  1 
ATOM   1940 C  C   . ASP A 1 242 ? 20.280  -8.674  11.598  1.00 10.85 ? 242 ASP A C   1 
ATOM   1941 O  O   . ASP A 1 242 ? 21.401  -8.461  12.065  1.00 12.28 ? 242 ASP A O   1 
ATOM   1942 C  CB  . ASP A 1 242 ? 20.889  -11.163 11.556  1.00 11.97 ? 242 ASP A CB  1 
ATOM   1943 C  CG  . ASP A 1 242 ? 20.276  -12.541 11.621  1.00 12.53 ? 242 ASP A CG  1 
ATOM   1944 O  OD1 . ASP A 1 242 ? 19.200  -12.713 12.242  1.00 11.57 ? 242 ASP A OD1 1 
ATOM   1945 O  OD2 . ASP A 1 242 ? 20.878  -13.470 11.009  1.00 15.11 ? 242 ASP A OD2 1 
ATOM   1946 N  N   . ASN A 1 243 ? 19.426  -7.722  11.293  1.00 10.61 ? 243 ASN A N   1 
ATOM   1947 C  CA  . ASN A 1 243 ? 19.748  -6.327  11.554  1.00 10.96 ? 243 ASN A CA  1 
ATOM   1948 C  C   . ASN A 1 243 ? 19.119  -5.904  12.883  1.00 10.03 ? 243 ASN A C   1 
ATOM   1949 O  O   . ASN A 1 243 ? 18.466  -4.876  12.942  1.00 11.08 ? 243 ASN A O   1 
ATOM   1950 C  CB  . ASN A 1 243 ? 19.204  -5.435  10.424  1.00 11.40 ? 243 ASN A CB  1 
ATOM   1951 C  CG  . ASN A 1 243 ? 17.725  -5.579  10.132  1.00 12.44 ? 243 ASN A CG  1 
ATOM   1952 O  OD1 . ASN A 1 243 ? 17.088  -6.494  10.657  1.00 13.03 ? 243 ASN A OD1 1 
ATOM   1953 N  ND2 . ASN A 1 243 ? 17.181  -4.717  9.260   1.00 14.81 ? 243 ASN A ND2 1 
ATOM   1954 N  N   . TRP A 1 244 ? 19.408  -6.668  13.927  1.00 9.94  ? 244 TRP A N   1 
ATOM   1955 C  CA  . TRP A 1 244 ? 18.944  -6.432  15.286  1.00 10.36 ? 244 TRP A CA  1 
ATOM   1956 C  C   . TRP A 1 244 ? 20.115  -6.328  16.242  1.00 11.39 ? 244 TRP A C   1 
ATOM   1957 O  O   . TRP A 1 244 ? 21.116  -7.021  16.054  1.00 11.48 ? 244 TRP A O   1 
ATOM   1958 C  CB  . TRP A 1 244 ? 17.953  -7.517  15.770  1.00 10.54 ? 244 TRP A CB  1 
ATOM   1959 C  CG  . TRP A 1 244 ? 18.431  -8.925  15.558  1.00 10.63 ? 244 TRP A CG  1 
ATOM   1960 C  CD1 . TRP A 1 244 ? 18.319  -9.652  14.414  1.00 11.14 ? 244 TRP A CD1 1 
ATOM   1961 C  CD2 . TRP A 1 244 ? 18.999  -9.799  16.549  1.00 10.46 ? 244 TRP A CD2 1 
ATOM   1962 N  NE1 . TRP A 1 244 ? 18.822  -10.910 14.623  1.00 10.72 ? 244 TRP A NE1 1 
ATOM   1963 C  CE2 . TRP A 1 244 ? 19.266  -11.027 15.920  1.00 10.80 ? 244 TRP A CE2 1 
ATOM   1964 C  CE3 . TRP A 1 244 ? 19.314  -9.644  17.908  1.00 10.99 ? 244 TRP A CE3 1 
ATOM   1965 C  CZ2 . TRP A 1 244 ? 19.824  -12.113 16.602  1.00 11.09 ? 244 TRP A CZ2 1 
ATOM   1966 C  CZ3 . TRP A 1 244 ? 19.848  -10.715 18.571  1.00 11.91 ? 244 TRP A CZ3 1 
ATOM   1967 C  CH2 . TRP A 1 244 ? 20.116  -11.927 17.932  1.00 11.95 ? 244 TRP A CH2 1 
ATOM   1968 N  N   . ARG A 1 245 ? 19.991  -5.426  17.220  1.00 10.50 ? 245 ARG A N   1 
ATOM   1969 C  CA  . ARG A 1 245 ? 20.983  -5.337  18.297  1.00 10.66 ? 245 ARG A CA  1 
ATOM   1970 C  C   . ARG A 1 245 ? 20.536  -6.268  19.413  1.00 11.30 ? 245 ARG A C   1 
ATOM   1971 O  O   . ARG A 1 245 ? 19.331  -6.306  19.711  1.00 11.52 ? 245 ARG A O   1 
ATOM   1972 C  CB  . ARG A 1 245 ? 21.034  -3.900  18.823  1.00 11.08 ? 245 ARG A CB  1 
ATOM   1973 C  CG  . ARG A 1 245 ? 22.162  -3.705  19.836  1.00 11.04 ? 245 ARG A CG  1 
ATOM   1974 C  CD  . ARG A 1 245 ? 22.087  -2.330  20.480  1.00 10.73 ? 245 ARG A CD  1 
ATOM   1975 N  NE  . ARG A 1 245 ? 23.358  -2.050  21.204  1.00 11.76 ? 245 ARG A NE  1 
ATOM   1976 C  CZ  . ARG A 1 245 ? 23.528  -1.056  22.069  1.00 12.49 ? 245 ARG A CZ  1 
ATOM   1977 N  NH1 . ARG A 1 245 ? 22.529  -0.234  22.336  1.00 12.60 ? 245 ARG A NH1 1 
ATOM   1978 N  NH2 . ARG A 1 245 ? 24.696  -0.889  22.662  1.00 12.63 ? 245 ARG A NH2 1 
ATOM   1979 N  N   . PRO A 1 246 ? 21.398  -7.060  20.063  1.00 11.70 ? 246 PRO A N   1 
ATOM   1980 C  CA  . PRO A 1 246 ? 20.972  -7.922  21.156  1.00 11.50 ? 246 PRO A CA  1 
ATOM   1981 C  C   . PRO A 1 246 ? 20.634  -7.108  22.402  1.00 10.72 ? 246 PRO A C   1 
ATOM   1982 O  O   . PRO A 1 246 ? 20.996  -5.934  22.534  1.00 11.82 ? 246 PRO A O   1 
ATOM   1983 C  CB  . PRO A 1 246 ? 22.226  -8.760  21.502  1.00 13.70 ? 246 PRO A CB  1 
ATOM   1984 C  CG  . PRO A 1 246 ? 23.100  -8.647  20.258  1.00 16.54 ? 246 PRO A CG  1 
ATOM   1985 C  CD  . PRO A 1 246 ? 22.800  -7.293  19.646  1.00 13.12 ? 246 PRO A CD  1 
ATOM   1986 N  N   . ALA A 1 247 ? 19.973  -7.795  23.359  1.00 11.34 ? 247 ALA A N   1 
ATOM   1987 C  CA  . ALA A 1 247 ? 19.643  -7.174  24.626  1.00 11.03 ? 247 ALA A CA  1 
ATOM   1988 C  C   . ALA A 1 247 ? 20.887  -6.641  25.319  1.00 11.38 ? 247 ALA A C   1 
ATOM   1989 O  O   . ALA A 1 247 ? 21.921  -7.336  25.382  1.00 13.57 ? 247 ALA A O   1 
ATOM   1990 C  CB  . ALA A 1 247 ? 18.844  -8.156  25.474  1.00 13.20 ? 247 ALA A CB  1 
ATOM   1991 N  N   . GLN A 1 248 ? 20.712  -5.463  25.925  1.00 11.04 ? 248 GLN A N   1 
ATOM   1992 C  CA  . GLN A 1 248 ? 21.780  -4.762  26.625  1.00 12.80 ? 248 GLN A CA  1 
ATOM   1993 C  C   . GLN A 1 248 ? 21.476  -4.789  28.115  1.00 13.16 ? 248 GLN A C   1 
ATOM   1994 O  O   . GLN A 1 248 ? 20.335  -4.981  28.514  1.00 13.61 ? 248 GLN A O   1 
ATOM   1995 C  CB  . GLN A 1 248 ? 21.833  -3.321  26.148  1.00 12.32 ? 248 GLN A CB  1 
ATOM   1996 C  CG  . GLN A 1 248 ? 22.135  -3.266  24.642  1.00 12.95 ? 248 GLN A CG  1 
ATOM   1997 C  CD  . GLN A 1 248 ? 23.459  -3.932  24.302  1.00 14.63 ? 248 GLN A CD  1 
ATOM   1998 O  OE1 . GLN A 1 248 ? 24.505  -3.682  24.934  1.00 16.56 ? 248 GLN A OE1 1 
ATOM   1999 N  NE2 . GLN A 1 248 ? 23.427  -4.887  23.376  1.00 15.06 ? 248 GLN A NE2 1 
