data_6RMX
# 
_entry.id   6RMX 
# 
_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   6RMX         pdb_00006rmx 10.2210/pdb6rmx/pdb 
WWPDB D_1292102202 ?            ?                   
# 
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 2020-06-03 
2 'Structure model' 1 1 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' Advisory                 
2 2 'Structure model' 'Data collection'        
3 2 'Structure model' 'Database references'    
4 2 'Structure model' 'Derived calculations'   
5 2 'Structure model' 'Refinement description' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' chem_comp_atom                
2 2 'Structure model' chem_comp_bond                
3 2 'Structure model' database_2                    
4 2 'Structure model' pdbx_initial_refinement_model 
5 2 'Structure model' pdbx_struct_conn_angle        
6 2 'Structure model' pdbx_unobs_or_zero_occ_atoms  
7 2 'Structure model' refine                        
8 2 'Structure model' struct_conn                   
# 
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'         
3  2 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_comp_id'  
4  2 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_seq_id'   
5  2 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_asym_id' 
6  2 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_atom_id' 
7  2 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_comp_id' 
8  2 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_seq_id'  
9  2 'Structure model' '_pdbx_struct_conn_angle.ptnr1_symmetry'      
10 2 'Structure model' '_pdbx_struct_conn_angle.ptnr2_auth_comp_id'  
11 2 'Structure model' '_pdbx_struct_conn_angle.ptnr2_auth_seq_id'   
12 2 'Structure model' '_pdbx_struct_conn_angle.ptnr2_label_asym_id' 
13 2 'Structure model' '_pdbx_struct_conn_angle.ptnr2_label_atom_id' 
14 2 'Structure model' '_pdbx_struct_conn_angle.ptnr2_label_comp_id' 
15 2 'Structure model' '_pdbx_struct_conn_angle.ptnr2_symmetry'      
16 2 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_comp_id'  
17 2 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_seq_id'   
18 2 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_asym_id' 
19 2 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_atom_id' 
20 2 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_comp_id' 
21 2 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_seq_id'  
22 2 'Structure model' '_pdbx_struct_conn_angle.ptnr3_symmetry'      
23 2 'Structure model' '_pdbx_struct_conn_angle.value'               
24 2 'Structure model' '_refine.pdbx_diffrn_id'                      
25 2 'Structure model' '_struct_conn.pdbx_dist_value'                
26 2 'Structure model' '_struct_conn.ptnr1_auth_comp_id'             
27 2 'Structure model' '_struct_conn.ptnr1_auth_seq_id'              
28 2 'Structure model' '_struct_conn.ptnr1_label_asym_id'            
29 2 'Structure model' '_struct_conn.ptnr1_label_atom_id'            
30 2 'Structure model' '_struct_conn.ptnr1_label_comp_id'            
31 2 'Structure model' '_struct_conn.ptnr1_label_seq_id'             
32 2 'Structure model' '_struct_conn.ptnr2_auth_comp_id'             
33 2 'Structure model' '_struct_conn.ptnr2_auth_seq_id'              
34 2 'Structure model' '_struct_conn.ptnr2_label_asym_id'            
35 2 'Structure model' '_struct_conn.ptnr2_label_atom_id'            
36 2 'Structure model' '_struct_conn.ptnr2_label_comp_id'            
37 2 'Structure model' '_struct_conn.ptnr2_symmetry'                 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        6RMX 
_pdbx_database_status.recvd_initial_deposition_date   2019-05-07 
_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 0000-0001-5080-9367 
'Paketuryte, V.' 2 0000-0003-0919-7826 
'Manakova, E.'   3 0000-0002-6027-2265 
'Grazulis, S.'   4 0000-0002-7928-5218 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
;Human Carbonic anhydrase II mutant T199V bound by 2-[(1S)-2,3-Dihydro-1H-inden-1-ylamino]-3,5,6-trifluoro-4-[(2-hydroxyethyl)thio]benzenesulfonamide
;
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Smirnov, A.'    1 ? 
primary 'Manakova, E.'   2 ? 
primary 'Paketuryte, V.' 3 ? 
# 
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'                                                                                   
28930.668 1   4.2.1.1 T199V 'Human Carbonic anhydrase II mutant T199V' ? 
2 non-polymer syn 'ZINC ION'                                                                                               65.409 
1   ?       ?     ?                                          ? 
3 non-polymer syn 'SODIUM ION'                                                                                             22.990 
1   ?       ?     ?                                          ? 
4 non-polymer syn '2-[(1S)-2,3-dihydro-1H-inden-1-ylamino]-3,5,6-trifluoro-4-[(2-hydroxyethyl)sulfanyl]benzenesulfonamide' 418.454 
1   ?       ?     ?                                          ? 
5 non-polymer syn 'DIMETHYL SULFOXIDE'                                                                                     78.133 
1   ?       ?     ?                                          ? 
6 non-polymer syn 'BENZOIC ACID'                                                                                           122.121 
1   ?       ?     ?                                          ? 
7 water       nat water                                                                                                    18.015 
217 ?       ?     ?                                          ? 
# 
_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       
;HWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLKGGP
LDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVVDVL
DSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTVPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELMVDN
WRPAQPLKNRQIKASFK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;HWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLKGGP
LDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVVDVL
DSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTVPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELMVDN
WRPAQPLKNRQIKASFK
;
_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 'SODIUM ION'                                                                                             NA  
4 '2-[(1S)-2,3-dihydro-1H-inden-1-ylamino]-3,5,6-trifluoro-4-[(2-hydroxyethyl)sulfanyl]benzenesulfonamide' 5DU 
5 'DIMETHYL SULFOXIDE'                                                                                     DMS 
6 'BENZOIC ACID'                                                                                           BEZ 
7 water                                                                                                    HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   HIS n 
1 2   TRP n 
1 3   GLY n 
1 4   TYR n 
1 5   GLY n 
1 6   LYS n 
1 7   HIS n 
1 8   ASN n 
1 9   GLY n 
1 10  PRO n 
1 11  GLU n 
1 12  HIS n 
1 13  TRP n 
1 14  HIS n 
1 15  LYS n 
1 16  ASP n 
1 17  PHE n 
1 18  PRO n 
1 19  ILE n 
1 20  ALA n 
1 21  LYS n 
1 22  GLY n 
1 23  GLU n 
1 24  ARG n 
1 25  GLN n 
1 26  SER n 
1 27  PRO n 
1 28  VAL n 
1 29  ASP n 
1 30  ILE n 
1 31  ASP n 
1 32  THR n 
1 33  HIS n 
1 34  THR n 
1 35  ALA n 
1 36  LYS n 
1 37  TYR n 
1 38  ASP n 
1 39  PRO n 
1 40  SER n 
1 41  LEU n 
1 42  LYS n 
1 43  PRO n 
1 44  LEU n 
1 45  SER n 
1 46  VAL n 
1 47  SER n 
1 48  TYR n 
1 49  ASP n 
1 50  GLN n 
1 51  ALA n 
1 52  THR n 
1 53  SER n 
1 54  LEU n 
1 55  ARG n 
1 56  ILE n 
1 57  LEU n 
1 58  ASN n 
1 59  ASN n 
1 60  GLY n 
1 61  HIS n 
1 62  ALA n 
1 63  PHE n 
1 64  ASN n 
1 65  VAL n 
1 66  GLU n 
1 67  PHE n 
1 68  ASP n 
1 69  ASP n 
1 70  SER n 
1 71  GLN n 
1 72  ASP n 
1 73  LYS n 
1 74  ALA n 
1 75  VAL n 
1 76  LEU n 
1 77  LYS n 
1 78  GLY n 
1 79  GLY n 
1 80  PRO n 
1 81  LEU n 
1 82  ASP n 
1 83  GLY n 
1 84  THR n 
1 85  TYR n 
1 86  ARG n 
1 87  LEU n 
1 88  ILE n 
1 89  GLN n 
1 90  PHE n 
1 91  HIS n 
1 92  PHE n 
1 93  HIS n 
1 94  TRP n 
1 95  GLY n 
1 96  SER n 
1 97  LEU n 
1 98  ASP n 
1 99  GLY n 
1 100 GLN n 
1 101 GLY n 
1 102 SER n 
1 103 GLU n 
1 104 HIS n 
1 105 THR n 
1 106 VAL n 
1 107 ASP n 
1 108 LYS n 
1 109 LYS n 
1 110 LYS n 
1 111 TYR n 
1 112 ALA n 
1 113 ALA n 
1 114 GLU n 
1 115 LEU n 
1 116 HIS n 
1 117 LEU n 
1 118 VAL n 
1 119 HIS n 
1 120 TRP n 
1 121 ASN n 
1 122 THR n 
1 123 LYS n 
1 124 TYR n 
1 125 GLY n 
1 126 ASP n 
1 127 PHE n 
1 128 GLY n 
1 129 LYS n 
1 130 ALA n 
1 131 VAL n 
1 132 GLN n 
1 133 GLN n 
1 134 PRO n 
1 135 ASP n 
1 136 GLY n 
1 137 LEU n 
1 138 ALA n 
1 139 VAL n 
1 140 LEU n 
1 141 GLY n 
1 142 ILE n 
1 143 PHE n 
1 144 LEU n 
1 145 LYS n 
1 146 VAL n 
1 147 GLY n 
1 148 SER n 
1 149 ALA n 
1 150 LYS n 
1 151 PRO n 
1 152 GLY n 
1 153 LEU n 
1 154 GLN n 
1 155 LYS n 
1 156 VAL n 
1 157 VAL n 
1 158 ASP n 
1 159 VAL n 
1 160 LEU n 
1 161 ASP n 
1 162 SER n 
1 163 ILE n 
1 164 LYS n 
1 165 THR n 
1 166 LYS n 
1 167 GLY n 
1 168 LYS n 
1 169 SER n 
1 170 ALA n 
1 171 ASP n 
1 172 PHE n 
1 173 THR n 
1 174 ASN n 
1 175 PHE n 
1 176 ASP n 
1 177 PRO n 
1 178 ARG n 
1 179 GLY n 
1 180 LEU n 
1 181 LEU n 
1 182 PRO n 
1 183 GLU n 
1 184 SER n 
1 185 LEU n 
1 186 ASP n 
1 187 TYR n 
1 188 TRP n 
1 189 THR n 
1 190 TYR n 
1 191 PRO n 
1 192 GLY n 
1 193 SER n 
1 194 LEU n 
1 195 THR n 
1 196 VAL n 
1 197 PRO n 
1 198 PRO n 
1 199 LEU n 
1 200 LEU n 
1 201 GLU n 
1 202 CYS n 
1 203 VAL n 
1 204 THR n 
1 205 TRP n 
1 206 ILE n 
1 207 VAL n 
1 208 LEU n 
1 209 LYS n 
1 210 GLU n 
1 211 PRO n 
1 212 ILE n 
1 213 SER n 
1 214 VAL n 
1 215 SER n 
1 216 SER n 
1 217 GLU n 
1 218 GLN n 
1 219 VAL n 
1 220 LEU n 
1 221 LYS n 
1 222 PHE n 
1 223 ARG n 
1 224 LYS n 
1 225 LEU n 
1 226 ASN n 
1 227 PHE n 
1 228 ASN n 
1 229 GLY n 
1 230 GLU n 
1 231 GLY n 
1 232 GLU n 
1 233 PRO n 
1 234 GLU n 
1 235 GLU n 
1 236 LEU n 
1 237 MET n 
1 238 VAL n 
1 239 ASP n 
1 240 ASN n 
1 241 TRP n 
1 242 ARG n 
1 243 PRO n 
1 244 ALA n 
1 245 GLN n 
1 246 PRO n 
1 247 LEU n 
1 248 LYS n 
1 249 ASN n 
1 250 ARG n 
1 251 GLN n 
1 252 ILE n 
1 253 LYS n 
1 254 ALA n 
1 255 SER n 
1 256 PHE n 
1 257 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                   257 
_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 
5DU non-polymer         . '2-[(1S)-2,3-dihydro-1H-inden-1-ylamino]-3,5,6-trifluoro-4-[(2-hydroxyethyl)sulfanyl]benzenesulfonamide' 
? 'C17 H17 F3 N2 O3 S2' 418.454 
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 
BEZ non-polymer         . 'BENZOIC ACID'                                                                                           
? 'C7 H6 O2'            122.121 
CYS 'L-peptide linking' y CYSTEINE                                                                                                 
? 'C3 H7 N O2 S'        121.158 
DMS non-polymer         . 'DIMETHYL SULFOXIDE'                                                                                     
? 'C2 H6 O S'           78.133  
GLN 'L-peptide linking' y GLUTAMINE                                                                                                
? 'C5 H10 N2 O3'        146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                                                                          
? 'C5 H9 N O4'          147.129 
GLY 'peptide linking'   y GLYCINE                                                                                                  
? 'C2 H5 N O2'          75.067  
HIS 'L-peptide linking' y HISTIDINE                                                                                                
? 'C6 H10 N3 O2 1'      156.162 
HOH non-polymer         . WATER                                                                                                    
? 'H2 O'                18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                                                                               
? 'C6 H13 N O2'         131.173 
LEU 'L-peptide linking' y LEUCINE                                                                                                  
? 'C6 H13 N O2'         131.173 
LYS 'L-peptide linking' y LYSINE                                                                                                   
? 'C6 H15 N2 O2 1'      147.195 
MET 'L-peptide linking' y METHIONINE                                                                                               
? 'C5 H11 N O2 S'       149.211 
NA  non-polymer         . 'SODIUM ION'                                                                                             
? 'Na 1'                22.990  
PHE 'L-peptide linking' y PHENYLALANINE                                                                                            
? 'C9 H11 N O2'         165.189 
PRO 'L-peptide linking' y PROLINE                                                                                                  
? 'C5 H9 N O2'          115.130 
SER 'L-peptide linking' y SERINE                                                                                                   
? 'C3 H7 N O3'          105.093 
THR 'L-peptide linking' y THREONINE                                                                                                
? 'C4 H9 N O3'          119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                                                                               
? 'C11 H12 N2 O2'       204.225 
TYR 'L-peptide linking' y TYROSINE                                                                                                 
? 'C9 H11 N O3'         181.189 
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   HIS 1   4   4   HIS HIS A . n 
A 1 2   TRP 2   5   5   TRP TRP A . n 
A 1 3   GLY 3   6   6   GLY GLY A . n 
A 1 4   TYR 4   7   7   TYR TYR A . n 
A 1 5   GLY 5   8   8   GLY GLY A . n 
A 1 6   LYS 6   9   9   LYS LYS A . n 
A 1 7   HIS 7   10  10  HIS HIS A . n 
A 1 8   ASN 8   11  11  ASN ASN A . n 
A 1 9   GLY 9   12  12  GLY GLY A . n 
A 1 10  PRO 10  13  13  PRO PRO A . n 
A 1 11  GLU 11  14  14  GLU GLU A . n 
A 1 12  HIS 12  15  15  HIS HIS A . n 
A 1 13  TRP 13  16  16  TRP TRP A . n 
A 1 14  HIS 14  17  17  HIS HIS A . n 
A 1 15  LYS 15  18  18  LYS LYS A . n 
A 1 16  ASP 16  19  19  ASP ASP A . n 
A 1 17  PHE 17  20  20  PHE PHE A . n 
A 1 18  PRO 18  21  21  PRO PRO A . n 
A 1 19  ILE 19  22  22  ILE ILE A . n 
A 1 20  ALA 20  23  23  ALA ALA A . n 
A 1 21  LYS 21  24  24  LYS LYS A . n 
A 1 22  GLY 22  25  25  GLY GLY A . n 
A 1 23  GLU 23  26  26  GLU GLU A . n 
A 1 24  ARG 24  27  27  ARG ARG A . n 
A 1 25  GLN 25  28  28  GLN GLN A . n 
A 1 26  SER 26  29  29  SER SER A . n 
A 1 27  PRO 27  30  30  PRO PRO A . n 
A 1 28  VAL 28  31  31  VAL VAL A . n 
A 1 29  ASP 29  32  32  ASP ASP A . n 
A 1 30  ILE 30  33  33  ILE ILE A . n 
A 1 31  ASP 31  34  34  ASP ASP A . n 
A 1 32  THR 32  35  35  THR THR A . n 
A 1 33  HIS 33  36  36  HIS HIS A . n 
A 1 34  THR 34  37  37  THR THR A . n 
A 1 35  ALA 35  38  38  ALA ALA A . n 
A 1 36  LYS 36  39  39  LYS LYS A . n 
A 1 37  TYR 37  40  40  TYR TYR A . n 
A 1 38  ASP 38  41  41  ASP ASP A . n 
A 1 39  PRO 39  42  42  PRO PRO A . n 
A 1 40  SER 40  43  43  SER SER A . n 
A 1 41  LEU 41  44  44  LEU LEU A . n 
A 1 42  LYS 42  45  45  LYS LYS A . n 
A 1 43  PRO 43  46  46  PRO PRO A . n 
A 1 44  LEU 44  47  47  LEU LEU A . n 
A 1 45  SER 45  48  48  SER SER A . n 
A 1 46  VAL 46  49  49  VAL VAL A . n 
A 1 47  SER 47  50  50  SER SER A . n 
A 1 48  TYR 48  51  51  TYR TYR A . n 
A 1 49  ASP 49  52  52  ASP ASP A . n 
A 1 50  GLN 50  53  53  GLN GLN A . n 
A 1 51  ALA 51  54  54  ALA ALA A . n 
A 1 52  THR 52  55  55  THR THR A . n 
A 1 53  SER 53  56  56  SER SER A . n 
A 1 54  LEU 54  57  57  LEU LEU A . n 
A 1 55  ARG 55  58  58  ARG ARG A . n 
A 1 56  ILE 56  59  59  ILE ILE A . n 
A 1 57  LEU 57  60  60  LEU LEU A . n 
A 1 58  ASN 58  61  61  ASN ASN A . n 
A 1 59  ASN 59  62  62  ASN ASN A . n 
A 1 60  GLY 60  63  63  GLY GLY A . n 
A 1 61  HIS 61  64  64  HIS HIS A . n 
A 1 62  ALA 62  65  65  ALA ALA A . n 
A 1 63  PHE 63  66  66  PHE PHE A . n 
A 1 64  ASN 64  67  67  ASN ASN A . n 
A 1 65  VAL 65  68  68  VAL VAL A . n 
A 1 66  GLU 66  69  69  GLU GLU A . n 
A 1 67  PHE 67  70  70  PHE PHE A . n 
A 1 68  ASP 68  71  71  ASP ASP A . n 
A 1 69  ASP 69  72  72  ASP ASP A . n 
A 1 70  SER 70  73  73  SER SER A . n 
A 1 71  GLN 71  74  74  GLN GLN A . n 
A 1 72  ASP 72  75  75  ASP ASP A . n 
A 1 73  LYS 73  76  76  LYS LYS A . n 
A 1 74  ALA 74  77  77  ALA ALA A . n 
A 1 75  VAL 75  78  78  VAL VAL A . n 
A 1 76  LEU 76  79  79  LEU LEU A . n 
A 1 77  LYS 77  80  80  LYS LYS A . n 
A 1 78  GLY 78  81  81  GLY GLY A . n 
A 1 79  GLY 79  82  82  GLY GLY A . n 
A 1 80  PRO 80  83  83  PRO PRO A . n 
A 1 81  LEU 81  84  84  LEU LEU A . n 
A 1 82  ASP 82  85  85  ASP ASP A . n 
A 1 83  GLY 83  86  86  GLY GLY A . n 
A 1 84  THR 84  87  87  THR THR A . n 
A 1 85  TYR 85  88  88  TYR TYR A . n 
A 1 86  ARG 86  89  89  ARG ARG A . n 
A 1 87  LEU 87  90  90  LEU LEU A . n 
A 1 88  ILE 88  91  91  ILE ILE A . n 
A 1 89  GLN 89  92  92  GLN GLN A . n 
A 1 90  PHE 90  93  93  PHE PHE A . n 
A 1 91  HIS 91  94  94  HIS HIS A . n 
A 1 92  PHE 92  95  95  PHE PHE A . n 
A 1 93  HIS 93  96  96  HIS HIS A . n 
A 1 94  TRP 94  97  97  TRP TRP A . n 
A 1 95  GLY 95  98  98  GLY GLY A . n 
A 1 96  SER 96  99  99  SER SER A . n 
A 1 97  LEU 97  100 100 LEU LEU A . n 
A 1 98  ASP 98  101 101 ASP ASP A . n 
A 1 99  GLY 99  102 102 GLY GLY A . n 
A 1 100 GLN 100 103 103 GLN GLN A . n 
A 1 101 GLY 101 104 104 GLY GLY A . n 
A 1 102 SER 102 105 105 SER SER A . n 
A 1 103 GLU 103 106 106 GLU GLU A . n 
A 1 104 HIS 104 107 107 HIS HIS A . n 
A 1 105 THR 105 108 108 THR THR A . n 
A 1 106 VAL 106 109 109 VAL VAL A . n 
A 1 107 ASP 107 110 110 ASP ASP A . n 
A 1 108 LYS 108 111 111 LYS LYS A . n 
A 1 109 LYS 109 112 112 LYS LYS A . n 
A 1 110 LYS 110 113 113 LYS LYS A . n 
A 1 111 TYR 111 114 114 TYR TYR A . n 
A 1 112 ALA 112 115 115 ALA ALA A . n 
A 1 113 ALA 113 116 116 ALA ALA A . n 
A 1 114 GLU 114 117 117 GLU GLU A . n 
A 1 115 LEU 115 118 118 LEU LEU A . n 
A 1 116 HIS 116 119 119 HIS HIS A . n 
A 1 117 LEU 117 120 120 LEU LEU A . n 
A 1 118 VAL 118 121 121 VAL VAL A . n 
A 1 119 HIS 119 122 122 HIS HIS A . n 
A 1 120 TRP 120 123 123 TRP TRP A . n 
A 1 121 ASN 121 124 124 ASN ASN A . n 
A 1 122 THR 122 125 125 THR THR A . n 
A 1 123 LYS 123 127 127 LYS LYS A . n 
A 1 124 TYR 124 128 128 TYR TYR A . n 
A 1 125 GLY 125 129 129 GLY GLY A . n 
A 1 126 ASP 126 130 130 ASP ASP A . n 
A 1 127 PHE 127 131 131 PHE PHE A . n 
A 1 128 GLY 128 132 132 GLY GLY A . n 
A 1 129 LYS 129 133 133 LYS LYS A . n 
A 1 130 ALA 130 134 134 ALA ALA A . n 
A 1 131 VAL 131 135 135 VAL VAL A . n 
A 1 132 GLN 132 136 136 GLN GLN A . n 
A 1 133 GLN 133 137 137 GLN GLN A . n 
A 1 134 PRO 134 138 138 PRO PRO A . n 
A 1 135 ASP 135 139 139 ASP ASP A . n 
A 1 136 GLY 136 140 140 GLY GLY A . n 
A 1 137 LEU 137 141 141 LEU LEU A . n 
A 1 138 ALA 138 142 142 ALA ALA A . n 
A 1 139 VAL 139 143 143 VAL VAL A . n 
A 1 140 LEU 140 144 144 LEU LEU A . n 
A 1 141 GLY 141 145 145 GLY GLY A . n 
A 1 142 ILE 142 146 146 ILE ILE A . n 
A 1 143 PHE 143 147 147 PHE PHE A . n 
A 1 144 LEU 144 148 148 LEU LEU A . n 
A 1 145 LYS 145 149 149 LYS LYS A . n 
A 1 146 VAL 146 150 150 VAL VAL A . n 
A 1 147 GLY 147 151 151 GLY GLY A . n 
A 1 148 SER 148 152 152 SER SER A . n 
A 1 149 ALA 149 153 153 ALA ALA A . n 
A 1 150 LYS 150 154 154 LYS LYS A . n 
A 1 151 PRO 151 155 155 PRO PRO A . n 
A 1 152 GLY 152 156 156 GLY GLY A . n 
A 1 153 LEU 153 157 157 LEU LEU A . n 
A 1 154 GLN 154 158 158 GLN GLN A . n 
A 1 155 LYS 155 159 159 LYS LYS A . n 
A 1 156 VAL 156 160 160 VAL VAL A . n 
A 1 157 VAL 157 161 161 VAL VAL A . n 
A 1 158 ASP 158 162 162 ASP ASP A . n 
A 1 159 VAL 159 163 163 VAL VAL A . n 
A 1 160 LEU 160 164 164 LEU LEU A . n 
A 1 161 ASP 161 165 165 ASP ASP A . n 
A 1 162 SER 162 166 166 SER SER A . n 
A 1 163 ILE 163 167 167 ILE ILE A . n 
A 1 164 LYS 164 168 168 LYS LYS A . n 
A 1 165 THR 165 169 169 THR THR A . n 
A 1 166 LYS 166 170 170 LYS LYS A . n 
A 1 167 GLY 167 171 171 GLY GLY A . n 
A 1 168 LYS 168 172 172 LYS LYS A . n 
A 1 169 SER 169 173 173 SER SER A . n 
A 1 170 ALA 170 174 174 ALA ALA A . n 
A 1 171 ASP 171 175 175 ASP ASP A . n 
A 1 172 PHE 172 176 176 PHE PHE A . n 
A 1 173 THR 173 177 177 THR THR A . n 
A 1 174 ASN 174 178 178 ASN ASN A . n 
A 1 175 PHE 175 179 179 PHE PHE A . n 
A 1 176 ASP 176 180 180 ASP ASP A . n 
A 1 177 PRO 177 181 181 PRO PRO A . n 
A 1 178 ARG 178 182 182 ARG ARG A . n 
A 1 179 GLY 179 183 183 GLY GLY A . n 
A 1 180 LEU 180 184 184 LEU LEU A . n 
A 1 181 LEU 181 185 185 LEU LEU A . n 
A 1 182 PRO 182 186 186 PRO PRO A . n 
A 1 183 GLU 183 187 187 GLU GLU A . n 
A 1 184 SER 184 188 188 SER SER A . n 
A 1 185 LEU 185 189 189 LEU LEU A . n 
A 1 186 ASP 186 190 190 ASP ASP A . n 
A 1 187 TYR 187 191 191 TYR TYR A . n 
A 1 188 TRP 188 192 192 TRP TRP A . n 
A 1 189 THR 189 193 193 THR THR A . n 
A 1 190 TYR 190 194 194 TYR TYR A . n 
A 1 191 PRO 191 195 195 PRO PRO A . n 
A 1 192 GLY 192 196 196 GLY GLY A . n 
A 1 193 SER 193 197 197 SER SER A . n 
A 1 194 LEU 194 198 198 LEU LEU A . n 
A 1 195 THR 195 199 199 THR THR A . n 
A 1 196 VAL 196 200 200 VAL VAL A . n 
A 1 197 PRO 197 201 201 PRO PRO A . n 
A 1 198 PRO 198 202 202 PRO PRO A . n 
A 1 199 LEU 199 203 203 LEU LEU A . n 
A 1 200 LEU 200 204 204 LEU LEU A . n 
A 1 201 GLU 201 205 205 GLU GLU A . n 
A 1 202 CYS 202 206 206 CYS CYS A . n 
A 1 203 VAL 203 207 207 VAL VAL A . n 
A 1 204 THR 204 208 208 THR THR A . n 
A 1 205 TRP 205 209 209 TRP TRP A . n 
A 1 206 ILE 206 210 210 ILE ILE A . n 
A 1 207 VAL 207 211 211 VAL VAL A . n 
A 1 208 LEU 208 212 212 LEU LEU A . n 
A 1 209 LYS 209 213 213 LYS LYS A . n 
A 1 210 GLU 210 214 214 GLU GLU A . n 
A 1 211 PRO 211 215 215 PRO PRO A . n 
A 1 212 ILE 212 216 216 ILE ILE A . n 
A 1 213 SER 213 217 217 SER SER A . n 
A 1 214 VAL 214 218 218 VAL VAL A . n 
A 1 215 SER 215 219 219 SER SER A . n 
A 1 216 SER 216 220 220 SER SER A . n 
A 1 217 GLU 217 221 221 GLU GLU A . n 
A 1 218 GLN 218 222 222 GLN GLN A . n 
A 1 219 VAL 219 223 223 VAL VAL A . n 
A 1 220 LEU 220 224 224 LEU LEU A . n 
A 1 221 LYS 221 225 225 LYS LYS A . n 
A 1 222 PHE 222 226 226 PHE PHE A . n 
A 1 223 ARG 223 227 227 ARG ARG A . n 
A 1 224 LYS 224 228 228 LYS LYS A . n 
A 1 225 LEU 225 229 229 LEU LEU A . n 
A 1 226 ASN 226 230 230 ASN ASN A . n 
A 1 227 PHE 227 231 231 PHE PHE A . n 
A 1 228 ASN 228 232 232 ASN ASN A . n 
A 1 229 GLY 229 233 233 GLY GLY A . n 
A 1 230 GLU 230 234 234 GLU GLU A . n 
A 1 231 GLY 231 235 235 GLY GLY A . n 
A 1 232 GLU 232 236 236 GLU GLU A . n 
A 1 233 PRO 233 237 237 PRO PRO A . n 
A 1 234 GLU 234 238 238 GLU GLU A . n 
A 1 235 GLU 235 239 239 GLU GLU A . n 
A 1 236 LEU 236 240 240 LEU LEU A . n 
A 1 237 MET 237 241 241 MET MET A . n 
A 1 238 VAL 238 242 242 VAL VAL A . n 
A 1 239 ASP 239 243 243 ASP ASP A . n 
A 1 240 ASN 240 244 244 ASN ASN A . n 
A 1 241 TRP 241 245 245 TRP TRP A . n 
A 1 242 ARG 242 246 246 ARG ARG A . n 
A 1 243 PRO 243 247 247 PRO PRO A . n 
A 1 244 ALA 244 248 248 ALA ALA A . n 
A 1 245 GLN 245 249 249 GLN GLN A . n 
A 1 246 PRO 246 250 250 PRO PRO A . n 
A 1 247 LEU 247 251 251 LEU LEU A . n 
A 1 248 LYS 248 252 252 LYS LYS A . n 
A 1 249 ASN 249 253 253 ASN ASN A . n 
A 1 250 ARG 250 254 254 ARG ARG A . n 
A 1 251 GLN 251 255 255 GLN GLN A . n 
A 1 252 ILE 252 256 256 ILE ILE A . n 
A 1 253 LYS 253 257 257 LYS LYS A . n 
A 1 254 ALA 254 258 258 ALA ALA A . n 
A 1 255 SER 255 259 259 SER SER A . n 
A 1 256 PHE 256 260 260 PHE PHE A . n 
A 1 257 LYS 257 261 261 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 NA  1   302 1   NA  NA  A . 
