data_6R6J
# 
_entry.id   6R6J 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.383 
_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   6R6J         pdb_00006r6j 10.2210/pdb6r6j/pdb 
WWPDB D_1292101509 ?            ?                   
# 
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 2020-04-08 
2 'Structure model' 1 1 2021-10-06 
3 'Structure model' 1 2 2024-01-24 
# 
_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' 'Database references'    
3 2 'Structure model' 'Structure summary'      
4 3 'Structure model' 'Data collection'        
5 3 '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' database_2                    
2 2 'Structure model' pdbx_contact_author           
3 2 'Structure model' pdbx_database_proc            
4 3 'Structure model' chem_comp_atom                
5 3 'Structure model' chem_comp_bond                
6 3 'Structure model' pdbx_initial_refinement_model 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_database_2.pdbx_DOI'                
2 2 'Structure model' '_database_2.pdbx_database_accession' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        6R6J 
_pdbx_database_status.recvd_initial_deposition_date   2019-03-27 
_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.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_nmr_data            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Smirnov, A.'  1 ? 
'Manakova, E.' 2 ? 
'Grazulis, S.' 3 ? 
# 
_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                   FR 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Eur.J.Med.Chem. 
_citation.journal_id_ASTM           EJMCA5 
_citation.journal_id_CSD            0493 
_citation.journal_id_ISSN           0223-5234 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            185 
_citation.language                  ? 
_citation.page_first                111825 
_citation.page_last                 111825 
_citation.title                     
'Halogenated and di-substituted benzenesulfonamides as selective inhibitors of carbonic anhydrase isoforms.' 
_citation.year                      2020 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.ejmech.2019.111825 
_citation.pdbx_database_id_PubMed   31740053 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Zaksauskas, A.'   1  ? 
primary 'Capkauskaite, E.' 2  ? 
primary 'Jezepcikas, L.'   3  ? 
primary 'Linkuviene, V.'   4  ? 
primary 'Paketuryte, V.'   5  ? 
primary 'Smirnov, A.'      6  ? 
primary 'Leitans, J.'      7  ? 
primary 'Kazaks, A.'       8  ? 
primary 'Dvinskis, E.'     9  ? 
primary 'Manakova, E.'     10 ? 
primary 'Grazulis, S.'     11 ? 
primary 'Tars, K.'         12 ? 
primary 'Matulis, D.'      13 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Carbonic anhydrase 2'                                                       29289.062 1   4.2.1.1 ? 
'human carbonic anhydrase II' ? 
2 non-polymer syn 'ZINC ION'                                                                   65.409    1   ?       ? ? ? 
3 non-polymer syn 'DIMETHYL SULFOXIDE'                                                         78.133    1   ?       ? ? ? 
4 non-polymer syn '2-(N-MORPHOLINO)-ETHANESULFONIC ACID'                                       195.237   1   ?       ? ? ? 
5 non-polymer syn '4-chloranyl-~{N}-(2-hydroxyethyl)-2-(phenylsulfonyl)-5-sulfamoyl-benzamide' 418.872   1   ?       ? ? ? 
6 water       nat water                                                                        18.015    182 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Carbonate dehydratase II,Carbonic anhydrase C,CAC,Carbonic anhydrase II,CA-II' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION'                                                                   ZN  
3 'DIMETHYL SULFOXIDE'                                                         DMS 
4 '2-(N-MORPHOLINO)-ETHANESULFONIC ACID'                                       MES 
5 '4-chloranyl-~{N}-(2-hydroxyethyl)-2-(phenylsulfonyl)-5-sulfamoyl-benzamide' JTW 
6 water                                                                        HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   SER n 
1 3   HIS n 
1 4   HIS n 
1 5   TRP n 
1 6   GLY n 
1 7   TYR n 
1 8   GLY n 
1 9   LYS n 
1 10  HIS n 
1 11  ASN n 
1 12  GLY n 
1 13  PRO n 
1 14  GLU n 
1 15  HIS n 
1 16  TRP n 
1 17  HIS n 
1 18  LYS n 
1 19  ASP n 
1 20  PHE n 
1 21  PRO n 
1 22  ILE n 
1 23  ALA n 
1 24  LYS n 
1 25  GLY n 
1 26  GLU n 
1 27  ARG n 
1 28  GLN n 
1 29  SER n 
1 30  PRO n 
1 31  VAL n 
1 32  ASP n 
1 33  ILE n 
1 34  ASP n 
1 35  THR n 
1 36  HIS n 
1 37  THR n 
1 38  ALA n 
1 39  LYS n 
1 40  TYR n 
1 41  ASP n 
1 42  PRO n 
1 43  SER n 
1 44  LEU n 
1 45  LYS n 
1 46  PRO n 
1 47  LEU n 
1 48  SER n 
1 49  VAL n 
1 50  SER n 
1 51  TYR n 
1 52  ASP n 
1 53  GLN n 
1 54  ALA n 
1 55  THR n 
1 56  SER n 
1 57  LEU n 
1 58  ARG n 
1 59  ILE n 
1 60  LEU n 
1 61  ASN n 
1 62  ASN n 
1 63  GLY n 
1 64  HIS n 
1 65  ALA n 
1 66  PHE n 
1 67  ASN n 
1 68  VAL n 
1 69  GLU n 
1 70  PHE n 
1 71  ASP n 
1 72  ASP n 
1 73  SER n 
1 74  GLN n 
1 75  ASP n 
1 76  LYS n 
1 77  ALA n 
1 78  VAL n 
1 79  LEU n 
1 80  LYS n 
1 81  GLY n 
1 82  GLY n 
1 83  PRO n 
1 84  LEU n 
1 85  ASP n 
1 86  GLY n 
1 87  THR n 
1 88  TYR n 
1 89  ARG n 
1 90  LEU n 
1 91  ILE n 
1 92  GLN n 
1 93  PHE n 
1 94  HIS n 
1 95  PHE n 
1 96  HIS n 
1 97  TRP n 
1 98  GLY n 
1 99  SER n 
1 100 LEU n 
1 101 ASP n 
1 102 GLY n 
1 103 GLN n 
1 104 GLY n 
1 105 SER n 
1 106 GLU n 
1 107 HIS n 
1 108 THR n 
1 109 VAL n 
1 110 ASP n 
1 111 LYS n 
1 112 LYS n 
1 113 LYS n 
1 114 TYR n 
1 115 ALA n 
1 116 ALA n 
1 117 GLU n 
1 118 LEU n 
1 119 HIS n 
1 120 LEU n 
1 121 VAL n 
1 122 HIS n 
1 123 TRP n 
1 124 ASN n 
1 125 THR n 
1 126 LYS n 
1 127 TYR n 
1 128 GLY n 
1 129 ASP n 
1 130 PHE n 
1 131 GLY n 
1 132 LYS n 
1 133 ALA n 
1 134 VAL n 
1 135 GLN n 
1 136 GLN n 
1 137 PRO n 
1 138 ASP n 
1 139 GLY n 
1 140 LEU n 
1 141 ALA n 
1 142 VAL n 
1 143 LEU n 
1 144 GLY n 
1 145 ILE n 
1 146 PHE n 
1 147 LEU n 
1 148 LYS n 
1 149 VAL n 
1 150 GLY n 
1 151 SER n 
1 152 ALA n 
1 153 LYS n 
1 154 PRO n 
1 155 GLY n 
1 156 LEU n 
1 157 GLN n 
1 158 LYS n 
1 159 VAL n 
1 160 VAL n 
1 161 ASP n 
1 162 VAL n 
1 163 LEU n 
1 164 ASP n 
1 165 SER n 
1 166 ILE n 
1 167 LYS n 
1 168 THR n 
1 169 LYS n 
1 170 GLY n 
1 171 LYS n 
1 172 SER n 
1 173 ALA n 
1 174 ASP n 
1 175 PHE n 
1 176 THR n 
1 177 ASN n 
1 178 PHE n 
1 179 ASP n 
1 180 PRO n 
1 181 ARG n 
1 182 GLY n 
1 183 LEU n 
1 184 LEU n 
1 185 PRO n 
1 186 GLU n 
1 187 SER n 
1 188 LEU n 
1 189 ASP n 
1 190 TYR n 
1 191 TRP n 
1 192 THR n 
1 193 TYR n 
1 194 PRO n 
1 195 GLY n 
1 196 SER n 
1 197 LEU n 
1 198 THR n 
1 199 THR n 
1 200 PRO n 
1 201 PRO n 
1 202 LEU n 
1 203 LEU n 
1 204 GLU n 
1 205 CYS n 
1 206 VAL n 
1 207 THR n 
1 208 TRP n 
1 209 ILE n 
1 210 VAL n 
1 211 LEU n 
1 212 LYS n 
1 213 GLU n 
1 214 PRO n 
1 215 ILE n 
1 216 SER n 
1 217 VAL n 
1 218 SER n 
1 219 SER n 
1 220 GLU n 
1 221 GLN n 
1 222 VAL n 
1 223 LEU n 
1 224 LYS n 
1 225 PHE n 
1 226 ARG n 
1 227 LYS n 
1 228 LEU n 
1 229 ASN n 
1 230 PHE n 
1 231 ASN n 
1 232 GLY n 
1 233 GLU n 
1 234 GLY n 
1 235 GLU n 
1 236 PRO n 
1 237 GLU n 
1 238 GLU n 
1 239 LEU n 
1 240 MET n 
1 241 VAL n 
1 242 ASP n 
1 243 ASN n 
1 244 TRP n 
1 245 ARG n 
1 246 PRO n 
1 247 ALA n 
1 248 GLN n 
1 249 PRO n 
1 250 LEU n 
1 251 LYS n 
1 252 ASN n 
1 253 ARG n 
1 254 GLN n 
1 255 ILE n 
1 256 LYS n 
1 257 ALA n 
1 258 SER n 
1 259 PHE n 
1 260 LYS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   260 
_entity_src_gen.gene_src_common_name               Human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 CA2 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pET15b 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
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 
JTW non-polymer         . '4-chloranyl-~{N}-(2-hydroxyethyl)-2-(phenylsulfonyl)-5-sulfamoyl-benzamide' ? 'C15 H15 Cl N2 O6 S2' 
418.872 
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 
MES non-polymer         . '2-(N-MORPHOLINO)-ETHANESULFONIC ACID'                                       ? 'C6 H13 N O4 S'       
195.237 
MET 'L-peptide linking' y METHIONINE                                                                   ? 'C5 H11 N O2 S'       
149.211 
PHE 'L-peptide linking' y PHENYLALANINE                                                                ? 'C9 H11 N O2'         
165.189 
PRO 'L-peptide linking' y PROLINE                                                                      ? 'C5 H9 N O2'          
115.130 
SER 'L-peptide linking' y SERINE                                                                       ? 'C3 H7 N O3'          
105.093 
THR 'L-peptide linking' y THREONINE                                                                    ? 'C4 H9 N O3'          
119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                                                   ? 'C11 H12 N2 O2'       
204.225 
TYR 'L-peptide linking' y TYROSINE                                                                     ? 'C9 H11 N O3'         
181.189 
VAL 'L-peptide linking' y VALINE                                                                       ? 'C5 H11 N O2'         
117.146 
ZN  non-polymer         . 'ZINC ION'                                                                   ? 'Zn 2'                
65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   SER 2   2   ?   ?   ?   A . n 
A 1 3   HIS 3   3   ?   ?   ?   A . n 
A 1 4   HIS 4   4   4   HIS HIS A . n 
A 1 5   TRP 5   5   5   TRP TRP A . n 
A 1 6   GLY 6   6   6   GLY GLY A . n 
A 1 7   TYR 7   7   7   TYR TYR A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   LYS 9   9   9   LYS LYS A . n 
A 1 10  HIS 10  10  10  HIS HIS A . n 
A 1 11  ASN 11  11  11  ASN ASN A . n 
A 1 12  GLY 12  12  12  GLY GLY A . n 
A 1 13  PRO 13  13  13  PRO PRO A . n 
A 1 14  GLU 14  14  14  GLU GLU A . n 
A 1 15  HIS 15  15  15  HIS HIS A . n 
A 1 16  TRP 16  16  16  TRP TRP A . n 
A 1 17  HIS 17  17  17  HIS HIS A . n 
A 1 18  LYS 18  18  18  LYS LYS A . n 
A 1 19  ASP 19  19  19  ASP ASP A . n 
A 1 20  PHE 20  20  20  PHE PHE A . n 
A 1 21  PRO 21  21  21  PRO PRO A . n 
A 1 22  ILE 22  22  22  ILE ILE A . n 
A 1 23  ALA 23  23  23  ALA ALA A . n 
A 1 24  LYS 24  24  24  LYS LYS A . n 
A 1 25  GLY 25  25  25  GLY GLY A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  ARG 27  27  27  ARG ARG A . n 
A 1 28  GLN 28  28  28  GLN GLN A . n 
A 1 29  SER 29  29  29  SER SER A . n 
A 1 30  PRO 30  30  30  PRO PRO A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  ASP 32  32  32  ASP ASP A . n 
A 1 33  ILE 33  33  33  ILE ILE A . n 
A 1 34  ASP 34  34  34  ASP ASP A . n 
A 1 35  THR 35  35  35  THR THR A . n 
A 1 36  HIS 36  36  36  HIS HIS A . n 
A 1 37  THR 37  37  37  THR THR A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  LYS 39  39  39  LYS LYS A . n 
A 1 40  TYR 40  40  40  TYR TYR A . n 
A 1 41  ASP 41  41  41  ASP ASP A . n 
A 1 42  PRO 42  42  42  PRO PRO A . n 
A 1 43  SER 43  43  43  SER SER A . n 
A 1 44  LEU 44  44  44  LEU LEU A . n 
A 1 45  LYS 45  45  45  LYS LYS A . n 
A 1 46  PRO 46  46  46  PRO PRO A . n 
A 1 47  LEU 47  47  47  LEU LEU A . n 
A 1 48  SER 48  48  48  SER SER A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  SER 50  50  50  SER SER A . n 
A 1 51  TYR 51  51  51  TYR TYR A . n 
A 1 52  ASP 52  52  52  ASP ASP A . n 
A 1 53  GLN 53  53  53  GLN GLN A . n 
A 1 54  ALA 54  54  54  ALA ALA A . n 
A 1 55  THR 55  55  55  THR THR A . n 
A 1 56  SER 56  56  56  SER SER A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  ARG 58  58  58  ARG ARG A . n 
A 1 59  ILE 59  59  59  ILE ILE A . n 
A 1 60  LEU 60  60  60  LEU LEU A . n 
A 1 61  ASN 61  61  61  ASN ASN A . n 
A 1 62  ASN 62  62  62  ASN ASN A . n 
A 1 63  GLY 63  63  63  GLY GLY A . n 
A 1 64  HIS 64  64  64  HIS HIS A . n 
A 1 65  ALA 65  65  65  ALA ALA A . n 
A 1 66  PHE 66  66  66  PHE PHE A . n 
A 1 67  ASN 67  67  67  ASN ASN A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  GLU 69  69  69  GLU GLU A . n 
A 1 70  PHE 70  70  70  PHE PHE A . n 
A 1 71  ASP 71  71  71  ASP ASP A . n 
A 1 72  ASP 72  72  72  ASP ASP A . n 
A 1 73  SER 73  73  73  SER SER A . n 
A 1 74  GLN 74  74  74  GLN GLN A . n 
A 1 75  ASP 75  75  75  ASP ASP A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  ALA 77  77  77  ALA ALA A . n 
A 1 78  VAL 78  78  78  VAL VAL A . n 
A 1 79  LEU 79  79  79  LEU LEU A . n 
A 1 80  LYS 80  80  80  LYS LYS A . n 
A 1 81  GLY 81  81  81  GLY GLY A . n 
A 1 82  GLY 82  82  82  GLY GLY A . n 
A 1 83  PRO 83  83  83  PRO PRO A . n 
A 1 84  LEU 84  84  84  LEU LEU A . n 
A 1 85  ASP 85  85  85  ASP ASP A . n 
A 1 86  GLY 86  86  86  GLY GLY A . n 
A 1 87  THR 87  87  87  THR THR A . n 
A 1 88  TYR 88  88  88  TYR TYR A . n 
A 1 89  ARG 89  89  89  ARG ARG A . n 
A 1 90  LEU 90  90  90  LEU LEU A . n 
A 1 91  ILE 91  91  91  ILE ILE A . n 
A 1 92  GLN 92  92  92  GLN GLN A . n 
A 1 93  PHE 93  93  93  PHE PHE A . n 
A 1 94  HIS 94  94  94  HIS HIS A . n 
A 1 95  PHE 95  95  95  PHE PHE A . n 
A 1 96  HIS 96  96  96  HIS HIS A . n 
A 1 97  TRP 97  97  97  TRP TRP A . n 
A 1 98  GLY 98  98  98  GLY GLY A . n 
A 1 99  SER 99  99  99  SER SER A . n 
A 1 100 LEU 100 100 100 LEU LEU A . n 
A 1 101 ASP 101 101 101 ASP ASP A . n 
A 1 102 GLY 102 102 102 GLY GLY A . n 
A 1 103 GLN 103 103 103 GLN GLN A . n 
A 1 104 GLY 104 104 104 GLY GLY A . n 
A 1 105 SER 105 105 105 SER SER A . n 
A 1 106 GLU 106 106 106 GLU GLU A . n 
A 1 107 HIS 107 107 107 HIS HIS A . n 
A 1 108 THR 108 108 108 THR THR A . n 
A 1 109 VAL 109 109 109 VAL VAL A . n 
A 1 110 ASP 110 110 110 ASP ASP A . n 
A 1 111 LYS 111 111 111 LYS LYS A . n 
A 1 112 LYS 112 112 112 LYS LYS A . n 
A 1 113 LYS 113 113 113 LYS LYS A . n 
A 1 114 TYR 114 114 114 TYR TYR A . n 
A 1 115 ALA 115 115 115 ALA ALA A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 GLU 117 117 117 GLU GLU A . n 
A 1 118 LEU 118 118 118 LEU LEU A . n 
A 1 119 HIS 119 119 119 HIS HIS A . n 
A 1 120 LEU 120 120 120 LEU LEU A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 HIS 122 122 122 HIS HIS A . n 
A 1 123 TRP 123 123 123 TRP TRP A . n 
A 1 124 ASN 124 124 124 ASN ASN A . n 
A 1 125 THR 125 125 125 THR THR A . n 
A 1 126 LYS 126 127 127 LYS LYS A . n 
A 1 127 TYR 127 128 128 TYR TYR A . n 
A 1 128 GLY 128 129 129 GLY GLY A . n 
A 1 129 ASP 129 130 130 ASP ASP A . n 
A 1 130 PHE 130 131 131 PHE PHE A . n 
A 1 131 GLY 131 132 132 GLY GLY A . n 
A 1 132 LYS 132 133 133 LYS LYS A . n 
A 1 133 ALA 133 134 134 ALA ALA A . n 
A 1 134 VAL 134 135 135 VAL VAL A . n 
A 1 135 GLN 135 136 136 GLN GLN A . n 
A 1 136 GLN 136 137 137 GLN GLN A . n 
A 1 137 PRO 137 138 138 PRO PRO A . n 
A 1 138 ASP 138 139 139 ASP ASP A . n 
A 1 139 GLY 139 140 140 GLY GLY A . n 
A 1 140 LEU 140 141 141 LEU LEU A . n 
A 1 141 ALA 141 142 142 ALA ALA A . n 
A 1 142 VAL 142 143 143 VAL VAL A . n 
A 1 143 LEU 143 144 144 LEU LEU A . n 
A 1 144 GLY 144 145 145 GLY GLY A . n 
A 1 145 ILE 145 146 146 ILE ILE A . n 
A 1 146 PHE 146 147 147 PHE PHE A . n 
A 1 147 LEU 147 148 148 LEU LEU A . n 
A 1 148 LYS 148 149 149 LYS LYS A . n 
A 1 149 VAL 149 150 150 VAL VAL A . n 
A 1 150 GLY 150 151 151 GLY GLY A . n 
A 1 151 SER 151 152 152 SER SER A . n 
A 1 152 ALA 152 153 153 ALA ALA A . n 
A 1 153 LYS 153 154 154 LYS LYS A . n 
A 1 154 PRO 154 155 155 PRO PRO A . n 
A 1 155 GLY 155 156 156 GLY GLY A . n 
A 1 156 LEU 156 157 157 LEU LEU A . n 
A 1 157 GLN 157 158 158 GLN GLN A . n 
A 1 158 LYS 158 159 159 LYS LYS A . n 
A 1 159 VAL 159 160 160 VAL VAL A . n 
A 1 160 VAL 160 161 161 VAL VAL A . n 
A 1 161 ASP 161 162 162 ASP ASP A . n 
A 1 162 VAL 162 163 163 VAL VAL A . n 
A 1 163 LEU 163 164 164 LEU LEU A . n 
A 1 164 ASP 164 165 165 ASP ASP A . n 
A 1 165 SER 165 166 166 SER SER A . n 
A 1 166 ILE 166 167 167 ILE ILE A . n 
A 1 167 LYS 167 168 168 LYS LYS A . n 
A 1 168 THR 168 169 169 THR THR A . n 
A 1 169 LYS 169 170 170 LYS LYS A . n 
A 1 170 GLY 170 171 171 GLY GLY A . n 
A 1 171 LYS 171 172 172 LYS LYS A . n 
A 1 172 SER 172 173 173 SER SER A . n 
A 1 173 ALA 173 174 174 ALA ALA A . n 
A 1 174 ASP 174 175 175 ASP ASP A . n 
A 1 175 PHE 175 176 176 PHE PHE A . n 
A 1 176 THR 176 177 177 THR THR A . n 
A 1 177 ASN 177 178 178 ASN ASN A . n 
A 1 178 PHE 178 179 179 PHE PHE A . n 
A 1 179 ASP 179 180 180 ASP ASP A . n 
A 1 180 PRO 180 181 181 PRO PRO A . n 
A 1 181 ARG 181 182 182 ARG ARG A . n 
A 1 182 GLY 182 183 183 GLY GLY A . n 
A 1 183 LEU 183 184 184 LEU LEU A . n 
A 1 184 LEU 184 185 185 LEU LEU A . n 
A 1 185 PRO 185 186 186 PRO PRO A . n 
A 1 186 GLU 186 187 187 GLU GLU A . n 
A 1 187 SER 187 188 188 SER SER A . n 
A 1 188 LEU 188 189 189 LEU LEU A . n 
A 1 189 ASP 189 190 190 ASP ASP A . n 
A 1 190 TYR 190 191 191 TYR TYR A . n 
A 1 191 TRP 191 192 192 TRP TRP A . n 
A 1 192 THR 192 193 193 THR THR A . n 
A 1 193 TYR 193 194 194 TYR TYR A . n 
A 1 194 PRO 194 195 195 PRO PRO A . n 
A 1 195 GLY 195 196 196 GLY GLY A . n 
A 1 196 SER 196 197 197 SER SER A . n 
A 1 197 LEU 197 198 198 LEU LEU A . n 
A 1 198 THR 198 199 199 THR THR A . n 
A 1 199 THR 199 200 200 THR THR A . n 
A 1 200 PRO 200 201 201 PRO PRO A . n 
A 1 201 PRO 201 202 202 PRO PRO A . n 
A 1 202 LEU 202 203 203 LEU LEU A . n 
A 1 203 LEU 203 204 204 LEU LEU A . n 
A 1 204 GLU 204 205 205 GLU GLU A . n 
A 1 205 CYS 205 206 206 CYS CYS A . n 
A 1 206 VAL 206 207 207 VAL VAL A . n 
A 1 207 THR 207 208 208 THR THR A . n 
A 1 208 TRP 208 209 209 TRP TRP A . n 
A 1 209 ILE 209 210 210 ILE ILE A . n 
A 1 210 VAL 210 211 211 VAL VAL A . n 
A 1 211 LEU 211 212 212 LEU LEU A . n 
A 1 212 LYS 212 213 213 LYS LYS A . n 
A 1 213 GLU 213 214 214 GLU GLU A . n 
A 1 214 PRO 214 215 215 PRO PRO A . n 
A 1 215 ILE 215 216 216 ILE ILE A . n 
A 1 216 SER 216 217 217 SER SER A . n 
A 1 217 VAL 217 218 218 VAL VAL A . n 
A 1 218 SER 218 219 219 SER SER A . n 
A 1 219 SER 219 220 220 SER SER A . n 
A 1 220 GLU 220 221 221 GLU GLU A . n 
A 1 221 GLN 221 222 222 GLN GLN A . n 
A 1 222 VAL 222 223 223 VAL VAL A . n 
A 1 223 LEU 223 224 224 LEU LEU A . n 
A 1 224 LYS 224 225 225 LYS LYS A . n 
A 1 225 PHE 225 226 226 PHE PHE A . n 
A 1 226 ARG 226 227 227 ARG ARG A . n 
A 1 227 LYS 227 228 228 LYS LYS A . n 
A 1 228 LEU 228 229 229 LEU LEU A . n 
A 1 229 ASN 229 230 230 ASN ASN A . n 
A 1 230 PHE 230 231 231 PHE PHE A . n 
A 1 231 ASN 231 232 232 ASN ASN A . n 
A 1 232 GLY 232 233 233 GLY GLY A . n 
A 1 233 GLU 233 234 234 GLU GLU A . n 
A 1 234 GLY 234 235 235 GLY GLY A . n 
A 1 235 GLU 235 236 236 GLU GLU A . n 
A 1 236 PRO 236 237 237 PRO PRO A . n 
A 1 237 GLU 237 238 238 GLU GLU A . n 
A 1 238 GLU 238 239 239 GLU GLU A . n 
A 1 239 LEU 239 240 240 LEU LEU A . n 
A 1 240 MET 240 241 241 MET MET A . n 
A 1 241 VAL 241 242 242 VAL VAL A . n 
A 1 242 ASP 242 243 243 ASP ASP A . n 
A 1 243 ASN 243 244 244 ASN ASN A . n 
A 1 244 TRP 244 245 245 TRP TRP A . n 
A 1 245 ARG 245 246 246 ARG ARG A . n 
A 1 246 PRO 246 247 247 PRO PRO A . n 
A 1 247 ALA 247 248 248 ALA ALA A . n 
A 1 248 GLN 248 249 249 GLN GLN A . n 
A 1 249 PRO 249 250 250 PRO PRO A . n 
A 1 250 LEU 250 251 251 LEU LEU A . n 
A 1 251 LYS 251 252 252 LYS LYS A . n 
A 1 252 ASN 252 253 253 ASN ASN A . n 
A 1 253 ARG 253 254 254 ARG ARG A . n 
A 1 254 GLN 254 255 255 GLN GLN A . n 
A 1 255 ILE 255 256 256 ILE ILE A . n 
A 1 256 LYS 256 257 257 LYS LYS A . n 
A 1 257 ALA 257 258 258 ALA ALA A . n 
A 1 258 SER 258 259 259 SER SER A . n 
A 1 259 PHE 259 260 260 PHE PHE A . n 
A 1 260 LYS 260 261 261 LYS LYS A . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 ZN  1   301 1   ZN  ZN  A . 
C 3 DMS 1   302 1   DMS DMS A . 
D 4 MES 1   303 2   MES MES A . 
E 5 JTW 1   304 1   JTW EAZ A . 
F 6 HOH 1   401 54  HOH HOH A . 
F 6 HOH 2   402 86  HOH HOH A . 
F 6 HOH 3   403 145 HOH HOH A . 
F 6 HOH 4   404 66  HOH HOH A . 
F 6 HOH 5   405 120 HOH HOH A . 
F 6 HOH 6   406 138 HOH HOH A . 
F 6 HOH 7   407 142 HOH HOH A . 
F 6 HOH 8   408 160 HOH HOH A . 
F 6 HOH 9   409 170 HOH HOH A . 
F 6 HOH 10  410 168 HOH HOH A . 
F 6 HOH 11  411 70  HOH HOH A . 
F 6 HOH 12  412 126 HOH HOH A . 
F 6 HOH 13  413 153 HOH HOH A . 
F 6 HOH 14  414 89  HOH HOH A . 
F 6 HOH 15  415 152 HOH HOH A . 
F 6 HOH 16  416 161 HOH HOH A . 
F 6 HOH 17  417 144 HOH HOH A . 
F 6 HOH 18  418 105 HOH HOH A . 
F 6 HOH 19  419 2   HOH HOH A . 
F 6 HOH 20  420 90  HOH HOH A . 
F 6 HOH 21  421 28  HOH HOH A . 
F 6 HOH 22  422 58  HOH HOH A . 
F 6 HOH 23  423 8   HOH HOH A . 
F 6 HOH 24  424 171 HOH HOH A . 
F 6 HOH 25  425 38  HOH HOH A . 
F 6 HOH 26  426 141 HOH HOH A . 
F 6 HOH 27  427 15  HOH HOH A . 
F 6 HOH 28  428 137 HOH HOH A . 
F 6 HOH 29  429 5   HOH HOH A . 
F 6 HOH 30  430 118 HOH HOH A . 
F 6 HOH 31  431 136 HOH HOH A . 
F 6 HOH 32  432 17  HOH HOH A . 
F 6 HOH 33  433 83  HOH HOH A . 
F 6 HOH 34  434 40  HOH HOH A . 
F 6 HOH 35  435 46  HOH HOH A . 
F 6 HOH 36  436 169 HOH HOH A . 
F 6 HOH 37  437 77  HOH HOH A . 
F 6 HOH 38  438 19  HOH HOH A . 
F 6 HOH 39  439 79  HOH HOH A . 
F 6 HOH 40  440 31  HOH HOH A . 
F 6 HOH 41  441 183 HOH HOH A . 
F 6 HOH 42  442 78  HOH HOH A . 
F 6 HOH 43  443 63  HOH HOH A . 
F 6 HOH 44  444 140 HOH HOH A . 
F 6 HOH 45  445 21  HOH HOH A . 
F 6 HOH 46  446 37  HOH HOH A . 
F 6 HOH 47  447 13  HOH HOH A . 
F 6 HOH 48  448 104 HOH HOH A . 
F 6 HOH 49  449 52  HOH HOH A . 
F 6 HOH 50  450 177 HOH HOH A . 
F 6 HOH 51  451 68  HOH HOH A . 
F 6 HOH 52  452 93  HOH HOH A . 
F 6 HOH 53  453 18  HOH HOH A . 
F 6 HOH 54  454 99  HOH HOH A . 
F 6 HOH 55  455 122 HOH HOH A . 
F 6 HOH 56  456 162 HOH HOH A . 
F 6 HOH 57  457 69  HOH HOH A . 
F 6 HOH 58  458 10  HOH HOH A . 
F 6 HOH 59  459 151 HOH HOH A . 
F 6 HOH 60  460 4   HOH HOH A . 
F 6 HOH 61  461 130 HOH HOH A . 
F 6 HOH 62  462 32  HOH HOH A . 
F 6 HOH 63  463 59  HOH HOH A . 
F 6 HOH 64  464 123 HOH HOH A . 
F 6 HOH 65  465 3   HOH HOH A . 
F 6 HOH 66  466 56  HOH HOH A . 
F 6 HOH 67  467 179 HOH HOH A . 
F 6 HOH 68  468 45  HOH HOH A . 
F 6 HOH 69  469 43  HOH HOH A . 
F 6 HOH 70  470 133 HOH HOH A . 
F 6 HOH 71  471 88  HOH HOH A . 
F 6 HOH 72  472 62  HOH HOH A . 
F 6 HOH 73  473 53  HOH HOH A . 
F 6 HOH 74  474 29  HOH HOH A . 
F 6 HOH 75  475 6   HOH HOH A . 
F 6 HOH 76  476 76  HOH HOH A . 
F 6 HOH 77  477 67  HOH HOH A . 
F 6 HOH 78  478 41  HOH HOH A . 
F 6 HOH 79  479 178 HOH HOH A . 
F 6 HOH 80  480 33  HOH HOH A . 
F 6 HOH 81  481 25  HOH HOH A . 
F 6 HOH 82  482 121 HOH HOH A . 
F 6 HOH 83  483 11  HOH HOH A . 
F 6 HOH 84  484 71  HOH HOH A . 
F 6 HOH 85  485 20  HOH HOH A . 
F 6 HOH 86  486 1   HOH HOH A . 
F 6 HOH 87  487 181 HOH HOH A . 
F 6 HOH 88  488 9   HOH HOH A . 
F 6 HOH 89  489 92  HOH HOH A . 
F 6 HOH 90  490 64  HOH HOH A . 
F 6 HOH 91  491 112 HOH HOH A . 
F 6 HOH 92  492 114 HOH HOH A . 
F 6 HOH 93  493 95  HOH HOH A . 
F 6 HOH 94  494 39  HOH HOH A . 
F 6 HOH 95  495 42  HOH HOH A . 
F 6 HOH 96  496 47  HOH HOH A . 
F 6 HOH 97  497 87  HOH HOH A . 
F 6 HOH 98  498 7   HOH HOH A . 
F 6 HOH 99  499 14  HOH HOH A . 
F 6 HOH 100 500 12  HOH HOH A . 
F 6 HOH 101 501 24  HOH HOH A . 
F 6 HOH 102 502 119 HOH HOH A . 
F 6 HOH 103 503 98  HOH HOH A . 
F 6 HOH 104 504 72  HOH HOH A . 
F 6 HOH 105 505 100 HOH HOH A . 
F 6 HOH 106 506 109 HOH HOH A . 
F 6 HOH 107 507 50  HOH HOH A . 
F 6 HOH 108 508 57  HOH HOH A . 
F 6 HOH 109 509 117 HOH HOH A . 
F 6 HOH 110 510 16  HOH HOH A . 
F 6 HOH 111 511 176 HOH HOH A . 
F 6 HOH 112 512 23  HOH HOH A . 
F 6 HOH 113 513 139 HOH HOH A . 
F 6 HOH 114 514 26  HOH HOH A . 
F 6 HOH 115 515 158 HOH HOH A . 
F 6 HOH 116 516 108 HOH HOH A . 
F 6 HOH 117 517 80  HOH HOH A . 
F 6 HOH 118 518 65  HOH HOH A . 
F 6 HOH 119 519 27  HOH HOH A . 
F 6 HOH 120 520 82  HOH HOH A . 
F 6 HOH 121 521 164 HOH HOH A . 
F 6 HOH 122 522 115 HOH HOH A . 
F 6 HOH 123 523 135 HOH HOH A . 
F 6 HOH 124 524 51  HOH HOH A . 
F 6 HOH 125 525 75  HOH HOH A . 
F 6 HOH 126 526 74  HOH HOH A . 
F 6 HOH 127 527 102 HOH HOH A . 
F 6 HOH 128 528 60  HOH HOH A . 
F 6 HOH 129 529 44  HOH HOH A . 
F 6 HOH 130 530 103 HOH HOH A . 
F 6 HOH 131 531 148 HOH HOH A . 
F 6 HOH 132 532 55  HOH HOH A . 
F 6 HOH 133 533 97  HOH HOH A . 
F 6 HOH 134 534 48  HOH HOH A . 
F 6 HOH 135 535 116 HOH HOH A . 
F 6 HOH 136 536 96  HOH HOH A . 
F 6 HOH 137 537 124 HOH HOH A . 
F 6 HOH 138 538 22  HOH HOH A . 
F 6 HOH 139 539 159 HOH HOH A . 
F 6 HOH 140 540 106 HOH HOH A . 
F 6 HOH 141 541 149 HOH HOH A . 
F 6 HOH 142 542 128 HOH HOH A . 
F 6 HOH 143 543 73  HOH HOH A . 
F 6 HOH 144 544 81  HOH HOH A . 
F 6 HOH 145 545 30  HOH HOH A . 
F 6 HOH 146 546 35  HOH HOH A . 
F 6 HOH 147 547 134 HOH HOH A . 
F 6 HOH 148 548 49  HOH HOH A . 
F 6 HOH 149 549 157 HOH HOH A . 
F 6 HOH 150 550 113 HOH HOH A . 
F 6 HOH 151 551 156 HOH HOH A . 
F 6 HOH 152 552 167 HOH HOH A . 
F 6 HOH 153 553 34  HOH HOH A . 
F 6 HOH 154 554 61  HOH HOH A . 
F 6 HOH 155 555 85  HOH HOH A . 
F 6 HOH 156 556 175 HOH HOH A . 
F 6 HOH 157 557 129 HOH HOH A . 
F 6 HOH 158 558 173 HOH HOH A . 
F 6 HOH 159 559 172 HOH HOH A . 
F 6 HOH 160 560 84  HOH HOH A . 
F 6 HOH 161 561 91  HOH HOH A . 
F 6 HOH 162 562 127 HOH HOH A . 
F 6 HOH 163 563 143 HOH HOH A . 
F 6 HOH 164 564 182 HOH HOH A . 
F 6 HOH 165 565 132 HOH HOH A . 
F 6 HOH 166 566 150 HOH HOH A . 
F 6 HOH 167 567 155 HOH HOH A . 
F 6 HOH 168 568 125 HOH HOH A . 
F 6 HOH 169 569 180 HOH HOH A . 
F 6 HOH 170 570 166 HOH HOH A . 
F 6 HOH 171 571 146 HOH HOH A . 
F 6 HOH 172 572 165 HOH HOH A . 
F 6 HOH 173 573 131 HOH HOH A . 
F 6 HOH 174 574 147 HOH HOH A . 
F 6 HOH 175 575 110 HOH HOH A . 
F 6 HOH 176 576 101 HOH HOH A . 
F 6 HOH 177 577 36  HOH HOH A . 
F 6 HOH 178 578 154 HOH HOH A . 
F 6 HOH 179 579 174 HOH HOH A . 
F 6 HOH 180 580 163 HOH HOH A . 
F 6 HOH 181 581 94  HOH HOH A . 
F 6 HOH 182 582 111 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 N 1 A MES 303 ? S   ? D MES 1 S   
2 1 N 1 A MES 303 ? O1S ? D MES 1 O1S 
3 1 N 1 A MES 303 ? O2S ? D MES 1 O2S 
4 1 N 1 A MES 303 ? O3S ? D MES 1 O3S 
# 
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 
? refinement        ? ? ? ? ? ? ? ? ? ? ? REFMAC      ? ? ? .    1 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.10 2 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? XDS         ? ? ? .    3 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? SCALA       ? ? ? .    4 
? phasing           ? ? ? ? ? ? ? ? ? ? ? MOLREP      ? ? ? .    5 
? 'model building'  ? ? ? ? ? ? ? ? ? ? ? Coot        ? ? ? .    6 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   104.140 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     6R6J 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     41.949 
_cell.length_a_esd                 ? 
_cell.length_b                     41.070 
_cell.length_b_esd                 ? 
_cell.length_c                     71.542 
_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                         6R6J 
_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                   6R6J 
_exptl.crystals_number            2 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                      ? 
_exptl_crystal.density_diffrn              ? 
_exptl_crystal.density_Matthews            2.04 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         39.72 
_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              7.0 
_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: 0.1M sodium bicine (pH 9), 0.2M ammonium sulfate and 2M sodium malonate (pH 7)' 
_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                     CCD 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'MARMOSAIC 225 mm CCD' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2014-11-28 
_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   0.91000 
_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                        'MAX II BEAMLINE I911-3' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.91000 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I911-3 
_diffrn_source.pdbx_synchrotron_site       'MAX II' 
# 
_reflns.B_iso_Wilson_estimate            ? 
_reflns.entry_id                         6R6J 
_reflns.data_reduction_details           ? 
_reflns.data_reduction_method            ? 
_reflns.d_resolution_high                1.550 
_reflns.d_resolution_low                 40.679 
_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                       34169 
_reflns.number_obs                       34169 
_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             99.000 
_reflns.R_free_details                   ? 
_reflns.Rmerge_F_all                     ? 
_reflns.Rmerge_F_obs                     ? 
_reflns.Friedel_coverage                 ? 
_reflns.number_gt                        ? 
_reflns.threshold_expression             ? 
_reflns.pdbx_redundancy                  3.200 
_reflns.pdbx_Rmerge_I_obs                ? 
_reflns.pdbx_Rmerge_I_all                ? 
_reflns.pdbx_Rsym_value                  0.049 
_reflns.pdbx_netI_over_av_sigmaI         10.269 
_reflns.pdbx_netI_over_sigmaI            9.600 
_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                  0.070 
_reflns.pdbx_Rpim_I_all                  0.040 
_reflns.pdbx_d_opt                       ? 
_reflns.pdbx_number_measured_all         107711 
_reflns.pdbx_diffrn_id                   1 
_reflns.pdbx_ordinal                     1 
_reflns.pdbx_CC_half                     ? 
_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_R_split 
1.550 1.630  ? 2.2  ? ? ? ? 4854 97.000  ? ? ? ? 0.347 ? ? ? ? ? ? ? ? 3.000 0.347 ? ? ? 0.523 0.290 ? 1  1 ? ? 
1.630 1.730  ? 3.0  ? ? ? ? 4669 98.500  ? ? ? ? 0.245 ? ? ? ? ? ? ? ? 3.100 0.245 ? ? ? 0.361 0.201 ? 2  1 ? ? 
1.730 1.850  ? 4.5  ? ? ? ? 4375 98.800  ? ? ? ? 0.158 ? ? ? ? ? ? ? ? 3.100 0.158 ? ? ? 0.235 0.132 ? 3  1 ? ? 
1.850 2.000  ? 6.4  ? ? ? ? 4126 99.100  ? ? ? ? 0.102 ? ? ? ? ? ? ? ? 3.200 0.102 ? ? ? 0.148 0.085 ? 4  1 ? ? 
2.000 2.190  ? 8.2  ? ? ? ? 3806 99.700  ? ? ? ? 0.075 ? ? ? ? ? ? ? ? 3.200 0.075 ? ? ? 0.109 0.062 ? 5  1 ? ? 
2.190 2.450  ? 9.3  ? ? ? ? 3479 99.600  ? ? ? ? 0.062 ? ? ? ? ? ? ? ? 3.200 0.062 ? ? ? 0.089 0.051 ? 6  1 ? ? 
2.450 2.830  ? 11.9 ? ? ? ? 3059 99.800  ? ? ? ? 0.049 ? ? ? ? ? ? ? ? 3.200 0.049 ? ? ? 0.070 0.041 ? 7  1 ? ? 
2.830 3.470  ? 15.8 ? ? ? ? 2614 100.000 ? ? ? ? 0.033 ? ? ? ? ? ? ? ? 3.200 0.033 ? ? ? 0.049 0.028 ? 8  1 ? ? 
3.470 4.900  ? 22.9 ? ? ? ? 2029 100.000 ? ? ? ? 0.024 ? ? ? ? ? ? ? ? 3.200 0.024 ? ? ? 0.034 0.019 ? 9  1 ? ? 
4.900 40.679 ? 26.3 ? ? ? ? 1158 99.600  ? ? ? ? 0.022 ? ? ? ? ? ? ? ? 3.000 0.022 ? ? ? 0.031 0.017 ? 10 1 ? ? 
# 
_refine.aniso_B[1][1]                            -0.0500 
_refine.aniso_B[1][2]                            0.0000 
_refine.aniso_B[1][3]                            0.0600 
_refine.aniso_B[2][2]                            -1.6500 
_refine.aniso_B[2][3]                            0.0000 
_refine.aniso_B[3][3]                            1.4900 
_refine.B_iso_max                                62.940 
_refine.B_iso_mean                               18.9587 
_refine.B_iso_min                                7.330 
_refine.correlation_coeff_Fo_to_Fc               0.9600 
_refine.correlation_coeff_Fo_to_Fc_free          0.9430 
_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                                 6R6J 
_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                            1.5500 
_refine.ls_d_res_low                             34.6900 
_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                     33894 
_refine.ls_number_reflns_R_free                  3410 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.0300 
_refine.ls_percent_reflns_R_free                 10.1000 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1915 
_refine.ls_R_factor_R_free                       0.2233 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1880 
_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                    ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_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                      3HLJ 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.1020 
_refine.pdbx_overall_ESU_R_Free                  0.1000 
_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             0.1015 
_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                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.5500 
_refine_hist.d_res_low                        34.6900 
_refine_hist.number_atoms_solvent             182 
_refine_hist.number_atoms_total               2270 
_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       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        2049 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         39 
_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' ? 0.010  0.012  2238 ? r_bond_refined_d       ? ? 
'X-RAY DIFFRACTION' ? 1.917  1.670  3049 ? r_angle_refined_deg    ? ? 
'X-RAY DIFFRACTION' ? 7.459  5.000  269  ? r_dihedral_angle_1_deg ? ? 
'X-RAY DIFFRACTION' ? 34.837 23.578 109  ? r_dihedral_angle_2_deg ? ? 
'X-RAY DIFFRACTION' ? 15.825 15.000 366  ? r_dihedral_angle_3_deg ? ? 
'X-RAY DIFFRACTION' ? 20.236 15.000 8    ? r_dihedral_angle_4_deg ? ? 
'X-RAY DIFFRACTION' ? 0.140  0.200  267  ? r_chiral_restr         ? ? 
'X-RAY DIFFRACTION' ? 0.013  0.020  1748 ? r_gen_planes_refined   ? ? 
'X-RAY DIFFRACTION' ? 1.836  1.687  1061 ? r_mcbond_it            ? ? 
'X-RAY DIFFRACTION' ? 2.704  2.522  1335 ? r_mcangle_it           ? ? 
'X-RAY DIFFRACTION' ? 2.513  1.888  1177 ? r_scbond_it            ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.5500 
_refine_ls_shell.d_res_low                        1.5900 
_refine_ls_shell.number_reflns_all                2465 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             247 
_refine_ls_shell.number_reflns_R_work             2218 
_refine_ls_shell.percent_reflns_obs               96.5500 
_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                  0.2750 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.2510 
_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_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                     6R6J 
_struct.title                        
'Crystal structure of human carbonic anhydrase isozyme II with 2-(benzenesulfonyl)-4-chloro-N-(2-hydroxyethyl)-5-sulfamoyl-benzamide' 
_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        6R6J 
_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              6R6J 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 260 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P00918 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  260 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       261 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 580   ? 
1 MORE         8     ? 
1 'SSA (A^2)'  11240 ? 
# 
_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  ? TRP A 16  ? GLY A 12  TRP A 16  5 ? 5 
HELX_P HELX_P2 AA2 PHE A 20  ? GLY A 25  ? PHE A 20  GLY A 25  5 ? 6 
HELX_P HELX_P3 AA3 LYS A 126 ? GLY A 128 ? LYS A 127 GLY A 129 5 ? 3 
HELX_P HELX_P4 AA4 ASP A 129 ? VAL A 134 ? ASP A 130 VAL A 135 1 ? 6 
HELX_P HELX_P5 AA5 LYS A 153 ? GLY A 155 ? LYS A 154 GLY A 156 5 ? 3 
HELX_P HELX_P6 AA6 LEU A 156 ? LEU A 163 ? LEU A 157 LEU A 164 1 ? 8 
HELX_P HELX_P7 AA7 ASP A 164 ? LYS A 167 ? ASP A 165 LYS A 168 5 ? 4 
HELX_P HELX_P8 AA8 ASP A 179 ? LEU A 184 ? ASP A 180 LEU A 185 5 ? 6 
HELX_P HELX_P9 AA9 SER A 218 ? ARG A 226 ? SER A 219 ARG A 227 1 ? 9 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A HIS 94  NE2 ? ? ? 1_555 B ZN  . ZN ? ? A HIS 94  A ZN  301 1_555 ? ? ? ? ? ? ? 1.993 ? ? 
metalc2 metalc ? ? A HIS 96  NE2 ? ? ? 1_555 B ZN  . ZN ? ? A HIS 96  A ZN  301 1_555 ? ? ? ? ? ? ? 1.976 ? ? 
metalc3 metalc ? ? A HIS 119 ND1 ? ? ? 1_555 B ZN  . ZN ? ? A HIS 119 A ZN  301 1_555 ? ? ? ? ? ? ? 2.054 ? ? 
metalc4 metalc ? ? B ZN  .   ZN  ? ? ? 1_555 E JTW . N1 A ? A ZN  301 A JTW 304 1_555 ? ? ? ? ? ? ? 1.951 ? ? 
metalc5 metalc ? ? B ZN  .   ZN  ? ? ? 1_555 E JTW . N1 B ? A ZN  301 A JTW 304 1_555 ? ? ? ? ? ? ? 1.944 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 101.6 ? 
2  NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 114.5 ? 
3  NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 99.6  ? 
4  NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N1  A E JTW .   ? A JTW 304 ? 1_555 110.5 ? 
5  NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N1  A E JTW .   ? A JTW 304 ? 1_555 112.0 ? 
6  ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N1  A E JTW .   ? A JTW 304 ? 1_555 117.0 ? 
7  NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N1  B E JTW .   ? A JTW 304 ? 1_555 110.9 ? 
8  NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N1  B E JTW .   ? A JTW 304 ? 1_555 111.9 ? 
9  ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N1  B E JTW .   ? A JTW 304 ? 1_555 116.7 ? 
10 N1  A E JTW .   ? A JTW 304 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N1  B E JTW .   ? A JTW 304 ? 1_555 0.3   ? 
# 
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 4.33 
2 PRO 200 A . ? PRO 201 A PRO 201 A ? PRO 202 A 1 1.49 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2  ? 
AA2 ? 10 ? 
AA3 ? 6  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2  ? parallel      
AA2 1 2  ? parallel      
AA2 2 3  ? anti-parallel 
AA2 3 4  ? anti-parallel 
AA2 4 5  ? parallel      
AA2 5 6  ? anti-parallel 
AA2 6 7  ? anti-parallel 
AA2 7 8  ? anti-parallel 
AA2 8 9  ? anti-parallel 
AA2 9 10 ? anti-parallel 
AA3 1 2  ? anti-parallel 
AA3 2 3  ? anti-parallel 
AA3 3 4  ? anti-parallel 
AA3 4 5  ? anti-parallel 
AA3 5 6  ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1  ASP A 32  ? ILE A 33  ? ASP A 32  ILE A 33  
AA1 2  THR A 108 ? VAL A 109 ? THR A 108 VAL A 109 
AA2 1  LYS A 39  ? TYR A 40  ? LYS A 39  TYR A 40  
AA2 2  LYS A 256 ? ALA A 257 ? LYS A 257 ALA A 258 
AA2 3  TYR A 190 ? GLY A 195 ? TYR A 191 GLY A 196 
AA2 4  VAL A 206 ? LEU A 211 ? VAL A 207 LEU A 212 
AA2 5  LEU A 140 ? VAL A 149 ? LEU A 141 VAL A 150 
AA2 6  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
AA2 7  TYR A 88  ? TRP A 97  ? TYR A 88  TRP A 97  
AA2 8  PHE A 66  ? PHE A 70  ? PHE A 66  PHE A 70  
AA2 9  SER A 56  ? ASN A 61  ? SER A 56  ASN A 61  
AA2 10 SER A 172 ? ASP A 174 ? SER A 173 ASP A 175 
AA3 1  LEU A 47  ? SER A 50  ? LEU A 47  SER A 50  
AA3 2  VAL A 78  ? GLY A 81  ? VAL A 78  GLY A 81  
AA3 3  TYR A 88  ? TRP A 97  ? TYR A 88  TRP A 97  
AA3 4  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
AA3 5  LEU A 140 ? VAL A 149 ? LEU A 141 VAL A 150 
AA3 6  ILE A 215 ? VAL A 217 ? ILE A 216 VAL A 218 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2  N ILE A 33  ? N ILE A 33  O THR A 108 ? O THR A 108 
AA2 1 2  N LYS A 39  ? N LYS A 39  O ALA A 257 ? O ALA A 258 
AA2 2 3  O LYS A 256 ? O LYS A 257 N THR A 192 ? N THR A 193 
AA2 3 4  N GLY A 195 ? N GLY A 196 O VAL A 206 ? O VAL A 207 
AA2 4 5  O ILE A 209 ? O ILE A 210 N GLY A 144 ? N GLY A 145 
AA2 5 6  O ILE A 145 ? O ILE A 146 N LEU A 118 ? N LEU A 118 
AA2 6 7  O VAL A 121 ? O VAL A 121 N GLN A 92  ? N GLN A 92  
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 174 
AA3 1 2  N SER A 48  ? N SER A 48  O LYS A 80  ? O LYS A 80  
AA3 2 3  N LEU A 79  ? N LEU A 79  O TYR A 88  ? O TYR A 88  
AA3 3 4  N GLN A 92  ? N GLN A 92  O VAL A 121 ? O VAL A 121 
AA3 4 5  N LEU A 118 ? N LEU A 118 O ILE A 145 ? O ILE A 146 
AA3 5 6  N PHE A 146 ? N PHE A 147 O ILE A 215 ? O ILE A 216 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software A ZN  301 ? 4  'binding site for residue ZN A 301'  
AC2 Software A DMS 302 ? 4  'binding site for residue DMS A 302' 
AC3 Software A MES 303 ? 5  'binding site for residue MES A 303' 
AC4 Software A JTW 304 ? 15 'binding site for residue JTW A 304' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  AC1 4  HIS A 94  ? HIS A 94  . ? 1_555 ? 