ATOM   2000 N  N   . PRO A 1 249 ? 22.471  -4.500  28.993  1.00 15.03 ? 249 PRO A N   1 
ATOM   2001 C  CA  . PRO A 1 249 ? 22.218  -4.570  30.430  1.00 14.92 ? 249 PRO A CA  1 
ATOM   2002 C  C   . PRO A 1 249 ? 21.148  -3.573  30.889  1.00 14.25 ? 249 PRO A C   1 
ATOM   2003 O  O   . PRO A 1 249 ? 21.173  -2.402  30.508  1.00 15.40 ? 249 PRO A O   1 
ATOM   2004 C  CB  . PRO A 1 249 ? 23.604  -4.245  31.019  1.00 17.91 ? 249 PRO A CB  1 
ATOM   2005 C  CG  . PRO A 1 249 ? 24.575  -4.620  29.925  1.00 17.03 ? 249 PRO A CG  1 
ATOM   2006 C  CD  . PRO A 1 249 ? 23.871  -4.219  28.638  1.00 15.87 ? 249 PRO A CD  1 
ATOM   2007 N  N   . LEU A 1 250 ? 20.276  -4.038  31.791  1.00 16.04 ? 250 LEU A N   1 
ATOM   2008 C  CA  . LEU A 1 250 ? 19.204  -3.156  32.238  1.00 15.38 ? 250 LEU A CA  1 
ATOM   2009 C  C   . LEU A 1 250 ? 19.760  -2.071  33.171  1.00 16.97 ? 250 LEU A C   1 
ATOM   2010 O  O   . LEU A 1 250 ? 19.263  -0.941  33.245  1.00 17.09 ? 250 LEU A O   1 
ATOM   2011 C  CB  . LEU A 1 250 ? 18.154  -4.008  32.941  1.00 16.61 ? 250 LEU A CB  1 
ATOM   2012 C  CG  . LEU A 1 250 ? 16.876  -3.260  33.331  1.00 18.56 ? 250 LEU A CG  1 
ATOM   2013 C  CD1 . LEU A 1 250 ? 16.124  -2.691  32.125  1.00 16.40 ? 250 LEU A CD1 1 
ATOM   2014 C  CD2 . LEU A 1 250 ? 15.966  -4.188  34.120  1.00 20.80 ? 250 LEU A CD2 1 
ATOM   2015 N  N   . LYS A 1 251 ? 20.808  -2.425  33.914  1.00 17.98 ? 251 LYS A N   1 
ATOM   2016 C  CA  . LYS A 1 251 ? 21.477  -1.494  34.849  1.00 17.95 ? 251 LYS A CA  1 
ATOM   2017 C  C   . LYS A 1 251 ? 20.443  -1.044  35.884  1.00 19.49 ? 251 LYS A C   1 
ATOM   2018 O  O   . LYS A 1 251 ? 19.414  -1.737  36.038  1.00 24.21 ? 251 LYS A O   1 
ATOM   2019 C  CB  . LYS A 1 251 ? 22.281  -0.425  34.078  1.00 18.89 ? 251 LYS A CB  1 
ATOM   2020 C  CG  . LYS A 1 251 ? 23.505  -1.075  33.453  1.00 21.91 ? 251 LYS A CG  1 
ATOM   2021 C  CD  . LYS A 1 251 ? 24.312  -0.164  32.602  1.00 25.70 ? 251 LYS A CD  1 
ATOM   2022 C  CE  . LYS A 1 251 ? 25.618  -0.828  32.231  1.00 26.74 ? 251 LYS A CE  1 
ATOM   2023 N  NZ  . LYS A 1 251 ? 26.325  -0.005  31.223  1.00 27.52 ? 251 LYS A NZ  1 
ATOM   2024 N  N   A ASN A 1 252 ? 20.381  0.153   36.447  0.50 21.27 ? 252 ASN A N   1 
ATOM   2025 N  N   B ASN A 1 252 ? 20.502  0.269   36.137  0.50 20.30 ? 252 ASN A N   1 
ATOM   2026 C  CA  A ASN A 1 252 ? 19.396  0.231   37.565  0.50 20.95 ? 252 ASN A CA  1 
ATOM   2027 C  CA  B ASN A 1 252 ? 19.645  0.977   37.123  0.50 21.63 ? 252 ASN A CA  1 
ATOM   2028 C  C   A ASN A 1 252 ? 17.929  0.277   37.102  0.50 19.93 ? 252 ASN A C   1 
ATOM   2029 C  C   B ASN A 1 252 ? 18.381  1.512   36.441  0.50 20.57 ? 252 ASN A C   1 
ATOM   2030 O  O   A ASN A 1 252 ? 17.078  0.231   37.993  0.50 22.21 ? 252 ASN A O   1 
ATOM   2031 O  O   B ASN A 1 252 ? 18.240  2.739   36.352  0.50 22.48 ? 252 ASN A O   1 
ATOM   2032 C  CB  A ASN A 1 252 ? 19.705  1.401   38.504  0.50 23.03 ? 252 ASN A CB  1 
ATOM   2033 C  CB  B ASN A 1 252 ? 20.408  2.096   37.837  0.50 22.84 ? 252 ASN A CB  1 
ATOM   2034 C  CG  A ASN A 1 252 ? 21.012  1.231   39.250  0.50 26.00 ? 252 ASN A CG  1 
ATOM   2035 C  CG  B ASN A 1 252 ? 19.604  2.750   38.941  0.50 25.31 ? 252 ASN A CG  1 
ATOM   2036 O  OD1 A ASN A 1 252 ? 21.802  2.167   39.351  0.50 30.61 ? 252 ASN A OD1 1 
ATOM   2037 O  OD1 B ASN A 1 252 ? 18.912  2.071   39.696  0.50 29.69 ? 252 ASN A OD1 1 
ATOM   2038 N  ND2 A ASN A 1 252 ? 21.248  0.040   39.777  0.50 25.73 ? 252 ASN A ND2 1 
ATOM   2039 N  ND2 B ASN A 1 252 ? 19.688  4.066   39.041  0.50 25.42 ? 252 ASN A ND2 1 
ATOM   2040 N  N   A ARG A 1 253 ? 17.589  0.221   35.808  0.50 16.68 ? 253 ARG A N   1 
ATOM   2041 N  N   B ARG A 1 253 ? 17.550  0.590   35.922  0.50 18.40 ? 253 ARG A N   1 
ATOM   2042 C  CA  A ARG A 1 253 ? 16.290  0.682   35.329  0.50 15.68 ? 253 ARG A CA  1 
ATOM   2043 C  CA  B ARG A 1 253 ? 16.252  0.890   35.339  0.50 17.16 ? 253 ARG A CA  1 
ATOM   2044 C  C   A ARG A 1 253 ? 15.157  -0.243  35.756  0.50 16.83 ? 253 ARG A C   1 
ATOM   2045 C  C   B ARG A 1 253 ? 15.207  -0.131  35.790  0.50 17.88 ? 253 ARG A C   1 
ATOM   2046 O  O   A ARG A 1 253 ? 15.330  -1.451  35.876  0.50 17.86 ? 253 ARG A O   1 
ATOM   2047 O  O   B ARG A 1 253 ? 15.503  -1.301  36.015  0.50 20.12 ? 253 ARG A O   1 
ATOM   2048 C  CB  A ARG A 1 253 ? 16.271  0.801   33.794  0.50 14.14 ? 253 ARG A CB  1 
ATOM   2049 C  CB  B ARG A 1 253 ? 16.327  0.907   33.803  0.50 15.94 ? 253 ARG A CB  1 
ATOM   2050 C  CG  A ARG A 1 253 ? 17.128  1.941   33.277  0.50 13.96 ? 253 ARG A CG  1 
ATOM   2051 C  CG  B ARG A 1 253 ? 17.270  1.971   33.273  0.50 16.16 ? 253 ARG A CG  1 
ATOM   2052 C  CD  A ARG A 1 253 ? 17.233  1.874   31.780  0.50 13.72 ? 253 ARG A CD  1 
ATOM   2053 C  CD  B ARG A 1 253 ? 17.292  1.901   31.772  0.50 15.82 ? 253 ARG A CD  1 
ATOM   2054 N  NE  A ARG A 1 253 ? 18.089  0.770   31.350  0.50 12.14 ? 253 ARG A NE  1 
ATOM   2055 N  NE  B ARG A 1 253 ? 18.133  0.793   31.332  0.50 14.24 ? 253 ARG A NE  1 
ATOM   2056 C  CZ  A ARG A 1 253 ? 18.359  0.495   30.062  0.50 11.00 ? 253 ARG A CZ  1 
ATOM   2057 C  CZ  B ARG A 1 253 ? 18.379  0.503   30.048  0.50 12.85 ? 253 ARG A CZ  1 
ATOM   2058 N  NH1 A ARG A 1 253 ? 17.772  1.180   29.080  0.50 10.84 ? 253 ARG A NH1 1 
ATOM   2059 N  NH1 B ARG A 1 253 ? 17.781  1.185   29.072  0.50 12.51 ? 253 ARG A NH1 1 
ATOM   2060 N  NH2 A ARG A 1 253 ? 19.192  -0.491  29.741  0.50 10.56 ? 253 ARG A NH2 1 