D 4 5DU 1   303 1   5DU V12 A . 
E 5 DMS 1   304 2   DMS DMS A . 
F 6 BEZ 1   305 1   BEZ BEZ A . 
G 7 HOH 1   401 107 HOH HOH A . 
G 7 HOH 2   402 39  HOH HOH A . 
G 7 HOH 3   403 191 HOH HOH A . 
G 7 HOH 4   404 48  HOH HOH A . 
G 7 HOH 5   405 136 HOH HOH A . 
G 7 HOH 6   406 19  HOH HOH A . 
G 7 HOH 7   407 98  HOH HOH A . 
G 7 HOH 8   408 35  HOH HOH A . 
G 7 HOH 9   409 216 HOH HOH A . 
G 7 HOH 10  410 124 HOH HOH A . 
G 7 HOH 11  411 80  HOH HOH A . 
G 7 HOH 12  412 135 HOH HOH A . 
G 7 HOH 13  413 150 HOH HOH A . 
G 7 HOH 14  414 88  HOH HOH A . 
G 7 HOH 15  415 73  HOH HOH A . 
G 7 HOH 16  416 177 HOH HOH A . 
G 7 HOH 17  417 51  HOH HOH A . 
G 7 HOH 18  418 186 HOH HOH A . 
G 7 HOH 19  419 96  HOH HOH A . 
G 7 HOH 20  420 86  HOH HOH A . 
G 7 HOH 21  421 56  HOH HOH A . 
G 7 HOH 22  422 132 HOH HOH A . 
G 7 HOH 23  423 217 HOH HOH A . 
G 7 HOH 24  424 29  HOH HOH A . 
G 7 HOH 25  425 34  HOH HOH A . 
G 7 HOH 26  426 193 HOH HOH A . 
G 7 HOH 27  427 83  HOH HOH A . 
G 7 HOH 28  428 23  HOH HOH A . 
G 7 HOH 29  429 84  HOH HOH A . 
G 7 HOH 30  430 161 HOH HOH A . 
G 7 HOH 31  431 167 HOH HOH A . 
G 7 HOH 32  432 62  HOH HOH A . 
G 7 HOH 33  433 125 HOH HOH A . 
G 7 HOH 34  434 99  HOH HOH A . 
G 7 HOH 35  435 42  HOH HOH A . 
G 7 HOH 36  436 162 HOH HOH A . 
G 7 HOH 37  437 40  HOH HOH A . 
G 7 HOH 38  438 15  HOH HOH A . 
G 7 HOH 39  439 69  HOH HOH A . 
G 7 HOH 40  440 114 HOH HOH A . 
G 7 HOH 41  441 10  HOH HOH A . 
G 7 HOH 42  442 215 HOH HOH A . 
G 7 HOH 43  443 60  HOH HOH A . 
G 7 HOH 44  444 95  HOH HOH A . 
G 7 HOH 45  445 43  HOH HOH A . 
G 7 HOH 46  446 12  HOH HOH A . 
G 7 HOH 47  447 14  HOH HOH A . 
G 7 HOH 48  448 2   HOH HOH A . 
G 7 HOH 49  449 90  HOH HOH A . 
G 7 HOH 50  450 92  HOH HOH A . 
G 7 HOH 51  451 3   HOH HOH A . 
G 7 HOH 52  452 22  HOH HOH A . 
G 7 HOH 53  453 6   HOH HOH A . 
G 7 HOH 54  454 77  HOH HOH A . 
G 7 HOH 55  455 85  HOH HOH A . 
G 7 HOH 56  456 127 HOH HOH A . 
G 7 HOH 57  457 115 HOH HOH A . 
G 7 HOH 58  458 147 HOH HOH A . 
G 7 HOH 59  459 118 HOH HOH A . 
G 7 HOH 60  460 27  HOH HOH A . 
G 7 HOH 61  461 122 HOH HOH A . 
G 7 HOH 62  462 8   HOH HOH A . 
G 7 HOH 63  463 11  HOH HOH A . 
G 7 HOH 64  464 67  HOH HOH A . 
G 7 HOH 65  465 143 HOH HOH A . 
G 7 HOH 66  466 137 HOH HOH A . 
G 7 HOH 67  467 45  HOH HOH A . 
G 7 HOH 68  468 131 HOH HOH A . 
G 7 HOH 69  469 1   HOH HOH A . 
G 7 HOH 70  470 146 HOH HOH A . 
G 7 HOH 71  471 175 HOH HOH A . 
G 7 HOH 72  472 208 HOH HOH A . 
G 7 HOH 73  473 47  HOH HOH A . 
G 7 HOH 74  474 25  HOH HOH A . 
G 7 HOH 75  475 195 HOH HOH A . 
G 7 HOH 76  476 202 HOH HOH A . 
G 7 HOH 77  477 18  HOH HOH A . 
G 7 HOH 78  478 93  HOH HOH A . 
G 7 HOH 79  479 9   HOH HOH A . 
G 7 HOH 80  480 212 HOH HOH A . 
G 7 HOH 81  481 117 HOH HOH A . 
G 7 HOH 82  482 59  HOH HOH A . 
G 7 HOH 83  483 109 HOH HOH A . 
G 7 HOH 84  484 104 HOH HOH A . 
G 7 HOH 85  485 120 HOH HOH A . 
G 7 HOH 86  486 65  HOH HOH A . 
G 7 HOH 87  487 110 HOH HOH A . 
G 7 HOH 88  488 192 HOH HOH A . 
G 7 HOH 89  489 179 HOH HOH A . 
G 7 HOH 90  490 54  HOH HOH A . 
G 7 HOH 91  491 159 HOH HOH A . 
G 7 HOH 92  492 70  HOH HOH A . 
G 7 HOH 93  493 4   HOH HOH A . 
G 7 HOH 94  494 123 HOH HOH A . 
G 7 HOH 95  495 28  HOH HOH A . 
G 7 HOH 96  496 176 HOH HOH A . 
G 7 HOH 97  497 140 HOH HOH A . 
G 7 HOH 98  498 30  HOH HOH A . 
G 7 HOH 99  499 128 HOH HOH A . 
G 7 HOH 100 500 7   HOH HOH A . 
G 7 HOH 101 501 72  HOH HOH A . 
G 7 HOH 102 502 87  HOH HOH A . 
G 7 HOH 103 503 209 HOH HOH A . 
G 7 HOH 104 504 13  HOH HOH A . 
G 7 HOH 105 505 38  HOH HOH A . 
G 7 HOH 106 506 46  HOH HOH A . 
G 7 HOH 107 507 53  HOH HOH A . 
G 7 HOH 108 508 94  HOH HOH A . 
G 7 HOH 109 509 197 HOH HOH A . 
G 7 HOH 110 510 91  HOH HOH A . 
G 7 HOH 111 511 116 HOH HOH A . 
G 7 HOH 112 512 204 HOH HOH A . 
G 7 HOH 113 513 203 HOH HOH A . 
G 7 HOH 114 514 133 HOH HOH A . 
G 7 HOH 115 515 41  HOH HOH A . 
G 7 HOH 116 516 74  HOH HOH A . 
G 7 HOH 117 517 44  HOH HOH A . 
G 7 HOH 118 518 108 HOH HOH A . 
G 7 HOH 119 519 173 HOH HOH A . 
G 7 HOH 120 520 89  HOH HOH A . 
G 7 HOH 121 521 111 HOH HOH A . 
G 7 HOH 122 522 5   HOH HOH A . 
G 7 HOH 123 523 160 HOH HOH A . 
G 7 HOH 124 524 71  HOH HOH A . 
G 7 HOH 125 525 164 HOH HOH A . 
G 7 HOH 126 526 153 HOH HOH A . 
G 7 HOH 127 527 198 HOH HOH A . 
G 7 HOH 128 528 100 HOH HOH A . 
G 7 HOH 129 529 183 HOH HOH A . 
G 7 HOH 130 530 190 HOH HOH A . 
G 7 HOH 131 531 50  HOH HOH A . 
G 7 HOH 132 532 121 HOH HOH A . 
G 7 HOH 133 533 33  HOH HOH A . 
G 7 HOH 134 534 130 HOH HOH A . 
G 7 HOH 135 535 63  HOH HOH A . 
G 7 HOH 136 536 199 HOH HOH A . 
G 7 HOH 137 537 76  HOH HOH A . 
G 7 HOH 138 538 17  HOH HOH A . 
G 7 HOH 139 539 55  HOH HOH A . 
G 7 HOH 140 540 81  HOH HOH A . 
G 7 HOH 141 541 32  HOH HOH A . 
G 7 HOH 142 542 52  HOH HOH A . 
G 7 HOH 143 543 101 HOH HOH A . 
G 7 HOH 144 544 119 HOH HOH A . 
G 7 HOH 145 545 58  HOH HOH A . 
G 7 HOH 146 546 36  HOH HOH A . 
G 7 HOH 147 547 155 HOH HOH A . 
G 7 HOH 148 548 64  HOH HOH A . 
G 7 HOH 149 549 184 HOH HOH A . 
G 7 HOH 150 550 174 HOH HOH A . 
G 7 HOH 151 551 152 HOH HOH A . 
G 7 HOH 152 552 166 HOH HOH A . 
G 7 HOH 153 553 105 HOH HOH A . 
G 7 HOH 154 554 134 HOH HOH A . 
G 7 HOH 155 555 26  HOH HOH A . 
G 7 HOH 156 556 31  HOH HOH A . 
G 7 HOH 157 557 141 HOH HOH A . 
G 7 HOH 158 558 37  HOH HOH A . 
G 7 HOH 159 559 142 HOH HOH A . 
G 7 HOH 160 560 49  HOH HOH A . 
G 7 HOH 161 561 82  HOH HOH A . 
G 7 HOH 162 562 201 HOH HOH A . 
G 7 HOH 163 563 20  HOH HOH A . 
G 7 HOH 164 564 158 HOH HOH A . 
G 7 HOH 165 565 129 HOH HOH A . 
G 7 HOH 166 566 102 HOH HOH A . 
G 7 HOH 167 567 21  HOH HOH A . 
G 7 HOH 168 568 168 HOH HOH A . 
G 7 HOH 169 569 61  HOH HOH A . 
G 7 HOH 170 570 148 HOH HOH A . 
G 7 HOH 171 571 16  HOH HOH A . 
G 7 HOH 172 572 211 HOH HOH A . 
G 7 HOH 173 573 182 HOH HOH A . 
G 7 HOH 174 574 79  HOH HOH A . 
G 7 HOH 175 575 97  HOH HOH A . 
G 7 HOH 176 576 181 HOH HOH A . 
G 7 HOH 177 577 106 HOH HOH A . 
G 7 HOH 178 578 57  HOH HOH A . 
G 7 HOH 179 579 24  HOH HOH A . 
G 7 HOH 180 580 194 HOH HOH A . 
G 7 HOH 181 581 126 HOH HOH A . 
G 7 HOH 182 582 170 HOH HOH A . 
G 7 HOH 183 583 66  HOH HOH A . 
G 7 HOH 184 584 112 HOH HOH A . 
G 7 HOH 185 585 213 HOH HOH A . 
G 7 HOH 186 586 138 HOH HOH A . 
G 7 HOH 187 587 145 HOH HOH A . 
G 7 HOH 188 588 185 HOH HOH A . 
G 7 HOH 189 589 165 HOH HOH A . 
G 7 HOH 190 590 210 HOH HOH A . 
G 7 HOH 191 591 196 HOH HOH A . 
G 7 HOH 192 592 214 HOH HOH A . 
G 7 HOH 193 593 157 HOH HOH A . 
G 7 HOH 194 594 206 HOH HOH A . 
G 7 HOH 195 595 78  HOH HOH A . 
G 7 HOH 196 596 178 HOH HOH A . 
G 7 HOH 197 597 180 HOH HOH A . 
G 7 HOH 198 598 188 HOH HOH A . 
G 7 HOH 199 599 156 HOH HOH A . 
G 7 HOH 200 600 187 HOH HOH A . 
G 7 HOH 201 601 68  HOH HOH A . 
G 7 HOH 202 602 144 HOH HOH A . 
G 7 HOH 203 603 171 HOH HOH A . 
G 7 HOH 204 604 200 HOH HOH A . 
G 7 HOH 205 605 151 HOH HOH A . 
G 7 HOH 206 606 189 HOH HOH A . 
G 7 HOH 207 607 113 HOH HOH A . 
G 7 HOH 208 608 163 HOH HOH A . 
G 7 HOH 209 609 75  HOH HOH A . 
G 7 HOH 210 610 149 HOH HOH A . 
G 7 HOH 211 611 205 HOH HOH A . 
G 7 HOH 212 612 154 HOH HOH A . 
G 7 HOH 213 613 172 HOH HOH A . 
G 7 HOH 214 614 139 HOH HOH A . 
G 7 HOH 215 615 207 HOH HOH A . 
G 7 HOH 216 616 103 HOH HOH A . 
G 7 HOH 217 617 169 HOH HOH A . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 9   ? CD  ? A LYS 6   CD  
2  1 Y 1 A LYS 9   ? CE  ? A LYS 6   CE  
3  1 Y 1 A LYS 9   ? NZ  ? A LYS 6   NZ  
4  1 Y 1 A LYS 45  ? CE  ? A LYS 42  CE  
5  1 Y 1 A LYS 45  ? NZ  ? A LYS 42  NZ  
6  1 Y 0 A LYS 159 ? CD  ? A LYS 155 CD  
7  1 Y 0 A LYS 159 ? CE  ? A LYS 155 CE  
8  1 Y 0 A LYS 159 ? NZ  ? A LYS 155 NZ  
9  1 Y 1 A LYS 228 ? CE  ? A LYS 224 CE  
10 1 Y 1 A LYS 228 ? NZ  ? A LYS 224 NZ  
11 1 Y 1 A GLU 239 ? CG  ? A GLU 235 CG  
12 1 Y 1 A GLU 239 ? CD  ? A GLU 235 CD  
13 1 Y 1 A GLU 239 ? OE1 ? A GLU 235 OE1 
14 1 Y 1 A GLU 239 ? OE2 ? A GLU 235 OE2 
15 1 Y 0 A LYS 257 ? CD  ? A LYS 253 CD  
16 1 Y 0 A LYS 257 ? CE  ? A LYS 253 CE  
17 1 Y 0 A LYS 257 ? NZ  ? A LYS 253 NZ  
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? SCALA       ? ? ? 3.3.22   1 
? refinement        ? ? ? ? ? ? ? ? ? ? ? REFMAC      ? ? ? 5.8.0232 2 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.25     3 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? XDS         ? ? ? .        4 
? phasing           ? ? ? ? ? ? ? ? ? ? ? MOLREP      ? ? ? .        5 
? 'model building'  ? ? ? ? ? ? ? ? ? ? ? Coot        ? ? ? .        6 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   104.140 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     6RMX 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     42.260 
_cell.length_a_esd                 ? 
_cell.length_b                     41.050 
_cell.length_b_esd                 ? 
_cell.length_c                     71.770 
_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                         6RMX 
_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                   6RMX 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                      ? 
_exptl_crystal.density_diffrn              ? 
_exptl_crystal.density_Matthews            2.09 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         41.05 
_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 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp            291 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;Crystallization buffer was 0.1M sodium BICINE, pH 9, 0.2 M ammonium sulfate and 2M sodium malonate pH 7 made from 1M sodium BICINE and 3.4M sodium malonate
;
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS3 R 200K-A' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2019-03-14 
_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   1.54187 
_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                      'ROTATING ANODE' 
_diffrn_source.target                      ? 
_diffrn_source.type                        'RIGAKU MICROMAX-007 HF' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.54187 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ? 
_diffrn_source.pdbx_synchrotron_site       ? 
# 
_reflns.B_iso_Wilson_estimate            ? 
_reflns.entry_id                         6RMX 
_reflns.data_reduction_details           ? 
_reflns.data_reduction_method            ? 
_reflns.d_resolution_high                1.600 
_reflns.d_resolution_low                 41.050 
_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                       31450 
_reflns.number_obs                       31450 
_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             99.100 
_reflns.R_free_details                   ? 
_reflns.Rmerge_F_all                     ? 
_reflns.Rmerge_F_obs                     ? 
_reflns.Friedel_coverage                 ? 
_reflns.number_gt                        ? 
_reflns.threshold_expression             ? 
_reflns.pdbx_redundancy                  4.600 
_reflns.pdbx_Rmerge_I_obs                ? 
_reflns.pdbx_Rmerge_I_all                ? 
_reflns.pdbx_Rsym_value                  0.019 
_reflns.pdbx_netI_over_av_sigmaI         23.200 
_reflns.pdbx_netI_over_sigmaI            38.100 
_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                  0.028 
_reflns.pdbx_Rpim_I_all                  0.011 
_reflns.pdbx_d_opt                       ? 
_reflns.pdbx_number_measured_all         145890 
_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 
1.600 1.690  ? 5.000  11919 ? ? ? 4469 96.600  ? ? ? ? 0.096 ? ? ? ? ? ? ? ? 2.700 0.096 ? ? 5.300   0.262 0.143 ? 1  1 ? ? 
1.690 1.790  ? 8.400  12319 ? ? ? 4250 98.200  ? ? ? ? 0.060 ? ? ? ? ? ? ? ? 2.900 0.060 ? ? 9.000   0.159 0.085 ? 2  1 ? ? 
1.790 1.910  ? 13.400 12904 ? ? ? 4053 99.200  ? ? ? ? 0.040 ? ? ? ? ? ? ? ? 3.200 0.040 ? ? 14.800  0.098 0.051 ? 3  1 ? ? 
1.910 2.070  ? 21.100 13286 ? ? ? 3806 99.700  ? ? ? ? 0.027 ? ? ? ? ? ? ? ? 3.500 0.027 ? ? 24.400  0.058 0.029 ? 4  1 ? ? 
2.070 2.260  ? 25.600 15557 ? ? ? 3536 100.000 ? ? ? ? 0.025 ? ? ? ? ? ? ? ? 4.400 0.025 ? ? 37.100  0.042 0.019 ? 5  1 ? ? 
2.260 2.530  ? 26.700 19009 ? ? ? 3178 100.000 ? ? ? ? 0.025 ? ? ? ? ? ? ? ? 6.000 0.025 ? ? 50.900  0.035 0.014 ? 6  1 ? ? 
2.530 2.920  ? 27.600 21875 ? ? ? 2830 100.000 ? ? ? ? 0.023 ? ? ? ? ? ? ? ? 7.700 0.023 ? ? 69.000  0.029 0.010 ? 7  1 ? ? 
2.920 3.580  ? 32.800 18433 ? ? ? 2407 100.000 ? ? ? ? 0.018 ? ? ? ? ? ? ? ? 7.700 0.018 ? ? 88.200  0.023 0.008 ? 8  1 ? ? 
3.580 5.060  ? 35.300 13770 ? ? ? 1868 99.900  ? ? ? ? 0.015 ? ? ? ? ? ? ? ? 7.400 0.015 ? ? 101.800 0.019 0.007 ? 9  1 ? ? 
5.060 41.050 ? 34.000 6818  ? ? ? 1053 98.600  ? ? ? ? 0.017 ? ? ? ? ? ? ? ? 6.500 0.017 ? ? 88.700  0.022 0.008 ? 10 1 ? ? 
# 
_refine.aniso_B[1][1]                            0.2200 
_refine.aniso_B[1][2]                            -0.0000 
_refine.aniso_B[1][3]                            -0.3800 
_refine.aniso_B[2][2]                            -0.1700 
_refine.aniso_B[2][3]                            0.0000 
_refine.aniso_B[3][3]                            0.1200 
_refine.B_iso_max                                78.050 
_refine.B_iso_mean                               18.9070 
_refine.B_iso_min                                6.680 
_refine.correlation_coeff_Fo_to_Fc               0.9670 
_refine.correlation_coeff_Fo_to_Fc_free          0.9470 
_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                                 6RMX 
_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                            1.6000 
_refine.ls_d_res_low                             29.0200 
_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                     28366 
_refine.ls_number_reflns_R_free                  3018 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.7700 
_refine.ls_percent_reflns_R_free                 9.6000 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1742 
_refine.ls_R_factor_R_free                       0.2127 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1702 
_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                      4HT0 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.0990 
_refine.pdbx_overall_ESU_R_Free                  0.1010 
_refine.pdbx_solvent_vdw_probe_radii             1.4000 
_refine.pdbx_solvent_ion_probe_radii             0.8000 
_refine.pdbx_solvent_shrinkage_radii             0.8000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         final 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.6000 
_refine_hist.d_res_low                        29.0200 
_refine_hist.number_atoms_solvent             217 
_refine_hist.number_atoms_total               2297 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       257 
_refine_hist.pdbx_B_iso_mean_ligand           30.94 
_refine_hist.pdbx_B_iso_mean_solvent          30.86 
_refine_hist.pdbx_number_atoms_protein        2038 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         42 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.011  0.012  2177 ? r_bond_refined_d       ? ? 