2  AC1 4  HIS A 96  ? HIS A 96  . ? 1_555 ? 
3  AC1 4  HIS A 119 ? HIS A 119 . ? 1_555 ? 
4  AC1 4  JTW E .   ? JTW A 304 . ? 1_555 ? 
5  AC2 4  TYR A 7   ? TYR A 7   . ? 1_555 ? 
6  AC2 4  ASP A 242 ? ASP A 243 . ? 1_555 ? 
7  AC2 4  TRP A 244 ? TRP A 245 . ? 1_555 ? 
8  AC2 4  PRO A 246 ? PRO A 247 . ? 1_555 ? 
9  AC3 5  LEU A 163 ? LEU A 164 . ? 1_555 ? 
10 AC3 5  ASP A 164 ? ASP A 165 . ? 1_555 ? 
11 AC3 5  LYS A 224 ? LYS A 225 . ? 1_555 ? 
12 AC3 5  LYS A 227 ? LYS A 228 . ? 1_555 ? 
13 AC3 5  HOH F .   ? HOH A 439 . ? 1_555 ? 
14 AC4 15 ASN A 67  ? ASN A 67  . ? 1_555 ? 
15 AC4 15 GLU A 69  ? GLU A 69  . ? 1_555 ? 
16 AC4 15 GLN A 92  ? GLN A 92  . ? 1_555 ? 
17 AC4 15 HIS A 94  ? HIS A 94  . ? 1_555 ? 
18 AC4 15 HIS A 96  ? HIS A 96  . ? 1_555 ? 
19 AC4 15 HIS A 119 ? HIS A 119 . ? 1_555 ? 
20 AC4 15 PHE A 130 ? PHE A 131 . ? 1_555 ? 
21 AC4 15 VAL A 142 ? VAL A 143 . ? 1_555 ? 
22 AC4 15 LEU A 197 ? LEU A 198 . ? 1_555 ? 
23 AC4 15 THR A 198 ? THR A 199 . ? 1_555 ? 
24 AC4 15 THR A 199 ? THR A 200 . ? 1_555 ? 
25 AC4 15 PRO A 200 ? PRO A 201 . ? 1_555 ? 
26 AC4 15 TRP A 208 ? TRP A 209 . ? 1_555 ? 
27 AC4 15 ZN  B .   ? ZN  A 301 . ? 1_555 ? 
28 AC4 15 HOH F .   ? HOH A 494 . ? 1_555 ? 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ARG A 27  ? ? -142.94 59.92   
2 1 LYS A 111 ? ? 76.90   -2.86   
3 1 PHE A 176 ? ? -152.45 84.70   
4 1 ASN A 244 ? ? -97.75  48.82   
5 1 LYS A 252 ? ? 55.64   -132.52 
6 1 ASN A 253 ? ? -90.01  56.44   
# 
_phasing.method   MR 
# 
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 
JTW C12  C  N N 193 
JTW C21  C  Y N 194 
JTW C22  C  Y N 195 
JTW C23  C  Y N 196 
JTW C5   C  Y N 197 
JTW C6   C  Y N 198 
JTW C8   C  Y N 199 
JTW C9   C  Y N 200 
JTW C10  C  Y N 201 
JTW O20  O  N N 202 
JTW S18  S  N N 203 
JTW O19  O  N N 204 
JTW C25  C  Y N 205 
JTW C26  C  Y N 206 
JTW C24  C  Y N 207 
JTW C7   C  Y N 208 
JTW CL1  CL N N 209 
JTW S2   S  N N 210 
JTW O3   O  N N 211 
JTW O4   O  N N 212 
JTW N1   N  N N 213 
JTW O13  O  N N 214 
JTW N14  N  N N 215 
JTW C15  C  N N 216 
JTW C16  C  N N 217 
JTW O17  O  N N 218 
JTW H1   H  N N 219 
JTW H2   H  N N 220 
JTW H3   H  N N 221 
JTW H4   H  N N 222 
JTW H5   H  N N 223 
JTW H6   H  N N 224 
JTW H7   H  N N 225 
JTW H8   H  N N 226 
JTW H9   H  N N 227 
JTW H10  H  N N 228 
JTW H11  H  N N 229 
JTW H12  H  N N 230 
JTW H13  H  N N 231 
JTW H14  H  N N 232 
JTW H15  H  N N 233 
LEU N    N  N N 234 
LEU CA   C  N S 235 
LEU C    C  N N 236 
LEU O    O  N N 237 
LEU CB   C  N N 238 
LEU CG   C  N N 239 
LEU CD1  C  N N 240 
LEU CD2  C  N N 241 
LEU OXT  O  N N 242 
LEU H    H  N N 243 
LEU H2   H  N N 244 
LEU HA   H  N N 245 
LEU HB2  H  N N 246 
LEU HB3  H  N N 247 
LEU HG   H  N N 248 
LEU HD11 H  N N 249 
LEU HD12 H  N N 250 
LEU HD13 H  N N 251 
LEU HD21 H  N N 252 
LEU HD22 H  N N 253 
LEU HD23 H  N N 254 
LEU HXT  H  N N 255 
LYS N    N  N N 256 
LYS CA   C  N S 257 
LYS C    C  N N 258 
LYS O    O  N N 259 
LYS CB   C  N N 260 
LYS CG   C  N N 261 
LYS CD   C  N N 262 
LYS CE   C  N N 263 
LYS NZ   N  N N 264 
LYS OXT  O  N N 265 
LYS H    H  N N 266 
LYS H2   H  N N 267 
LYS HA   H  N N 268 
LYS HB2  H  N N 269 
LYS HB3  H  N N 270 
LYS HG2  H  N N 271 
LYS HG3  H  N N 272 
LYS HD2  H  N N 273 
LYS HD3  H  N N 274 
LYS HE2  H  N N 275 
LYS HE3  H  N N 276 
LYS HZ1  H  N N 277 
LYS HZ2  H  N N 278 
LYS HZ3  H  N N 279 
LYS HXT  H  N N 280 
MES O1   O  N N 281 
MES C2   C  N N 282 
MES C3   C  N N 283 
MES N4   N  N N 284 
MES C5   C  N N 285 
MES C6   C  N N 286 
MES C7   C  N N 287 
MES C8   C  N N 288 
MES S    S  N N 289 
MES O1S  O  N N 290 
MES O2S  O  N N 291 
MES O3S  O  N N 292 
MES H21  H  N N 293 
MES H22  H  N N 294 
MES H31  H  N N 295 
MES H32  H  N N 296 
MES HN4  H  N N 297 
MES H51  H  N N 298 
MES H52  H  N N 299 
MES H61  H  N N 300 
MES H62  H  N N 301 
MES H71  H  N N 302 
MES H72  H  N N 303 
MES H81  H  N N 304 
MES H82  H  N N 305 
MET N    N  N N 306 
MET CA   C  N S 307 
MET C    C  N N 308 
MET O    O  N N 309 
MET CB   C  N N 310 
MET CG   C  N N 311 
MET SD   S  N N 312 
MET CE   C  N N 313 
MET OXT  O  N N 314 
MET H    H  N N 315 
MET H2   H  N N 316 
MET HA   H  N N 317 
MET HB2  H  N N 318 
MET HB3  H  N N 319 
MET HG2  H  N N 320 
MET HG3  H  N N 321 
MET HE1  H  N N 322 
MET HE2  H  N N 323 
MET HE3  H  N N 324 
MET HXT  H  N N 325 
PHE N    N  N N 326 
PHE CA   C  N S 327 
PHE C    C  N N 328 
PHE O    O  N N 329 
PHE CB   C  N N 330 
PHE CG   C  Y N 331 
PHE CD1  C  Y N 332 
PHE CD2  C  Y N 333 
PHE CE1  C  Y N 334 
PHE CE2  C  Y N 335 
PHE CZ   C  Y N 336 
PHE OXT  O  N N 337 
PHE H    H  N N 338 
PHE H2   H  N N 339 
PHE HA   H  N N 340 
PHE HB2  H  N N 341 
PHE HB3  H  N N 342 
PHE HD1  H  N N 343 
PHE HD2  H  N N 344 
PHE HE1  H  N N 345 
PHE HE2  H  N N 346 
PHE HZ   H  N N 347 
PHE HXT  H  N N 348 
PRO N    N  N N 349 
PRO CA   C  N S 350 
PRO C    C  N N 351 
PRO O    O  N N 352 
PRO CB   C  N N 353 
PRO CG   C  N N 354 
PRO CD   C  N N 355 
PRO OXT  O  N N 356 
PRO H    H  N N 357 
PRO HA   H  N N 358 
PRO HB2  H  N N 359 
PRO HB3  H  N N 360 
PRO HG2  H  N N 361 
PRO HG3  H  N N 362 
PRO HD2  H  N N 363 
PRO HD3  H  N N 364 
PRO HXT  H  N N 365 
SER N    N  N N 366 
SER CA   C  N S 367 
SER C    C  N N 368 
SER O    O  N N 369 
SER CB   C  N N 370 
SER OG   O  N N 371 
SER OXT  O  N N 372 
SER H    H  N N 373 
SER H2   H  N N 374 
SER HA   H  N N 375 
SER HB2  H  N N 376 
SER HB3  H  N N 377 
SER HG   H  N N 378 
SER HXT  H  N N 379 
THR N    N  N N 380 
THR CA   C  N S 381 
THR C    C  N N 382 
THR O    O  N N 383 
THR CB   C  N R 384 
THR OG1  O  N N 385 
THR CG2  C  N N 386 
THR OXT  O  N N 387 
THR H    H  N N 388 
THR H2   H  N N 389 
THR HA   H  N N 390 
THR HB   H  N N 391 
THR HG1  H  N N 392 
THR HG21 H  N N 393 
THR HG22 H  N N 394 
THR HG23 H  N N 395 
THR HXT  H  N N 396 
TRP N    N  N N 397 
TRP CA   C  N S 398 
TRP C    C  N N 399 
TRP O    O  N N 400 
TRP CB   C  N N 401 
TRP CG   C  Y N 402 
TRP CD1  C  Y N 403 
TRP CD2  C  Y N 404 
TRP NE1  N  Y N 405 
TRP CE2  C  Y N 406 
TRP CE3  C  Y N 407 
TRP CZ2  C  Y N 408 
TRP CZ3  C  Y N 409 
TRP CH2  C  Y N 410 
TRP OXT  O  N N 411 
TRP H    H  N N 412 
TRP H2   H  N N 413 
TRP HA   H  N N 414 
TRP HB2  H  N N 415 
TRP HB3  H  N N 416 
TRP HD1  H  N N 417 
TRP HE1  H  N N 418 
TRP HE3  H  N N 419 
TRP HZ2  H  N N 420 
TRP HZ3  H  N N 421 
TRP HH2  H  N N 422 
TRP HXT  H  N N 423 
TYR N    N  N N 424 
TYR CA   C  N S 425 
TYR C    C  N N 426 
TYR O    O  N N 427 
TYR CB   C  N N 428 
TYR CG   C  Y N 429 
TYR CD1  C  Y N 430 
TYR CD2  C  Y N 431 
TYR CE1  C  Y N 432 
TYR CE2  C  Y N 433 
TYR CZ   C  Y N 434 
TYR OH   O  N N 435 
TYR OXT  O  N N 436 
TYR H    H  N N 437 
TYR H2   H  N N 438 
TYR HA   H  N N 439 
TYR HB2  H  N N 440 
TYR HB3  H  N N 441 
TYR HD1  H  N N 442 
TYR HD2  H  N N 443 
TYR HE1  H  N N 444 
TYR HE2  H  N N 445 
TYR HH   H  N N 446 
TYR HXT  H  N N 447 
VAL N    N  N N 448 
VAL CA   C  N S 449 
VAL C    C  N N 450 
VAL O    O  N N 451 
VAL CB   C  N N 452 
VAL CG1  C  N N 453 
VAL CG2  C  N N 454 
VAL OXT  O  N N 455 
VAL H    H  N N 456 
VAL H2   H  N N 457 
VAL HA   H  N N 458 
VAL HB   H  N N 459 
VAL HG11 H  N N 460 
VAL HG12 H  N N 461 
VAL HG13 H  N N 462 
VAL HG21 H  N N 463 
VAL HG22 H  N N 464 
VAL HG23 H  N N 465 
VAL HXT  H  N N 466 
ZN  ZN   ZN N N 467 
# 
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 
JTW C26 C24  doub Y N 182 
JTW C26 C25  sing Y N 183 
JTW C24 C23  sing Y N 184 
JTW C16 C15  sing N N 185 
JTW C16 O17  sing N N 186 
JTW C25 C21  doub Y N 187 
JTW C15 N14  sing N N 188 
JTW O13 C12  doub N N 189 
JTW C23 C22  doub Y N 190 
JTW C21 C22  sing Y N 191 
JTW C21 S18  sing N N 192 
JTW O20 S18  doub N N 193 
JTW N14 C12  sing N N 194 
JTW C12 C9   sing N N 195 
JTW S18 O19  doub N N 196 
JTW S18 C8   sing N N 197 
JTW C9  C8   doub Y N 198 
JTW C9  C10  sing Y N 199 
JTW C8  C7   sing Y N 200 
JTW C10 C5   doub Y N 201 
JTW C7  C6   doub Y N 202 
JTW C5  C6   sing Y N 203 
JTW C5  S2   sing N N 204 
JTW C6  CL1  sing N N 205 
JTW N1  S2   sing N N 206 
JTW S2  O4   doub N N 207 
JTW S2  O3   doub N N 208 
JTW C22 H1   sing N N 209 
JTW C23 H2   sing N N 210 
JTW C10 H3   sing N N 211 
JTW C25 H4   sing N N 212 
JTW C26 H5   sing N N 213 
JTW C24 H6   sing N N 214 
JTW C7  H7   sing N N 215 
JTW N1  H8   sing N N 216 
JTW N1  H9   sing N N 217 
JTW N14 H10  sing N N 218 
JTW C15 H11  sing N N 219 
JTW C15 H12  sing N N 220 
JTW C16 H13  sing N N 221 
JTW C16 H14  sing N N 222 
JTW O17 H15  sing N N 223 
LEU N   CA   sing N N 224 
LEU N   H    sing N N 225 
LEU N   H2   sing N N 226 
LEU CA  C    sing N N 227 
LEU CA  CB   sing N N 228 
LEU CA  HA   sing N N 229 
LEU C   O    doub N N 230 
LEU C   OXT  sing N N 231 
LEU CB  CG   sing N N 232 
LEU CB  HB2  sing N N 233 
LEU CB  HB3  sing N N 234 
LEU CG  CD1  sing N N 235 
LEU CG  CD2  sing N N 236 
LEU CG  HG   sing N N 237 
LEU CD1 HD11 sing N N 238 
LEU CD1 HD12 sing N N 239 
LEU CD1 HD13 sing N N 240 
LEU CD2 HD21 sing N N 241 
LEU CD2 HD22 sing N N 242 
LEU CD2 HD23 sing N N 243 
LEU OXT HXT  sing N N 244 
LYS N   CA   sing N N 245 
LYS N   H    sing N N 246 
LYS N   H2   sing N N 247 
LYS CA  C    sing N N 248 
LYS CA  CB   sing N N 249 
LYS CA  HA   sing N N 250 
LYS C   O    doub N N 251 
LYS C   OXT  sing N N 252 
LYS CB  CG   sing N N 253 
LYS CB  HB2  sing N N 254 
LYS CB  HB3  sing N N 255 
LYS CG  CD   sing N N 256 
LYS CG  HG2  sing N N 257 
LYS CG  HG3  sing N N 258 
LYS CD  CE   sing N N 259 
LYS CD  HD2  sing N N 260 
LYS CD  HD3  sing N N 261 
LYS CE  NZ   sing N N 262 
LYS CE  HE2  sing N N 263 
LYS CE  HE3  sing N N 264 
LYS NZ  HZ1  sing N N 265 
LYS NZ  HZ2  sing N N 266 
LYS NZ  HZ3  sing N N 267 
LYS OXT HXT  sing N N 268 
MES O1  C2   sing N N 269 
MES O1  C6   sing N N 270 
MES C2  C3   sing N N 271 
MES C2  H21  sing N N 272 
MES C2  H22  sing N N 273 
MES C3  N4   sing N N 274 
MES C3  H31  sing N N 275 
MES C3  H32  sing N N 276 
MES N4  C5   sing N N 277 
MES N4  C7   sing N N 278 
MES N4  HN4  sing N N 279 
MES C5  C6   sing N N 280 
MES C5  H51  sing N N 281 
MES C5  H52  sing N N 282 
MES C6  H61  sing N N 283 
MES C6  H62  sing N N 284 
MES C7  C8   sing N N 285 
MES C7  H71  sing N N 286 
MES C7  H72  sing N N 287 
MES C8  S    sing N N 288 
MES C8  H81  sing N N 289 
MES C8  H82  sing N N 290 
MES S   O1S  doub N N 291 
MES S   O2S  doub N N 292 
MES S   O3S  sing N N 293 
MET N   CA   sing N N 294 
MET N   H    sing N N 295 
MET N   H2   sing N N 296 
MET CA  C    sing N N 297 
MET CA  CB   sing N N 298 
MET CA  HA   sing N N 299 
MET C   O    doub N N 300 
MET C   OXT  sing N N 301 
MET CB  CG   sing N N 302 
MET CB  HB2  sing N N 303 
MET CB  HB3  sing N N 304 
MET CG  SD   sing N N 305 
MET CG  HG2  sing N N 306 
MET CG  HG3  sing N N 307 
MET SD  CE   sing N N 308 
MET CE  HE1  sing N N 309 
MET CE  HE2  sing N N 310 
MET CE  HE3  sing N N 311 
MET OXT HXT  sing N N 312 
PHE N   CA   sing N N 313 
PHE N   H    sing N N 314 
PHE N   H2   sing N N 315 
PHE CA  C    sing N N 316 
PHE CA  CB   sing N N 317 
PHE CA  HA   sing N N 318 
PHE C   O    doub N N 319 
PHE C   OXT  sing N N 320 
PHE CB  CG   sing N N 321 
PHE CB  HB2  sing N N 322 
PHE CB  HB3  sing N N 323 
PHE CG  CD1  doub Y N 324 
PHE CG  CD2  sing Y N 325 
PHE CD1 CE1  sing Y N 326 
PHE CD1 HD1  sing N N 327 
PHE CD2 CE2  doub Y N 328 
PHE CD2 HD2  sing N N 329 
PHE CE1 CZ   doub Y N 330 
PHE CE1 HE1  sing N N 331 
PHE CE2 CZ   sing Y N 332 
PHE CE2 HE2  sing N N 333 
PHE CZ  HZ   sing N N 334 
PHE OXT HXT  sing N N 335 
PRO N   CA   sing N N 336 
PRO N   CD   sing N N 337 
PRO N   H    sing N N 338 
PRO CA  C    sing N N 339 
PRO CA  CB   sing N N 340 
PRO CA  HA   sing N N 341 
PRO C   O    doub N N 342 
PRO C   OXT  sing N N 343 
PRO CB  CG   sing N N 344 
PRO CB  HB2  sing N N 345 
PRO CB  HB3  sing N N 346 
PRO CG  CD   sing N N 347 
PRO CG  HG2  sing N N 348 
PRO CG  HG3  sing N N 349 
PRO CD  HD2  sing N N 350 
PRO CD  HD3  sing N N 351 
PRO OXT HXT  sing N N 352 
SER N   CA   sing N N 353 
SER N   H    sing N N 354 
SER N   H2   sing N N 355 
SER CA  C    sing N N 356 
SER CA  CB   sing N N 357 
SER CA  HA   sing N N 358 
SER C   O    doub N N 359 
SER C   OXT  sing N N 360 
SER CB  OG   sing N N 361 
SER CB  HB2  sing N N 362 
SER CB  HB3  sing N N 363 
SER OG  HG   sing N N 364 
SER OXT HXT  sing N N 365 
THR N   CA   sing N N 366 
THR N   H    sing N N 367 
THR N   H2   sing N N 368 
THR CA  C    sing N N 369 
THR CA  CB   sing N N 370 
THR CA  HA   sing N N 371 
THR C   O    doub N N 372 
THR C   OXT  sing N N 373 
THR CB  OG1  sing N N 374 
THR CB  CG2  sing N N 375 
THR CB  HB   sing N N 376 
THR OG1 HG1  sing N N 377 
THR CG2 HG21 sing N N 378 
THR CG2 HG22 sing N N 379 
THR CG2 HG23 sing N N 380 
THR OXT HXT  sing N N 381 
TRP N   CA   sing N N 382 
TRP N   H    sing N N 383 
TRP N   H2   sing N N 384 
TRP CA  C    sing N N 385 
TRP CA  CB   sing N N 386 
TRP CA  HA   sing N N 387 
TRP C   O    doub N N 388 
TRP C   OXT  sing N N 389 
TRP CB  CG   sing N N 390 
TRP CB  HB2  sing N N 391 
TRP CB  HB3  sing N N 392 
TRP CG  CD1  doub Y N 393 
TRP CG  CD2  sing Y N 394 
TRP CD1 NE1  sing Y N 395 
TRP CD1 HD1  sing N N 396 
TRP CD2 CE2  doub Y N 397 
TRP CD2 CE3  sing Y N 398 
TRP NE1 CE2  sing Y N 399 
TRP NE1 HE1  sing N N 400 
TRP CE2 CZ2  sing Y N 401 
TRP CE3 CZ3  doub Y N 402 
TRP CE3 HE3  sing N N 403 
TRP CZ2 CH2  doub Y N 404 
TRP CZ2 HZ2  sing N N 405 
TRP CZ3 CH2  sing Y N 406 
TRP CZ3 HZ3  sing N N 407 
TRP CH2 HH2  sing N N 408 
TRP OXT HXT  sing N N 409 
TYR N   CA   sing N N 410 
TYR N   H    sing N N 411 
TYR N   H2   sing N N 412 
TYR CA  C    sing N N 413 
TYR CA  CB   sing N N 414 
TYR CA  HA   sing N N 415 
TYR C   O    doub N N 416 
TYR C   OXT  sing N N 417 
TYR CB  CG   sing N N 418 
TYR CB  HB2  sing N N 419 
TYR CB  HB3  sing N N 420 
TYR CG  CD1  doub Y N 421 
TYR CG  CD2  sing Y N 422 
TYR CD1 CE1  sing Y N 423 
TYR CD1 HD1  sing N N 424 
TYR CD2 CE2  doub Y N 425 
TYR CD2 HD2  sing N N 426 
TYR CE1 CZ   doub Y N 427 
TYR CE1 HE1  sing N N 428 
TYR CE2 CZ   sing Y N 429 
TYR CE2 HE2  sing N N 430 
TYR CZ  OH   sing N N 431 
TYR OH  HH   sing N N 432 
TYR OXT HXT  sing N N 433 
VAL N   CA   sing N N 434 
VAL N   H    sing N N 435 
VAL N   H2   sing N N 436 
VAL CA  C    sing N N 437 
VAL CA  CB   sing N N 438 
VAL CA  HA   sing N N 439 
VAL C   O    doub N N 440 
VAL C   OXT  sing N N 441 
VAL CB  CG1  sing N N 442 
VAL CB  CG2  sing N N 443 
VAL CB  HB   sing N N 444 
VAL CG1 HG11 sing N N 445 
VAL CG1 HG12 sing N N 446 
VAL CG1 HG13 sing N N 447 
VAL CG2 HG21 sing N N 448 
VAL CG2 HG22 sing N N 449 
VAL CG2 HG23 sing N N 450 
VAL OXT HXT  sing N N 451 
# 
_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   3HLJ 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    6R6J 
_atom_sites.fract_transf_matrix[1][1]   0.023838 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.006004 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.024349 
_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]   0.014414 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
# 
loop_
_atom_type.symbol 
C  
CL 
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . HIS A 1 4   ? 8.968   1.283   8.150   1.00 39.75 ? 4   HIS A N   1 
ATOM   2    C  CA  . HIS A 1 4   ? 9.859   0.107   8.444   1.00 39.34 ? 4   HIS A CA  1 
ATOM   3    C  C   . HIS A 1 4   ? 9.146   -0.929  9.312   1.00 31.63 ? 4   HIS A C   1 
ATOM   4    O  O   . HIS A 1 4   ? 9.376   -2.122  9.143   1.00 26.93 ? 4   HIS A O   1 
ATOM   5    C  CB  . HIS A 1 4   ? 11.173  0.539   9.116   1.00 50.24 ? 4   HIS A CB  1 
ATOM   6    C  CG  . HIS A 1 4   ? 12.294  -0.447  8.988   1.00 56.22 ? 4   HIS A CG  1 
ATOM   7    N  ND1 . HIS A 1 4   ? 12.716  -1.241  10.052  1.00 61.44 ? 4   HIS A ND1 1 
ATOM   8    C  CD2 . HIS A 1 4   ? 13.093  -0.768  7.939   1.00 59.32 ? 4   HIS A CD2 1 
ATOM   9    C  CE1 . HIS A 1 4   ? 13.715  -2.017  9.660   1.00 61.18 ? 4   HIS A CE1 1 
ATOM   10   N  NE2 . HIS A 1 4   ? 13.973  -1.735  8.363   1.00 62.94 ? 4   HIS A NE2 1 
ATOM   11   N  N   . TRP A 1 5   ? 8.320   -0.488  10.263  1.00 24.19 ? 5   TRP A N   1 
ATOM   12   C  CA  . TRP A 1 5   ? 7.687   -1.449  11.170  1.00 20.19 ? 5   TRP A CA  1 
ATOM   13   C  C   . TRP A 1 5   ? 6.739   -2.371  10.395  1.00 20.31 ? 5   TRP A C   1 
ATOM   14   O  O   . TRP A 1 5   ? 6.189   -1.997  9.362   1.00 19.50 ? 5   TRP A O   1 
ATOM   15   C  CB  . TRP A 1 5   ? 6.988   -0.744  12.362  1.00 18.34 ? 5   TRP A CB  1 
ATOM   16   C  CG  . TRP A 1 5   ? 5.737   0.001   11.994  1.00 17.85 ? 5   TRP A CG  1 
ATOM   17   C  CD1 . TRP A 1 5   ? 5.625   1.308   11.590  1.00 17.23 ? 5   TRP A CD1 1 
ATOM   18   C  CD2 . TRP A 1 5   ? 4.406   -0.525  11.983  1.00 15.35 ? 5   TRP A CD2 1 
ATOM   19   N  NE1 . TRP A 1 5   ? 4.315   1.625   11.331  1.00 18.33 ? 5   TRP A NE1 1 
ATOM   20   C  CE2 . TRP A 1 5   ? 3.552   0.515   11.556  1.00 15.52 ? 5   TRP A CE2 1 
ATOM   21   C  CE3 . TRP A 1 5   ? 3.856   -1.779  12.265  1.00 14.10 ? 5   TRP A CE3 1 
ATOM   22   C  CZ2 . TRP A 1 5   ? 2.177   0.364   11.445  1.00 14.44 ? 5   TRP A CZ2 1 
ATOM   23   C  CZ3 . TRP A 1 5   ? 2.483   -1.943  12.102  1.00 13.13 ? 5   TRP A CZ3 1 
ATOM   24   C  CH2 . TRP A 1 5   ? 1.663   -0.869  11.751  1.00 14.04 ? 5   TRP A CH2 1 
ATOM   25   N  N   . GLY A 1 6   ? 6.539   -3.584  10.924  1.00 17.81 ? 6   GLY A N   1 
ATOM   26   C  CA  . GLY A 1 6   ? 5.469   -4.417  10.398  1.00 18.65 ? 6   GLY A CA  1 
ATOM   27   C  C   . GLY A 1 6   ? 5.172   -5.584  11.318  1.00 17.17 ? 6   GLY A C   1 
ATOM   28   O  O   . GLY A 1 6   ? 5.199   -5.454  12.542  1.00 16.61 ? 6   GLY A O   1 
ATOM   29   N  N   . TYR A 1 7   ? 4.955   -6.754  10.708  1.00 19.14 ? 7   TYR A N   1 
ATOM   30   C  CA  . TYR A 1 7   ? 4.547   -7.868  11.537  1.00 18.43 ? 7   TYR A CA  1 
ATOM   31   C  C   . TYR A 1 7   ? 5.435   -9.100  11.362  1.00 22.57 ? 7   TYR A C   1 
ATOM   32   O  O   . TYR A 1 7   ? 5.047   -10.157 11.872  1.00 22.91 ? 7   TYR A O   1 
ATOM   33   C  CB  . TYR A 1 7   ? 3.059   -8.177  11.315  1.00 15.38 ? 7   TYR A CB  1 
ATOM   34   C  CG  . TYR A 1 7   ? 2.115   -7.108  11.819  1.00 13.77 ? 7   TYR A CG  1 
ATOM   35   C  CD1 . TYR A 1 7   ? 1.746   -7.058  13.170  1.00 12.89 ? 7   TYR A CD1 1 
ATOM   36   C  CD2 . TYR A 1 7   ? 1.625   -6.137  10.954  1.00 12.15 ? 7   TYR A CD2 1 
ATOM   37   C  CE1 . TYR A 1 7   ? 0.890   -6.050  13.623  1.00 12.70 ? 7   TYR A CE1 1 
ATOM   38   C  CE2 . TYR A 1 7   ? 0.782   -5.121  11.388  1.00 11.39 ? 7   TYR A CE2 1 
ATOM   39   C  CZ  . TYR A 1 7   ? 0.419   -5.088  12.744  1.00 11.76 ? 7   TYR A CZ  1 
ATOM   40   O  OH  . TYR A 1 7   ? -0.454  -4.125  13.193  1.00 11.31 ? 7   TYR A OH  1 
ATOM   41   N  N   . GLY A 1 8   ? 6.579   -8.970  10.653  1.00 24.41 ? 8   GLY A N   1 
ATOM   42   C  CA  . GLY A 1 8   ? 7.507   -10.093 10.440  1.00 24.34 ? 8   GLY A CA  1 
ATOM   43   C  C   . GLY A 1 8   ? 8.513   -10.325 11.580  1.00 25.28 ? 8   GLY A C   1 
ATOM   44   O  O   . GLY A 1 8   ? 8.546   -9.575  12.561  1.00 28.82 ? 8   GLY A O   1 
ATOM   45   N  N   . LYS A 1 9   ? 9.373   -11.373 11.455  1.00 23.01 ? 9   LYS A N   1 
ATOM   46   C  CA  . LYS A 1 9   ? 10.330  -11.793 12.488  1.00 23.44 ? 9   LYS A CA  1 
ATOM   47   C  C   . LYS A 1 9   ? 11.318  -10.673 12.812  1.00 21.08 ? 9   LYS A C   1 
ATOM   48   O  O   . LYS A 1 9   ? 11.757  -10.538 13.955  1.00 23.06 ? 9   LYS A O   1 
ATOM   49   C  CB  . LYS A 1 9   ? 11.217  -12.951 12.006  1.00 25.20 ? 9   LYS A CB  1 
ATOM   50   C  CG  . LYS A 1 9   ? 11.898  -13.761 13.102  0.01 24.53 ? 9   LYS A CG  1 
ATOM   51   C  CD  . LYS A 1 9   ? 12.737  -14.903 12.571  0.01 24.60 ? 9   LYS A CD  1 
ATOM   52   C  CE  . LYS A 1 9   ? 13.401  -15.710 13.667  0.01 24.62 ? 9   LYS A CE  1 
ATOM   53   N  NZ  . LYS A 1 9   ? 12.407  -16.301 14.593  0.01 24.59 ? 9   LYS A NZ  1 
ATOM   54   N  N   . HIS A 1 10  ? 11.648  -9.882  11.795  1.00 23.03 ? 10  HIS A N   1 
ATOM   55   C  CA  . HIS A 1 10  ? 12.695  -8.874  11.915  1.00 23.31 ? 10  HIS A CA  1 
ATOM   56   C  C   . HIS A 1 10  ? 12.144  -7.471  12.138  1.00 21.60 ? 10  HIS A C   1 
ATOM   57   O  O   . HIS A 1 10  ? 12.915  -6.599  12.550  1.00 21.01 ? 10  HIS A O   1 
ATOM   58   C  CB  . HIS A 1 10  ? 13.609  -8.889  10.680  1.00 21.03 ? 10  HIS A CB  1 
ATOM   59   C  CG  . HIS A 1 10  ? 14.309  -10.203 10.561  1.00 23.11 ? 10  HIS A CG  1 
ATOM   60   N  ND1 . HIS A 1 10  ? 15.293  -10.604 11.451  1.00 25.70 ? 10  HIS A ND1 1 
ATOM   61   C  CD2 . HIS A 1 10  ? 14.136  -11.216 9.689   1.00 24.64 ? 10  HIS A CD2 1 
ATOM   62   C  CE1 . HIS A 1 10  ? 15.702  -11.813 11.130  1.00 23.69 ? 10  HIS A CE1 1 
ATOM   63   N  NE2 . HIS A 1 10  ? 14.992  -12.229 10.055  1.00 23.99 ? 10  HIS A NE2 1 
ATOM   64   N  N   . ASN A 1 11  ? 10.829  -7.254  11.923  1.00 23.17 ? 11  ASN A N   1 
ATOM   65   C  CA  . ASN A 1 11  ? 10.286  -5.912  12.130  1.00 20.96 ? 11  ASN A CA  1 
ATOM   66   C  C   . ASN A 1 11  ? 8.940   -5.933  12.864  1.00 23.59 ? 11  ASN A C   1 
ATOM   67   O  O   . ASN A 1 11  ? 8.270   -4.894  12.910  1.00 20.47 ? 11  ASN A O   1 
ATOM   68   C  CB  . ASN A 1 11  ? 10.024  -5.212  10.799  1.00 20.50 ? 11  ASN A CB  1 
ATOM   69   C  CG  . ASN A 1 11  ? 8.969   -5.891  9.937   1.00 22.55 ? 11  ASN A CG  1 
ATOM   70   O  OD1 . ASN A 1 11  ? 8.429   -6.936  10.299  1.00 21.90 ? 11  ASN A OD1 1 
ATOM   71   N  ND2 . ASN A 1 11  ? 8.635   -5.286  8.809   1.00 21.12 ? 11  ASN A ND2 1 
ATOM   72   N  N   . GLY A 1 12  ? 8.568   -7.101  13.408  1.00 21.13 ? 12  GLY A N   1 
ATOM   73   C  CA  . GLY A 1 12  ? 7.273   -7.286  14.052  1.00 19.29 ? 12  GLY A CA  1 
ATOM   74   C  C   . GLY A 1 12  ? 7.195   -6.682  15.449  1.00 17.87 ? 12  GLY A C   1 
ATOM   75   O  O   . GLY A 1 12  ? 8.064   -5.932  15.917  1.00 16.52 ? 12  GLY A O   1 
ATOM   76   N  N   . PRO A 1 13  ? 6.094   -6.970  16.184  1.00 16.64 ? 13  PRO A N   1 
ATOM   77   C  CA  . PRO A 1 13  ? 5.899   -6.372  17.500  1.00 17.96 ? 13  PRO A CA  1 
ATOM   78   C  C   . PRO A 1 13  ? 7.062   -6.311  18.489  1.00 17.65 ? 13  PRO A C   1 
ATOM   79   O  O   . PRO A 1 13  ? 7.169   -5.312  19.209  1.00 17.70 ? 13  PRO A O   1 
ATOM   80   C  CB  . PRO A 1 13  ? 4.728   -7.180  18.080  1.00 18.82 ? 13  PRO A CB  1 
ATOM   81   C  CG  . PRO A 1 13  ? 3.951   -7.627  16.877  1.00 17.78 ? 13  PRO A CG  1 
ATOM   82   C  CD  . PRO A 1 13  ? 4.925   -7.743  15.722  1.00 17.74 ? 13  PRO A CD  1 
ATOM   83   N  N   . GLU A 1 14  ? 7.858   -7.393  18.573  1.00 17.12 ? 14  GLU A N   1 
ATOM   84   C  CA  . GLU A 1 14  ? 8.956   -7.487  19.525  1.00 19.98 ? 14  GLU A CA  1 
ATOM   85   C  C   . GLU A 1 14  ? 10.072  -6.469  19.212  1.00 18.07 ? 14  GLU A C   1 
ATOM   86   O  O   . GLU A 1 14  ? 10.866  -6.172  20.094  1.00 19.39 ? 14  GLU A O   1 
ATOM   87   C  CB  . GLU A 1 14  ? 9.437   -8.940  19.523  1.00 22.67 ? 14  GLU A CB  1 
ATOM   88   C  CG  . GLU A 1 14  ? 10.038  -9.352  18.175  1.00 30.16 ? 14  GLU A CG  1 
ATOM   89   C  CD  . GLU A 1 14  ? 9.253   -9.979  17.013  1.00 37.37 ? 14  GLU A CD  1 
ATOM   90   O  OE1 . GLU A 1 14  ? 8.022   -9.743  16.897  1.00 26.50 ? 14  GLU A OE1 1 
ATOM   91   O  OE2 . GLU A 1 14  ? 9.910   -10.689 16.165  1.00 36.95 ? 14  GLU A OE2 1 
ATOM   92   N  N   . HIS A 1 15  ? 10.088  -5.924  17.991  1.00 17.48 ? 15  HIS A N   1 
ATOM   93   C  CA  . HIS A 1 15  ? 11.046  -4.930  17.530  1.00 16.93 ? 15  HIS A CA  1 
ATOM   94   C  C   . HIS A 1 15  ? 10.580  -3.481  17.722  1.00 16.93 ? 15  HIS A C   1 
ATOM   95   O  O   . HIS A 1 15  ? 11.390  -2.549  17.657  1.00 17.36 ? 15  HIS A O   1 
ATOM   96   C  CB  . HIS A 1 15  ? 11.327  -5.140  16.045  1.00 18.11 ? 15  HIS A CB  1 
ATOM   97   C  CG  . HIS A 1 15  ? 12.055  -6.415  15.818  1.00 20.15 ? 15  HIS A CG  1 
ATOM   98   N  ND1 . HIS A 1 15  ? 13.423  -6.459  15.914  1.00 19.44 ? 15  HIS A ND1 1 
ATOM   99   C  CD2 . HIS A 1 15  ? 11.639  -7.668  15.506  1.00 20.60 ? 15  HIS A CD2 1 
ATOM   100  C  CE1 . HIS A 1 15  ? 13.835  -7.694  15.695  1.00 20.76 ? 15  HIS A CE1 1 
ATOM   101  N  NE2 . HIS A 1 15  ? 12.775  -8.456  15.440  1.00 20.71 ? 15  HIS A NE2 1 
ATOM   102  N  N   . TRP A 1 16  ? 9.271   -3.261  17.871  1.00 14.11 ? 16  TRP A N   1 
ATOM   103  C  CA  . TRP A 1 16  ? 8.734   -1.914  17.771  1.00 15.21 ? 16  TRP A CA  1 
ATOM   104  C  C   . TRP A 1 16  ? 9.343   -0.917  18.760  1.00 14.25 ? 16  TRP A C   1 
ATOM   105  O  O   . TRP A 1 16  ? 9.352   0.300   18.479  1.00 15.26 ? 16  TRP A O   1 
ATOM   106  C  CB  . TRP A 1 16  ? 7.190   -1.978  17.910  1.00 14.30 ? 16  TRP A CB  1 
ATOM   107  C  CG  . TRP A 1 16  ? 6.513   -2.646  16.742  1.00 14.66 ? 16  TRP A CG  1 
ATOM   108  C  CD1 . TRP A 1 16  ? 7.034   -3.055  15.539  1.00 14.93 ? 16  TRP A CD1 1 
ATOM   109  C  CD2 . TRP A 1 16  ? 5.108   -2.960  16.689  1.00 15.12 ? 16  TRP A CD2 1 
ATOM   110  N  NE1 . TRP A 1 16  ? 6.066   -3.639  14.763  1.00 15.09 ? 16  TRP A NE1 1 
ATOM   111  C  CE2 . TRP A 1 16  ? 4.868   -3.559  15.436  1.00 15.34 ? 16  TRP A CE2 1 
ATOM   112  C  CE3 . TRP A 1 16  ? 4.040   -2.777  17.581  1.00 14.39 ? 16  TRP A CE3 1 
ATOM   113  C  CZ2 . TRP A 1 16  ? 3.608   -3.997  15.046  1.00 16.07 ? 16  TRP A CZ2 1 
ATOM   114  C  CZ3 . TRP A 1 16  ? 2.793   -3.231  17.210  1.00 14.36 ? 16  TRP A CZ3 1 
ATOM   115  C  CH2 . TRP A 1 16  ? 2.569   -3.803  15.950  1.00 15.46 ? 16  TRP A CH2 1 
ATOM   116  N  N   . HIS A 1 17  ? 9.754   -1.390  19.938  1.00 14.82 ? 17  HIS A N   1 
ATOM   117  C  CA  . HIS A 1 17  ? 10.182  -0.512  21.011  1.00 15.41 ? 17  HIS A CA  1 
ATOM   118  C  C   . HIS A 1 17  ? 11.425  0.284   20.600  1.00 15.17 ? 17  HIS A C   1 
ATOM   119  O  O   . HIS A 1 17  ? 11.679  1.317   21.197  1.00 16.79 ? 17  HIS A O   1 
ATOM   120  C  CB  . HIS A 1 17  ? 10.425  -1.235  22.336  1.00 15.32 ? 17  HIS A CB  1 
ATOM   121  C  CG  . HIS A 1 17  ? 11.626  -2.124  22.208  1.00 16.48 ? 17  HIS A CG  1 
ATOM   122  N  ND1 . HIS A 1 17  ? 12.882  -1.740  22.672  1.00 19.53 ? 17  HIS A ND1 1 
ATOM   123  C  CD2 . HIS A 1 17  ? 11.786  -3.330  21.642  1.00 17.08 ? 17  HIS A CD2 1 
ATOM   124  C  CE1 . HIS A 1 17  ? 13.747  -2.707  22.402  1.00 17.37 ? 17  HIS A CE1 1 
ATOM   125  N  NE2 . HIS A 1 17  ? 13.118  -3.678  21.777  1.00 19.29 ? 17  HIS A NE2 1 
ATOM   126  N  N   A LYS A 1 18  ? 12.168  -0.204  19.602  0.50 15.13 ? 18  LYS A N   1 
ATOM   127  N  N   B LYS A 1 18  ? 12.119  -0.162  19.544  0.50 15.95 ? 18  LYS A N   1 
ATOM   128  C  CA  A LYS A 1 18  ? 13.366  0.519   19.180  0.50 16.27 ? 18  LYS A CA  1 
ATOM   129  C  CA  B LYS A 1 18  ? 13.382  0.464   19.149  0.50 17.94 ? 18  LYS A CA  1 
ATOM   130  C  C   A LYS A 1 18  ? 12.953  1.876   18.605  0.50 17.34 ? 18  LYS A C   1 
ATOM   131  C  C   B LYS A 1 18  ? 13.147  1.743   18.336  0.50 18.34 ? 18  LYS A C   1 
ATOM   132  O  O   A LYS A 1 18  ? 13.448  2.933   19.035  0.50 16.09 ? 18  LYS A O   1 
ATOM   133  O  O   B LYS A 1 18  ? 13.973  2.646   18.333  0.50 18.68 ? 18  LYS A O   1 
ATOM   134  C  CB  A LYS A 1 18  ? 14.184  -0.328  18.197  0.50 15.94 ? 18  LYS A CB  1 
ATOM   135  C  CB  B LYS A 1 18  ? 14.270  -0.555  18.428  0.50 18.79 ? 18  LYS A CB  1 
ATOM   136  C  CG  A LYS A 1 18  ? 14.882  -1.532  18.821  0.50 15.32 ? 18  LYS A CG  1 
ATOM   137  C  CG  B LYS A 1 18  ? 14.754  -1.709  19.296  0.50 19.88 ? 18  LYS A CG  1 
ATOM   138  C  CD  A LYS A 1 18  ? 15.591  -2.456  17.853  0.50 14.36 ? 18  LYS A CD  1 
ATOM   139  C  CD  B LYS A 1 18  ? 14.598  -3.068  18.643  0.50 19.64 ? 18  LYS A CD  1 
ATOM   140  C  CE  A LYS A 1 18  ? 14.671  -3.490  17.216  0.50 13.80 ? 18  LYS A CE  1 
ATOM   141  C  CE  B LYS A 1 18  ? 15.350  -3.185  17.332  0.50 21.14 ? 18  LYS A CE  1 
ATOM   142  N  NZ  A LYS A 1 18  ? 15.341  -4.382  16.223  0.50 13.81 ? 18  LYS A NZ  1 
ATOM   143  N  NZ  B LYS A 1 18  ? 15.287  -4.551  16.759  0.50 21.47 ? 18  LYS A NZ  1 
ATOM   144  N  N   . ASP A 1 19  ? 12.006  1.851   17.650  1.00 18.00 ? 19  ASP A N   1 
ATOM   145  C  CA  . ASP A 1 19  ? 11.601  3.100   17.029  1.00 20.33 ? 19  ASP A CA  1 
ATOM   146  C  C   . ASP A 1 19  ? 10.591  3.857   17.889  1.00 22.18 ? 19  ASP A C   1 
ATOM   147  O  O   . ASP A 1 19  ? 10.488  5.073   17.777  1.00 22.21 ? 19  ASP A O   1 
ATOM   148  C  CB  . ASP A 1 19  ? 11.074  2.883   15.612  1.00 23.28 ? 19  ASP A CB  1 
ATOM   149  C  CG  . ASP A 1 19  ? 12.171  2.979   14.587  1.00 28.24 ? 19  ASP A CG  1 
ATOM   150  O  OD1 . ASP A 1 19  ? 13.109  3.756   14.818  1.00 34.27 ? 19  ASP A OD1 1 
ATOM   151  O  OD2 . ASP A 1 19  ? 12.046  2.323   13.557  1.00 34.96 ? 19  ASP A OD2 1 
ATOM   152  N  N   . PHE A 1 20  ? 9.825   3.130   18.724  1.00 18.78 ? 20  PHE A N   1 
ATOM   153  C  CA  . PHE A 1 20  ? 8.707   3.693   19.474  1.00 18.53 ? 20  PHE A CA  1 
ATOM   154  C  C   . PHE A 1 20  ? 8.833   3.207   20.916  1.00 18.64 ? 20  PHE A C   1 
ATOM   155  O  O   . PHE A 1 20  ? 8.254   2.201   21.316  1.00 17.04 ? 20  PHE A O   1 
ATOM   156  C  CB  . PHE A 1 20  ? 7.387   3.252   18.822  1.00 16.62 ? 20  PHE A CB  1 
ATOM   157  C  CG  . PHE A 1 20  ? 7.297   3.620   17.371  1.00 16.21 ? 20  PHE A CG  1 
ATOM   158  C  CD1 . PHE A 1 20  ? 6.957   4.919   17.014  1.00 17.07 ? 20  PHE A CD1 1 
ATOM   159  C  CD2 . PHE A 1 20  ? 7.585   2.699   16.373  1.00 16.13 ? 20  PHE A CD2 1 
ATOM   160  C  CE1 . PHE A 1 20  ? 6.907   5.260   15.673  1.00 17.83 ? 20  PHE A CE1 1 
ATOM   161  C  CE2 . PHE A 1 20  ? 7.544   3.051   15.031  1.00 16.83 ? 20  PHE A CE2 1 
ATOM   162  C  CZ  . PHE A 1 20  ? 7.213   4.345   14.691  1.00 19.69 ? 20  PHE A CZ  1 
ATOM   163  N  N   . PRO A 1 21  ? 9.733   3.804   21.718  1.00 19.80 ? 21  PRO A N   1 
ATOM   164  C  CA  . PRO A 1 21  ? 9.975   3.345   23.085  1.00 19.35 ? 21  PRO A CA  1 
ATOM   165  C  C   . PRO A 1 21  ? 8.770   3.205   24.022  1.00 19.36 ? 21  PRO A C   1 
ATOM   166  O  O   . PRO A 1 21  ? 8.816   2.429   24.979  1.00 19.50 ? 21  PRO A O   1 
ATOM   167  C  CB  . PRO A 1 21  ? 11.050  4.286   23.659  1.00 21.00 ? 21  PRO A CB  1 
ATOM   168  C  CG  . PRO A 1 21  ? 11.404  5.228   22.544  1.00 21.68 ? 21  PRO A CG  1 
ATOM   169  C  CD  . PRO A 1 21  ? 10.666  4.852   21.277  1.00 20.45 ? 21  PRO A CD  1 
ATOM   170  N  N   . ILE A 1 22  ? 7.693   3.966   23.736  1.00 18.03 ? 22  ILE A N   1 
ATOM   171  C  CA  . ILE A 1 22  ? 6.459   3.871   24.493  1.00 18.76 ? 22  ILE A CA  1 
ATOM   172  C  C   . ILE A 1 22  ? 5.875   2.458   24.374  1.00 16.32 ? 22  ILE A C   1 
ATOM   173  O  O   . ILE A 1 22  ? 4.989   2.097   25.146  1.00 14.72 ? 22  ILE A O   1 
ATOM   174  C  CB  . ILE A 1 22  ? 5.472   4.948   24.010  1.00 17.16 ? 22  ILE A CB  1 
ATOM   175  C  CG1 . ILE A 1 22  ? 4.359   5.226   25.024  1.00 20.09 ? 22  ILE A CG1 1 
ATOM   176  C  CG2 . ILE A 1 22  ? 4.932   4.573   22.625  1.00 19.15 ? 22  ILE A CG2 1 
ATOM   177  C  CD1 . ILE A 1 22  ? 3.502   6.469   24.725  1.00 21.80 ? 22  ILE A CD1 1 
ATOM   178  N  N   . ALA A 1 23  ? 6.375   1.660   23.425  1.00 14.65 ? 23  ALA A N   1 
ATOM   179  C  CA  . ALA A 1 23  ? 5.984   0.247   23.336  1.00 15.00 ? 23  ALA A CA  1 
ATOM   180  C  C   . ALA A 1 23  ? 6.025   -0.463  24.687  1.00 15.83 ? 23  ALA A C   1 
ATOM   181  O  O   . ALA A 1 23  ? 5.310   -1.460  24.913  1.00 15.12 ? 23  ALA A O   1 
ATOM   182  C  CB  . ALA A 1 23  ? 6.797   -0.526  22.336  1.00 14.47 ? 23  ALA A CB  1 
ATOM   183  N  N   . LYS A 1 24  ? 6.927   -0.021  25.568  1.00 17.61 ? 24  LYS A N   1 
ATOM   184  C  CA  . LYS A 1 24  ? 7.124   -0.674  26.855  1.00 17.86 ? 24  LYS A CA  1 
ATOM   185  C  C   . LYS A 1 24  ? 6.543   0.220   27.938  1.00 18.47 ? 24  LYS A C   1 
ATOM   186  O  O   . LYS A 1 24  ? 6.932   0.108   29.098  1.00 20.05 ? 24  LYS A O   1 
ATOM   187  C  CB  . LYS A 1 24  ? 8.636   -0.858  27.089  1.00 16.87 ? 24  LYS A CB  1 
ATOM   188  C  CG  . LYS A 1 24  ? 9.263   -2.009  26.307  1.00 17.92 ? 24  LYS A CG  1 
ATOM   189  C  CD  . LYS A 1 24  ? 10.783  -2.043  26.479  1.00 21.38 ? 24  LYS A CD  1 
ATOM   190  C  CE  . LYS A 1 24  ? 11.475  -3.070  25.600  1.00 20.27 ? 24  LYS A CE  1 