ATOM   2061 N  NH2 B ARG A 1 253 ? 19.201  -0.490  29.729  0.50 12.25 ? 253 ARG A NH2 1 
ATOM   2062 N  N   . GLN A 1 254 ? 13.957  0.335   35.858  1.00 16.47 ? 254 GLN A N   1 
ATOM   2063 C  CA  . GLN A 1 254 ? 12.765  -0.472  36.092  1.00 17.63 ? 254 GLN A CA  1 
ATOM   2064 C  C   . GLN A 1 254 ? 11.895  -0.428  34.835  1.00 17.08 ? 254 GLN A C   1 
ATOM   2065 O  O   . GLN A 1 254 ? 11.765  0.630   34.203  1.00 21.46 ? 254 GLN A O   1 
ATOM   2066 C  CB  . GLN A 1 254 ? 11.978  0.004   37.323  1.00 22.72 ? 254 GLN A CB  1 
ATOM   2067 C  CG  . GLN A 1 254 ? 11.572  1.470   37.270  1.00 28.62 ? 254 GLN A CG  1 
ATOM   2068 N  N   . ILE A 1 255 ? 11.399  -1.599  34.451  1.00 14.58 ? 255 ILE A N   1 
ATOM   2069 C  CA  . ILE A 1 255 ? 10.404  -1.702  33.404  1.00 15.05 ? 255 ILE A CA  1 
ATOM   2070 C  C   . ILE A 1 255 ? 9.029   -1.682  34.060  1.00 15.35 ? 255 ILE A C   1 
ATOM   2071 O  O   . ILE A 1 255 ? 8.808   -2.394  35.025  1.00 17.32 ? 255 ILE A O   1 
ATOM   2072 C  CB  . ILE A 1 255 ? 10.618  -2.964  32.536  1.00 13.32 ? 255 ILE A CB  1 
ATOM   2073 C  CG1 . ILE A 1 255 ? 12.027  -2.964  31.924  1.00 14.54 ? 255 ILE A CG1 1 
ATOM   2074 C  CG2 . ILE A 1 255 ? 9.534   -3.045  31.431  1.00 14.22 ? 255 ILE A CG2 1 
ATOM   2075 C  CD1 . ILE A 1 255 ? 12.319  -4.236  31.121  1.00 15.40 ? 255 ILE A CD1 1 
ATOM   2076 N  N   . LYS A 1 256 ? 8.157   -0.794  33.579  1.00 13.14 ? 256 LYS A N   1 
ATOM   2077 C  CA  . LYS A 1 256 ? 6.796   -0.694  34.099  1.00 14.11 ? 256 LYS A CA  1 
ATOM   2078 C  C   . LYS A 1 256 ? 5.807   -1.357  33.159  1.00 13.96 ? 256 LYS A C   1 
ATOM   2079 O  O   . LYS A 1 256 ? 6.012   -1.317  31.951  1.00 15.55 ? 256 LYS A O   1 
ATOM   2080 C  CB  . LYS A 1 256 ? 6.496   0.785   34.377  1.00 15.77 ? 256 LYS A CB  1 
ATOM   2081 C  CG  . LYS A 1 256 ? 7.309   1.314   35.555  1.00 20.70 ? 256 LYS A CG  1 
ATOM   2082 C  CD  . LYS A 1 256 ? 7.224   2.796   35.807  1.00 29.23 ? 256 LYS A CD  1 
ATOM   2083 N  N   . ALA A 1 257 ? 4.775   -2.007  33.681  1.00 15.19 ? 257 ALA A N   1 
ATOM   2084 C  CA  . ALA A 1 257 ? 3.715   -2.636  32.915  1.00 14.64 ? 257 ALA A CA  1 
ATOM   2085 C  C   . ALA A 1 257 ? 2.437   -1.831  33.074  1.00 15.15 ? 257 ALA A C   1 
ATOM   2086 O  O   . ALA A 1 257 ? 2.102   -1.354  34.183  1.00 16.58 ? 257 ALA A O   1 
ATOM   2087 C  CB  . ALA A 1 257 ? 3.503   -4.094  33.311  1.00 13.78 ? 257 ALA A CB  1 
ATOM   2088 N  N   . SER A 1 258 ? 1.702   -1.710  31.985  1.00 14.55 ? 258 SER A N   1 
ATOM   2089 C  CA  . SER A 1 258 ? 0.429   -1.016  32.013  1.00 16.52 ? 258 SER A CA  1 
ATOM   2090 C  C   . SER A 1 258 ? -0.701  -1.925  32.465  1.00 17.15 ? 258 SER A C   1 
ATOM   2091 O  O   . SER A 1 258 ? -1.835  -1.434  32.537  1.00 21.48 ? 258 SER A O   1 
ATOM   2092 C  CB  . SER A 1 258 ? 0.118   -0.426  30.650  1.00 14.70 ? 258 SER A CB  1 
ATOM   2093 O  OG  . SER A 1 258 ? -0.288  -1.428  29.739  1.00 15.57 ? 258 SER A OG  1 
ATOM   2094 N  N   . PHE A 1 259 ? -0.399  -3.196  32.749  1.00 18.14 ? 259 PHE A N   1 
ATOM   2095 C  CA  . PHE A 1 259 ? -1.440  -4.193  32.841  1.00 21.06 ? 259 PHE A CA  1 
ATOM   2096 C  C   . PHE A 1 259 ? -1.100  -5.156  33.962  1.00 24.77 ? 259 PHE A C   1 
ATOM   2097 O  O   . PHE A 1 259 ? 0.065   -5.279  34.359  1.00 23.37 ? 259 PHE A O   1 
ATOM   2098 C  CB  . PHE A 1 259 ? -1.612  -4.936  31.510  1.00 22.35 ? 259 PHE A CB  1 
ATOM   2099 C  CG  . PHE A 1 259 ? -0.358  -5.684  31.107  1.00 21.94 ? 259 PHE A CG  1 
ATOM   2100 C  CD1 . PHE A 1 259 ? 0.630   -5.059  30.355  1.00 21.05 ? 259 PHE A CD1 1 
ATOM   2101 C  CD2 . PHE A 1 259 ? -0.135  -6.987  31.555  1.00 24.49 ? 259 PHE A CD2 1 
ATOM   2102 C  CE1 . PHE A 1 259 ? 1.798   -5.740  30.032  1.00 21.83 ? 259 PHE A CE1 1 
ATOM   2103 C  CE2 . PHE A 1 259 ? 1.051   -7.651  31.258  1.00 25.47 ? 259 PHE A CE2 1 
ATOM   2104 C  CZ  . PHE A 1 259 ? 2.004   -7.031  30.474  1.00 23.74 ? 259 PHE A CZ  1 
ATOM   2105 N  N   . LYS A 1 260 ? -2.201  -5.789  34.420  1.00 34.96 ? 260 LYS A N   1 
ATOM   2106 C  CA  . LYS A 1 260 ? -2.368  -7.078  35.086  1.00 45.59 ? 260 LYS A CA  1 
ATOM   2107 C  C   . LYS A 1 260 ? -1.520  -7.149  36.356  1.00 51.52 ? 260 LYS A C   1 
ATOM   2108 O  O   . LYS A 1 260 ? -0.399  -7.634  36.318  1.00 60.91 ? 260 LYS A O   1 
ATOM   2109 C  CB  . LYS A 1 260 ? -2.184  -8.261  34.122  1.00 43.90 ? 260 LYS A CB  1 
ATOM   2110 O  OXT . LYS A 1 260 ? -1.969  -6.718  37.425  1.00 60.74 ? 260 LYS A OXT 1 
HETATM 2111 ZN ZN  . ZN  B 2 .   ? 14.387  0.222   15.319  1.00 9.83  ? 301 ZN  A ZN  1 
HETATM 2112 F  F13 A V50 C 3 .   ? 14.548  5.506   17.004  0.50 16.27 ? 302 V50 A F13 1 
HETATM 2113 F  F13 C V50 C 3 .   ? 18.232  3.206   16.564  0.50 11.71 ? 302 V50 A F13 1 
HETATM 2114 C  C4  A V50 C 3 .   ? 15.000  5.218   15.833  0.50 17.42 ? 302 V50 A C4  1 
HETATM 2115 C  C4  C V50 C 3 .   ? 17.467  4.197   16.121  0.50 13.06 ? 302 V50 A C4  1 
HETATM 2116 C  C5  A V50 C 3 .   ? 15.467  3.928   15.576  0.50 13.71 ? 302 V50 A C5  1 
HETATM 2117 C  C5  C V50 C 3 .   ? 16.052  4.070   16.162  0.50 12.15 ? 302 V50 A C5  1 
HETATM 2118 S  S7  A V50 C 3 .   ? 15.230  2.775   16.876  0.50 10.79 ? 302 V50 A S7  1 
HETATM 2119 S  S7  C V50 C 3 .   ? 15.238  2.665   16.868  0.50 9.95  ? 302 V50 A S7  1 
HETATM 2120 O  O9  A V50 C 3 .   ? 13.784  2.712   16.902  0.50 9.98  ? 302 V50 A O9  1 