'X-RAY DIFFRACTION' ? 1.907  1.651  2968 ? r_angle_refined_deg    ? ? 
'X-RAY DIFFRACTION' ? 6.956  5.000  265  ? r_dihedral_angle_1_deg ? ? 
'X-RAY DIFFRACTION' ? 36.166 23.714 105  ? r_dihedral_angle_2_deg ? ? 
'X-RAY DIFFRACTION' ? 13.645 15.000 345  ? r_dihedral_angle_3_deg ? ? 
'X-RAY DIFFRACTION' ? 20.916 15.000 7    ? r_dihedral_angle_4_deg ? ? 
'X-RAY DIFFRACTION' ? 0.139  0.200  263  ? r_chiral_restr         ? ? 
'X-RAY DIFFRACTION' ? 0.012  0.020  1709 ? r_gen_planes_refined   ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.6000 
_refine_ls_shell.d_res_low                        1.6420 
_refine_ls_shell.number_reflns_all                2262 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             213 
_refine_ls_shell.number_reflns_R_work             2049 
_refine_ls_shell.percent_reflns_obs               95.7700 
_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                  0.3770 
_refine_ls_shell.R_factor_R_free_error            0.0000 
_refine_ls_shell.R_factor_R_work                  0.3180 
_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                     6RMX 
_struct.title                        
;Human Carbonic anhydrase II mutant T199V bound by 2-[(1S)-2,3-Dihydro-1H-inden-1-ylamino]-3,5,6-trifluoro-4-[(2-hydroxyethyl)thio]benzenesulfonamide
;
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        6RMX 
_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 ? 
G N N 7 ? 
# 
_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   
;HWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLKGGP
LDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVVDVL
DSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELMVDN
WRPAQPLKNRQIKASFK
;
_struct_ref.pdbx_align_begin           4 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              6RMX 
_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                 257 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P00918 
_struct_ref_seq.db_align_beg                  4 
_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       4 
_struct_ref_seq.pdbx_auth_seq_align_end       261 
# 
_struct_ref_seq_dif.align_id                     1 
_struct_ref_seq_dif.pdbx_pdb_id_code             6RMX 
_struct_ref_seq_dif.mon_id                       VAL 
_struct_ref_seq_dif.pdbx_pdb_strand_id           A 
_struct_ref_seq_dif.seq_num                      196 
_struct_ref_seq_dif.pdbx_pdb_ins_code            ? 
_struct_ref_seq_dif.pdbx_seq_db_name             UNP 
_struct_ref_seq_dif.pdbx_seq_db_accession_code   P00918 
_struct_ref_seq_dif.db_mon_id                    THR 
_struct_ref_seq_dif.pdbx_seq_db_seq_num          199 
_struct_ref_seq_dif.details                      'engineered mutation' 
_struct_ref_seq_dif.pdbx_auth_seq_num            200 
_struct_ref_seq_dif.pdbx_ordinal                 1 
# 
_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)' 650   ? 
1 MORE         0     ? 
1 'SSA (A^2)'  11070 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G 
# 
_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 9   ? GLU A 11  ? GLY A 12  GLU A 14  5 ? 3 
HELX_P HELX_P2  AA2 HIS A 12  ? PHE A 17  ? HIS A 15  PHE A 20  1 ? 6 
HELX_P HELX_P3  AA3 PRO A 18  ? GLY A 22  ? PRO A 21  GLY A 25  5 ? 5 
HELX_P HELX_P4  AA4 LYS A 123 ? GLY A 125 ? LYS A 127 GLY A 129 5 ? 3 
HELX_P HELX_P5  AA5 ASP A 126 ? VAL A 131 ? ASP A 130 VAL A 135 1 ? 6 
HELX_P HELX_P6  AA6 LYS A 150 ? GLY A 152 ? LYS A 154 GLY A 156 5 ? 3 
HELX_P HELX_P7  AA7 LEU A 153 ? LEU A 160 ? LEU A 157 LEU A 164 1 ? 8 
HELX_P HELX_P8  AA8 ASP A 161 ? LYS A 164 ? ASP A 165 LYS A 168 5 ? 4 
HELX_P HELX_P9  AA9 ASP A 176 ? LEU A 181 ? ASP A 180 LEU A 185 5 ? 6 
HELX_P HELX_P10 AB1 SER A 215 ? ARG A 223 ? 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 SER 70  OG  ? ? ? 1_555 C NA  . NA ? ? A SER 73  A NA  302 1_565 ? ? ? ? ? ? ? 2.327 ? ? 
metalc2  metalc ? ? A HIS 91  NE2 ? ? ? 1_555 B ZN  . ZN ? ? A HIS 94  A ZN  301 1_555 ? ? ? ? ? ? ? 2.007 ? ? 
metalc3  metalc ? ? A HIS 93  NE2 ? ? ? 1_555 B ZN  . ZN ? ? A HIS 96  A ZN  301 1_555 ? ? ? ? ? ? ? 2.047 ? ? 
metalc4  metalc ? ? A HIS 116 ND1 ? ? ? 1_555 B ZN  . ZN ? ? A HIS 119 A ZN  301 1_555 ? ? ? ? ? ? ? 1.972 ? ? 
metalc5  metalc ? ? A SER 216 OG  ? ? ? 1_555 C NA  . NA ? ? A SER 220 A NA  302 1_555 ? ? ? ? ? ? ? 2.708 ? ? 
metalc6  metalc ? ? B ZN  .   ZN  ? ? ? 1_555 D 5DU . N4 ? ? A ZN  301 A 5DU 303 1_555 ? ? ? ? ? ? ? 1.902 ? ? 
metalc7  metalc ? ? C NA  .   NA  ? ? ? 1_555 G HOH . O  ? ? A NA  302 A HOH 424 1_545 ? ? ? ? ? ? ? 2.345 ? ? 
metalc8  metalc ? ? C NA  .   NA  ? ? ? 1_555 G HOH . O  ? ? A NA  302 A HOH 437 1_555 ? ? ? ? ? ? ? 2.219 ? ? 
metalc9  metalc ? ? C NA  .   NA  ? ? ? 1_555 G HOH . O  ? ? A NA  302 A HOH 479 1_555 ? ? ? ? ? ? ? 2.394 ? ? 
metalc10 metalc ? ? C NA  .   NA  ? ? ? 1_555 G HOH . O  ? ? A NA  302 A HOH 586 1_555 ? ? ? ? ? ? ? 2.349 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  OG  ? A SER 70  ? A SER 73  ? 1_555 NA ? C NA . ? A NA 302 ? 1_565 OG  ? A SER 216 ? A SER 220 ? 1_555 46.4  ? 
2  OG  ? A SER 70  ? A SER 73  ? 1_555 NA ? C NA . ? A NA 302 ? 1_565 O   ? G HOH .   ? A HOH 424 ? 1_545 49.4  ? 
3  OG  ? A SER 216 ? A SER 220 ? 1_555 NA ? C NA . ? A NA 302 ? 1_565 O   ? G HOH .   ? A HOH 424 ? 1_545 5.7   ? 
4  OG  ? A SER 70  ? A SER 73  ? 1_555 NA ? C NA . ? A NA 302 ? 1_565 O   ? G HOH .   ? A HOH 437 ? 1_555 50.5  ? 
5  OG  ? A SER 216 ? A SER 220 ? 1_555 NA ? C NA . ? A NA 302 ? 1_565 O   ? G HOH .   ? A HOH 437 ? 1_555 5.4   ? 
6  O   ? G HOH .   ? A HOH 424 ? 1_545 NA ? C NA . ? A NA 302 ? 1_565 O   ? G HOH .   ? A HOH 437 ? 1_555 1.8   ? 
7  OG  ? A SER 70  ? A SER 73  ? 1_555 NA ? C NA . ? A NA 302 ? 1_565 O   ? G HOH .   ? A HOH 479 ? 1_555 45.8  ? 
8  OG  ? A SER 216 ? A SER 220 ? 1_555 NA ? C NA . ? A NA 302 ? 1_565 O   ? G HOH .   ? A HOH 479 ? 1_555 4.9   ? 
9  O   ? G HOH .   ? A HOH 424 ? 1_545 NA ? C NA . ? A NA 302 ? 1_565 O   ? G HOH .   ? A HOH 479 ? 1_555 3.6   ? 
10 O   ? G HOH .   ? A HOH 437 ? 1_555 NA ? C NA . ? A NA 302 ? 1_565 O   ? G HOH .   ? A HOH 479 ? 1_555 5.0   ? 
11 OG  ? A SER 70  ? A SER 73  ? 1_555 NA ? C NA . ? A NA 302 ? 1_565 O   ? G HOH .   ? A HOH 586 ? 1_555 49.6  ? 
12 OG  ? A SER 216 ? A SER 220 ? 1_555 NA ? C NA . ? A NA 302 ? 1_565 O   ? G HOH .   ? A HOH 586 ? 1_555 3.4   ? 
13 O   ? G HOH .   ? A HOH 424 ? 1_545 NA ? C NA . ? A NA 302 ? 1_565 O   ? G HOH .   ? A HOH 586 ? 1_555 4.0   ? 
14 O   ? G HOH .   ? A HOH 437 ? 1_555 NA ? C NA . ? A NA 302 ? 1_565 O   ? G HOH .   ? A HOH 586 ? 1_555 2.8   ? 
15 O   ? G HOH .   ? A HOH 479 ? 1_555 NA ? C NA . ? A NA 302 ? 1_565 O   ? G HOH .   ? A HOH 586 ? 1_555 5.5   ? 
16 NE2 ? A HIS 91  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 NE2 ? A HIS 93  ? A HIS 96  ? 1_555 103.0 ? 
17 NE2 ? A HIS 91  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 116 ? A HIS 119 ? 1_555 112.8 ? 
18 NE2 ? A HIS 93  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 116 ? A HIS 119 ? 1_555 99.0  ? 
19 NE2 ? A HIS 91  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N4  ? D 5DU .   ? A 5DU 303 ? 1_555 118.4 ? 
20 NE2 ? A HIS 93  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N4  ? D 5DU .   ? A 5DU 303 ? 1_555 113.6 ? 
21 ND1 ? A HIS 116 ? A HIS 119 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N4  ? D 5DU .   ? A 5DU 303 ? 1_555 108.4 ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 SER 26  A . ? SER 29  A PRO 27  A ? PRO 30  A 1 -7.27 
2 PRO 197 A . ? PRO 201 A PRO 198 A ? PRO 202 A 1 6.06  
# 
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 29  ? ILE A 30  ? ASP A 32  ILE A 33  
AA1 2  THR A 105 ? VAL A 106 ? THR A 108 VAL A 109 
AA2 1  LYS A 36  ? TYR A 37  ? LYS A 39  TYR A 40  
AA2 2  LYS A 253 ? ALA A 254 ? LYS A 257 ALA A 258 
AA2 3  TYR A 187 ? GLY A 192 ? TYR A 191 GLY A 196 
AA2 4  VAL A 203 ? LEU A 208 ? VAL A 207 LEU A 212 
AA2 5  LEU A 137 ? VAL A 146 ? LEU A 141 VAL A 150 
AA2 6  ALA A 113 ? ASN A 121 ? ALA A 116 ASN A 124 
AA2 7  TYR A 85  ? TRP A 94  ? TYR A 88  TRP A 97  
AA2 8  PHE A 63  ? PHE A 67  ? PHE A 66  PHE A 70  
AA2 9  SER A 53  ? ASN A 58  ? SER A 56  ASN A 61  
AA2 10 SER A 169 ? ASP A 171 ? SER A 173 ASP A 175 
AA3 1  LEU A 44  ? SER A 47  ? LEU A 47  SER A 50  
AA3 2  VAL A 75  ? GLY A 78  ? VAL A 78  GLY A 81  
AA3 3  TYR A 85  ? TRP A 94  ? TYR A 88  TRP A 97  
AA3 4  ALA A 113 ? ASN A 121 ? ALA A 116 ASN A 124 
AA3 5  LEU A 137 ? VAL A 146 ? LEU A 141 VAL A 150 
AA3 6  ILE A 212 ? VAL A 214 ? 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 30  ? N ILE A 33  O THR A 105 ? O THR A 108 
AA2 1 2  N LYS A 36  ? N LYS A 39  O ALA A 254 ? O ALA A 258 
AA2 2 3  O LYS A 253 ? O LYS A 257 N THR A 189 ? N THR A 193 
AA2 3 4  N GLY A 192 ? N GLY A 196 O VAL A 203 ? O VAL A 207 
AA2 4 5  O LEU A 208 ? O LEU A 212 N GLY A 141 ? N GLY A 145 
AA2 5 6  O ILE A 142 ? O ILE A 146 N LEU A 115 ? N LEU A 118 
AA2 6 7  O HIS A 116 ? O HIS A 119 N HIS A 91  ? N HIS A 94  
AA2 7 8  O ILE A 88  ? O ILE A 91  N PHE A 67  ? N PHE A 70  
AA2 8 9  O GLU A 66  ? O GLU A 69  N LEU A 54  ? N LEU A 57  
AA2 9 10 N ILE A 56  ? N ILE A 59  O ALA A 170 ? O ALA A 174 
AA3 1 2  N SER A 47  ? N SER A 50  O VAL A 75  ? O VAL A 78  
AA3 2 3  N LEU A 76  ? N LEU A 79  O TYR A 85  ? O TYR A 88  
AA3 3 4  N HIS A 91  ? N HIS A 94  O HIS A 116 ? O HIS A 119 
AA3 4 5  N LEU A 115 ? N LEU A 118 O ILE A 142 ? O ILE A 146 
AA3 5 6  N LYS A 145 ? N LYS A 149 O VAL A 214 ? O VAL A 218 
# 
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 NA  302 ? 6  'binding site for residue NA A 302'  
AC3 Software A 5DU 303 ? 11 'binding site for residue 5DU A 303' 
AC4 Software A DMS 304 ? 4  'binding site for residue DMS A 304' 
AC5 Software A BEZ 305 ? 4  'binding site for residue BEZ A 305' 
# 
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 91  ? HIS A 94  . ? 1_555 ? 
2  AC1 4  HIS A 93  ? HIS A 96  . ? 1_555 ? 
3  AC1 4  HIS A 116 ? HIS A 119 . ? 1_555 ? 
4  AC1 4  5DU D .   ? 5DU A 303 . ? 1_555 ? 
5  AC2 6  SER A 70  ? SER A 73  . ? 1_545 ? 
6  AC2 6  SER A 216 ? SER A 220 . ? 1_555 ? 
7  AC2 6  HOH G .   ? HOH A 424 . ? 1_545 ? 
8  AC2 6  HOH G .   ? HOH A 437 . ? 1_555 ? 
9  AC2 6  HOH G .   ? HOH A 479 . ? 1_555 ? 
10 AC2 6  HOH G .   ? HOH A 586 . ? 1_555 ? 
11 AC3 11 ASN A 59  ? ASN A 62  . ? 1_555 ? 
12 AC3 11 GLN A 89  ? GLN A 92  . ? 1_555 ? 
13 AC3 11 HIS A 91  ? HIS A 94  . ? 1_555 ? 
14 AC3 11 HIS A 93  ? HIS A 96  . ? 1_555 ? 
15 AC3 11 HIS A 116 ? HIS A 119 . ? 1_555 ? 
16 AC3 11 PHE A 127 ? PHE A 131 . ? 1_555 ? 
17 AC3 11 LEU A 194 ? LEU A 198 . ? 1_555 ? 
18 AC3 11 THR A 195 ? THR A 199 . ? 1_555 ? 
19 AC3 11 VAL A 196 ? VAL A 200 . ? 1_555 ? 
20 AC3 11 PRO A 198 ? PRO A 202 . ? 1_555 ? 
21 AC3 11 ZN  B .   ? ZN  A 301 . ? 1_555 ? 
22 AC4 4  TYR A 4   ? TYR A 7   . ? 1_555 ? 
23 AC4 4  ASP A 239 ? ASP A 243 . ? 1_555 ? 
24 AC4 4  TRP A 241 ? TRP A 245 . ? 1_555 ? 
25 AC4 4  PRO A 243 ? PRO A 247 . ? 1_555 ? 
26 AC5 4  ASP A 161 ? ASP A 165 . ? 1_555 ? 
27 AC5 4  LYS A 221 ? LYS A 225 . ? 1_555 ? 
28 AC5 4  LYS A 224 ? LYS A 228 . ? 1_555 ? 
29 AC5 4  HOH G .   ? HOH A 450 . ? 1_555 ? 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             CG 
_pdbx_validate_rmsd_angle.auth_asym_id_1             A 
_pdbx_validate_rmsd_angle.auth_comp_id_1             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_1              89 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CD 
_pdbx_validate_rmsd_angle.auth_asym_id_2             A 
_pdbx_validate_rmsd_angle.auth_comp_id_2             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_2              89 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             NE 
_pdbx_validate_rmsd_angle.auth_asym_id_3             A 
_pdbx_validate_rmsd_angle.auth_comp_id_3             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_3              89 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                98.73 
_pdbx_validate_rmsd_angle.angle_target_value         111.80 
_pdbx_validate_rmsd_angle.angle_deviation            -13.07 
_pdbx_validate_rmsd_angle.angle_standard_deviation   2.10 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ARG A 27  ? ? -144.12 58.48   
2 1 LYS A 111 ? ? 76.99   -2.06   
3 1 PHE A 176 ? ? -150.11 77.88   
4 1 ASN A 244 ? ? -102.73 52.62   
5 1 LYS A 252 ? ? 58.71   -139.02 
# 
_pdbx_validate_main_chain_plane.id                       1 
_pdbx_validate_main_chain_plane.PDB_model_num            1 
_pdbx_validate_main_chain_plane.auth_comp_id             THR 
_pdbx_validate_main_chain_plane.auth_asym_id             A 
_pdbx_validate_main_chain_plane.auth_seq_id              125 
_pdbx_validate_main_chain_plane.PDB_ins_code             ? 
_pdbx_validate_main_chain_plane.label_alt_id             ? 
_pdbx_validate_main_chain_plane.improper_torsion_angle   -12.57 
# 
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 
5DU F13  F  N N 1   
5DU C9   C  Y N 2   
5DU C8   C  Y N 3   
5DU S24  S  N N 4   
5DU C25  C  N N 5   
5DU C26  C  N N 6   
5DU O27  O  N N 7   
5DU C7   C  Y N 8   
5DU F12  F  N N 9   
5DU C6   C  Y N 10  
5DU F11  F  N N 11  
5DU C10  C  Y N 12  
5DU C5   C  Y N 13  
5DU S1   S  N N 14  
5DU O3   O  N N 15  
5DU N4   N  N N 16  
5DU O2   O  N N 17  
5DU N14  N  N N 18  
5DU C15  C  N S 19  
5DU C19  C  Y N 20  
5DU C20  C  Y N 21  
5DU C21  C  Y N 22  
5DU C22  C  Y N 23  
5DU C23  C  Y N 24  
5DU C18  C  Y N 25  
5DU C17  C  N N 26  
5DU C16  C  N N 27  
5DU H1   H  N N 28  
5DU H2   H  N N 29  
5DU H3   H  N N 30  
5DU H4   H  N N 31  
5DU H5   H  N N 32  
5DU H6   H  N N 33  
5DU H7   H  N N 34  
5DU H8   H  N N 35  
5DU H9   H  N N 36  
5DU H10  H  N N 37  
5DU H11  H  N N 38  
5DU H12  H  N N 39  
5DU H13  H  N N 40  
5DU H14  H  N N 41  
5DU H15  H  N N 42  
5DU H16  H  N N 43  
5DU H17  H  N N 44  
ALA N    N  N N 45  
ALA CA   C  N S 46  
ALA C    C  N N 47  
ALA O    O  N N 48  
ALA CB   C  N N 49  
ALA OXT  O  N N 50  
ALA H    H  N N 51  
ALA H2   H  N N 52  
ALA HA   H  N N 53  
ALA HB1  H  N N 54  
ALA HB2  H  N N 55  
ALA HB3  H  N N 56  
ALA HXT  H  N N 57  
ARG N    N  N N 58  
ARG CA   C  N S 59  
ARG C    C  N N 60  
ARG O    O  N N 61  
ARG CB   C  N N 62  
ARG CG   C  N N 63  
ARG CD   C  N N 64  
ARG NE   N  N N 65  
ARG CZ   C  N N 66  
ARG NH1  N  N N 67  
ARG NH2  N  N N 68  
ARG OXT  O  N N 69  
ARG H    H  N N 70  
ARG H2   H  N N 71  
ARG HA   H  N N 72  
ARG HB2  H  N N 73  
ARG HB3  H  N N 74  
ARG HG2  H  N N 75  
ARG HG3  H  N N 76  
ARG HD2  H  N N 77  
ARG HD3  H  N N 78  
ARG HE   H  N N 79  
ARG HH11 H  N N 80  
ARG HH12 H  N N 81  
ARG HH21 H  N N 82  
ARG HH22 H  N N 83  
ARG HXT  H  N N 84  
ASN N    N  N N 85  
ASN CA   C  N S 86  
ASN C    C  N N 87  
ASN O    O  N N 88  
ASN CB   C  N N 89  
ASN CG   C  N N 90  
ASN OD1  O  N N 91  
ASN ND2  N  N N 92  
ASN OXT  O  N N 93  
ASN H    H  N N 94  
ASN H2   H  N N 95  
ASN HA   H  N N 96  
ASN HB2  H  N N 97  
ASN HB3  H  N N 98  
ASN HD21 H  N N 99  
ASN HD22 H  N N 100 
ASN HXT  H  N N 101 
ASP N    N  N N 102 
ASP CA   C  N S 103 
ASP C    C  N N 104 
ASP O    O  N N 105 
ASP CB   C  N N 106 
ASP CG   C  N N 107 
ASP OD1  O  N N 108 
ASP OD2  O  N N 109 
ASP OXT  O  N N 110 
ASP H    H  N N 111 
ASP H2   H  N N 112 
ASP HA   H  N N 113 
ASP HB2  H  N N 114 
ASP HB3  H  N N 115 
ASP HD2  H  N N 116 
ASP HXT  H  N N 117 
BEZ C    C  N N 118 
BEZ O1   O  N N 119 
BEZ O2   O  N N 120 
BEZ C1   C  Y N 121 
BEZ C2   C  Y N 122 
BEZ C3   C  Y N 123 
BEZ C4   C  Y N 124 
BEZ C5   C  Y N 125 
BEZ C6   C  Y N 126 
BEZ HO2  H  N N 127 
BEZ H2   H  N N 128 
BEZ H3   H  N N 129 
BEZ H4   H  N N 130 
BEZ H5   H  N N 131 
BEZ H6   H  N N 132 
CYS N    N  N N 133 
CYS CA   C  N R 134 
CYS C    C  N N 135 
CYS O    O  N N 136 
CYS CB   C  N N 137 
CYS SG   S  N N 138 
CYS OXT  O  N N 139 
CYS H    H  N N 140 
CYS H2   H  N N 141 
CYS HA   H  N N 142 
CYS HB2  H  N N 143 
CYS HB3  H  N N 144 
CYS HG   H  N N 145 
CYS HXT  H  N N 146 
DMS S    S  N N 147 
DMS O    O  N N 148 
DMS C1   C  N N 149 
DMS C2   C  N N 150 
DMS H11  H  N N 151 
DMS H12  H  N N 152 
DMS H13  H  N N 153 
DMS H21  H  N N 154 
DMS H22  H  N N 155 
DMS H23  H  N N 156 
GLN N    N  N N 157 
GLN CA   C  N S 158 
GLN C    C  N N 159 