ATOM   191  N  NZ  . LYS A 1 24  ? 11.255  -4.471  26.047  1.00 25.52 ? 24  LYS A NZ  1 
ATOM   192  N  N   . GLY A 1 25  ? 5.562   1.071   27.566  1.00 18.75 ? 25  GLY A N   1 
ATOM   193  C  CA  . GLY A 1 25  ? 4.975   2.036   28.488  1.00 17.96 ? 25  GLY A CA  1 
ATOM   194  C  C   . GLY A 1 25  ? 3.998   1.437   29.493  1.00 16.96 ? 25  GLY A C   1 
ATOM   195  O  O   . GLY A 1 25  ? 3.828   0.224   29.619  1.00 18.06 ? 25  GLY A O   1 
ATOM   196  N  N   . GLU A 1 26  ? 3.331   2.340   30.210  1.00 17.64 ? 26  GLU A N   1 
ATOM   197  C  CA  . GLU A 1 26  ? 2.539   1.930   31.343  1.00 19.32 ? 26  GLU A CA  1 
ATOM   198  C  C   . GLU A 1 26  ? 1.090   1.622   30.971  1.00 16.44 ? 26  GLU A C   1 
ATOM   199  O  O   . GLU A 1 26  ? 0.353   1.116   31.812  1.00 15.52 ? 26  GLU A O   1 
ATOM   200  C  CB  . GLU A 1 26  ? 2.561   3.028   32.417  1.00 24.70 ? 26  GLU A CB  1 
ATOM   201  C  CG  . GLU A 1 26  ? 3.918   3.239   33.093  1.00 29.59 ? 26  GLU A CG  1 
ATOM   202  C  CD  . GLU A 1 26  ? 4.658   2.002   33.612  1.00 37.20 ? 26  GLU A CD  1 
ATOM   203  O  OE1 . GLU A 1 26  ? 4.116   1.304   34.534  1.00 39.40 ? 26  GLU A OE1 1 
ATOM   204  O  OE2 . GLU A 1 26  ? 5.780   1.720   33.084  1.00 36.72 ? 26  GLU A OE2 1 
ATOM   205  N  N   . ARG A 1 27  ? 0.629   1.942   29.741  1.00 14.27 ? 27  ARG A N   1 
ATOM   206  C  CA  . ARG A 1 27  ? -0.775  1.691   29.388  1.00 13.51 ? 27  ARG A CA  1 
ATOM   207  C  C   . ARG A 1 27  ? -0.830  1.240   27.912  1.00 12.42 ? 27  ARG A C   1 
ATOM   208  O  O   . ARG A 1 27  ? -1.514  1.836   27.072  1.00 13.31 ? 27  ARG A O   1 
ATOM   209  C  CB  . ARG A 1 27  ? -1.701  2.873   29.716  1.00 15.59 ? 27  ARG A CB  1 
ATOM   210  C  CG  . ARG A 1 27  ? -1.370  4.216   29.070  1.00 16.62 ? 27  ARG A CG  1 
ATOM   211  C  CD  . ARG A 1 27  ? -2.287  5.440   29.272  1.00 21.81 ? 27  ARG A CD  1 
ATOM   212  N  NE  . ARG A 1 27  ? -3.529  5.331   28.519  1.00 22.60 ? 27  ARG A NE  1 
ATOM   213  C  CZ  . ARG A 1 27  ? -4.376  6.334   28.315  1.00 19.98 ? 27  ARG A CZ  1 
ATOM   214  N  NH1 . ARG A 1 27  ? -4.114  7.531   28.811  1.00 16.07 ? 27  ARG A NH1 1 
ATOM   215  N  NH2 . ARG A 1 27  ? -5.479  6.136   27.616  1.00 17.14 ? 27  ARG A NH2 1 
ATOM   216  N  N   . GLN A 1 28  ? -0.146  0.128   27.628  1.00 11.13 ? 28  GLN A N   1 
ATOM   217  C  CA  . GLN A 1 28  ? -0.124  -0.392  26.265  1.00 9.55  ? 28  GLN A CA  1 
ATOM   218  C  C   . GLN A 1 28  ? -1.304  -1.359  26.021  1.00 9.09  ? 28  GLN A C   1 
ATOM   219  O  O   . GLN A 1 28  ? -1.779  -2.017  26.932  1.00 10.38 ? 28  GLN A O   1 
ATOM   220  C  CB  . GLN A 1 28  ? 1.245   -1.037  25.995  1.00 10.21 ? 28  GLN A CB  1 
ATOM   221  C  CG  . GLN A 1 28  ? 2.323   0.041   25.876  1.00 9.67  ? 28  GLN A CG  1 
ATOM   222  C  CD  . GLN A 1 28  ? 2.189   0.792   24.565  1.00 10.39 ? 28  GLN A CD  1 
ATOM   223  O  OE1 . GLN A 1 28  ? 2.384   0.266   23.477  1.00 11.43 ? 28  GLN A OE1 1 
ATOM   224  N  NE2 . GLN A 1 28  ? 1.892   2.072   24.642  1.00 10.69 ? 28  GLN A NE2 1 
ATOM   225  N  N   . SER A 1 29  ? -1.653  -1.475  24.734  1.00 9.58  ? 29  SER A N   1 
ATOM   226  C  CA  . SER A 1 29  ? -2.768  -2.275  24.228  1.00 9.99  ? 29  SER A CA  1 
ATOM   227  C  C   . SER A 1 29  ? -2.236  -3.153  23.097  1.00 10.74 ? 29  SER A C   1 
ATOM   228  O  O   . SER A 1 29  ? -1.296  -2.773  22.404  1.00 11.86 ? 29  SER A O   1 
ATOM   229  C  CB  . SER A 1 29  ? -3.865  -1.380  23.695  1.00 9.59  ? 29  SER A CB  1 
ATOM   230  O  OG  . SER A 1 29  ? -4.479  -0.739  24.802  1.00 9.97  ? 29  SER A OG  1 
ATOM   231  N  N   . PRO A 1 30  ? -2.815  -4.340  22.871  1.00 9.71  ? 30  PRO A N   1 
ATOM   232  C  CA  . PRO A 1 30  ? -4.002  -4.815  23.594  1.00 10.78 ? 30  PRO A CA  1 
ATOM   233  C  C   . PRO A 1 30  ? -3.606  -5.483  24.912  1.00 11.55 ? 30  PRO A C   1 
ATOM   234  O  O   . PRO A 1 30  ? -2.415  -5.586  25.200  1.00 10.17 ? 30  PRO A O   1 
ATOM   235  C  CB  . PRO A 1 30  ? -4.496  -5.941  22.678  1.00 10.68 ? 30  PRO A CB  1 
ATOM   236  C  CG  . PRO A 1 30  ? -3.205  -6.489  22.001  1.00 9.89  ? 30  PRO A CG  1 
ATOM   237  C  CD  . PRO A 1 30  ? -2.377  -5.237  21.792  1.00 10.33 ? 30  PRO A CD  1 
ATOM   238  N  N   . VAL A 1 31  ? -4.577  -6.136  25.552  1.00 11.57 ? 31  VAL A N   1 
ATOM   239  C  CA  . VAL A 1 31  ? -4.392  -6.858  26.798  1.00 10.83 ? 31  VAL A CA  1 
ATOM   240  C  C   . VAL A 1 31  ? -5.276  -8.099  26.770  1.00 11.01 ? 31  VAL A C   1 
ATOM   241  O  O   . VAL A 1 31  ? -6.282  -8.184  26.035  1.00 11.05 ? 31  VAL A O   1 
ATOM   242  C  CB  . VAL A 1 31  ? -4.682  -6.029  28.076  1.00 11.69 ? 31  VAL A CB  1 
ATOM   243  C  CG1 . VAL A 1 31  ? -3.731  -4.827  28.205  1.00 12.55 ? 31  VAL A CG1 1 
ATOM   244  C  CG2 . VAL A 1 31  ? -6.135  -5.559  28.167  1.00 11.38 ? 31  VAL A CG2 1 
ATOM   245  N  N   . ASP A 1 32  ? -4.926  -9.049  27.648  1.00 11.19 ? 32  ASP A N   1 
ATOM   246  C  CA  . ASP A 1 32  ? -5.830  -10.142 27.932  1.00 11.91 ? 32  ASP A CA  1 
ATOM   247  C  C   . ASP A 1 32  ? -6.922  -9.656  28.884  1.00 12.29 ? 32  ASP A C   1 
ATOM   248  O  O   . ASP A 1 32  ? -6.653  -9.006  29.895  1.00 13.94 ? 32  ASP A O   1 
ATOM   249  C  CB  . ASP A 1 32  ? -5.078  -11.339 28.512  1.00 12.29 ? 32  ASP A CB  1 
ATOM   250  C  CG  . ASP A 1 32  ? -6.046  -12.483 28.807  1.00 15.44 ? 32  ASP A CG  1 
ATOM   251  O  OD1 . ASP A 1 32  ? -6.800  -12.887 27.884  1.00 13.60 ? 32  ASP A OD1 1 
ATOM   252  O  OD2 . ASP A 1 32  ? -6.102  -12.939 30.009  1.00 17.04 ? 32  ASP A OD2 1 
ATOM   253  N  N   . ILE A 1 33  ? -8.185  -9.988  28.579  1.00 12.82 ? 33  ILE A N   1 
ATOM   254  C  CA  . ILE A 1 33  ? -9.292  -9.599  29.413  1.00 13.09 ? 33  ILE A CA  1 
ATOM   255  C  C   . ILE A 1 33  ? -9.641  -10.811 30.265  1.00 14.95 ? 33  ILE A C   1 
ATOM   256  O  O   . ILE A 1 33  ? -10.203 -11.798 29.790  1.00 15.83 ? 33  ILE A O   1 
ATOM   257  C  CB  . ILE A 1 33  ? -10.513 -9.076  28.631  1.00 14.71 ? 33  ILE A CB  1 
ATOM   258  C  CG1 . ILE A 1 33  ? -10.177 -7.816  27.822  1.00 13.37 ? 33  ILE A CG1 1 
ATOM   259  C  CG2 . ILE A 1 33  ? -11.701 -8.835  29.559  1.00 14.45 ? 33  ILE A CG2 1 
ATOM   260  C  CD1 . ILE A 1 33  ? -11.148 -7.590  26.617  1.00 14.69 ? 33  ILE A CD1 1 
ATOM   261  N  N   A ASP A 1 34  ? -9.265  -10.741 31.537  0.50 15.39 ? 34  ASP A N   1 
ATOM   262  N  N   B ASP A 1 34  ? -9.282  -10.696 31.548  0.50 15.56 ? 34  ASP A N   1 
ATOM   263  C  CA  A ASP A 1 34  ? -9.585  -11.863 32.398  0.50 16.94 ? 34  ASP A CA  1 
ATOM   264  C  CA  B ASP A 1 34  ? -9.602  -11.696 32.553  0.50 17.69 ? 34  ASP A CA  1 
ATOM   265  C  C   A ASP A 1 34  ? -10.936 -11.556 33.041  0.50 16.76 ? 34  ASP A C   1 
ATOM   266  C  C   B ASP A 1 34  ? -11.028 -11.431 33.017  0.50 17.23 ? 34  ASP A C   1 
ATOM   267  O  O   A ASP A 1 34  ? -11.019 -10.697 33.912  0.50 16.69 ? 34  ASP A O   1 
ATOM   268  O  O   B ASP A 1 34  ? -11.261 -10.484 33.758  0.50 18.01 ? 34  ASP A O   1 
ATOM   269  C  CB  A ASP A 1 34  ? -8.416  -12.164 33.343  0.50 17.91 ? 34  ASP A CB  1 
ATOM   270  C  CB  B ASP A 1 34  ? -8.666  -11.549 33.756  0.50 18.15 ? 34  ASP A CB  1 
ATOM   271  C  CG  A ASP A 1 34  ? -8.736  -13.339 34.255  0.50 19.47 ? 34  ASP A CG  1 
ATOM   272  C  CG  B ASP A 1 34  ? -8.815  -12.685 34.754  0.50 19.85 ? 34  ASP A CG  1 
ATOM   273  O  OD1 A ASP A 1 34  ? -8.489  -14.510 33.837  0.50 18.48 ? 34  ASP A OD1 1 
ATOM   274  O  OD1 B ASP A 1 34  ? -9.923  -13.286 34.795  0.50 19.66 ? 34  ASP A OD1 1 
ATOM   275  O  OD2 A ASP A 1 34  ? -9.304  -13.069 35.331  0.50 19.86 ? 34  ASP A OD2 1 
ATOM   276  O  OD2 B ASP A 1 34  ? -7.803  -13.006 35.432  0.50 21.76 ? 34  ASP A OD2 1 
ATOM   277  N  N   . THR A 1 35  ? -11.970 -12.260 32.574  1.00 17.68 ? 35  THR A N   1 
ATOM   278  C  CA  . THR A 1 35  ? -13.367 -11.915 32.721  1.00 20.00 ? 35  THR A CA  1 
ATOM   279  C  C   . THR A 1 35  ? -13.758 -12.079 34.181  1.00 18.71 ? 35  THR A C   1 
ATOM   280  O  O   . THR A 1 35  ? -14.738 -11.476 34.609  1.00 21.67 ? 35  THR A O   1 
ATOM   281  C  CB  . THR A 1 35  ? -14.271 -12.841 31.906  1.00 21.71 ? 35  THR A CB  1 
ATOM   282  O  OG1 . THR A 1 35  ? -14.047 -14.189 32.326  1.00 20.87 ? 35  THR A OG1 1 
ATOM   283  C  CG2 . THR A 1 35  ? -14.003 -12.762 30.422  1.00 22.66 ? 35  THR A CG2 1 
ATOM   284  N  N   . HIS A 1 36  ? -12.983 -12.926 34.874  1.00 20.78 ? 36  HIS A N   1 
ATOM   285  C  CA  . HIS A 1 36  ? -13.171 -13.197 36.292  1.00 22.69 ? 36  HIS A CA  1 
ATOM   286  C  C   . HIS A 1 36  ? -12.695 -12.035 37.164  1.00 25.24 ? 36  HIS A C   1 
ATOM   287  O  O   . HIS A 1 36  ? -13.384 -11.728 38.124  1.00 31.94 ? 36  HIS A O   1 
ATOM   288  C  CB  . HIS A 1 36  ? -12.711 -14.630 36.630  1.00 21.52 ? 36  HIS A CB  1 
ATOM   289  C  CG  . HIS A 1 36  ? -13.617 -15.641 36.017  1.00 21.29 ? 36  HIS A CG  1 
ATOM   290  N  ND1 . HIS A 1 36  ? -14.957 -15.736 36.371  1.00 23.59 ? 36  HIS A ND1 1 
ATOM   291  C  CD2 . HIS A 1 36  ? -13.407 -16.554 35.049  1.00 22.24 ? 36  HIS A CD2 1 
ATOM   292  C  CE1 . HIS A 1 36  ? -15.532 -16.685 35.648  1.00 27.13 ? 36  HIS A CE1 1 
ATOM   293  N  NE2 . HIS A 1 36  ? -14.596 -17.191 34.817  1.00 28.46 ? 36  HIS A NE2 1 
ATOM   294  N  N   . THR A 1 37  ? -11.590 -11.355 36.821  1.00 23.51 ? 37  THR A N   1 
ATOM   295  C  CA  . THR A 1 37  ? -11.099 -10.230 37.613  1.00 24.14 ? 37  THR A CA  1 
ATOM   296  C  C   . THR A 1 37  ? -11.517 -8.839  37.089  1.00 20.67 ? 37  THR A C   1 
ATOM   297  O  O   . THR A 1 37  ? -11.138 -7.813  37.681  1.00 20.95 ? 37  THR A O   1 
ATOM   298  C  CB  . THR A 1 37  ? -9.605  -10.345 37.939  1.00 30.24 ? 37  THR A CB  1 
ATOM   299  O  OG1 . THR A 1 37  ? -8.859  -9.973  36.782  1.00 30.59 ? 37  THR A OG1 1 
ATOM   300  C  CG2 . THR A 1 37  ? -9.178  -11.729 38.389  1.00 29.78 ? 37  THR A CG2 1 
ATOM   301  N  N   . ALA A 1 38  ? -12.270 -8.782  35.977  1.00 18.30 ? 38  ALA A N   1 
ATOM   302  C  CA  . ALA A 1 38  ? -12.883 -7.521  35.561  1.00 17.86 ? 38  ALA A CA  1 
ATOM   303  C  C   . ALA A 1 38  ? -13.903 -7.089  36.617  1.00 20.38 ? 38  ALA A C   1 
ATOM   304  O  O   . ALA A 1 38  ? -14.665 -7.913  37.114  1.00 23.78 ? 38  ALA A O   1 
ATOM   305  C  CB  . ALA A 1 38  ? -13.492 -7.650  34.178  1.00 19.41 ? 38  ALA A CB  1 
ATOM   306  N  N   . LYS A 1 39  ? -13.928 -5.793  36.916  1.00 19.72 ? 39  LYS A N   1 
ATOM   307  C  CA  . LYS A 1 39  ? -14.795 -5.249  37.953  1.00 20.72 ? 39  LYS A CA  1 
ATOM   308  C  C   . LYS A 1 39  ? -16.114 -4.744  37.341  1.00 21.75 ? 39  LYS A C   1 
ATOM   309  O  O   . LYS A 1 39  ? -16.130 -3.782  36.559  1.00 19.00 ? 39  LYS A O   1 
ATOM   310  C  CB  . LYS A 1 39  ? -14.069 -4.076  38.614  1.00 22.69 ? 39  LYS A CB  1 
ATOM   311  C  CG  . LYS A 1 39  ? -14.895 -3.276  39.620  1.00 25.42 ? 39  LYS A CG  1 
ATOM   312  C  CD  . LYS A 1 39  ? -15.125 -3.935  40.973  1.00 26.07 ? 39  LYS A CD  1 
ATOM   313  C  CE  . LYS A 1 39  ? -15.887 -3.043  41.945  1.00 31.27 ? 39  LYS A CE  1 
ATOM   314  N  NZ  . LYS A 1 39  ? -16.191 -3.710  43.245  1.00 29.50 ? 39  LYS A NZ  1 
ATOM   315  N  N   . TYR A 1 40  ? -17.246 -5.325  37.777  1.00 21.79 ? 40  TYR A N   1 
ATOM   316  C  CA  . TYR A 1 40  ? -18.542 -4.773  37.390  1.00 23.05 ? 40  TYR A CA  1 
ATOM   317  C  C   . TYR A 1 40  ? -18.736 -3.382  37.989  1.00 22.35 ? 40  TYR A C   1 
ATOM   318  O  O   . TYR A 1 40  ? -18.602 -3.152  39.204  1.00 19.06 ? 40  TYR A O   1 
ATOM   319  C  CB  . TYR A 1 40  ? -19.706 -5.731  37.668  1.00 25.98 ? 40  TYR A CB  1 
ATOM   320  C  CG  . TYR A 1 40  ? -21.077 -5.100  37.545  1.00 29.42 ? 40  TYR A CG  1 
ATOM   321  C  CD1 . TYR A 1 40  ? -21.562 -4.648  36.323  1.00 27.24 ? 40  TYR A CD1 1 
ATOM   322  C  CD2 . TYR A 1 40  ? -21.888 -4.929  38.663  1.00 32.89 ? 40  TYR A CD2 1 
ATOM   323  C  CE1 . TYR A 1 40  ? -22.806 -4.064  36.197  1.00 31.97 ? 40  TYR A CE1 1 
ATOM   324  C  CE2 . TYR A 1 40  ? -23.143 -4.340  38.557  1.00 33.79 ? 40  TYR A CE2 1 
ATOM   325  C  CZ  . TYR A 1 40  ? -23.599 -3.902  37.323  1.00 35.71 ? 40  TYR A CZ  1 
ATOM   326  O  OH  . TYR A 1 40  ? -24.825 -3.320  37.217  1.00 39.09 ? 40  TYR A OH  1 
ATOM   327  N  N   . ASP A 1 41  ? -19.086 -2.441  37.120  1.00 21.86 ? 41  ASP A N   1 
ATOM   328  C  CA  . ASP A 1 41  ? -19.253 -1.070  37.583  1.00 24.26 ? 41  ASP A CA  1 
ATOM   329  C  C   . ASP A 1 41  ? -20.652 -0.571  37.246  1.00 29.20 ? 41  ASP A C   1 
ATOM   330  O  O   . ASP A 1 41  ? -20.927 -0.184  36.111  1.00 22.98 ? 41  ASP A O   1 
ATOM   331  C  CB  . ASP A 1 41  ? -18.158 -0.139  37.097  1.00 26.73 ? 41  ASP A CB  1 
ATOM   332  C  CG  . ASP A 1 41  ? -18.378 1.285   37.560  1.00 30.63 ? 41  ASP A CG  1 
ATOM   333  O  OD1 . ASP A 1 41  ? -19.413 1.522   38.244  1.00 31.75 ? 41  ASP A OD1 1 
ATOM   334  O  OD2 . ASP A 1 41  ? -17.507 2.132   37.238  1.00 32.94 ? 41  ASP A OD2 1 
ATOM   335  N  N   . PRO A 1 42  ? -21.573 -0.537  38.231  1.00 33.68 ? 42  PRO A N   1 
ATOM   336  C  CA  . PRO A 1 42  ? -22.977 -0.231  37.945  1.00 34.94 ? 42  PRO A CA  1 
ATOM   337  C  C   . PRO A 1 42  ? -23.210 1.258   37.674  1.00 35.12 ? 42  PRO A C   1 
ATOM   338  O  O   . PRO A 1 42  ? -24.333 1.644   37.334  1.00 41.70 ? 42  PRO A O   1 
ATOM   339  C  CB  . PRO A 1 42  ? -23.729 -0.735  39.198  1.00 37.68 ? 42  PRO A CB  1 
ATOM   340  C  CG  . PRO A 1 42  ? -22.684 -0.719  40.315  1.00 39.69 ? 42  PRO A CG  1 
ATOM   341  C  CD  . PRO A 1 42  ? -21.306 -0.743  39.666  1.00 37.28 ? 42  PRO A CD  1 
ATOM   342  N  N   . SER A 1 43  ? -22.145 2.080   37.788  1.00 34.84 ? 43  SER A N   1 
ATOM   343  C  CA  . SER A 1 43  ? -22.191 3.491   37.412  1.00 34.96 ? 43  SER A CA  1 
ATOM   344  C  C   . SER A 1 43  ? -21.866 3.708   35.926  1.00 36.36 ? 43  SER A C   1 
ATOM   345  O  O   . SER A 1 43  ? -21.923 4.842   35.426  1.00 34.50 ? 43  SER A O   1 
ATOM   346  C  CB  . SER A 1 43  ? -21.267 4.310   38.278  1.00 40.51 ? 43  SER A CB  1 
ATOM   347  O  OG  . SER A 1 43  ? -19.916 4.198   37.835  1.00 37.94 ? 43  SER A OG  1 
ATOM   348  N  N   . LEU A 1 44  ? -21.476 2.632   35.225  1.00 32.25 ? 44  LEU A N   1 
ATOM   349  C  CA  . LEU A 1 44  ? -21.200 2.736   33.793  1.00 26.30 ? 44  LEU A CA  1 
ATOM   350  C  C   . LEU A 1 44  ? -22.515 2.826   33.029  1.00 28.80 ? 44  LEU A C   1 
ATOM   351  O  O   . LEU A 1 44  ? -23.409 1.998   33.225  1.00 28.25 ? 44  LEU A O   1 
ATOM   352  C  CB  . LEU A 1 44  ? -20.380 1.530   33.323  1.00 24.62 ? 44  LEU A CB  1 
ATOM   353  C  CG  . LEU A 1 44  ? -18.885 1.594   33.634  1.00 23.04 ? 44  LEU A CG  1 
ATOM   354  C  CD1 . LEU A 1 44  ? -18.238 0.251   33.332  1.00 22.89 ? 44  LEU A CD1 1 
ATOM   355  C  CD2 . LEU A 1 44  ? -18.218 2.706   32.841  1.00 21.44 ? 44  LEU A CD2 1 
ATOM   356  N  N   . LYS A 1 45  ? -22.561 3.792   32.104  1.00 26.86 ? 45  LYS A N   1 
ATOM   357  C  CA  . LYS A 1 45  ? -23.726 4.083   31.268  1.00 25.53 ? 45  LYS A CA  1 
ATOM   358  C  C   . LYS A 1 45  ? -23.737 3.125   30.080  1.00 26.54 ? 45  LYS A C   1 
ATOM   359  O  O   . LYS A 1 45  ? -22.688 2.565   29.716  1.00 25.24 ? 45  LYS A O   1 
ATOM   360  C  CB  . LYS A 1 45  ? -23.596 5.515   30.750  1.00 27.18 ? 45  LYS A CB  1 
ATOM   361  C  CG  . LYS A 1 45  ? -23.487 6.597   31.828  1.00 30.81 ? 45  LYS A CG  1 
ATOM   362  C  CD  . LYS A 1 45  ? -23.391 8.006   31.276  0.01 29.51 ? 45  LYS A CD  1 
ATOM   363  C  CE  . LYS A 1 45  ? -22.014 8.358   30.750  0.01 29.76 ? 45  LYS A CE  1 
ATOM   364  N  NZ  . LYS A 1 45  ? -21.969 9.738   30.212  0.01 29.77 ? 45  LYS A NZ  1 
ATOM   365  N  N   . PRO A 1 46  ? -24.928 2.860   29.481  1.00 23.87 ? 46  PRO A N   1 
ATOM   366  C  CA  . PRO A 1 46  ? -25.016 2.167   28.199  1.00 22.64 ? 46  PRO A CA  1 
ATOM   367  C  C   . PRO A 1 46  ? -24.134 2.957   27.230  1.00 19.40 ? 46  PRO A C   1 
ATOM   368  O  O   . PRO A 1 46  ? -24.030 4.171   27.335  1.00 18.92 ? 46  PRO A O   1 
ATOM   369  C  CB  . PRO A 1 46  ? -26.501 2.271   27.794  1.00 25.35 ? 46  PRO A CB  1 
ATOM   370  C  CG  . PRO A 1 46  ? -27.243 2.526   29.092  1.00 24.51 ? 46  PRO A CG  1 
ATOM   371  C  CD  . PRO A 1 46  ? -26.258 3.207   30.027  1.00 23.48 ? 46  PRO A CD  1 
ATOM   372  N  N   . LEU A 1 47  ? -23.505 2.236   26.302  1.00 22.59 ? 47  LEU A N   1 
ATOM   373  C  CA  . LEU A 1 47  ? -22.768 2.857   25.222  1.00 22.21 ? 47  LEU A CA  1 
ATOM   374  C  C   . LEU A 1 47  ? -23.800 3.463   24.274  1.00 23.81 ? 47  LEU A C   1 
ATOM   375  O  O   . LEU A 1 47  ? -24.827 2.836   24.018  1.00 23.27 ? 47  LEU A O   1 
ATOM   376  C  CB  . LEU A 1 47  ? -22.001 1.738   24.504  1.00 22.08 ? 47  LEU A CB  1 
ATOM   377  C  CG  . LEU A 1 47  ? -20.903 2.209   23.563  1.00 24.89 ? 47  LEU A CG  1 
ATOM   378  C  CD1 . LEU A 1 47  ? -19.897 3.089   24.301  1.00 25.51 ? 47  LEU A CD1 1 
ATOM   379  C  CD2 . LEU A 1 47  ? -20.212 0.996   22.957  1.00 26.05 ? 47  LEU A CD2 1 
ATOM   380  N  N   . SER A 1 48  ? -23.509 4.651   23.731  1.00 19.57 ? 48  SER A N   1 
ATOM   381  C  CA  . SER A 1 48  ? -24.367 5.235   22.719  1.00 21.14 ? 48  SER A CA  1 
ATOM   382  C  C   . SER A 1 48  ? -23.630 5.234   21.380  1.00 20.93 ? 48  SER A C   1 
ATOM   383  O  O   . SER A 1 48  ? -22.638 5.956   21.228  1.00 15.87 ? 48  SER A O   1 
ATOM   384  C  CB  . SER A 1 48  ? -24.755 6.629   23.142  1.00 22.81 ? 48  SER A CB  1 
ATOM   385  O  OG  . SER A 1 48  ? -25.503 7.300   22.147  1.00 25.35 ? 48  SER A OG  1 
ATOM   386  N  N   . VAL A 1 49  ? -24.128 4.438   20.427  1.00 21.07 ? 49  VAL A N   1 
ATOM   387  C  CA  . VAL A 1 49  ? -23.604 4.375   19.070  1.00 21.00 ? 49  VAL A CA  1 
ATOM   388  C  C   . VAL A 1 49  ? -24.599 5.021   18.110  1.00 23.94 ? 49  VAL A C   1 
ATOM   389  O  O   . VAL A 1 49  ? -25.661 4.476   17.822  1.00 26.14 ? 49  VAL A O   1 
ATOM   390  C  CB  . VAL A 1 49  ? -23.283 2.923   18.678  1.00 22.82 ? 49  VAL A CB  1 
ATOM   391  C  CG1 . VAL A 1 49  ? -22.637 2.847   17.304  1.00 23.56 ? 49  VAL A CG1 1 
ATOM   392  C  CG2 . VAL A 1 49  ? -22.422 2.265   19.745  1.00 23.60 ? 49  VAL A CG2 1 
ATOM   393  N  N   . SER A 1 50  ? -24.292 6.232   17.665  1.00 21.63 ? 50  SER A N   1 
ATOM   394  C  CA  . SER A 1 50  ? -25.148 6.898   16.698  1.00 23.17 ? 50  SER A CA  1 
ATOM   395  C  C   . SER A 1 50  ? -24.492 6.927   15.321  1.00 22.01 ? 50  SER A C   1 
ATOM   396  O  O   . SER A 1 50  ? -23.826 7.886   14.983  1.00 21.70 ? 50  SER A O   1 
ATOM   397  C  CB  . SER A 1 50  ? -25.543 8.280   17.145  1.00 24.74 ? 50  SER A CB  1 
ATOM   398  O  OG  . SER A 1 50  ? -26.045 8.242   18.467  1.00 33.70 ? 50  SER A OG  1 
ATOM   399  N  N   . TYR A 1 51  ? -24.764 5.908   14.504  1.00 22.31 ? 51  TYR A N   1 
ATOM   400  C  CA  . TYR A 1 51  ? -24.154 5.743   13.196  1.00 19.90 ? 51  TYR A CA  1 
ATOM   401  C  C   . TYR A 1 51  ? -25.132 5.968   12.033  1.00 21.59 ? 51  TYR A C   1 
ATOM   402  O  O   . TYR A 1 51  ? -24.744 5.725   10.886  1.00 20.08 ? 51  TYR A O   1 
ATOM   403  C  CB  . TYR A 1 51  ? -23.486 4.363   13.079  1.00 18.83 ? 51  TYR A CB  1 
ATOM   404  C  CG  . TYR A 1 51  ? -22.195 4.127   13.837  1.00 17.48 ? 51  TYR A CG  1 
ATOM   405  C  CD1 . TYR A 1 51  ? -21.470 5.142   14.469  1.00 17.19 ? 51  TYR A CD1 1 
ATOM   406  C  CD2 . TYR A 1 51  ? -21.685 2.836   13.891  1.00 15.47 ? 51  TYR A CD2 1 
ATOM   407  C  CE1 . TYR A 1 51  ? -20.281 4.853   15.142  1.00 16.23 ? 51  TYR A CE1 1 
ATOM   408  C  CE2 . TYR A 1 51  ? -20.507 2.529   14.553  1.00 16.66 ? 51  TYR A CE2 1 
ATOM   409  C  CZ  . TYR A 1 51  ? -19.800 3.547   15.186  1.00 15.56 ? 51  TYR A CZ  1 
ATOM   410  O  OH  . TYR A 1 51  ? -18.635 3.167   15.831  1.00 15.73 ? 51  TYR A OH  1 
ATOM   411  N  N   . ASP A 1 52  ? -26.346 6.496   12.316  1.00 25.86 ? 52  ASP A N   1 
ATOM   412  C  CA  . ASP A 1 52  ? -27.375 6.744   11.305  1.00 30.35 ? 52  ASP A CA  1 
ATOM   413  C  C   . ASP A 1 52  ? -26.857 7.508   10.081  1.00 29.28 ? 52  ASP A C   1 
ATOM   414  O  O   . ASP A 1 52  ? -27.126 7.105   8.943   1.00 30.66 ? 52  ASP A O   1 
ATOM   415  C  CB  . ASP A 1 52  ? -28.692 7.319   11.851  1.00 33.83 ? 52  ASP A CB  1 
ATOM   416  C  CG  . ASP A 1 52  ? -28.621 8.203   13.094  1.00 44.17 ? 52  ASP A CG  1 
ATOM   417  O  OD1 . ASP A 1 52  ? -28.032 7.763   14.124  1.00 52.05 ? 52  ASP A OD1 1 
ATOM   418  O  OD2 . ASP A 1 52  ? -29.187 9.327   13.046  1.00 48.98 ? 52  ASP A OD2 1 
ATOM   419  N  N   . GLN A 1 53  ? -26.116 8.598   10.293  1.00 29.65 ? 53  GLN A N   1 
ATOM   420  C  CA  . GLN A 1 53  ? -25.753 9.404   9.128   1.00 29.66 ? 53  GLN A CA  1 
ATOM   421  C  C   . GLN A 1 53  ? -24.264 9.300   8.782   1.00 24.88 ? 53  GLN A C   1 
ATOM   422  O  O   . GLN A 1 53  ? -23.699 10.257  8.259   1.00 24.73 ? 53  GLN A O   1 
ATOM   423  C  CB  . GLN A 1 53  ? -26.182 10.867  9.318   1.00 33.09 ? 53  GLN A CB  1 
ATOM   424  C  CG  . GLN A 1 53  ? -27.696 11.088  9.398   1.00 36.63 ? 53  GLN A CG  1 
ATOM   425  C  CD  . GLN A 1 53  ? -28.509 10.403  8.319   1.00 46.33 ? 53  GLN A CD  1 
ATOM   426  O  OE1 . GLN A 1 53  ? -28.264 10.545  7.109   1.00 42.94 ? 53  GLN A OE1 1 
ATOM   427  N  NE2 . GLN A 1 53  ? -29.518 9.660   8.755   1.00 45.87 ? 53  GLN A NE2 1 
ATOM   428  N  N   . ALA A 1 54  ? -23.641 8.133   9.010   1.00 20.35 ? 54  ALA A N   1 
ATOM   429  C  CA  . ALA A 1 54  ? -22.232 7.951   8.684   1.00 17.74 ? 54  ALA A CA  1 
ATOM   430  C  C   . ALA A 1 54  ? -22.009 8.120   7.174   1.00 20.47 ? 54  ALA A C   1 
ATOM   431  O  O   . ALA A 1 54  ? -22.839 7.675   6.370   1.00 21.34 ? 54  ALA A O   1 
ATOM   432  C  CB  . ALA A 1 54  ? -21.743 6.603   9.160   1.00 19.46 ? 54  ALA A CB  1 
ATOM   433  N  N   . THR A 1 55  ? -20.872 8.732   6.813   1.00 16.20 ? 55  THR A N   1 
ATOM   434  C  CA  . THR A 1 55  ? -20.442 8.880   5.429   1.00 15.99 ? 55  THR A CA  1 
ATOM   435  C  C   . THR A 1 55  ? -19.064 8.265   5.215   1.00 15.88 ? 55  THR A C   1 
ATOM   436  O  O   . THR A 1 55  ? -18.076 8.886   5.574   1.00 15.34 ? 55  THR A O   1 
ATOM   437  C  CB  . THR A 1 55  ? -20.243 10.373  5.099   1.00 17.02 ? 55  THR A CB  1 
ATOM   438  O  OG1 . THR A 1 55  ? -21.545 10.945  5.144   1.00 19.99 ? 55  THR A OG1 1 
ATOM   439  C  CG2 . THR A 1 55  ? -19.728 10.540  3.684   1.00 19.75 ? 55  THR A CG2 1 
ATOM   440  N  N   . SER A 1 56  ? -19.006 7.030   4.674   1.00 15.72 ? 56  SER A N   1 
ATOM   441  C  CA  . SER A 1 56  ? -17.743 6.434   4.298   1.00 17.96 ? 56  SER A CA  1 
ATOM   442  C  C   . SER A 1 56  ? -17.241 7.138   3.041   1.00 17.97 ? 56  SER A C   1 
ATOM   443  O  O   . SER A 1 56  ? -18.038 7.634   2.218   1.00 19.01 ? 56  SER A O   1 
ATOM   444  C  CB  . SER A 1 56  ? -17.893 4.923   4.111   1.00 17.37 ? 56  SER A CB  1 
ATOM   445  O  OG  . SER A 1 56  ? -18.769 4.622   3.010   1.00 19.61 ? 56  SER A OG  1 
ATOM   446  N  N   . LEU A 1 57  ? -15.932 7.254   2.926   1.00 18.63 ? 57  LEU A N   1 
ATOM   447  C  CA  . LEU A 1 57  ? -15.396 7.903   1.737   1.00 19.16 ? 57  LEU A CA  1 
ATOM   448  C  C   . LEU A 1 57  ? -14.562 6.956   0.887   1.00 20.31 ? 57  LEU A C   1 
ATOM   449  O  O   . LEU A 1 57  ? -14.701 6.957   -0.351  1.00 20.00 ? 57  LEU A O   1 
ATOM   450  C  CB  . LEU A 1 57  ? -14.531 9.079   2.175   1.00 19.99 ? 57  LEU A CB  1 
ATOM   451  C  CG  . LEU A 1 57  ? -15.320 10.207  2.839   1.00 22.81 ? 57  LEU A CG  1 
ATOM   452  C  CD1 . LEU A 1 57  ? -14.361 11.267  3.346   1.00 20.77 ? 57  LEU A CD1 1 
ATOM   453  C  CD2 . LEU A 1 57  ? -16.368 10.798  1.888   1.00 26.73 ? 57  LEU A CD2 1 
ATOM   454  N  N   A ARG A 1 58  ? -13.797 6.092   1.536   0.50 19.06 ? 58  ARG A N   1 
ATOM   455  N  N   B ARG A 1 58  ? -13.552 6.308   1.516   0.50 18.19 ? 58  ARG A N   1 
ATOM   456  C  CA  A ARG A 1 58  ? -12.787 5.417   0.765   0.50 19.69 ? 58  ARG A CA  1 
ATOM   457  C  CA  B ARG A 1 58  ? -12.441 5.649   0.830   0.50 18.80 ? 58  ARG A CA  1 
ATOM   458  C  C   A ARG A 1 58  ? -12.337 4.206   1.555   0.50 19.86 ? 58  ARG A C   1 
ATOM   459  C  C   B ARG A 1 58  ? -11.915 4.460   1.644   0.50 18.68 ? 58  ARG A C   1 
ATOM   460  O  O   A ARG A 1 58  ? -12.749 4.074   2.707   0.50 17.00 ? 58  ARG A O   1 
ATOM   461  O  O   B ARG A 1 58  ? -11.974 4.472   2.880   0.50 15.89 ? 58  ARG A O   1 
ATOM   462  C  CB  A ARG A 1 58  ? -11.600 6.371   0.694   0.50 20.49 ? 58  ARG A CB  1 
ATOM   463  C  CB  B ARG A 1 58  ? -11.258 6.603   0.603   0.50 18.62 ? 58  ARG A CB  1 
ATOM   464  C  CG  A ARG A 1 58  ? -10.700 6.144   -0.500  0.50 20.35 ? 58  ARG A CG  1 
ATOM   465  C  CG  B ARG A 1 58  ? -11.428 7.593   -0.542  0.50 18.58 ? 58  ARG A CG  1 
ATOM   466  C  CD  A ARG A 1 58  ? -9.820  7.368   -0.470  0.50 21.14 ? 58  ARG A CD  1 
ATOM   467  C  CD  B ARG A 1 58  ? -10.147 8.313   -0.924  0.50 17.85 ? 58  ARG A CD  1 
ATOM   468  N  NE  A ARG A 1 58  ? -9.067  7.284   0.760   0.50 19.40 ? 58  ARG A NE  1 
ATOM   469  N  NE  B ARG A 1 58  ? -9.324  7.439   -1.754  0.50 16.82 ? 58  ARG A NE  1 
ATOM   470  C  CZ  A ARG A 1 58  ? -7.751  7.299   0.762   0.50 19.43 ? 58  ARG A CZ  1 
ATOM   471  C  CZ  B ARG A 1 58  ? -9.491  7.295   -3.065  0.50 16.11 ? 58  ARG A CZ  1 
ATOM   472  N  NH1 A ARG A 1 58  ? -7.129  7.460   -0.390  0.50 18.96 ? 58  ARG A NH1 1 
ATOM   473  N  NH1 B ARG A 1 58  ? -10.453 7.956   -3.688  0.50 17.23 ? 58  ARG A NH1 1 
ATOM   474  N  NH2 A ARG A 1 58  ? -7.082  7.239   1.898   0.50 19.41 ? 58  ARG A NH2 1 
ATOM   475  N  NH2 B ARG A 1 58  ? -8.696  6.494   -3.743  0.50 15.67 ? 58  ARG A NH2 1 
ATOM   476  N  N   . ILE A 1 59  ? -11.452 3.425   0.917   1.00 19.68 ? 59  ILE A N   1 
ATOM   477  C  CA  . ILE A 1 59  ? -10.802 2.250   1.491   1.00 19.28 ? 59  ILE A CA  1 
ATOM   478  C  C   . ILE A 1 59  ? -9.382  2.170   0.953   1.00 20.87 ? 59  ILE A C   1 
ATOM   479  O  O   . ILE A 1 59  ? -9.125  2.356   -0.245  1.00 19.83 ? 59  ILE A O   1 
ATOM   480  C  CB  . ILE A 1 59  ? -11.589 0.940   1.259   1.00 17.48 ? 59  ILE A CB  1 
ATOM   481  C  CG1 . ILE A 1 59  ? -11.146 -0.180  2.214   1.00 17.75 ? 59  ILE A CG1 1 
ATOM   482  C  CG2 . ILE A 1 59  ? -11.484 0.508   -0.218  1.00 17.83 ? 59  ILE A CG2 1 
ATOM   483  C  CD1 . ILE A 1 59  ? -11.911 -1.494  2.033   1.00 18.18 ? 59  ILE A CD1 1 
ATOM   484  N  N   . LEU A 1 60  ? -8.441  1.886   1.856   1.00 19.07 ? 60  LEU A N   1 
ATOM   485  C  CA  . LEU A 1 60  ? -7.036  1.941   1.540   1.00 19.84 ? 60  LEU A CA  1 
ATOM   486  C  C   . LEU A 1 60  ? -6.297  0.766   2.182   1.00 20.71 ? 60  LEU A C   1 
ATOM   487  O  O   . LEU A 1 60  ? -6.459  0.494   3.385   1.00 20.40 ? 60  LEU A O   1 
ATOM   488  C  CB  . LEU A 1 60  ? -6.536  3.280   2.095   1.00 23.75 ? 60  LEU A CB  1 
ATOM   489  C  CG  . LEU A 1 60  ? -5.032  3.417   2.285   1.00 25.11 ? 60  LEU A CG  1 
ATOM   490  C  CD1 . LEU A 1 60  ? -4.310  3.496   0.939   1.00 26.65 ? 60  LEU A CD1 1 
ATOM   491  C  CD2 . LEU A 1 60  ? -4.734  4.647   3.136   1.00 24.13 ? 60  LEU A CD2 1 
ATOM   492  N  N   . ASN A 1 61  ? -5.457  0.100   1.380   1.00 17.04 ? 61  ASN A N   1 
ATOM   493  C  CA  . ASN A 1 61  ? -4.418  -0.805  1.867   1.00 18.18 ? 61  ASN A CA  1 
ATOM   494  C  C   . ASN A 1 61  ? -3.157  -0.006  2.214   1.00 19.10 ? 61  ASN A C   1 
ATOM   495  O  O   . ASN A 1 61  ? -2.441  0.425   1.313   1.00 18.41 ? 61  ASN A O   1 
ATOM   496  C  CB  . ASN A 1 61  ? -4.086  -1.876  0.822   1.00 16.08 ? 61  ASN A CB  1 
ATOM   497  C  CG  . ASN A 1 61  ? -3.086  -2.932  1.226   1.00 18.81 ? 61  ASN A CG  1 
ATOM   498  O  OD1 . ASN A 1 61  ? -2.168  -2.706  2.039   1.00 17.42 ? 61  ASN A OD1 1 
ATOM   499  N  ND2 . ASN A 1 61  ? -3.211  -4.109  0.616   1.00 15.86 ? 61  ASN A ND2 1 
ATOM   500  N  N   . ASN A 1 62  ? -2.816  0.099   3.514   1.00 17.25 ? 62  ASN A N   1 
ATOM   501  C  CA  . ASN A 1 62  ? -1.680  0.920   3.938   1.00 18.21 ? 62  ASN A CA  1 
ATOM   502  C  C   . ASN A 1 62  ? -0.459  0.031   4.193   1.00 19.24 ? 62  ASN A C   1 
ATOM   503  O  O   . ASN A 1 62  ? 0.566   0.457   4.766   1.00 20.29 ? 62  ASN A O   1 
ATOM   504  C  CB  . ASN A 1 62  ? -1.987  1.718   5.205   1.00 18.03 ? 62  ASN A CB  1 
ATOM   505  C  CG  . ASN A 1 62  ? -2.558  0.850   6.312   1.00 17.63 ? 62  ASN A CG  1 
ATOM   506  O  OD1 . ASN A 1 62  ? -2.198  -0.305  6.433   1.00 16.40 ? 62  ASN A OD1 1 
ATOM   507  N  ND2 . ASN A 1 62  ? -3.456  1.410   7.105   1.00 21.27 ? 62  ASN A ND2 1 
ATOM   508  N  N   . GLY A 1 63  ? -0.567  -1.227  3.757   1.00 17.18 ? 63  GLY A N   1 
ATOM   509  C  CA  . GLY A 1 63  ? 0.468   -2.214  3.928   1.00 17.22 ? 63  GLY A CA  1 
ATOM   510  C  C   . GLY A 1 63  ? 0.571   -2.805  5.338   1.00 15.25 ? 63  GLY A C   1 
ATOM   511  O  O   . GLY A 1 63  ? 1.480   -3.589  5.575   1.00 16.69 ? 63  GLY A O   1 
ATOM   512  N  N   . HIS A 1 64  ? -0.366  -2.440  6.234   1.00 16.59 ? 64  HIS A N   1 
ATOM   513  C  CA  . HIS A 1 64  ? -0.497  -3.076  7.551   1.00 15.56 ? 64  HIS A CA  1 
ATOM   514  C  C   . HIS A 1 64  ? -1.886  -3.697  7.708   1.00 14.53 ? 64  HIS A C   1 
ATOM   515  O  O   . HIS A 1 64  ? -2.029  -4.823  8.200   1.00 16.83 ? 64  HIS A O   1 
ATOM   516  C  CB  . HIS A 1 64  ? -0.298  -2.055  8.659   1.00 14.84 ? 64  HIS A CB  1 
ATOM   517  C  CG  . HIS A 1 64  ? 0.960   -1.262  8.474   1.00 15.31 ? 64  HIS A CG  1 
ATOM   518  N  ND1 . HIS A 1 64  ? 2.215   -1.839  8.628   1.00 17.78 ? 64  HIS A ND1 1 
ATOM   519  C  CD2 . HIS A 1 64  ? 1.152   0.029   8.156   1.00 17.82 ? 64  HIS A CD2 1 
ATOM   520  C  CE1 . HIS A 1 64  ? 3.129   -0.917  8.409   1.00 16.93 ? 64  HIS A CE1 1 
ATOM   521  N  NE2 . HIS A 1 64  ? 2.508   0.215   8.119   1.00 17.19 ? 64  HIS A NE2 1 
ATOM   522  N  N   . ALA A 1 65  ? -2.893  -2.971  7.273   1.00 13.77 ? 65  ALA A N   1 
ATOM   523  C  CA  . ALA A 1 65  ? -4.264  -3.460  7.196   1.00 15.10 ? 65  ALA A CA  1 
ATOM   524  C  C   . ALA A 1 65  ? -4.998  -2.675  6.094   1.00 13.95 ? 65  ALA A C   1 
ATOM   525  O  O   . ALA A 1 65  ? -4.321  -2.034  5.286   1.00 16.91 ? 65  ALA A O   1 
ATOM   526  C  CB  . ALA A 1 65  ? -4.925  -3.377  8.580   1.00 14.42 ? 65  ALA A CB  1 
ATOM   527  N  N   . PHE A 1 66  ? -6.346  -2.697  6.070   1.00 14.17 ? 66  PHE A N   1 
ATOM   528  C  CA  . PHE A 1 66  ? -7.131  -1.796  5.228   1.00 15.64 ? 66  PHE A CA  1 
ATOM   529  C  C   . PHE A 1 66  ? -7.993  -0.927  6.136   1.00 15.87 ? 66  PHE A C   1 
ATOM   530  O  O   . PHE A 1 66  ? -8.601  -1.425  7.094   1.00 14.67 ? 66  PHE A O   1 
ATOM   531  C  CB  . PHE A 1 66  ? -7.928  -2.528  4.123   1.00 14.25 ? 66  PHE A CB  1 
ATOM   532  C  CG  . PHE A 1 66  ? -8.990  -3.488  4.590   1.00 13.30 ? 66  PHE A CG  1 
ATOM   533  C  CD1 . PHE A 1 66  ? -10.275 -3.024  4.907   1.00 13.80 ? 66  PHE A CD1 1 
ATOM   534  C  CD2 . PHE A 1 66  ? -8.718  -4.849  4.754   1.00 14.15 ? 66  PHE A CD2 1 
ATOM   535  C  CE1 . PHE A 1 66  ? -11.256 -3.884  5.373   1.00 15.49 ? 66  PHE A CE1 1 
ATOM   536  C  CE2 . PHE A 1 66  ? -9.701  -5.699  5.256   1.00 13.96 ? 66  PHE A CE2 1 
ATOM   537  C  CZ  . PHE A 1 66  ? -10.971 -5.232  5.539   1.00 14.01 ? 66  PHE A CZ  1 
ATOM   538  N  N   . ASN A 1 67  ? -7.989  0.379   5.849   1.00 16.61 ? 67  ASN A N   1 
ATOM   539  C  CA  . ASN A 1 67  ? -8.786  1.333   6.601   1.00 17.94 ? 67  ASN A CA  1 
ATOM   540  C  C   . ASN A 1 67  ? -9.952  1.775   5.749   1.00 17.75 ? 67  ASN A C   1 
ATOM   541  O  O   . ASN A 1 67  ? -9.721  2.218   4.616   1.00 21.04 ? 67  ASN A O   1 
ATOM   542  C  CB  . ASN A 1 67  ? -7.985  2.586   6.974   1.00 19.38 ? 67  ASN A CB  1 
ATOM   543  C  CG  . ASN A 1 67  ? -6.994  2.345   8.091   1.00 21.37 ? 67  ASN A CG  1 
ATOM   544  O  OD1 . ASN A 1 67  ? -6.959  1.255   8.656   1.00 21.86 ? 67  ASN A OD1 1 
ATOM   545  N  ND2 . ASN A 1 67  ? -6.149  3.326   8.375   1.00 22.27 ? 67  ASN A ND2 1 
ATOM   546  N  N   . VAL A 1 68  ? -11.166 1.650   6.283   1.00 17.92 ? 68  VAL A N   1 
ATOM   547  C  CA  . VAL A 1 68  ? -12.282 2.388   5.724   1.00 17.72 ? 68  VAL A CA  1 
ATOM   548  C  C   . VAL A 1 68  ? -12.354 3.735   6.445   1.00 19.14 ? 68  VAL A C   1 
ATOM   549  O  O   . VAL A 1 68  ? -12.582 3.765   7.653   1.00 17.80 ? 68  VAL A O   1 
ATOM   550  C  CB  . VAL A 1 68  ? -13.599 1.600   5.842   1.00 19.07 ? 68  VAL A CB  1 
ATOM   551  C  CG1 . VAL A 1 68  ? -14.808 2.414   5.381   1.00 19.12 ? 68  VAL A CG1 1 