HETATM 2121 O  O9  C V50 C 3 .   ? 13.836  2.880   16.683  0.50 9.85  ? 302 V50 A O9  1 
HETATM 2122 N  N23 A V50 C 3 .   ? 15.589  1.260   16.509  0.50 10.99 ? 302 V50 A N23 1 
HETATM 2123 N  N23 C V50 C 3 .   ? 15.773  1.382   15.988  0.50 10.79 ? 302 V50 A N23 1 
HETATM 2124 O  O8  A V50 C 3 .   ? 15.900  3.174   18.073  0.50 8.72  ? 302 V50 A O8  1 
HETATM 2125 O  O8  C V50 C 3 .   ? 15.793  2.621   18.222  0.50 9.96  ? 302 V50 A O8  1 
HETATM 2126 C  C6  A V50 C 3 .   ? 15.899  3.710   14.261  0.50 16.95 ? 302 V50 A C6  1 
HETATM 2127 C  C6  C V50 C 3 .   ? 15.416  5.182   15.656  0.50 14.54 ? 302 V50 A C6  1 
HETATM 2128 F  F11 A V50 C 3 .   ? 16.395  2.503   13.931  0.50 20.18 ? 302 V50 A F11 1 
HETATM 2129 F  F11 C V50 C 3 .   ? 14.088  5.216   15.656  0.50 15.90 ? 302 V50 A F11 1 
HETATM 2130 C  C1  A V50 C 3 .   ? 15.827  4.835   13.362  0.50 19.31 ? 302 V50 A C1  1 
HETATM 2131 C  C1  C V50 C 3 .   ? 16.051  6.298   15.159  0.50 16.24 ? 302 V50 A C1  1 
HETATM 2132 F  F10 A V50 C 3 .   ? 16.228  4.603   12.139  0.50 20.85 ? 302 V50 A F10 1 
HETATM 2133 F  F10 C V50 C 3 .   ? 15.208  7.242   14.697  0.50 16.23 ? 302 V50 A F10 1 
HETATM 2134 C  C3  A V50 C 3 .   ? 14.939  6.294   14.990  0.50 19.42 ? 302 V50 A C3  1 
HETATM 2135 C  C3  C V50 C 3 .   ? 18.130  5.329   15.644  0.50 14.07 ? 302 V50 A C3  1 
HETATM 2136 F  F12 A V50 C 3 .   ? 14.519  7.482   15.484  0.50 19.34 ? 302 V50 A F12 1 
HETATM 2137 F  F12 C V50 C 3 .   ? 19.477  5.359   15.653  0.50 13.48 ? 302 V50 A F12 1 
HETATM 2138 C  C2  A V50 C 3 .   ? 15.360  6.145   13.705  0.50 20.14 ? 302 V50 A C2  1 
HETATM 2139 C  C2  C V50 C 3 .   ? 17.438  6.388   15.095  0.50 15.10 ? 302 V50 A C2  1 
HETATM 2140 S  S14 A V50 C 3 .   ? 15.169  7.618   12.681  0.50 23.63 ? 302 V50 A S14 1 
HETATM 2141 S  S14 C V50 C 3 .   ? 18.220  7.874   14.562  0.50 18.43 ? 302 V50 A S14 1 
HETATM 2142 C  C15 A V50 C 3 .   ? 16.807  8.099   12.402  0.50 23.62 ? 302 V50 A C15 1 
HETATM 2143 C  C15 C V50 C 3 .   ? 19.558  7.507   13.486  0.50 20.63 ? 302 V50 A C15 1 
HETATM 2144 N  N20 A V50 C 3 .   ? 17.722  7.356   12.965  0.50 23.68 ? 302 V50 A N20 1 
HETATM 2145 N  N20 C V50 C 3 .   ? 20.376  8.545   13.330  0.50 20.65 ? 302 V50 A N20 1 
HETATM 2146 C  C19 A V50 C 3 .   ? 18.959  7.794   12.732  0.50 26.32 ? 302 V50 A C19 1 
HETATM 2147 C  C19 C V50 C 3 .   ? 21.435  8.371   12.518  0.50 21.96 ? 302 V50 A C19 1 
HETATM 2148 C  C21 A V50 C 3 .   ? 20.034  6.941   13.352  0.50 28.33 ? 302 V50 A C21 1 
HETATM 2149 C  C21 C V50 C 3 .   ? 22.322  9.605   12.420  0.50 20.26 ? 302 V50 A C21 1 
HETATM 2150 C  C18 A V50 C 3 .   ? 19.293  8.893   11.992  0.50 26.35 ? 302 V50 A C18 1 
HETATM 2151 C  C18 C V50 C 3 .   ? 21.714  7.190   11.869  0.50 20.06 ? 302 V50 A C18 1 
HETATM 2152 C  C17 A V50 C 3 .   ? 18.211  9.567   11.495  0.50 25.27 ? 302 V50 A C17 1 
HETATM 2153 C  C17 C V50 C 3 .   ? 20.777  6.202   12.100  0.50 20.10 ? 302 V50 A C17 1 
HETATM 2154 N  N16 A V50 C 3 .   ? 16.957  9.204   11.679  0.50 25.80 ? 302 V50 A N16 1 
HETATM 2155 N  N16 C V50 C 3 .   ? 19.701  6.312   12.917  0.50 20.78 ? 302 V50 A N16 1 
HETATM 2156 C  C22 A V50 C 3 .   ? 18.404  10.813  10.670  0.50 24.41 ? 302 V50 A C22 1 
HETATM 2157 C  C22 C V50 C 3 .   ? 20.951  4.878   11.442  0.50 21.58 ? 302 V50 A C22 1 
HETATM 2158 NA NA  . NA  D 4 .   ? 3.310   21.092  6.081   1.00 30.97 ? 303 NA  A NA  1 
HETATM 2159 S  S   . DMS E 5 .   ? 22.416  -9.802  14.920  1.00 26.90 ? 304 DMS A S   1 
HETATM 2160 O  O   . DMS E 5 .   ? 22.987  -11.169 14.483  1.00 29.76 ? 304 DMS A O   1 
HETATM 2161 C  C1  . DMS E 5 .   ? 23.664  -8.620  14.486  1.00 29.01 ? 304 DMS A C1  1 
HETATM 2162 C  C2  . DMS E 5 .   ? 22.765  -9.778  16.649  1.00 23.62 ? 304 DMS A C2  1 
HETATM 2163 O  O   . HOH F 6 .   ? -4.483  -8.871  17.484  1.00 30.71 ? 401 HOH A O   1 
HETATM 2164 O  O   . HOH F 6 .   ? 10.240  -13.215 33.903  1.00 32.05 ? 402 HOH A O   1 
HETATM 2165 O  O   . HOH F 6 .   ? 1.858   19.331  19.049  1.00 43.67 ? 403 HOH A O   1 
HETATM 2166 O  O   . HOH F 6 .   ? 10.820  -3.920  38.309  1.00 45.82 ? 404 HOH A O   1 
HETATM 2167 O  O   . HOH F 6 .   ? -3.069  -1.689  29.519  1.00 31.56 ? 405 HOH A O   1 
HETATM 2168 O  O   . HOH F 6 .   ? 19.121  10.498  28.922  1.00 32.12 ? 406 HOH A O   1 
HETATM 2169 O  O   . HOH F 6 .   ? 25.632  -0.824  29.036  1.00 25.12 ? 407 HOH A O   1 
HETATM 2170 O  O   . HOH F 6 .   ? 6.728   -14.700 29.075  1.00 29.95 ? 408 HOH A O   1 
HETATM 2171 O  O   . HOH F 6 .   ? 0.693   10.544  30.136  1.00 29.53 ? 409 HOH A O   1 
HETATM 2172 O  O   . HOH F 6 .   ? 7.026   -3.253  -6.397  1.00 37.31 ? 410 HOH A O   1 
HETATM 2173 O  O   . HOH F 6 .   ? 1.723   19.224  6.059   1.00 29.38 ? 411 HOH A O   1 
HETATM 2174 O  O   . HOH F 6 .   ? -6.849  13.649  5.233   1.00 37.44 ? 412 HOH A O   1 
HETATM 2175 O  O   . HOH F 6 .   ? 19.035  -1.367  11.453  1.00 24.64 ? 413 HOH A O   1 
HETATM 2176 O  O   . HOH F 6 .   ? 16.325  3.898   37.533  1.00 30.93 ? 414 HOH A O   1 
HETATM 2177 O  O   . HOH F 6 .   ? 22.963  3.339   36.178  1.00 44.79 ? 415 HOH A O   1 
HETATM 2178 O  O   . HOH F 6 .   ? 8.840   12.467  5.839   1.00 27.74 ? 416 HOH A O   1 
HETATM 2179 O  O   . HOH F 6 .   ? 32.588  -5.388  22.393  1.00 34.55 ? 417 HOH A O   1 
HETATM 2180 O  O   . HOH F 6 .   ? 15.117  -9.687  36.397  1.00 38.09 ? 418 HOH A O   1 
HETATM 2181 O  O   . HOH F 6 .   ? 5.833   -8.572  37.533  1.00 26.67 ? 419 HOH A O   1 