GLN O    O  N N 160 
GLN CB   C  N N 161 
GLN CG   C  N N 162 
GLN CD   C  N N 163 
GLN OE1  O  N N 164 
GLN NE2  N  N N 165 
GLN OXT  O  N N 166 
GLN H    H  N N 167 
GLN H2   H  N N 168 
GLN HA   H  N N 169 
GLN HB2  H  N N 170 
GLN HB3  H  N N 171 
GLN HG2  H  N N 172 
GLN HG3  H  N N 173 
GLN HE21 H  N N 174 
GLN HE22 H  N N 175 
GLN HXT  H  N N 176 
GLU N    N  N N 177 
GLU CA   C  N S 178 
GLU C    C  N N 179 
GLU O    O  N N 180 
GLU CB   C  N N 181 
GLU CG   C  N N 182 
GLU CD   C  N N 183 
GLU OE1  O  N N 184 
GLU OE2  O  N N 185 
GLU OXT  O  N N 186 
GLU H    H  N N 187 
GLU H2   H  N N 188 
GLU HA   H  N N 189 
GLU HB2  H  N N 190 
GLU HB3  H  N N 191 
GLU HG2  H  N N 192 
GLU HG3  H  N N 193 
GLU HE2  H  N N 194 
GLU HXT  H  N N 195 
GLY N    N  N N 196 
GLY CA   C  N N 197 
GLY C    C  N N 198 
GLY O    O  N N 199 
GLY OXT  O  N N 200 
GLY H    H  N N 201 
GLY H2   H  N N 202 
GLY HA2  H  N N 203 
GLY HA3  H  N N 204 
GLY HXT  H  N N 205 
HIS N    N  N N 206 
HIS CA   C  N S 207 
HIS C    C  N N 208 
HIS O    O  N N 209 
HIS CB   C  N N 210 
HIS CG   C  Y N 211 
HIS ND1  N  Y N 212 
HIS CD2  C  Y N 213 
HIS CE1  C  Y N 214 
HIS NE2  N  Y N 215 
HIS OXT  O  N N 216 
HIS H    H  N N 217 
HIS H2   H  N N 218 
HIS HA   H  N N 219 
HIS HB2  H  N N 220 
HIS HB3  H  N N 221 
HIS HD1  H  N N 222 
HIS HD2  H  N N 223 
HIS HE1  H  N N 224 
HIS HE2  H  N N 225 
HIS HXT  H  N N 226 
HOH O    O  N N 227 
HOH H1   H  N N 228 
HOH H2   H  N N 229 
ILE N    N  N N 230 
ILE CA   C  N S 231 
ILE C    C  N N 232 
ILE O    O  N N 233 
ILE CB   C  N S 234 
ILE CG1  C  N N 235 
ILE CG2  C  N N 236 
ILE CD1  C  N N 237 
ILE OXT  O  N N 238 
ILE H    H  N N 239 
ILE H2   H  N N 240 
ILE HA   H  N N 241 
ILE HB   H  N N 242 
ILE HG12 H  N N 243 
ILE HG13 H  N N 244 
ILE HG21 H  N N 245 
ILE HG22 H  N N 246 
ILE HG23 H  N N 247 
ILE HD11 H  N N 248 
ILE HD12 H  N N 249 
ILE HD13 H  N N 250 
ILE HXT  H  N N 251 
LEU N    N  N N 252 
LEU CA   C  N S 253 
LEU C    C  N N 254 
LEU O    O  N N 255 
LEU CB   C  N N 256 
LEU CG   C  N N 257 
LEU CD1  C  N N 258 
LEU CD2  C  N N 259 
LEU OXT  O  N N 260 
LEU H    H  N N 261 
LEU H2   H  N N 262 
LEU HA   H  N N 263 
LEU HB2  H  N N 264 
LEU HB3  H  N N 265 
LEU HG   H  N N 266 
LEU HD11 H  N N 267 
LEU HD12 H  N N 268 
LEU HD13 H  N N 269 
LEU HD21 H  N N 270 
LEU HD22 H  N N 271 
LEU HD23 H  N N 272 
LEU HXT  H  N N 273 
LYS N    N  N N 274 
LYS CA   C  N S 275 
LYS C    C  N N 276 
LYS O    O  N N 277 
LYS CB   C  N N 278 
LYS CG   C  N N 279 
LYS CD   C  N N 280 
LYS CE   C  N N 281 
LYS NZ   N  N N 282 
LYS OXT  O  N N 283 
LYS H    H  N N 284 
LYS H2   H  N N 285 
LYS HA   H  N N 286 
LYS HB2  H  N N 287 
LYS HB3  H  N N 288 
LYS HG2  H  N N 289 
LYS HG3  H  N N 290 
LYS HD2  H  N N 291 
LYS HD3  H  N N 292 
LYS HE2  H  N N 293 
LYS HE3  H  N N 294 
LYS HZ1  H  N N 295 
LYS HZ2  H  N N 296 
LYS HZ3  H  N N 297 
LYS HXT  H  N N 298 
MET N    N  N N 299 
MET CA   C  N S 300 
MET C    C  N N 301 
MET O    O  N N 302 
MET CB   C  N N 303 
MET CG   C  N N 304 
MET SD   S  N N 305 
MET CE   C  N N 306 
MET OXT  O  N N 307 
MET H    H  N N 308 
MET H2   H  N N 309 
MET HA   H  N N 310 
MET HB2  H  N N 311 
MET HB3  H  N N 312 
MET HG2  H  N N 313 
MET HG3  H  N N 314 
MET HE1  H  N N 315 
MET HE2  H  N N 316 
MET HE3  H  N N 317 
MET HXT  H  N N 318 
NA  NA   NA N N 319 
PHE N    N  N N 320 
PHE CA   C  N S 321 
PHE C    C  N N 322 
PHE O    O  N N 323 
PHE CB   C  N N 324 
PHE CG   C  Y N 325 
PHE CD1  C  Y N 326 
PHE CD2  C  Y N 327 
PHE CE1  C  Y N 328 
PHE CE2  C  Y N 329 
PHE CZ   C  Y N 330 
PHE OXT  O  N N 331 
PHE H    H  N N 332 
PHE H2   H  N N 333 
PHE HA   H  N N 334 
PHE HB2  H  N N 335 
PHE HB3  H  N N 336 
PHE HD1  H  N N 337 
PHE HD2  H  N N 338 
PHE HE1  H  N N 339 
PHE HE2  H  N N 340 
PHE HZ   H  N N 341 
PHE HXT  H  N N 342 
PRO N    N  N N 343 
PRO CA   C  N S 344 
PRO C    C  N N 345 
PRO O    O  N N 346 
PRO CB   C  N N 347 
PRO CG   C  N N 348 
PRO CD   C  N N 349 
PRO OXT  O  N N 350 
PRO H    H  N N 351 
PRO HA   H  N N 352 
PRO HB2  H  N N 353 
PRO HB3  H  N N 354 
PRO HG2  H  N N 355 
PRO HG3  H  N N 356 
PRO HD2  H  N N 357 
PRO HD3  H  N N 358 
PRO HXT  H  N N 359 
SER N    N  N N 360 
SER CA   C  N S 361 
SER C    C  N N 362 
SER O    O  N N 363 
SER CB   C  N N 364 
SER OG   O  N N 365 
SER OXT  O  N N 366 
SER H    H  N N 367 
SER H2   H  N N 368 
SER HA   H  N N 369 
SER HB2  H  N N 370 
SER HB3  H  N N 371 
SER HG   H  N N 372 
SER HXT  H  N N 373 
THR N    N  N N 374 
THR CA   C  N S 375 
THR C    C  N N 376 
THR O    O  N N 377 
THR CB   C  N R 378 
THR OG1  O  N N 379 
THR CG2  C  N N 380 
THR OXT  O  N N 381 
THR H    H  N N 382 
THR H2   H  N N 383 
THR HA   H  N N 384 
THR HB   H  N N 385 
THR HG1  H  N N 386 
THR HG21 H  N N 387 
THR HG22 H  N N 388 
THR HG23 H  N N 389 
THR HXT  H  N N 390 
TRP N    N  N N 391 
TRP CA   C  N S 392 
TRP C    C  N N 393 
TRP O    O  N N 394 
TRP CB   C  N N 395 
TRP CG   C  Y N 396 
TRP CD1  C  Y N 397 
TRP CD2  C  Y N 398 
TRP NE1  N  Y N 399 
TRP CE2  C  Y N 400 
TRP CE3  C  Y N 401 
TRP CZ2  C  Y N 402 
TRP CZ3  C  Y N 403 
TRP CH2  C  Y N 404 
TRP OXT  O  N N 405 
TRP H    H  N N 406 
TRP H2   H  N N 407 
TRP HA   H  N N 408 
TRP HB2  H  N N 409 
TRP HB3  H  N N 410 
TRP HD1  H  N N 411 
TRP HE1  H  N N 412 
TRP HE3  H  N N 413 
TRP HZ2  H  N N 414 
TRP HZ3  H  N N 415 
TRP HH2  H  N N 416 
TRP HXT  H  N N 417 
TYR N    N  N N 418 
TYR CA   C  N S 419 
TYR C    C  N N 420 
TYR O    O  N N 421 
TYR CB   C  N N 422 
TYR CG   C  Y N 423 
TYR CD1  C  Y N 424 
TYR CD2  C  Y N 425 
TYR CE1  C  Y N 426 
TYR CE2  C  Y N 427 
TYR CZ   C  Y N 428 
TYR OH   O  N N 429 
TYR OXT  O  N N 430 
TYR H    H  N N 431 
TYR H2   H  N N 432 
TYR HA   H  N N 433 
TYR HB2  H  N N 434 
TYR HB3  H  N N 435 
TYR HD1  H  N N 436 
TYR HD2  H  N N 437 
TYR HE1  H  N N 438 
TYR HE2  H  N N 439 
TYR HH   H  N N 440 
TYR HXT  H  N N 441 
VAL N    N  N N 442 
VAL CA   C  N S 443 
VAL C    C  N N 444 
VAL O    O  N N 445 
VAL CB   C  N N 446 
VAL CG1  C  N N 447 
VAL CG2  C  N N 448 
VAL OXT  O  N N 449 
VAL H    H  N N 450 
VAL H2   H  N N 451 
VAL HA   H  N N 452 
VAL HB   H  N N 453 
VAL HG11 H  N N 454 
VAL HG12 H  N N 455 
VAL HG13 H  N N 456 
VAL HG21 H  N N 457 
VAL HG22 H  N N 458 
VAL HG23 H  N N 459 
VAL HXT  H  N N 460 
ZN  ZN   ZN N N 461 
# 
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 
5DU O27 C26  sing N N 1   
5DU C26 C25  sing N N 2   
5DU C23 C18  doub Y N 3   
5DU C23 C22  sing Y N 4   
5DU C17 C18  sing N N 5   
5DU C17 C16  sing N N 6   
5DU C18 C19  sing Y N 7   
5DU C22 C21  doub Y N 8   
5DU C21 C20  sing Y N 9   
5DU C19 C20  doub Y N 10  
5DU C19 C15  sing N N 11  
5DU F13 C9   sing N N 12  
5DU C15 C16  sing N N 13  
5DU C15 N14  sing N N 14  
5DU C25 S24  sing N N 15  
5DU S24 C8   sing N N 16  
5DU N14 C10  sing N N 17  
5DU C9  C8   doub Y N 18  
5DU C9  C10  sing Y N 19  
5DU C8  C7   sing Y N 20  
5DU C10 C5   doub Y N 21  
5DU C7  C6   doub Y N 22  
5DU C7  F12  sing N N 23  
5DU C5  C6   sing Y N 24  
5DU C5  S1   sing N N 25  
5DU C6  F11  sing N N 26  
5DU N4  S1   sing N N 27  
5DU S1  O2   doub N N 28  
5DU S1  O3   doub N N 29  
5DU C25 H1   sing N N 30  
5DU C25 H2   sing N N 31  
5DU C26 H3   sing N N 32  
5DU C26 H4   sing N N 33  
5DU O27 H5   sing N N 34  
5DU N4  H6   sing N N 35  
5DU N4  H7   sing N N 36  
5DU N14 H8   sing N N 37  
5DU C15 H9   sing N N 38  
5DU C20 H10  sing N N 39  
5DU C21 H11  sing N N 40  
5DU C22 H12  sing N N 41  
5DU C23 H13  sing N N 42  
5DU C17 H14  sing N N 43  
5DU C17 H15  sing N N 44  
5DU C16 H16  sing N N 45  
5DU C16 H17  sing N N 46  
ALA N   CA   sing N N 47  
ALA N   H    sing N N 48  
ALA N   H2   sing N N 49  
ALA CA  C    sing N N 50  
ALA CA  CB   sing N N 51  
ALA CA  HA   sing N N 52  
ALA C   O    doub N N 53  
ALA C   OXT  sing N N 54  
ALA CB  HB1  sing N N 55  
ALA CB  HB2  sing N N 56  
ALA CB  HB3  sing N N 57  
ALA OXT HXT  sing N N 58  
ARG N   CA   sing N N 59  
ARG N   H    sing N N 60  
ARG N   H2   sing N N 61  
ARG CA  C    sing N N 62  
ARG CA  CB   sing N N 63  
ARG CA  HA   sing N N 64  
ARG C   O    doub N N 65  
ARG C   OXT  sing N N 66  
ARG CB  CG   sing N N 67  
ARG CB  HB2  sing N N 68  
ARG CB  HB3  sing N N 69  
ARG CG  CD   sing N N 70  
ARG CG  HG2  sing N N 71  
ARG CG  HG3  sing N N 72  
ARG CD  NE   sing N N 73  
ARG CD  HD2  sing N N 74  
ARG CD  HD3  sing N N 75  
ARG NE  CZ   sing N N 76  
ARG NE  HE   sing N N 77  
ARG CZ  NH1  sing N N 78  
ARG CZ  NH2  doub N N 79  
ARG NH1 HH11 sing N N 80  
ARG NH1 HH12 sing N N 81  
ARG NH2 HH21 sing N N 82  
ARG NH2 HH22 sing N N 83  
ARG OXT HXT  sing N N 84  
ASN N   CA   sing N N 85  
ASN N   H    sing N N 86  
ASN N   H2   sing N N 87  
ASN CA  C    sing N N 88  
ASN CA  CB   sing N N 89  
ASN CA  HA   sing N N 90  
ASN C   O    doub N N 91  
ASN C   OXT  sing N N 92  
ASN CB  CG   sing N N 93  
ASN CB  HB2  sing N N 94  
ASN CB  HB3  sing N N 95  
ASN CG  OD1  doub N N 96  
ASN CG  ND2  sing N N 97  
ASN ND2 HD21 sing N N 98  
ASN ND2 HD22 sing N N 99  
ASN OXT HXT  sing N N 100 
ASP N   CA   sing N N 101 
ASP N   H    sing N N 102 
ASP N   H2   sing N N 103 
ASP CA  C    sing N N 104 
ASP CA  CB   sing N N 105 
ASP CA  HA   sing N N 106 
ASP C   O    doub N N 107 
ASP C   OXT  sing N N 108 
ASP CB  CG   sing N N 109 
ASP CB  HB2  sing N N 110 
ASP CB  HB3  sing N N 111 
ASP CG  OD1  doub N N 112 
ASP CG  OD2  sing N N 113 
ASP OD2 HD2  sing N N 114 
ASP OXT HXT  sing N N 115 
BEZ C   O1   doub N N 116 
BEZ C   O2   sing N N 117 
BEZ C   C1   sing N N 118 
BEZ O2  HO2  sing N N 119 
BEZ C1  C2   doub Y N 120 
BEZ C1  C6   sing Y N 121 
BEZ C2  C3   sing Y N 122 
BEZ C2  H2   sing N N 123 
BEZ C3  C4   doub Y N 124 
BEZ C3  H3   sing N N 125 
BEZ C4  C5   sing Y N 126 
BEZ C4  H4   sing N N 127 
BEZ C5  C6   doub Y N 128 
BEZ C5  H5   sing N N 129 
BEZ C6  H6   sing N N 130 
CYS N   CA   sing N N 131 
CYS N   H    sing N N 132 
CYS N   H2   sing N N 133 
CYS CA  C    sing N N 134 
CYS CA  CB   sing N N 135 
CYS CA  HA   sing N N 136 
CYS C   O    doub N N 137 
CYS C   OXT  sing N N 138 
CYS CB  SG   sing N N 139 
CYS CB  HB2  sing N N 140 
CYS CB  HB3  sing N N 141 
CYS SG  HG   sing N N 142 
CYS OXT HXT  sing N N 143 
DMS S   O    doub N N 144 
DMS S   C1   sing N N 145 
DMS S   C2   sing N N 146 
DMS C1  H11  sing N N 147 
DMS C1  H12  sing N N 148 
DMS C1  H13  sing N N 149 
DMS C2  H21  sing N N 150 
DMS C2  H22  sing N N 151 
DMS C2  H23  sing N N 152 
GLN N   CA   sing N N 153 
GLN N   H    sing N N 154 
GLN N   H2   sing N N 155 
GLN CA  C    sing N N 156 
GLN CA  CB   sing N N 157 
GLN CA  HA   sing N N 158 
GLN C   O    doub N N 159 
GLN C   OXT  sing N N 160 
GLN CB  CG   sing N N 161 
GLN CB  HB2  sing N N 162 
GLN CB  HB3  sing N N 163 
GLN CG  CD   sing N N 164 
GLN CG  HG2  sing N N 165 
GLN CG  HG3  sing N N 166 
GLN CD  OE1  doub N N 167 
GLN CD  NE2  sing N N 168 
GLN NE2 HE21 sing N N 169 
GLN NE2 HE22 sing N N 170 
GLN OXT HXT  sing N N 171 
GLU N   CA   sing N N 172 
GLU N   H    sing N N 173 
GLU N   H2   sing N N 174 
GLU CA  C    sing N N 175 
GLU CA  CB   sing N N 176 
GLU CA  HA   sing N N 177 
GLU C   O    doub N N 178 
GLU C   OXT  sing N N 179 
GLU CB  CG   sing N N 180 
GLU CB  HB2  sing N N 181 
GLU CB  HB3  sing N N 182 
GLU CG  CD   sing N N 183 
GLU CG  HG2  sing N N 184 
GLU CG  HG3  sing N N 185 
GLU CD  OE1  doub N N 186 
GLU CD  OE2  sing N N 187 
GLU OE2 HE2  sing N N 188 
GLU OXT HXT  sing N N 189 
GLY N   CA   sing N N 190 
GLY N   H    sing N N 191 
GLY N   H2   sing N N 192 
GLY CA  C    sing N N 193 
GLY CA  HA2  sing N N 194 
GLY CA  HA3  sing N N 195 
GLY C   O    doub N N 196 
GLY C   OXT  sing N N 197 
GLY OXT HXT  sing N N 198 
HIS N   CA   sing N N 199 
HIS N   H    sing N N 200 
HIS N   H2   sing N N 201 
HIS CA  C    sing N N 202 
HIS CA  CB   sing N N 203 
HIS CA  HA   sing N N 204 
HIS C   O    doub N N 205 
HIS C   OXT  sing N N 206 
HIS CB  CG   sing N N 207 
HIS CB  HB2  sing N N 208 
HIS CB  HB3  sing N N 209 
HIS CG  ND1  sing Y N 210 
HIS CG  CD2  doub Y N 211 
HIS ND1 CE1  doub Y N 212 
HIS ND1 HD1  sing N N 213 
HIS CD2 NE2  sing Y N 214 
HIS CD2 HD2  sing N N 215 
HIS CE1 NE2  sing Y N 216 
HIS CE1 HE1  sing N N 217 
HIS NE2 HE2  sing N N 218 
HIS OXT HXT  sing N N 219 
HOH O   H1   sing N N 220 
HOH O   H2   sing N N 221 
ILE N   CA   sing N N 222 
ILE N   H    sing N N 223 
ILE N   H2   sing N N 224 
ILE CA  C    sing N N 225 
ILE CA  CB   sing N N 226 
ILE CA  HA   sing N N 227 
ILE C   O    doub N N 228 
ILE C   OXT  sing N N 229 
ILE CB  CG1  sing N N 230 
ILE CB  CG2  sing N N 231 
ILE CB  HB   sing N N 232 
ILE CG1 CD1  sing N N 233 
ILE CG1 HG12 sing N N 234 
ILE CG1 HG13 sing N N 235 
ILE CG2 HG21 sing N N 236 
ILE CG2 HG22 sing N N 237 
ILE CG2 HG23 sing N N 238 
ILE CD1 HD11 sing N N 239 
ILE CD1 HD12 sing N N 240 
ILE CD1 HD13 sing N N 241 
ILE OXT HXT  sing N N 242 
LEU N   CA   sing N N 243 
LEU N   H    sing N N 244 
LEU N   H2   sing N N 245 
LEU CA  C    sing N N 246 
LEU CA  CB   sing N N 247 
LEU CA  HA   sing N N 248 
LEU C   O    doub N N 249 
LEU C   OXT  sing N N 250 
LEU CB  CG   sing N N 251 
LEU CB  HB2  sing N N 252 
LEU CB  HB3  sing N N 253 
LEU CG  CD1  sing N N 254 
LEU CG  CD2  sing N N 255 
LEU CG  HG   sing N N 256 
LEU CD1 HD11 sing N N 257 
LEU CD1 HD12 sing N N 258 
LEU CD1 HD13 sing N N 259 
LEU CD2 HD21 sing N N 260 
LEU CD2 HD22 sing N N 261 
LEU CD2 HD23 sing N N 262 
LEU OXT HXT  sing N N 263 
LYS N   CA   sing N N 264 
LYS N   H    sing N N 265 
LYS N   H2   sing N N 266 
LYS CA  C    sing N N 267 
LYS CA  CB   sing N N 268 
LYS CA  HA   sing N N 269 
LYS C   O    doub N N 270 
LYS C   OXT  sing N N 271 
LYS CB  CG   sing N N 272 
LYS CB  HB2  sing N N 273 
LYS CB  HB3  sing N N 274 
LYS CG  CD   sing N N 275 
LYS CG  HG2  sing N N 276 
LYS CG  HG3  sing N N 277 
LYS CD  CE   sing N N 278 
LYS CD  HD2  sing N N 279 
LYS CD  HD3  sing N N 280 
LYS CE  NZ   sing N N 281 
LYS CE  HE2  sing N N 282 
LYS CE  HE3  sing N N 283 
LYS NZ  HZ1  sing N N 284 
LYS NZ  HZ2  sing N N 285 
LYS NZ  HZ3  sing N N 286 
LYS OXT HXT  sing N N 287 
MET N   CA   sing N N 288 
MET N   H    sing N N 289 
MET N   H2   sing N N 290 
MET CA  C    sing N N 291 
MET CA  CB   sing N N 292 
MET CA  HA   sing N N 293 
MET C   O    doub N N 294 
MET C   OXT  sing N N 295 
MET CB  CG   sing N N 296 
MET CB  HB2  sing N N 297 
MET CB  HB3  sing N N 298 
MET CG  SD   sing N N 299 
MET CG  HG2  sing N N 300 
MET CG  HG3  sing N N 301 
MET SD  CE   sing N N 302 
MET CE  HE1  sing N N 303 
MET CE  HE2  sing N N 304 
MET CE  HE3  sing N N 305 
MET OXT HXT  sing N N 306 
PHE N   CA   sing N N 307 
PHE N   H    sing N N 308 
PHE N   H2   sing N N 309 
PHE CA  C    sing N N 310 
PHE CA  CB   sing N N 311 
PHE CA  HA   sing N N 312 
PHE C   O    doub N N 313 
PHE C   OXT  sing N N 314 
PHE CB  CG   sing N N 315 
PHE CB  HB2  sing N N 316 
PHE CB  HB3  sing N N 317 
PHE CG  CD1  doub Y N 318 
PHE CG  CD2  sing Y N 319 
PHE CD1 CE1  sing Y N 320 
PHE CD1 HD1  sing N N 321 
PHE CD2 CE2  doub Y N 322 
PHE CD2 HD2  sing N N 323 
PHE CE1 CZ   doub Y N 324 
PHE CE1 HE1  sing N N 325 
PHE CE2 CZ   sing Y N 326 
PHE CE2 HE2  sing N N 327 
PHE CZ  HZ   sing N N 328 
PHE OXT HXT  sing N N 329 
PRO N   CA   sing N N 330 
PRO N   CD   sing N N 331 
PRO N   H    sing N N 332 
PRO CA  C    sing N N 333 
PRO CA  CB   sing N N 334 
PRO CA  HA   sing N N 335 
PRO C   O    doub N N 336 
PRO C   OXT  sing N N 337 
PRO CB  CG   sing N N 338 
PRO CB  HB2  sing N N 339 
PRO CB  HB3  sing N N 340 
PRO CG  CD   sing N N 341 
PRO CG  HG2  sing N N 342 
PRO CG  HG3  sing N N 343 
PRO CD  HD2  sing N N 344 
PRO CD  HD3  sing N N 345 
PRO OXT HXT  sing N N 346 
SER N   CA   sing N N 347 
SER N   H    sing N N 348 
SER N   H2   sing N N 349 
SER CA  C    sing N N 350 
SER CA  CB   sing N N 351 
SER CA  HA   sing N N 352 
SER C   O    doub N N 353 
SER C   OXT  sing N N 354 
SER CB  OG   sing N N 355 
SER CB  HB2  sing N N 356 
SER CB  HB3  sing N N 357 
SER OG  HG   sing N N 358 
SER OXT HXT  sing N N 359 
THR N   CA   sing N N 360 
THR N   H    sing N N 361 
THR N   H2   sing N N 362 
THR CA  C    sing N N 363 