ATOM   552  C  CG2 . VAL A 1 68  ? -13.517 0.282   5.078   1.00 18.55 ? 68  VAL A CG2 1 
ATOM   553  N  N   A GLU A 1 69  ? -12.315 4.808   5.655   0.50 19.78 ? 69  GLU A N   1 
ATOM   554  N  N   B GLU A 1 69  ? -12.110 4.848   5.729   0.50 19.35 ? 69  GLU A N   1 
ATOM   555  C  CA  A GLU A 1 69  ? -12.267 6.170   6.153   0.50 19.72 ? 69  GLU A CA  1 
ATOM   556  C  CA  B GLU A 1 69  ? -12.081 6.198   6.298   0.50 19.07 ? 69  GLU A CA  1 
ATOM   557  C  C   A GLU A 1 69  ? -13.639 6.813   6.011   0.50 19.42 ? 69  GLU A C   1 
ATOM   558  C  C   B GLU A 1 69  ? -13.356 6.969   5.949   0.50 18.23 ? 69  GLU A C   1 
ATOM   559  O  O   A GLU A 1 69  ? -14.424 6.494   5.108   0.50 19.58 ? 69  GLU A O   1 
ATOM   560  O  O   B GLU A 1 69  ? -13.781 6.880   4.793   0.50 16.33 ? 69  GLU A O   1 
ATOM   561  C  CB  A GLU A 1 69  ? -11.159 6.924   5.423   0.50 20.74 ? 69  GLU A CB  1 
ATOM   562  C  CB  B GLU A 1 69  ? -10.855 6.972   5.791   0.50 19.89 ? 69  GLU A CB  1 
ATOM   563  C  CG  A GLU A 1 69  ? -10.076 5.948   5.037   0.50 22.96 ? 69  GLU A CG  1 
ATOM   564  C  CG  B GLU A 1 69  ? -9.548  6.453   6.370   0.50 22.96 ? 69  GLU A CG  1 
ATOM   565  C  CD  A GLU A 1 69  ? -8.770  6.406   4.421   0.50 24.92 ? 69  GLU A CD  1 
ATOM   566  C  CD  B GLU A 1 69  ? -8.291  7.279   6.150   0.50 22.68 ? 69  GLU A CD  1 
ATOM   567  O  OE1 A GLU A 1 69  ? -8.386  5.826   3.378   0.50 23.71 ? 69  GLU A OE1 1 
ATOM   568  O  OE1 B GLU A 1 69  ? -7.476  6.866   5.290   0.50 27.56 ? 69  GLU A OE1 1 
ATOM   569  O  OE2 A GLU A 1 69  ? -8.099  7.246   5.051   0.50 29.34 ? 69  GLU A OE2 1 
ATOM   570  O  OE2 B GLU A 1 69  ? -8.102  8.299   6.855   0.50 24.42 ? 69  GLU A OE2 1 
ATOM   571  N  N   . PHE A 1 70  ? -13.904 7.726   6.936   1.00 16.79 ? 70  PHE A N   1 
ATOM   572  C  CA  . PHE A 1 70  ? -15.207 8.382   6.982   1.00 16.65 ? 70  PHE A CA  1 
ATOM   573  C  C   . PHE A 1 70  ? -15.021 9.897   6.995   1.00 16.49 ? 70  PHE A C   1 
ATOM   574  O  O   . PHE A 1 70  ? -13.974 10.379  7.386   1.00 18.23 ? 70  PHE A O   1 
ATOM   575  C  CB  . PHE A 1 70  ? -15.968 7.986   8.257   1.00 14.04 ? 70  PHE A CB  1 
ATOM   576  C  CG  . PHE A 1 70  ? -16.568 6.594   8.201   1.00 14.39 ? 70  PHE A CG  1 
ATOM   577  C  CD1 . PHE A 1 70  ? -15.777 5.467   8.381   1.00 14.65 ? 70  PHE A CD1 1 
ATOM   578  C  CD2 . PHE A 1 70  ? -17.905 6.408   7.922   1.00 13.90 ? 70  PHE A CD2 1 
ATOM   579  C  CE1 . PHE A 1 70  ? -16.305 4.182   8.290   1.00 14.33 ? 70  PHE A CE1 1 
ATOM   580  C  CE2 . PHE A 1 70  ? -18.456 5.132   7.840   1.00 14.23 ? 70  PHE A CE2 1 
ATOM   581  C  CZ  . PHE A 1 70  ? -17.650 4.024   8.018   1.00 14.56 ? 70  PHE A CZ  1 
ATOM   582  N  N   . ASP A 1 71  ? -16.040 10.624  6.553   1.00 17.52 ? 71  ASP A N   1 
ATOM   583  C  CA  . ASP A 1 71  ? -16.015 12.073  6.676   1.00 16.91 ? 71  ASP A CA  1 
ATOM   584  C  C   . ASP A 1 71  ? -16.341 12.419  8.129   1.00 17.01 ? 71  ASP A C   1 
ATOM   585  O  O   . ASP A 1 71  ? -17.452 12.194  8.609   1.00 19.70 ? 71  ASP A O   1 
ATOM   586  C  CB  . ASP A 1 71  ? -16.951 12.726  5.658   1.00 19.75 ? 71  ASP A CB  1 
ATOM   587  C  CG  . ASP A 1 71  ? -17.378 14.129  6.055   1.00 22.65 ? 71  ASP A CG  1 
ATOM   588  O  OD1 . ASP A 1 71  ? -16.563 14.837  6.672   1.00 20.74 ? 71  ASP A OD1 1 
ATOM   589  O  OD2 . ASP A 1 71  ? -18.543 14.500  5.786   1.00 25.64 ? 71  ASP A OD2 1 
ATOM   590  N  N   . ASP A 1 72  ? -15.352 12.961  8.834   1.00 15.66 ? 72  ASP A N   1 
ATOM   591  C  CA  . ASP A 1 72  ? -15.473 13.295  10.246  1.00 14.77 ? 72  ASP A CA  1 
ATOM   592  C  C   . ASP A 1 72  ? -15.475 14.817  10.439  1.00 15.83 ? 72  ASP A C   1 
ATOM   593  O  O   . ASP A 1 72  ? -15.063 15.303  11.491  1.00 16.63 ? 72  ASP A O   1 
ATOM   594  C  CB  . ASP A 1 72  ? -14.328 12.620  11.008  1.00 15.59 ? 72  ASP A CB  1 
ATOM   595  C  CG  . ASP A 1 72  ? -12.964 13.140  10.621  1.00 16.77 ? 72  ASP A CG  1 
ATOM   596  O  OD1 . ASP A 1 72  ? -12.829 13.838  9.563   1.00 18.84 ? 72  ASP A OD1 1 
ATOM   597  O  OD2 . ASP A 1 72  ? -12.028 12.860  11.363  1.00 17.59 ? 72  ASP A OD2 1 
ATOM   598  N  N   . SER A 1 73  ? -15.987 15.544  9.441   1.00 17.96 ? 73  SER A N   1 
ATOM   599  C  CA  . SER A 1 73  ? -15.950 17.011  9.491   1.00 18.63 ? 73  SER A CA  1 
ATOM   600  C  C   . SER A 1 73  ? -17.240 17.570  10.097  1.00 20.46 ? 73  SER A C   1 
ATOM   601  O  O   . SER A 1 73  ? -17.378 18.789  10.250  1.00 18.85 ? 73  SER A O   1 
ATOM   602  C  CB  . SER A 1 73  ? -15.651 17.581  8.112   1.00 19.63 ? 73  SER A CB  1 
ATOM   603  O  OG  . SER A 1 73  ? -16.771 17.408  7.262   1.00 20.09 ? 73  SER A OG  1 
ATOM   604  N  N   . GLN A 1 74  ? -18.137 16.666  10.535  1.00 20.63 ? 74  GLN A N   1 
ATOM   605  C  CA  . GLN A 1 74  ? -19.368 17.027  11.216  1.00 23.13 ? 74  GLN A CA  1 
ATOM   606  C  C   . GLN A 1 74  ? -19.756 15.887  12.141  1.00 24.96 ? 74  GLN A C   1 
ATOM   607  O  O   . GLN A 1 74  ? -19.237 14.788  11.966  1.00 23.54 ? 74  GLN A O   1 
ATOM   608  C  CB  . GLN A 1 74  ? -20.520 17.182  10.218  1.00 26.77 ? 74  GLN A CB  1 
ATOM   609  C  CG  . GLN A 1 74  ? -20.367 18.360  9.270   1.00 27.63 ? 74  GLN A CG  1 
ATOM   610  C  CD  . GLN A 1 74  ? -21.659 18.524  8.508   1.00 32.79 ? 74  GLN A CD  1 
ATOM   611  O  OE1 . GLN A 1 74  ? -22.628 19.099  9.016   1.00 40.32 ? 74  GLN A OE1 1 
ATOM   612  N  NE2 . GLN A 1 74  ? -21.697 17.970  7.305   1.00 32.25 ? 74  GLN A NE2 1 
ATOM   613  N  N   . ASP A 1 75  ? -20.658 16.147  13.098  1.00 25.50 ? 75  ASP A N   1 
ATOM   614  C  CA  . ASP A 1 75  ? -21.065 15.109  14.035  1.00 31.62 ? 75  ASP A CA  1 
ATOM   615  C  C   . ASP A 1 75  ? -22.109 14.235  13.351  1.00 30.96 ? 75  ASP A C   1 
ATOM   616  O  O   . ASP A 1 75  ? -23.290 14.565  13.384  1.00 33.02 ? 75  ASP A O   1 
ATOM   617  C  CB  . ASP A 1 75  ? -21.685 15.655  15.329  1.00 38.96 ? 75  ASP A CB  1 
ATOM   618  C  CG  . ASP A 1 75  ? -20.697 16.186  16.361  1.00 42.07 ? 75  ASP A CG  1 
ATOM   619  O  OD1 . ASP A 1 75  ? -19.589 15.622  16.470  1.00 39.57 ? 75  ASP A OD1 1 
ATOM   620  O  OD2 . ASP A 1 75  ? -21.053 17.167  17.056  1.00 45.86 ? 75  ASP A OD2 1 
ATOM   621  N  N   . LYS A 1 76  ? -21.657 13.147  12.724  1.00 27.80 ? 76  LYS A N   1 
ATOM   622  C  CA  . LYS A 1 76  ? -22.512 12.337  11.874  1.00 27.39 ? 76  LYS A CA  1 
ATOM   623  C  C   . LYS A 1 76  ? -22.527 10.878  12.319  1.00 28.40 ? 76  LYS A C   1 
ATOM   624  O  O   . LYS A 1 76  ? -23.527 10.180  12.147  1.00 35.10 ? 76  LYS A O   1 
ATOM   625  C  CB  . LYS A 1 76  ? -22.002 12.369  10.438  1.00 27.83 ? 76  LYS A CB  1 
ATOM   626  C  CG  . LYS A 1 76  ? -22.620 13.466  9.582   1.00 29.52 ? 76  LYS A CG  1 
ATOM   627  C  CD  . LYS A 1 76  ? -21.775 13.687  8.364   1.00 30.84 ? 76  LYS A CD  1 
ATOM   628  C  CE  . LYS A 1 76  ? -22.536 13.980  7.090   1.00 32.32 ? 76  LYS A CE  1 
ATOM   629  N  NZ  . LYS A 1 76  ? -21.574 13.982  5.964   1.00 28.33 ? 76  LYS A NZ  1 
ATOM   630  N  N   . ALA A 1 77  ? -21.374 10.399  12.764  1.00 22.66 ? 77  ALA A N   1 
ATOM   631  C  CA  . ALA A 1 77  ? -21.207 9.043   13.280  1.00 19.76 ? 77  ALA A CA  1 
ATOM   632  C  C   . ALA A 1 77  ? -20.458 9.177   14.601  1.00 18.98 ? 77  ALA A C   1 
ATOM   633  O  O   . ALA A 1 77  ? -19.246 9.428   14.581  1.00 22.12 ? 77  ALA A O   1 
ATOM   634  C  CB  . ALA A 1 77  ? -20.349 8.291   12.307  1.00 20.91 ? 77  ALA A CB  1 
ATOM   635  N  N   . VAL A 1 78  ? -21.179 9.114   15.724  1.00 17.92 ? 78  VAL A N   1 
ATOM   636  C  CA  . VAL A 1 78  ? -20.565 9.435   17.009  1.00 18.80 ? 78  VAL A CA  1 
ATOM   637  C  C   . VAL A 1 78  ? -20.793 8.334   18.042  1.00 18.05 ? 78  VAL A C   1 
ATOM   638  O  O   . VAL A 1 78  ? -21.831 7.669   18.067  1.00 18.32 ? 78  VAL A O   1 
ATOM   639  C  CB  . VAL A 1 78  ? -21.005 10.807  17.567  1.00 21.77 ? 78  VAL A CB  1 
ATOM   640  C  CG1 . VAL A 1 78  ? -20.810 11.924  16.557  1.00 23.02 ? 78  VAL A CG1 1 
ATOM   641  C  CG2 . VAL A 1 78  ? -22.442 10.763  18.062  1.00 22.57 ? 78  VAL A CG2 1 
ATOM   642  N  N   . LEU A 1 79  ? -19.784 8.190   18.921  1.00 16.58 ? 79  LEU A N   1 
ATOM   643  C  CA  . LEU A 1 79  ? -19.829 7.355   20.105  1.00 17.45 ? 79  LEU A CA  1 
ATOM   644  C  C   . LEU A 1 79  ? -19.846 8.279   21.318  1.00 16.23 ? 79  LEU A C   1 
ATOM   645  O  O   . LEU A 1 79  ? -19.148 9.298   21.353  1.00 14.99 ? 79  LEU A O   1 
ATOM   646  C  CB  . LEU A 1 79  ? -18.560 6.490   20.071  1.00 16.23 ? 79  LEU A CB  1 
ATOM   647  C  CG  . LEU A 1 79  ? -18.422 5.358   21.074  1.00 17.81 ? 79  LEU A CG  1 
ATOM   648  C  CD1 . LEU A 1 79  ? -19.488 4.306   20.808  1.00 18.69 ? 79  LEU A CD1 1 
ATOM   649  C  CD2 . LEU A 1 79  ? -17.035 4.734   20.943  1.00 16.33 ? 79  LEU A CD2 1 
ATOM   650  N  N   . LYS A 1 80  ? -20.712 7.959   22.269  1.00 17.64 ? 80  LYS A N   1 
ATOM   651  C  CA  . LYS A 1 80  ? -20.712 8.654   23.549  1.00 20.47 ? 80  LYS A CA  1 
ATOM   652  C  C   . LYS A 1 80  ? -21.311 7.746   24.618  1.00 18.77 ? 80  LYS A C   1 
ATOM   653  O  O   . LYS A 1 80  ? -21.566 6.577   24.353  1.00 17.05 ? 80  LYS A O   1 
ATOM   654  C  CB  . LYS A 1 80  ? -21.400 10.023  23.478  1.00 24.37 ? 80  LYS A CB  1 
ATOM   655  C  CG  . LYS A 1 80  ? -22.884 9.978   23.135  1.00 29.42 ? 80  LYS A CG  1 
ATOM   656  C  CD  . LYS A 1 80  ? -23.550 11.335  22.817  1.00 33.84 ? 80  LYS A CD  1 
ATOM   657  C  CE  . LYS A 1 80  ? -23.008 12.024  21.574  1.00 41.76 ? 80  LYS A CE  1 
ATOM   658  N  NZ  . LYS A 1 80  ? -24.040 12.774  20.802  1.00 44.55 ? 80  LYS A NZ  1 
ATOM   659  N  N   . GLY A 1 81  ? -21.516 8.296   25.829  1.00 19.23 ? 81  GLY A N   1 
ATOM   660  C  CA  . GLY A 1 81  ? -22.015 7.480   26.915  1.00 20.61 ? 81  GLY A CA  1 
ATOM   661  C  C   . GLY A 1 81  ? -21.008 6.393   27.255  1.00 22.18 ? 81  GLY A C   1 
ATOM   662  O  O   . GLY A 1 81  ? -19.814 6.609   27.098  1.00 18.29 ? 81  GLY A O   1 
ATOM   663  N  N   . GLY A 1 82  ? -21.482 5.225   27.685  1.00 23.91 ? 82  GLY A N   1 
ATOM   664  C  CA  . GLY A 1 82  ? -20.547 4.215   28.155  1.00 23.99 ? 82  GLY A CA  1 
ATOM   665  C  C   . GLY A 1 82  ? -19.584 4.785   29.203  1.00 22.13 ? 82  GLY A C   1 
ATOM   666  O  O   . GLY A 1 82  ? -20.024 5.433   30.151  1.00 26.82 ? 82  GLY A O   1 
ATOM   667  N  N   . PRO A 1 83  ? -18.239 4.604   29.103  1.00 19.20 ? 83  PRO A N   1 
ATOM   668  C  CA  . PRO A 1 83  ? -17.344 5.249   30.063  1.00 17.57 ? 83  PRO A CA  1 
ATOM   669  C  C   . PRO A 1 83  ? -16.931 6.678   29.699  1.00 19.68 ? 83  PRO A C   1 
ATOM   670  O  O   . PRO A 1 83  ? -16.164 7.328   30.415  1.00 23.40 ? 83  PRO A O   1 
ATOM   671  C  CB  . PRO A 1 83  ? -16.117 4.304   29.988  1.00 18.49 ? 83  PRO A CB  1 
ATOM   672  C  CG  . PRO A 1 83  ? -16.067 3.985   28.494  1.00 15.00 ? 83  PRO A CG  1 
ATOM   673  C  CD  . PRO A 1 83  ? -17.527 3.749   28.119  1.00 17.75 ? 83  PRO A CD  1 
ATOM   674  N  N   . LEU A 1 84  ? -17.449 7.201   28.592  1.00 19.94 ? 84  LEU A N   1 
ATOM   675  C  CA  . LEU A 1 84  ? -16.863 8.399   28.014  1.00 19.58 ? 84  LEU A CA  1 
ATOM   676  C  C   . LEU A 1 84  ? -17.535 9.638   28.591  1.00 23.32 ? 84  LEU A C   1 
ATOM   677  O  O   . LEU A 1 84  ? -18.720 9.584   28.908  1.00 22.56 ? 84  LEU A O   1 
ATOM   678  C  CB  . LEU A 1 84  ? -16.997 8.371   26.484  1.00 17.96 ? 84  LEU A CB  1 
ATOM   679  C  CG  . LEU A 1 84  ? -16.508 7.082   25.823  1.00 16.74 ? 84  LEU A CG  1 
ATOM   680  C  CD1 . LEU A 1 84  ? -16.949 7.006   24.371  1.00 16.81 ? 84  LEU A CD1 1 
ATOM   681  C  CD2 . LEU A 1 84  ? -14.967 6.967   25.941  1.00 17.81 ? 84  LEU A CD2 1 
ATOM   682  N  N   . ASP A 1 85  ? -16.759 10.729  28.661  1.00 25.76 ? 85  ASP A N   1 
ATOM   683  C  CA  . ASP A 1 85  ? -17.249 12.086  28.859  1.00 34.01 ? 85  ASP A CA  1 
ATOM   684  C  C   . ASP A 1 85  ? -17.245 12.783  27.501  1.00 37.92 ? 85  ASP A C   1 
ATOM   685  O  O   . ASP A 1 85  ? -16.202 12.926  26.862  1.00 40.95 ? 85  ASP A O   1 
ATOM   686  C  CB  . ASP A 1 85  ? -16.353 12.879  29.828  1.00 37.21 ? 85  ASP A CB  1 
ATOM   687  C  CG  . ASP A 1 85  ? -16.416 12.443  31.286  1.00 46.55 ? 85  ASP A CG  1 
ATOM   688  O  OD1 . ASP A 1 85  ? -17.549 12.188  31.785  1.00 42.56 ? 85  ASP A OD1 1 
ATOM   689  O  OD2 . ASP A 1 85  ? -15.326 12.370  31.923  1.00 47.46 ? 85  ASP A OD2 1 
ATOM   690  N  N   . GLY A 1 86  ? -18.414 13.226  27.047  1.00 38.39 ? 86  GLY A N   1 
ATOM   691  C  CA  . GLY A 1 86  ? -18.458 13.899  25.761  1.00 35.30 ? 86  GLY A CA  1 
ATOM   692  C  C   . GLY A 1 86  ? -18.402 12.934  24.574  1.00 34.22 ? 86  GLY A C   1 
ATOM   693  O  O   . GLY A 1 86  ? -18.579 11.726  24.718  1.00 32.19 ? 86  GLY A O   1 
ATOM   694  N  N   . THR A 1 87  ? -18.073 13.502  23.410  1.00 29.48 ? 87  THR A N   1 
ATOM   695  C  CA  . THR A 1 87  ? -18.501 13.000  22.116  1.00 24.60 ? 87  THR A CA  1 
ATOM   696  C  C   . THR A 1 87  ? -17.289 12.672  21.270  1.00 20.06 ? 87  THR A C   1 
ATOM   697  O  O   . THR A 1 87  ? -16.385 13.488  21.137  1.00 18.12 ? 87  THR A O   1 
ATOM   698  C  CB  . THR A 1 87  ? -19.275 14.102  21.382  1.00 28.74 ? 87  THR A CB  1 
ATOM   699  O  OG1 . THR A 1 87  ? -20.443 14.185  22.197  1.00 35.98 ? 87  THR A OG1 1 
ATOM   700  C  CG2 . THR A 1 87  ? -19.648 13.732  19.957  1.00 29.08 ? 87  THR A CG2 1 
ATOM   701  N  N   . TYR A 1 88  ? -17.271 11.445  20.742  1.00 18.31 ? 88  TYR A N   1 
ATOM   702  C  CA  . TYR A 1 88  ? -16.179 11.011  19.890  1.00 14.92 ? 88  TYR A CA  1 
ATOM   703  C  C   . TYR A 1 88  ? -16.702 10.713  18.480  1.00 14.59 ? 88  TYR A C   1 
ATOM   704  O  O   . TYR A 1 88  ? -17.704 10.002  18.302  1.00 18.68 ? 88  TYR A O   1 
ATOM   705  C  CB  . TYR A 1 88  ? -15.543 9.754   20.505  1.00 12.26 ? 88  TYR A CB  1 
ATOM   706  C  CG  . TYR A 1 88  ? -14.819 9.930   21.828  1.00 13.43 ? 88  TYR A CG  1 
ATOM   707  C  CD1 . TYR A 1 88  ? -15.503 10.248  22.998  1.00 14.20 ? 88  TYR A CD1 1 
ATOM   708  C  CD2 . TYR A 1 88  ? -13.433 9.844   21.880  1.00 13.21 ? 88  TYR A CD2 1 
ATOM   709  C  CE1 . TYR A 1 88  ? -14.821 10.459  24.196  1.00 14.22 ? 88  TYR A CE1 1 
ATOM   710  C  CE2 . TYR A 1 88  ? -12.734 10.077  23.058  1.00 12.59 ? 88  TYR A CE2 1 
ATOM   711  C  CZ  . TYR A 1 88  ? -13.428 10.339  24.235  1.00 13.87 ? 88  TYR A CZ  1 
ATOM   712  O  OH  . TYR A 1 88  ? -12.727 10.493  25.390  1.00 13.49 ? 88  TYR A OH  1 
ATOM   713  N  N   . ARG A 1 89  ? -16.015 11.222  17.478  1.00 13.28 ? 89  ARG A N   1 
ATOM   714  C  CA  . ARG A 1 89  ? -16.444 11.041  16.095  1.00 15.44 ? 89  ARG A CA  1 
ATOM   715  C  C   . ARG A 1 89  ? -15.677 9.919   15.396  1.00 13.11 ? 89  ARG A C   1 
ATOM   716  O  O   . ARG A 1 89  ? -14.453 9.851   15.467  1.00 12.44 ? 89  ARG A O   1 
ATOM   717  C  CB  . ARG A 1 89  ? -16.031 12.261  15.283  1.00 18.00 ? 89  ARG A CB  1 
ATOM   718  C  CG  . ARG A 1 89  ? -17.060 13.364  15.364  1.00 20.40 ? 89  ARG A CG  1 
ATOM   719  C  CD  . ARG A 1 89  ? -16.740 14.357  14.267  1.00 21.48 ? 89  ARG A CD  1 
ATOM   720  N  NE  . ARG A 1 89  ? -17.483 15.512  14.718  1.00 25.74 ? 89  ARG A NE  1 
ATOM   721  C  CZ  . ARG A 1 89  ? -17.186 16.767  14.403  1.00 26.33 ? 89  ARG A CZ  1 
ATOM   722  N  NH1 . ARG A 1 89  ? -16.148 17.027  13.626  1.00 22.67 ? 89  ARG A NH1 1 
ATOM   723  N  NH2 . ARG A 1 89  ? -17.927 17.759  14.865  1.00 29.74 ? 89  ARG A NH2 1 
ATOM   724  N  N   . LEU A 1 90  ? -16.417 9.073   14.647  1.00 12.75 ? 90  LEU A N   1 
ATOM   725  C  CA  . LEU A 1 90  ? -15.793 7.996   13.887  1.00 11.73 ? 90  LEU A CA  1 
ATOM   726  C  C   . LEU A 1 90  ? -14.960 8.562   12.737  1.00 12.35 ? 90  LEU A C   1 
ATOM   727  O  O   . LEU A 1 90  ? -15.474 9.333   11.911  1.00 14.42 ? 90  LEU A O   1 
ATOM   728  C  CB  . LEU A 1 90  ? -16.916 7.113   13.331  1.00 12.46 ? 90  LEU A CB  1 
ATOM   729  C  CG  . LEU A 1 90  ? -16.472 5.989   12.403  1.00 12.54 ? 90  LEU A CG  1 
ATOM   730  C  CD1 . LEU A 1 90  ? -15.541 5.015   13.096  1.00 14.62 ? 90  LEU A CD1 1 
ATOM   731  C  CD2 . LEU A 1 90  ? -17.712 5.244   11.846  1.00 12.30 ? 90  LEU A CD2 1 
ATOM   732  N  N   . ILE A 1 91  ? -13.680 8.139   12.694  1.00 11.82 ? 91  ILE A N   1 
ATOM   733  C  CA  . ILE A 1 91  ? -12.768 8.527   11.616  1.00 12.77 ? 91  ILE A CA  1 
ATOM   734  C  C   . ILE A 1 91  ? -12.506 7.364   10.656  1.00 11.95 ? 91  ILE A C   1 
ATOM   735  O  O   . ILE A 1 91  ? -12.506 7.539   9.431   1.00 12.21 ? 91  ILE A O   1 
ATOM   736  C  CB  . ILE A 1 91  ? -11.463 9.234   12.085  1.00 12.48 ? 91  ILE A CB  1 
ATOM   737  C  CG1 . ILE A 1 91  ? -10.517 9.451   10.904  1.00 12.38 ? 91  ILE A CG1 1 
ATOM   738  C  CG2 . ILE A 1 91  ? -10.752 8.446   13.154  1.00 12.76 ? 91  ILE A CG2 1 
ATOM   739  C  CD1 . ILE A 1 91  ? -9.492  10.549  11.165  1.00 14.33 ? 91  ILE A CD1 1 
ATOM   740  N  N   . GLN A 1 92  ? -12.368 6.132   11.164  1.00 11.39 ? 92  GLN A N   1 
ATOM   741  C  CA  . GLN A 1 92  ? -12.013 4.997   10.316  1.00 12.47 ? 92  GLN A CA  1 
ATOM   742  C  C   . GLN A 1 92  ? -12.307 3.704   11.067  1.00 11.53 ? 92  GLN A C   1 
ATOM   743  O  O   . GLN A 1 92  ? -12.401 3.697   12.306  1.00 11.50 ? 92  GLN A O   1 
ATOM   744  C  CB  . GLN A 1 92  ? -10.540 5.010   9.861   1.00 13.10 ? 92  GLN A CB  1 
ATOM   745  C  CG  . GLN A 1 92  ? -9.532  5.014   11.006  1.00 12.76 ? 92  GLN A CG  1 
ATOM   746  C  CD  . GLN A 1 92  ? -8.789  3.710   11.154  1.00 13.39 ? 92  GLN A CD  1 
ATOM   747  O  OE1 . GLN A 1 92  ? -9.369  2.641   11.096  1.00 12.81 ? 92  GLN A OE1 1 
ATOM   748  N  NE2 . GLN A 1 92  ? -7.510  3.792   11.420  1.00 15.14 ? 92  GLN A NE2 1 
ATOM   749  N  N   . PHE A 1 93  ? -12.473 2.620   10.316  1.00 11.99 ? 93  PHE A N   1 
ATOM   750  C  CA  . PHE A 1 93  ? -12.345 1.299   10.917  1.00 11.34 ? 93  PHE A CA  1 
ATOM   751  C  C   . PHE A 1 93  ? -11.399 0.418   10.119  1.00 12.15 ? 93  PHE A C   1 
ATOM   752  O  O   . PHE A 1 93  ? -11.152 0.613   8.933   1.00 11.99 ? 93  PHE A O   1 
ATOM   753  C  CB  . PHE A 1 93  ? -13.711 0.633   11.147  1.00 11.89 ? 93  PHE A CB  1 
ATOM   754  C  CG  . PHE A 1 93  ? -14.406 0.185   9.889   1.00 13.46 ? 93  PHE A CG  1 
ATOM   755  C  CD1 . PHE A 1 93  ? -14.079 -1.005  9.246   1.00 14.04 ? 93  PHE A CD1 1 
ATOM   756  C  CD2 . PHE A 1 93  ? -15.475 0.930   9.415   1.00 13.82 ? 93  PHE A CD2 1 
ATOM   757  C  CE1 . PHE A 1 93  ? -14.747 -1.405  8.089   1.00 14.85 ? 93  PHE A CE1 1 
ATOM   758  C  CE2 . PHE A 1 93  ? -16.152 0.528   8.270   1.00 14.42 ? 93  PHE A CE2 1 
ATOM   759  C  CZ  . PHE A 1 93  ? -15.810 -0.652  7.644   1.00 16.40 ? 93  PHE A CZ  1 
ATOM   760  N  N   . HIS A 1 94  ? -10.892 -0.624  10.773  1.00 10.76 ? 94  HIS A N   1 
ATOM   761  C  CA  . HIS A 1 94  ? -10.007 -1.578  10.173  1.00 10.15 ? 94  HIS A CA  1 
ATOM   762  C  C   . HIS A 1 94  ? -10.122 -2.856  10.994  1.00 10.83 ? 94  HIS A C   1 
ATOM   763  O  O   . HIS A 1 94  ? -10.804 -2.854  12.033  1.00 9.54  ? 94  HIS A O   1 
ATOM   764  C  CB  . HIS A 1 94  ? -8.548  -1.070  10.100  1.00 10.28 ? 94  HIS A CB  1 
ATOM   765  C  CG  . HIS A 1 94  ? -8.020  -0.817  11.489  1.00 9.88  ? 94  HIS A CG  1 
ATOM   766  N  ND1 . HIS A 1 94  ? -8.158  0.399   12.155  1.00 11.03 ? 94  HIS A ND1 1 
ATOM   767  C  CD2 . HIS A 1 94  ? -7.445  -1.683  12.339  1.00 11.36 ? 94  HIS A CD2 1 
ATOM   768  C  CE1 . HIS A 1 94  ? -7.682  0.210   13.412  1.00 8.56  ? 94  HIS A CE1 1 
ATOM   769  N  NE2 . HIS A 1 94  ? -7.215  -1.050  13.522  1.00 9.78  ? 94  HIS A NE2 1 
ATOM   770  N  N   . PHE A 1 95  ? -9.411  -3.891  10.546  1.00 11.01 ? 95  PHE A N   1 
ATOM   771  C  CA  . PHE A 1 95  ? -9.416  -5.182  11.221  1.00 10.67 ? 95  PHE A CA  1 
ATOM   772  C  C   . PHE A 1 95  ? -7.982  -5.652  11.393  1.00 10.30 ? 95  PHE A C   1 
ATOM   773  O  O   . PHE A 1 95  ? -7.065  -5.167  10.724  1.00 12.56 ? 95  PHE A O   1 
ATOM   774  C  CB  . PHE A 1 95  ? -10.132 -6.290  10.403  1.00 9.86  ? 95  PHE A CB  1 
ATOM   775  C  CG  . PHE A 1 95  ? -11.565 -5.975  10.062  1.00 10.69 ? 95  PHE A CG  1 
ATOM   776  C  CD1 . PHE A 1 95  ? -11.864 -5.102  9.016   1.00 11.15 ? 95  PHE A CD1 1 
ATOM   777  C  CD2 . PHE A 1 95  ? -12.605 -6.651  10.684  1.00 9.93  ? 95  PHE A CD2 1 
ATOM   778  C  CE1 . PHE A 1 95  ? -13.175 -4.841  8.672   1.00 10.85 ? 95  PHE A CE1 1 
ATOM   779  C  CE2 . PHE A 1 95  ? -13.925 -6.362  10.357  1.00 10.95 ? 95  PHE A CE2 1 
ATOM   780  C  CZ  . PHE A 1 95  ? -14.199 -5.501  9.298   1.00 10.57 ? 95  PHE A CZ  1 
ATOM   781  N  N   . HIS A 1 96  ? -7.818  -6.591  12.334  1.00 9.83  ? 96  HIS A N   1 
ATOM   782  C  CA  . HIS A 1 96  ? -6.635  -7.407  12.507  1.00 9.11  ? 96  HIS A CA  1 
ATOM   783  C  C   . HIS A 1 96  ? -7.076  -8.858  12.370  1.00 9.05  ? 96  HIS A C   1 
ATOM   784  O  O   . HIS A 1 96  ? -8.144  -9.236  12.883  1.00 10.11 ? 96  HIS A O   1 
ATOM   785  C  CB  . HIS A 1 96  ? -5.999  -7.175  13.899  1.00 9.25  ? 96  HIS A CB  1 
ATOM   786  C  CG  . HIS A 1 96  ? -5.698  -5.731  14.160  1.00 9.08  ? 96  HIS A CG  1 
ATOM   787  N  ND1 . HIS A 1 96  ? -4.462  -5.153  13.908  1.00 10.07 ? 96  HIS A ND1 1 
ATOM   788  C  CD2 . HIS A 1 96  ? -6.514  -4.719  14.571  1.00 10.13 ? 96  HIS A CD2 1 
ATOM   789  C  CE1 . HIS A 1 96  ? -4.514  -3.844  14.223  1.00 9.50  ? 96  HIS A CE1 1 
ATOM   790  N  NE2 . HIS A 1 96  ? -5.799  -3.547  14.626  1.00 10.20 ? 96  HIS A NE2 1 
ATOM   791  N  N   . TRP A 1 97  ? -6.275  -9.704  11.704  1.00 8.66  ? 97  TRP A N   1 
ATOM   792  C  CA  . TRP A 1 97  ? -6.720  -11.074 11.524  1.00 8.57  ? 97  TRP A CA  1 
ATOM   793  C  C   . TRP A 1 97  ? -5.520  -12.005 11.418  1.00 8.50  ? 97  TRP A C   1 
ATOM   794  O  O   . TRP A 1 97  ? -4.378  -11.563 11.289  1.00 11.02 ? 97  TRP A O   1 
ATOM   795  C  CB  . TRP A 1 97  ? -7.593  -11.243 10.269  1.00 10.04 ? 97  TRP A CB  1 
ATOM   796  C  CG  . TRP A 1 97  ? -6.943  -10.821 8.978   1.00 11.89 ? 97  TRP A CG  1 
ATOM   797  C  CD1 . TRP A 1 97  ? -6.207  -11.612 8.143   1.00 13.34 ? 97  TRP A CD1 1 
ATOM   798  C  CD2 . TRP A 1 97  ? -6.863  -9.484  8.436   1.00 11.81 ? 97  TRP A CD2 1 
ATOM   799  N  NE1 . TRP A 1 97  ? -5.772  -10.902 7.051   1.00 13.29 ? 97  TRP A NE1 1 
ATOM   800  C  CE2 . TRP A 1 97  ? -6.145  -9.588  7.217   1.00 13.11 ? 97  TRP A CE2 1 
ATOM   801  C  CE3 . TRP A 1 97  ? -7.373  -8.226  8.826   1.00 12.91 ? 97  TRP A CE3 1 
ATOM   802  C  CZ2 . TRP A 1 97  ? -5.924  -8.475  6.407   1.00 14.36 ? 97  TRP A CZ2 1 
ATOM   803  C  CZ3 . TRP A 1 97  ? -7.139  -7.118  8.020   1.00 12.85 ? 97  TRP A CZ3 1 
ATOM   804  C  CH2 . TRP A 1 97  ? -6.443  -7.262  6.816   1.00 13.56 ? 97  TRP A CH2 1 
ATOM   805  N  N   . GLY A 1 98  ? -5.806  -13.305 11.415  1.00 9.08  ? 98  GLY A N   1 
ATOM   806  C  CA  . GLY A 1 98  ? -4.803  -14.355 11.435  1.00 10.52 ? 98  GLY A CA  1 
ATOM   807  C  C   . GLY A 1 98  ? -4.541  -15.068 10.093  1.00 11.09 ? 98  GLY A C   1 
ATOM   808  O  O   . GLY A 1 98  ? -5.207  -14.842 9.096   1.00 11.41 ? 98  GLY A O   1 
ATOM   809  N  N   . SER A 1 99  ? -3.499  -15.905 10.106  1.00 13.52 ? 99  SER A N   1 
ATOM   810  C  CA  . SER A 1 99  ? -3.266  -16.856 9.024   1.00 13.36 ? 99  SER A CA  1 
ATOM   811  C  C   . SER A 1 99  ? -4.221  -18.065 9.104   1.00 16.03 ? 99  SER A C   1 
ATOM   812  O  O   . SER A 1 99  ? -4.365  -18.786 8.113   1.00 16.86 ? 99  SER A O   1 
ATOM   813  C  CB  . SER A 1 99  ? -1.812  -17.284 9.073   1.00 14.31 ? 99  SER A CB  1 
ATOM   814  O  OG  . SER A 1 99  ? -1.487  -17.817 10.343  1.00 16.66 ? 99  SER A OG  1 
ATOM   815  N  N   . LEU A 1 100 ? -4.796  -18.336 10.289  1.00 13.53 ? 100 LEU A N   1 
ATOM   816  C  CA  . LEU A 1 100 ? -5.698  -19.453 10.552  1.00 15.66 ? 100 LEU A CA  1 
ATOM   817  C  C   . LEU A 1 100 ? -6.831  -18.904 11.417  1.00 14.13 ? 100 LEU A C   1 
ATOM   818  O  O   . LEU A 1 100 ? -6.648  -17.865 12.082  1.00 13.21 ? 100 LEU A O   1 
ATOM   819  C  CB  . LEU A 1 100 ? -4.935  -20.508 11.361  1.00 21.32 ? 100 LEU A CB  1 
ATOM   820  C  CG  . LEU A 1 100 ? -3.632  -20.996 10.747  1.00 23.99 ? 100 LEU A CG  1 
ATOM   821  C  CD1 . LEU A 1 100 ? -2.558  -21.053 11.814  1.00 27.28 ? 100 LEU A CD1 1 
ATOM   822  C  CD2 . LEU A 1 100 ? -3.833  -22.354 10.101  1.00 27.79 ? 100 LEU A CD2 1 
ATOM   823  N  N   . ASP A 1 101 ? -7.956  -19.640 11.471  1.00 12.62 ? 101 ASP A N   1 
ATOM   824  C  CA  . ASP A 1 101 ? -9.096  -19.144 12.237  1.00 12.59 ? 101 ASP A CA  1 
ATOM   825  C  C   . ASP A 1 101 ? -8.795  -19.115 13.745  1.00 13.83 ? 101 ASP A C   1 
ATOM   826  O  O   . ASP A 1 101 ? -9.541  -18.472 14.484  1.00 16.66 ? 101 ASP A O   1 
ATOM   827  C  CB  . ASP A 1 101 ? -10.372 -19.950 11.970  1.00 12.63 ? 101 ASP A CB  1 
ATOM   828  C  CG  . ASP A 1 101 ? -10.837 -19.985 10.527  1.00 14.70 ? 101 ASP A CG  1 
ATOM   829  O  OD1 . ASP A 1 101 ? -10.474 -19.113 9.734   1.00 17.63 ? 101 ASP A OD1 1 
ATOM   830  O  OD2 . ASP A 1 101 ? -11.653 -20.869 10.221  1.00 18.36 ? 101 ASP A OD2 1 
ATOM   831  N  N   . GLY A 1 102 ? -7.737  -19.825 14.201  1.00 13.28 ? 102 GLY A N   1 
ATOM   832  C  CA  . GLY A 1 102 ? -7.496  -19.924 15.643  1.00 12.86 ? 102 GLY A CA  1 
ATOM   833  C  C   . GLY A 1 102 ? -6.687  -18.758 16.226  1.00 12.60 ? 102 GLY A C   1 
ATOM   834  O  O   . GLY A 1 102 ? -6.383  -18.716 17.422  1.00 13.57 ? 102 GLY A O   1 
ATOM   835  N  N   . GLN A 1 103 ? -6.401  -17.764 15.397  1.00 11.90 ? 103 GLN A N   1 
ATOM   836  C  CA  . GLN A 1 103 ? -5.709  -16.589 15.916  1.00 12.52 ? 103 GLN A CA  1 
ATOM   837  C  C   . GLN A 1 103 ? -6.035  -15.391 15.050  1.00 11.54 ? 103 GLN A C   1 
ATOM   838  O  O   . GLN A 1 103 ? -6.535  -15.576 13.947  1.00 11.72 ? 103 GLN A O   1 
ATOM   839  C  CB  . GLN A 1 103 ? -4.193  -16.828 15.975  1.00 13.72 ? 103 GLN A CB  1 
ATOM   840  C  CG  . GLN A 1 103 ? -3.562  -16.992 14.581  1.00 13.98 ? 103 GLN A CG  1 
ATOM   841  C  CD  . GLN A 1 103 ? -2.166  -17.577 14.657  1.00 18.63 ? 103 GLN A CD  1 
ATOM   842  O  OE1 . GLN A 1 103 ? -1.913  -18.504 15.434  1.00 22.19 ? 103 GLN A OE1 1 
ATOM   843  N  NE2 . GLN A 1 103 ? -1.252  -17.047 13.852  1.00 17.10 ? 103 GLN A NE2 1 
ATOM   844  N  N   . GLY A 1 104 ? -5.708  -14.185 15.518  1.00 11.81 ? 104 GLY A N   1 
ATOM   845  C  CA  . GLY A 1 104 ? -5.942  -12.972 14.727  1.00 11.41 ? 104 GLY A CA  1 
ATOM   846  C  C   . GLY A 1 104 ? -6.423  -11.777 15.550  1.00 11.33 ? 104 GLY A C   1 
ATOM   847  O  O   . GLY A 1 104 ? -6.137  -10.609 15.214  1.00 10.58 ? 104 GLY A O   1 
ATOM   848  N  N   . SER A 1 105 ? -7.116  -12.051 16.684  1.00 9.29  ? 105 SER A N   1 
ATOM   849  C  CA  . SER A 1 105 ? -7.522  -10.939 17.530  1.00 11.02 ? 105 SER A CA  1 
ATOM   850  C  C   . SER A 1 105 ? -6.310  -10.381 18.296  1.00 9.45  ? 105 SER A C   1 
ATOM   851  O  O   . SER A 1 105 ? -5.305  -11.076 18.487  1.00 10.64 ? 105 SER A O   1 
ATOM   852  C  CB  . SER A 1 105 ? -8.658  -11.284 18.448  1.00 11.72 ? 105 SER A CB  1 
ATOM   853  O  OG  . SER A 1 105 ? -8.254  -12.193 19.443  1.00 12.13 ? 105 SER A OG  1 
ATOM   854  N  N   . GLU A 1 106 ? -6.417  -9.099  18.641  1.00 9.50  ? 106 GLU A N   1 
ATOM   855  C  CA  . GLU A 1 106 ? -5.412  -8.441  19.484  1.00 8.69  ? 106 GLU A CA  1 
ATOM   856  C  C   . GLU A 1 106 ? -5.754  -8.629  20.976  1.00 8.95  ? 106 GLU A C   1 
ATOM   857  O  O   . GLU A 1 106 ? -4.996  -9.202  21.761  1.00 10.25 ? 106 GLU A O   1 
ATOM   858  C  CB  . GLU A 1 106 ? -5.301  -6.957  19.108  1.00 8.63  ? 106 GLU A CB  1 
ATOM   859  C  CG  . GLU A 1 106 ? -4.838  -6.820  17.651  1.00 9.31  ? 106 GLU A CG  1 
ATOM   860  C  CD  . GLU A 1 106 ? -4.202  -5.500  17.295  1.00 9.36  ? 106 GLU A CD  1 
ATOM   861  O  OE1 . GLU A 1 106 ? -4.798  -4.455  17.531  1.00 9.34  ? 106 GLU A OE1 1 
ATOM   862  O  OE2 . GLU A 1 106 ? -3.008  -5.542  16.850  1.00 10.37 ? 106 GLU A OE2 1 
ATOM   863  N  N   . HIS A 1 107 ? -6.966  -8.214  21.380  1.00 9.26  ? 107 HIS A N   1 
ATOM   864  C  CA  . HIS A 1 107 ? -7.361  -8.543  22.737  1.00 7.84  ? 107 HIS A CA  1 
ATOM   865  C  C   . HIS A 1 107 ? -7.730  -10.020 22.748  1.00 8.76  ? 107 HIS A C   1 
ATOM   866  O  O   . HIS A 1 107 ? -8.054  -10.604 21.696  1.00 8.91  ? 107 HIS A O   1 
ATOM   867  C  CB  . HIS A 1 107 ? -8.619  -7.727  23.109  1.00 7.90  ? 107 HIS A CB  1 
ATOM   868  C  CG  . HIS A 1 107 ? -8.279  -6.280  23.227  1.00 7.93  ? 107 HIS A CG  1 
ATOM   869  N  ND1 . HIS A 1 107 ? -8.377  -5.398  22.186  1.00 9.33  ? 107 HIS A ND1 1 
ATOM   870  C  CD2 . HIS A 1 107 ? -7.906  -5.569  24.312  1.00 8.33  ? 107 HIS A CD2 1 
ATOM   871  C  CE1 . HIS A 1 107 ? -7.965  -4.198  22.583  1.00 8.12  ? 107 HIS A CE1 1 
ATOM   872  N  NE2 . HIS A 1 107 ? -7.719  -4.265  23.920  1.00 7.33  ? 107 HIS A NE2 1 
ATOM   873  N  N   . THR A 1 108 ? -7.599  -10.569 23.942  1.00 9.55  ? 108 THR A N   1 
ATOM   874  C  CA  . THR A 1 108 ? -8.009  -11.947 24.184  1.00 10.09 ? 108 THR A CA  1 
ATOM   875  C  C   . THR A 1 108 ? -8.970  -11.958 25.369  1.00 10.83 ? 108 THR A C   1 
ATOM   876  O  O   . THR A 1 108 ? -8.955  -11.051 26.186  1.00 12.60 ? 108 THR A O   1 
ATOM   877  C  CB  . THR A 1 108 ? -6.790  -12.858 24.343  1.00 10.27 ? 108 THR A CB  1 
ATOM   878  O  OG1 . THR A 1 108 ? -6.040  -12.408 25.478  1.00 11.10 ? 108 THR A OG1 1 
ATOM   879  C  CG2 . THR A 1 108 ? -5.953  -12.930 23.077  1.00 9.67  ? 108 THR A CG2 1 
ATOM   880  N  N   . VAL A 1 109 ? -9.770  -13.022 25.463  1.00 11.87 ? 109 VAL A N   1 
ATOM   881  C  CA  . VAL A 1 109 ? -10.738 -13.164 26.553  1.00 12.87 ? 109 VAL A CA  1 
ATOM   882  C  C   . VAL A 1 109 ? -10.422 -14.458 27.296  1.00 14.40 ? 109 VAL A C   1 
ATOM   883  O  O   . VAL A 1 109 ? -10.554 -15.529 26.742  1.00 14.47 ? 109 VAL A O   1 
ATOM   884  C  CB  . VAL A 1 109 ? -12.186 -13.104 26.020  1.00 14.52 ? 109 VAL A CB  1 
ATOM   885  C  CG1 . VAL A 1 109 ? -13.170 -13.149 27.178  1.00 15.06 ? 109 VAL A CG1 1 
ATOM   886  C  CG2 . VAL A 1 109 ? -12.442 -11.814 25.216  1.00 12.62 ? 109 VAL A CG2 1 
ATOM   887  N  N   . ASP A 1 110 ? -10.000 -14.361 28.554  1.00 13.84 ? 110 ASP A N   1 
ATOM   888  C  CA  . ASP A 1 110 ? -9.488  -15.549 29.272  1.00 15.04 ? 110 ASP A CA  1 
ATOM   889  C  C   . ASP A 1 110 ? -8.524  -16.373 28.400  1.00 12.94 ? 110 ASP A C   1 
ATOM   890  O  O   . ASP A 1 110 ? -8.587  -17.607 28.358  1.00 13.93 ? 110 ASP A O   1 
ATOM   891  C  CB  . ASP A 1 110 ? -10.656 -16.388 29.812  1.00 16.09 ? 110 ASP A CB  1 
ATOM   892  C  CG  . ASP A 1 110 ? -11.522 -15.581 30.766  1.00 15.88 ? 110 ASP A CG  1 
ATOM   893  O  OD1 . ASP A 1 110 ? -10.955 -14.782 31.495  1.00 18.26 ? 110 ASP A OD1 1 
ATOM   894  O  OD2 . ASP A 1 110 ? -12.754 -15.784 30.768  1.00 21.31 ? 110 ASP A OD2 1 
ATOM   895  N  N   . LYS A 1 111 ? -7.612  -15.668 27.707  1.00 14.63 ? 111 LYS A N   1 
ATOM   896  C  CA  . LYS A 1 111 ? -6.527  -16.147 26.841  1.00 15.55 ? 111 LYS A CA  1 
ATOM   897  C  C   . LYS A 1 111 ? -7.020  -16.609 25.469  1.00 14.10 ? 111 LYS A C   1 
ATOM   898  O  O   . LYS A 1 111 ? -6.225  -17.059 24.651  1.00 15.09 ? 111 LYS A O   1 
ATOM   899  C  CB  . LYS A 1 111 ? -5.652  -17.229 27.504  1.00 17.73 ? 111 LYS A CB  1 
ATOM   900  C  CG  . LYS A 1 111 ? -4.947  -16.800 28.783  1.00 19.74 ? 111 LYS A CG  1 
ATOM   901  C  CD  . LYS A 1 111 ? -3.898  -15.791 28.418  1.00 23.01 ? 111 LYS A CD  1 
ATOM   902  C  CE  . LYS A 1 111 ? -3.254  -15.075 29.592  1.00 27.17 ? 111 LYS A CE  1 
ATOM   903  N  NZ  . LYS A 1 111 ? -1.816  -15.421 29.659  1.00 32.46 ? 111 LYS A NZ  1 
ATOM   904  N  N   . LYS A 1 112 ? -8.341  -16.578 25.256  1.00 13.12 ? 112 LYS A N   1 
ATOM   905  C  CA  . LYS A 1 112 ? -8.917  -17.013 23.998  1.00 14.00 ? 112 LYS A CA  1 
ATOM   906  C  C   . LYS A 1 112 ? -8.666  -15.942 22.922  1.00 13.11 ? 112 LYS A C   1 
ATOM   907  O  O   . LYS A 1 112 ? -8.965  -14.746 23.095  1.00 11.16 ? 112 LYS A O   1 
ATOM   908  C  CB  . LYS A 1 112 ? -10.417 -17.310 24.139  1.00 15.24 ? 112 LYS A CB  1 
ATOM   909  C  CG  . LYS A 1 112 ? -11.149 -17.485 22.808  1.00 16.64 ? 112 LYS A CG  1 
ATOM   910  C  CD  . LYS A 1 112 ? -12.668 -17.354 22.953  1.00 19.14 ? 112 LYS A CD  1 
ATOM   911  C  CE  . LYS A 1 112 ? -13.235 -17.484 21.554  1.00 20.24 ? 112 LYS A CE  1 