HETATM 2182 O  O   . HOH F 6 .   ? 20.632  2.795   34.412  1.00 31.81 ? 420 HOH A O   1 
HETATM 2183 O  O   . HOH F 6 .   ? 0.854   12.621  26.808  1.00 21.89 ? 421 HOH A O   1 
HETATM 2184 O  O   . HOH F 6 .   ? -4.626  -4.067  13.147  1.00 36.85 ? 422 HOH A O   1 
HETATM 2185 O  O   . HOH F 6 .   ? 10.637  -16.385 16.900  1.00 19.81 ? 423 HOH A O   1 
HETATM 2186 O  O   . HOH F 6 .   ? 23.123  9.611   27.839  1.00 21.99 ? 424 HOH A O   1 
HETATM 2187 O  O   . HOH F 6 .   ? 8.682   14.748  31.899  1.00 26.16 ? 425 HOH A O   1 
HETATM 2188 O  O   . HOH F 6 .   ? 5.606   -19.889 13.348  1.00 24.24 ? 426 HOH A O   1 
HETATM 2189 O  O   . HOH F 6 .   ? 18.560  -17.182 21.868  1.00 31.84 ? 427 HOH A O   1 
HETATM 2190 O  O   . HOH F 6 .   ? 11.423  17.632  29.490  1.00 31.68 ? 428 HOH A O   1 
HETATM 2191 O  O   . HOH F 6 .   ? 32.630  1.258   15.827  1.00 33.50 ? 429 HOH A O   1 
HETATM 2192 O  O   . HOH F 6 .   ? 8.961   14.314  29.226  1.00 24.46 ? 430 HOH A O   1 
HETATM 2193 O  O   . HOH F 6 .   ? 10.475  2.925   34.148  1.00 40.51 ? 431 HOH A O   1 
HETATM 2194 O  O   . HOH F 6 .   ? 2.471   -19.307 14.734  1.00 23.55 ? 432 HOH A O   1 
HETATM 2195 O  O   . HOH F 6 .   ? 14.221  -18.321 19.479  1.00 22.97 ? 433 HOH A O   1 
HETATM 2196 O  O   . HOH F 6 .   ? -6.151  -6.076  26.124  1.00 33.35 ? 434 HOH A O   1 
HETATM 2197 O  O   . HOH F 6 .   ? -4.540  -13.400 7.756   1.00 29.76 ? 435 HOH A O   1 
HETATM 2198 O  O   . HOH F 6 .   ? 24.534  6.657   30.216  1.00 19.82 ? 436 HOH A O   1 
HETATM 2199 O  O   . HOH F 6 .   ? 19.912  -2.321  15.747  1.00 11.73 ? 437 HOH A O   1 
HETATM 2200 O  O   . HOH F 6 .   ? 14.868  -2.706  -6.424  1.00 23.64 ? 438 HOH A O   1 
HETATM 2201 O  O   . HOH F 6 .   ? 16.382  -10.166 32.020  1.00 21.13 ? 439 HOH A O   1 
HETATM 2202 O  O   . HOH F 6 .   ? -3.102  10.594  20.393  1.00 24.88 ? 440 HOH A O   1 
HETATM 2203 O  O   . HOH F 6 .   ? 10.546  -17.526 19.976  1.00 23.88 ? 441 HOH A O   1 
HETATM 2204 O  O   . HOH F 6 .   ? 24.509  -7.067  25.864  1.00 40.74 ? 442 HOH A O   1 
HETATM 2205 O  O   . HOH F 6 .   ? -2.118  -9.473  17.159  1.00 26.05 ? 443 HOH A O   1 
HETATM 2206 O  O   . HOH F 6 .   ? 23.613  -11.383 5.112   1.00 21.55 ? 444 HOH A O   1 
HETATM 2207 O  O   . HOH F 6 .   ? 1.886   -18.952 5.203   1.00 24.27 ? 445 HOH A O   1 
HETATM 2208 O  O   . HOH F 6 .   ? 2.661   -10.585 -3.507  1.00 30.83 ? 446 HOH A O   1 
HETATM 2209 O  O   . HOH F 6 .   ? -0.148  -5.154  -1.665  1.00 32.54 ? 447 HOH A O   1 
HETATM 2210 O  O   . HOH F 6 .   ? 12.191  7.728   28.944  1.00 23.80 ? 448 HOH A O   1 
HETATM 2211 O  O   . HOH F 6 .   ? 3.063   12.631  11.404  1.00 21.48 ? 449 HOH A O   1 
HETATM 2212 O  O   . HOH F 6 .   ? -0.617  -12.360 18.551  1.00 31.16 ? 450 HOH A O   1 
HETATM 2213 O  O   . HOH F 6 .   ? 10.733  10.493  25.563  1.00 13.06 ? 451 HOH A O   1 
HETATM 2214 O  O   . HOH F 6 .   ? 20.668  -18.676 15.098  1.00 35.96 ? 452 HOH A O   1 
HETATM 2215 O  O   . HOH F 6 .   ? 20.957  1.019   -4.715  1.00 19.72 ? 453 HOH A O   1 
HETATM 2216 O  O   . HOH F 6 .   ? 26.594  8.780   20.214  1.00 20.07 ? 454 HOH A O   1 
HETATM 2217 O  O   . HOH F 6 .   ? 12.709  -13.444 36.686  1.00 35.44 ? 455 HOH A O   1 
HETATM 2218 O  O   . HOH F 6 .   ? 24.453  10.514  20.937  1.00 25.54 ? 456 HOH A O   1 
HETATM 2219 O  O   . HOH F 6 .   ? 1.335   -15.159 2.925   1.00 27.79 ? 457 HOH A O   1 
HETATM 2220 O  O   . HOH F 6 .   ? 6.369   -16.893 18.790  1.00 20.80 ? 458 HOH A O   1 
HETATM 2221 O  O   . HOH F 6 .   ? -0.457  -5.314  23.588  1.00 15.73 ? 459 HOH A O   1 
HETATM 2222 O  O   . HOH F 6 .   ? -4.803  8.033   26.919  1.00 30.32 ? 460 HOH A O   1 
HETATM 2223 O  O   . HOH F 6 .   ? 7.184   -19.078 3.602   1.00 36.11 ? 461 HOH A O   1 
HETATM 2224 O  O   . HOH F 6 .   ? 13.876  -6.488  -7.045  1.00 35.60 ? 462 HOH A O   1 
HETATM 2225 O  O   . HOH F 6 .   ? 8.071   -7.131  -3.053  1.00 30.33 ? 463 HOH A O   1 
HETATM 2226 O  O   . HOH F 6 .   ? 36.874  4.729   21.050  1.00 29.06 ? 464 HOH A O   1 
HETATM 2227 O  O   . HOH F 6 .   ? 14.365  -3.487  37.346  1.00 23.04 ? 465 HOH A O   1 
HETATM 2228 O  O   . HOH F 6 .   ? 25.375  -1.741  26.583  1.00 21.97 ? 466 HOH A O   1 
HETATM 2229 O  O   . HOH F 6 .   ? 17.176  5.140   9.528   1.00 37.54 ? 467 HOH A O   1 
HETATM 2230 O  O   . HOH F 6 .   ? 7.235   21.999  15.284  1.00 24.33 ? 468 HOH A O   1 
HETATM 2231 O  O   . HOH F 6 .   ? 25.936  4.539   8.361   1.00 35.85 ? 469 HOH A O   1 
HETATM 2232 O  O   . HOH F 6 .   ? 14.227  -13.124 31.543  1.00 24.88 ? 470 HOH A O   1 
HETATM 2233 O  O   . HOH F 6 .   ? 13.082  -13.588 11.244  1.00 12.21 ? 471 HOH A O   1 
HETATM 2234 O  O   . HOH F 6 .   ? 22.741  -13.958 -4.486  1.00 30.89 ? 472 HOH A O   1 
HETATM 2235 O  O   . HOH F 6 .   ? 3.937   -21.071 4.282   1.00 30.82 ? 473 HOH A O   1 
HETATM 2236 O  O   . HOH F 6 .   ? 2.731   -2.099  -2.604  1.00 28.01 ? 474 HOH A O   1 
HETATM 2237 O  O   . HOH F 6 .   ? 17.284  -14.054 24.276  1.00 15.89 ? 475 HOH A O   1 
HETATM 2238 O  O   . HOH F 6 .   ? 4.064   -6.504  20.385  1.00 11.27 ? 476 HOH A O   1 
HETATM 2239 O  O   . HOH F 6 .   ? 23.048  -13.627 9.405   1.00 27.62 ? 477 HOH A O   1 
HETATM 2240 O  O   . HOH F 6 .   ? 24.835  1.748   -6.006  1.00 45.80 ? 478 HOH A O   1 
HETATM 2241 O  O   . HOH F 6 .   ? 12.371  2.627   -6.435  1.00 26.69 ? 479 HOH A O   1 