THR CA  CB   sing N N 364 
THR CA  HA   sing N N 365 
THR C   O    doub N N 366 
THR C   OXT  sing N N 367 
THR CB  OG1  sing N N 368 
THR CB  CG2  sing N N 369 
THR CB  HB   sing N N 370 
THR OG1 HG1  sing N N 371 
THR CG2 HG21 sing N N 372 
THR CG2 HG22 sing N N 373 
THR CG2 HG23 sing N N 374 
THR OXT HXT  sing N N 375 
TRP N   CA   sing N N 376 
TRP N   H    sing N N 377 
TRP N   H2   sing N N 378 
TRP CA  C    sing N N 379 
TRP CA  CB   sing N N 380 
TRP CA  HA   sing N N 381 
TRP C   O    doub N N 382 
TRP C   OXT  sing N N 383 
TRP CB  CG   sing N N 384 
TRP CB  HB2  sing N N 385 
TRP CB  HB3  sing N N 386 
TRP CG  CD1  doub Y N 387 
TRP CG  CD2  sing Y N 388 
TRP CD1 NE1  sing Y N 389 
TRP CD1 HD1  sing N N 390 
TRP CD2 CE2  doub Y N 391 
TRP CD2 CE3  sing Y N 392 
TRP NE1 CE2  sing Y N 393 
TRP NE1 HE1  sing N N 394 
TRP CE2 CZ2  sing Y N 395 
TRP CE3 CZ3  doub Y N 396 
TRP CE3 HE3  sing N N 397 
TRP CZ2 CH2  doub Y N 398 
TRP CZ2 HZ2  sing N N 399 
TRP CZ3 CH2  sing Y N 400 
TRP CZ3 HZ3  sing N N 401 
TRP CH2 HH2  sing N N 402 
TRP OXT HXT  sing N N 403 
TYR N   CA   sing N N 404 
TYR N   H    sing N N 405 
TYR N   H2   sing N N 406 
TYR CA  C    sing N N 407 
TYR CA  CB   sing N N 408 
TYR CA  HA   sing N N 409 
TYR C   O    doub N N 410 
TYR C   OXT  sing N N 411 
TYR CB  CG   sing N N 412 
TYR CB  HB2  sing N N 413 
TYR CB  HB3  sing N N 414 
TYR CG  CD1  doub Y N 415 
TYR CG  CD2  sing Y N 416 
TYR CD1 CE1  sing Y N 417 
TYR CD1 HD1  sing N N 418 
TYR CD2 CE2  doub Y N 419 
TYR CD2 HD2  sing N N 420 
TYR CE1 CZ   doub Y N 421 
TYR CE1 HE1  sing N N 422 
TYR CE2 CZ   sing Y N 423 
TYR CE2 HE2  sing N N 424 
TYR CZ  OH   sing N N 425 
TYR OH  HH   sing N N 426 
TYR OXT HXT  sing N N 427 
VAL N   CA   sing N N 428 
VAL N   H    sing N N 429 
VAL N   H2   sing N N 430 
VAL CA  C    sing N N 431 
VAL CA  CB   sing N N 432 
VAL CA  HA   sing N N 433 
VAL C   O    doub N N 434 
VAL C   OXT  sing N N 435 
VAL CB  CG1  sing N N 436 
VAL CB  CG2  sing N N 437 
VAL CB  HB   sing N N 438 
VAL CG1 HG11 sing N N 439 
VAL CG1 HG12 sing N N 440 
VAL CG1 HG13 sing N N 441 
VAL CG2 HG21 sing N N 442 
VAL CG2 HG22 sing N N 443 
VAL CG2 HG23 sing N N 444 
VAL OXT HXT  sing N N 445 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        5DU 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   5DU 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   4HT0 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    6RMX 
_atom_sites.fract_transf_matrix[1][1]   0.023663 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.005963 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.024361 
_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]   0.014369 
_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  
F  
N  
NA 
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . HIS A 1 1   ? 11.136  -0.559  7.645   1.00 38.73 ? 4   HIS A N   1 
ATOM   2    C  CA  . HIS A 1 1   ? 10.188  0.116   8.570   1.00 38.98 ? 4   HIS A CA  1 
ATOM   3    C  C   . HIS A 1 1   ? 9.474   -0.941  9.412   1.00 31.40 ? 4   HIS A C   1 
ATOM   4    O  O   . HIS A 1 1   ? 9.736   -2.132  9.256   1.00 28.46 ? 4   HIS A O   1 
ATOM   5    C  CB  . HIS A 1 1   ? 9.273   1.089   7.813   1.00 50.62 ? 4   HIS A CB  1 
ATOM   6    C  CG  . HIS A 1 1   ? 9.034   2.346   8.584   1.00 66.89 ? 4   HIS A CG  1 
ATOM   7    N  ND1 . HIS A 1 1   ? 7.847   3.065   8.494   1.00 74.16 ? 4   HIS A ND1 1 
ATOM   8    C  CD2 . HIS A 1 1   ? 9.810   2.998   9.484   1.00 68.06 ? 4   HIS A CD2 1 
ATOM   9    C  CE1 . HIS A 1 1   ? 7.916   4.116   9.293   1.00 78.05 ? 4   HIS A CE1 1 
ATOM   10   N  NE2 . HIS A 1 1   ? 9.113   4.093   9.919   1.00 77.25 ? 4   HIS A NE2 1 
ATOM   11   N  N   . TRP A 1 2   ? 8.627   -0.498  10.346  1.00 26.54 ? 5   TRP A N   1 
ATOM   12   C  CA  . TRP A 1 2   ? 7.961   -1.435  11.248  1.00 21.79 ? 5   TRP A CA  1 
ATOM   13   C  C   . TRP A 1 2   ? 6.938   -2.258  10.478  1.00 19.92 ? 5   TRP A C   1 
ATOM   14   O  O   . TRP A 1 2   ? 6.389   -1.815  9.464   1.00 21.88 ? 5   TRP A O   1 
ATOM   15   C  CB  . TRP A 1 2   ? 7.287   -0.734  12.435  1.00 20.90 ? 5   TRP A CB  1 
ATOM   16   C  CG  . TRP A 1 2   ? 6.124   0.136   12.050  1.00 20.47 ? 5   TRP A CG  1 
ATOM   17   C  CD1 . TRP A 1 2   ? 6.158   1.465   11.738  1.00 20.73 ? 5   TRP A CD1 1 
ATOM   18   C  CD2 . TRP A 1 2   ? 4.739   -0.264  11.956  1.00 17.60 ? 5   TRP A CD2 1 
ATOM   19   N  NE1 . TRP A 1 2   ? 4.892   1.931   11.483  1.00 21.75 ? 5   TRP A NE1 1 
ATOM   20   C  CE2 . TRP A 1 2   ? 4.005   0.891   11.618  1.00 18.78 ? 5   TRP A CE2 1 
ATOM   21   C  CE3 . TRP A 1 2   ? 4.064   -1.482  12.177  1.00 16.19 ? 5   TRP A CE3 1 
ATOM   22   C  CZ2 . TRP A 1 2   ? 2.623   0.863   11.451  1.00 17.10 ? 5   TRP A CZ2 1 
ATOM   23   C  CZ3 . TRP A 1 2   ? 2.692   -1.517  12.020  1.00 15.22 ? 5   TRP A CZ3 1 
ATOM   24   C  CH2 . TRP A 1 2   ? 2.004   -0.338  11.689  1.00 16.68 ? 5   TRP A CH2 1 
ATOM   25   N  N   . GLY A 1 3   ? 6.675   -3.458  11.007  1.00 18.37 ? 6   GLY A N   1 
ATOM   26   C  CA  . GLY A 1 3   ? 5.623   -4.280  10.420  1.00 18.59 ? 6   GLY A CA  1 
ATOM   27   C  C   . GLY A 1 3   ? 5.286   -5.461  11.316  1.00 17.99 ? 6   GLY A C   1 
ATOM   28   O  O   . GLY A 1 3   ? 5.337   -5.333  12.531  1.00 18.36 ? 6   GLY A O   1 
ATOM   29   N  N   . TYR A 1 4   ? 4.945   -6.603  10.694  1.00 19.82 ? 7   TYR A N   1 
ATOM   30   C  CA  . TYR A 1 4   ? 4.532   -7.785  11.437  1.00 19.56 ? 7   TYR A CA  1 
ATOM   31   C  C   . TYR A 1 4   ? 5.414   -9.021  11.187  1.00 26.10 ? 7   TYR A C   1 
ATOM   32   O  O   . TYR A 1 4   ? 5.116   -10.104 11.708  1.00 26.30 ? 7   TYR A O   1 
ATOM   33   C  CB  . TYR A 1 4   ? 3.036   -8.042  11.221  1.00 17.05 ? 7   TYR A CB  1 
ATOM   34   C  CG  . TYR A 1 4   ? 2.117   -6.949  11.709  1.00 14.74 ? 7   TYR A CG  1 
ATOM   35   C  CD1 . TYR A 1 4   ? 1.712   -6.934  13.041  1.00 16.19 ? 7   TYR A CD1 1 
ATOM   36   C  CD2 . TYR A 1 4   ? 1.664   -5.944  10.866  1.00 14.37 ? 7   TYR A CD2 1 
ATOM   37   C  CE1 . TYR A 1 4   ? 0.866   -5.926  13.490  1.00 13.91 ? 7   TYR A CE1 1 
ATOM   38   C  CE2 . TYR A 1 4   ? 0.765   -4.965  11.281  1.00 15.32 ? 7   TYR A CE2 1 
ATOM   39   C  CZ  . TYR A 1 4   ? 0.349   -4.996  12.606  1.00 16.42 ? 7   TYR A CZ  1 
ATOM   40   O  OH  . TYR A 1 4   ? -0.519  -4.048  13.032  1.00 15.13 ? 7   TYR A OH  1 
ATOM   41   N  N   . GLY A 1 5   ? 6.542   -8.862  10.470  1.00 28.27 ? 8   GLY A N   1 
ATOM   42   C  CA  . GLY A 1 5   ? 7.431   -9.994  10.202  1.00 29.50 ? 8   GLY A CA  1 
ATOM   43   C  C   . GLY A 1 5   ? 8.441   -10.322 11.317  1.00 31.10 ? 8   GLY A C   1 
ATOM   44   O  O   . GLY A 1 5   ? 8.454   -9.709  12.392  1.00 32.54 ? 8   GLY A O   1 
ATOM   45   N  N   . LYS A 1 6   ? 9.352   -11.279 11.030  1.00 35.11 ? 9   LYS A N   1 
ATOM   46   C  CA  . LYS A 1 6   ? 10.336  -11.783 11.990  1.00 33.53 ? 9   LYS A CA  1 
ATOM   47   C  C   . LYS A 1 6   ? 11.324  -10.689 12.389  1.00 33.65 ? 9   LYS A C   1 
ATOM   48   O  O   . LYS A 1 6   ? 11.811  -10.650 13.529  1.00 31.10 ? 9   LYS A O   1 
ATOM   49   C  CB  . LYS A 1 6   ? 11.077  -13.010 11.435  1.00 35.65 ? 9   LYS A CB  1 
ATOM   50   C  CG  . LYS A 1 6   ? 12.208  -13.555 12.302  1.00 34.39 ? 9   LYS A CG  1 
ATOM   51   N  N   . HIS A 1 7   ? 11.609  -9.804  11.431  1.00 30.76 ? 10  HIS A N   1 
ATOM   52   C  CA  . HIS A 1 7   ? 12.683  -8.849  11.632  1.00 29.93 ? 10  HIS A CA  1 
ATOM   53   C  C   . HIS A 1 7   ? 12.150  -7.454  11.929  1.00 25.85 ? 10  HIS A C   1 
ATOM   54   O  O   . HIS A 1 7   ? 12.930  -6.613  12.403  1.00 25.53 ? 10  HIS A O   1 
ATOM   55   C  CB  . HIS A 1 7   ? 13.692  -8.893  10.464  1.00 29.85 ? 10  HIS A CB  1 
ATOM   56   C  CG  . HIS A 1 7   ? 14.367  -10.231 10.359  1.00 33.44 ? 10  HIS A CG  1 
ATOM   57   N  ND1 . HIS A 1 7   ? 15.352  -10.632 11.243  1.00 38.57 ? 10  HIS A ND1 1 
ATOM   58   C  CD2 . HIS A 1 7   ? 14.161  -11.269 9.518   1.00 38.95 ? 10  HIS A CD2 1 
ATOM   59   C  CE1 . HIS A 1 7   ? 15.744  -11.854 10.940  1.00 39.82 ? 10  HIS A CE1 1 
ATOM   60   N  NE2 . HIS A 1 7   ? 15.016  -12.275 9.883   1.00 40.31 ? 10  HIS A NE2 1 
ATOM   61   N  N   . ASN A 1 8   ? 10.832  -7.234  11.759  1.00 24.48 ? 11  ASN A N   1 
ATOM   62   C  CA  . ASN A 1 8   ? 10.346  -5.891  12.041  1.00 21.52 ? 11  ASN A CA  1 
ATOM   63   C  C   . ASN A 1 8   ? 9.007   -5.903  12.786  1.00 21.07 ? 11  ASN A C   1 
ATOM   64   O  O   . ASN A 1 8   ? 8.351   -4.873  12.819  1.00 18.39 ? 11  ASN A O   1 
ATOM   65   C  CB  . ASN A 1 8   ? 10.134  -5.108  10.757  1.00 22.06 ? 11  ASN A CB  1 
ATOM   66   C  CG  . ASN A 1 8   ? 9.064   -5.701  9.862   1.00 25.35 ? 11  ASN A CG  1 
ATOM   67   O  OD1 . ASN A 1 8   ? 8.491   -6.760  10.179  1.00 25.77 ? 11  ASN A OD1 1 
ATOM   68   N  ND2 . ASN A 1 8   ? 8.764   -5.018  8.762   1.00 24.81 ? 11  ASN A ND2 1 
ATOM   69   N  N   . GLY A 1 9   ? 8.636   -7.067  13.320  1.00 18.80 ? 12  GLY A N   1 
ATOM   70   C  CA  . GLY A 1 9   ? 7.337   -7.263  13.964  1.00 18.37 ? 12  GLY A CA  1 
ATOM   71   C  C   . GLY A 1 9   ? 7.263   -6.625  15.345  1.00 18.24 ? 12  GLY A C   1 
ATOM   72   O  O   . GLY A 1 9   ? 8.160   -5.923  15.806  1.00 16.89 ? 12  GLY A O   1 
ATOM   73   N  N   . PRO A 1 10  ? 6.151   -6.832  16.085  1.00 15.27 ? 13  PRO A N   1 
ATOM   74   C  CA  . PRO A 1 10  ? 5.994   -6.196  17.394  1.00 16.26 ? 13  PRO A CA  1 
ATOM   75   C  C   . PRO A 1 10  ? 7.130   -6.270  18.418  1.00 14.91 ? 13  PRO A C   1 
ATOM   76   O  O   . PRO A 1 10  ? 7.300   -5.345  19.209  1.00 16.67 ? 13  PRO A O   1 
ATOM   77   C  CB  . PRO A 1 10  ? 4.722   -6.887  17.961  1.00 16.17 ? 13  PRO A CB  1 
ATOM   78   C  CG  . PRO A 1 10  ? 3.952   -7.290  16.710  1.00 15.27 ? 13  PRO A CG  1 
ATOM   79   C  CD  . PRO A 1 10  ? 4.988   -7.635  15.660  1.00 16.93 ? 13  PRO A CD  1 
ATOM   80   N  N   . GLU A 1 11  ? 7.886   -7.374  18.466  1.00 16.10 ? 14  GLU A N   1 
ATOM   81   C  CA  . GLU A 1 11  ? 8.984   -7.480  19.414  1.00 17.77 ? 14  GLU A CA  1 
ATOM   82   C  C   . GLU A 1 11  ? 10.130  -6.497  19.093  1.00 15.82 ? 14  GLU A C   1 
ATOM   83   O  O   . GLU A 1 11  ? 11.026  -6.349  19.931  1.00 16.42 ? 14  GLU A O   1 
ATOM   84   C  CB  . GLU A 1 11  ? 9.468   -8.941  19.415  1.00 21.08 ? 14  GLU A CB  1 
ATOM   85   C  CG  . GLU A 1 11  ? 10.030  -9.378  18.060  1.00 21.40 ? 14  GLU A CG  1 
ATOM   86   C  CD  . GLU A 1 11  ? 9.163   -9.933  16.919  1.00 32.63 ? 14  GLU A CD  1 
ATOM   87   O  OE1 . GLU A 1 11  ? 7.924   -9.661  16.868  1.00 23.74 ? 14  GLU A OE1 1 
ATOM   88   O  OE2 . GLU A 1 11  ? 9.752   -10.634 16.016  1.00 33.33 ? 14  GLU A OE2 1 
ATOM   89   N  N   . HIS A 1 12  ? 10.123  -5.855  17.912  1.00 15.78 ? 15  HIS A N   1 
ATOM   90   C  CA  . HIS A 1 12  ? 11.152  -4.921  17.452  1.00 14.58 ? 15  HIS A CA  1 
ATOM   91   C  C   . HIS A 1 12  ? 10.721  -3.469  17.667  1.00 16.05 ? 15  HIS A C   1 
ATOM   92   O  O   . HIS A 1 12  ? 11.546  -2.544  17.600  1.00 14.72 ? 15  HIS A O   1 
ATOM   93   C  CB  . HIS A 1 12  ? 11.455  -5.134  15.959  1.00 17.04 ? 15  HIS A CB  1 
ATOM   94   C  CG  . HIS A 1 12  ? 12.128  -6.440  15.725  1.00 19.24 ? 15  HIS A CG  1 
ATOM   95   N  ND1 . HIS A 1 12  ? 13.469  -6.636  15.997  1.00 19.27 ? 15  HIS A ND1 1 
ATOM   96   C  CD2 . HIS A 1 12  ? 11.637  -7.637  15.329  1.00 20.27 ? 15  HIS A CD2 1 
ATOM   97   C  CE1 . HIS A 1 12  ? 13.762  -7.914  15.757  1.00 21.79 ? 15  HIS A CE1 1 
ATOM   98   N  NE2 . HIS A 1 12  ? 12.681  -8.545  15.357  1.00 22.28 ? 15  HIS A NE2 1 
ATOM   99   N  N   . TRP A 1 13  ? 9.407   -3.245  17.872  1.00 12.26 ? 16  TRP A N   1 
ATOM   100  C  CA  . TRP A 1 13  ? 8.899   -1.876  17.826  1.00 12.35 ? 16  TRP A CA  1 
ATOM   101  C  C   . TRP A 1 13  ? 9.505   -0.933  18.881  1.00 12.76 ? 16  TRP A C   1 
ATOM   102  O  O   . TRP A 1 13  ? 9.610   0.262   18.618  1.00 13.61 ? 16  TRP A O   1 
ATOM   103  C  CB  . TRP A 1 13  ? 7.360   -1.924  17.972  1.00 11.40 ? 16  TRP A CB  1 
ATOM   104  C  CG  . TRP A 1 13  ? 6.689   -2.576  16.804  1.00 12.81 ? 16  TRP A CG  1 
ATOM   105  C  CD1 . TRP A 1 13  ? 7.243   -3.006  15.618  1.00 12.63 ? 16  TRP A CD1 1 
ATOM   106  C  CD2 . TRP A 1 13  ? 5.279   -2.869  16.716  1.00 12.56 ? 16  TRP A CD2 1 
ATOM   107  N  NE1 . TRP A 1 13  ? 6.270   -3.536  14.794  1.00 13.87 ? 16  TRP A NE1 1 
ATOM   108  C  CE2 . TRP A 1 13  ? 5.056   -3.450  15.443  1.00 13.09 ? 16  TRP A CE2 1 
ATOM   109  C  CE3 . TRP A 1 13  ? 4.201   -2.652  17.589  1.00 12.35 ? 16  TRP A CE3 1 
ATOM   110  C  CZ2 . TRP A 1 13  ? 3.798   -3.880  15.014  1.00 13.60 ? 16  TRP A CZ2 1 
ATOM   111  C  CZ3 . TRP A 1 13  ? 2.963   -3.085  17.159  1.00 11.87 ? 16  TRP A CZ3 1 
ATOM   112  C  CH2 . TRP A 1 13  ? 2.767   -3.681  15.914  1.00 13.57 ? 16  TRP A CH2 1 
ATOM   113  N  N   . HIS A 1 14  ? 9.910   -1.437  20.045  1.00 13.99 ? 17  HIS A N   1 
ATOM   114  C  CA  . HIS A 1 14  ? 10.398  -0.601  21.120  1.00 15.95 ? 17  HIS A CA  1 
ATOM   115  C  C   . HIS A 1 14  ? 11.675  0.134   20.723  1.00 16.16 ? 17  HIS A C   1 
ATOM   116  O  O   . HIS A 1 14  ? 11.941  1.186   21.295  1.00 16.58 ? 17  HIS A O   1 
ATOM   117  C  CB  . HIS A 1 14  ? 10.618  -1.451  22.372  1.00 16.01 ? 17  HIS A CB  1 
ATOM   118  C  CG  . HIS A 1 14  ? 11.795  -2.351  22.229  1.00 16.94 ? 17  HIS A CG  1 
ATOM   119  N  ND1 . HIS A 1 14  ? 13.024  -2.009  22.744  1.00 18.52 ? 17  HIS A ND1 1 
ATOM   120  C  CD2 . HIS A 1 14  ? 11.957  -3.524  21.590  1.00 16.71 ? 17  HIS A CD2 1 
ATOM   121  C  CE1 . HIS A 1 14  ? 13.901  -2.952  22.451  1.00 17.93 ? 17  HIS A CE1 1 
ATOM   122  N  NE2 . HIS A 1 14  ? 13.287  -3.898  21.768  1.00 16.88 ? 17  HIS A NE2 1 
ATOM   123  N  N   . LYS A 1 15  ? 12.405  -0.401  19.743  1.00 16.06 ? 18  LYS A N   1 
ATOM   124  C  CA  . LYS A 1 15  ? 13.664  0.278   19.408  1.00 16.76 ? 18  LYS A CA  1 
ATOM   125  C  C   . LYS A 1 15  ? 13.381  1.621   18.740  1.00 20.06 ? 18  LYS A C   1 
ATOM   126  O  O   . LYS A 1 15  ? 14.134  2.574   18.960  1.00 23.73 ? 18  LYS A O   1 
ATOM   127  C  CB  . LYS A 1 15  ? 14.488  -0.606  18.475  1.00 16.11 ? 18  LYS A CB  1 
ATOM   128  C  CG  . LYS A 1 15  ? 15.016  -1.850  19.164  1.00 16.55 ? 18  LYS A CG  1 
ATOM   129  C  CD  . LYS A 1 15  ? 15.702  -2.760  18.180  1.00 18.18 ? 18  LYS A CD  1 
ATOM   130  C  CE  . LYS A 1 15  ? 14.771  -3.790  17.577  1.00 18.98 ? 18  LYS A CE  1 
ATOM   131  N  NZ  . LYS A 1 15  ? 15.430  -4.504  16.453  1.00 17.13 ? 18  LYS A NZ  1 
ATOM   132  N  N   . ASP A 1 16  ? 12.325  1.713   17.919  1.00 19.21 ? 19  ASP A N   1 
ATOM   133  C  CA  . ASP A 1 16  ? 11.947  3.015   17.369  1.00 19.29 ? 19  ASP A CA  1 
ATOM   134  C  C   . ASP A 1 16  ? 10.917  3.749   18.227  1.00 20.72 ? 19  ASP A C   1 
ATOM   135  O  O   . ASP A 1 16  ? 10.812  4.966   18.127  1.00 19.84 ? 19  ASP A O   1 
ATOM   136  C  CB  . ASP A 1 16  ? 11.412  2.942   15.947  1.00 23.65 ? 19  ASP A CB  1 
ATOM   137  C  CG  . ASP A 1 16  ? 12.498  2.567   14.967  1.00 28.35 ? 19  ASP A CG  1 
ATOM   138  O  OD1 . ASP A 1 16  ? 13.381  3.398   14.788  1.00 28.87 ? 19  ASP A OD1 1 
ATOM   139  O  OD2 . ASP A 1 16  ? 12.506  1.395   14.515  1.00 31.52 ? 19  ASP A OD2 1 
ATOM   140  N  N   . PHE A 1 17  ? 10.129  3.011   19.020  1.00 16.29 ? 20  PHE A N   1 
ATOM   141  C  CA  . PHE A 1 17  ? 8.979   3.574   19.716  1.00 17.68 ? 20  PHE A CA  1 
ATOM   142  C  C   . PHE A 1 17  ? 9.042   3.080   21.137  1.00 17.30 ? 20  PHE A C   1 
ATOM   143  O  O   . PHE A 1 17  ? 8.432   2.080   21.479  1.00 14.68 ? 20  PHE A O   1 
ATOM   144  C  CB  . PHE A 1 17  ? 7.649   3.182   19.034  1.00 17.04 ? 20  PHE A CB  1 
ATOM   145  C  CG  . PHE A 1 17  ? 7.596   3.664   17.615  1.00 17.65 ? 20  PHE A CG  1 
ATOM   146  C  CD1 . PHE A 1 17  ? 7.191   4.958   17.333  1.00 20.84 ? 20  PHE A CD1 1 
ATOM   147  C  CD2 . PHE A 1 17  ? 8.030   2.846   16.579  1.00 18.66 ? 20  PHE A CD2 1 
ATOM   148  C  CE1 . PHE A 1 17  ? 7.179   5.402   16.021  1.00 19.81 ? 20  PHE A CE1 1 
ATOM   149  C  CE2 . PHE A 1 17  ? 8.047   3.297   15.268  1.00 17.93 ? 20  PHE A CE2 1 
ATOM   150  C  CZ  . PHE A 1 17  ? 7.642   4.591   15.011  1.00 19.04 ? 20  PHE A CZ  1 
ATOM   151  N  N   . PRO A 1 18  ? 9.875   3.713   21.989  1.00 15.23 ? 21  PRO A N   1 