ATOM   912  N  NZ  . LYS A 1 112 ? -13.241 -18.902 21.153  1.00 21.33 ? 112 LYS A NZ  1 
ATOM   913  N  N   . LYS A 1 113 ? -8.137  -16.415 21.781  1.00 13.41 ? 113 LYS A N   1 
ATOM   914  C  CA  . LYS A 1 113 ? -7.928  -15.634 20.568  1.00 13.16 ? 113 LYS A CA  1 
ATOM   915  C  C   . LYS A 1 113 ? -9.056  -15.875 19.591  1.00 12.09 ? 113 LYS A C   1 
ATOM   916  O  O   . LYS A 1 113 ? -9.420  -17.037 19.348  1.00 12.47 ? 113 LYS A O   1 
ATOM   917  C  CB  . LYS A 1 113 ? -6.622  -16.059 19.894  1.00 12.95 ? 113 LYS A CB  1 
ATOM   918  C  CG  . LYS A 1 113 ? -5.385  -15.546 20.606  1.00 13.99 ? 113 LYS A CG  1 
ATOM   919  C  CD  . LYS A 1 113 ? -4.175  -16.284 20.063  1.00 14.26 ? 113 LYS A CD  1 
ATOM   920  C  CE  . LYS A 1 113 ? -2.891  -15.590 20.478  1.00 16.39 ? 113 LYS A CE  1 
ATOM   921  N  NZ  . LYS A 1 113 ? -2.066  -16.493 21.295  1.00 23.57 ? 113 LYS A NZ  1 
ATOM   922  N  N   . TYR A 1 114 ? -9.603  -14.770 19.055  1.00 10.92 ? 114 TYR A N   1 
ATOM   923  C  CA  . TYR A 1 114 ? -10.649 -14.877 18.039  1.00 9.93  ? 114 TYR A CA  1 
ATOM   924  C  C   . TYR A 1 114 ? -9.995  -14.810 16.664  1.00 9.79  ? 114 TYR A C   1 
ATOM   925  O  O   . TYR A 1 114 ? -8.815  -14.463 16.587  1.00 11.13 ? 114 TYR A O   1 
ATOM   926  C  CB  . TYR A 1 114 ? -11.715 -13.777 18.217  1.00 10.61 ? 114 TYR A CB  1 
ATOM   927  C  CG  . TYR A 1 114 ? -12.651 -13.963 19.379  1.00 11.76 ? 114 TYR A CG  1 
ATOM   928  C  CD1 . TYR A 1 114 ? -12.296 -13.563 20.648  1.00 12.96 ? 114 TYR A CD1 1 
ATOM   929  C  CD2 . TYR A 1 114 ? -13.847 -14.629 19.186  1.00 13.61 ? 114 TYR A CD2 1 
ATOM   930  C  CE1 . TYR A 1 114 ? -13.145 -13.795 21.709  1.00 15.11 ? 114 TYR A CE1 1 
ATOM   931  C  CE2 . TYR A 1 114 ? -14.736 -14.822 20.221  1.00 14.53 ? 114 TYR A CE2 1 
ATOM   932  C  CZ  . TYR A 1 114 ? -14.358 -14.426 21.488  1.00 14.93 ? 114 TYR A CZ  1 
ATOM   933  O  OH  . TYR A 1 114 ? -15.231 -14.617 22.522  1.00 20.98 ? 114 TYR A OH  1 
ATOM   934  N  N   . ALA A 1 115 ? -10.742 -15.110 15.590  1.00 10.74 ? 115 ALA A N   1 
ATOM   935  C  CA  . ALA A 1 115 ? -10.197 -15.133 14.227  1.00 10.49 ? 115 ALA A CA  1 
ATOM   936  C  C   . ALA A 1 115 ? -9.738  -13.732 13.790  1.00 11.63 ? 115 ALA A C   1 
ATOM   937  O  O   . ALA A 1 115 ? -8.909  -13.551 12.867  1.00 12.64 ? 115 ALA A O   1 
ATOM   938  C  CB  . ALA A 1 115 ? -11.240 -15.726 13.287  1.00 13.35 ? 115 ALA A CB  1 
ATOM   939  N  N   . ALA A 1 116 ? -10.453 -12.723 14.300  1.00 10.37 ? 116 ALA A N   1 
ATOM   940  C  CA  . ALA A 1 116 ? -10.142 -11.363 13.898  1.00 9.53  ? 116 ALA A CA  1 
ATOM   941  C  C   . ALA A 1 116 ? -10.715 -10.386 14.912  1.00 9.97  ? 116 ALA A C   1 
ATOM   942  O  O   . ALA A 1 116 ? -11.467 -10.771 15.811  1.00 9.62  ? 116 ALA A O   1 
ATOM   943  C  CB  . ALA A 1 116 ? -10.701 -11.064 12.487  1.00 9.13  ? 116 ALA A CB  1 
ATOM   944  N  N   . GLU A 1 117 ? -10.400 -9.103  14.714  1.00 9.78  ? 117 GLU A N   1 
ATOM   945  C  CA  . GLU A 1 117 ? -10.923 -8.069  15.586  1.00 10.45 ? 117 GLU A CA  1 
ATOM   946  C  C   . GLU A 1 117 ? -11.073 -6.801  14.771  1.00 10.56 ? 117 GLU A C   1 
ATOM   947  O  O   . GLU A 1 117 ? -10.157 -6.440  14.039  1.00 11.83 ? 117 GLU A O   1 
ATOM   948  C  CB  . GLU A 1 117 ? -9.956  -7.801  16.758  1.00 10.09 ? 117 GLU A CB  1 
ATOM   949  C  CG  . GLU A 1 117 ? -10.508 -6.906  17.900  1.00 8.78  ? 117 GLU A CG  1 
ATOM   950  C  CD  . GLU A 1 117 ? -9.545  -6.814  19.080  1.00 11.27 ? 117 GLU A CD  1 
ATOM   951  O  OE1 . GLU A 1 117 ? -8.867  -7.826  19.332  1.00 9.70  ? 117 GLU A OE1 1 
ATOM   952  O  OE2 . GLU A 1 117 ? -9.494  -5.708  19.771  1.00 11.24 ? 117 GLU A OE2 1 
ATOM   953  N  N   . LEU A 1 118 ? -12.267 -6.204  14.890  1.00 9.83  ? 118 LEU A N   1 
ATOM   954  C  CA  . LEU A 1 118 ? -12.658 -4.951  14.254  1.00 8.91  ? 118 LEU A CA  1 
ATOM   955  C  C   . LEU A 1 118 ? -12.432 -3.800  15.233  1.00 8.94  ? 118 LEU A C   1 
ATOM   956  O  O   . LEU A 1 118 ? -12.843 -3.882  16.399  1.00 9.21  ? 118 LEU A O   1 
ATOM   957  C  CB  . LEU A 1 118 ? -14.154 -5.078  13.899  1.00 8.27  ? 118 LEU A CB  1 
ATOM   958  C  CG  . LEU A 1 118 ? -14.859 -3.755  13.585  1.00 8.83  ? 118 LEU A CG  1 
ATOM   959  C  CD1 . LEU A 1 118 ? -14.334 -3.159  12.283  1.00 9.81  ? 118 LEU A CD1 1 
ATOM   960  C  CD2 . LEU A 1 118 ? -16.351 -3.993  13.400  1.00 9.85  ? 118 LEU A CD2 1 
ATOM   961  N  N   . HIS A 1 119 ? -11.806 -2.709  14.750  1.00 8.11  ? 119 HIS A N   1 
ATOM   962  C  CA  . HIS A 1 119 ? -11.553 -1.492  15.515  1.00 8.69  ? 119 HIS A CA  1 
ATOM   963  C  C   . HIS A 1 119 ? -12.213 -0.303  14.843  1.00 9.03  ? 119 HIS A C   1 
ATOM   964  O  O   . HIS A 1 119 ? -11.924 -0.044  13.675  1.00 10.80 ? 119 HIS A O   1 
ATOM   965  C  CB  . HIS A 1 119 ? -10.041 -1.237  15.582  1.00 7.64  ? 119 HIS A CB  1 
ATOM   966  C  CG  . HIS A 1 119 ? -9.405  -2.248  16.491  1.00 8.60  ? 119 HIS A CG  1 
ATOM   967  N  ND1 . HIS A 1 119 ? -8.058  -2.543  16.462  1.00 8.55  ? 119 HIS A ND1 1 
ATOM   968  C  CD2 . HIS A 1 119 ? -9.915  -3.026  17.467  1.00 9.05  ? 119 HIS A CD2 1 
ATOM   969  C  CE1 . HIS A 1 119 ? -7.754  -3.439  17.401  1.00 8.57  ? 119 HIS A CE1 1 
ATOM   970  N  NE2 . HIS A 1 119 ? -8.885  -3.796  17.987  1.00 8.81  ? 119 HIS A NE2 1 
ATOM   971  N  N   . LEU A 1 120 ? -13.194 0.311   15.503  1.00 9.06  ? 120 LEU A N   1 
ATOM   972  C  CA  . LEU A 1 120 ? -13.866 1.523   15.052  1.00 9.61  ? 120 LEU A CA  1 
ATOM   973  C  C   . LEU A 1 120 ? -13.269 2.666   15.837  1.00 8.95  ? 120 LEU A C   1 
ATOM   974  O  O   . LEU A 1 120 ? -13.396 2.690   17.056  1.00 9.26  ? 120 LEU A O   1 
ATOM   975  C  CB  . LEU A 1 120 ? -15.377 1.375   15.249  1.00 10.44 ? 120 LEU A CB  1 
ATOM   976  C  CG  . LEU A 1 120 ? -15.992 0.285   14.359  1.00 11.64 ? 120 LEU A CG  1 
ATOM   977  C  CD1 . LEU A 1 120 ? -16.919 -0.577  15.206  1.00 13.32 ? 120 LEU A CD1 1 
ATOM   978  C  CD2 . LEU A 1 120 ? -16.842 0.955   13.276  1.00 13.26 ? 120 LEU A CD2 1 
ATOM   979  N  N   . VAL A 1 121 ? -12.441 3.437   15.157  1.00 9.49  ? 121 VAL A N   1 
ATOM   980  C  CA  . VAL A 1 121 ? -11.609 4.450   15.801  1.00 8.62  ? 121 VAL A CA  1 
ATOM   981  C  C   . VAL A 1 121 ? -12.340 5.785   15.794  1.00 8.88  ? 121 VAL A C   1 
ATOM   982  O  O   . VAL A 1 121 ? -12.705 6.269   14.725  1.00 8.33  ? 121 VAL A O   1 
ATOM   983  C  CB  . VAL A 1 121 ? -10.258 4.590   15.057  1.00 9.78  ? 121 VAL A CB  1 
ATOM   984  C  CG1 . VAL A 1 121 ? -9.371  5.624   15.736  1.00 11.14 ? 121 VAL A CG1 1 
ATOM   985  C  CG2 . VAL A 1 121 ? -9.534  3.257   14.916  1.00 9.78  ? 121 VAL A CG2 1 
ATOM   986  N  N   . HIS A 1 122 ? -12.488 6.381   16.990  1.00 8.82  ? 122 HIS A N   1 
ATOM   987  C  CA  . HIS A 1 122 ? -13.191 7.657   17.142  1.00 11.11 ? 122 HIS A CA  1 
ATOM   988  C  C   . HIS A 1 122 ? -12.325 8.675   17.883  1.00 11.16 ? 122 HIS A C   1 
ATOM   989  O  O   . HIS A 1 122 ? -11.519 8.304   18.725  1.00 11.32 ? 122 HIS A O   1 
ATOM   990  C  CB  . HIS A 1 122 ? -14.464 7.485   17.976  1.00 10.92 ? 122 HIS A CB  1 
ATOM   991  C  CG  . HIS A 1 122 ? -15.361 6.368   17.560  1.00 11.32 ? 122 HIS A CG  1 
ATOM   992  N  ND1 . HIS A 1 122 ? -15.030 5.034   17.794  1.00 10.93 ? 122 HIS A ND1 1 
ATOM   993  C  CD2 . HIS A 1 122 ? -16.596 6.379   16.985  1.00 11.50 ? 122 HIS A CD2 1 
ATOM   994  C  CE1 . HIS A 1 122 ? -16.027 4.270   17.367  1.00 11.67 ? 122 HIS A CE1 1 
ATOM   995  N  NE2 . HIS A 1 122 ? -17.025 5.071   16.864  1.00 12.44 ? 122 HIS A NE2 1 
ATOM   996  N  N   . TRP A 1 123 ? -12.517 9.978   17.617  1.00 10.99 ? 123 TRP A N   1 
ATOM   997  C  CA  . TRP A 1 123 ? -11.738 10.976  18.344  1.00 12.42 ? 123 TRP A CA  1 
ATOM   998  C  C   . TRP A 1 123 ? -12.619 11.975  19.076  1.00 12.71 ? 123 TRP A C   1 
ATOM   999  O  O   . TRP A 1 123 ? -13.728 12.320  18.646  1.00 12.86 ? 123 TRP A O   1 
ATOM   1000 C  CB  . TRP A 1 123 ? -10.774 11.715  17.423  1.00 12.20 ? 123 TRP A CB  1 
ATOM   1001 C  CG  . TRP A 1 123 ? -11.424 12.313  16.215  1.00 13.46 ? 123 TRP A CG  1 
ATOM   1002 C  CD1 . TRP A 1 123 ? -11.602 11.729  14.985  1.00 14.75 ? 123 TRP A CD1 1 
ATOM   1003 C  CD2 . TRP A 1 123 ? -11.904 13.665  16.093  1.00 13.36 ? 123 TRP A CD2 1 
ATOM   1004 N  NE1 . TRP A 1 123 ? -12.201 12.611  14.116  1.00 16.14 ? 123 TRP A NE1 1 
ATOM   1005 C  CE2 . TRP A 1 123 ? -12.356 13.823  14.752  1.00 14.73 ? 123 TRP A CE2 1 
ATOM   1006 C  CE3 . TRP A 1 123 ? -11.919 14.772  16.946  1.00 15.33 ? 123 TRP A CE3 1 
ATOM   1007 C  CZ2 . TRP A 1 123 ? -12.891 15.029  14.299  1.00 16.89 ? 123 TRP A CZ2 1 
ATOM   1008 C  CZ3 . TRP A 1 123 ? -12.489 15.948  16.509  1.00 15.04 ? 123 TRP A CZ3 1 
ATOM   1009 C  CH2 . TRP A 1 123 ? -12.897 16.093  15.170  1.00 15.74 ? 123 TRP A CH2 1 
ATOM   1010 N  N   . ASN A 1 124 ? -12.056 12.514  20.155  1.00 12.39 ? 124 ASN A N   1 
ATOM   1011 C  CA  . ASN A 1 124 ? -12.804 13.373  21.063  1.00 12.04 ? 124 ASN A CA  1 
ATOM   1012 C  C   . ASN A 1 124 ? -12.963 14.767  20.449  1.00 13.24 ? 124 ASN A C   1 
ATOM   1013 O  O   . ASN A 1 124 ? -11.969 15.418  20.096  1.00 11.78 ? 124 ASN A O   1 
ATOM   1014 C  CB  . ASN A 1 124 ? -12.054 13.357  22.393  1.00 14.72 ? 124 ASN A CB  1 
ATOM   1015 C  CG  . ASN A 1 124 ? -12.816 13.998  23.523  1.00 14.47 ? 124 ASN A CG  1 
ATOM   1016 O  OD1 . ASN A 1 124 ? -13.641 14.891  23.299  1.00 16.82 ? 124 ASN A OD1 1 
ATOM   1017 N  ND2 . ASN A 1 124 ? -12.504 13.544  24.738  1.00 14.56 ? 124 ASN A ND2 1 
ATOM   1018 N  N   . THR A 1 125 ? -14.226 15.203  20.255  1.00 15.59 ? 125 THR A N   1 
ATOM   1019 C  CA  . THR A 1 125 ? -14.459 16.428  19.480  1.00 18.01 ? 125 THR A CA  1 
ATOM   1020 C  C   . THR A 1 125 ? -13.873 17.657  20.212  1.00 19.19 ? 125 THR A C   1 
ATOM   1021 O  O   . THR A 1 125 ? -13.744 18.728  19.577  1.00 22.43 ? 125 THR A O   1 
ATOM   1022 C  CB  . THR A 1 125 ? -15.946 16.576  19.137  1.00 20.16 ? 125 THR A CB  1 
ATOM   1023 O  OG1 . THR A 1 125 ? -16.697 16.511  20.339  1.00 21.90 ? 125 THR A OG1 1 
ATOM   1024 C  CG2 . THR A 1 125 ? -16.440 15.484  18.218  1.00 21.38 ? 125 THR A CG2 1 
ATOM   1025 N  N   . LYS A 1 126 ? -13.630 17.452  21.638  1.00 17.45 ? 127 LYS A N   1 
ATOM   1026 C  CA  . LYS A 1 126 ? -13.100 18.682  22.289  1.00 19.85 ? 127 LYS A CA  1 
ATOM   1027 C  C   . LYS A 1 126 ? -11.732 19.070  21.701  1.00 20.53 ? 127 LYS A C   1 
ATOM   1028 O  O   . LYS A 1 126 ? -11.264 20.198  21.888  1.00 22.54 ? 127 LYS A O   1 
ATOM   1029 C  CB  . LYS A 1 126 ? -13.207 18.479  23.803  1.00 22.42 ? 127 LYS A CB  1 
ATOM   1030 C  CG  . LYS A 1 126 ? -12.149 17.574  24.409  1.00 24.28 ? 127 LYS A CG  1 
ATOM   1031 C  CD  . LYS A 1 126 ? -12.330 17.415  25.919  1.00 30.75 ? 127 LYS A CD  1 
ATOM   1032 C  CE  . LYS A 1 126 ? -11.593 16.214  26.466  1.00 34.03 ? 127 LYS A CE  1 
ATOM   1033 N  NZ  . LYS A 1 126 ? -11.856 16.059  27.920  1.00 40.70 ? 127 LYS A NZ  1 
ATOM   1034 N  N   . TYR A 1 127 ? -11.070 18.161  20.971  1.00 16.68 ? 128 TYR A N   1 
ATOM   1035 C  CA  . TYR A 1 127 ? -9.709  18.451  20.511  1.00 16.88 ? 128 TYR A CA  1 
ATOM   1036 C  C   . TYR A 1 127 ? -9.607  18.844  19.042  1.00 17.84 ? 128 TYR A C   1 
ATOM   1037 O  O   . TYR A 1 127 ? -8.494  19.071  18.547  1.00 19.07 ? 128 TYR A O   1 
ATOM   1038 C  CB  . TYR A 1 127 ? -8.803  17.240  20.691  1.00 17.45 ? 128 TYR A CB  1 
ATOM   1039 C  CG  . TYR A 1 127 ? -8.639  16.985  22.154  1.00 15.59 ? 128 TYR A CG  1 
ATOM   1040 C  CD1 . TYR A 1 127 ? -8.235  18.020  22.987  1.00 17.82 ? 128 TYR A CD1 1 
ATOM   1041 C  CD2 . TYR A 1 127 ? -8.891  15.736  22.686  1.00 14.85 ? 128 TYR A CD2 1 
ATOM   1042 C  CE1 . TYR A 1 127 ? -8.089  17.803  24.343  1.00 16.39 ? 128 TYR A CE1 1 
ATOM   1043 C  CE2 . TYR A 1 127 ? -8.767  15.505  24.038  1.00 16.34 ? 128 TYR A CE2 1 
ATOM   1044 C  CZ  . TYR A 1 127 ? -8.383  16.553  24.857  1.00 16.43 ? 128 TYR A CZ  1 
ATOM   1045 O  OH  . TYR A 1 127 ? -8.274  16.262  26.169  1.00 17.78 ? 128 TYR A OH  1 
ATOM   1046 N  N   . GLY A 1 128 ? -10.767 18.944  18.393  1.00 16.71 ? 129 GLY A N   1 
ATOM   1047 C  CA  . GLY A 1 128 ? -10.911 19.638  17.122  1.00 18.29 ? 129 GLY A CA  1 
ATOM   1048 C  C   . GLY A 1 128 ? -10.640 18.748  15.915  1.00 19.61 ? 129 GLY A C   1 
ATOM   1049 O  O   . GLY A 1 128 ? -11.249 18.914  14.851  1.00 19.10 ? 129 GLY A O   1 
ATOM   1050 N  N   . ASP A 1 129 ? -9.680  17.830  16.047  1.00 18.88 ? 130 ASP A N   1 
ATOM   1051 C  CA  . ASP A 1 129 ? -9.521  16.851  14.992  1.00 20.47 ? 130 ASP A CA  1 
ATOM   1052 C  C   . ASP A 1 129 ? -8.641  15.719  15.489  1.00 21.16 ? 130 ASP A C   1 
ATOM   1053 O  O   . ASP A 1 129 ? -8.166  15.722  16.638  1.00 17.68 ? 130 ASP A O   1 
ATOM   1054 C  CB  . ASP A 1 129 ? -8.947  17.467  13.716  1.00 24.04 ? 130 ASP A CB  1 
ATOM   1055 C  CG  . ASP A 1 129 ? -7.506  17.940  13.838  1.00 24.49 ? 130 ASP A CG  1 
ATOM   1056 O  OD1 . ASP A 1 129 ? -6.867  17.750  14.887  1.00 27.68 ? 130 ASP A OD1 1 
ATOM   1057 O  OD2 . ASP A 1 129 ? -7.008  18.471  12.849  1.00 28.98 ? 130 ASP A OD2 1 
ATOM   1058 N  N   . PHE A 1 130 ? -8.449  14.748  14.601  1.00 19.13 ? 131 PHE A N   1 
ATOM   1059 C  CA  . PHE A 1 130 ? -7.757  13.518  14.956  1.00 18.59 ? 131 PHE A CA  1 
ATOM   1060 C  C   . PHE A 1 130 ? -6.296  13.745  15.341  1.00 18.10 ? 131 PHE A C   1 
ATOM   1061 O  O   . PHE A 1 130 ? -5.841  13.176  16.325  1.00 15.41 ? 131 PHE A O   1 
ATOM   1062 C  CB  . PHE A 1 130 ? -7.918  12.442  13.873  1.00 17.13 ? 131 PHE A CB  1 
ATOM   1063 C  CG  . PHE A 1 130 ? -7.206  11.158  14.192  1.00 17.63 ? 131 PHE A CG  1 
ATOM   1064 C  CD1 . PHE A 1 130 ? -5.876  10.979  13.858  1.00 20.50 ? 131 PHE A CD1 1 
ATOM   1065 C  CD2 . PHE A 1 130 ? -7.875  10.143  14.855  1.00 18.40 ? 131 PHE A CD2 1 
ATOM   1066 C  CE1 . PHE A 1 130 ? -5.226  9.795   14.161  1.00 23.27 ? 131 PHE A CE1 1 
ATOM   1067 C  CE2 . PHE A 1 130 ? -7.227  8.966   15.169  1.00 19.67 ? 131 PHE A CE2 1 
ATOM   1068 C  CZ  . PHE A 1 130 ? -5.900  8.809   14.839  1.00 23.65 ? 131 PHE A CZ  1 
ATOM   1069 N  N   . GLY A 1 131 ? -5.560  14.528  14.540  1.00 18.30 ? 132 GLY A N   1 
ATOM   1070 C  CA  . GLY A 1 131 ? -4.153  14.782  14.797  1.00 19.59 ? 132 GLY A CA  1 
ATOM   1071 C  C   . GLY A 1 131 ? -3.877  15.367  16.182  1.00 17.86 ? 132 GLY A C   1 
ATOM   1072 O  O   . GLY A 1 131 ? -2.851  15.059  16.781  1.00 19.48 ? 132 GLY A O   1 
ATOM   1073 N  N   . LYS A 1 132 ? -4.740  16.294  16.603  1.00 19.07 ? 133 LYS A N   1 
ATOM   1074 C  CA  . LYS A 1 132 ? -4.614  16.852  17.942  1.00 18.77 ? 133 LYS A CA  1 
ATOM   1075 C  C   . LYS A 1 132 ? -5.052  15.842  19.004  1.00 17.63 ? 133 LYS A C   1 
ATOM   1076 O  O   . LYS A 1 132 ? -4.434  15.720  20.066  1.00 16.36 ? 133 LYS A O   1 
ATOM   1077 C  CB  . LYS A 1 132 ? -5.444  18.124  18.039  1.00 22.35 ? 133 LYS A CB  1 
ATOM   1078 C  CG  . LYS A 1 132 ? -4.714  19.386  17.634  1.00 28.02 ? 133 LYS A CG  1 
ATOM   1079 C  CD  . LYS A 1 132 ? -4.610  20.322  18.823  1.00 34.92 ? 133 LYS A CD  1 
ATOM   1080 C  CE  . LYS A 1 132 ? -3.334  20.190  19.620  1.00 37.82 ? 133 LYS A CE  1 
ATOM   1081 N  NZ  . LYS A 1 132 ? -2.209  20.844  18.915  1.00 40.93 ? 133 LYS A NZ  1 
ATOM   1082 N  N   . ALA A 1 133 ? -6.162  15.153  18.754  1.00 15.03 ? 134 ALA A N   1 
ATOM   1083 C  CA  . ALA A 1 133 ? -6.651  14.192  19.736  1.00 15.65 ? 134 ALA A CA  1 
ATOM   1084 C  C   . ALA A 1 133 ? -5.607  13.138  20.117  1.00 15.23 ? 134 ALA A C   1 
ATOM   1085 O  O   . ALA A 1 133 ? -5.548  12.751  21.292  1.00 13.21 ? 134 ALA A O   1 
ATOM   1086 C  CB  . ALA A 1 133 ? -7.928  13.536  19.246  1.00 14.73 ? 134 ALA A CB  1 
ATOM   1087 N  N   . VAL A 1 134 ? -4.840  12.591  19.162  1.00 15.34 ? 135 VAL A N   1 
ATOM   1088 C  CA  . VAL A 1 134 ? -3.940  11.493  19.520  1.00 18.07 ? 135 VAL A CA  1 
ATOM   1089 C  C   . VAL A 1 134 ? -2.846  11.916  20.504  1.00 17.53 ? 135 VAL A C   1 
ATOM   1090 O  O   . VAL A 1 134 ? -2.118  11.081  21.013  1.00 17.72 ? 135 VAL A O   1 
ATOM   1091 C  CB  . VAL A 1 134 ? -3.287  10.775  18.320  1.00 19.28 ? 135 VAL A CB  1 
ATOM   1092 C  CG1 . VAL A 1 134 ? -4.282  9.909   17.603  1.00 20.32 ? 135 VAL A CG1 1 
ATOM   1093 C  CG2 . VAL A 1 134 ? -2.460  11.678  17.408  1.00 19.39 ? 135 VAL A CG2 1 
ATOM   1094 N  N   . GLN A 1 135 ? -2.661  13.231  20.680  1.00 16.68 ? 136 GLN A N   1 
ATOM   1095 C  CA  . GLN A 1 135 ? -1.614  13.708  21.569  1.00 20.97 ? 136 GLN A CA  1 
ATOM   1096 C  C   . GLN A 1 135 ? -2.170  13.896  22.980  1.00 19.32 ? 136 GLN A C   1 
ATOM   1097 O  O   . GLN A 1 135 ? -1.506  14.472  23.838  1.00 21.66 ? 136 GLN A O   1 
ATOM   1098 C  CB  . GLN A 1 135 ? -1.074  15.040  21.033  1.00 23.60 ? 136 GLN A CB  1 
ATOM   1099 C  CG  . GLN A 1 135 ? -0.490  14.935  19.631  1.00 29.71 ? 136 GLN A CG  1 
ATOM   1100 C  CD  . GLN A 1 135 ? -0.058  16.281  19.088  1.00 38.48 ? 136 GLN A CD  1 
ATOM   1101 O  OE1 . GLN A 1 135 ? 0.431   17.152  19.816  1.00 43.74 ? 136 GLN A OE1 1 
ATOM   1102 N  NE2 . GLN A 1 135 ? -0.232  16.460  17.787  1.00 41.47 ? 136 GLN A NE2 1 
ATOM   1103 N  N   . GLN A 1 136 ? -3.422  13.488  23.211  1.00 17.72 ? 137 GLN A N   1 
ATOM   1104 C  CA  . GLN A 1 136 ? -4.042  13.716  24.518  1.00 16.06 ? 137 GLN A CA  1 
ATOM   1105 C  C   . GLN A 1 136 ? -4.428  12.397  25.164  1.00 14.94 ? 137 GLN A C   1 
ATOM   1106 O  O   . GLN A 1 136 ? -4.781  11.410  24.503  1.00 13.09 ? 137 GLN A O   1 
ATOM   1107 C  CB  . GLN A 1 136 ? -5.336  14.527  24.401  1.00 16.45 ? 137 GLN A CB  1 
ATOM   1108 C  CG  . GLN A 1 136 ? -5.250  15.679  23.406  1.00 19.32 ? 137 GLN A CG  1 
ATOM   1109 C  CD  . GLN A 1 136 ? -4.249  16.752  23.789  1.00 24.72 ? 137 GLN A CD  1 
ATOM   1110 O  OE1 . GLN A 1 136 ? -4.001  16.989  24.983  1.00 22.61 ? 137 GLN A OE1 1 
ATOM   1111 N  NE2 . GLN A 1 136 ? -3.681  17.412  22.769  1.00 26.04 ? 137 GLN A NE2 1 
ATOM   1112 N  N   . PRO A 1 137 ? -4.407  12.296  26.520  1.00 14.99 ? 138 PRO A N   1 
ATOM   1113 C  CA  . PRO A 1 137 ? -4.621  11.013  27.172  1.00 14.27 ? 138 PRO A CA  1 
ATOM   1114 C  C   . PRO A 1 137 ? -6.048  10.493  27.067  1.00 13.90 ? 138 PRO A C   1 
ATOM   1115 O  O   . PRO A 1 137 ? -6.282  9.294   27.246  1.00 14.70 ? 138 PRO A O   1 
ATOM   1116 C  CB  . PRO A 1 137 ? -4.321  11.213  28.666  1.00 15.90 ? 138 PRO A CB  1 
ATOM   1117 C  CG  . PRO A 1 137 ? -4.080  12.700  28.807  1.00 18.29 ? 138 PRO A CG  1 
ATOM   1118 C  CD  . PRO A 1 137 ? -4.072  13.372  27.446  1.00 17.66 ? 138 PRO A CD  1 
ATOM   1119 N  N   . ASP A 1 138 ? -6.986  11.402  26.764  1.00 13.05 ? 139 ASP A N   1 
ATOM   1120 C  CA  . ASP A 1 138 ? -8.360  11.025  26.511  1.00 13.52 ? 139 ASP A CA  1 
ATOM   1121 C  C   . ASP A 1 138 ? -8.805  11.365  25.074  1.00 12.28 ? 139 ASP A C   1 
ATOM   1122 O  O   . ASP A 1 138 ? -9.950  11.763  24.845  1.00 11.71 ? 139 ASP A O   1 
ATOM   1123 C  CB  . ASP A 1 138 ? -9.304  11.714  27.498  1.00 15.60 ? 139 ASP A CB  1 
ATOM   1124 C  CG  . ASP A 1 138 ? -9.212  13.225  27.481  1.00 17.67 ? 139 ASP A CG  1 
ATOM   1125 O  OD1 . ASP A 1 138 ? -8.286  13.803  26.820  1.00 18.15 ? 139 ASP A OD1 1 
ATOM   1126 O  OD2 . ASP A 1 138 ? -10.049 13.832  28.176  1.00 21.16 ? 139 ASP A OD2 1 
ATOM   1127 N  N   . GLY A 1 139 ? -7.875  11.282  24.126  1.00 11.13 ? 140 GLY A N   1 
ATOM   1128 C  CA  . GLY A 1 139 ? -8.083  11.708  22.739  1.00 11.16 ? 140 GLY A CA  1 
ATOM   1129 C  C   . GLY A 1 139 ? -8.962  10.780  21.902  1.00 10.42 ? 140 GLY A C   1 
ATOM   1130 O  O   . GLY A 1 139 ? -9.712  11.264  21.063  1.00 10.31 ? 140 GLY A O   1 
ATOM   1131 N  N   . LEU A 1 140 ? -8.827  9.456   22.104  1.00 10.63 ? 141 LEU A N   1 
ATOM   1132 C  CA  . LEU A 1 140 ? -9.485  8.490   21.239  1.00 9.85  ? 141 LEU A CA  1 
ATOM   1133 C  C   . LEU A 1 140 ? -10.362 7.537   22.039  1.00 10.53 ? 141 LEU A C   1 
ATOM   1134 O  O   . LEU A 1 140 ? -10.139 7.328   23.243  1.00 10.42 ? 141 LEU A O   1 
ATOM   1135 C  CB  . LEU A 1 140 ? -8.457  7.653   20.472  1.00 11.12 ? 141 LEU A CB  1 
ATOM   1136 C  CG  . LEU A 1 140 ? -7.415  8.373   19.618  1.00 14.07 ? 141 LEU A CG  1 
ATOM   1137 C  CD1 . LEU A 1 140 ? -6.823  7.363   18.658  1.00 15.20 ? 141 LEU A CD1 1 
ATOM   1138 C  CD2 . LEU A 1 140 ? -7.968  9.540   18.819  1.00 14.39 ? 141 LEU A CD2 1 
ATOM   1139 N  N   . ALA A 1 141 ? -11.424 7.034   21.380  1.00 10.28 ? 142 ALA A N   1 
ATOM   1140 C  CA  . ALA A 1 141 ? -12.171 5.901   21.909  1.00 10.02 ? 142 ALA A CA  1 
ATOM   1141 C  C   . ALA A 1 141 ? -12.214 4.901   20.755  1.00 10.23 ? 142 ALA A C   1 
ATOM   1142 O  O   . ALA A 1 141 ? -12.557 5.261   19.635  1.00 11.05 ? 142 ALA A O   1 
ATOM   1143 C  CB  . ALA A 1 141 ? -13.565 6.306   22.385  1.00 11.83 ? 142 ALA A CB  1 
ATOM   1144 N  N   . VAL A 1 142 ? -11.745 3.673   21.012  1.00 10.87 ? 143 VAL A N   1 
ATOM   1145 C  CA  . VAL A 1 142 ? -11.817 2.629   20.010  1.00 9.57  ? 143 VAL A CA  1 
ATOM   1146 C  C   . VAL A 1 142 ? -12.798 1.552   20.476  1.00 10.08 ? 143 VAL A C   1 
ATOM   1147 O  O   . VAL A 1 142 ? -12.711 1.039   21.594  1.00 11.38 ? 143 VAL A O   1 
ATOM   1148 C  CB  . VAL A 1 142 ? -10.465 1.981   19.698  1.00 10.06 ? 143 VAL A CB  1 
ATOM   1149 C  CG1 . VAL A 1 142 ? -10.598 0.991   18.531  1.00 9.47  ? 143 VAL A CG1 1 
ATOM   1150 C  CG2 . VAL A 1 142 ? -9.512  3.101   19.301  1.00 9.93  ? 143 VAL A CG2 1 
ATOM   1151 N  N   . LEU A 1 143 ? -13.793 1.291   19.640  1.00 9.17  ? 144 LEU A N   1 
ATOM   1152 C  CA  . LEU A 1 143 ? -14.758 0.238   19.879  1.00 10.15 ? 144 LEU A CA  1 
ATOM   1153 C  C   . LEU A 1 143 ? -14.208 -1.012  19.189  1.00 9.12  ? 144 LEU A C   1 
ATOM   1154 O  O   . LEU A 1 143 ? -14.082 -1.072  17.931  1.00 9.71  ? 144 LEU A O   1 
ATOM   1155 C  CB  . LEU A 1 143 ? -16.128 0.721   19.343  1.00 9.22  ? 144 LEU A CB  1 
ATOM   1156 C  CG  . LEU A 1 143 ? -17.268 -0.300  19.417  1.00 9.41  ? 144 LEU A CG  1 
ATOM   1157 C  CD1 . LEU A 1 143 ? -17.488 -0.624  20.886  1.00 9.56  ? 144 LEU A CD1 1 
ATOM   1158 C  CD2 . LEU A 1 143 ? -18.553 0.243   18.756  1.00 10.53 ? 144 LEU A CD2 1 
ATOM   1159 N  N   . GLY A 1 144 ? -13.901 -2.015  20.014  1.00 9.30  ? 145 GLY A N   1 
ATOM   1160 C  CA  . GLY A 1 144 ? -13.313 -3.264  19.540  1.00 8.79  ? 145 GLY A CA  1 
ATOM   1161 C  C   . GLY A 1 144 ? -14.377 -4.367  19.506  1.00 9.35  ? 145 GLY A C   1 
ATOM   1162 O  O   . GLY A 1 144 ? -15.092 -4.553  20.476  1.00 10.51 ? 145 GLY A O   1 
ATOM   1163 N  N   . ILE A 1 145 ? -14.482 -5.101  18.398  1.00 8.89  ? 146 ILE A N   1 
ATOM   1164 C  CA  . ILE A 1 145 ? -15.492 -6.165  18.267  1.00 9.25  ? 146 ILE A CA  1 
ATOM   1165 C  C   . ILE A 1 145 ? -14.749 -7.402  17.762  1.00 11.30 ? 146 ILE A C   1 
ATOM   1166 O  O   . ILE A 1 145 ? -14.096 -7.367  16.723  1.00 11.31 ? 146 ILE A O   1 
ATOM   1167 C  CB  . ILE A 1 145 ? -16.576 -5.724  17.264  1.00 10.11 ? 146 ILE A CB  1 
ATOM   1168 C  CG1 . ILE A 1 145 ? -17.265 -4.453  17.760  1.00 10.92 ? 146 ILE A CG1 1 
ATOM   1169 C  CG2 . ILE A 1 145 ? -17.594 -6.859  17.024  1.00 10.18 ? 146 ILE A CG2 1 
ATOM   1170 C  CD1 . ILE A 1 145 ? -18.243 -3.843  16.754  1.00 11.93 ? 146 ILE A CD1 1 
ATOM   1171 N  N   . PHE A 1 146 ? -15.007 -8.543  18.387  1.00 10.15 ? 147 PHE A N   1 
ATOM   1172 C  CA  . PHE A 1 146 ? -14.346 -9.789  17.994  1.00 9.78  ? 147 PHE A CA  1 
ATOM   1173 C  C   . PHE A 1 146 ? -15.119 -10.446 16.855  1.00 10.60 ? 147 PHE A C   1 
ATOM   1174 O  O   . PHE A 1 146 ? -16.347 -10.302 16.751  1.00 10.85 ? 147 PHE A O   1 
ATOM   1175 C  CB  . PHE A 1 146 ? -14.358 -10.737 19.178  1.00 9.92  ? 147 PHE A CB  1 
ATOM   1176 C  CG  . PHE A 1 146 ? -13.506 -10.262 20.316  1.00 8.61  ? 147 PHE A CG  1 
ATOM   1177 C  CD1 . PHE A 1 146 ? -12.136 -10.095 20.130  1.00 9.38  ? 147 PHE A CD1 1 
ATOM   1178 C  CD2 . PHE A 1 146 ? -14.020 -10.078 21.579  1.00 9.49  ? 147 PHE A CD2 1 
ATOM   1179 C  CE1 . PHE A 1 146 ? -11.309 -9.700  21.169  1.00 8.30  ? 147 PHE A CE1 1 
ATOM   1180 C  CE2 . PHE A 1 146 ? -13.216 -9.709  22.642  1.00 9.14  ? 147 PHE A CE2 1 
ATOM   1181 C  CZ  . PHE A 1 146 ? -11.843 -9.553  22.455  1.00 8.37  ? 147 PHE A CZ  1 
ATOM   1182 N  N   . LEU A 1 147 ? -14.390 -11.111 15.965  1.00 11.12 ? 148 LEU A N   1 
ATOM   1183 C  CA  . LEU A 1 147 ? -14.973 -11.952 14.927  1.00 10.59 ? 148 LEU A CA  1 
ATOM   1184 C  C   . LEU A 1 147 ? -14.632 -13.421 15.166  1.00 11.45 ? 148 LEU A C   1 
ATOM   1185 O  O   . LEU A 1 147 ? -13.456 -13.790 15.294  1.00 11.28 ? 148 LEU A O   1 
ATOM   1186 C  CB  . LEU A 1 147 ? -14.444 -11.565 13.532  1.00 10.86 ? 148 LEU A CB  1 
ATOM   1187 C  CG  . LEU A 1 147 ? -14.930 -10.256 12.890  1.00 10.53 ? 148 LEU A CG  1 
ATOM   1188 C  CD1 . LEU A 1 147 ? -14.736 -9.018  13.780  1.00 11.66 ? 148 LEU A CD1 1 
ATOM   1189 C  CD2 . LEU A 1 147 ? -14.300 -10.062 11.485  1.00 12.08 ? 148 LEU A CD2 1 
ATOM   1190 N  N   . LYS A 1 148 ? -15.676 -14.262 15.104  1.00 12.28 ? 149 LYS A N   1 
ATOM   1191 C  CA  . LYS A 1 148 ? -15.536 -15.708 15.051  1.00 13.53 ? 149 LYS A CA  1 
ATOM   1192 C  C   . LYS A 1 148 ? -16.001 -16.203 13.686  1.00 13.23 ? 149 LYS A C   1 
ATOM   1193 O  O   . LYS A 1 148 ? -16.812 -15.553 13.031  1.00 12.74 ? 149 LYS A O   1 
ATOM   1194 C  CB  . LYS A 1 148 ? -16.303 -16.437 16.160  1.00 16.03 ? 149 LYS A CB  1 
ATOM   1195 C  CG  . LYS A 1 148 ? -17.822 -16.327 16.142  1.00 18.62 ? 149 LYS A CG  1 
ATOM   1196 C  CD  . LYS A 1 148 ? -18.392 -17.086 17.338  1.00 22.56 ? 149 LYS A CD  1 
ATOM   1197 C  CE  . LYS A 1 148 ? -19.906 -17.084 17.407  1.00 28.98 ? 149 LYS A CE  1 
ATOM   1198 N  NZ  . LYS A 1 148 ? -20.391 -17.421 18.775  1.00 34.17 ? 149 LYS A NZ  1 
ATOM   1199 N  N   . VAL A 1 149 ? -15.501 -17.378 13.295  1.00 13.37 ? 150 VAL A N   1 
ATOM   1200 C  CA  . VAL A 1 149 ? -15.892 -17.930 12.012  1.00 12.99 ? 150 VAL A CA  1 
ATOM   1201 C  C   . VAL A 1 149 ? -17.096 -18.846 12.258  1.00 13.66 ? 150 VAL A C   1 
ATOM   1202 O  O   . VAL A 1 149 ? -17.088 -19.784 13.082  1.00 13.35 ? 150 VAL A O   1 
ATOM   1203 C  CB  . VAL A 1 149 ? -14.699 -18.671 11.378  1.00 12.93 ? 150 VAL A CB  1 
ATOM   1204 C  CG1 . VAL A 1 149 ? -15.044 -19.461 10.118  1.00 13.75 ? 150 VAL A CG1 1 
ATOM   1205 C  CG2 . VAL A 1 149 ? -13.598 -17.685 11.062  1.00 14.36 ? 150 VAL A CG2 1 
ATOM   1206 N  N   . GLY A 1 150 ? -18.110 -18.581 11.444  1.00 12.59 ? 151 GLY A N   1 
ATOM   1207 C  CA  . GLY A 1 150 ? -19.338 -19.355 11.495  1.00 14.35 ? 151 GLY A CA  1 
ATOM   1208 C  C   . GLY A 1 150 ? -20.257 -18.953 10.358  1.00 13.76 ? 151 GLY A C   1 
ATOM   1209 O  O   . GLY A 1 150 ? -19.850 -19.084 9.201   1.00 13.51 ? 151 GLY A O   1 
ATOM   1210 N  N   . SER A 1 151 ? -21.468 -18.444 10.717  1.00 15.87 ? 152 SER A N   1 
ATOM   1211 C  CA  . SER A 1 151 ? -22.396 -17.853 9.736   1.00 17.08 ? 152 SER A CA  1 
ATOM   1212 C  C   . SER A 1 151 ? -21.784 -16.584 9.124   1.00 18.71 ? 152 SER A C   1 
ATOM   1213 O  O   . SER A 1 151 ? -20.953 -15.942 9.772   1.00 16.74 ? 152 SER A O   1 
ATOM   1214 C  CB  . SER A 1 151 ? -23.708 -17.491 10.392  1.00 22.07 ? 152 SER A CB  1 
ATOM   1215 O  OG  . SER A 1 151 ? -24.279 -18.630 11.008  1.00 30.27 ? 152 SER A OG  1 
ATOM   1216 N  N   . ALA A 1 152 ? -22.123 -16.238 7.869   1.00 17.75 ? 153 ALA A N   1 
ATOM   1217 C  CA  . ALA A 1 152 ? -21.630 -15.009 7.253   1.00 14.92 ? 153 ALA A CA  1 
ATOM   1218 C  C   . ALA A 1 152 ? -22.216 -13.791 7.957   1.00 15.20 ? 153 ALA A C   1 
ATOM   1219 O  O   . ALA A 1 152 ? -23.303 -13.883 8.497   1.00 15.76 ? 153 ALA A O   1 
ATOM   1220 C  CB  . ALA A 1 152 ? -21.994 -14.978 5.775   1.00 15.29 ? 153 ALA A CB  1 
ATOM   1221 N  N   . LYS A 1 153 ? -21.522 -12.642 7.885   1.00 14.21 ? 154 LYS A N   1 
ATOM   1222 C  CA  . LYS A 1 153 ? -22.091 -11.380 8.319   1.00 16.49 ? 154 LYS A CA  1 
ATOM   1223 C  C   . LYS A 1 153 ? -22.474 -10.635 7.046   1.00 14.65 ? 154 LYS A C   1 
ATOM   1224 O  O   . LYS A 1 153 ? -21.626 -10.211 6.283   1.00 14.00 ? 154 LYS A O   1 
ATOM   1225 C  CB  . LYS A 1 153 ? -21.063 -10.598 9.158   1.00 17.10 ? 154 LYS A CB  1 
ATOM   1226 C  CG  . LYS A 1 153 ? -21.650 -9.428  9.948   1.00 18.15 ? 154 LYS A CG  1 
ATOM   1227 C  CD  . LYS A 1 153 ? -22.615 -9.849  11.045  1.00 19.76 ? 154 LYS A CD  1 
ATOM   1228 C  CE  . LYS A 1 153 ? -22.937 -8.781  12.092  1.00 19.83 ? 154 LYS A CE  1 
ATOM   1229 N  NZ  . LYS A 1 153 ? -24.227 -9.017  12.790  1.00 25.36 ? 154 LYS A NZ  1 
ATOM   1230 N  N   . PRO A 1 154 ? -23.787 -10.486 6.751   1.00 16.02 ? 155 PRO A N   1 
ATOM   1231 C  CA  . PRO A 1 154 ? -24.194 -9.931  5.451   1.00 17.41 ? 155 PRO A CA  1 
ATOM   1232 C  C   . PRO A 1 154 ? -23.649 -8.523  5.302   1.00 16.10 ? 155 PRO A C   1 
ATOM   1233 O  O   . PRO A 1 154 ? -23.247 -8.123  4.223   1.00 16.63 ? 155 PRO A O   1 
ATOM   1234 C  CB  . PRO A 1 154 ? -25.741 -9.878  5.552   1.00 19.46 ? 155 PRO A CB  1 
ATOM   1235 C  CG  . PRO A 1 154 ? -26.078 -10.990 6.535   1.00 20.31 ? 155 PRO A CG  1 
ATOM   1236 C  CD  . PRO A 1 154 ? -24.925 -10.996 7.523   1.00 17.59 ? 155 PRO A CD  1 
ATOM   1237 N  N   . GLY A 1 155 ? -23.573 -7.829  6.429   1.00 15.95 ? 156 GLY A N   1 
ATOM   1238 C  CA  . GLY A 1 155 ? -23.217 -6.418  6.404   1.00 16.95 ? 156 GLY A CA  1 
ATOM   1239 C  C   . GLY A 1 155 ? -21.730 -6.191  6.181   1.00 17.19 ? 156 GLY A C   1 
ATOM   1240 O  O   . GLY A 1 155 ? -21.305 -5.045  5.987   1.00 18.51 ? 156 GLY A O   1 
ATOM   1241 N  N   . LEU A 1 156 ? -20.944 -7.281  6.234   1.00 14.99 ? 157 LEU A N   1 
ATOM   1242 C  CA  . LEU A 1 156 ? -19.513 -7.222  5.950   1.00 14.46 ? 157 LEU A CA  1 
ATOM   1243 C  C   . LEU A 1 156 ? -19.213 -7.405  4.465   1.00 13.20 ? 157 LEU A C   1 
ATOM   1244 O  O   . LEU A 1 156 ? -18.092 -7.164  4.001   1.00 13.92 ? 157 LEU A O   1 
ATOM   1245 C  CB  . LEU A 1 156 ? -18.776 -8.241  6.834   1.00 15.47 ? 157 LEU A CB  1 
ATOM   1246 C  CG  . LEU A 1 156 ? -17.262 -8.377  6.583   1.00 13.47 ? 157 LEU A CG  1 
ATOM   1247 C  CD1 . LEU A 1 156 ? -16.520 -7.078  6.945   1.00 14.49 ? 157 LEU A CD1 1 
ATOM   1248 C  CD2 . LEU A 1 156 ? -16.659 -9.523  7.397   1.00 13.87 ? 157 LEU A CD2 1 
ATOM   1249 N  N   . GLN A 1 157 ? -20.202 -7.910  3.697   1.00 14.79 ? 158 GLN A N   1 
ATOM   1250 C  CA  . GLN A 1 157 ? -19.875 -8.396  2.367   1.00 15.82 ? 158 GLN A CA  1 
ATOM   1251 C  C   . GLN A 1 157 ? -19.449 -7.298  1.405   1.00 14.82 ? 158 GLN A C   1 
ATOM   1252 O  O   . GLN A 1 157 ? -18.517 -7.506  0.620   1.00 15.68 ? 158 GLN A O   1 
ATOM   1253 C  CB  . GLN A 1 157 ? -21.024 -9.229  1.817   1.00 16.16 ? 158 GLN A CB  1 
ATOM   1254 C  CG  . GLN A 1 157 ? -20.622 -9.894  0.498   1.00 18.05 ? 158 GLN A CG  1 
ATOM   1255 C  CD  . GLN A 1 157 ? -19.615 -11.008 0.760   1.00 18.66 ? 158 GLN A CD  1 
ATOM   1256 O  OE1 . GLN A 1 157 ? -19.575 -11.616 1.839   1.00 19.72 ? 158 GLN A OE1 1 
ATOM   1257 N  NE2 . GLN A 1 157 ? -18.792 -11.305 -0.223  1.00 18.94 ? 158 GLN A NE2 1 
ATOM   1258 N  N   . LYS A 1 158 ? -20.091 -6.114  1.496   1.00 18.60 ? 159 LYS A N   1 
ATOM   1259 C  CA  . LYS A 1 158 ? -19.650 -4.965  0.713   1.00 19.02 ? 159 LYS A CA  1 
ATOM   1260 C  C   . LYS A 1 158 ? -18.151 -4.695  0.906   1.00 19.29 ? 159 LYS A C   1 
ATOM   1261 O  O   . LYS A 1 158 ? -17.451 -4.367  -0.029  1.00 17.36 ? 159 LYS A O   1 
ATOM   1262 C  CB  . LYS A 1 158 ? -20.650 -3.815  0.915   1.00 24.33 ? 159 LYS A CB  1 
ATOM   1263 C  CG  . LYS A 1 158 ? -20.392 -2.545  0.103   1.00 34.41 ? 159 LYS A CG  1 
ATOM   1264 C  CD  . LYS A 1 158 ? -20.769 -2.638  -1.390  1.00 40.53 ? 159 LYS A CD  1 
ATOM   1265 C  CE  . LYS A 1 158 ? -20.335 -1.455  -2.249  1.00 42.24 ? 159 LYS A CE  1 
ATOM   1266 N  NZ  . LYS A 1 158 ? -21.111 -0.229  -1.940  1.00 45.15 ? 159 LYS A NZ  1 
ATOM   1267 N  N   . VAL A 1 159 ? -17.627 -4.826  2.133   1.00 16.34 ? 160 VAL A N   1 
ATOM   1268 C  CA  . VAL A 1 159 ? -16.198 -4.650  2.353   1.00 16.01 ? 160 VAL A CA  1 
ATOM   1269 C  C   . VAL A 1 159 ? -15.379 -5.749  1.662   1.00 15.56 ? 160 VAL A C   1 
ATOM   1270 O  O   . VAL A 1 159 ? -14.357 -5.505  1.038   1.00 15.18 ? 160 VAL A O   1 
ATOM   1271 C  CB  . VAL A 1 159 ? -15.924 -4.667  3.870   1.00 15.23 ? 160 VAL A CB  1 
ATOM   1272 C  CG1 . VAL A 1 159 ? -14.431 -4.801  4.169   1.00 15.93 ? 160 VAL A CG1 1 