HETATM 2242 O  O   . HOH F 6 .   ? -2.235  -11.505 11.265  1.00 26.56 ? 480 HOH A O   1 
HETATM 2243 O  O   . HOH F 6 .   ? 16.585  -14.009 1.214   1.00 33.26 ? 481 HOH A O   1 
HETATM 2244 O  O   . HOH F 6 .   ? 1.199   -2.226  41.298  1.00 32.50 ? 482 HOH A O   1 
HETATM 2245 O  O   . HOH F 6 .   ? 22.337  -10.002 25.050  1.00 24.30 ? 483 HOH A O   1 
HETATM 2246 O  O   . HOH F 6 .   ? 29.177  -4.143  -10.409 1.00 50.54 ? 484 HOH A O   1 
HETATM 2247 O  O   . HOH F 6 .   ? 5.010   -10.442 24.365  1.00 17.74 ? 485 HOH A O   1 
HETATM 2248 O  O   . HOH F 6 .   ? 19.140  -2.622  -7.012  1.00 28.00 ? 486 HOH A O   1 
HETATM 2249 O  O   . HOH F 6 .   ? 5.448   10.797  -1.882  1.00 30.13 ? 487 HOH A O   1 
HETATM 2250 O  O   . HOH F 6 .   ? 7.544   12.312  27.960  1.00 18.65 ? 488 HOH A O   1 
HETATM 2251 O  O   . HOH F 6 .   ? 19.185  3.051   8.880   1.00 29.32 ? 489 HOH A O   1 
HETATM 2252 O  O   . HOH F 6 .   ? -1.066  -16.419 13.597  1.00 28.26 ? 490 HOH A O   1 
HETATM 2253 O  O   . HOH F 6 .   ? 17.461  -10.952 -2.901  1.00 28.77 ? 491 HOH A O   1 
HETATM 2254 O  O   . HOH F 6 .   ? 17.548  -9.342  20.855  1.00 11.57 ? 492 HOH A O   1 
HETATM 2255 O  O   . HOH F 6 .   ? 8.153   -20.608 12.089  1.00 28.46 ? 493 HOH A O   1 
HETATM 2256 O  O   . HOH F 6 .   ? 28.712  -5.785  -0.746  1.00 27.73 ? 494 HOH A O   1 
HETATM 2257 O  O   . HOH F 6 .   ? -5.255  5.578   15.582  1.00 27.53 ? 495 HOH A O   1 
HETATM 2258 O  O   . HOH F 6 .   ? 36.540  -0.595  14.572  1.00 22.89 ? 496 HOH A O   1 
HETATM 2259 O  O   . HOH F 6 .   ? 16.540  -11.650 17.944  1.00 9.73  ? 497 HOH A O   1 
HETATM 2260 O  O   . HOH F 6 .   ? 32.252  2.968   26.050  1.00 27.52 ? 498 HOH A O   1 
HETATM 2261 O  O   . HOH F 6 .   ? 3.759   -14.321 22.080  1.00 30.62 ? 499 HOH A O   1 
HETATM 2262 O  O   . HOH F 6 .   ? -4.494  0.648   35.031  1.00 38.19 ? 500 HOH A O   1 
HETATM 2263 O  O   . HOH F 6 .   ? -4.222  11.604  13.187  1.00 31.25 ? 501 HOH A O   1 
HETATM 2264 O  O   . HOH F 6 .   ? 15.239  9.749   5.361   1.00 27.06 ? 502 HOH A O   1 
HETATM 2265 O  O   . HOH F 6 .   ? 13.949  -14.850 1.693   1.00 23.17 ? 503 HOH A O   1 
HETATM 2266 O  O   . HOH F 6 .   ? -1.001  7.638   4.949   1.00 21.69 ? 504 HOH A O   1 
HETATM 2267 O  O   . HOH F 6 .   ? -2.116  -1.158  6.968   1.00 26.92 ? 505 HOH A O   1 
HETATM 2268 O  O   . HOH F 6 .   ? 29.755  -2.093  21.178  1.00 17.15 ? 506 HOH A O   1 
HETATM 2269 O  O   . HOH F 6 .   ? -4.805  5.242   33.925  1.00 40.07 ? 507 HOH A O   1 
HETATM 2270 O  O   . HOH F 6 .   ? -0.222  9.725   2.016   1.00 20.01 ? 508 HOH A O   1 
HETATM 2271 O  O   . HOH F 6 .   ? 18.517  -6.985  29.106  1.00 14.29 ? 509 HOH A O   1 
HETATM 2272 O  O   . HOH F 6 .   ? -1.691  -4.044  2.833   1.00 24.13 ? 510 HOH A O   1 
HETATM 2273 O  O   . HOH F 6 .   ? 17.522  -2.899  37.703  1.00 38.92 ? 511 HOH A O   1 
HETATM 2274 O  O   . HOH F 6 .   ? 19.446  6.341   -4.804  1.00 29.12 ? 512 HOH A O   1 
HETATM 2275 O  O   . HOH F 6 .   ? 32.178  -2.132  7.777   1.00 45.60 ? 513 HOH A O   1 
HETATM 2276 O  O   . HOH F 6 .   ? 17.635  -11.471 25.059  1.00 13.73 ? 514 HOH A O   1 
HETATM 2277 O  O   . HOH F 6 .   ? -3.833  6.789   8.500   1.00 40.54 ? 515 HOH A O   1 
HETATM 2278 O  O   . HOH F 6 .   ? 7.583   1.077   -6.073  1.00 29.16 ? 516 HOH A O   1 
HETATM 2279 O  O   . HOH F 6 .   ? 3.201   -18.645 8.011   1.00 17.90 ? 517 HOH A O   1 
HETATM 2280 O  O   . HOH F 6 .   ? 29.232  -7.638  16.767  1.00 25.12 ? 518 HOH A O   1 
HETATM 2281 O  O   . HOH F 6 .   ? 9.161   11.222  3.318   1.00 24.87 ? 519 HOH A O   1 
HETATM 2282 O  O   . HOH F 6 .   ? -1.275  -10.604 24.712  1.00 33.23 ? 520 HOH A O   1 
HETATM 2283 O  O   . HOH F 6 .   ? 7.628   -16.724 14.731  1.00 21.34 ? 521 HOH A O   1 
HETATM 2284 O  O   . HOH F 6 .   ? -4.829  9.928   6.364   1.00 36.31 ? 522 HOH A O   1 
HETATM 2285 O  O   . HOH F 6 .   ? 34.582  2.034   24.591  1.00 23.89 ? 523 HOH A O   1 
HETATM 2286 O  O   . HOH F 6 .   ? 5.976   -9.229  -3.560  1.00 43.66 ? 524 HOH A O   1 
HETATM 2287 O  O   . HOH F 6 .   ? 7.563   15.905  27.466  1.00 24.90 ? 525 HOH A O   1 
HETATM 2288 O  O   . HOH F 6 .   ? 23.808  2.937   -2.220  1.00 32.44 ? 526 HOH A O   1 
HETATM 2289 O  O   . HOH F 6 .   ? 21.015  -15.508 28.818  1.00 47.34 ? 527 HOH A O   1 
HETATM 2290 O  O   . HOH F 6 .   ? -2.891  1.169   26.341  1.00 24.58 ? 528 HOH A O   1 
HETATM 2291 O  O   . HOH F 6 .   ? 14.705  -17.865 23.878  1.00 28.81 ? 529 HOH A O   1 
HETATM 2292 O  O   . HOH F 6 .   ? 16.851  -6.833  31.267  1.00 25.25 ? 530 HOH A O   1 
HETATM 2293 O  O   . HOH F 6 .   ? 6.119   13.198  34.691  1.00 31.22 ? 531 HOH A O   1 
HETATM 2294 O  O   . HOH F 6 .   ? -2.139  1.546   34.605  1.00 35.93 ? 532 HOH A O   1 
HETATM 2295 O  O   . HOH F 6 .   ? 9.125   4.648   30.735  1.00 22.65 ? 533 HOH A O   1 
HETATM 2296 O  O   . HOH F 6 .   ? 4.814   -8.178  32.931  1.00 20.17 ? 534 HOH A O   1 
HETATM 2297 O  O   . HOH F 6 .   ? 9.930   -17.381 6.948   1.00 24.89 ? 535 HOH A O   1 
HETATM 2298 O  O   . HOH F 6 .   ? 25.060  -1.074  3.928   1.00 36.41 ? 536 HOH A O   1 
HETATM 2299 O  O   . HOH F 6 .   ? 26.022  -3.127  21.052  1.00 15.32 ? 537 HOH A O   1 
HETATM 2300 O  O   . HOH F 6 .   ? 8.028   -15.032 26.591  1.00 21.09 ? 538 HOH A O   1 
HETATM 2301 O  O   . HOH F 6 .   ? 26.282  -5.454  22.402  1.00 32.80 ? 539 HOH A O   1 
HETATM 2302 O  O   . HOH F 6 .   ? 5.021   17.797  23.831  1.00 23.82 ? 540 HOH A O   1 