ATOM   152  C  CA  . PRO A 1 18  ? 10.105  3.241   23.348  1.00 16.11 ? 21  PRO A CA  1 
ATOM   153  C  C   . PRO A 1 18  ? 8.879   3.110   24.245  1.00 14.85 ? 21  PRO A C   1 
ATOM   154  O  O   . PRO A 1 18  ? 8.914   2.357   25.226  1.00 17.23 ? 21  PRO A O   1 
ATOM   155  C  CB  . PRO A 1 18  ? 11.118  4.248   23.956  1.00 17.25 ? 21  PRO A CB  1 
ATOM   156  C  CG  . PRO A 1 18  ? 11.757  4.865   22.728  1.00 22.35 ? 21  PRO A CG  1 
ATOM   157  C  CD  . PRO A 1 18  ? 10.747  4.834   21.601  1.00 19.51 ? 21  PRO A CD  1 
ATOM   158  N  N   A ILE A 1 19  ? 7.804   3.832   23.884  0.50 13.67 ? 22  ILE A N   1 
ATOM   159  N  N   B ILE A 1 19  ? 7.796   3.832   23.897  0.50 14.18 ? 22  ILE A N   1 
ATOM   160  C  CA  A ILE A 1 19  ? 6.528   3.734   24.581  0.50 13.11 ? 22  ILE A CA  1 
ATOM   161  C  CA  B ILE A 1 19  ? 6.534   3.708   24.620  0.50 13.96 ? 22  ILE A CA  1 
ATOM   162  C  C   A ILE A 1 19  ? 5.918   2.340   24.417  0.50 12.67 ? 22  ILE A C   1 
ATOM   163  C  C   B ILE A 1 19  ? 5.934   2.313   24.445  0.50 13.22 ? 22  ILE A C   1 
ATOM   164  O  O   A ILE A 1 19  ? 4.997   1.998   25.171  0.50 12.76 ? 22  ILE A O   1 
ATOM   165  O  O   B ILE A 1 19  ? 5.030   1.948   25.208  0.50 13.29 ? 22  ILE A O   1 
ATOM   166  C  CB  A ILE A 1 19  ? 5.580   4.853   24.104  0.50 12.36 ? 22  ILE A CB  1 
ATOM   167  C  CB  B ILE A 1 19  ? 5.532   4.814   24.226  0.50 13.79 ? 22  ILE A CB  1 
ATOM   168  C  CG1 A ILE A 1 19  ? 4.446   5.118   25.097  0.50 12.30 ? 22  ILE A CG1 1 
ATOM   169  C  CG1 B ILE A 1 19  ? 4.469   5.015   25.306  0.50 14.69 ? 22  ILE A CG1 1 
ATOM   170  C  CG2 A ILE A 1 19  ? 5.063   4.510   22.718  0.50 13.43 ? 22  ILE A CG2 1 
ATOM   171  C  CG2 B ILE A 1 19  ? 4.893   4.468   22.892  0.50 14.74 ? 22  ILE A CG2 1 
ATOM   172  C  CD1 A ILE A 1 19  ? 3.543   6.278   24.719  0.50 10.93 ? 22  ILE A CD1 1 
ATOM   173  C  CD1 B ILE A 1 19  ? 5.036   5.452   26.625  0.50 15.01 ? 22  ILE A CD1 1 
ATOM   174  N  N   . ALA A 1 20  ? 6.444   1.532   23.484  1.00 12.18 ? 23  ALA A N   1 
ATOM   175  C  CA  . ALA A 1 20  ? 6.061   0.106   23.384  1.00 13.18 ? 23  ALA A CA  1 
ATOM   176  C  C   . ALA A 1 20  ? 6.165   -0.623  24.725  1.00 14.80 ? 23  ALA A C   1 
ATOM   177  O  O   . ALA A 1 20  ? 5.446   -1.604  24.971  1.00 15.08 ? 23  ALA A O   1 
ATOM   178  C  CB  . ALA A 1 20  ? 6.926   -0.594  22.346  1.00 13.56 ? 23  ALA A CB  1 
ATOM   179  N  N   . LYS A 1 21  ? 7.093   -0.186  25.605  1.00 15.68 ? 24  LYS A N   1 
ATOM   180  C  CA  . LYS A 1 21  ? 7.192   -0.790  26.920  1.00 17.81 ? 24  LYS A CA  1 
ATOM   181  C  C   . LYS A 1 21  ? 6.557   0.089   27.988  1.00 19.12 ? 24  LYS A C   1 
ATOM   182  O  O   . LYS A 1 21  ? 6.923   -0.013  29.168  1.00 22.57 ? 24  LYS A O   1 
ATOM   183  C  CB  . LYS A 1 21  ? 8.656   -1.105  27.253  1.00 19.80 ? 24  LYS A CB  1 
ATOM   184  C  CG  . LYS A 1 21  ? 9.294   -2.099  26.308  1.00 20.81 ? 24  LYS A CG  1 
ATOM   185  C  CD  . LYS A 1 21  ? 10.746  -2.281  26.703  1.00 25.09 ? 24  LYS A CD  1 
ATOM   186  C  CE  . LYS A 1 21  ? 11.489  -3.187  25.743  1.00 25.36 ? 24  LYS A CE  1 
ATOM   187  N  NZ  . LYS A 1 21  ? 11.164  -4.603  26.046  1.00 26.01 ? 24  LYS A NZ  1 
ATOM   188  N  N   . GLY A 1 22  ? 5.562   0.906   27.607  1.00 17.20 ? 25  GLY A N   1 
ATOM   189  C  CA  . GLY A 1 22  ? 4.989   1.887   28.511  1.00 17.63 ? 25  GLY A CA  1 
ATOM   190  C  C   . GLY A 1 22  ? 3.991   1.326   29.516  1.00 15.72 ? 25  GLY A C   1 
ATOM   191  O  O   . GLY A 1 22  ? 3.760   0.119   29.602  1.00 19.06 ? 25  GLY A O   1 
ATOM   192  N  N   . GLU A 1 23  ? 3.334   2.248   30.225  1.00 16.15 ? 26  GLU A N   1 
ATOM   193  C  CA  . GLU A 1 23  ? 2.514   1.900   31.370  1.00 17.93 ? 26  GLU A CA  1 
ATOM   194  C  C   . GLU A 1 23  ? 1.087   1.502   30.990  1.00 16.89 ? 26  GLU A C   1 
ATOM   195  O  O   . GLU A 1 23  ? 0.353   0.943   31.815  1.00 16.14 ? 26  GLU A O   1 
ATOM   196  C  CB  . GLU A 1 23  ? 2.499   3.081   32.364  1.00 24.07 ? 26  GLU A CB  1 
ATOM   197  C  CG  . GLU A 1 23  ? 3.823   3.303   33.084  1.00 31.58 ? 26  GLU A CG  1 
ATOM   198  C  CD  . GLU A 1 23  ? 4.415   2.060   33.750  1.00 37.05 ? 26  GLU A CD  1 
ATOM   199  O  OE1 . GLU A 1 23  ? 3.740   1.479   34.637  1.00 42.09 ? 26  GLU A OE1 1 
ATOM   200  O  OE2 . GLU A 1 23  ? 5.547   1.650   33.364  1.00 40.43 ? 26  GLU A OE2 1 
ATOM   201  N  N   . ARG A 1 24  ? 0.666   1.820   29.763  1.00 13.98 ? 27  ARG A N   1 
ATOM   202  C  CA  . ARG A 1 24  ? -0.722  1.586   29.420  1.00 13.04 ? 27  ARG A CA  1 
ATOM   203  C  C   . ARG A 1 24  ? -0.822  1.145   27.949  1.00 11.88 ? 27  ARG A C   1 
ATOM   204  O  O   . ARG A 1 24  ? -1.537  1.755   27.121  1.00 11.92 ? 27  ARG A O   1 
ATOM   205  C  CB  . ARG A 1 24  ? -1.621  2.780   29.794  1.00 16.58 ? 27  ARG A CB  1 
ATOM   206  C  CG  . ARG A 1 24  ? -1.334  4.090   29.070  1.00 19.95 ? 27  ARG A CG  1 
ATOM   207  C  CD  . ARG A 1 24  ? -2.255  5.285   29.411  1.00 22.54 ? 27  ARG A CD  1 
ATOM   208  N  NE  . ARG A 1 24  ? -3.425  5.194   28.552  1.00 23.01 ? 27  ARG A NE  1 
ATOM   209  C  CZ  . ARG A 1 24  ? -4.374  6.115   28.388  1.00 20.76 ? 27  ARG A CZ  1 
ATOM   210  N  NH1 . ARG A 1 24  ? -4.384  7.270   29.058  1.00 20.14 ? 27  ARG A NH1 1 
ATOM   211  N  NH2 . ARG A 1 24  ? -5.324  5.877   27.533  1.00 18.57 ? 27  ARG A NH2 1 
ATOM   212  N  N   . GLN A 1 25  ? -0.138  0.041   27.631  1.00 10.64 ? 28  GLN A N   1 
ATOM   213  C  CA  . GLN A 1 25  ? -0.102  -0.414  26.243  1.00 9.83  ? 28  GLN A CA  1 
ATOM   214  C  C   . GLN A 1 25  ? -1.215  -1.420  25.986  1.00 9.64  ? 28  GLN A C   1 
ATOM   215  O  O   . GLN A 1 25  ? -1.769  -2.049  26.900  1.00 9.88  ? 28  GLN A O   1 
ATOM   216  C  CB  . GLN A 1 25  ? 1.237   -1.097  25.965  1.00 10.29 ? 28  GLN A CB  1 
ATOM   217  C  CG  . GLN A 1 25  ? 2.357   -0.049  25.907  1.00 10.20 ? 28  GLN A CG  1 
ATOM   218  C  CD  . GLN A 1 25  ? 2.238   0.752   24.616  1.00 10.24 ? 28  GLN A CD  1 
ATOM   219  O  OE1 . GLN A 1 25  ? 2.541   0.236   23.529  1.00 10.43 ? 28  GLN A OE1 1 
ATOM   220  N  NE2 . GLN A 1 25  ? 1.911   2.039   24.729  1.00 10.86 ? 28  GLN A NE2 1 
ATOM   221  N  N   . SER A 1 26  ? -1.613  -1.480  24.705  1.00 9.72  ? 29  SER A N   1 
ATOM   222  C  CA  . SER A 1 26  ? -2.673  -2.349  24.257  1.00 8.93  ? 29  SER A CA  1 
ATOM   223  C  C   . SER A 1 26  ? -2.137  -3.228  23.156  1.00 8.95  ? 29  SER A C   1 
ATOM   224  O  O   . SER A 1 26  ? -1.208  -2.811  22.487  1.00 9.77  ? 29  SER A O   1 
ATOM   225  C  CB  . SER A 1 26  ? -3.774  -1.503  23.657  1.00 8.84  ? 29  SER A CB  1 
ATOM   226  O  OG  . SER A 1 26  ? -4.411  -0.826  24.754  1.00 8.08  ? 29  SER A OG  1 
ATOM   227  N  N   . PRO A 1 27  ? -2.788  -4.360  22.819  1.00 8.47  ? 30  PRO A N   1 
ATOM   228  C  CA  . PRO A 1 27  ? -3.917  -4.887  23.555  1.00 9.32  ? 30  PRO A CA  1 
ATOM   229  C  C   . PRO A 1 27  ? -3.530  -5.567  24.855  1.00 9.09  ? 30  PRO A C   1 
ATOM   230  O  O   . PRO A 1 27  ? -2.337  -5.617  25.202  1.00 9.52  ? 30  PRO A O   1 
ATOM   231  C  CB  . PRO A 1 27  ? -4.409  -5.935  22.519  1.00 8.87  ? 30  PRO A CB  1 
ATOM   232  C  CG  . PRO A 1 27  ? -3.085  -6.484  21.959  1.00 9.70  ? 30  PRO A CG  1 
ATOM   233  C  CD  . PRO A 1 27  ? -2.300  -5.223  21.734  1.00 9.59  ? 30  PRO A CD  1 
ATOM   234  N  N   . VAL A 1 28  ? -4.526  -6.144  25.539  1.00 9.70  ? 31  VAL A N   1 
ATOM   235  C  CA  . VAL A 1 28  ? -4.337  -6.892  26.768  1.00 9.92  ? 31  VAL A CA  1 
ATOM   236  C  C   . VAL A 1 28  ? -5.224  -8.126  26.728  1.00 10.21 ? 31  VAL A C   1 
ATOM   237  O  O   . VAL A 1 28  ? -6.149  -8.235  25.933  1.00 9.99  ? 31  VAL A O   1 
ATOM   238  C  CB  . VAL A 1 28  ? -4.713  -6.026  28.001  1.00 10.71 ? 31  VAL A CB  1 
ATOM   239  C  CG1 . VAL A 1 28  ? -3.804  -4.790  28.098  1.00 11.41 ? 31  VAL A CG1 1 
ATOM   240  C  CG2 . VAL A 1 28  ? -6.196  -5.651  28.029  1.00 11.34 ? 31  VAL A CG2 1 
ATOM   241  N  N   . ASP A 1 29  ? -4.921  -9.085  27.584  1.00 10.18 ? 32  ASP A N   1 
ATOM   242  C  CA  . ASP A 1 29  ? -5.823  -10.183 27.804  1.00 10.58 ? 32  ASP A CA  1 
ATOM   243  C  C   . ASP A 1 29  ? -6.880  -9.716  28.806  1.00 11.07 ? 32  ASP A C   1 
ATOM   244  O  O   . ASP A 1 29  ? -6.576  -9.092  29.816  1.00 13.15 ? 32  ASP A O   1 
ATOM   245  C  CB  . ASP A 1 29  ? -5.012  -11.356 28.366  1.00 11.81 ? 32  ASP A CB  1 
ATOM   246  C  CG  . ASP A 1 29  ? -5.949  -12.520 28.713  1.00 13.76 ? 32  ASP A CG  1 
ATOM   247  O  OD1 . ASP A 1 29  ? -6.685  -12.986 27.823  1.00 13.53 ? 32  ASP A OD1 1 
ATOM   248  O  OD2 . ASP A 1 29  ? -5.997  -12.936 29.954  1.00 16.19 ? 32  ASP A OD2 1 
ATOM   249  N  N   . ILE A 1 30  ? -8.130  -10.004 28.478  1.00 12.11 ? 33  ILE A N   1 
ATOM   250  C  CA  . ILE A 1 30  ? -9.244  -9.681  29.343  1.00 11.41 ? 33  ILE A CA  1 
ATOM   251  C  C   . ILE A 1 30  ? -9.547  -10.939 30.151  1.00 13.65 ? 33  ILE A C   1 
ATOM   252  O  O   . ILE A 1 30  ? -10.095 -11.898 29.616  1.00 13.97 ? 33  ILE A O   1 
ATOM   253  C  CB  . ILE A 1 30  ? -10.463 -9.236  28.525  1.00 12.73 ? 33  ILE A CB  1 
ATOM   254  C  CG1 . ILE A 1 30  ? -10.135 -7.980  27.724  1.00 10.98 ? 33  ILE A CG1 1 
ATOM   255  C  CG2 . ILE A 1 30  ? -11.625 -8.998  29.509  1.00 12.65 ? 33  ILE A CG2 1 
ATOM   256  C  CD1 . ILE A 1 30  ? -11.160 -7.567  26.628  1.00 11.94 ? 33  ILE A CD1 1 
ATOM   257  N  N   A ASP A 1 31  ? -9.187  -10.876 31.434  0.50 14.50 ? 34  ASP A N   1 
ATOM   258  N  N   B ASP A 1 31  ? -9.178  -10.886 31.436  0.50 13.83 ? 34  ASP A N   1 
ATOM   259  C  CA  A ASP A 1 31  ? -9.488  -11.959 32.359  0.50 16.15 ? 34  ASP A CA  1 
ATOM   260  C  CA  B ASP A 1 31  ? -9.487  -11.960 32.375  0.50 14.92 ? 34  ASP A CA  1 
ATOM   261  C  C   A ASP A 1 31  ? -10.899 -11.736 32.891  0.50 16.50 ? 34  ASP A C   1 
ATOM   262  C  C   B ASP A 1 31  ? -10.903 -11.732 32.890  0.50 15.71 ? 34  ASP A C   1 
ATOM   263  O  O   A ASP A 1 31  ? -11.108 -10.811 33.666  0.50 19.02 ? 34  ASP A O   1 
ATOM   264  O  O   B ASP A 1 31  ? -11.122 -10.793 33.645  0.50 18.10 ? 34  ASP A O   1 
ATOM   265  C  CB  A ASP A 1 31  ? -8.445  -11.980 33.477  0.50 17.30 ? 34  ASP A CB  1 
ATOM   266  C  CB  B ASP A 1 31  ? -8.447  -11.982 33.501  0.50 14.79 ? 34  ASP A CB  1 
ATOM   267  C  CG  A ASP A 1 31  ? -8.632  -13.176 34.389  0.50 18.35 ? 34  ASP A CG  1 
ATOM   268  C  CG  B ASP A 1 31  ? -8.746  -13.021 34.573  0.50 14.63 ? 34  ASP A CG  1 
ATOM   269  O  OD1 A ASP A 1 31  ? -8.158  -14.273 34.010  0.50 17.81 ? 34  ASP A OD1 1 
ATOM   270  O  OD1 B ASP A 1 31  ? -9.895  -13.535 34.597  0.50 14.48 ? 34  ASP A OD1 1 
ATOM   271  O  OD2 A ASP A 1 31  ? -9.261  -12.999 35.457  0.50 21.65 ? 34  ASP A OD2 1 
ATOM   272  O  OD2 B ASP A 1 31  ? -7.818  -13.320 35.376  0.50 15.00 ? 34  ASP A OD2 1 
ATOM   273  N  N   . THR A 1 32  ? -11.866 -12.546 32.437  1.00 16.79 ? 35  THR A N   1 
ATOM   274  C  CA  . THR A 1 32  ? -13.278 -12.187 32.592  1.00 16.94 ? 35  THR A CA  1 
ATOM   275  C  C   . THR A 1 32  ? -13.683 -12.323 34.051  1.00 17.92 ? 35  THR A C   1 
ATOM   276  O  O   . THR A 1 32  ? -14.671 -11.729 34.488  1.00 20.67 ? 35  THR A O   1 
ATOM   277  C  CB  . THR A 1 32  ? -14.225 -13.077 31.788  1.00 19.81 ? 35  THR A CB  1 
ATOM   278  O  OG1 . THR A 1 32  ? -13.983 -14.408 32.218  1.00 19.62 ? 35  THR A OG1 1 
ATOM   279  C  CG2 . THR A 1 32  ? -13.993 -12.976 30.301  1.00 16.67 ? 35  THR A CG2 1 
ATOM   280  N  N   . HIS A 1 33  ? -12.869 -13.103 34.774  1.00 19.88 ? 36  HIS A N   1 
ATOM   281  C  CA  . HIS A 1 33  ? -13.176 -13.393 36.166  1.00 20.71 ? 36  HIS A CA  1 
ATOM   282  C  C   . HIS A 1 33  ? -12.771 -12.241 37.067  1.00 22.80 ? 36  HIS A C   1 
ATOM   283  O  O   . HIS A 1 33  ? -13.480 -12.001 38.045  1.00 29.05 ? 36  HIS A O   1 
ATOM   284  C  CB  . HIS A 1 33  ? -12.508 -14.714 36.553  1.00 21.34 ? 36  HIS A CB  1 
ATOM   285  C  CG  . HIS A 1 33  ? -13.187 -15.803 35.823  1.00 24.92 ? 36  HIS A CG  1 
ATOM   286  N  ND1 . HIS A 1 33  ? -12.573 -16.474 34.792  1.00 26.28 ? 36  HIS A ND1 1 
ATOM   287  C  CD2 . HIS A 1 33  ? -14.459 -16.233 35.876  1.00 26.39 ? 36  HIS A CD2 1 
ATOM   288  C  CE1 . HIS A 1 33  ? -13.429 -17.325 34.274  1.00 26.86 ? 36  HIS A CE1 1 
ATOM   289  N  NE2 . HIS A 1 33  ? -14.576 -17.210 34.930  1.00 25.64 ? 36  HIS A NE2 1 
ATOM   290  N  N   . THR A 1 34  ? -11.707 -11.513 36.699  1.00 20.68 ? 37  THR A N   1 
ATOM   291  C  CA  . THR A 1 34  ? -11.176 -10.420 37.495  1.00 21.11 ? 37  THR A CA  1 
ATOM   292  C  C   . THR A 1 34  ? -11.567 -9.029  36.970  1.00 18.90 ? 37  THR A C   1 
ATOM   293  O  O   . THR A 1 34  ? -11.200 -8.022  37.566  1.00 20.49 ? 37  THR A O   1 
ATOM   294  C  CB  . THR A 1 34  ? -9.670  -10.549 37.719  1.00 24.09 ? 37  THR A CB  1 
ATOM   295  O  OG1 . THR A 1 34  ? -9.004  -10.527 36.457  1.00 24.85 ? 37  THR A OG1 1 
ATOM   296  C  CG2 . THR A 1 34  ? -9.289  -11.800 38.475  1.00 21.81 ? 37  THR A CG2 1 
ATOM   297  N  N   . ALA A 1 35  ? -12.314 -8.950  35.858  1.00 18.85 ? 38  ALA A N   1 
ATOM   298  C  CA  . ALA A 1 35  ? -12.838 -7.652  35.439  1.00 17.51 ? 38  ALA A CA  1 
ATOM   299  C  C   . ALA A 1 35  ? -13.848 -7.214  36.506  1.00 19.45 ? 38  ALA A C   1 
ATOM   300  O  O   . ALA A 1 35  ? -14.573 -8.051  37.020  1.00 24.29 ? 38  ALA A O   1 
ATOM   301  C  CB  . ALA A 1 35  ? -13.443 -7.820  34.063  1.00 19.28 ? 38  ALA A CB  1 
ATOM   302  N  N   . LYS A 1 36  ? -13.822 -5.928  36.884  1.00 19.60 ? 39  LYS A N   1 
ATOM   303  C  CA  . LYS A 1 36  ? -14.708 -5.379  37.914  1.00 22.55 ? 39  LYS A CA  1 
ATOM   304  C  C   . LYS A 1 36  ? -16.018 -4.918  37.263  1.00 21.04 ? 39  LYS A C   1 
ATOM   305  O  O   . LYS A 1 36  ? -16.033 -3.981  36.461  1.00 19.22 ? 39  LYS A O   1 
ATOM   306  C  CB  . LYS A 1 36  ? -13.973 -4.201  38.573  1.00 22.80 ? 39  LYS A CB  1 
ATOM   307  C  CG  . LYS A 1 36  ? -14.761 -3.374  39.586  1.00 23.91 ? 39  LYS A CG  1 
ATOM   308  C  CD  . LYS A 1 36  ? -14.956 -4.098  40.916  1.00 25.63 ? 39  LYS A CD  1 
ATOM   309  C  CE  . LYS A 1 36  ? -15.701 -3.256  41.934  1.00 26.45 ? 39  LYS A CE  1 
ATOM   310  N  NZ  . LYS A 1 36  ? -16.323 -4.105  42.986  1.00 30.61 ? 39  LYS A NZ  1 
ATOM   311  N  N   . TYR A 1 37  ? -17.143 -5.507  37.680  1.00 22.04 ? 40  TYR A N   1 
ATOM   312  C  CA  . TYR A 1 37  ? -18.418 -4.924  37.286  1.00 24.55 ? 40  TYR A CA  1 
ATOM   313  C  C   . TYR A 1 37  ? -18.579 -3.545  37.907  1.00 25.75 ? 40  TYR A C   1 
ATOM   314  O  O   . TYR A 1 37  ? -18.459 -3.386  39.132  1.00 23.28 ? 40  TYR A O   1 
ATOM   315  C  CB  . TYR A 1 37  ? -19.610 -5.817  37.662  1.00 24.78 ? 40  TYR A CB  1 
ATOM   316  C  CG  . TYR A 1 37  ? -20.970 -5.177  37.506  1.00 27.99 ? 40  TYR A CG  1 
ATOM   317  C  CD1 . TYR A 1 37  ? -21.472 -4.885  36.250  1.00 28.70 ? 40  TYR A CD1 1 
ATOM   318  C  CD2 . TYR A 1 37  ? -21.782 -4.911  38.605  1.00 31.66 ? 40  TYR A CD2 1 
ATOM   319  C  CE1 . TYR A 1 37  ? -22.729 -4.342  36.077  1.00 29.27 ? 40  TYR A CE1 1 
ATOM   320  C  CE2 . TYR A 1 37  ? -23.039 -4.327  38.450  1.00 32.44 ? 40  TYR A CE2 1 
ATOM   321  C  CZ  . TYR A 1 37  ? -23.517 -4.054  37.176  1.00 34.19 ? 40  TYR A CZ  1 
ATOM   322  O  OH  . TYR A 1 37  ? -24.737 -3.481  36.950  1.00 31.39 ? 40  TYR A OH  1 
ATOM   323  N  N   . ASP A 1 38  ? -18.893 -2.560  37.051  1.00 23.69 ? 41  ASP A N   1 
ATOM   324  C  CA  . ASP A 1 38  ? -19.123 -1.208  37.519  1.00 26.01 ? 41  ASP A CA  1 
ATOM   325  C  C   . ASP A 1 38  ? -20.570 -0.852  37.196  1.00 30.23 ? 41  ASP A C   1 
ATOM   326  O  O   . ASP A 1 38  ? -20.932 -0.679  36.028  1.00 28.74 ? 41  ASP A O   1 
ATOM   327  C  CB  . ASP A 1 38  ? -18.106 -0.210  36.977  1.00 29.10 ? 41  ASP A CB  1 
ATOM   328  C  CG  . ASP A 1 38  ? -18.357 1.179   37.536  1.00 31.61 ? 41  ASP A CG  1 
ATOM   329  O  OD1 . ASP A 1 38  ? -19.359 1.323   38.270  1.00 33.38 ? 41  ASP A OD1 1 
ATOM   330  O  OD2 . ASP A 1 38  ? -17.521 2.076   37.271  1.00 31.98 ? 41  ASP A OD2 1 
ATOM   331  N  N   . PRO A 1 39  ? -21.477 -0.798  38.201  1.00 35.17 ? 42  PRO A N   1 
ATOM   332  C  CA  . PRO A 1 39  ? -22.892 -0.557  37.912  1.00 31.69 ? 42  PRO A CA  1 
ATOM   333  C  C   . PRO A 1 39  ? -23.114 0.896   37.495  1.00 30.86 ? 42  PRO A C   1 