ATOM   1273 C  CG2 . VAL A 1 159 ? -16.528 -3.441  4.533   1.00 17.11 ? 160 VAL A CG2 1 
ATOM   1274 N  N   . VAL A 1 160 ? -15.794 -7.001  1.846   1.00 15.07 ? 161 VAL A N   1 
ATOM   1275 C  CA  . VAL A 1 160 ? -15.031 -8.129  1.341   1.00 15.99 ? 161 VAL A CA  1 
ATOM   1276 C  C   . VAL A 1 160 ? -14.955 -8.036  -0.199  1.00 14.84 ? 161 VAL A C   1 
ATOM   1277 O  O   . VAL A 1 160 ? -13.921 -8.294  -0.811  1.00 15.11 ? 161 VAL A O   1 
ATOM   1278 C  CB  . VAL A 1 160 ? -15.736 -9.432  1.796   1.00 17.14 ? 161 VAL A CB  1 
ATOM   1279 C  CG1 . VAL A 1 160 ? -15.386 -10.604 0.897   1.00 19.81 ? 161 VAL A CG1 1 
ATOM   1280 C  CG2 . VAL A 1 160 ? -15.505 -9.769  3.268   1.00 17.43 ? 161 VAL A CG2 1 
ATOM   1281 N  N   . ASP A 1 161 ? -16.035 -7.555  -0.806  1.00 18.06 ? 162 ASP A N   1 
ATOM   1282 C  CA  . ASP A 1 161 ? -16.151 -7.555  -2.268  1.00 20.03 ? 162 ASP A CA  1 
ATOM   1283 C  C   . ASP A 1 161 ? -15.257 -6.501  -2.932  1.00 22.40 ? 162 ASP A C   1 
ATOM   1284 O  O   . ASP A 1 161 ? -14.955 -6.611  -4.126  1.00 26.98 ? 162 ASP A O   1 
ATOM   1285 C  CB  . ASP A 1 161 ? -17.632 -7.486  -2.678  1.00 23.80 ? 162 ASP A CB  1 
ATOM   1286 C  CG  . ASP A 1 161 ? -18.289 -8.858  -2.681  1.00 22.74 ? 162 ASP A CG  1 
ATOM   1287 O  OD1 . ASP A 1 161 ? -17.545 -9.869  -2.837  1.00 24.24 ? 162 ASP A OD1 1 
ATOM   1288 O  OD2 . ASP A 1 161 ? -19.532 -8.911  -2.524  1.00 25.20 ? 162 ASP A OD2 1 
ATOM   1289 N  N   . VAL A 1 162 ? -14.794 -5.489  -2.184  1.00 18.58 ? 163 VAL A N   1 
ATOM   1290 C  CA  . VAL A 1 162 ? -13.948 -4.459  -2.776  1.00 18.46 ? 163 VAL A CA  1 
ATOM   1291 C  C   . VAL A 1 162 ? -12.463 -4.791  -2.655  1.00 16.27 ? 163 VAL A C   1 
ATOM   1292 O  O   . VAL A 1 162 ? -11.616 -4.131  -3.252  1.00 17.19 ? 163 VAL A O   1 
ATOM   1293 C  CB  . VAL A 1 162 ? -14.257 -3.064  -2.198  1.00 20.41 ? 163 VAL A CB  1 
ATOM   1294 C  CG1 . VAL A 1 162 ? -13.539 -2.825  -0.878  1.00 20.34 ? 163 VAL A CG1 1 
ATOM   1295 C  CG2 . VAL A 1 162 ? -13.913 -1.943  -3.170  1.00 22.58 ? 163 VAL A CG2 1 
ATOM   1296 N  N   . LEU A 1 163 ? -12.096 -5.792  -1.821  1.00 17.20 ? 164 LEU A N   1 
ATOM   1297 C  CA  . LEU A 1 163 ? -10.693 -6.001  -1.489  1.00 18.09 ? 164 LEU A CA  1 
ATOM   1298 C  C   . LEU A 1 163 ? -9.824  -6.320  -2.708  1.00 19.16 ? 164 LEU A C   1 
ATOM   1299 O  O   . LEU A 1 163 ? -8.659  -5.942  -2.711  1.00 18.74 ? 164 LEU A O   1 
ATOM   1300 C  CB  . LEU A 1 163 ? -10.516 -7.049  -0.388  1.00 16.29 ? 164 LEU A CB  1 
ATOM   1301 C  CG  . LEU A 1 163 ? -11.195 -6.725  0.946   1.00 18.36 ? 164 LEU A CG  1 
ATOM   1302 C  CD1 . LEU A 1 163 ? -11.122 -7.939  1.867   1.00 18.18 ? 164 LEU A CD1 1 
ATOM   1303 C  CD2 . LEU A 1 163 ? -10.562 -5.489  1.601   1.00 15.90 ? 164 LEU A CD2 1 
ATOM   1304 N  N   . ASP A 1 164 ? -10.360 -7.085  -3.675  1.00 21.68 ? 165 ASP A N   1 
ATOM   1305 C  CA  . ASP A 1 164 ? -9.652  -7.361  -4.918  1.00 24.98 ? 165 ASP A CA  1 
ATOM   1306 C  C   . ASP A 1 164 ? -9.032  -6.087  -5.521  1.00 27.32 ? 165 ASP A C   1 
ATOM   1307 O  O   . ASP A 1 164 ? -7.941  -6.148  -6.086  1.00 27.42 ? 165 ASP A O   1 
ATOM   1308 C  CB  . ASP A 1 164 ? -10.543 -8.138  -5.901  1.00 26.57 ? 165 ASP A CB  1 
ATOM   1309 C  CG  . ASP A 1 164 ? -11.539 -7.291  -6.672  1.00 31.06 ? 165 ASP A CG  1 
ATOM   1310 O  OD1 . ASP A 1 164 ? -12.542 -6.802  -6.068  1.00 26.86 ? 165 ASP A OD1 1 
ATOM   1311 O  OD2 . ASP A 1 164 ? -11.311 -7.113  -7.892  1.00 37.68 ? 165 ASP A OD2 1 
ATOM   1312 N  N   . SER A 1 165 ? -9.719  -4.948  -5.381  1.00 23.69 ? 166 SER A N   1 
ATOM   1313 C  CA  . SER A 1 165 ? -9.322  -3.684  -5.989  1.00 25.25 ? 166 SER A CA  1 
ATOM   1314 C  C   . SER A 1 165 ? -8.214  -2.972  -5.209  1.00 24.45 ? 166 SER A C   1 
ATOM   1315 O  O   . SER A 1 165 ? -7.599  -2.032  -5.728  1.00 21.52 ? 166 SER A O   1 
ATOM   1316 C  CB  . SER A 1 165 ? -10.515 -2.804  -6.193  1.00 24.72 ? 166 SER A CB  1 
ATOM   1317 O  OG  . SER A 1 165 ? -10.965 -2.262  -4.955  1.00 27.42 ? 166 SER A OG  1 
ATOM   1318 N  N   . ILE A 1 166 ? -7.991  -3.367  -3.937  1.00 19.13 ? 167 ILE A N   1 
ATOM   1319 C  CA  . ILE A 1 166 ? -6.937  -2.753  -3.131  1.00 20.70 ? 167 ILE A CA  1 
ATOM   1320 C  C   . ILE A 1 166 ? -5.954  -3.823  -2.632  1.00 19.22 ? 167 ILE A C   1 
ATOM   1321 O  O   . ILE A 1 166 ? -5.594  -3.893  -1.437  1.00 17.90 ? 167 ILE A O   1 
ATOM   1322 C  CB  . ILE A 1 166 ? -7.565  -1.931  -1.980  1.00 18.87 ? 167 ILE A CB  1 
ATOM   1323 C  CG1 . ILE A 1 166 ? -8.388  -2.834  -1.059  1.00 17.13 ? 167 ILE A CG1 1 
ATOM   1324 C  CG2 . ILE A 1 166 ? -8.436  -0.779  -2.496  1.00 21.50 ? 167 ILE A CG2 1 
ATOM   1325 C  CD1 . ILE A 1 166 ? -8.398  -2.367  0.367   1.00 17.36 ? 167 ILE A CD1 1 
ATOM   1326 N  N   . LYS A 1 167 ? -5.534  -4.719  -3.537  1.00 19.55 ? 168 LYS A N   1 
ATOM   1327 C  CA  . LYS A 1 167 ? -4.732  -5.873  -3.140  1.00 19.56 ? 168 LYS A CA  1 
ATOM   1328 C  C   . LYS A 1 167 ? -3.414  -5.509  -2.448  1.00 19.24 ? 168 LYS A C   1 
ATOM   1329 O  O   . LYS A 1 167 ? -2.991  -6.214  -1.538  1.00 17.08 ? 168 LYS A O   1 
ATOM   1330 C  CB  . LYS A 1 167 ? -4.439  -6.799  -4.326  1.00 19.68 ? 168 LYS A CB  1 
ATOM   1331 C  CG  . LYS A 1 167 ? -3.720  -8.090  -3.990  1.00 21.60 ? 168 LYS A CG  1 
ATOM   1332 C  CD  . LYS A 1 167 ? -3.634  -9.023  -5.208  1.00 26.00 ? 168 LYS A CD  1 
ATOM   1333 C  CE  . LYS A 1 167 ? -2.337  -9.802  -5.278  1.00 33.46 ? 168 LYS A CE  1 
ATOM   1334 N  NZ  . LYS A 1 167 ? -2.525  -11.255 -5.537  1.00 34.50 ? 168 LYS A NZ  1 
ATOM   1335 N  N   . THR A 1 168 ? -2.724  -4.465  -2.939  1.00 16.15 ? 169 THR A N   1 
ATOM   1336 C  CA  . THR A 1 168 ? -1.331  -4.242  -2.551  1.00 17.50 ? 169 THR A CA  1 
ATOM   1337 C  C   . THR A 1 168 ? -1.219  -2.905  -1.835  1.00 15.70 ? 169 THR A C   1 
ATOM   1338 O  O   . THR A 1 168 ? -2.079  -2.082  -2.034  1.00 16.19 ? 169 THR A O   1 
ATOM   1339 C  CB  . THR A 1 168 ? -0.365  -4.383  -3.744  1.00 18.39 ? 169 THR A CB  1 
ATOM   1340 O  OG1 . THR A 1 168 ? -0.909  -3.604  -4.801  1.00 22.41 ? 169 THR A OG1 1 
ATOM   1341 C  CG2 . THR A 1 168 ? -0.152  -5.832  -4.151  1.00 16.69 ? 169 THR A CG2 1 
ATOM   1342 N  N   . LYS A 1 169 ? -0.153  -2.751  -1.041  1.00 19.84 ? 170 LYS A N   1 
ATOM   1343 C  CA  . LYS A 1 169 ? 0.220   -1.561  -0.275  1.00 19.14 ? 170 LYS A CA  1 
ATOM   1344 C  C   . LYS A 1 169 ? 0.129   -0.336  -1.169  1.00 22.61 ? 170 LYS A C   1 
ATOM   1345 O  O   . LYS A 1 169 ? 0.746   -0.318  -2.248  1.00 27.71 ? 170 LYS A O   1 
ATOM   1346 C  CB  . LYS A 1 169 ? 1.616   -1.736  0.323   1.00 20.40 ? 170 LYS A CB  1 
ATOM   1347 C  CG  . LYS A 1 169 ? 2.198   -0.568  1.146   1.00 20.57 ? 170 LYS A CG  1 
ATOM   1348 C  CD  . LYS A 1 169 ? 3.631   -0.860  1.524   1.00 26.32 ? 170 LYS A CD  1 
ATOM   1349 C  CE  . LYS A 1 169 ? 4.181   0.015   2.634   1.00 33.89 ? 170 LYS A CE  1 
ATOM   1350 N  NZ  . LYS A 1 169 ? 5.186   0.963   2.095   1.00 35.15 ? 170 LYS A NZ  1 
ATOM   1351 N  N   . GLY A 1 170 ? -0.640  0.646   -0.710  1.00 19.87 ? 171 GLY A N   1 
ATOM   1352 C  CA  . GLY A 1 170 ? -0.777  1.929   -1.376  1.00 22.38 ? 171 GLY A CA  1 
ATOM   1353 C  C   . GLY A 1 170 ? -2.002  2.049   -2.270  1.00 24.02 ? 171 GLY A C   1 
ATOM   1354 O  O   . GLY A 1 170 ? -2.310  3.141   -2.749  1.00 26.24 ? 171 GLY A O   1 
ATOM   1355 N  N   . LYS A 1 171 ? -2.696  0.932   -2.523  1.00 19.55 ? 172 LYS A N   1 
ATOM   1356 C  CA  . LYS A 1 171 ? -3.887  1.012   -3.353  1.00 22.02 ? 172 LYS A CA  1 
ATOM   1357 C  C   . LYS A 1 171 ? -5.090  1.494   -2.560  1.00 21.38 ? 172 LYS A C   1 
ATOM   1358 O  O   . LYS A 1 171 ? -5.339  1.076   -1.428  1.00 21.61 ? 172 LYS A O   1 
ATOM   1359 C  CB  . LYS A 1 171 ? -4.191  -0.335  -4.026  1.00 23.48 ? 172 LYS A CB  1 
ATOM   1360 C  CG  . LYS A 1 171 ? -3.203  -0.766  -5.099  1.00 27.36 ? 172 LYS A CG  1 
ATOM   1361 C  CD  . LYS A 1 171 ? -3.743  -1.750  -6.124  1.00 32.25 ? 172 LYS A CD  1 
ATOM   1362 C  CE  . LYS A 1 171 ? -4.689  -1.105  -7.124  1.00 38.81 ? 172 LYS A CE  1 
ATOM   1363 N  NZ  . LYS A 1 171 ? -5.307  -2.083  -8.061  1.00 37.86 ? 172 LYS A NZ  1 
ATOM   1364 N  N   A SER A 1 172 ? -5.895  2.330   -3.199  0.50 20.46 ? 173 SER A N   1 
ATOM   1365 N  N   B SER A 1 172 ? -5.872  2.372   -3.180  0.50 21.12 ? 173 SER A N   1 
ATOM   1366 C  CA  A SER A 1 172 ? -7.070  2.884   -2.560  0.50 20.50 ? 173 SER A CA  1 
ATOM   1367 C  CA  B SER A 1 172 ? -7.078  2.896   -2.565  0.50 21.60 ? 173 SER A CA  1 
ATOM   1368 C  C   A SER A 1 172 ? -8.228  2.923   -3.552  0.50 22.95 ? 173 SER A C   1 
ATOM   1369 C  C   B SER A 1 172 ? -8.233  2.871   -3.559  0.50 23.71 ? 173 SER A C   1 
ATOM   1370 O  O   A SER A 1 172 ? -8.006  2.961   -4.765  0.50 22.77 ? 173 SER A O   1 
ATOM   1371 O  O   B SER A 1 172 ? -8.019  2.841   -4.773  0.50 23.32 ? 173 SER A O   1 
ATOM   1372 C  CB  A SER A 1 172 ? -6.740  4.250   -1.994  0.50 20.42 ? 173 SER A CB  1 
ATOM   1373 C  CB  B SER A 1 172 ? -6.844  4.292   -2.012  0.50 22.74 ? 173 SER A CB  1 
ATOM   1374 O  OG  A SER A 1 172 ? -5.967  5.011   -2.916  0.50 15.88 ? 173 SER A OG  1 
ATOM   1375 O  OG  B SER A 1 172 ? -7.250  5.298   -2.938  0.50 18.56 ? 173 SER A OG  1 
ATOM   1376 N  N   . ALA A 1 173 ? -9.457  2.874   -3.030  1.00 22.76 ? 174 ALA A N   1 
ATOM   1377 C  CA  . ALA A 1 173 ? -10.669 2.924   -3.839  1.00 25.37 ? 174 ALA A CA  1 
ATOM   1378 C  C   . ALA A 1 173 ? -11.691 3.831   -3.172  1.00 27.91 ? 174 ALA A C   1 
ATOM   1379 O  O   . ALA A 1 173 ? -11.732 3.907   -1.943  1.00 24.57 ? 174 ALA A O   1 
ATOM   1380 C  CB  . ALA A 1 173 ? -11.263 1.549   -4.045  1.00 25.59 ? 174 ALA A CB  1 
ATOM   1381 N  N   . ASP A 1 174 ? -12.516 4.489   -3.994  1.00 25.42 ? 175 ASP A N   1 
ATOM   1382 C  CA  . ASP A 1 174 ? -13.740 5.095   -3.488  1.00 28.61 ? 175 ASP A CA  1 
ATOM   1383 C  C   . ASP A 1 174 ? -14.563 4.022   -2.777  1.00 27.20 ? 175 ASP A C   1 
ATOM   1384 O  O   . ASP A 1 174 ? -14.598 2.891   -3.249  1.00 25.05 ? 175 ASP A O   1 
ATOM   1385 C  CB  . ASP A 1 174 ? -14.622 5.673   -4.606  1.00 35.42 ? 175 ASP A CB  1 
ATOM   1386 C  CG  . ASP A 1 174 ? -13.986 6.796   -5.413  1.00 43.86 ? 175 ASP A CG  1 
ATOM   1387 O  OD1 . ASP A 1 174 ? -13.252 7.630   -4.817  1.00 42.83 ? 175 ASP A OD1 1 
ATOM   1388 O  OD2 . ASP A 1 174 ? -14.246 6.840   -6.649  1.00 47.17 ? 175 ASP A OD2 1 
ATOM   1389 N  N   . PHE A 1 175 ? -15.180 4.379   -1.631  1.00 22.35 ? 176 PHE A N   1 
ATOM   1390 C  CA  . PHE A 1 175 ? -16.012 3.467   -0.842  1.00 22.44 ? 176 PHE A CA  1 
ATOM   1391 C  C   . PHE A 1 175 ? -17.056 4.260   -0.070  1.00 23.85 ? 176 PHE A C   1 
ATOM   1392 O  O   . PHE A 1 175 ? -16.831 4.620   1.097   1.00 26.43 ? 176 PHE A O   1 
ATOM   1393 C  CB  . PHE A 1 175 ? -15.152 2.619   0.106   1.00 19.70 ? 176 PHE A CB  1 
ATOM   1394 C  CG  . PHE A 1 175 ? -15.810 1.361   0.614   1.00 21.24 ? 176 PHE A CG  1 
ATOM   1395 C  CD1 . PHE A 1 175 ? -16.141 0.328   -0.251  1.00 19.32 ? 176 PHE A CD1 1 
ATOM   1396 C  CD2 . PHE A 1 175 ? -16.088 1.195   1.967   1.00 19.43 ? 176 PHE A CD2 1 
ATOM   1397 C  CE1 . PHE A 1 175 ? -16.730 -0.833  0.227   1.00 20.86 ? 176 PHE A CE1 1 
ATOM   1398 C  CE2 . PHE A 1 175 ? -16.687 0.042   2.442   1.00 20.57 ? 176 PHE A CE2 1 
ATOM   1399 C  CZ  . PHE A 1 175 ? -16.988 -0.984  1.575   1.00 21.38 ? 176 PHE A CZ  1 
ATOM   1400 N  N   . THR A 1 176 ? -18.173 4.550   -0.747  1.00 19.34 ? 177 THR A N   1 
ATOM   1401 C  CA  . THR A 1 176 ? -19.255 5.372   -0.249  1.00 18.85 ? 177 THR A CA  1 
ATOM   1402 C  C   . THR A 1 176 ? -20.462 4.528   0.133   1.00 18.20 ? 177 THR A C   1 
ATOM   1403 O  O   . THR A 1 176 ? -20.617 3.375   -0.301  1.00 20.32 ? 177 THR A O   1 
ATOM   1404 C  CB  . THR A 1 176 ? -19.656 6.460   -1.259  1.00 20.94 ? 177 THR A CB  1 
ATOM   1405 O  OG1 . THR A 1 176 ? -20.043 5.818   -2.481  1.00 25.46 ? 177 THR A OG1 1 
ATOM   1406 C  CG2 . THR A 1 176 ? -18.541 7.449   -1.508  1.00 23.22 ? 177 THR A CG2 1 
ATOM   1407 N  N   . ASN A 1 177 ? -21.285 5.114   1.004   1.00 17.60 ? 178 ASN A N   1 
ATOM   1408 C  CA  . ASN A 1 177 ? -22.555 4.565   1.425   1.00 18.24 ? 178 ASN A CA  1 
ATOM   1409 C  C   . ASN A 1 177 ? -22.357 3.258   2.213   1.00 19.34 ? 178 ASN A C   1 
ATOM   1410 O  O   . ASN A 1 177 ? -23.277 2.469   2.234   1.00 20.88 ? 178 ASN A O   1 
ATOM   1411 C  CB  . ASN A 1 177 ? -23.543 4.463   0.247   1.00 19.33 ? 178 ASN A CB  1 
ATOM   1412 C  CG  . ASN A 1 177 ? -23.841 5.831   -0.345  1.00 18.95 ? 178 ASN A CG  1 
ATOM   1413 O  OD1 . ASN A 1 177 ? -24.532 6.611   0.278   1.00 19.39 ? 178 ASN A OD1 1 
ATOM   1414 N  ND2 . ASN A 1 177 ? -23.258 6.154   -1.493  1.00 21.01 ? 178 ASN A ND2 1 
ATOM   1415 N  N   . PHE A 1 178 ? -21.179 3.038   2.846   1.00 18.36 ? 179 PHE A N   1 
ATOM   1416 C  CA  . PHE A 1 178 ? -21.012 1.835   3.660   1.00 16.99 ? 179 PHE A CA  1 
ATOM   1417 C  C   . PHE A 1 178 ? -21.594 2.093   5.049   1.00 17.52 ? 179 PHE A C   1 
ATOM   1418 O  O   . PHE A 1 178 ? -21.195 3.065   5.669   1.00 18.24 ? 179 PHE A O   1 
ATOM   1419 C  CB  . PHE A 1 178 ? -19.562 1.382   3.754   1.00 17.06 ? 179 PHE A CB  1 
ATOM   1420 C  CG  . PHE A 1 178 ? -19.503 0.117   4.567   1.00 16.63 ? 179 PHE A CG  1 
ATOM   1421 C  CD1 . PHE A 1 178 ? -20.020 -1.073  4.069   1.00 18.38 ? 179 PHE A CD1 1 
ATOM   1422 C  CD2 . PHE A 1 178 ? -19.114 0.171   5.898   1.00 16.81 ? 179 PHE A CD2 1 
ATOM   1423 C  CE1 . PHE A 1 178 ? -20.043 -2.225  4.835   1.00 19.51 ? 179 PHE A CE1 1 
ATOM   1424 C  CE2 . PHE A 1 178 ? -19.159 -0.983  6.670   1.00 17.24 ? 179 PHE A CE2 1 
ATOM   1425 C  CZ  . PHE A 1 178 ? -19.590 -2.171  6.139   1.00 17.41 ? 179 PHE A CZ  1 
ATOM   1426 N  N   . ASP A 1 179 ? -22.525 1.243   5.519   1.00 16.40 ? 180 ASP A N   1 
ATOM   1427 C  CA  . ASP A 1 179 ? -23.201 1.449   6.792   1.00 17.36 ? 180 ASP A CA  1 
ATOM   1428 C  C   . ASP A 1 179 ? -22.571 0.628   7.923   1.00 17.05 ? 180 ASP A C   1 
ATOM   1429 O  O   . ASP A 1 179 ? -22.762 -0.597  7.970   1.00 15.18 ? 180 ASP A O   1 
ATOM   1430 C  CB  . ASP A 1 179 ? -24.667 1.037   6.705   1.00 19.54 ? 180 ASP A CB  1 
ATOM   1431 C  CG  . ASP A 1 179 ? -25.513 1.443   7.898   1.00 23.48 ? 180 ASP A CG  1 
ATOM   1432 O  OD1 . ASP A 1 179 ? -24.967 1.714   8.978   1.00 20.17 ? 180 ASP A OD1 1 
ATOM   1433 O  OD2 . ASP A 1 179 ? -26.759 1.518   7.736   1.00 28.28 ? 180 ASP A OD2 1 
ATOM   1434 N  N   . PRO A 1 180 ? -21.826 1.232   8.891   1.00 14.19 ? 181 PRO A N   1 
ATOM   1435 C  CA  . PRO A 1 180 ? -21.096 0.441   9.899   1.00 14.88 ? 181 PRO A CA  1 
ATOM   1436 C  C   . PRO A 1 180 ? -22.017 -0.223  10.910  1.00 15.18 ? 181 PRO A C   1 
ATOM   1437 O  O   . PRO A 1 180 ? -21.602 -1.187  11.560  1.00 13.56 ? 181 PRO A O   1 
ATOM   1438 C  CB  . PRO A 1 180 ? -20.113 1.447   10.508  1.00 16.07 ? 181 PRO A CB  1 
ATOM   1439 C  CG  . PRO A 1 180 ? -20.850 2.737   10.402  1.00 17.00 ? 181 PRO A CG  1 
ATOM   1440 C  CD  . PRO A 1 180 ? -21.555 2.680   9.046   1.00 14.84 ? 181 PRO A CD  1 
ATOM   1441 N  N   . ARG A 1 181 ? -23.302 0.139   10.923  1.00 15.11 ? 182 ARG A N   1 
ATOM   1442 C  CA  . ARG A 1 181 ? -24.218 -0.531  11.848  1.00 15.21 ? 182 ARG A CA  1 
ATOM   1443 C  C   . ARG A 1 181 ? -24.312 -2.022  11.530  1.00 16.06 ? 182 ARG A C   1 
ATOM   1444 O  O   . ARG A 1 181 ? -24.692 -2.810  12.385  1.00 18.57 ? 182 ARG A O   1 
ATOM   1445 C  CB  . ARG A 1 181 ? -25.625 0.086   11.795  1.00 15.26 ? 182 ARG A CB  1 
ATOM   1446 C  CG  . ARG A 1 181 ? -25.633 1.521   12.293  1.00 17.76 ? 182 ARG A CG  1 
ATOM   1447 C  CD  . ARG A 1 181 ? -26.987 2.212   12.210  1.00 20.35 ? 182 ARG A CD  1 
ATOM   1448 N  NE  . ARG A 1 181 ? -27.335 2.390   10.828  1.00 20.26 ? 182 ARG A NE  1 
ATOM   1449 C  CZ  . ARG A 1 181 ? -28.385 3.114   10.433  1.00 24.84 ? 182 ARG A CZ  1 
ATOM   1450 N  NH1 . ARG A 1 181 ? -29.132 3.700   11.343  1.00 25.14 ? 182 ARG A NH1 1 
ATOM   1451 N  NH2 . ARG A 1 181 ? -28.673 3.245   9.149   1.00 22.36 ? 182 ARG A NH2 1 
ATOM   1452 N  N   . GLY A 1 182 ? -24.044 -2.393  10.274  1.00 15.36 ? 183 GLY A N   1 
ATOM   1453 C  CA  . GLY A 1 182 ? -24.178 -3.784  9.845   1.00 15.22 ? 183 GLY A CA  1 
ATOM   1454 C  C   . GLY A 1 182 ? -23.061 -4.698  10.353  1.00 17.80 ? 183 GLY A C   1 
ATOM   1455 O  O   . GLY A 1 182 ? -23.110 -5.908  10.111  1.00 19.24 ? 183 GLY A O   1 
ATOM   1456 N  N   . LEU A 1 183 ? -22.066 -4.110  11.033  1.00 15.85 ? 184 LEU A N   1 
ATOM   1457 C  CA  . LEU A 1 183 ? -20.929 -4.831  11.605  1.00 14.00 ? 184 LEU A CA  1 
ATOM   1458 C  C   . LEU A 1 183 ? -21.125 -5.011  13.120  1.00 13.67 ? 184 LEU A C   1 
ATOM   1459 O  O   . LEU A 1 183 ? -20.305 -5.653  13.751  1.00 16.72 ? 184 LEU A O   1 
ATOM   1460 C  CB  . LEU A 1 183 ? -19.655 -4.020  11.354  1.00 13.87 ? 184 LEU A CB  1 
ATOM   1461 C  CG  . LEU A 1 183 ? -19.275 -3.817  9.883   1.00 14.25 ? 184 LEU A CG  1 
ATOM   1462 C  CD1 . LEU A 1 183 ? -18.043 -2.943  9.806   1.00 16.60 ? 184 LEU A CD1 1 
ATOM   1463 C  CD2 . LEU A 1 183 ? -18.999 -5.130  9.188   1.00 17.52 ? 184 LEU A CD2 1 
ATOM   1464 N  N   . LEU A 1 184 ? -22.232 -4.557  13.710  1.00 12.39 ? 185 LEU A N   1 
ATOM   1465 C  CA  . LEU A 1 184 ? -22.354 -4.581  15.177  1.00 13.13 ? 185 LEU A CA  1 
ATOM   1466 C  C   . LEU A 1 184 ? -23.101 -5.834  15.637  1.00 16.31 ? 185 LEU A C   1 
ATOM   1467 O  O   . LEU A 1 184 ? -24.093 -6.249  15.021  1.00 21.43 ? 185 LEU A O   1 
ATOM   1468 C  CB  . LEU A 1 184 ? -23.086 -3.351  15.718  1.00 12.99 ? 185 LEU A CB  1 
ATOM   1469 C  CG  . LEU A 1 184 ? -22.469 -2.018  15.343  1.00 13.11 ? 185 LEU A CG  1 
ATOM   1470 C  CD1 . LEU A 1 184 ? -23.321 -0.876  15.855  1.00 14.28 ? 185 LEU A CD1 1 
ATOM   1471 C  CD2 . LEU A 1 184 ? -21.052 -1.924  15.833  1.00 14.50 ? 185 LEU A CD2 1 
ATOM   1472 N  N   . PRO A 1 185 ? -22.764 -6.402  16.816  1.00 14.63 ? 186 PRO A N   1 
ATOM   1473 C  CA  . PRO A 1 185 ? -23.534 -7.524  17.360  1.00 14.51 ? 186 PRO A CA  1 
ATOM   1474 C  C   . PRO A 1 185 ? -24.808 -6.988  18.038  1.00 16.72 ? 186 PRO A C   1 
ATOM   1475 O  O   . PRO A 1 185 ? -24.988 -5.790  18.148  1.00 15.15 ? 186 PRO A O   1 
ATOM   1476 C  CB  . PRO A 1 185 ? -22.582 -8.096  18.435  1.00 14.12 ? 186 PRO A CB  1 
ATOM   1477 C  CG  . PRO A 1 185 ? -21.819 -6.835  18.913  1.00 13.42 ? 186 PRO A CG  1 
ATOM   1478 C  CD  . PRO A 1 185 ? -21.633 -5.981  17.659  1.00 13.77 ? 186 PRO A CD  1 
ATOM   1479 N  N   . GLU A 1 186 ? -25.675 -7.875  18.560  1.00 18.00 ? 187 GLU A N   1 
ATOM   1480 C  CA  . GLU A 1 186 ? -26.920 -7.457  19.197  1.00 18.50 ? 187 GLU A CA  1 
ATOM   1481 C  C   . GLU A 1 186 ? -26.637 -6.644  20.447  1.00 19.31 ? 187 GLU A C   1 
ATOM   1482 O  O   . GLU A 1 186 ? -27.216 -5.579  20.643  1.00 22.15 ? 187 GLU A O   1 
ATOM   1483 C  CB  . GLU A 1 186 ? -27.724 -8.657  19.712  1.00 18.74 ? 187 GLU A CB  1 
ATOM   1484 C  CG  . GLU A 1 186 ? -28.383 -9.465  18.622  1.00 27.15 ? 187 GLU A CG  1 
ATOM   1485 C  CD  . GLU A 1 186 ? -29.130 -10.689 19.158  1.00 24.36 ? 187 GLU A CD  1 
ATOM   1486 O  OE1 . GLU A 1 186 ? -29.439 -11.565 18.345  1.00 35.80 ? 187 GLU A OE1 1 
ATOM   1487 O  OE2 . GLU A 1 186 ? -29.360 -10.774 20.396  1.00 23.87 ? 187 GLU A OE2 1 
ATOM   1488 N  N   . SER A 1 187 ? -25.775 -7.192  21.319  1.00 17.36 ? 188 SER A N   1 
ATOM   1489 C  CA  . SER A 1 187 ? -25.520 -6.615  22.631  1.00 17.30 ? 188 SER A CA  1 
ATOM   1490 C  C   . SER A 1 187 ? -24.421 -5.557  22.574  1.00 16.57 ? 188 SER A C   1 
ATOM   1491 O  O   . SER A 1 187 ? -23.417 -5.802  21.916  1.00 15.84 ? 188 SER A O   1 
ATOM   1492 C  CB  . SER A 1 187 ? -25.117 -7.664  23.631  1.00 17.15 ? 188 SER A CB  1 
ATOM   1493 O  OG  . SER A 1 187 ? -24.944 -7.101  24.916  1.00 17.03 ? 188 SER A OG  1 
ATOM   1494 N  N   . LEU A 1 188 ? -24.556 -4.493  23.376  1.00 15.79 ? 189 LEU A N   1 
ATOM   1495 C  CA  . LEU A 1 188 ? -23.489 -3.503  23.550  1.00 15.51 ? 189 LEU A CA  1 
ATOM   1496 C  C   . LEU A 1 188 ? -22.872 -3.598  24.950  1.00 14.68 ? 189 LEU A C   1 
ATOM   1497 O  O   . LEU A 1 188 ? -22.224 -2.646  25.402  1.00 17.01 ? 189 LEU A O   1 
ATOM   1498 C  CB  . LEU A 1 188 ? -24.025 -2.083  23.276  1.00 15.83 ? 189 LEU A CB  1 
ATOM   1499 C  CG  . LEU A 1 188 ? -24.400 -1.697  21.842  1.00 17.36 ? 189 LEU A CG  1 
ATOM   1500 C  CD1 . LEU A 1 188 ? -24.847 -0.242  21.818  1.00 19.09 ? 189 LEU A CD1 1 
ATOM   1501 C  CD2 . LEU A 1 188 ? -23.289 -1.935  20.802  1.00 15.93 ? 189 LEU A CD2 1 
ATOM   1502 N  N   . ASP A 1 189 ? -23.050 -4.723  25.661  1.00 17.85 ? 190 ASP A N   1 
ATOM   1503 C  CA  . ASP A 1 189 ? -22.290 -4.963  26.892  1.00 16.40 ? 190 ASP A CA  1 
ATOM   1504 C  C   . ASP A 1 189 ? -20.799 -4.942  26.553  1.00 14.82 ? 190 ASP A C   1 
ATOM   1505 O  O   . ASP A 1 189 ? -20.405 -5.428  25.482  1.00 14.62 ? 190 ASP A O   1 
ATOM   1506 C  CB  . ASP A 1 189 ? -22.582 -6.343  27.500  1.00 18.58 ? 190 ASP A CB  1 
ATOM   1507 C  CG  . ASP A 1 189 ? -23.963 -6.473  28.143  1.00 21.71 ? 190 ASP A CG  1 
ATOM   1508 O  OD1 . ASP A 1 189 ? -24.617 -5.453  28.299  1.00 25.44 ? 190 ASP A OD1 1 
ATOM   1509 O  OD2 . ASP A 1 189 ? -24.369 -7.601  28.390  1.00 21.75 ? 190 ASP A OD2 1 
ATOM   1510 N  N   . TYR A 1 190 ? -19.986 -4.344  27.434  1.00 13.45 ? 191 TYR A N   1 
ATOM   1511 C  CA  . TYR A 1 190 ? -18.584 -4.092  27.078  1.00 12.59 ? 191 TYR A CA  1 
ATOM   1512 C  C   . TYR A 1 190 ? -17.692 -4.200  28.304  1.00 12.43 ? 191 TYR A C   1 
ATOM   1513 O  O   . TYR A 1 190 ? -18.124 -4.057  29.453  1.00 12.66 ? 191 TYR A O   1 
ATOM   1514 C  CB  . TYR A 1 190 ? -18.444 -2.702  26.431  1.00 14.31 ? 191 TYR A CB  1 
ATOM   1515 C  CG  . TYR A 1 190 ? -18.852 -1.545  27.320  1.00 13.85 ? 191 TYR A CG  1 
ATOM   1516 C  CD1 . TYR A 1 190 ? -17.970 -0.975  28.232  1.00 16.16 ? 191 TYR A CD1 1 
ATOM   1517 C  CD2 . TYR A 1 190 ? -20.141 -1.025  27.283  1.00 14.17 ? 191 TYR A CD2 1 
ATOM   1518 C  CE1 . TYR A 1 190 ? -18.350 0.097   29.044  1.00 15.41 ? 191 TYR A CE1 1 
ATOM   1519 C  CE2 . TYR A 1 190 ? -20.550 0.030   28.100  1.00 15.34 ? 191 TYR A CE2 1 
ATOM   1520 C  CZ  . TYR A 1 190 ? -19.653 0.572   29.008  1.00 16.72 ? 191 TYR A CZ  1 
ATOM   1521 O  OH  . TYR A 1 190 ? -20.038 1.623   29.809  1.00 16.08 ? 191 TYR A OH  1 
ATOM   1522 N  N   . TRP A 1 191 ? -16.392 -4.378  28.044  1.00 11.99 ? 192 TRP A N   1 
ATOM   1523 C  CA  . TRP A 1 191 ? -15.314 -4.137  28.995  1.00 10.97 ? 192 TRP A CA  1 
ATOM   1524 C  C   . TRP A 1 191 ? -14.630 -2.844  28.583  1.00 10.97 ? 192 TRP A C   1 
ATOM   1525 O  O   . TRP A 1 191 ? -14.667 -2.523  27.376  1.00 11.07 ? 192 TRP A O   1 
ATOM   1526 C  CB  . TRP A 1 191 ? -14.289 -5.260  28.897  1.00 11.77 ? 192 TRP A CB  1 
ATOM   1527 C  CG  . TRP A 1 191 ? -14.812 -6.592  29.331  1.00 11.74 ? 192 TRP A CG  1 
ATOM   1528 C  CD1 . TRP A 1 191 ? -15.035 -7.031  30.614  1.00 11.60 ? 192 TRP A CD1 1 
ATOM   1529 C  CD2 . TRP A 1 191 ? -15.041 -7.722  28.478  1.00 11.45 ? 192 TRP A CD2 1 
ATOM   1530 N  NE1 . TRP A 1 191 ? -15.462 -8.335  30.585  1.00 12.33 ? 192 TRP A NE1 1 
ATOM   1531 C  CE2 . TRP A 1 191 ? -15.482 -8.777  29.290  1.00 11.81 ? 192 TRP A CE2 1 
ATOM   1532 C  CE3 . TRP A 1 191 ? -14.972 -7.912  27.082  1.00 11.23 ? 192 TRP A CE3 1 
ATOM   1533 C  CZ2 . TRP A 1 191 ? -15.797 -10.031 28.768  1.00 12.80 ? 192 TRP A CZ2 1 
ATOM   1534 C  CZ3 . TRP A 1 191 ? -15.286 -9.148  26.565  1.00 12.58 ? 192 TRP A CZ3 1 
ATOM   1535 C  CH2 . TRP A 1 191 ? -15.693 -10.201 27.398  1.00 13.50 ? 192 TRP A CH2 1 
ATOM   1536 N  N   . THR A 1 192 ? -14.008 -2.130  29.535  1.00 9.70  ? 193 THR A N   1 
ATOM   1537 C  CA  . THR A 1 192 ? -13.369 -0.868  29.179  1.00 11.22 ? 193 THR A CA  1 
ATOM   1538 C  C   . THR A 1 192 ? -12.121 -0.661  30.045  1.00 11.96 ? 193 THR A C   1 
ATOM   1539 O  O   . THR A 1 192 ? -12.101 -1.055  31.210  1.00 13.68 ? 193 THR A O   1 
ATOM   1540 C  CB  . THR A 1 192 ? -14.294 0.365   29.267  1.00 11.34 ? 193 THR A CB  1 
ATOM   1541 O  OG1 . THR A 1 192 ? -13.580 1.543   28.814  1.00 11.77 ? 193 THR A OG1 1 
ATOM   1542 C  CG2 . THR A 1 192 ? -14.762 0.594   30.702  1.00 11.13 ? 193 THR A CG2 1 
ATOM   1543 N  N   . TYR A 1 193 ? -11.051 -0.101  29.476  1.00 12.80 ? 194 TYR A N   1 
ATOM   1544 C  CA  . TYR A 1 193 ? -9.807  0.112   30.208  1.00 12.30 ? 194 TYR A CA  1 
ATOM   1545 C  C   . TYR A 1 193 ? -9.054  1.173   29.417  1.00 11.79 ? 194 TYR A C   1 
ATOM   1546 O  O   . TYR A 1 193 ? -9.377  1.350   28.213  1.00 10.50 ? 194 TYR A O   1 
ATOM   1547 C  CB  . TYR A 1 193 ? -8.959  -1.179  30.394  1.00 12.77 ? 194 TYR A CB  1 
ATOM   1548 C  CG  . TYR A 1 193 ? -8.256  -1.650  29.138  1.00 11.47 ? 194 TYR A CG  1 
ATOM   1549 C  CD1 . TYR A 1 193 ? -8.944  -2.294  28.117  1.00 11.71 ? 194 TYR A CD1 1 
ATOM   1550 C  CD2 . TYR A 1 193 ? -6.926  -1.335  28.925  1.00 11.04 ? 194 TYR A CD2 1 
ATOM   1551 C  CE1 . TYR A 1 193 ? -8.326  -2.639  26.914  1.00 9.55  ? 194 TYR A CE1 1 
ATOM   1552 C  CE2 . TYR A 1 193 ? -6.278  -1.691  27.746  1.00 10.86 ? 194 TYR A CE2 1 
ATOM   1553 C  CZ  . TYR A 1 193 ? -6.981  -2.340  26.748  1.00 9.67  ? 194 TYR A CZ  1 
ATOM   1554 O  OH  . TYR A 1 193 ? -6.374  -2.645  25.568  1.00 10.46 ? 194 TYR A OH  1 
ATOM   1555 N  N   . PRO A 1 194 ? -8.095  1.902   30.026  1.00 10.20 ? 195 PRO A N   1 
ATOM   1556 C  CA  . PRO A 1 194 ? -7.276  2.900   29.343  1.00 10.65 ? 195 PRO A CA  1 
ATOM   1557 C  C   . PRO A 1 194 ? -6.028  2.279   28.733  1.00 10.98 ? 195 PRO A C   1 
ATOM   1558 O  O   . PRO A 1 194 ? -5.361  1.533   29.420  1.00 12.39 ? 195 PRO A O   1 
ATOM   1559 C  CB  . PRO A 1 194 ? -6.793  3.889   30.422  1.00 11.44 ? 195 PRO A CB  1 
ATOM   1560 C  CG  . PRO A 1 194 ? -6.995  3.131   31.726  1.00 11.20 ? 195 PRO A CG  1 
ATOM   1561 C  CD  . PRO A 1 194 ? -7.839  1.889   31.488  1.00 10.06 ? 195 PRO A CD  1 
ATOM   1562 N  N   . GLY A 1 195 ? -5.792  2.513   27.423  1.00 10.00 ? 196 GLY A N   1 
ATOM   1563 C  CA  . GLY A 1 195 ? -4.616  1.893   26.791  1.00 11.31 ? 196 GLY A CA  1 
ATOM   1564 C  C   . GLY A 1 195 ? -4.087  2.770   25.653  1.00 10.63 ? 196 GLY A C   1 
ATOM   1565 O  O   . GLY A 1 195 ? -4.053  3.999   25.782  1.00 9.44  ? 196 GLY A O   1 
ATOM   1566 N  N   . SER A 1 196 ? -3.766  2.153   24.488  1.00 11.27 ? 197 SER A N   1 
ATOM   1567 C  CA  . SER A 1 196 ? -2.938  2.806   23.491  1.00 10.26 ? 197 SER A CA  1 
ATOM   1568 C  C   . SER A 1 196 ? -3.378  2.379   22.100  1.00 9.58  ? 197 SER A C   1 
ATOM   1569 O  O   . SER A 1 196 ? -4.135  1.403   21.959  1.00 9.20  ? 197 SER A O   1 
ATOM   1570 C  CB  . SER A 1 196 ? -1.509  2.412   23.668  1.00 10.64 ? 197 SER A CB  1 
ATOM   1571 O  OG  . SER A 1 196 ? -1.278  1.042   23.301  1.00 9.55  ? 197 SER A OG  1 
ATOM   1572 N  N   . LEU A 1 197 ? -2.796  3.032   21.096  1.00 9.35  ? 198 LEU A N   1 
ATOM   1573 C  CA  . LEU A 1 197 ? -2.831  2.474   19.749  1.00 8.58  ? 198 LEU A CA  1 
ATOM   1574 C  C   . LEU A 1 197 ? -2.147  1.119   19.836  1.00 9.34  ? 198 LEU A C   1 
ATOM   1575 O  O   . LEU A 1 197 ? -1.152  1.011   20.576  1.00 9.75  ? 198 LEU A O   1 
ATOM   1576 C  CB  . LEU A 1 197 ? -2.045  3.379   18.807  1.00 9.61  ? 198 LEU A CB  1 
ATOM   1577 C  CG  . LEU A 1 197 ? -2.768  4.488   18.043  1.00 11.58 ? 198 LEU A CG  1 
ATOM   1578 C  CD1 . LEU A 1 197 ? -3.466  5.507   18.951  1.00 11.02 ? 198 LEU A CD1 1 
ATOM   1579 C  CD2 . LEU A 1 197 ? -1.749  5.183   17.133  1.00 12.15 ? 198 LEU A CD2 1 
ATOM   1580 N  N   . THR A 1 198 ? -2.659  0.146   19.044  1.00 8.49  ? 199 THR A N   1 
ATOM   1581 C  CA  . THR A 1 198 ? -1.983  -1.153  18.994  1.00 9.39  ? 199 THR A CA  1 
ATOM   1582 C  C   . THR A 1 198 ? -0.965  -1.235  17.852  1.00 10.21 ? 199 THR A C   1 
ATOM   1583 O  O   . THR A 1 198 ? -0.313  -2.265  17.688  1.00 10.23 ? 199 THR A O   1 
ATOM   1584 C  CB  . THR A 1 198 ? -2.989  -2.302  18.851  1.00 9.03  ? 199 THR A CB  1 
ATOM   1585 O  OG1 . THR A 1 198 ? -3.528  -2.276  17.523  1.00 10.16 ? 199 THR A OG1 1 
ATOM   1586 C  CG2 . THR A 1 198 ? -4.022  -2.274  19.943  1.00 10.09 ? 199 THR A CG2 1 
ATOM   1587 N  N   . THR A 1 199 ? -0.831  -0.170  17.066  1.00 12.02 ? 200 THR A N   1 
ATOM   1588 C  CA  . THR A 1 199 ? 0.174   -0.105  16.025  1.00 12.16 ? 200 THR A CA  1 
ATOM   1589 C  C   . THR A 1 199 ? 1.038   1.107   16.298  1.00 11.74 ? 200 THR A C   1 
ATOM   1590 O  O   . THR A 1 199 ? 0.579   2.095   16.882  1.00 10.91 ? 200 THR A O   1 
ATOM   1591 C  CB  . THR A 1 199 ? -0.426  0.083   14.621  1.00 11.85 ? 200 THR A CB  1 
ATOM   1592 O  OG1 . THR A 1 199 ? -1.066  1.365   14.522  1.00 13.66 ? 200 THR A OG1 1 
ATOM   1593 C  CG2 . THR A 1 199 ? -1.404  -1.007  14.235  1.00 14.04 ? 200 THR A CG2 1 
ATOM   1594 N  N   . PRO A 1 200 ? 2.308   1.109   15.864  1.00 12.26 ? 201 PRO A N   1 
ATOM   1595 C  CA  . PRO A 1 200 ? 3.046   2.358   15.956  1.00 12.27 ? 201 PRO A CA  1 
ATOM   1596 C  C   . PRO A 1 200 ? 2.133   3.472   15.456  1.00 12.08 ? 201 PRO A C   1 
ATOM   1597 O  O   . PRO A 1 200 ? 1.462   3.315   14.429  1.00 13.89 ? 201 PRO A O   1 
ATOM   1598 C  CB  . PRO A 1 200 ? 4.193   2.047   14.988  1.00 12.56 ? 201 PRO A CB  1 
ATOM   1599 C  CG  . PRO A 1 200 ? 4.457   0.590   15.217  1.00 12.75 ? 201 PRO A CG  1 
ATOM   1600 C  CD  . PRO A 1 200 ? 3.055   -0.013  15.237  1.00 12.32 ? 201 PRO A CD  1 
ATOM   1601 N  N   . PRO A 1 201 ? 2.230   4.711   16.004  1.00 12.50 ? 202 PRO A N   1 
ATOM   1602 C  CA  . PRO A 1 201 ? 3.188   5.111   17.055  1.00 12.62 ? 202 PRO A CA  1 
ATOM   1603 C  C   . PRO A 1 201 ? 2.845   4.756   18.500  1.00 10.91 ? 202 PRO A C   1 
ATOM   1604 O  O   . PRO A 1 201 ? 3.526   5.160   19.450  1.00 13.71 ? 202 PRO A O   1 
ATOM   1605 C  CB  . PRO A 1 201 ? 3.235   6.654   16.852  1.00 12.93 ? 202 PRO A CB  1 
ATOM   1606 C  CG  . PRO A 1 201 ? 1.821   6.975   16.448  1.00 13.00 ? 202 PRO A CG  1 
ATOM   1607 C  CD  . PRO A 1 201 ? 1.475   5.856   15.488  1.00 12.34 ? 202 PRO A CD  1 
ATOM   1608 N  N   . LEU A 1 202 ? 1.813   3.885   18.676  1.00 9.42  ? 203 LEU A N   1 
ATOM   1609 C  CA  . LEU A 1 202 ? 1.607   3.304   19.988  1.00 10.01 ? 203 LEU A CA  1 
ATOM   1610 C  C   . LEU A 1 202 ? 1.247   4.324   21.064  1.00 10.61 ? 203 LEU A C   1 
ATOM   1611 O  O   . LEU A 1 202 ? 1.431   4.037   22.246  1.00 11.00 ? 203 LEU A O   1 
ATOM   1612 C  CB  . LEU A 1 202 ? 2.802   2.433   20.402  1.00 11.22 ? 203 LEU A CB  1 
ATOM   1613 C  CG  . LEU A 1 202 ? 3.091   1.232   19.498  1.00 11.75 ? 203 LEU A CG  1 
ATOM   1614 C  CD1 . LEU A 1 202 ? 4.356   0.553   19.956  1.00 12.83 ? 203 LEU A CD1 1 
ATOM   1615 C  CD2 . LEU A 1 202 ? 1.921   0.232   19.512  1.00 11.55 ? 203 LEU A CD2 1 
ATOM   1616 N  N   . LEU A 1 203 ? 0.631   5.458   20.669  1.00 11.04 ? 204 LEU A N   1 
ATOM   1617 C  CA  . LEU A 1 203 ? 0.388   6.556   21.590  1.00 11.74 ? 204 LEU A CA  1 
ATOM   1618 C  C   . LEU A 1 203 ? -0.668  6.165   22.616  1.00 11.35 ? 204 LEU A C   1 
ATOM   1619 O  O   . LEU A 1 203 ? -1.628  5.432   22.297  1.00 11.67 ? 204 LEU A O   1 
ATOM   1620 C  CB  . LEU A 1 203 ? -0.037  7.796   20.809  1.00 13.29 ? 204 LEU A CB  1 
ATOM   1621 C  CG  . LEU A 1 203 ? 1.004   8.323   19.824  1.00 14.29 ? 204 LEU A CG  1 
ATOM   1622 C  CD1 . LEU A 1 203 ? 0.395   9.311   18.817  1.00 17.75 ? 204 LEU A CD1 1 
ATOM   1623 C  CD2 . LEU A 1 203 ? 2.159   8.992   20.583  1.00 17.59 ? 204 LEU A CD2 1 
ATOM   1624 N  N   . GLU A 1 204 ? -0.422  6.598   23.860  1.00 11.94 ? 205 GLU A N   1 
ATOM   1625 C  CA  . GLU A 1 204 ? -1.255  6.241   24.998  1.00 12.96 ? 205 GLU A CA  1 
ATOM   1626 C  C   . GLU A 1 204 ? -2.440  7.199   25.141  1.00 12.98 ? 205 GLU A C   1 
ATOM   1627 O  O   . GLU A 1 204 ? -2.474  8.008   26.069  1.00 13.67 ? 205 GLU A O   1 
ATOM   1628 C  CB  . GLU A 1 204 ? -0.424  6.093   26.269  1.00 13.23 ? 205 GLU A CB  1 
ATOM   1629 C  CG  . GLU A 1 204 ? 0.510   4.889   26.113  1.00 14.58 ? 205 GLU A CG  1 
ATOM   1630 C  CD  . GLU A 1 204 ? 1.448   4.577   27.269  1.00 16.19 ? 205 GLU A CD  1 
ATOM   1631 O  OE1 . GLU A 1 204 ? 1.874   5.541   27.935  1.00 18.25 ? 205 GLU A OE1 1 
ATOM   1632 O  OE2 . GLU A 1 204 ? 1.746   3.388   27.458  1.00 14.19 ? 205 GLU A OE2 1 