HETATM 2303 O  O   . HOH F 6 .   ? 6.046   22.003  17.764  1.00 21.67 ? 541 HOH A O   1 
HETATM 2304 O  O   . HOH F 6 .   ? 24.117  -12.559 1.309   1.00 30.15 ? 542 HOH A O   1 
HETATM 2305 O  O   . HOH F 6 .   ? 13.684  -6.890  32.648  1.00 21.18 ? 543 HOH A O   1 
HETATM 2306 O  O   . HOH F 6 .   ? 1.722   11.951  8.936   1.00 17.52 ? 544 HOH A O   1 
HETATM 2307 O  O   . HOH F 6 .   ? -2.654  -16.168 6.416   1.00 33.34 ? 545 HOH A O   1 
HETATM 2308 O  O   . HOH F 6 .   ? 3.178   -5.840  39.310  1.00 32.83 ? 546 HOH A O   1 
HETATM 2309 O  O   . HOH F 6 .   ? 21.535  -17.593 10.916  1.00 27.58 ? 547 HOH A O   1 
HETATM 2310 O  O   . HOH F 6 .   ? 10.992  7.927   -3.943  1.00 39.06 ? 548 HOH A O   1 
HETATM 2311 O  O   . HOH F 6 .   ? 12.408  -13.468 33.116  1.00 34.20 ? 549 HOH A O   1 
HETATM 2312 O  O   . HOH F 6 .   ? 23.718  -9.496  9.506   1.00 23.63 ? 550 HOH A O   1 
HETATM 2313 O  O   . HOH F 6 .   ? 25.647  -4.967  7.908   1.00 31.49 ? 551 HOH A O   1 
HETATM 2314 O  O   . HOH F 6 .   ? -5.316  -5.708  30.422  1.00 35.49 ? 552 HOH A O   1 
HETATM 2315 O  O   . HOH F 6 .   ? -3.926  -5.920  9.228   1.00 21.31 ? 553 HOH A O   1 
HETATM 2316 O  O   . HOH F 6 .   ? 29.561  5.035   27.993  1.00 37.72 ? 554 HOH A O   1 
HETATM 2317 O  O   . HOH F 6 .   ? 34.251  -4.094  24.393  1.00 28.80 ? 555 HOH A O   1 
HETATM 2318 O  O   . HOH F 6 .   ? 23.770  8.326   32.653  1.00 38.91 ? 556 HOH A O   1 
HETATM 2319 O  O   . HOH F 6 .   ? 22.390  -4.794  34.376  1.00 28.47 ? 557 HOH A O   1 
HETATM 2320 O  O   . HOH F 6 .   ? 8.469   9.645   28.965  1.00 29.12 ? 558 HOH A O   1 
HETATM 2321 O  O   . HOH F 6 .   ? 22.830  9.976   25.080  1.00 20.32 ? 559 HOH A O   1 
HETATM 2322 O  O   . HOH F 6 .   ? 19.779  10.676  15.231  1.00 44.24 ? 560 HOH A O   1 
HETATM 2323 O  O   . HOH F 6 .   ? 22.361  0.110   29.541  1.00 17.10 ? 561 HOH A O   1 
HETATM 2324 O  O   . HOH F 6 .   ? 20.399  -6.831  32.671  1.00 25.23 ? 562 HOH A O   1 
HETATM 2325 O  O   . HOH F 6 .   ? 35.325  7.481   19.588  1.00 33.63 ? 563 HOH A O   1 
HETATM 2326 O  O   . HOH F 6 .   ? 9.761   11.346  7.889   1.00 34.16 ? 564 HOH A O   1 
HETATM 2327 O  O   . HOH F 6 .   ? 20.739  11.335  18.035  1.00 33.18 ? 565 HOH A O   1 
HETATM 2328 O  O   . HOH F 6 .   ? 19.900  25.500  17.950  1.00 30.70 ? 566 HOH A O   1 
HETATM 2329 O  O   . HOH F 6 .   ? 35.135  3.920   23.049  1.00 33.84 ? 567 HOH A O   1 
HETATM 2330 O  O   . HOH F 6 .   ? 14.695  17.590  11.891  1.00 27.64 ? 568 HOH A O   1 
HETATM 2331 O  O   . HOH F 6 .   ? 8.640   11.593  -5.847  1.00 34.35 ? 569 HOH A O   1 
HETATM 2332 O  O   . HOH F 6 .   ? -5.749  -2.067  25.252  1.00 24.72 ? 570 HOH A O   1 
HETATM 2333 O  O   . HOH F 6 .   ? -9.696  -10.608 22.224  1.00 35.32 ? 571 HOH A O   1 
HETATM 2334 O  O   . HOH F 6 .   ? 3.247   8.353   38.586  1.00 39.44 ? 572 HOH A O   1 
HETATM 2335 O  O   . HOH F 6 .   ? 11.996  -4.115  35.896  1.00 22.10 ? 573 HOH A O   1 
HETATM 2336 O  O   . HOH F 6 .   ? 18.971  -10.538 22.810  1.00 12.05 ? 574 HOH A O   1 
HETATM 2337 O  O   . HOH F 6 .   ? 12.551  -18.010 26.503  1.00 30.64 ? 575 HOH A O   1 
HETATM 2338 O  O   . HOH F 6 .   ? 26.177  -8.985  18.800  1.00 48.20 ? 576 HOH A O   1 
HETATM 2339 O  O   . HOH F 6 .   ? 30.902  -11.798 9.529   1.00 44.15 ? 577 HOH A O   1 
HETATM 2340 O  O   . HOH F 6 .   ? -1.934  -9.900  14.075  1.00 22.91 ? 578 HOH A O   1 
HETATM 2341 O  O   . HOH F 6 .   ? -3.133  1.124   4.085   1.00 24.73 ? 579 HOH A O   1 
HETATM 2342 O  O   . HOH F 6 .   ? -10.545 7.309   12.858  1.00 41.57 ? 580 HOH A O   1 
HETATM 2343 O  O   . HOH F 6 .   ? 24.615  -2.688  6.818   1.00 38.79 ? 581 HOH A O   1 
HETATM 2344 O  O   . HOH F 6 .   ? 12.912  -17.525 21.720  1.00 20.40 ? 582 HOH A O   1 
HETATM 2345 O  O   . HOH F 6 .   ? 14.102  3.288   35.342  1.00 32.55 ? 583 HOH A O   1 
HETATM 2346 O  O   . HOH F 6 .   ? 8.237   5.497   -6.792  1.00 26.89 ? 584 HOH A O   1 
HETATM 2347 O  O   . HOH F 6 .   ? 5.775   -18.485 22.613  1.00 35.36 ? 585 HOH A O   1 
HETATM 2348 O  O   . HOH F 6 .   ? 1.940   5.225   -3.302  1.00 29.79 ? 586 HOH A O   1 
HETATM 2349 O  O   . HOH F 6 .   ? -0.041  -17.944 6.681   1.00 30.45 ? 587 HOH A O   1 
HETATM 2350 O  O   . HOH F 6 .   ? 20.840  -12.453 22.175  1.00 23.72 ? 588 HOH A O   1 
HETATM 2351 O  O   . HOH F 6 .   ? 15.485  5.518   -5.640  1.00 32.36 ? 589 HOH A O   1 
HETATM 2352 O  O   . HOH F 6 .   ? -10.838 -8.962  16.359  1.00 30.22 ? 590 HOH A O   1 
HETATM 2353 O  O   . HOH F 6 .   ? -6.645  6.338   24.560  1.00 31.47 ? 591 HOH A O   1 
HETATM 2354 O  O   . HOH F 6 .   ? 6.094   -14.032 25.180  1.00 48.34 ? 592 HOH A O   1 
HETATM 2355 O  O   . HOH F 6 .   ? 28.727  7.958   22.056  1.00 19.29 ? 593 HOH A O   1 
HETATM 2356 O  O   . HOH F 6 .   ? 11.519  -6.112  34.000  1.00 22.64 ? 594 HOH A O   1 
HETATM 2357 O  O   . HOH F 6 .   ? 10.969  16.815  12.062  1.00 28.38 ? 595 HOH A O   1 
HETATM 2358 O  O   . HOH F 6 .   ? -3.607  -7.684  1.996   1.00 28.61 ? 596 HOH A O   1 
HETATM 2359 O  O   . HOH F 6 .   ? -3.143  1.555   1.198   1.00 30.23 ? 597 HOH A O   1 
HETATM 2360 O  O   . HOH F 6 .   ? 15.535  -10.651 -5.435  1.00 35.83 ? 598 HOH A O   1 
HETATM 2361 O  O   . HOH F 6 .   ? -2.525  1.581   31.984  1.00 35.91 ? 599 HOH A O   1 
HETATM 2362 O  O   . HOH F 6 .   ? 4.031   21.437  21.533  1.00 39.45 ? 600 HOH A O   1 
HETATM 2363 O  O   . HOH F 6 .   ? 20.473  12.035  25.554  1.00 38.48 ? 601 HOH A O   1 