ATOM   334  O  O   . PRO A 1 39  ? -24.151 1.216   36.922  1.00 34.59 ? 42  PRO A O   1 
ATOM   335  C  CB  . PRO A 1 39  ? -23.569 -0.877  39.256  1.00 38.39 ? 42  PRO A CB  1 
ATOM   336  C  CG  . PRO A 1 39  ? -22.507 -0.455  40.264  1.00 34.97 ? 42  PRO A CG  1 
ATOM   337  C  CD  . PRO A 1 39  ? -21.199 -0.919  39.643  1.00 37.31 ? 42  PRO A CD  1 
ATOM   338  N  N   . SER A 1 40  ? -22.131 1.770   37.747  1.00 26.92 ? 43  SER A N   1 
ATOM   339  C  CA  . SER A 1 40  ? -22.253 3.165   37.341  1.00 32.90 ? 43  SER A CA  1 
ATOM   340  C  C   . SER A 1 40  ? -21.869 3.380   35.867  1.00 32.78 ? 43  SER A C   1 
ATOM   341  O  O   . SER A 1 40  ? -21.998 4.494   35.335  1.00 33.35 ? 43  SER A O   1 
ATOM   342  C  CB  . SER A 1 40  ? -21.445 4.057   38.251  1.00 39.40 ? 43  SER A CB  1 
ATOM   343  O  OG  . SER A 1 40  ? -20.071 4.084   37.871  1.00 38.92 ? 43  SER A OG  1 
ATOM   344  N  N   . LEU A 1 41  ? -21.357 2.338   35.190  1.00 29.73 ? 44  LEU A N   1 
ATOM   345  C  CA  . LEU A 1 41  ? -21.061 2.510   33.764  1.00 23.01 ? 44  LEU A CA  1 
ATOM   346  C  C   . LEU A 1 41  ? -22.372 2.662   32.991  1.00 25.99 ? 44  LEU A C   1 
ATOM   347  O  O   . LEU A 1 41  ? -23.287 1.866   33.161  1.00 27.81 ? 44  LEU A O   1 
ATOM   348  C  CB  . LEU A 1 41  ? -20.284 1.297   33.242  1.00 20.94 ? 44  LEU A CB  1 
ATOM   349  C  CG  . LEU A 1 41  ? -18.771 1.304   33.463  1.00 19.30 ? 44  LEU A CG  1 
ATOM   350  C  CD1 . LEU A 1 41  ? -18.211 -0.077  33.086  1.00 17.58 ? 44  LEU A CD1 1 
ATOM   351  C  CD2 . LEU A 1 41  ? -18.098 2.426   32.681  1.00 18.64 ? 44  LEU A CD2 1 
ATOM   352  N  N   . LYS A 1 42  ? -22.416 3.614   32.055  1.00 25.34 ? 45  LYS A N   1 
ATOM   353  C  CA  . LYS A 1 42  ? -23.637 3.851   31.292  1.00 26.64 ? 45  LYS A CA  1 
ATOM   354  C  C   . LYS A 1 42  ? -23.666 2.913   30.091  1.00 25.61 ? 45  LYS A C   1 
ATOM   355  O  O   . LYS A 1 42  ? -22.608 2.436   29.653  1.00 23.38 ? 45  LYS A O   1 
ATOM   356  C  CB  . LYS A 1 42  ? -23.661 5.279   30.754  1.00 26.81 ? 45  LYS A CB  1 
ATOM   357  C  CG  . LYS A 1 42  ? -23.601 6.377   31.812  1.00 33.57 ? 45  LYS A CG  1 
ATOM   358  C  CD  . LYS A 1 42  ? -23.828 7.774   31.246  1.00 38.81 ? 45  LYS A CD  1 
ATOM   359  N  N   . PRO A 1 43  ? -24.861 2.627   29.512  1.00 24.42 ? 46  PRO A N   1 
ATOM   360  C  CA  . PRO A 1 43  ? -24.947 1.939   28.221  1.00 21.99 ? 46  PRO A CA  1 
ATOM   361  C  C   . PRO A 1 43  ? -24.159 2.759   27.202  1.00 19.37 ? 46  PRO A C   1 
ATOM   362  O  O   . PRO A 1 43  ? -24.105 3.991   27.302  1.00 17.78 ? 46  PRO A O   1 
ATOM   363  C  CB  . PRO A 1 43  ? -26.424 2.090   27.829  1.00 24.32 ? 46  PRO A CB  1 
ATOM   364  C  CG  . PRO A 1 43  ? -27.137 2.174   29.154  1.00 26.43 ? 46  PRO A CG  1 
ATOM   365  C  CD  . PRO A 1 43  ? -26.190 2.930   30.081  1.00 25.64 ? 46  PRO A CD  1 
ATOM   366  N  N   . LEU A 1 44  ? -23.557 2.054   26.234  1.00 19.52 ? 47  LEU A N   1 
ATOM   367  C  CA  . LEU A 1 44  ? -22.855 2.712   25.156  1.00 20.12 ? 47  LEU A CA  1 
ATOM   368  C  C   . LEU A 1 44  ? -23.885 3.356   24.228  1.00 22.06 ? 47  LEU A C   1 
ATOM   369  O  O   . LEU A 1 44  ? -24.968 2.789   24.022  1.00 21.61 ? 47  LEU A O   1 
ATOM   370  C  CB  . LEU A 1 44  ? -22.061 1.603   24.463  1.00 22.17 ? 47  LEU A CB  1 
ATOM   371  C  CG  . LEU A 1 44  ? -20.922 1.993   23.553  1.00 27.13 ? 47  LEU A CG  1 
ATOM   372  C  CD1 . LEU A 1 44  ? -19.936 2.891   24.292  1.00 24.37 ? 47  LEU A CD1 1 
ATOM   373  C  CD2 . LEU A 1 44  ? -20.240 0.704   23.089  1.00 23.77 ? 47  LEU A CD2 1 
ATOM   374  N  N   . SER A 1 45  ? -23.580 4.565   23.736  1.00 18.74 ? 48  SER A N   1 
ATOM   375  C  CA  . SER A 1 45  ? -24.378 5.242   22.725  1.00 20.71 ? 48  SER A CA  1 
ATOM   376  C  C   . SER A 1 45  ? -23.622 5.252   21.399  1.00 19.69 ? 48  SER A C   1 
ATOM   377  O  O   . SER A 1 45  ? -22.730 6.054   21.198  1.00 18.69 ? 48  SER A O   1 
ATOM   378  C  CB  . SER A 1 45  ? -24.759 6.646   23.182  1.00 21.16 ? 48  SER A CB  1 
ATOM   379  O  OG  . SER A 1 45  ? -25.406 7.382   22.144  1.00 25.38 ? 48  SER A OG  1 
ATOM   380  N  N   . VAL A 1 46  ? -24.019 4.371   20.491  1.00 19.24 ? 49  VAL A N   1 
ATOM   381  C  CA  . VAL A 1 46  ? -23.485 4.324   19.144  1.00 20.75 ? 49  VAL A CA  1 
ATOM   382  C  C   . VAL A 1 46  ? -24.492 4.990   18.213  1.00 23.06 ? 49  VAL A C   1 
ATOM   383  O  O   . VAL A 1 46  ? -25.565 4.436   17.940  1.00 25.61 ? 49  VAL A O   1 
ATOM   384  C  CB  . VAL A 1 46  ? -23.275 2.858   18.714  1.00 20.77 ? 49  VAL A CB  1 
ATOM   385  C  CG1 . VAL A 1 46  ? -22.770 2.741   17.272  1.00 24.14 ? 49  VAL A CG1 1 
ATOM   386  C  CG2 . VAL A 1 46  ? -22.421 2.072   19.683  1.00 22.41 ? 49  VAL A CG2 1 
ATOM   387  N  N   . SER A 1 47  ? -24.148 6.181   17.718  1.00 18.47 ? 50  SER A N   1 
ATOM   388  C  CA  . SER A 1 47  ? -25.047 6.911   16.841  1.00 21.46 ? 50  SER A CA  1 
ATOM   389  C  C   . SER A 1 47  ? -24.450 6.993   15.451  1.00 21.65 ? 50  SER A C   1 
ATOM   390  O  O   . SER A 1 47  ? -23.810 7.970   15.159  1.00 20.75 ? 50  SER A O   1 
ATOM   391  C  CB  . SER A 1 47  ? -25.368 8.304   17.331  1.00 24.14 ? 50  SER A CB  1 
ATOM   392  O  OG  . SER A 1 47  ? -25.886 8.228   18.635  1.00 32.79 ? 50  SER A OG  1 
ATOM   393  N  N   . TYR A 1 48  ? -24.751 6.002   14.608  1.00 20.71 ? 51  TYR A N   1 
ATOM   394  C  CA  . TYR A 1 48  ? -24.149 5.836   13.291  1.00 20.27 ? 51  TYR A CA  1 
ATOM   395  C  C   . TYR A 1 48  ? -25.136 6.108   12.143  1.00 22.92 ? 51  TYR A C   1 
ATOM   396  O  O   . TYR A 1 48  ? -24.757 5.989   10.973  1.00 21.54 ? 51  TYR A O   1 
ATOM   397  C  CB  . TYR A 1 48  ? -23.523 4.443   13.172  1.00 17.68 ? 51  TYR A CB  1 
ATOM   398  C  CG  . TYR A 1 48  ? -22.243 4.155   13.937  1.00 18.98 ? 51  TYR A CG  1 
ATOM   399  C  CD1 . TYR A 1 48  ? -21.508 5.138   14.585  1.00 17.42 ? 51  TYR A CD1 1 
ATOM   400  C  CD2 . TYR A 1 48  ? -21.731 2.867   13.944  1.00 16.42 ? 51  TYR A CD2 1 
ATOM   401  C  CE1 . TYR A 1 48  ? -20.333 4.812   15.259  1.00 16.28 ? 51  TYR A CE1 1 
ATOM   402  C  CE2 . TYR A 1 48  ? -20.549 2.530   14.587  1.00 17.56 ? 51  TYR A CE2 1 
ATOM   403  C  CZ  . TYR A 1 48  ? -19.823 3.528   15.235  1.00 16.00 ? 51  TYR A CZ  1 
ATOM   404  O  OH  . TYR A 1 48  ? -18.659 3.184   15.879  1.00 14.82 ? 51  TYR A OH  1 
ATOM   405  N  N   . ASP A 1 49  ? -26.352 6.598   12.457  1.00 26.39 ? 52  ASP A N   1 
ATOM   406  C  CA  . ASP A 1 49  ? -27.353 6.897   11.429  1.00 30.53 ? 52  ASP A CA  1 
ATOM   407  C  C   . ASP A 1 49  ? -26.874 7.825   10.295  1.00 29.85 ? 52  ASP A C   1 
ATOM   408  O  O   . ASP A 1 49  ? -27.253 7.625   9.143   1.00 31.06 ? 52  ASP A O   1 
ATOM   409  C  CB  . ASP A 1 49  ? -28.697 7.308   12.041  1.00 36.30 ? 52  ASP A CB  1 
ATOM   410  C  CG  . ASP A 1 49  ? -28.576 8.198   13.274  1.00 42.56 ? 52  ASP A CG  1 
ATOM   411  O  OD1 . ASP A 1 49  ? -27.959 7.750   14.293  1.00 45.56 ? 52  ASP A OD1 1 
ATOM   412  O  OD2 . ASP A 1 49  ? -29.101 9.339   13.220  1.00 50.21 ? 52  ASP A OD2 1 
ATOM   413  N  N   . GLN A 1 50  ? -26.031 8.830   10.550  1.00 29.60 ? 53  GLN A N   1 
ATOM   414  C  CA  . GLN A 1 50  ? -25.694 9.739   9.458   1.00 28.46 ? 53  GLN A CA  1 
ATOM   415  C  C   . GLN A 1 50  ? -24.287 9.516   8.902   1.00 22.64 ? 53  GLN A C   1 
ATOM   416  O  O   . GLN A 1 50  ? -23.704 10.429  8.336   1.00 22.60 ? 53  GLN A O   1 
ATOM   417  C  CB  . GLN A 1 50  ? -25.819 11.199  9.897   1.00 34.33 ? 53  GLN A CB  1 
ATOM   418  C  CG  . GLN A 1 50  ? -27.257 11.668  10.072  1.00 40.40 ? 53  GLN A CG  1 
ATOM   419  C  CD  . GLN A 1 50  ? -28.005 11.517  8.769   1.00 43.79 ? 53  GLN A CD  1 
ATOM   420  O  OE1 . GLN A 1 50  ? -27.566 11.991  7.710   1.00 41.09 ? 53  GLN A OE1 1 
ATOM   421  N  NE2 . GLN A 1 50  ? -29.116 10.794  8.835   1.00 37.84 ? 53  GLN A NE2 1 
ATOM   422  N  N   . ALA A 1 51  ? -23.714 8.322   9.118   1.00 21.61 ? 54  ALA A N   1 
ATOM   423  C  CA  . ALA A 1 51  ? -22.348 8.027   8.742   1.00 18.34 ? 54  ALA A CA  1 
ATOM   424  C  C   . ALA A 1 51  ? -22.128 8.266   7.249   1.00 20.00 ? 54  ALA A C   1 
ATOM   425  O  O   . ALA A 1 51  ? -22.960 7.907   6.397   1.00 19.64 ? 54  ALA A O   1 
ATOM   426  C  CB  . ALA A 1 51  ? -22.026 6.585   9.132   1.00 19.32 ? 54  ALA A CB  1 
ATOM   427  N  N   . THR A 1 52  ? -21.003 8.874   6.920   1.00 14.92 ? 55  THR A N   1 
ATOM   428  C  CA  . THR A 1 52  ? -20.608 9.022   5.524   1.00 15.08 ? 55  THR A CA  1 
ATOM   429  C  C   . THR A 1 52  ? -19.270 8.354   5.277   1.00 15.00 ? 55  THR A C   1 
ATOM   430  O  O   . THR A 1 52  ? -18.227 8.941   5.500   1.00 15.52 ? 55  THR A O   1 
ATOM   431  C  CB  . THR A 1 52  ? -20.467 10.495  5.119   1.00 15.86 ? 55  THR A CB  1 
ATOM   432  O  OG1 . THR A 1 52  ? -21.737 11.111  5.255   1.00 22.04 ? 55  THR A OG1 1 
ATOM   433  C  CG2 . THR A 1 52  ? -20.021 10.627  3.681   1.00 19.17 ? 55  THR A CG2 1 
ATOM   434  N  N   . SER A 1 53  ? -19.275 7.110   4.772   1.00 15.51 ? 56  SER A N   1 
ATOM   435  C  CA  . SER A 1 53  ? -18.033 6.489   4.384   1.00 15.84 ? 56  SER A CA  1 
ATOM   436  C  C   . SER A 1 53  ? -17.571 7.132   3.080   1.00 17.35 ? 56  SER A C   1 
ATOM   437  O  O   . SER A 1 53  ? -18.391 7.605   2.276   1.00 18.94 ? 56  SER A O   1 
ATOM   438  C  CB  . SER A 1 53  ? -18.197 4.977   4.205   1.00 16.54 ? 56  SER A CB  1 
ATOM   439  O  OG  . SER A 1 53  ? -19.195 4.683   3.200   1.00 20.06 ? 56  SER A OG  1 
ATOM   440  N  N   . LEU A 1 54  ? -16.257 7.190   2.911   1.00 15.71 ? 57  LEU A N   1 
ATOM   441  C  CA  . LEU A 1 54  ? -15.670 7.865   1.758   1.00 18.58 ? 57  LEU A CA  1 
ATOM   442  C  C   . LEU A 1 54  ? -14.901 6.891   0.873   1.00 18.31 ? 57  LEU A C   1 
ATOM   443  O  O   . LEU A 1 54  ? -14.972 6.938   -0.364  1.00 19.25 ? 57  LEU A O   1 
ATOM   444  C  CB  . LEU A 1 54  ? -14.702 8.937   2.281   1.00 19.80 ? 57  LEU A CB  1 
ATOM   445  C  CG  . LEU A 1 54  ? -15.400 10.127  2.935   1.00 23.27 ? 57  LEU A CG  1 
ATOM   446  C  CD1 . LEU A 1 54  ? -14.367 11.133  3.440   1.00 25.06 ? 57  LEU A CD1 1 
ATOM   447  C  CD2 . LEU A 1 54  ? -16.433 10.758  2.005   1.00 25.72 ? 57  LEU A CD2 1 
ATOM   448  N  N   . ARG A 1 55  ? -14.047 6.075   1.493   1.00 17.95 ? 58  ARG A N   1 
ATOM   449  C  CA  . ARG A 1 55  ? -12.990 5.420   0.749   1.00 19.35 ? 58  ARG A CA  1 
ATOM   450  C  C   . ARG A 1 55  ? -12.522 4.223   1.558   1.00 18.20 ? 58  ARG A C   1 
ATOM   451  O  O   . ARG A 1 55  ? -12.610 4.239   2.790   1.00 16.83 ? 58  ARG A O   1 
ATOM   452  C  CB  . ARG A 1 55  ? -11.785 6.363   0.674   1.00 23.51 ? 58  ARG A CB  1 
ATOM   453  C  CG  . ARG A 1 55  ? -10.890 6.159   -0.531  1.00 30.30 ? 58  ARG A CG  1 
ATOM   454  C  CD  . ARG A 1 55  ? -10.029 7.402   -0.546  1.00 32.91 ? 58  ARG A CD  1 
ATOM   455  N  NE  . ARG A 1 55  ? -9.213  7.409   0.661   1.00 31.99 ? 58  ARG A NE  1 
ATOM   456  C  CZ  . ARG A 1 55  ? -7.893  7.580   0.662   1.00 30.97 ? 58  ARG A CZ  1 
ATOM   457  N  NH1 . ARG A 1 55  ? -7.261  7.753   -0.484  1.00 28.94 ? 58  ARG A NH1 1 
ATOM   458  N  NH2 . ARG A 1 55  ? -7.221  7.592   1.797   1.00 27.74 ? 58  ARG A NH2 1 
ATOM   459  N  N   . ILE A 1 56  ? -11.954 3.260   0.846   1.00 15.90 ? 59  ILE A N   1 
ATOM   460  C  CA  . ILE A 1 56  ? -11.284 2.159   1.511   1.00 16.64 ? 59  ILE A CA  1 
ATOM   461  C  C   . ILE A 1 56  ? -9.856  2.118   0.989   1.00 18.26 ? 59  ILE A C   1 
ATOM   462  O  O   . ILE A 1 56  ? -9.639  2.302   -0.217  1.00 17.69 ? 59  ILE A O   1 
ATOM   463  C  CB  . ILE A 1 56  ? -12.055 0.841   1.274   1.00 13.99 ? 59  ILE A CB  1 
ATOM   464  C  CG1 . ILE A 1 56  ? -11.404 -0.312  2.056   1.00 13.82 ? 59  ILE A CG1 1 
ATOM   465  C  CG2 . ILE A 1 56  ? -12.092 0.479   -0.225  1.00 14.80 ? 59  ILE A CG2 1 
ATOM   466  C  CD1 . ILE A 1 56  ? -12.267 -1.598  2.049   1.00 14.00 ? 59  ILE A CD1 1 
ATOM   467  N  N   . LEU A 1 57  ? -8.881  1.851   1.884   1.00 17.82 ? 60  LEU A N   1 
ATOM   468  C  CA  . LEU A 1 57  ? -7.475  1.999   1.552   1.00 18.71 ? 60  LEU A CA  1 
ATOM   469  C  C   . LEU A 1 57  ? -6.668  0.867   2.177   1.00 18.71 ? 60  LEU A C   1 
ATOM   470  O  O   . LEU A 1 57  ? -6.882  0.494   3.340   1.00 18.30 ? 60  LEU A O   1 
ATOM   471  C  CB  . LEU A 1 57  ? -7.016  3.387   2.043   1.00 20.98 ? 60  LEU A CB  1 
ATOM   472  C  CG  . LEU A 1 57  ? -5.513  3.559   2.238   1.00 23.22 ? 60  LEU A CG  1 
ATOM   473  C  CD1 . LEU A 1 57  ? -4.783  3.654   0.901   1.00 26.87 ? 60  LEU A CD1 1 
ATOM   474  C  CD2 . LEU A 1 57  ? -5.206  4.786   3.084   1.00 23.09 ? 60  LEU A CD2 1 
ATOM   475  N  N   . ASN A 1 58  ? -5.796  0.275   1.357   1.00 15.34 ? 61  ASN A N   1 
ATOM   476  C  CA  . ASN A 1 58  ? -4.740  -0.608  1.816   1.00 16.10 ? 61  ASN A CA  1 
ATOM   477  C  C   . ASN A 1 58  ? -3.524  0.232   2.172   1.00 19.61 ? 61  ASN A C   1 
ATOM   478  O  O   . ASN A 1 58  ? -2.909  0.799   1.275   1.00 18.68 ? 61  ASN A O   1 
ATOM   479  C  CB  . ASN A 1 58  ? -4.413  -1.693  0.786   1.00 16.58 ? 61  ASN A CB  1 
ATOM   480  C  CG  . ASN A 1 58  ? -3.321  -2.658  1.182   1.00 16.32 ? 61  ASN A CG  1 
ATOM   481  O  OD1 . ASN A 1 58  ? -2.450  -2.380  2.013   1.00 17.18 ? 61  ASN A OD1 1 
ATOM   482  N  ND2 . ASN A 1 58  ? -3.342  -3.852  0.623   1.00 15.42 ? 61  ASN A ND2 1 
ATOM   483  N  N   . ASN A 1 59  ? -3.151  0.288   3.464   1.00 17.22 ? 62  ASN A N   1 
ATOM   484  C  CA  . ASN A 1 59  ? -2.003  1.104   3.866   1.00 17.46 ? 62  ASN A CA  1 
ATOM   485  C  C   . ASN A 1 59  ? -0.752  0.252   4.078   1.00 18.35 ? 62  ASN A C   1 
ATOM   486  O  O   . ASN A 1 59  ? 0.280   0.746   4.572   1.00 21.62 ? 62  ASN A O   1 
ATOM   487  C  CB  . ASN A 1 59  ? -2.295  1.917   5.131   1.00 18.88 ? 62  ASN A CB  1 
ATOM   488  C  CG  . ASN A 1 59  ? -2.868  1.014   6.215   1.00 19.67 ? 62  ASN A CG  1 
ATOM   489  O  OD1 . ASN A 1 59  ? -2.342  -0.062  6.463   1.00 17.68 ? 62  ASN A OD1 1 
ATOM   490  N  ND2 . ASN A 1 59  ? -4.016  1.398   6.751   1.00 23.45 ? 62  ASN A ND2 1 
ATOM   491  N  N   . GLY A 1 60  ? -0.772  -1.029  3.685   1.00 17.12 ? 63  GLY A N   1 
ATOM   492  C  CA  . GLY A 1 60  ? 0.366   -1.902  3.884   1.00 16.16 ? 63  GLY A CA  1 
ATOM   493  C  C   . GLY A 1 60  ? 0.480   -2.578  5.253   1.00 15.28 ? 63  GLY A C   1 
ATOM   494  O  O   . GLY A 1 60  ? 1.371   -3.410  5.452   1.00 17.21 ? 63  GLY A O   1 
ATOM   495  N  N   . HIS A 1 61  ? -0.441  -2.218  6.165   1.00 15.65 ? 64  HIS A N   1 
ATOM   496  C  CA  . HIS A 1 61  ? -0.523  -2.853  7.483   1.00 15.15 ? 64  HIS A CA  1 
ATOM   497  C  C   . HIS A 1 61  ? -1.901  -3.510  7.663   1.00 13.96 ? 64  HIS A C   1 
ATOM   498  O  O   . HIS A 1 61  ? -1.979  -4.643  8.171   1.00 15.30 ? 64  HIS A O   1 
ATOM   499  C  CB  . HIS A 1 61  ? -0.310  -1.816  8.592   1.00 17.35 ? 64  HIS A CB  1 
ATOM   500  C  CG  . HIS A 1 61  ? 0.974   -1.071  8.431   1.00 18.98 ? 64  HIS A CG  1 
ATOM   501  N  ND1 . HIS A 1 61  ? 2.218   -1.686  8.529   1.00 20.39 ? 64  HIS A ND1 1 
ATOM   502  C  CD2 . HIS A 1 61  ? 1.204   0.237   8.171   1.00 20.48 ? 64  HIS A CD2 1 
ATOM   503  C  CE1 . HIS A 1 61  ? 3.159   -0.783  8.346   1.00 20.53 ? 64  HIS A CE1 1 
ATOM   504  N  NE2 . HIS A 1 61  ? 2.582   0.390   8.147   1.00 20.21 ? 64  HIS A NE2 1 
ATOM   505  N  N   . ALA A 1 62  ? -2.959  -2.789  7.298   1.00 13.66 ? 65  ALA A N   1 
ATOM   506  C  CA  . ALA A 1 62  ? -4.314  -3.341  7.290   1.00 12.91 ? 65  ALA A CA  1 
ATOM   507  C  C   . ALA A 1 62  ? -5.069  -2.637  6.159   1.00 13.37 ? 65  ALA A C   1 
ATOM   508  O  O   . ALA A 1 62  ? -4.431  -1.969  5.329   1.00 15.99 ? 65  ALA A O   1 
ATOM   509  C  CB  . ALA A 1 62  ? -4.973  -3.109  8.636   1.00 13.07 ? 65  ALA A CB  1 
ATOM   510  N  N   . PHE A 1 63  ? -6.414  -2.725  6.112   1.00 12.71 ? 66  PHE A N   1 
ATOM   511  C  CA  . PHE A 1 63  ? -7.135  -1.811  5.241   1.00 13.98 ? 66  PHE A CA  1 
ATOM   512  C  C   . PHE A 1 63  ? -8.046  -0.955  6.096   1.00 14.22 ? 66  PHE A C   1 
ATOM   513  O  O   . PHE A 1 63  ? -8.533  -1.418  7.133   1.00 15.57 ? 66  PHE A O   1 
ATOM   514  C  CB  . PHE A 1 63  ? -7.912  -2.561  4.144   1.00 13.42 ? 66  PHE A CB  1 
ATOM   515  C  CG  . PHE A 1 63  ? -9.004  -3.473  4.668   1.00 14.10 ? 66  PHE A CG  1 