ATOM   1633 N  N   . CYS A 1 205 ? -3.422  7.059   24.239  1.00 12.55 ? 206 CYS A N   1 
ATOM   1634 C  CA  . CYS A 1 205 ? -4.433  8.092   24.085  1.00 10.93 ? 206 CYS A CA  1 
ATOM   1635 C  C   . CYS A 1 205 ? -5.823  7.472   23.955  1.00 10.69 ? 206 CYS A C   1 
ATOM   1636 O  O   . CYS A 1 205 ? -6.763  8.191   23.644  1.00 11.22 ? 206 CYS A O   1 
ATOM   1637 C  CB  . CYS A 1 205 ? -4.153  8.947   22.863  1.00 11.90 ? 206 CYS A CB  1 
ATOM   1638 S  SG  . CYS A 1 205 ? -4.138  8.054   21.279  1.00 13.75 ? 206 CYS A SG  1 
ATOM   1639 N  N   . VAL A 1 206 ? -5.915  6.163   24.189  1.00 10.07 ? 207 VAL A N   1 
ATOM   1640 C  CA  . VAL A 1 206 ? -7.144  5.436   23.844  1.00 10.37 ? 207 VAL A CA  1 
ATOM   1641 C  C   . VAL A 1 206 ? -7.911  5.013   25.092  1.00 10.41 ? 207 VAL A C   1 
ATOM   1642 O  O   . VAL A 1 206 ? -7.360  4.350   25.973  1.00 12.16 ? 207 VAL A O   1 
ATOM   1643 C  CB  . VAL A 1 206 ? -6.859  4.168   23.017  1.00 9.72  ? 207 VAL A CB  1 
ATOM   1644 C  CG1 . VAL A 1 206 ? -8.194  3.466   22.630  1.00 9.71  ? 207 VAL A CG1 1 
ATOM   1645 C  CG2 . VAL A 1 206 ? -6.009  4.479   21.758  1.00 11.05 ? 207 VAL A CG2 1 
ATOM   1646 N  N   . THR A 1 207 ? -9.231  5.311   25.114  1.00 10.22 ? 208 THR A N   1 
ATOM   1647 C  CA  . THR A 1 207 ? -10.167 4.589   25.960  1.00 10.55 ? 208 THR A CA  1 
ATOM   1648 C  C   . THR A 1 207 ? -10.710 3.404   25.164  1.00 10.18 ? 208 THR A C   1 
ATOM   1649 O  O   . THR A 1 207 ? -11.357 3.625   24.119  1.00 9.96  ? 208 THR A O   1 
ATOM   1650 C  CB  . THR A 1 207 ? -11.333 5.505   26.384  1.00 11.09 ? 208 THR A CB  1 
ATOM   1651 O  OG1 . THR A 1 207 ? -10.806 6.551   27.213  1.00 12.22 ? 208 THR A OG1 1 
ATOM   1652 C  CG2 . THR A 1 207 ? -12.368 4.785   27.226  1.00 10.37 ? 208 THR A CG2 1 
ATOM   1653 N  N   . TRP A 1 208 ? -10.289 2.180   25.529  1.00 9.80  ? 209 TRP A N   1 
ATOM   1654 C  CA  . TRP A 1 208 ? -10.740 0.942   24.900  1.00 9.05  ? 209 TRP A CA  1 
ATOM   1655 C  C   . TRP A 1 208 ? -12.129 0.508   25.379  1.00 10.25 ? 209 TRP A C   1 
ATOM   1656 O  O   . TRP A 1 208 ? -12.400 0.498   26.581  1.00 10.25 ? 209 TRP A O   1 
ATOM   1657 C  CB  . TRP A 1 208 ? -9.717  -0.207  25.066  1.00 9.48  ? 209 TRP A CB  1 
ATOM   1658 C  CG  . TRP A 1 208 ? -8.605  -0.045  24.074  1.00 8.86  ? 209 TRP A CG  1 
ATOM   1659 C  CD1 . TRP A 1 208 ? -7.356  0.512   24.236  1.00 8.71  ? 209 TRP A CD1 1 
ATOM   1660 C  CD2 . TRP A 1 208 ? -8.713  -0.446  22.685  1.00 9.28  ? 209 TRP A CD2 1 
ATOM   1661 N  NE1 . TRP A 1 208 ? -6.706  0.497   23.047  1.00 8.44  ? 209 TRP A NE1 1 
ATOM   1662 C  CE2 . TRP A 1 208 ? -7.462  -0.121  22.090  1.00 7.92  ? 209 TRP A CE2 1 
ATOM   1663 C  CE3 . TRP A 1 208 ? -9.706  -1.120  21.937  1.00 8.30  ? 209 TRP A CE3 1 
ATOM   1664 C  CZ2 . TRP A 1 208 ? -7.215  -0.276  20.724  1.00 8.41  ? 209 TRP A CZ2 1 
ATOM   1665 C  CZ3 . TRP A 1 208 ? -9.446  -1.344  20.593  1.00 9.20  ? 209 TRP A CZ3 1 
ATOM   1666 C  CH2 . TRP A 1 208 ? -8.209  -0.961  20.031  1.00 8.92  ? 209 TRP A CH2 1 
ATOM   1667 N  N   . ILE A 1 209 ? -12.997 0.273   24.412  1.00 9.53  ? 210 ILE A N   1 
ATOM   1668 C  CA  . ILE A 1 209 ? -14.320 -0.284  24.720  1.00 9.83  ? 210 ILE A CA  1 
ATOM   1669 C  C   . ILE A 1 209 ? -14.436 -1.570  23.911  1.00 9.56  ? 210 ILE A C   1 
ATOM   1670 O  O   . ILE A 1 209 ? -14.549 -1.486  22.691  1.00 9.60  ? 210 ILE A O   1 
ATOM   1671 C  CB  . ILE A 1 209 ? -15.428 0.757   24.398  1.00 10.14 ? 210 ILE A CB  1 
ATOM   1672 C  CG1 . ILE A 1 209 ? -15.206 2.050   25.205  1.00 12.21 ? 210 ILE A CG1 1 
ATOM   1673 C  CG2 . ILE A 1 209 ? -16.839 0.176   24.639  1.00 10.60 ? 210 ILE A CG2 1 
ATOM   1674 C  CD1 . ILE A 1 209 ? -15.914 3.329   24.723  1.00 12.31 ? 210 ILE A CD1 1 
ATOM   1675 N  N   . VAL A 1 210 ? -14.395 -2.739  24.558  1.00 9.92  ? 211 VAL A N   1 
ATOM   1676 C  CA  . VAL A 1 210 ? -14.375 -4.021  23.857  1.00 10.09 ? 211 VAL A CA  1 
ATOM   1677 C  C   . VAL A 1 210 ? -15.722 -4.721  24.088  1.00 10.11 ? 211 VAL A C   1 
ATOM   1678 O  O   . VAL A 1 210 ? -16.077 -4.962  25.246  1.00 10.67 ? 211 VAL A O   1 
ATOM   1679 C  CB  . VAL A 1 210 ? -13.161 -4.896  24.230  1.00 9.83  ? 211 VAL A CB  1 
ATOM   1680 C  CG1 . VAL A 1 210 ? -13.230 -6.239  23.465  1.00 9.21  ? 211 VAL A CG1 1 
ATOM   1681 C  CG2 . VAL A 1 210 ? -11.819 -4.156  23.983  1.00 8.88  ? 211 VAL A CG2 1 
ATOM   1682 N  N   . LEU A 1 211 ? -16.449 -5.015  23.006  1.00 9.61  ? 212 LEU A N   1 
ATOM   1683 C  CA  . LEU A 1 211 ? -17.745 -5.668  23.161  1.00 10.06 ? 212 LEU A CA  1 
ATOM   1684 C  C   . LEU A 1 211 ? -17.551 -7.110  23.598  1.00 10.24 ? 212 LEU A C   1 
ATOM   1685 O  O   . LEU A 1 211 ? -16.703 -7.831  23.080  1.00 10.80 ? 212 LEU A O   1 
ATOM   1686 C  CB  . LEU A 1 211 ? -18.547 -5.568  21.854  1.00 9.01  ? 212 LEU A CB  1 
ATOM   1687 C  CG  . LEU A 1 211 ? -18.957 -4.153  21.462  1.00 10.15 ? 212 LEU A CG  1 
ATOM   1688 C  CD1 . LEU A 1 211 ? -19.969 -4.123  20.296  1.00 12.55 ? 212 LEU A CD1 1 
ATOM   1689 C  CD2 . LEU A 1 211 ? -19.416 -3.351  22.674  1.00 9.49  ? 212 LEU A CD2 1 
ATOM   1690 N  N   . LYS A 1 212 ? -18.448 -7.552  24.509  1.00 12.61 ? 213 LYS A N   1 
ATOM   1691 C  CA  . LYS A 1 212 ? -18.441 -8.933  24.965  1.00 14.11 ? 213 LYS A CA  1 
ATOM   1692 C  C   . LYS A 1 212 ? -18.925 -9.910  23.903  1.00 13.31 ? 213 LYS A C   1 
ATOM   1693 O  O   . LYS A 1 212 ? -18.396 -11.009 23.821  1.00 13.91 ? 213 LYS A O   1 
ATOM   1694 C  CB  . LYS A 1 212 ? -19.174 -9.025  26.314  1.00 16.42 ? 213 LYS A CB  1 
ATOM   1695 C  CG  . LYS A 1 212 ? -19.833 -10.344 26.690  1.00 22.39 ? 213 LYS A CG  1 
ATOM   1696 C  CD  . LYS A 1 212 ? -21.076 -10.018 27.523  1.00 24.63 ? 213 LYS A CD  1 
ATOM   1697 C  CE  . LYS A 1 212 ? -22.353 -10.600 26.953  1.00 29.99 ? 213 LYS A CE  1 
ATOM   1698 N  NZ  . LYS A 1 212 ? -23.470 -9.624  27.027  1.00 32.39 ? 213 LYS A NZ  1 
ATOM   1699 N  N   . GLU A 1 213 ? -19.872 -9.495  23.053  1.00 12.75 ? 214 GLU A N   1 
ATOM   1700 C  CA  . GLU A 1 213 ? -20.467 -10.403 22.078  1.00 12.43 ? 214 GLU A CA  1 
ATOM   1701 C  C   . GLU A 1 213 ? -19.740 -10.305 20.740  1.00 11.30 ? 214 GLU A C   1 
ATOM   1702 O  O   . GLU A 1 213 ? -19.672 -9.225  20.143  1.00 12.07 ? 214 GLU A O   1 
ATOM   1703 C  CB  . GLU A 1 213 ? -21.948 -10.059 21.899  1.00 13.52 ? 214 GLU A CB  1 
ATOM   1704 C  CG  . GLU A 1 213 ? -22.653 -10.979 20.905  1.00 16.07 ? 214 GLU A CG  1 
ATOM   1705 C  CD  . GLU A 1 213 ? -24.138 -10.664 20.724  1.00 18.97 ? 214 GLU A CD  1 
ATOM   1706 O  OE1 . GLU A 1 213 ? -24.653 -9.917  21.518  1.00 19.20 ? 214 GLU A OE1 1 
ATOM   1707 O  OE2 . GLU A 1 213 ? -24.730 -11.103 19.692  1.00 27.78 ? 214 GLU A OE2 1 
ATOM   1708 N  N   . PRO A 1 214 ? -19.152 -11.405 20.231  1.00 11.79 ? 215 PRO A N   1 
ATOM   1709 C  CA  . PRO A 1 214 ? -18.476 -11.362 18.934  1.00 12.99 ? 215 PRO A CA  1 
ATOM   1710 C  C   . PRO A 1 214 ? -19.520 -11.332 17.836  1.00 14.10 ? 215 PRO A C   1 
ATOM   1711 O  O   . PRO A 1 214 ? -20.695 -11.696 18.074  1.00 15.61 ? 215 PRO A O   1 
ATOM   1712 C  CB  . PRO A 1 214 ? -17.691 -12.692 18.907  1.00 13.57 ? 215 PRO A CB  1 
ATOM   1713 C  CG  . PRO A 1 214 ? -18.625 -13.633 19.668  1.00 16.19 ? 215 PRO A CG  1 
ATOM   1714 C  CD  . PRO A 1 214 ? -19.134 -12.758 20.822  1.00 12.75 ? 215 PRO A CD  1 
ATOM   1715 N  N   . ILE A 1 215 ? -19.079 -10.924 16.641  1.00 11.92 ? 216 ILE A N   1 
ATOM   1716 C  CA  . ILE A 1 215 ? -19.873 -11.155 15.444  1.00 13.40 ? 216 ILE A CA  1 
ATOM   1717 C  C   . ILE A 1 215 ? -19.397 -12.440 14.795  1.00 12.90 ? 216 ILE A C   1 
ATOM   1718 O  O   . ILE A 1 215 ? -18.245 -12.810 14.941  1.00 13.67 ? 216 ILE A O   1 
ATOM   1719 C  CB  . ILE A 1 215 ? -19.888 -9.958  14.459  1.00 13.30 ? 216 ILE A CB  1 
ATOM   1720 C  CG1 . ILE A 1 215 ? -18.492 -9.581  13.942  1.00 14.50 ? 216 ILE A CG1 1 
ATOM   1721 C  CG2 . ILE A 1 215 ? -20.636 -8.762  15.086  1.00 14.39 ? 216 ILE A CG2 1 
ATOM   1722 C  CD1 . ILE A 1 215 ? -18.524 -8.617  12.723  1.00 13.21 ? 216 ILE A CD1 1 
ATOM   1723 N  N   A SER A 1 216 ? -20.277 -13.118 14.061  0.50 14.13 ? 217 SER A N   1 
ATOM   1724 N  N   B SER A 1 216 ? -20.290 -13.084 14.031  0.50 13.62 ? 217 SER A N   1 
ATOM   1725 C  CA  A SER A 1 216 ? -19.733 -14.217 13.287  0.50 13.29 ? 217 SER A CA  1 
ATOM   1726 C  CA  B SER A 1 216 ? -19.905 -14.241 13.236  0.50 12.70 ? 217 SER A CA  1 
ATOM   1727 C  C   A SER A 1 216 ? -19.631 -13.819 11.822  0.50 13.70 ? 217 SER A C   1 
ATOM   1728 C  C   B SER A 1 216 ? -19.666 -13.824 11.784  0.50 13.19 ? 217 SER A C   1 
ATOM   1729 O  O   A SER A 1 216 ? -20.493 -13.108 11.300  0.50 14.94 ? 217 SER A O   1 
ATOM   1730 O  O   B SER A 1 216 ? -20.476 -13.089 11.216  0.50 14.46 ? 217 SER A O   1 
ATOM   1731 C  CB  A SER A 1 216 ? -20.522 -15.459 13.437  0.50 15.54 ? 217 SER A CB  1 
ATOM   1732 C  CB  B SER A 1 216 ? -20.968 -15.306 13.304  0.50 13.82 ? 217 SER A CB  1 
ATOM   1733 O  OG  A SER A 1 216 ? -21.827 -15.252 12.950  0.50 15.66 ? 217 SER A OG  1 
ATOM   1734 O  OG  B SER A 1 216 ? -20.970 -15.936 14.587  0.50 14.02 ? 217 SER A OG  1 
ATOM   1735 N  N   . VAL A 1 217 ? -18.572 -14.326 11.191  1.00 11.96 ? 218 VAL A N   1 
ATOM   1736 C  CA  . VAL A 1 217 ? -18.313 -14.070 9.784   1.00 11.92 ? 218 VAL A CA  1 
ATOM   1737 C  C   . VAL A 1 217 ? -18.046 -15.417 9.153   1.00 11.74 ? 218 VAL A C   1 
ATOM   1738 O  O   . VAL A 1 217 ? -17.692 -16.364 9.859   1.00 13.29 ? 218 VAL A O   1 
ATOM   1739 C  CB  . VAL A 1 217 ? -17.115 -13.122 9.573   1.00 11.24 ? 218 VAL A CB  1 
ATOM   1740 C  CG1 . VAL A 1 217 ? -17.360 -11.752 10.169  1.00 11.34 ? 218 VAL A CG1 1 
ATOM   1741 C  CG2 . VAL A 1 217 ? -15.775 -13.722 10.011  1.00 12.53 ? 218 VAL A CG2 1 
ATOM   1742 N  N   . SER A 1 218 ? -18.243 -15.544 7.833   1.00 11.24 ? 219 SER A N   1 
ATOM   1743 C  CA  . SER A 1 218 ? -18.011 -16.867 7.274   1.00 12.61 ? 219 SER A CA  1 
ATOM   1744 C  C   . SER A 1 218 ? -16.531 -17.124 6.979   1.00 11.87 ? 219 SER A C   1 
ATOM   1745 O  O   . SER A 1 218 ? -15.718 -16.193 6.895   1.00 11.83 ? 219 SER A O   1 
ATOM   1746 C  CB  . SER A 1 218 ? -18.811 -17.063 6.029   1.00 13.24 ? 219 SER A CB  1 
ATOM   1747 O  OG  . SER A 1 218 ? -18.281 -16.249 4.999   1.00 16.71 ? 219 SER A OG  1 
ATOM   1748 N  N   . SER A 1 219 ? -16.180 -18.406 6.784   1.00 12.28 ? 220 SER A N   1 
ATOM   1749 C  CA  . SER A 1 219 ? -14.807 -18.739 6.444   1.00 13.88 ? 220 SER A CA  1 
ATOM   1750 C  C   . SER A 1 219 ? -14.408 -18.048 5.140   1.00 15.28 ? 220 SER A C   1 
ATOM   1751 O  O   . SER A 1 219 ? -13.261 -17.604 4.999   1.00 15.05 ? 220 SER A O   1 
ATOM   1752 C  CB  . SER A 1 219 ? -14.639 -20.243 6.353   1.00 16.99 ? 220 SER A CB  1 
ATOM   1753 O  OG  . SER A 1 219 ? -15.704 -20.805 5.598   1.00 22.44 ? 220 SER A OG  1 
ATOM   1754 N  N   . GLU A 1 220 ? -15.350 -17.951 4.184   1.00 17.12 ? 221 GLU A N   1 
ATOM   1755 C  CA  . GLU A 1 220 ? -15.068 -17.365 2.880   1.00 16.81 ? 221 GLU A CA  1 
ATOM   1756 C  C   . GLU A 1 220 ? -14.810 -15.863 3.047   1.00 15.61 ? 221 GLU A C   1 
ATOM   1757 O  O   . GLU A 1 220 ? -13.979 -15.332 2.331   1.00 17.41 ? 221 GLU A O   1 
ATOM   1758 C  CB  . GLU A 1 220 ? -16.229 -17.558 1.913   1.00 19.59 ? 221 GLU A CB  1 
ATOM   1759 C  CG  . GLU A 1 220 ? -16.452 -19.017 1.602   1.00 21.79 ? 221 GLU A CG  1 
ATOM   1760 C  CD  . GLU A 1 220 ? -17.609 -19.666 2.332   1.00 24.89 ? 221 GLU A CD  1 
ATOM   1761 O  OE1 . GLU A 1 220 ? -18.036 -19.160 3.387   1.00 24.70 ? 221 GLU A OE1 1 
ATOM   1762 O  OE2 . GLU A 1 220 ? -18.075 -20.720 1.842   1.00 29.77 ? 221 GLU A OE2 1 
ATOM   1763 N  N   . GLN A 1 221 ? -15.514 -15.202 3.984   1.00 14.24 ? 222 GLN A N   1 
ATOM   1764 C  CA  . GLN A 1 221 ? -15.255 -13.774 4.212   1.00 14.23 ? 222 GLN A CA  1 
ATOM   1765 C  C   . GLN A 1 221 ? -13.831 -13.570 4.743   1.00 15.84 ? 222 GLN A C   1 
ATOM   1766 O  O   . GLN A 1 221 ? -13.093 -12.700 4.266   1.00 14.29 ? 222 GLN A O   1 
ATOM   1767 C  CB  . GLN A 1 221 ? -16.311 -13.222 5.183   1.00 14.71 ? 222 GLN A CB  1 
ATOM   1768 C  CG  . GLN A 1 221 ? -17.656 -13.038 4.475   1.00 14.47 ? 222 GLN A CG  1 
ATOM   1769 C  CD  . GLN A 1 221 ? -18.803 -12.554 5.332   1.00 13.86 ? 222 GLN A CD  1 
ATOM   1770 O  OE1 . GLN A 1 221 ? -18.913 -12.894 6.508   1.00 12.75 ? 222 GLN A OE1 1 
ATOM   1771 N  NE2 . GLN A 1 221 ? -19.622 -11.659 4.785   1.00 13.67 ? 222 GLN A NE2 1 
ATOM   1772 N  N   . VAL A 1 222 ? -13.415 -14.376 5.735   1.00 15.15 ? 223 VAL A N   1 
ATOM   1773 C  CA  . VAL A 1 222 ? -12.088 -14.121 6.303   1.00 15.01 ? 223 VAL A CA  1 
ATOM   1774 C  C   . VAL A 1 222 ? -10.990 -14.622 5.354   1.00 15.73 ? 223 VAL A C   1 
ATOM   1775 O  O   . VAL A 1 222 ? -9.886  -14.066 5.290   1.00 14.33 ? 223 VAL A O   1 
ATOM   1776 C  CB  . VAL A 1 222 ? -11.953 -14.670 7.734   1.00 17.15 ? 223 VAL A CB  1 
ATOM   1777 C  CG1 . VAL A 1 222 ? -12.034 -16.180 7.760   1.00 18.11 ? 223 VAL A CG1 1 
ATOM   1778 C  CG2 . VAL A 1 222 ? -10.673 -14.177 8.385   1.00 16.90 ? 223 VAL A CG2 1 
ATOM   1779 N  N   . LEU A 1 223 ? -11.319 -15.659 4.569   1.00 15.45 ? 224 LEU A N   1 
ATOM   1780 C  CA  . LEU A 1 223 ? -10.386 -16.101 3.543   1.00 17.43 ? 224 LEU A CA  1 
ATOM   1781 C  C   . LEU A 1 223 ? -10.057 -14.959 2.582   1.00 17.96 ? 224 LEU A C   1 
ATOM   1782 O  O   . LEU A 1 223 ? -8.920  -14.877 2.116   1.00 18.57 ? 224 LEU A O   1 
ATOM   1783 C  CB  . LEU A 1 223 ? -10.939 -17.333 2.815   1.00 20.88 ? 224 LEU A CB  1 
ATOM   1784 C  CG  . LEU A 1 223 ? -10.685 -18.698 3.475   1.00 25.10 ? 224 LEU A CG  1 
ATOM   1785 C  CD1 . LEU A 1 223 ? -11.427 -19.791 2.696   1.00 25.33 ? 224 LEU A CD1 1 
ATOM   1786 C  CD2 . LEU A 1 223 ? -9.196  -19.037 3.559   1.00 27.51 ? 224 LEU A CD2 1 
ATOM   1787 N  N   . LYS A 1 224 ? -11.029 -14.081 2.301   1.00 15.94 ? 225 LYS A N   1 
ATOM   1788 C  CA  . LYS A 1 224 ? -10.807 -12.998 1.350   1.00 16.75 ? 225 LYS A CA  1 
ATOM   1789 C  C   . LYS A 1 224 ? -9.886  -11.933 1.958   1.00 15.28 ? 225 LYS A C   1 
ATOM   1790 O  O   . LYS A 1 224 ? -9.073  -11.342 1.259   1.00 16.06 ? 225 LYS A O   1 
ATOM   1791 C  CB  . LYS A 1 224 ? -12.130 -12.492 0.735   1.00 16.75 ? 225 LYS A CB  1 
ATOM   1792 C  CG  . LYS A 1 224 ? -12.716 -13.494 -0.282  1.00 20.86 ? 225 LYS A CG  1 
ATOM   1793 C  CD  . LYS A 1 224 ? -14.039 -13.126 -0.941  1.00 27.85 ? 225 LYS A CD  1 
ATOM   1794 C  CE  . LYS A 1 224 ? -14.623 -14.269 -1.767  1.00 31.85 ? 225 LYS A CE  1 
ATOM   1795 N  NZ  . LYS A 1 224 ? -15.763 -13.844 -2.631  1.00 31.71 ? 225 LYS A NZ  1 
ATOM   1796 N  N   . PHE A 1 225 ? -9.999  -11.648 3.275   1.00 13.82 ? 226 PHE A N   1 
ATOM   1797 C  CA  . PHE A 1 225 ? -9.046  -10.764 3.919   1.00 12.48 ? 226 PHE A CA  1 
ATOM   1798 C  C   . PHE A 1 225 ? -7.622  -11.286 3.729   1.00 12.80 ? 226 PHE A C   1 
ATOM   1799 O  O   . PHE A 1 225 ? -6.681  -10.505 3.613   1.00 13.06 ? 226 PHE A O   1 
ATOM   1800 C  CB  . PHE A 1 225 ? -9.243  -10.778 5.452   1.00 12.68 ? 226 PHE A CB  1 
ATOM   1801 C  CG  . PHE A 1 225 ? -10.407 -10.004 6.062   1.00 13.36 ? 226 PHE A CG  1 
ATOM   1802 C  CD1 . PHE A 1 225 ? -11.469 -9.511  5.323   1.00 14.69 ? 226 PHE A CD1 1 
ATOM   1803 C  CD2 . PHE A 1 225 ? -10.470 -9.865  7.466   1.00 14.78 ? 226 PHE A CD2 1 
ATOM   1804 C  CE1 . PHE A 1 225 ? -12.494 -8.814  5.956   1.00 14.88 ? 226 PHE A CE1 1 
ATOM   1805 C  CE2 . PHE A 1 225 ? -11.513 -9.209  8.109   1.00 15.84 ? 226 PHE A CE2 1 
ATOM   1806 C  CZ  . PHE A 1 225 ? -12.527 -8.673  7.338   1.00 16.12 ? 226 PHE A CZ  1 
ATOM   1807 N  N   . ARG A 1 226 ? -7.440  -12.608 3.811   1.00 13.53 ? 227 ARG A N   1 
ATOM   1808 C  CA  . ARG A 1 226 ? -6.128  -13.232 3.745   1.00 13.86 ? 227 ARG A CA  1 
ATOM   1809 C  C   . ARG A 1 226 ? -5.516  -13.244 2.334   1.00 14.86 ? 227 ARG A C   1 
ATOM   1810 O  O   . ARG A 1 226 ? -4.363  -13.664 2.187   1.00 16.72 ? 227 ARG A O   1 
ATOM   1811 C  CB  . ARG A 1 226 ? -6.224  -14.689 4.223   1.00 14.28 ? 227 ARG A CB  1 
ATOM   1812 C  CG  . ARG A 1 226 ? -6.566  -14.865 5.702   1.00 13.09 ? 227 ARG A CG  1 
ATOM   1813 C  CD  . ARG A 1 226 ? -6.486  -16.302 6.169   1.00 14.37 ? 227 ARG A CD  1 
ATOM   1814 N  NE  . ARG A 1 226 ? -6.993  -16.427 7.551   1.00 14.64 ? 227 ARG A NE  1 
ATOM   1815 C  CZ  . ARG A 1 226 ? -7.965  -17.272 7.899   1.00 15.63 ? 227 ARG A CZ  1 
ATOM   1816 N  NH1 . ARG A 1 226 ? -8.407  -18.145 6.991   1.00 16.23 ? 227 ARG A NH1 1 
ATOM   1817 N  NH2 . ARG A 1 226 ? -8.418  -17.293 9.148   1.00 15.68 ? 227 ARG A NH2 1 
ATOM   1818 N  N   . LYS A 1 227 ? -6.253  -12.779 1.336   1.00 15.26 ? 228 LYS A N   1 
ATOM   1819 C  CA  . LYS A 1 227 ? -5.731  -12.669 -0.022  1.00 16.29 ? 228 LYS A CA  1 
ATOM   1820 C  C   . LYS A 1 227 ? -5.022  -11.329 -0.258  1.00 16.57 ? 228 LYS A C   1 
ATOM   1821 O  O   . LYS A 1 227 ? -4.340  -11.152 -1.277  1.00 16.91 ? 228 LYS A O   1 
ATOM   1822 C  CB  . LYS A 1 227 ? -6.871  -12.896 -1.009  1.00 17.60 ? 228 LYS A CB  1 
ATOM   1823 C  CG  . LYS A 1 227 ? -7.237  -14.362 -1.116  1.00 20.11 ? 228 LYS A CG  1 
ATOM   1824 C  CD  . LYS A 1 227 ? -8.543  -14.614 -1.815  1.00 27.71 ? 228 LYS A CD  1 
ATOM   1825 C  CE  . LYS A 1 227 ? -8.408  -15.619 -2.937  1.00 34.27 ? 228 LYS A CE  1 
ATOM   1826 N  NZ  . LYS A 1 227 ? -8.168  -14.914 -4.225  1.00 36.91 ? 228 LYS A NZ  1 
ATOM   1827 N  N   . LEU A 1 228 ? -5.173  -10.389 0.686   1.00 16.54 ? 229 LEU A N   1 
ATOM   1828 C  CA  . LEU A 1 228 ? -4.485  -9.112  0.552   1.00 15.02 ? 229 LEU A CA  1 
ATOM   1829 C  C   . LEU A 1 228 ? -2.979  -9.278  0.714   1.00 15.13 ? 229 LEU A C   1 
ATOM   1830 O  O   . LEU A 1 228 ? -2.507  -10.295 1.187   1.00 15.37 ? 229 LEU A O   1 
ATOM   1831 C  CB  . LEU A 1 228 ? -5.007  -8.184  1.640   1.00 14.39 ? 229 LEU A CB  1 
ATOM   1832 C  CG  . LEU A 1 228 ? -6.443  -7.709  1.448   1.00 14.39 ? 229 LEU A CG  1 
ATOM   1833 C  CD1 . LEU A 1 228 ? -6.984  -7.131  2.766   1.00 15.57 ? 229 LEU A CD1 1 
ATOM   1834 C  CD2 . LEU A 1 228 ? -6.493  -6.626  0.358   1.00 15.74 ? 229 LEU A CD2 1 
ATOM   1835 N  N   . ASN A 1 229 ? -2.223  -8.226  0.348   1.00 16.74 ? 230 ASN A N   1 
ATOM   1836 C  CA  . ASN A 1 229 ? -0.771  -8.242  0.376   1.00 18.16 ? 230 ASN A CA  1 
ATOM   1837 C  C   . ASN A 1 229 ? -0.268  -7.073  1.231   1.00 18.36 ? 230 ASN A C   1 
ATOM   1838 O  O   . ASN A 1 229 ? -0.820  -5.963  1.154   1.00 18.03 ? 230 ASN A O   1 
ATOM   1839 C  CB  . ASN A 1 229 ? -0.156  -8.061  -1.025  1.00 18.66 ? 230 ASN A CB  1 
ATOM   1840 C  CG  . ASN A 1 229 ? -0.332  -9.213  -2.009  1.00 21.62 ? 230 ASN A CG  1 
ATOM   1841 O  OD1 . ASN A 1 229 ? 0.160   -9.113  -3.141  1.00 21.17 ? 230 ASN A OD1 1 
ATOM   1842 N  ND2 . ASN A 1 229 ? -0.980  -10.303 -1.609  1.00 19.46 ? 230 ASN A ND2 1 
ATOM   1843 N  N   . PHE A 1 230 ? 0.786   -7.361  2.008   1.00 18.85 ? 231 PHE A N   1 
ATOM   1844 C  CA  . PHE A 1 230 ? 1.539   -6.325  2.708   1.00 19.52 ? 231 PHE A CA  1 
ATOM   1845 C  C   . PHE A 1 230 ? 2.456   -5.586  1.737   1.00 22.19 ? 231 PHE A C   1 
ATOM   1846 O  O   . PHE A 1 230 ? 2.784   -4.418  1.959   1.00 20.48 ? 231 PHE A O   1 
ATOM   1847 C  CB  . PHE A 1 230 ? 2.471   -6.915  3.761   1.00 19.76 ? 231 PHE A CB  1 
ATOM   1848 C  CG  . PHE A 1 230 ? 1.897   -7.540  5.018   1.00 19.29 ? 231 PHE A CG  1 
ATOM   1849 C  CD1 . PHE A 1 230 ? 1.140   -6.799  5.923   1.00 17.77 ? 231 PHE A CD1 1 
ATOM   1850 C  CD2 . PHE A 1 230 ? 2.261   -8.844  5.355   1.00 19.68 ? 231 PHE A CD2 1 
ATOM   1851 C  CE1 . PHE A 1 230 ? 0.704   -7.399  7.108   1.00 17.45 ? 231 PHE A CE1 1 
ATOM   1852 C  CE2 . PHE A 1 230 ? 1.842   -9.434  6.542   1.00 20.57 ? 231 PHE A CE2 1 
ATOM   1853 C  CZ  . PHE A 1 230 ? 1.060   -8.701  7.413   1.00 18.54 ? 231 PHE A CZ  1 
ATOM   1854 N  N   . ASN A 1 231 ? 2.918   -6.290  0.707   1.00 21.90 ? 232 ASN A N   1 
ATOM   1855 C  CA  . ASN A 1 231 ? 3.869   -5.706  -0.233  1.00 22.30 ? 232 ASN A CA  1 
ATOM   1856 C  C   . ASN A 1 231 ? 3.136   -4.765  -1.189  1.00 21.89 ? 232 ASN A C   1 
ATOM   1857 O  O   . ASN A 1 231 ? 1.913   -4.855  -1.387  1.00 21.37 ? 232 ASN A O   1 
ATOM   1858 C  CB  . ASN A 1 231 ? 4.556   -6.805  -1.040  1.00 22.21 ? 232 ASN A CB  1 
ATOM   1859 C  CG  . ASN A 1 231 ? 3.519   -7.720  -1.655  1.00 22.90 ? 232 ASN A CG  1 
ATOM   1860 O  OD1 . ASN A 1 231 ? 3.075   -8.664  -0.998  1.00 26.83 ? 232 ASN A OD1 1 
ATOM   1861 N  ND2 . ASN A 1 231 ? 3.135   -7.476  -2.908  1.00 24.34 ? 232 ASN A ND2 1 
ATOM   1862 N  N   . GLY A 1 232 ? 3.904   -3.865  -1.832  1.00 21.69 ? 233 GLY A N   1 
ATOM   1863 C  CA  . GLY A 1 232 ? 3.368   -3.044  -2.914  1.00 23.36 ? 233 GLY A CA  1 
ATOM   1864 C  C   . GLY A 1 232 ? 3.405   -3.816  -4.234  1.00 25.61 ? 233 GLY A C   1 
ATOM   1865 O  O   . GLY A 1 232 ? 4.144   -4.801  -4.308  1.00 26.44 ? 233 GLY A O   1 
ATOM   1866 N  N   . GLU A 1 233 ? 2.580   -3.364  -5.205  1.00 27.73 ? 234 GLU A N   1 
ATOM   1867 C  CA  . GLU A 1 233 ? 2.451   -3.903  -6.560  1.00 32.24 ? 234 GLU A CA  1 
ATOM   1868 C  C   . GLU A 1 233 ? 3.833   -3.970  -7.204  1.00 33.34 ? 234 GLU A C   1 
ATOM   1869 O  O   . GLU A 1 233 ? 4.625   -3.029  -7.113  1.00 30.77 ? 234 GLU A O   1 
ATOM   1870 C  CB  . GLU A 1 233 ? 1.455   -3.096  -7.402  1.00 30.03 ? 234 GLU A CB  1 
ATOM   1871 C  CG  . GLU A 1 233 ? 1.122   -3.700  -8.775  1.00 33.86 ? 234 GLU A CG  1 
ATOM   1872 C  CD  . GLU A 1 233 ? 0.373   -2.740  -9.683  1.00 37.62 ? 234 GLU A CD  1 
ATOM   1873 O  OE1 . GLU A 1 233 ? -0.028  -1.665  -9.193  1.00 36.33 ? 234 GLU A OE1 1 
ATOM   1874 O  OE2 . GLU A 1 233 ? 0.222   -3.042  -10.895 1.00 40.72 ? 234 GLU A OE2 1 
ATOM   1875 N  N   . GLY A 1 234 ? 4.134   -5.144  -7.765  1.00 32.81 ? 235 GLY A N   1 
ATOM   1876 C  CA  . GLY A 1 234 ? 5.446   -5.454  -8.306  1.00 37.34 ? 235 GLY A CA  1 
ATOM   1877 C  C   . GLY A 1 234 ? 6.556   -5.511  -7.257  1.00 42.39 ? 235 GLY A C   1 
ATOM   1878 O  O   . GLY A 1 234 ? 7.668   -5.058  -7.547  1.00 37.97 ? 235 GLY A O   1 
ATOM   1879 N  N   . GLU A 1 235 ? 6.252   -6.056  -6.056  1.00 39.93 ? 236 GLU A N   1 
ATOM   1880 C  CA  . GLU A 1 235 ? 7.256   -6.577  -5.124  1.00 34.71 ? 236 GLU A CA  1 
ATOM   1881 C  C   . GLU A 1 235 ? 6.930   -8.042  -4.806  1.00 29.91 ? 236 GLU A C   1 
ATOM   1882 O  O   . GLU A 1 235 ? 5.859   -8.514  -5.169  1.00 36.21 ? 236 GLU A O   1 
ATOM   1883 C  CB  . GLU A 1 235 ? 7.366   -5.724  -3.853  1.00 42.14 ? 236 GLU A CB  1 
ATOM   1884 C  CG  . GLU A 1 235 ? 7.350   -4.227  -4.106  1.00 41.19 ? 236 GLU A CG  1 
ATOM   1885 C  CD  . GLU A 1 235 ? 7.281   -3.337  -2.874  1.00 51.14 ? 236 GLU A CD  1 
ATOM   1886 O  OE1 . GLU A 1 235 ? 7.064   -3.873  -1.749  1.00 53.42 ? 236 GLU A OE1 1 
ATOM   1887 O  OE2 . GLU A 1 235 ? 7.442   -2.097  -3.038  1.00 49.61 ? 236 GLU A OE2 1 
ATOM   1888 N  N   . PRO A 1 236 ? 7.840   -8.844  -4.206  1.00 31.10 ? 237 PRO A N   1 
ATOM   1889 C  CA  . PRO A 1 236 ? 7.543   -10.249 -3.908  1.00 28.56 ? 237 PRO A CA  1 
ATOM   1890 C  C   . PRO A 1 236 ? 6.290   -10.320 -3.029  1.00 29.96 ? 237 PRO A C   1 
ATOM   1891 O  O   . PRO A 1 236 ? 6.063   -9.428  -2.209  1.00 25.92 ? 237 PRO A O   1 
ATOM   1892 C  CB  . PRO A 1 236 ? 8.780   -10.741 -3.157  1.00 34.58 ? 237 PRO A CB  1 
ATOM   1893 C  CG  . PRO A 1 236 ? 9.884   -9.806  -3.630  1.00 30.90 ? 237 PRO A CG  1 
ATOM   1894 C  CD  . PRO A 1 236 ? 9.205   -8.464  -3.804  1.00 31.23 ? 237 PRO A CD  1 
ATOM   1895 N  N   . GLU A 1 237 ? 5.445   -11.332 -3.264  1.00 27.40 ? 238 GLU A N   1 
ATOM   1896 C  CA  . GLU A 1 237 ? 4.150   -11.384 -2.608  1.00 23.77 ? 238 GLU A CA  1 
ATOM   1897 C  C   . GLU A 1 237 ? 4.320   -11.914 -1.181  1.00 19.96 ? 238 GLU A C   1 
ATOM   1898 O  O   . GLU A 1 237 ? 4.888   -12.978 -0.945  1.00 20.98 ? 238 GLU A O   1 
ATOM   1899 C  CB  . GLU A 1 237 ? 3.129   -12.180 -3.438  1.00 24.63 ? 238 GLU A CB  1 
ATOM   1900 C  CG  . GLU A 1 237 ? 1.744   -12.253 -2.796  1.00 26.07 ? 238 GLU A CG  1 
ATOM   1901 C  CD  . GLU A 1 237 ? 0.598   -12.907 -3.553  1.00 29.14 ? 238 GLU A CD  1 
ATOM   1902 O  OE1 . GLU A 1 237 ? 0.853   -13.893 -4.287  1.00 34.44 ? 238 GLU A OE1 1 
ATOM   1903 O  OE2 . GLU A 1 237 ? -0.559  -12.429 -3.416  1.00 25.06 ? 238 GLU A OE2 1 
ATOM   1904 N  N   . GLU A 1 238 ? 3.780   -11.152 -0.238  1.00 18.84 ? 239 GLU A N   1 
ATOM   1905 C  CA  . GLU A 1 238 ? 3.665   -11.524 1.164   1.00 19.59 ? 239 GLU A CA  1 
ATOM   1906 C  C   . GLU A 1 238 ? 2.198   -11.306 1.557   1.00 16.67 ? 239 GLU A C   1 
ATOM   1907 O  O   . GLU A 1 238 ? 1.690   -10.182 1.544   1.00 17.37 ? 239 GLU A O   1 
ATOM   1908 C  CB  . GLU A 1 238 ? 4.609   -10.686 2.044   1.00 24.18 ? 239 GLU A CB  1 
ATOM   1909 C  CG  . GLU A 1 238 ? 5.791   -11.483 2.604   1.00 34.07 ? 239 GLU A CG  1 
ATOM   1910 C  CD  . GLU A 1 238 ? 6.940   -10.676 3.200   1.00 34.22 ? 239 GLU A CD  1 
ATOM   1911 O  OE1 . GLU A 1 238 ? 7.146   -10.744 4.449   1.00 35.66 ? 239 GLU A OE1 1 
ATOM   1912 O  OE2 . GLU A 1 238 ? 7.626   -9.957  2.423   1.00 41.90 ? 239 GLU A OE2 1 
ATOM   1913 N  N   A LEU A 1 239 ? 1.511   -12.401 1.891   0.50 15.23 ? 240 LEU A N   1 
ATOM   1914 N  N   B LEU A 1 239 ? 1.499   -12.403 1.866   0.50 16.45 ? 240 LEU A N   1 
ATOM   1915 C  CA  A LEU A 1 239 ? 0.102   -12.291 2.230   0.50 14.68 ? 240 LEU A CA  1 
ATOM   1916 C  CA  B LEU A 1 239 ? 0.085   -12.292 2.188   0.50 16.58 ? 240 LEU A CA  1 
ATOM   1917 C  C   A LEU A 1 239 ? -0.057  -11.476 3.509   0.50 14.81 ? 240 LEU A C   1 
ATOM   1918 C  C   B LEU A 1 239 ? -0.076  -11.503 3.490   0.50 15.99 ? 240 LEU A C   1 
ATOM   1919 O  O   A LEU A 1 239 ? 0.659   -11.714 4.482   0.50 17.17 ? 240 LEU A O   1 
ATOM   1920 O  O   B LEU A 1 239 ? 0.639   -11.764 4.458   0.50 17.97 ? 240 LEU A O   1 
ATOM   1921 C  CB  A LEU A 1 239 ? -0.459  -13.697 2.445   0.50 14.09 ? 240 LEU A CB  1 
ATOM   1922 C  CB  B LEU A 1 239 ? -0.505  -13.698 2.336   0.50 18.29 ? 240 LEU A CB  1 
ATOM   1923 C  CG  A LEU A 1 239 ? -0.515  -14.529 1.167   0.50 13.78 ? 240 LEU A CG  1 
ATOM   1924 C  CG  B LEU A 1 239 ? -0.724  -14.462 1.025   0.50 19.15 ? 240 LEU A CG  1 
ATOM   1925 C  CD1 A LEU A 1 239 ? -1.064  -15.911 1.464   0.50 15.17 ? 240 LEU A CD1 1 
ATOM   1926 C  CD1 B LEU A 1 239 ? 0.600   -14.969 0.454   0.50 20.68 ? 240 LEU A CD1 1 
ATOM   1927 C  CD2 A LEU A 1 239 ? -1.317  -13.817 0.098   0.50 11.86 ? 240 LEU A CD2 1 
ATOM   1928 C  CD2 B LEU A 1 239 ? -1.668  -15.634 1.261   0.50 22.90 ? 240 LEU A CD2 1 
ATOM   1929 N  N   . MET A 1 240 ? -1.047  -10.581 3.500   1.00 16.16 ? 241 MET A N   1 
ATOM   1930 C  CA  . MET A 1 240 ? -1.412  -9.828  4.696   1.00 14.93 ? 241 MET A CA  1 
ATOM   1931 C  C   . MET A 1 240 ? -2.178  -10.765 5.632   1.00 14.31 ? 241 MET A C   1 
ATOM   1932 O  O   . MET A 1 240 ? -3.401  -10.892 5.531   1.00 14.77 ? 241 MET A O   1 
ATOM   1933 C  CB  . MET A 1 240 ? -2.275  -8.624  4.313   1.00 15.21 ? 241 MET A CB  1 
ATOM   1934 C  CG  . MET A 1 240 ? -2.542  -7.661  5.494   1.00 15.01 ? 241 MET A CG  1 
ATOM   1935 S  SD  . MET A 1 240 ? -3.489  -6.276  4.934   1.00 17.22 ? 241 MET A SD  1 
ATOM   1936 C  CE  . MET A 1 240 ? -2.168  -5.222  4.316   1.00 15.12 ? 241 MET A CE  1 
ATOM   1937 N  N   . VAL A 1 241 ? -1.418  -11.425 6.516   1.00 15.07 ? 242 VAL A N   1 
ATOM   1938 C  CA  . VAL A 1 241 ? -1.984  -12.248 7.577   1.00 13.54 ? 242 VAL A CA  1 
ATOM   1939 C  C   . VAL A 1 241 ? -1.185  -11.995 8.853   1.00 14.40 ? 242 VAL A C   1 
ATOM   1940 O  O   . VAL A 1 241 ? 0.011   -11.637 8.813   1.00 14.27 ? 242 VAL A O   1 
ATOM   1941 C  CB  . VAL A 1 241 ? -1.946  -13.750 7.241   1.00 13.97 ? 242 VAL A CB  1 
ATOM   1942 C  CG1 . VAL A 1 241 ? -2.845  -14.107 6.055   1.00 14.09 ? 242 VAL A CG1 1 
ATOM   1943 C  CG2 . VAL A 1 241 ? -0.512  -14.210 7.023   1.00 13.71 ? 242 VAL A CG2 1 
ATOM   1944 N  N   . ASP A 1 242 ? -1.837  -12.275 9.978   1.00 10.94 ? 243 ASP A N   1 
ATOM   1945 C  CA  . ASP A 1 242 ? -1.204  -12.133 11.277  1.00 11.61 ? 243 ASP A CA  1 
ATOM   1946 C  C   . ASP A 1 242 ? -0.711  -10.691 11.469  1.00 11.05 ? 243 ASP A C   1 
ATOM   1947 O  O   . ASP A 1 242 ? 0.376   -10.450 12.029  1.00 12.43 ? 243 ASP A O   1 
ATOM   1948 C  CB  . ASP A 1 242 ? -0.131  -13.207 11.569  1.00 12.72 ? 243 ASP A CB  1 
ATOM   1949 C  CG  . ASP A 1 242 ? -0.689  -14.608 11.670  1.00 15.25 ? 243 ASP A CG  1 
ATOM   1950 O  OD1 . ASP A 1 242 ? -1.735  -14.785 12.329  1.00 13.80 ? 243 ASP A OD1 1 
ATOM   1951 O  OD2 . ASP A 1 242 ? -0.082  -15.540 11.078  1.00 16.35 ? 243 ASP A OD2 1 
ATOM   1952 N  N   . ASN A 1 243 ? -1.620  -9.757  11.247  1.00 10.96 ? 244 ASN A N   1 
ATOM   1953 C  CA  . ASN A 1 243 ? -1.346  -8.333  11.466  1.00 10.80 ? 244 ASN A CA  1 
ATOM   1954 C  C   . ASN A 1 243 ? -1.870  -7.870  12.829  1.00 10.95 ? 244 ASN A C   1 
ATOM   1955 O  O   . ASN A 1 243 ? -2.504  -6.813  12.924  1.00 11.92 ? 244 ASN A O   1 
ATOM   1956 C  CB  . ASN A 1 243 ? -1.853  -7.481  10.303  1.00 12.55 ? 244 ASN A CB  1 
ATOM   1957 C  CG  . ASN A 1 243 ? -3.344  -7.629  10.072  1.00 14.16 ? 244 ASN A CG  1 
ATOM   1958 O  OD1 . ASN A 1 243 ? -3.963  -8.485  10.709  1.00 14.19 ? 244 ASN A OD1 1 
ATOM   1959 N  ND2 . ASN A 1 243 ? -3.930  -6.786  9.216   1.00 15.30 ? 244 ASN A ND2 1 
ATOM   1960 N  N   . TRP A 1 244 ? -1.537  -8.635  13.857  1.00 9.93  ? 245 TRP A N   1 
ATOM   1961 C  CA  . TRP A 1 244 ? -2.017  -8.415  15.216  1.00 10.40 ? 245 TRP A CA  1 
ATOM   1962 C  C   . TRP A 1 244 ? -0.851  -8.281  16.169  1.00 11.63 ? 245 TRP A C   1 
ATOM   1963 O  O   . TRP A 1 244 ? 0.145   -8.997  16.051  1.00 11.42 ? 245 TRP A O   1 
ATOM   1964 C  CB  . TRP A 1 244 ? -3.006  -9.511  15.677  1.00 10.28 ? 245 TRP A CB  1 
ATOM   1965 C  CG  . TRP A 1 244 ? -2.552  -10.916 15.509  1.00 10.05 ? 245 TRP A CG  1 
ATOM   1966 C  CD1 . TRP A 1 244 ? -2.671  -11.661 14.382  1.00 11.00 ? 245 TRP A CD1 1 
ATOM   1967 C  CD2 . TRP A 1 244 ? -1.993  -11.775 16.510  1.00 10.86 ? 245 TRP A CD2 1 
ATOM   1968 N  NE1 . TRP A 1 244 ? -2.210  -12.930 14.617  1.00 11.02 ? 245 TRP A NE1 1 
ATOM   1969 C  CE2 . TRP A 1 244 ? -1.774  -13.031 15.911  1.00 12.15 ? 245 TRP A CE2 1 
ATOM   1970 C  CE3 . TRP A 1 244 ? -1.703  -11.637 17.878  1.00 11.73 ? 245 TRP A CE3 1 
ATOM   1971 C  CZ2 . TRP A 1 244 ? -1.149  -14.090 16.588  1.00 11.07 ? 245 TRP A CZ2 1 
ATOM   1972 C  CZ3 . TRP A 1 244 ? -1.100  -12.682 18.555  1.00 12.82 ? 245 TRP A CZ3 1 
ATOM   1973 C  CH2 . TRP A 1 244 ? -0.889  -13.923 17.932  1.00 10.99 ? 245 TRP A CH2 1 
ATOM   1974 N  N   . ARG A 1 245 ? -0.967  -7.335  17.097  1.00 11.39 ? 246 ARG A N   1 
ATOM   1975 C  CA  . ARG A 1 245 ? -0.058  -7.261  18.232  1.00 11.83 ? 246 ARG A CA  1 
ATOM   1976 C  C   . ARG A 1 245 ? -0.543  -8.141  19.379  1.00 12.73 ? 246 ARG A C   1 
ATOM   1977 O  O   . ARG A 1 245 ? -1.734  -8.217  19.697  1.00 11.49 ? 246 ARG A O   1 
ATOM   1978 C  CB  . ARG A 1 245 ? -0.024  -5.816  18.737  1.00 11.78 ? 246 ARG A CB  1 
ATOM   1979 C  CG  . ARG A 1 245 ? 1.140   -5.571  19.694  1.00 10.89 ? 246 ARG A CG  1 
ATOM   1980 C  CD  . ARG A 1 245 ? 1.019   -4.243  20.442  1.00 10.80 ? 246 ARG A CD  1 
ATOM   1981 N  NE  . ARG A 1 245 ? 2.298   -3.945  21.148  1.00 11.74 ? 246 ARG A NE  1 
ATOM   1982 C  CZ  . ARG A 1 245 ? 2.514   -2.874  21.924  1.00 12.31 ? 246 ARG A CZ  1 
ATOM   1983 N  NH1 . ARG A 1 245 ? 1.538   -2.036  22.244  1.00 10.98 ? 246 ARG A NH1 1 
ATOM   1984 N  NH2 . ARG A 1 245 ? 3.728   -2.639  22.388  1.00 14.19 ? 246 ARG A NH2 1 
ATOM   1985 N  N   . PRO A 1 246 ? 0.338   -8.944  20.007  1.00 14.32 ? 247 PRO A N   1 
ATOM   1986 C  CA  . PRO A 1 246 ? -0.071  -9.757  21.147  1.00 13.14 ? 247 PRO A CA  1 
ATOM   1987 C  C   . PRO A 1 246 ? -0.371  -8.936  22.401  1.00 13.54 ? 247 PRO A C   1 
ATOM   1988 O  O   . PRO A 1 246 ? -0.010  -7.754  22.505  1.00 12.73 ? 247 PRO A O   1 
ATOM   1989 C  CB  . PRO A 1 246 ? 1.195   -10.581 21.449  1.00 16.31 ? 247 PRO A CB  1 
ATOM   1990 C  CG  . PRO A 1 246 ? 2.012   -10.483 20.225  1.00 18.33 ? 247 PRO A CG  1 
ATOM   1991 C  CD  . PRO A 1 246 ? 1.769   -9.109  19.661  1.00 15.60 ? 247 PRO A CD  1 
ATOM   1992 N  N   . ALA A 1 247 ? -1.000  -9.613  23.363  1.00 13.39 ? 248 ALA A N   1 
ATOM   1993 C  CA  . ALA A 1 247 ? -1.324  -9.030  24.650  1.00 11.87 ? 248 ALA A CA  1 