HETATM 2364 O  O   . HOH F 6 .   ? -5.827  -10.902 20.169  1.00 33.30 ? 602 HOH A O   1 
HETATM 2365 O  O   . HOH F 6 .   ? 23.372  -12.763 -1.268  1.00 37.03 ? 603 HOH A O   1 
HETATM 2366 O  O   . HOH F 6 .   ? 7.250   18.051  29.024  1.00 30.18 ? 604 HOH A O   1 
HETATM 2367 O  O   . HOH F 6 .   ? 16.596  22.303  20.986  1.00 44.04 ? 605 HOH A O   1 
HETATM 2368 O  O   . HOH F 6 .   ? 34.018  -1.888  13.544  1.00 27.86 ? 606 HOH A O   1 
HETATM 2369 O  O   . HOH F 6 .   ? 29.780  -2.808  23.783  1.00 29.83 ? 607 HOH A O   1 
HETATM 2370 O  O   . HOH F 6 .   ? 22.177  13.836  20.168  1.00 35.13 ? 608 HOH A O   1 
HETATM 2371 O  O   . HOH F 6 .   ? 13.970  13.252  7.718   1.00 41.57 ? 609 HOH A O   1 
HETATM 2372 O  O   . HOH F 6 .   ? 23.971  5.892   10.045  1.00 49.34 ? 610 HOH A O   1 
HETATM 2373 O  O   . HOH F 6 .   ? 25.499  -9.663  23.336  1.00 38.79 ? 611 HOH A O   1 
HETATM 2374 O  O   . HOH F 6 .   ? 27.428  0.361   34.959  1.00 43.46 ? 612 HOH A O   1 
HETATM 2375 O  O   . HOH F 6 .   ? 11.505  -2.984  -9.291  1.00 36.95 ? 613 HOH A O   1 
HETATM 2376 O  O   . HOH F 6 .   ? 8.240   -15.362 16.941  1.00 19.67 ? 614 HOH A O   1 
HETATM 2377 O  O   . HOH F 6 .   ? 31.343  -7.183  8.392   1.00 41.29 ? 615 HOH A O   1 
HETATM 2378 O  O   . HOH F 6 .   ? -4.071  7.069   35.682  1.00 41.98 ? 616 HOH A O   1 
HETATM 2379 O  O   . HOH F 6 .   ? 2.989   -6.991  34.899  1.00 29.35 ? 617 HOH A O   1 
HETATM 2380 O  O   . HOH F 6 .   ? 24.701  -12.675 -6.117  1.00 29.94 ? 618 HOH A O   1 
HETATM 2381 O  O   . HOH F 6 .   ? -4.063  13.212  19.785  1.00 32.36 ? 619 HOH A O   1 
HETATM 2382 O  O   . HOH F 6 .   ? 19.057  -15.592 25.234  1.00 28.53 ? 620 HOH A O   1 
HETATM 2383 O  O   . HOH F 6 .   ? 31.510  -0.357  13.800  1.00 30.53 ? 621 HOH A O   1 
HETATM 2384 O  O   . HOH F 6 .   ? 3.305   21.841  17.560  1.00 25.87 ? 622 HOH A O   1 
HETATM 2385 O  O   . HOH F 6 .   ? -2.815  -1.623  4.054   1.00 35.01 ? 623 HOH A O   1 
HETATM 2386 O  O   . HOH F 6 .   ? 21.662  2.732   -6.543  1.00 26.54 ? 624 HOH A O   1 
HETATM 2387 O  O   . HOH F 6 .   ? 8.585   7.933   31.014  1.00 33.59 ? 625 HOH A O   1 
HETATM 2388 O  O   . HOH F 6 .   ? -3.546  11.410  26.847  1.00 43.84 ? 626 HOH A O   1 
HETATM 2389 O  O   . HOH F 6 .   ? 22.086  5.165   1.743   1.00 37.42 ? 627 HOH A O   1 
HETATM 2390 O  O   . HOH F 6 .   ? 22.652  -14.268 19.138  1.00 43.40 ? 628 HOH A O   1 
HETATM 2391 O  O   . HOH F 6 .   ? 4.270   -16.122 20.191  1.00 27.31 ? 629 HOH A O   1 
HETATM 2392 O  O   . HOH F 6 .   ? 10.760  6.741   30.639  1.00 33.31 ? 630 HOH A O   1 
HETATM 2393 O  O   . HOH F 6 .   ? 24.004  -11.732 8.219   1.00 32.37 ? 631 HOH A O   1 
HETATM 2394 O  O   . HOH F 6 .   ? 19.039  -10.353 31.553  1.00 33.05 ? 632 HOH A O   1 
HETATM 2395 O  O   . HOH F 6 .   ? 19.768  -11.224 26.847  1.00 25.41 ? 633 HOH A O   1 
HETATM 2396 O  O   . HOH F 6 .   ? 19.396  1.422   11.115  1.00 36.52 ? 634 HOH A O   1 
HETATM 2397 O  O   . HOH F 6 .   ? 21.894  -14.021 23.994  1.00 37.70 ? 635 HOH A O   1 
HETATM 2398 O  O   . HOH F 6 .   ? -2.976  -5.464  0.403   1.00 37.40 ? 636 HOH A O   1 
HETATM 2399 O  O   . HOH F 6 .   ? 4.090   -12.100 26.232  1.00 25.87 ? 637 HOH A O   1 
HETATM 2400 O  O   . HOH F 6 .   ? 25.245  -11.430 21.398  1.00 32.70 ? 638 HOH A O   1 
HETATM 2401 O  O   . HOH F 6 .   ? 12.691  -15.807 34.490  1.00 26.44 ? 639 HOH A O   1 
HETATM 2402 O  O   . HOH F 6 .   ? 15.981  -8.020  33.743  1.00 33.54 ? 640 HOH A O   1 
HETATM 2403 O  O   . HOH F 6 .   ? -0.421  -11.967 23.079  1.00 29.77 ? 641 HOH A O   1 
HETATM 2404 O  O   . HOH F 6 .   ? 36.621  0.466   26.198  1.00 31.92 ? 642 HOH A O   1 
HETATM 2405 O  O   . HOH F 6 .   ? 9.525   12.731  0.868   1.00 29.36 ? 643 HOH A O   1 
HETATM 2406 O  O   . HOH F 6 .   ? 16.675  2.934   43.251  1.00 33.57 ? 644 HOH A O   1 
HETATM 2407 O  O   . HOH F 6 .   ? 22.346  5.250   -4.864  1.00 37.59 ? 645 HOH A O   1 
HETATM 2408 O  O   . HOH F 6 .   ? 9.814   -9.388  -2.869  1.00 34.04 ? 646 HOH A O   1 
HETATM 2409 O  O   . HOH F 6 .   ? 13.958  -8.081  -4.499  1.00 32.36 ? 647 HOH A O   1 
HETATM 2410 O  O   . HOH F 6 .   ? 3.185   -10.332 31.617  1.00 34.23 ? 648 HOH A O   1 
HETATM 2411 O  O   . HOH F 6 .   ? 27.131  7.253   30.028  1.00 35.15 ? 649 HOH A O   1 
HETATM 2412 O  O   . HOH F 6 .   ? 19.998  -9.425  28.957  1.00 20.48 ? 650 HOH A O   1 
HETATM 2413 O  O   . HOH F 6 .   ? 8.885   15.471  4.975   1.00 29.01 ? 651 HOH A O   1 
HETATM 2414 O  O   . HOH F 6 .   ? 23.175  -12.254 20.430  1.00 33.97 ? 652 HOH A O   1 
HETATM 2415 O  O   . HOH F 6 .   ? 1.381   -13.137 25.370  1.00 39.96 ? 653 HOH A O   1 
HETATM 2416 O  O   . HOH F 6 .   ? 19.366  4.900   -7.012  1.00 35.38 ? 654 HOH A O   1 
HETATM 2417 O  O   . HOH F 6 .   ? 27.769  10.239  18.253  1.00 34.60 ? 655 HOH A O   1 
HETATM 2418 O  O   . HOH F 6 .   ? 20.739  -5.086  -7.547  1.00 38.15 ? 656 HOH A O   1 
HETATM 2419 O  O   . HOH F 6 .   ? 1.110   -13.648 22.527  1.00 28.99 ? 657 HOH A O   1 
HETATM 2420 O  O   . HOH F 6 .   ? 25.117  10.669  23.783  1.00 30.93 ? 658 HOH A O   1 
HETATM 2421 O  O   . HOH F 6 .   ? 7.054   5.413   33.366  1.00 35.10 ? 659 HOH A O   1 
HETATM 2422 O  O   . HOH F 6 .   ? 0.863   -14.741 20.339  1.00 45.11 ? 660 HOH A O   1 
HETATM 2423 O  O   . HOH F 6 .   ? 33.463  -5.453  -1.920  1.00 33.77 ? 661 HOH A O   1 
# 