ATOM   1994 C  C   . ALA A 1 247 ? -0.083  -8.489  25.350  1.00 12.88 ? 248 ALA A C   1 
ATOM   1995 O  O   . ALA A 1 247 ? 0.977   -9.127  25.347  1.00 13.75 ? 248 ALA A O   1 
ATOM   1996 C  CB  . ALA A 1 247 ? -2.033  -10.050 25.504  1.00 12.67 ? 248 ALA A CB  1 
ATOM   1997 N  N   . GLN A 1 248 ? -0.251  -7.309  25.925  1.00 11.64 ? 249 GLN A N   1 
ATOM   1998 C  CA  . GLN A 1 248 ? 0.778   -6.563  26.619  1.00 13.14 ? 249 GLN A CA  1 
ATOM   1999 C  C   . GLN A 1 248 ? 0.425   -6.596  28.103  1.00 13.79 ? 249 GLN A C   1 
ATOM   2000 O  O   . GLN A 1 248 ? -0.732  -6.865  28.465  1.00 15.10 ? 249 GLN A O   1 
ATOM   2001 C  CB  . GLN A 1 248 ? 0.822   -5.138  26.070  1.00 13.74 ? 249 GLN A CB  1 
ATOM   2002 C  CG  . GLN A 1 248 ? 1.138   -5.061  24.572  1.00 13.47 ? 249 GLN A CG  1 
ATOM   2003 C  CD  . GLN A 1 248 ? 2.461   -5.722  24.250  1.00 15.38 ? 249 GLN A CD  1 
ATOM   2004 O  OE1 . GLN A 1 248 ? 3.494   -5.378  24.834  1.00 17.03 ? 249 GLN A OE1 1 
ATOM   2005 N  NE2 . GLN A 1 248 ? 2.432   -6.685  23.326  1.00 15.10 ? 249 GLN A NE2 1 
ATOM   2006 N  N   . PRO A 1 249 ? 1.408   -6.302  28.985  1.00 14.49 ? 250 PRO A N   1 
ATOM   2007 C  CA  . PRO A 1 249 ? 1.194   -6.305  30.435  1.00 14.63 ? 250 PRO A CA  1 
ATOM   2008 C  C   . PRO A 1 249 ? 0.185   -5.230  30.832  1.00 14.67 ? 250 PRO A C   1 
ATOM   2009 O  O   . PRO A 1 249 ? 0.318   -4.064  30.471  1.00 17.60 ? 250 PRO A O   1 
ATOM   2010 C  CB  . PRO A 1 249 ? 2.583   -5.832  30.941  1.00 15.47 ? 250 PRO A CB  1 
ATOM   2011 C  CG  . PRO A 1 249 ? 3.517   -6.243  29.873  1.00 15.83 ? 250 PRO A CG  1 
ATOM   2012 C  CD  . PRO A 1 249 ? 2.774   -5.887  28.598  1.00 13.41 ? 250 PRO A CD  1 
ATOM   2013 N  N   . LEU A 1 250 ? -0.735  -5.652  31.698  1.00 15.26 ? 251 LEU A N   1 
ATOM   2014 C  CA  . LEU A 1 250 ? -1.809  -4.835  32.238  1.00 17.44 ? 251 LEU A CA  1 
ATOM   2015 C  C   . LEU A 1 250 ? -1.232  -3.772  33.172  1.00 18.42 ? 251 LEU A C   1 
ATOM   2016 O  O   . LEU A 1 250 ? -1.743  -2.650  33.208  1.00 16.17 ? 251 LEU A O   1 
ATOM   2017 C  CB  . LEU A 1 250 ? -2.811  -5.721  32.968  1.00 17.49 ? 251 LEU A CB  1 
ATOM   2018 C  CG  . LEU A 1 250 ? -4.134  -5.043  33.333  1.00 16.74 ? 251 LEU A CG  1 
ATOM   2019 C  CD1 . LEU A 1 250 ? -4.804  -4.441  32.098  1.00 16.04 ? 251 LEU A CD1 1 
ATOM   2020 C  CD2 . LEU A 1 250 ? -5.063  -6.039  34.025  1.00 21.81 ? 251 LEU A CD2 1 
ATOM   2021 N  N   . LYS A 1 251 ? -0.158  -4.142  33.893  1.00 19.45 ? 252 LYS A N   1 
ATOM   2022 C  CA  . LYS A 1 251 ? 0.527   -3.231  34.802  1.00 19.53 ? 252 LYS A CA  1 
ATOM   2023 C  C   . LYS A 1 251 ? -0.486  -2.684  35.799  1.00 19.96 ? 252 LYS A C   1 
ATOM   2024 O  O   . LYS A 1 251 ? -1.323  -3.413  36.313  1.00 21.15 ? 252 LYS A O   1 
ATOM   2025 C  CB  . LYS A 1 251 ? 1.321   -2.154  34.049  1.00 21.17 ? 252 LYS A CB  1 
ATOM   2026 C  CG  . LYS A 1 251 ? 2.520   -2.730  33.311  1.00 23.25 ? 252 LYS A CG  1 
ATOM   2027 C  CD  . LYS A 1 251 ? 3.351   -1.755  32.494  1.00 23.04 ? 252 LYS A CD  1 
ATOM   2028 C  CE  . LYS A 1 251 ? 4.508   -2.493  31.862  1.00 21.85 ? 252 LYS A CE  1 
ATOM   2029 N  NZ  . LYS A 1 251 ? 5.437   -1.601  31.149  1.00 24.98 ? 252 LYS A NZ  1 
ATOM   2030 N  N   . ASN A 1 252 ? -0.465  -1.377  35.990  1.00 20.39 ? 253 ASN A N   1 
ATOM   2031 C  CA  . ASN A 1 252 ? -1.282  -0.790  37.031  1.00 29.88 ? 253 ASN A CA  1 
ATOM   2032 C  C   . ASN A 1 252 ? -2.657  -0.425  36.468  1.00 28.27 ? 253 ASN A C   1 
ATOM   2033 O  O   . ASN A 1 252 ? -2.976  0.777   36.533  1.00 31.53 ? 253 ASN A O   1 
ATOM   2034 C  CB  . ASN A 1 252 ? -0.623  0.521   37.480  1.00 37.05 ? 253 ASN A CB  1 
ATOM   2035 C  CG  . ASN A 1 252 ? -0.611  0.708   38.983  1.00 48.43 ? 253 ASN A CG  1 
ATOM   2036 O  OD1 . ASN A 1 252 ? -1.662  0.691   39.631  1.00 49.75 ? 253 ASN A OD1 1 
ATOM   2037 N  ND2 . ASN A 1 252 ? 0.580   0.898   39.536  1.00 50.89 ? 253 ASN A ND2 1 
ATOM   2038 N  N   . ARG A 1 253 ? -3.412  -1.402  35.873  1.00 20.27 ? 254 ARG A N   1 
ATOM   2039 C  CA  . ARG A 1 253 ? -4.742  -1.080  35.358  1.00 16.31 ? 254 ARG A CA  1 
ATOM   2040 C  C   . ARG A 1 253 ? -5.814  -2.066  35.800  1.00 17.65 ? 254 ARG A C   1 
ATOM   2041 O  O   . ARG A 1 253 ? -5.572  -3.264  35.899  1.00 19.81 ? 254 ARG A O   1 
ATOM   2042 C  CB  . ARG A 1 253 ? -4.771  -0.999  33.819  1.00 13.56 ? 254 ARG A CB  1 
ATOM   2043 C  CG  . ARG A 1 253 ? -3.887  0.116   33.265  1.00 12.28 ? 254 ARG A CG  1 
ATOM   2044 C  CD  . ARG A 1 253 ? -3.840  0.098   31.724  1.00 12.69 ? 254 ARG A CD  1 
ATOM   2045 N  NE  . ARG A 1 253 ? -2.908  -0.945  31.300  1.00 11.50 ? 254 ARG A NE  1 
ATOM   2046 C  CZ  . ARG A 1 253 ? -2.642  -1.247  30.034  1.00 11.64 ? 254 ARG A CZ  1 
ATOM   2047 N  NH1 . ARG A 1 253 ? -3.238  -0.586  29.057  1.00 11.28 ? 254 ARG A NH1 1 
ATOM   2048 N  NH2 . ARG A 1 253 ? -1.783  -2.209  29.750  1.00 10.69 ? 254 ARG A NH2 1 
ATOM   2049 N  N   . GLN A 1 254 ? -7.045  -1.545  35.909  1.00 18.81 ? 255 GLN A N   1 
ATOM   2050 C  CA  . GLN A 1 254 ? -8.207  -2.381  36.137  1.00 22.50 ? 255 GLN A CA  1 
ATOM   2051 C  C   . GLN A 1 254 ? -9.134  -2.331  34.919  1.00 19.69 ? 255 GLN A C   1 
ATOM   2052 O  O   . GLN A 1 254 ? -9.445  -1.256  34.417  1.00 23.11 ? 255 GLN A O   1 
ATOM   2053 C  CB  . GLN A 1 254 ? -8.945  -1.830  37.355  1.00 26.66 ? 255 GLN A CB  1 
ATOM   2054 C  CG  . GLN A 1 254 ? -9.879  -2.840  37.989  1.00 36.11 ? 255 GLN A CG  1 
ATOM   2055 C  CD  . GLN A 1 254 ? -10.608 -2.185  39.136  1.00 44.34 ? 255 GLN A CD  1 
ATOM   2056 O  OE1 . GLN A 1 254 ? -10.724 -0.955  39.210  1.00 48.32 ? 255 GLN A OE1 1 
ATOM   2057 N  NE2 . GLN A 1 254 ? -11.094 -3.014  40.045  1.00 43.64 ? 255 GLN A NE2 1 
ATOM   2058 N  N   . ILE A 1 255 ? -9.574  -3.502  34.450  1.00 17.67 ? 256 ILE A N   1 
ATOM   2059 C  CA  . ILE A 1 255 ? -10.588 -3.552  33.406  1.00 16.71 ? 256 ILE A CA  1 
ATOM   2060 C  C   . ILE A 1 255 ? -11.949 -3.565  34.088  1.00 15.67 ? 256 ILE A C   1 
ATOM   2061 O  O   . ILE A 1 255 ? -12.140 -4.281  35.082  1.00 15.18 ? 256 ILE A O   1 
ATOM   2062 C  CB  . ILE A 1 255 ? -10.403 -4.788  32.502  1.00 15.86 ? 256 ILE A CB  1 
ATOM   2063 C  CG1 . ILE A 1 255 ? -8.982  -4.771  31.922  1.00 17.69 ? 256 ILE A CG1 1 
ATOM   2064 C  CG2 . ILE A 1 255 ? -11.508 -4.869  31.437  1.00 15.33 ? 256 ILE A CG2 1 
ATOM   2065 C  CD1 . ILE A 1 255 ? -8.633  -6.039  31.165  1.00 17.86 ? 256 ILE A CD1 1 
ATOM   2066 N  N   . LYS A 1 256 ? -12.810 -2.649  33.615  1.00 14.05 ? 257 LYS A N   1 
ATOM   2067 C  CA  . LYS A 1 256 ? -14.172 -2.494  34.121  1.00 16.00 ? 257 LYS A CA  1 
ATOM   2068 C  C   . LYS A 1 256 ? -15.179 -3.152  33.192  1.00 15.63 ? 257 LYS A C   1 
ATOM   2069 O  O   . LYS A 1 256 ? -14.980 -3.140  31.965  1.00 17.58 ? 257 LYS A O   1 
ATOM   2070 C  CB  . LYS A 1 256 ? -14.446 -1.002  34.319  1.00 16.37 ? 257 LYS A CB  1 
ATOM   2071 C  CG  . LYS A 1 256 ? -13.697 -0.387  35.496  1.00 20.32 ? 257 LYS A CG  1 
ATOM   2072 C  CD  . LYS A 1 256 ? -14.322 -0.694  36.844  0.01 18.94 ? 257 LYS A CD  1 
ATOM   2073 C  CE  . LYS A 1 256 ? -13.767 0.153   37.971  0.01 19.11 ? 257 LYS A CE  1 
ATOM   2074 N  NZ  . LYS A 1 256 ? -14.234 1.558   37.885  0.01 19.16 ? 257 LYS A NZ  1 
ATOM   2075 N  N   . ALA A 1 257 ? -16.240 -3.768  33.746  1.00 15.48 ? 258 ALA A N   1 
ATOM   2076 C  CA  . ALA A 1 257 ? -17.273 -4.374  32.923  1.00 14.95 ? 258 ALA A CA  1 
ATOM   2077 C  C   . ALA A 1 257 ? -18.606 -3.646  33.115  1.00 16.66 ? 258 ALA A C   1 
ATOM   2078 O  O   . ALA A 1 257 ? -18.952 -3.296  34.253  1.00 16.50 ? 258 ALA A O   1 
ATOM   2079 C  CB  . ALA A 1 257 ? -17.419 -5.867  33.156  1.00 16.27 ? 258 ALA A CB  1 
ATOM   2080 N  N   . SER A 1 258 ? -19.386 -3.507  32.032  1.00 14.30 ? 259 SER A N   1 
ATOM   2081 C  CA  . SER A 1 258 ? -20.672 -2.816  32.085  1.00 16.54 ? 259 SER A CA  1 
ATOM   2082 C  C   . SER A 1 258 ? -21.792 -3.773  32.475  1.00 18.56 ? 259 SER A C   1 
ATOM   2083 O  O   . SER A 1 258 ? -22.938 -3.346  32.549  1.00 22.80 ? 259 SER A O   1 
ATOM   2084 C  CB  . SER A 1 258 ? -20.987 -2.202  30.722  1.00 15.59 ? 259 SER A CB  1 
ATOM   2085 O  OG  . SER A 1 258 ? -21.449 -3.157  29.781  1.00 17.64 ? 259 SER A OG  1 
ATOM   2086 N  N   . PHE A 1 259 ? -21.455 -5.041  32.731  1.00 19.75 ? 260 PHE A N   1 
ATOM   2087 C  CA  . PHE A 1 259 ? -22.410 -6.135  32.855  1.00 20.46 ? 260 PHE A CA  1 
ATOM   2088 C  C   . PHE A 1 259 ? -21.918 -7.111  33.923  1.00 26.11 ? 260 PHE A C   1 
ATOM   2089 O  O   . PHE A 1 259 ? -20.707 -7.231  34.158  1.00 23.11 ? 260 PHE A O   1 
ATOM   2090 C  CB  . PHE A 1 259 ? -22.623 -6.845  31.508  1.00 20.98 ? 260 PHE A CB  1 
ATOM   2091 C  CG  . PHE A 1 259 ? -21.371 -7.517  30.989  1.00 19.76 ? 260 PHE A CG  1 
ATOM   2092 C  CD1 . PHE A 1 259 ? -20.417 -6.770  30.325  1.00 18.05 ? 260 PHE A CD1 1 
ATOM   2093 C  CD2 . PHE A 1 259 ? -21.126 -8.867  31.199  1.00 19.56 ? 260 PHE A CD2 1 
ATOM   2094 C  CE1 . PHE A 1 259 ? -19.223 -7.352  29.917  1.00 19.20 ? 260 PHE A CE1 1 
ATOM   2095 C  CE2 . PHE A 1 259 ? -19.930 -9.445  30.796  1.00 21.18 ? 260 PHE A CE2 1 
ATOM   2096 C  CZ  . PHE A 1 259 ? -18.985 -8.687  30.127  1.00 18.61 ? 260 PHE A CZ  1 
ATOM   2097 N  N   . LYS A 1 260 ? -22.916 -7.773  34.545  1.00 32.98 ? 261 LYS A N   1 
ATOM   2098 C  CA  . LYS A 1 260 ? -22.865 -8.937  35.427  1.00 40.75 ? 261 LYS A CA  1 
ATOM   2099 C  C   . LYS A 1 260 ? -22.061 -8.644  36.696  1.00 46.44 ? 261 LYS A C   1 
ATOM   2100 O  O   . LYS A 1 260 ? -20.830 -8.646  36.710  0.01 45.99 ? 261 LYS A O   1 
ATOM   2101 C  CB  . LYS A 1 260 ? -22.491 -10.239 34.707  1.00 41.38 ? 261 LYS A CB  1 
ATOM   2102 C  CG  . LYS A 1 260 ? -23.361 -10.613 33.510  1.00 43.60 ? 261 LYS A CG  1 
ATOM   2103 C  CD  . LYS A 1 260 ? -22.951 -11.923 32.807  1.00 49.25 ? 261 LYS A CD  1 
ATOM   2104 C  CE  . LYS A 1 260 ? -21.450 -12.160 32.712  1.00 46.60 ? 261 LYS A CE  1 
ATOM   2105 N  NZ  . LYS A 1 260 ? -21.096 -13.521 32.239  1.00 46.88 ? 261 LYS A NZ  1 
ATOM   2106 O  OXT . LYS A 1 260 ? -22.671 -8.403  37.752  1.00 51.15 ? 261 LYS A OXT 1 
HETATM 2107 ZN ZN  . ZN  B 2 .   ? -6.570  -1.833  15.237  1.00 9.91  ? 301 ZN  A ZN  1 
HETATM 2108 S  S   . DMS C 3 .   ? 1.563   -11.828 15.034  1.00 37.05 ? 302 DMS A S   1 
HETATM 2109 O  O   . DMS C 3 .   ? 2.186   -13.179 14.633  1.00 31.19 ? 302 DMS A O   1 
HETATM 2110 C  C1  . DMS C 3 .   ? 2.132   -11.591 16.705  1.00 31.75 ? 302 DMS A C1  1 
HETATM 2111 C  C2  . DMS C 3 .   ? 2.573   -10.584 14.257  1.00 36.05 ? 302 DMS A C2  1 
HETATM 2112 O  O1  . MES D 4 .   ? -7.678  -9.139  -2.956  1.00 30.06 ? 303 MES A O1  1 
HETATM 2113 C  C2  . MES D 4 .   ? -8.307  -9.748  -1.830  1.00 24.02 ? 303 MES A C2  1 
HETATM 2114 C  C3  . MES D 4 .   ? -9.642  -10.379 -2.149  1.00 25.40 ? 303 MES A C3  1 
HETATM 2115 N  N4  . MES D 4 .   ? -9.705  -10.830 -3.582  1.00 25.45 ? 303 MES A N4  1 
HETATM 2116 C  C5  . MES D 4 .   ? -8.343  -11.233 -4.061  1.00 25.35 ? 303 MES A C5  1 
HETATM 2117 C  C6  . MES D 4 .   ? -7.392  -10.062 -4.012  1.00 24.08 ? 303 MES A C6  1 
HETATM 2118 C  C7  . MES D 4 .   ? -10.747 -11.879 -3.862  1.00 28.51 ? 303 MES A C7  1 
HETATM 2119 C  C8  . MES D 4 .   ? -12.115 -11.481 -3.347  1.00 24.00 ? 303 MES A C8  1 
HETATM 2120 C  C12 A JTW E 5 .   ? -3.844  2.359   12.286  0.50 16.95 ? 304 JTW A C12 1 
HETATM 2121 C  C12 B JTW E 5 .   ? -3.826  2.322   12.274  0.50 18.30 ? 304 JTW A C12 1 
HETATM 2122 C  C21 A JTW E 5 .   ? -2.608  4.923   11.953  0.50 18.26 ? 304 JTW A C21 1 
HETATM 2123 C  C21 B JTW E 5 .   ? -5.057  6.334   11.772  0.50 17.90 ? 304 JTW A C21 1 
HETATM 2124 C  C22 A JTW E 5 .   ? -1.399  4.582   12.582  0.50 18.78 ? 304 JTW A C22 1 
HETATM 2125 C  C22 B JTW E 5 .   ? -4.800  6.187   10.406  0.50 17.87 ? 304 JTW A C22 1 
HETATM 2126 C  C23 A JTW E 5 .   ? -0.328  4.078   11.838  0.50 18.38 ? 304 JTW A C23 1 
HETATM 2127 C  C23 B JTW E 5 .   ? -5.668  6.840   9.525   0.50 18.63 ? 304 JTW A C23 1 
HETATM 2128 C  C5  A JTW E 5 .   ? -5.410  2.100   15.654  0.50 11.56 ? 304 JTW A C5  1 
HETATM 2129 C  C5  B JTW E 5 .   ? -5.402  2.085   15.649  0.50 12.43 ? 304 JTW A C5  1 
HETATM 2130 C  C6  A JTW E 5 .   ? -5.639  3.428   15.974  0.50 12.58 ? 304 JTW A C6  1 
HETATM 2131 C  C6  B JTW E 5 .   ? -5.633  3.408   15.976  0.50 13.44 ? 304 JTW A C6  1 
HETATM 2132 C  C8  A JTW E 5 .   ? -4.636  4.161   13.959  0.50 15.63 ? 304 JTW A C8  1 
HETATM 2133 C  C8  B JTW E 5 .   ? -4.609  4.125   13.952  0.50 16.30 ? 304 JTW A C8  1 
HETATM 2134 C  C9  A JTW E 5 .   ? -4.393  2.815   13.588  0.50 15.62 ? 304 JTW A C9  1 
HETATM 2135 C  C9  B JTW E 5 .   ? -4.374  2.783   13.572  0.50 16.64 ? 304 JTW A C9  1 
HETATM 2136 C  C10 A JTW E 5 .   ? -4.826  1.798   14.425  0.50 13.73 ? 304 JTW A C10 1 
HETATM 2137 C  C10 B JTW E 5 .   ? -4.814  1.776   14.422  0.50 14.68 ? 304 JTW A C10 1 
HETATM 2138 O  O20 A JTW E 5 .   ? -5.151  5.993   12.018  0.50 16.80 ? 304 JTW A O20 1 
HETATM 2139 O  O20 B JTW E 5 .   ? -3.642  6.560   14.078  0.50 18.57 ? 304 JTW A O20 1 
HETATM 2140 S  S18 A JTW E 5 .   ? -4.009  5.497   12.921  0.50 17.72 ? 304 JTW A S18 1 
HETATM 2141 S  S18 B JTW E 5 .   ? -4.065  5.565   13.020  0.50 17.73 ? 304 JTW A S18 1 
HETATM 2142 O  O19 A JTW E 5 .   ? -3.705  6.618   13.904  0.50 18.22 ? 304 JTW A O19 1 
HETATM 2143 O  O19 B JTW E 5 .   ? -2.651  5.281   12.500  0.50 17.59 ? 304 JTW A O19 1 
HETATM 2144 C  C25 A JTW E 5 .   ? -2.757  4.706   10.575  0.50 19.59 ? 304 JTW A C25 1 
HETATM 2145 C  C25 B JTW E 5 .   ? -6.119  7.111   12.244  0.50 17.74 ? 304 JTW A C25 1 
HETATM 2146 C  C26 A JTW E 5 .   ? -1.687  4.210   9.822   0.50 19.88 ? 304 JTW A C26 1 
HETATM 2147 C  C26 B JTW E 5 .   ? -6.969  7.765   11.348  0.50 17.03 ? 304 JTW A C26 1 
HETATM 2148 C  C24 A JTW E 5 .   ? -0.473  3.890   10.454  0.50 19.17 ? 304 JTW A C24 1 
HETATM 2149 C  C24 B JTW E 5 .   ? -6.741  7.615   9.982   0.50 17.63 ? 304 JTW A C24 1 
HETATM 2150 C  C7  A JTW E 5 .   ? -5.225  4.471   15.168  0.50 13.98 ? 304 JTW A C7  1 
HETATM 2151 C  C7  B JTW E 5 .   ? -5.216  4.432   15.155  0.50 14.75 ? 304 JTW A C7  1 
HETATM 2152 CL CL1 A JTW E 5 .   ? -6.427  3.834   17.453  0.50 12.16 ? 304 JTW A CL1 1 
HETATM 2153 CL CL1 B JTW E 5 .   ? -6.423  3.830   17.453  0.50 13.08 ? 304 JTW A CL1 1 
HETATM 2154 S  S2  A JTW E 5 .   ? -5.895  0.729   16.686  0.50 10.35 ? 304 JTW A S2  1 
HETATM 2155 S  S2  B JTW E 5 .   ? -5.890  0.728   16.689  0.50 11.27 ? 304 JTW A S2  1 
HETATM 2156 O  O3  A JTW E 5 .   ? -5.383  0.881   18.128  0.50 10.22 ? 304 JTW A O3  1 
HETATM 2157 O  O3  B JTW E 5 .   ? -5.378  0.883   18.131  0.50 11.10 ? 304 JTW A O3  1 
HETATM 2158 O  O4  A JTW E 5 .   ? -7.400  0.669   16.713  0.50 9.73  ? 304 JTW A O4  1 
HETATM 2159 O  O4  B JTW E 5 .   ? -7.399  0.676   16.715  0.50 10.53 ? 304 JTW A O4  1 
HETATM 2160 N  N1  A JTW E 5 .   ? -5.227  -0.678  16.054  0.50 9.89  ? 304 JTW A N1  1 
HETATM 2161 N  N1  B JTW E 5 .   ? -5.231  -0.689  16.060  0.50 10.78 ? 304 JTW A N1  1 
HETATM 2162 O  O13 A JTW E 5 .   ? -4.554  2.677   11.315  0.50 18.66 ? 304 JTW A O13 1 
HETATM 2163 O  O13 B JTW E 5 .   ? -4.516  2.663   11.300  0.50 20.72 ? 304 JTW A O13 1 
HETATM 2164 N  N14 A JTW E 5 .   ? -2.774  1.558   12.108  0.50 20.13 ? 304 JTW A N14 1 
HETATM 2165 N  N14 B JTW E 5 .   ? -2.779  1.488   12.110  0.50 21.77 ? 304 JTW A N14 1 
HETATM 2166 C  C15 A JTW E 5 .   ? -2.389  1.073   10.795  0.50 24.09 ? 304 JTW A C15 1 
HETATM 2167 C  C15 B JTW E 5 .   ? -2.379  0.990   10.808  0.50 25.19 ? 304 JTW A C15 1 
HETATM 2168 C  C16 A JTW E 5 .   ? -3.034  -0.298  10.496  0.50 25.81 ? 304 JTW A C16 1 
HETATM 2169 C  C16 B JTW E 5 .   ? -3.096  -0.338  10.481  0.50 26.66 ? 304 JTW A C16 1 
HETATM 2170 O  O17 A JTW E 5 .   ? -3.881  -0.924  11.467  0.50 28.10 ? 304 JTW A O17 1 
HETATM 2171 O  O17 B JTW E 5 .   ? -3.882  -0.992  11.484  0.50 27.79 ? 304 JTW A O17 1 
HETATM 2172 O  O   . HOH F 6 .   ? -14.336 -8.337  -5.335  1.00 23.90 ? 401 HOH A O   1 
HETATM 2173 O  O   . HOH F 6 .   ? -25.393 9.607   13.219  1.00 29.76 ? 402 HOH A O   1 
HETATM 2174 O  O   . HOH F 6 .   ? 9.878   -4.613  -7.668  1.00 32.97 ? 403 HOH A O   1 
HETATM 2175 O  O   . HOH F 6 .   ? -17.858 18.990  6.013   1.00 19.24 ? 404 HOH A O   1 
HETATM 2176 O  O   . HOH F 6 .   ? -25.673 -10.615 17.645  1.00 26.89 ? 405 HOH A O   1 
HETATM 2177 O  O   . HOH F 6 .   ? -15.496 19.290  13.338  1.00 29.73 ? 406 HOH A O   1 
HETATM 2178 O  O   . HOH F 6 .   ? -15.469 -10.151 37.269  1.00 34.77 ? 407 HOH A O   1 
HETATM 2179 O  O   . HOH F 6 .   ? -11.649 -2.866  42.364  1.00 33.29 ? 408 HOH A O   1 
HETATM 2180 O  O   . HOH F 6 .   ? -5.805  5.478   6.300   1.00 41.23 ? 409 HOH A O   1 
HETATM 2181 O  O   . HOH F 6 .   ? 9.855   1.630   12.739  1.00 36.60 ? 410 HOH A O   1 
HETATM 2182 O  O   . HOH F 6 .   ? -14.257 -16.504 28.979  1.00 26.44 ? 411 HOH A O   1 
HETATM 2183 O  O   . HOH F 6 .   ? -4.850  2.104   37.390  1.00 31.94 ? 412 HOH A O   1 
HETATM 2184 O  O   . HOH F 6 .   ? -12.821 -22.112 8.425   1.00 27.51 ? 413 HOH A O   1 
HETATM 2185 O  O   . HOH F 6 .   ? -8.210  21.382  19.422  1.00 40.46 ? 414 HOH A O   1 
HETATM 2186 O  O   . HOH F 6 .   ? -14.977 20.103  17.895  1.00 31.22 ? 415 HOH A O   1 
HETATM 2187 O  O   . HOH F 6 .   ? 1.756   2.623   5.169   1.00 27.35 ? 416 HOH A O   1 
HETATM 2188 O  O   . HOH F 6 .   ? -7.734  7.217   27.435  1.00 27.19 ? 417 HOH A O   1 
HETATM 2189 O  O   . HOH F 6 .   ? -16.453 -14.667 32.859  1.00 33.12 ? 418 HOH A O   1 
HETATM 2190 O  O   . HOH F 6 .   ? -1.130  -4.146  15.648  1.00 9.98  ? 419 HOH A O   1 
HETATM 2191 O  O   . HOH F 6 .   ? -3.365  5.467   -2.693  1.00 23.44 ? 420 HOH A O   1 
HETATM 2192 O  O   . HOH F 6 .   ? 0.367   1.174   34.369  1.00 20.23 ? 421 HOH A O   1 
HETATM 2193 O  O   . HOH F 6 .   ? -5.906  -4.640  -6.521  1.00 23.70 ? 422 HOH A O   1 
HETATM 2194 O  O   . HOH F 6 .   ? -2.419  -8.679  29.165  1.00 14.66 ? 423 HOH A O   1 
HETATM 2195 O  O   . HOH F 6 .   ? -9.731  1.400   38.839  1.00 32.02 ? 424 HOH A O   1 
HETATM 2196 O  O   . HOH F 6 .   ? 0.825   -1.528  -4.732  1.00 28.08 ? 425 HOH A O   1 
HETATM 2197 O  O   . HOH F 6 .   ? -19.823 -17.106 3.104   1.00 29.19 ? 426 HOH A O   1 
HETATM 2198 O  O   . HOH F 6 .   ? -18.024 -20.502 8.027   1.00 15.68 ? 427 HOH A O   1 
HETATM 2199 O  O   . HOH F 6 .   ? -24.114 8.641   20.155  1.00 28.03 ? 428 HOH A O   1 
HETATM 2200 O  O   . HOH F 6 .   ? 3.767   5.206   29.683  1.00 19.36 ? 429 HOH A O   1 
HETATM 2201 O  O   . HOH F 6 .   ? -1.343  23.089  17.921  1.00 31.02 ? 430 HOH A O   1 
HETATM 2202 O  O   . HOH F 6 .   ? -11.074 -15.492 34.023  1.00 31.37 ? 431 HOH A O   1 
HETATM 2203 O  O   . HOH F 6 .   ? -3.462  -11.140 20.937  1.00 13.53 ? 432 HOH A O   1 
HETATM 2204 O  O   . HOH F 6 .   ? -10.272 14.700  11.967  1.00 22.29 ? 433 HOH A O   1 
HETATM 2205 O  O   . HOH F 6 .   ? -25.877 -6.310  13.107  1.00 26.64 ? 434 HOH A O   1 
HETATM 2206 O  O   . HOH F 6 .   ? 4.503   -3.490  26.355  1.00 22.68 ? 435 HOH A O   1 
HETATM 2207 O  O   . HOH F 6 .   ? -18.820 -12.106 -3.325  1.00 33.04 ? 436 HOH A O   1 
HETATM 2208 O  O   . HOH F 6 .   ? -8.213  -15.028 37.062  1.00 23.88 ? 437 HOH A O   1 
HETATM 2209 O  O   . HOH F 6 .   ? -8.498  -3.966  7.807   1.00 14.49 ? 438 HOH A O   1 
HETATM 2210 O  O   . HOH F 6 .   ? -13.304 -8.902  -3.310  1.00 23.83 ? 439 HOH A O   1 
HETATM 2211 O  O   . HOH F 6 .   ? 15.196  -2.480  14.390  1.00 21.26 ? 440 HOH A O   1 
HETATM 2212 O  O   . HOH F 6 .   ? -14.184 -4.731  -6.367  1.00 28.77 ? 441 HOH A O   1 
HETATM 2213 O  O   . HOH F 6 .   ? -16.138 15.769  23.600  1.00 26.54 ? 442 HOH A O   1 
HETATM 2214 O  O   . HOH F 6 .   ? -15.452 8.816   -2.115  1.00 25.84 ? 443 HOH A O   1 
HETATM 2215 O  O   . HOH F 6 .   ? -19.396 17.424  6.049   1.00 30.63 ? 444 HOH A O   1 
HETATM 2216 O  O   . HOH F 6 .   ? -17.849 10.451  11.381  1.00 17.60 ? 445 HOH A O   1 
HETATM 2217 O  O   . HOH F 6 .   ? -3.934  -13.118 -3.050  1.00 24.81 ? 446 HOH A O   1 
HETATM 2218 O  O   . HOH F 6 .   ? -10.488 8.693   25.636  1.00 16.66 ? 447 HOH A O   1 
HETATM 2219 O  O   . HOH F 6 .   ? -14.587 -18.611 18.852  1.00 25.83 ? 448 HOH A O   1 
HETATM 2220 O  O   . HOH F 6 .   ? -10.348 -18.252 17.033  1.00 21.72 ? 449 HOH A O   1 
HETATM 2221 O  O   . HOH F 6 .   ? -8.672  -1.322  40.899  1.00 36.48 ? 450 HOH A O   1 
HETATM 2222 O  O   . HOH F 6 .   ? -13.856 14.134  27.357  1.00 28.33 ? 451 HOH A O   1 
HETATM 2223 O  O   . HOH F 6 .   ? -0.993  9.349   27.868  1.00 30.81 ? 452 HOH A O   1 
HETATM 2224 O  O   . HOH F 6 .   ? -22.965 -2.973  6.429   1.00 21.32 ? 453 HOH A O   1 
HETATM 2225 O  O   . HOH F 6 .   ? -10.267 13.571  8.782   1.00 27.56 ? 454 HOH A O   1 
HETATM 2226 O  O   . HOH F 6 .   ? -19.503 -20.760 4.985   1.00 24.77 ? 455 HOH A O   1 
HETATM 2227 O  O   . HOH F 6 .   ? -0.397  14.223  16.042  1.00 29.89 ? 456 HOH A O   1 
HETATM 2228 O  O   . HOH F 6 .   ? 4.152   -2.304  28.740  1.00 31.25 ? 457 HOH A O   1 
HETATM 2229 O  O   . HOH F 6 .   ? -7.930  -15.463 11.234  1.00 11.26 ? 458 HOH A O   1 
HETATM 2230 O  O   . HOH F 6 .   ? -23.489 -11.237 17.291  1.00 30.92 ? 459 HOH A O   1 
HETATM 2231 O  O   . HOH F 6 .   ? -4.412  -13.583 17.960  1.00 11.78 ? 460 HOH A O   1 
HETATM 2232 O  O   . HOH F 6 .   ? -27.498 2.648   23.573  1.00 30.68 ? 461 HOH A O   1 
HETATM 2233 O  O   . HOH F 6 .   ? -13.955 10.623  27.811  1.00 26.47 ? 462 HOH A O   1 
HETATM 2234 O  O   . HOH F 6 .   ? -6.925  -14.977 31.659  1.00 21.43 ? 463 HOH A O   1 
HETATM 2235 O  O   . HOH F 6 .   ? -25.764 -15.029 8.253   1.00 30.48 ? 464 HOH A O   1 
HETATM 2236 O  O   . HOH F 6 .   ? -16.941 -8.373  20.418  1.00 11.33 ? 465 HOH A O   1 
HETATM 2237 O  O   . HOH F 6 .   ? -5.970  -11.193 36.324  1.00 33.13 ? 466 HOH A O   1 
HETATM 2238 O  O   . HOH F 6 .   ? -13.755 19.943  15.181  1.00 28.91 ? 467 HOH A O   1 
HETATM 2239 O  O   . HOH F 6 .   ? -22.654 -5.942  2.682   1.00 22.77 ? 468 HOH A O   1 
HETATM 2240 O  O   . HOH F 6 .   ? 2.804   -4.436  7.976   1.00 21.26 ? 469 HOH A O   1 
HETATM 2241 O  O   . HOH F 6 .   ? 15.720  3.187   15.431  1.00 34.99 ? 470 HOH A O   1 
HETATM 2242 O  O   . HOH F 6 .   ? -4.762  -11.918 32.173  1.00 26.11 ? 471 HOH A O   1 
HETATM 2243 O  O   . HOH F 6 .   ? 1.366   -11.824 25.026  1.00 25.91 ? 472 HOH A O   1 
HETATM 2244 O  O   . HOH F 6 .   ? 13.094  -5.845  24.540  1.00 30.41 ? 473 HOH A O   1 
HETATM 2245 O  O   . HOH F 6 .   ? -21.215 -6.791  -2.026  1.00 31.57 ? 474 HOH A O   1 
HETATM 2246 O  O   . HOH F 6 .   ? -24.775 -7.808  9.015   1.00 18.17 ? 475 HOH A O   1 
HETATM 2247 O  O   . HOH F 6 .   ? -8.385  0.487   -6.517  1.00 26.66 ? 476 HOH A O   1 
HETATM 2248 O  O   . HOH F 6 .   ? -20.445 10.773  26.507  1.00 23.25 ? 477 HOH A O   1 
HETATM 2249 O  O   . HOH F 6 .   ? -10.995 -19.564 7.065   1.00 26.83 ? 478 HOH A O   1 
HETATM 2250 O  O   . HOH F 6 .   ? 11.722  -0.384  15.973  1.00 29.23 ? 479 HOH A O   1 
HETATM 2251 O  O   . HOH F 6 .   ? -23.974 -0.790  26.464  1.00 19.82 ? 480 HOH A O   1 
HETATM 2252 O  O   . HOH F 6 .   ? 8.547   -3.851  21.107  1.00 18.31 ? 481 HOH A O   1 
HETATM 2253 O  O   . HOH F 6 .   ? -16.873 -7.162  39.809  1.00 28.00 ? 482 HOH A O   1 
HETATM 2254 O  O   . HOH F 6 .   ? -16.364 -10.006 32.924  1.00 19.22 ? 483 HOH A O   1 
HETATM 2255 O  O   . HOH F 6 .   ? 2.723   -13.451 5.144   1.00 22.56 ? 484 HOH A O   1 
HETATM 2256 O  O   . HOH F 6 .   ? -19.137 10.012  8.866   1.00 17.36 ? 485 HOH A O   1 
HETATM 2257 O  O   . HOH F 6 .   ? -21.502 5.613   4.627   1.00 16.53 ? 486 HOH A O   1 
HETATM 2258 O  O   . HOH F 6 .   ? -6.513  4.966   -5.958  1.00 33.26 ? 487 HOH A O   1 
HETATM 2259 O  O   . HOH F 6 .   ? -3.674  -15.985 24.411  1.00 16.29 ? 488 HOH A O   1 
HETATM 2260 O  O   . HOH F 6 .   ? -12.990 -16.863 26.603  1.00 24.08 ? 489 HOH A O   1 
HETATM 2261 O  O   . HOH F 6 .   ? 1.113   -6.563  34.414  1.00 31.36 ? 490 HOH A O   1 
HETATM 2262 O  O   . HOH F 6 .   ? 4.657   -6.712  7.939   1.00 26.83 ? 491 HOH A O   1 
HETATM 2263 O  O   . HOH F 6 .   ? -4.727  -15.950 0.636   1.00 24.83 ? 492 HOH A O   1 
HETATM 2264 O  O   . HOH F 6 .   ? -5.987  -19.672 23.702  1.00 28.34 ? 493 HOH A O   1 
HETATM 2265 O  O   . HOH F 6 .   ? -2.366  -3.356  11.312  1.00 18.79 ? 494 HOH A O   1 
HETATM 2266 O  O   . HOH F 6 .   ? 2.654   -11.432 9.691   1.00 24.91 ? 495 HOH A O   1 
HETATM 2267 O  O   . HOH F 6 .   ? -23.381 -13.519 11.407  1.00 25.69 ? 496 HOH A O   1 
HETATM 2268 O  O   . HOH F 6 .   ? 5.538   7.016   20.019  1.00 21.13 ? 497 HOH A O   1 
HETATM 2269 O  O   . HOH F 6 .   ? 1.182   -1.618  29.426  1.00 15.91 ? 498 HOH A O   1 
HETATM 2270 O  O   . HOH F 6 .   ? -20.792 7.801   1.752   1.00 17.02 ? 499 HOH A O   1 
HETATM 2271 O  O   . HOH F 6 .   ? -21.492 -7.131  23.546  1.00 16.13 ? 500 HOH A O   1 
HETATM 2272 O  O   . HOH F 6 .   ? -3.406  -13.334 25.245  1.00 13.86 ? 501 HOH A O   1 
HETATM 2273 O  O   . HOH F 6 .   ? -18.901 12.183  12.950  1.00 28.04 ? 502 HOH A O   1 
HETATM 2274 O  O   . HOH F 6 .   ? -25.941 6.186   26.932  1.00 27.33 ? 503 HOH A O   1 
HETATM 2275 O  O   . HOH F 6 .   ? 8.205   3.016   27.660  1.00 30.50 ? 504 HOH A O   1 
HETATM 2276 O  O   . HOH F 6 .   ? -7.240  -8.743  32.636  1.00 22.60 ? 505 HOH A O   1 
HETATM 2277 O  O   . HOH F 6 .   ? -13.122 -22.396 12.075  1.00 26.72 ? 506 HOH A O   1 
HETATM 2278 O  O   . HOH F 6 .   ? 11.364  1.723   25.964  1.00 23.30 ? 507 HOH A O   1 
HETATM 2279 O  O   . HOH F 6 .   ? 3.300   4.017   10.230  1.00 30.51 ? 508 HOH A O   1 
HETATM 2280 O  O   . HOH F 6 .   ? -26.631 -4.008  25.232  1.00 26.73 ? 509 HOH A O   1 
HETATM 2281 O  O   . HOH F 6 .   ? 4.940   -4.941  20.929  1.00 16.97 ? 510 HOH A O   1 
HETATM 2282 O  O   . HOH F 6 .   ? -17.273 -16.444 21.805  1.00 31.95 ? 511 HOH A O   1 
HETATM 2283 O  O   . HOH F 6 .   ? -16.018 -12.449 24.385  1.00 21.55 ? 512 HOH A O   1 
HETATM 2284 O  O   . HOH F 6 .   ? -4.134  -8.764  31.204  1.00 27.82 ? 513 HOH A O   1 
HETATM 2285 O  O   . HOH F 6 .   ? -8.218  -22.197 10.238  1.00 19.50 ? 514 HOH A O   1 
HETATM 2286 O  O   . HOH F 6 .   ? -8.309  -19.847 26.610  1.00 27.25 ? 515 HOH A O   1 
HETATM 2287 O  O   . HOH F 6 .   ? -24.190 -17.887 6.742   1.00 29.18 ? 516 HOH A O   1 
HETATM 2288 O  O   . HOH F 6 .   ? -0.473  10.962  23.371  1.00 23.57 ? 517 HOH A O   1 
HETATM 2289 O  O   . HOH F 6 .   ? -12.097 3.078   30.755  1.00 27.60 ? 518 HOH A O   1 
HETATM 2290 O  O   . HOH F 6 .   ? -23.555 -0.870  3.814   1.00 21.31 ? 519 HOH A O   1 
HETATM 2291 O  O   . HOH F 6 .   ? -7.052  -16.947 1.273   1.00 24.67 ? 520 HOH A O   1 
HETATM 2292 O  O   . HOH F 6 .   ? -18.478 -9.097  34.369  1.00 29.61 ? 521 HOH A O   1 
HETATM 2293 O  O   . HOH F 6 .   ? -13.407 -18.797 14.752  1.00 23.79 ? 522 HOH A O   1 
HETATM 2294 O  O   . HOH F 6 .   ? -18.305 -3.588  -2.710  1.00 29.57 ? 523 HOH A O   1 
HETATM 2295 O  O   . HOH F 6 .   ? -16.373 -16.324 -4.053  1.00 32.59 ? 524 HOH A O   1 
HETATM 2296 O  O   . HOH F 6 .   ? -12.161 16.038  7.748   1.00 32.14 ? 525 HOH A O   1 
HETATM 2297 O  O   . HOH F 6 .   ? 13.355  0.523   24.475  1.00 20.09 ? 526 HOH A O   1 
HETATM 2298 O  O   . HOH F 6 .   ? 14.044  5.782   19.392  1.00 34.65 ? 527 HOH A O   1 
HETATM 2299 O  O   . HOH F 6 .   ? -7.952  -19.346 21.649  1.00 21.16 ? 528 HOH A O   1 
HETATM 2300 O  O   . HOH F 6 .   ? -22.167 -18.440 13.612  1.00 22.02 ? 529 HOH A O   1 
HETATM 2301 O  O   . HOH F 6 .   ? 1.310   8.964   24.318  1.00 21.87 ? 530 HOH A O   1 
HETATM 2302 O  O   . HOH F 6 .   ? -21.308 -19.669 6.658   1.00 31.70 ? 531 HOH A O   1 
HETATM 2303 O  O   . HOH F 6 .   ? -9.554  -8.037  34.013  1.00 21.36 ? 532 HOH A O   1 
HETATM 2304 O  O   . HOH F 6 .   ? -12.193 16.361  11.053  1.00 30.72 ? 533 HOH A O   1 
HETATM 2305 O  O   . HOH F 6 .   ? 8.104   -5.906  -10.404 1.00 24.56 ? 534 HOH A O   1 
HETATM 2306 O  O   . HOH F 6 .   ? -24.726 4.587   8.073   1.00 29.18 ? 535 HOH A O   1 
HETATM 2307 O  O   . HOH F 6 .   ? -8.927  -6.099  35.860  1.00 22.98 ? 536 HOH A O   1 
HETATM 2308 O  O   . HOH F 6 .   ? -23.376 -0.828  34.312  1.00 25.36 ? 537 HOH A O   1 
HETATM 2309 O  O   . HOH F 6 .   ? -2.006  -12.434 22.862  1.00 12.94 ? 538 HOH A O   1 
HETATM 2310 O  O   . HOH F 6 .   ? -8.443  -17.465 34.595  1.00 27.07 ? 539 HOH A O   1 
HETATM 2311 O  O   . HOH F 6 .   ? -17.796 4.026   -3.731  1.00 37.37 ? 540 HOH A O   1 
HETATM 2312 O  O   . HOH F 6 .   ? -6.556  15.687  11.660  1.00 32.57 ? 541 HOH A O   1 
HETATM 2313 O  O   . HOH F 6 .   ? 8.278   -8.598  -0.264  1.00 30.74 ? 542 HOH A O   1 
HETATM 2314 O  O   . HOH F 6 .   ? -0.561  -8.631  32.393  1.00 27.47 ? 543 HOH A O   1 
HETATM 2315 O  O   . HOH F 6 .   ? -24.857 -9.504  1.998   1.00 27.22 ? 544 HOH A O   1 
HETATM 2316 O  O   . HOH F 6 .   ? -23.083 -11.739 14.169  1.00 22.18 ? 545 HOH A O   1 
HETATM 2317 O  O   . HOH F 6 .   ? 7.593   6.251   21.625  1.00 20.79 ? 546 HOH A O   1 
HETATM 2318 O  O   . HOH F 6 .   ? 9.066   7.721   18.704  1.00 30.71 ? 547 HOH A O   1 
HETATM 2319 O  O   . HOH F 6 .   ? -1.477  -13.227 27.377  1.00 23.72 ? 548 HOH A O   1 
HETATM 2320 O  O   . HOH F 6 .   ? -17.275 17.755  4.113   1.00 31.66 ? 549 HOH A O   1 
HETATM 2321 O  O   . HOH F 6 .   ? 10.320  -2.551  13.718  1.00 27.35 ? 550 HOH A O   1 
HETATM 2322 O  O   . HOH F 6 .   ? 2.680   -13.295 8.103   1.00 28.64 ? 551 HOH A O   1 
HETATM 2323 O  O   . HOH F 6 .   ? -5.045  9.315   6.891   1.00 36.73 ? 552 HOH A O   1 
HETATM 2324 O  O   . HOH F 6 .   ? -12.775 -17.289 16.829  1.00 19.03 ? 553 HOH A O   1 
HETATM 2325 O  O   . HOH F 6 .   ? 0.002   -14.214 22.350  1.00 28.54 ? 554 HOH A O   1 
HETATM 2326 O  O   . HOH F 6 .   ? 5.492   -7.162  22.326  1.00 29.16 ? 555 HOH A O   1 
HETATM 2327 O  O   . HOH F 6 .   ? 0.816   0.393   -6.672  1.00 36.24 ? 556 HOH A O   1 
HETATM 2328 O  O   . HOH F 6 .   ? 3.281   -14.908 -6.426  1.00 44.72 ? 557 HOH A O   1 
HETATM 2329 O  O   . HOH F 6 .   ? -15.053 16.543  28.971  1.00 43.07 ? 558 HOH A O   1 
HETATM 2330 O  O   . HOH F 6 .   ? -15.352 -19.691 23.710  1.00 40.37 ? 559 HOH A O   1 
HETATM 2331 O  O   . HOH F 6 .   ? 8.815   -4.629  23.637  1.00 27.32 ? 560 HOH A O   1 
HETATM 2332 O  O   . HOH F 6 .   ? -14.918 11.071  35.145  1.00 35.30 ? 561 HOH A O   1 
HETATM 2333 O  O   . HOH F 6 .   ? -1.019  11.566  25.729  1.00 37.68 ? 562 HOH A O   1 
HETATM 2334 O  O   . HOH F 6 .   ? -17.792 19.785  17.750  1.00 25.88 ? 563 HOH A O   1 
HETATM 2335 O  O   . HOH F 6 .   ? -17.685 -12.327 31.911  1.00 35.12 ? 564 HOH A O   1 
HETATM 2336 O  O   . HOH F 6 .   ? 14.383  -0.119  14.899  1.00 28.69 ? 565 HOH A O   1 
HETATM 2337 O  O   . HOH F 6 .   ? 1.495   12.507  22.804  1.00 29.47 ? 566 HOH A O   1 
HETATM 2338 O  O   . HOH F 6 .   ? -16.943 -18.127 20.199  1.00 32.28 ? 567 HOH A O   1 
HETATM 2339 O  O   . HOH F 6 .   ? -1.824  -11.956 31.272  1.00 32.19 ? 568 HOH A O   1 
HETATM 2340 O  O   . HOH F 6 .   ? -27.800 4.948   25.596  1.00 34.22 ? 569 HOH A O   1 
HETATM 2341 O  O   . HOH F 6 .   ? -19.663 -15.817 22.477  1.00 30.70 ? 570 HOH A O   1 
HETATM 2342 O  O   . HOH F 6 .   ? -1.855  -17.405 25.304  1.00 28.96 ? 571 HOH A O   1 
HETATM 2343 O  O   . HOH F 6 .   ? 4.209   6.721   12.932  1.00 40.06 ? 572 HOH A O   1 
HETATM 2344 O  O   . HOH F 6 .   ? 15.354  -1.251  26.021  1.00 26.41 ? 573 HOH A O   1 
HETATM 2345 O  O   . HOH F 6 .   ? 4.058   4.999   2.500   1.00 29.33 ? 574 HOH A O   1 
HETATM 2346 O  O   . HOH F 6 .   ? -23.919 -7.199  0.117   1.00 30.11 ? 575 HOH A O   1 
HETATM 2347 O  O   . HOH F 6 .   ? -16.797 -13.948 26.514  1.00 30.10 ? 576 HOH A O   1 
HETATM 2348 O  O   . HOH F 6 .   ? -0.955  -11.209 29.023  1.00 22.37 ? 577 HOH A O   1 
HETATM 2349 O  O   . HOH F 6 .   ? 1.696   9.730   26.663  1.00 30.02 ? 578 HOH A O   1 
HETATM 2350 O  O   . HOH F 6 .   ? 6.429   5.399   28.570  1.00 36.54 ? 579 HOH A O   1 
HETATM 2351 O  O   . HOH F 6 .   ? 4.488   -11.605 23.421  1.00 31.89 ? 580 HOH A O   1 
HETATM 2352 O  O   . HOH F 6 .   ? 2.318   -14.395 20.678  1.00 35.88 ? 581 HOH A O   1 
HETATM 2353 O  O   . HOH F 6 .   ? 3.896   9.751   23.624  1.00 27.99 ? 582 HOH A O   1 
# 