ATOM   516  C  CD1 . PHE A 1 63  ? -10.274 -2.963  4.922   1.00 14.42 ? 66  PHE A CD1 1 
ATOM   517  C  CD2 . PHE A 1 63  ? -8.759  -4.838  4.861   1.00 15.11 ? 66  PHE A CD2 1 
ATOM   518  C  CE1 . PHE A 1 63  ? -11.285 -3.795  5.376   1.00 14.51 ? 66  PHE A CE1 1 
ATOM   519  C  CE2 . PHE A 1 63  ? -9.771  -5.663  5.362   1.00 15.41 ? 66  PHE A CE2 1 
ATOM   520  C  CZ  . PHE A 1 63  ? -11.027 -5.137  5.630   1.00 13.83 ? 66  PHE A CZ  1 
ATOM   521  N  N   . ASN A 1 64  ? -8.226  0.305   5.712   1.00 15.29 ? 67  ASN A N   1 
ATOM   522  C  CA  . ASN A 1 64  ? -9.000  1.202   6.534   1.00 16.20 ? 67  ASN A CA  1 
ATOM   523  C  C   . ASN A 1 64  ? -10.225 1.622   5.725   1.00 15.43 ? 67  ASN A C   1 
ATOM   524  O  O   . ASN A 1 64  ? -10.047 1.946   4.556   1.00 17.24 ? 67  ASN A O   1 
ATOM   525  C  CB  . ASN A 1 64  ? -8.264  2.512   6.805   1.00 18.27 ? 67  ASN A CB  1 
ATOM   526  C  CG  . ASN A 1 64  ? -7.096  2.390   7.759   1.00 23.17 ? 67  ASN A CG  1 
ATOM   527  O  OD1 . ASN A 1 64  ? -6.864  1.328   8.326   1.00 21.05 ? 67  ASN A OD1 1 
ATOM   528  N  ND2 . ASN A 1 64  ? -6.291  3.449   7.843   1.00 28.46 ? 67  ASN A ND2 1 
ATOM   529  N  N   . VAL A 1 65  ? -11.404 1.694   6.343   1.00 12.89 ? 68  VAL A N   1 
ATOM   530  C  CA  . VAL A 1 65  ? -12.545 2.348   5.698   1.00 13.18 ? 68  VAL A CA  1 
ATOM   531  C  C   . VAL A 1 65  ? -12.617 3.716   6.369   1.00 16.34 ? 68  VAL A C   1 
ATOM   532  O  O   . VAL A 1 65  ? -12.826 3.770   7.578   1.00 14.83 ? 68  VAL A O   1 
ATOM   533  C  CB  . VAL A 1 65  ? -13.850 1.536   5.870   1.00 13.43 ? 68  VAL A CB  1 
ATOM   534  C  CG1 . VAL A 1 65  ? -15.068 2.354   5.414   1.00 14.30 ? 68  VAL A CG1 1 
ATOM   535  C  CG2 . VAL A 1 65  ? -13.728 0.256   5.057   1.00 14.21 ? 68  VAL A CG2 1 
ATOM   536  N  N   . GLU A 1 66  ? -12.515 4.805   5.592   1.00 15.64 ? 69  GLU A N   1 
ATOM   537  C  CA  . GLU A 1 66  ? -12.490 6.145   6.187   1.00 16.03 ? 69  GLU A CA  1 
ATOM   538  C  C   . GLU A 1 66  ? -13.827 6.860   6.033   1.00 16.31 ? 69  GLU A C   1 
ATOM   539  O  O   . GLU A 1 66  ? -14.574 6.606   5.073   1.00 17.94 ? 69  GLU A O   1 
ATOM   540  C  CB  . GLU A 1 66  ? -11.507 6.983   5.401   1.00 19.96 ? 69  GLU A CB  1 
ATOM   541  C  CG  . GLU A 1 66  ? -10.109 6.484   5.552   1.00 24.23 ? 69  GLU A CG  1 
ATOM   542  C  CD  . GLU A 1 66  ? -9.345  6.950   4.326   1.00 34.16 ? 69  GLU A CD  1 
ATOM   543  O  OE1 . GLU A 1 66  ? -10.023 7.445   3.352   1.00 37.99 ? 69  GLU A OE1 1 
ATOM   544  O  OE2 . GLU A 1 66  ? -8.089  6.825   4.329   1.00 40.59 ? 69  GLU A OE2 1 
ATOM   545  N  N   . PHE A 1 67  ? -14.135 7.710   7.015   1.00 13.38 ? 70  PHE A N   1 
ATOM   546  C  CA  . PHE A 1 67  ? -15.422 8.393   7.127   1.00 13.23 ? 70  PHE A CA  1 
ATOM   547  C  C   . PHE A 1 67  ? -15.196 9.900   7.099   1.00 13.28 ? 70  PHE A C   1 
ATOM   548  O  O   . PHE A 1 67  ? -14.101 10.353  7.420   1.00 14.72 ? 70  PHE A O   1 
ATOM   549  C  CB  . PHE A 1 67  ? -16.192 7.998   8.381   1.00 13.43 ? 70  PHE A CB  1 
ATOM   550  C  CG  . PHE A 1 67  ? -16.765 6.601   8.301   1.00 12.87 ? 70  PHE A CG  1 
ATOM   551  C  CD1 . PHE A 1 67  ? -15.957 5.487   8.520   1.00 14.33 ? 70  PHE A CD1 1 
ATOM   552  C  CD2 . PHE A 1 67  ? -18.099 6.422   8.025   1.00 13.56 ? 70  PHE A CD2 1 
ATOM   553  C  CE1 . PHE A 1 67  ? -16.489 4.202   8.411   1.00 13.86 ? 70  PHE A CE1 1 
ATOM   554  C  CE2 . PHE A 1 67  ? -18.632 5.153   7.906   1.00 12.52 ? 70  PHE A CE2 1 
ATOM   555  C  CZ  . PHE A 1 67  ? -17.824 4.045   8.097   1.00 14.31 ? 70  PHE A CZ  1 
ATOM   556  N  N   . ASP A 1 68  ? -16.241 10.626  6.709   1.00 13.84 ? 71  ASP A N   1 
ATOM   557  C  CA  . ASP A 1 68  ? -16.207 12.076  6.859   1.00 14.03 ? 71  ASP A CA  1 
ATOM   558  C  C   . ASP A 1 68  ? -16.414 12.402  8.328   1.00 13.63 ? 71  ASP A C   1 
ATOM   559  O  O   . ASP A 1 68  ? -17.461 12.145  8.887   1.00 16.35 ? 71  ASP A O   1 
ATOM   560  C  CB  . ASP A 1 68  ? -17.289 12.687  5.971   1.00 14.70 ? 71  ASP A CB  1 
ATOM   561  C  CG  . ASP A 1 68  ? -17.533 14.166  6.269   1.00 17.77 ? 71  ASP A CG  1 
ATOM   562  O  OD1 . ASP A 1 68  ? -16.647 14.798  6.867   1.00 15.89 ? 71  ASP A OD1 1 
ATOM   563  O  OD2 . ASP A 1 68  ? -18.666 14.652  6.013   1.00 18.74 ? 71  ASP A OD2 1 
ATOM   564  N  N   . ASP A 1 69  ? -15.357 12.925  8.965   1.00 15.07 ? 72  ASP A N   1 
ATOM   565  C  CA  . ASP A 1 69  ? -15.407 13.265  10.374  1.00 14.58 ? 72  ASP A CA  1 
ATOM   566  C  C   . ASP A 1 69  ? -15.342 14.791  10.554  1.00 16.26 ? 72  ASP A C   1 
ATOM   567  O  O   . ASP A 1 69  ? -14.894 15.268  11.589  1.00 14.75 ? 72  ASP A O   1 
ATOM   568  C  CB  . ASP A 1 69  ? -14.215 12.635  11.116  1.00 16.09 ? 72  ASP A CB  1 
ATOM   569  C  CG  . ASP A 1 69  ? -12.846 13.106  10.648  1.00 18.36 ? 72  ASP A CG  1 
ATOM   570  O  OD1 . ASP A 1 69  ? -12.730 13.770  9.590   1.00 17.78 ? 72  ASP A OD1 1 
ATOM   571  O  OD2 . ASP A 1 69  ? -11.873 12.832  11.357  1.00 17.76 ? 72  ASP A OD2 1 
ATOM   572  N  N   . SER A 1 70  ? -15.867 15.548  9.587   1.00 15.55 ? 73  SER A N   1 
ATOM   573  C  CA  . SER A 1 70  ? -15.814 17.012  9.649   1.00 17.40 ? 73  SER A CA  1 
ATOM   574  C  C   . SER A 1 70  ? -17.087 17.582  10.275  1.00 19.40 ? 73  SER A C   1 
ATOM   575  O  O   . SER A 1 70  ? -17.242 18.802  10.413  1.00 16.63 ? 73  SER A O   1 
ATOM   576  C  CB  . SER A 1 70  ? -15.533 17.553  8.277   1.00 17.53 ? 73  SER A CB  1 
ATOM   577  O  OG  . SER A 1 70  ? -16.722 17.443  7.469   1.00 16.13 ? 73  SER A OG  1 
ATOM   578  N  N   . GLN A 1 71  ? -18.038 16.704  10.636  1.00 16.53 ? 74  GLN A N   1 
ATOM   579  C  CA  . GLN A 1 71  ? -19.212 17.065  11.421  1.00 17.71 ? 74  GLN A CA  1 
ATOM   580  C  C   . GLN A 1 71  ? -19.572 15.833  12.223  1.00 17.83 ? 74  GLN A C   1 
ATOM   581  O  O   . GLN A 1 71  ? -19.031 14.774  11.906  1.00 19.94 ? 74  GLN A O   1 
ATOM   582  C  CB  . GLN A 1 71  ? -20.447 17.356  10.548  1.00 20.92 ? 74  GLN A CB  1 
ATOM   583  C  CG  . GLN A 1 71  ? -20.236 18.373  9.454   1.00 23.42 ? 74  GLN A CG  1 
ATOM   584  C  CD  . GLN A 1 71  ? -21.558 18.534  8.734   1.00 28.22 ? 74  GLN A CD  1 
ATOM   585  O  OE1 . GLN A 1 71  ? -22.497 19.141  9.248   1.00 32.49 ? 74  GLN A OE1 1 
ATOM   586  N  NE2 . GLN A 1 71  ? -21.650 17.985  7.539   1.00 26.37 ? 74  GLN A NE2 1 
ATOM   587  N  N   . ASP A 1 72  ? -20.488 15.996  13.195  1.00 19.98 ? 75  ASP A N   1 
ATOM   588  C  CA  . ASP A 1 72  ? -20.894 14.933  14.115  1.00 21.66 ? 75  ASP A CA  1 
ATOM   589  C  C   . ASP A 1 72  ? -21.886 13.977  13.433  1.00 25.07 ? 75  ASP A C   1 
ATOM   590  O  O   . ASP A 1 72  ? -23.068 13.951  13.774  1.00 31.86 ? 75  ASP A O   1 
ATOM   591  C  CB  . ASP A 1 72  ? -21.554 15.496  15.375  1.00 24.65 ? 75  ASP A CB  1 
ATOM   592  C  CG  . ASP A 1 72  ? -20.585 16.100  16.381  1.00 30.66 ? 75  ASP A CG  1 
ATOM   593  O  OD1 . ASP A 1 72  ? -19.375 15.852  16.276  1.00 33.29 ? 75  ASP A OD1 1 
ATOM   594  O  OD2 . ASP A 1 72  ? -21.061 16.814  17.277  1.00 36.96 ? 75  ASP A OD2 1 
ATOM   595  N  N   . LYS A 1 73  ? -21.414 13.144  12.522  1.00 21.29 ? 76  LYS A N   1 
ATOM   596  C  CA  . LYS A 1 73  ? -22.335 12.347  11.721  1.00 20.57 ? 76  LYS A CA  1 
ATOM   597  C  C   . LYS A 1 73  ? -22.469 10.919  12.260  1.00 22.67 ? 76  LYS A C   1 
ATOM   598  O  O   . LYS A 1 73  ? -23.502 10.275  12.103  1.00 26.53 ? 76  LYS A O   1 
ATOM   599  C  CB  . LYS A 1 73  ? -21.716 12.231  10.340  1.00 21.94 ? 76  LYS A CB  1 
ATOM   600  C  CG  . LYS A 1 73  ? -21.987 13.457  9.487   1.00 21.49 ? 76  LYS A CG  1 
ATOM   601  C  CD  . LYS A 1 73  ? -21.345 13.275  8.156   1.00 22.08 ? 76  LYS A CD  1 
ATOM   602  C  CE  . LYS A 1 73  ? -21.904 14.280  7.168   1.00 24.38 ? 76  LYS A CE  1 
ATOM   603  N  NZ  . LYS A 1 73  ? -21.690 13.860  5.780   1.00 26.00 ? 76  LYS A NZ  1 
ATOM   604  N  N   . ALA A 1 74  ? -21.356 10.373  12.732  1.00 20.33 ? 77  ALA A N   1 
ATOM   605  C  CA  . ALA A 1 74  ? -21.273 9.028   13.309  1.00 17.55 ? 77  ALA A CA  1 
ATOM   606  C  C   . ALA A 1 74  ? -20.458 9.194   14.587  1.00 17.26 ? 77  ALA A C   1 
ATOM   607  O  O   . ALA A 1 74  ? -19.285 9.530   14.505  1.00 18.86 ? 77  ALA A O   1 
ATOM   608  C  CB  . ALA A 1 74  ? -20.567 8.125   12.323  1.00 17.64 ? 77  ALA A CB  1 
ATOM   609  N  N   . VAL A 1 75  ? -21.108 9.124   15.748  1.00 17.03 ? 78  VAL A N   1 
ATOM   610  C  CA  . VAL A 1 75  ? -20.417 9.412   17.001  1.00 16.43 ? 78  VAL A CA  1 
ATOM   611  C  C   . VAL A 1 75  ? -20.650 8.301   18.025  1.00 17.49 ? 78  VAL A C   1 
ATOM   612  O  O   . VAL A 1 75  ? -21.623 7.536   17.951  1.00 17.46 ? 78  VAL A O   1 
ATOM   613  C  CB  . VAL A 1 75  ? -20.777 10.791  17.607  1.00 19.60 ? 78  VAL A CB  1 
ATOM   614  C  CG1 . VAL A 1 75  ? -20.593 11.953  16.628  1.00 19.70 ? 78  VAL A CG1 1 
ATOM   615  C  CG2 . VAL A 1 75  ? -22.166 10.768  18.219  1.00 21.02 ? 78  VAL A CG2 1 
ATOM   616  N  N   . LEU A 1 76  ? -19.652 8.185   18.924  1.00 14.01 ? 79  LEU A N   1 
ATOM   617  C  CA  . LEU A 1 76  ? -19.772 7.336   20.076  1.00 15.75 ? 79  LEU A CA  1 
ATOM   618  C  C   . LEU A 1 76  ? -19.772 8.241   21.304  1.00 16.27 ? 79  LEU A C   1 
ATOM   619  O  O   . LEU A 1 76  ? -18.993 9.196   21.380  1.00 16.41 ? 79  LEU A O   1 
ATOM   620  C  CB  . LEU A 1 76  ? -18.584 6.368   20.012  1.00 15.22 ? 79  LEU A CB  1 
ATOM   621  C  CG  . LEU A 1 76  ? -18.500 5.362   21.135  1.00 14.89 ? 79  LEU A CG  1 
ATOM   622  C  CD1 . LEU A 1 76  ? -19.644 4.345   21.045  1.00 16.68 ? 79  LEU A CD1 1 
ATOM   623  C  CD2 . LEU A 1 76  ? -17.150 4.685   21.069  1.00 14.88 ? 79  LEU A CD2 1 
ATOM   624  N  N   . LYS A 1 77  ? -20.691 7.974   22.221  1.00 16.43 ? 80  LYS A N   1 
ATOM   625  C  CA  . LYS A 1 77  ? -20.687 8.637   23.520  1.00 17.94 ? 80  LYS A CA  1 
ATOM   626  C  C   . LYS A 1 77  ? -21.277 7.704   24.567  1.00 16.79 ? 80  LYS A C   1 
ATOM   627  O  O   . LYS A 1 77  ? -21.547 6.545   24.263  1.00 14.99 ? 80  LYS A O   1 
ATOM   628  C  CB  . LYS A 1 77  ? -21.450 9.962   23.455  1.00 24.70 ? 80  LYS A CB  1 
ATOM   629  C  CG  . LYS A 1 77  ? -22.919 9.809   23.069  1.00 31.88 ? 80  LYS A CG  1 
ATOM   630  C  CD  . LYS A 1 77  ? -23.638 11.147  22.815  1.00 37.60 ? 80  LYS A CD  1 
ATOM   631  C  CE  . LYS A 1 77  ? -23.014 11.983  21.715  1.00 44.89 ? 80  LYS A CE  1 
ATOM   632  N  NZ  . LYS A 1 77  ? -23.848 13.155  21.325  1.00 52.39 ? 80  LYS A NZ  1 
ATOM   633  N  N   . GLY A 1 78  ? -21.464 8.218   25.782  1.00 18.32 ? 81  GLY A N   1 
ATOM   634  C  CA  . GLY A 1 78  ? -21.979 7.363   26.837  1.00 19.66 ? 81  GLY A CA  1 
ATOM   635  C  C   . GLY A 1 78  ? -20.959 6.283   27.184  1.00 20.11 ? 81  GLY A C   1 
ATOM   636  O  O   . GLY A 1 78  ? -19.760 6.494   27.013  1.00 18.47 ? 81  GLY A O   1 
ATOM   637  N  N   . GLY A 1 79  ? -21.425 5.137   27.676  1.00 19.98 ? 82  GLY A N   1 
ATOM   638  C  CA  . GLY A 1 79  ? -20.451 4.180   28.165  1.00 21.45 ? 82  GLY A CA  1 
ATOM   639  C  C   . GLY A 1 79  ? -19.577 4.807   29.245  1.00 21.43 ? 82  GLY A C   1 
ATOM   640  O  O   . GLY A 1 79  ? -20.066 5.512   30.139  1.00 22.15 ? 82  GLY A O   1 
ATOM   641  N  N   . PRO A 1 80  ? -18.235 4.629   29.173  1.00 20.01 ? 83  PRO A N   1 
ATOM   642  C  CA  . PRO A 1 80  ? -17.317 5.248   30.124  1.00 18.97 ? 83  PRO A CA  1 
ATOM   643  C  C   . PRO A 1 80  ? -16.869 6.640   29.686  1.00 22.33 ? 83  PRO A C   1 
ATOM   644  O  O   . PRO A 1 80  ? -16.020 7.260   30.341  1.00 26.98 ? 83  PRO A O   1 
ATOM   645  C  CB  . PRO A 1 80  ? -16.097 4.296   30.054  1.00 22.38 ? 83  PRO A CB  1 
ATOM   646  C  CG  . PRO A 1 80  ? -16.086 3.855   28.592  1.00 18.19 ? 83  PRO A CG  1 
ATOM   647  C  CD  . PRO A 1 80  ? -17.541 3.765   28.185  1.00 18.87 ? 83  PRO A CD  1 
ATOM   648  N  N   . LEU A 1 81  ? -17.451 7.150   28.605  1.00 18.99 ? 84  LEU A N   1 
ATOM   649  C  CA  . LEU A 1 81  ? -16.916 8.352   27.983  1.00 18.68 ? 84  LEU A CA  1 
ATOM   650  C  C   . LEU A 1 81  ? -17.665 9.549   28.537  1.00 22.46 ? 84  LEU A C   1 
ATOM   651  O  O   . LEU A 1 81  ? -18.843 9.432   28.822  1.00 21.87 ? 84  LEU A O   1 
ATOM   652  C  CB  . LEU A 1 81  ? -17.061 8.290   26.467  1.00 16.20 ? 84  LEU A CB  1 
ATOM   653  C  CG  . LEU A 1 81  ? -16.474 6.995   25.880  1.00 15.23 ? 84  LEU A CG  1 
ATOM   654  C  CD1 . LEU A 1 81  ? -16.951 6.826   24.450  1.00 15.06 ? 84  LEU A CD1 1 
ATOM   655  C  CD2 . LEU A 1 81  ? -14.926 6.989   25.970  1.00 15.79 ? 84  LEU A CD2 1 
ATOM   656  N  N   . ASP A 1 82  ? -16.925 10.659  28.595  1.00 27.68 ? 85  ASP A N   1 
ATOM   657  C  CA  . ASP A 1 82  ? -17.459 11.937  29.023  1.00 32.53 ? 85  ASP A CA  1 
ATOM   658  C  C   . ASP A 1 82  ? -17.715 12.787  27.795  1.00 33.67 ? 85  ASP A C   1 
ATOM   659  O  O   . ASP A 1 82  ? -18.645 13.578  27.776  1.00 39.16 ? 85  ASP A O   1 
ATOM   660  C  CB  . ASP A 1 82  ? -16.555 12.598  30.061  1.00 34.67 ? 85  ASP A CB  1 
ATOM   661  C  CG  . ASP A 1 82  ? -16.886 12.146  31.474  1.00 42.92 ? 85  ASP A CG  1 
ATOM   662  O  OD1 . ASP A 1 82  ? -17.979 11.554  31.686  1.00 45.58 ? 85  ASP A OD1 1 
ATOM   663  O  OD2 . ASP A 1 82  ? -16.052 12.386  32.357  1.00 54.56 ? 85  ASP A OD2 1 
ATOM   664  N  N   . GLY A 1 83  ? -16.889 12.629  26.765  1.00 33.06 ? 86  GLY A N   1 
ATOM   665  C  CA  . GLY A 1 83  ? -17.109 13.447  25.590  1.00 32.11 ? 86  GLY A CA  1 
ATOM   666  C  C   . GLY A 1 83  ? -17.890 12.741  24.479  1.00 27.18 ? 86  GLY A C   1 
ATOM   667  O  O   . GLY A 1 83  ? -18.440 11.644  24.662  1.00 27.64 ? 86  GLY A O   1 
ATOM   668  N  N   . THR A 1 84  ? -17.956 13.447  23.352  1.00 19.99 ? 87  THR A N   1 
ATOM   669  C  CA  . THR A 1 84  ? -18.513 12.969  22.109  1.00 19.19 ? 87  THR A CA  1 
ATOM   670  C  C   . THR A 1 84  ? -17.318 12.625  21.234  1.00 15.73 ? 87  THR A C   1 
ATOM   671  O  O   . THR A 1 84  ? -16.389 13.422  21.152  1.00 16.27 ? 87  THR A O   1 
ATOM   672  C  CB  . THR A 1 84  ? -19.309 14.067  21.401  1.00 22.50 ? 87  THR A CB  1 
ATOM   673  O  OG1 . THR A 1 84  ? -20.406 14.241  22.305  1.00 27.32 ? 87  THR A OG1 1 
ATOM   674  C  CG2 . THR A 1 84  ? -19.784 13.671  20.014  1.00 21.66 ? 87  THR A CG2 1 
ATOM   675  N  N   . TYR A 1 85  ? -17.315 11.384  20.743  1.00 15.15 ? 88  TYR A N   1 
ATOM   676  C  CA  . TYR A 1 85  ? -16.219 10.988  19.890  1.00 14.36 ? 88  TYR A CA  1 
ATOM   677  C  C   . TYR A 1 85  ? -16.694 10.677  18.473  1.00 14.42 ? 88  TYR A C   1 
ATOM   678  O  O   . TYR A 1 85  ? -17.596 9.855   18.275  1.00 17.85 ? 88  TYR A O   1 
ATOM   679  C  CB  . TYR A 1 85  ? -15.565 9.747   20.520  1.00 13.54 ? 88  TYR A CB  1 
ATOM   680  C  CG  . TYR A 1 85  ? -14.801 9.956   21.809  1.00 12.63 ? 88  TYR A CG  1 
ATOM   681  C  CD1 . TYR A 1 85  ? -15.464 10.278  22.977  1.00 11.62 ? 88  TYR A CD1 1 
ATOM   682  C  CD2 . TYR A 1 85  ? -13.427 9.806   21.868  1.00 13.08 ? 88  TYR A CD2 1 
ATOM   683  C  CE1 . TYR A 1 85  ? -14.805 10.472  24.182  1.00 12.18 ? 88  TYR A CE1 1 
ATOM   684  C  CE2 . TYR A 1 85  ? -12.728 9.981   23.059  1.00 12.07 ? 88  TYR A CE2 1 
ATOM   685  C  CZ  . TYR A 1 85  ? -13.426 10.282  24.225  1.00 12.90 ? 88  TYR A CZ  1 
ATOM   686  O  OH  . TYR A 1 85  ? -12.759 10.466  25.386  1.00 12.79 ? 88  TYR A OH  1 
ATOM   687  N  N   . ARG A 1 86  ? -16.005 11.251  17.485  1.00 13.12 ? 89  ARG A N   1 
ATOM   688  C  CA  . ARG A 1 86  ? -16.391 11.073  16.087  1.00 14.02 ? 89  ARG A CA  1 
ATOM   689  C  C   . ARG A 1 86  ? -15.666 9.915   15.405  1.00 11.32 ? 89  ARG A C   1 
ATOM   690  O  O   . ARG A 1 86  ? -14.446 9.800   15.489  1.00 12.73 ? 89  ARG A O   1 
ATOM   691  C  CB  . ARG A 1 86  ? -15.984 12.257  15.211  1.00 15.82 ? 89  ARG A CB  1 
ATOM   692  C  CG  . ARG A 1 86  ? -17.013 13.357  15.229  1.00 20.08 ? 89  ARG A CG  1 
ATOM   693  C  CD  . ARG A 1 86  ? -16.577 14.412  14.235  1.00 19.72 ? 89  ARG A CD  1 
ATOM   694  N  NE  . ARG A 1 86  ? -17.285 15.532  14.782  1.00 21.89 ? 89  ARG A NE  1 
ATOM   695  C  CZ  . ARG A 1 86  ? -17.044 16.800  14.469  1.00 23.82 ? 89  ARG A CZ  1 
ATOM   696  N  NH1 . ARG A 1 86  ? -16.096 17.098  13.598  1.00 19.43 ? 89  ARG A NH1 1 
ATOM   697  N  NH2 . ARG A 1 86  ? -17.752 17.765  15.028  1.00 25.90 ? 89  ARG A NH2 1 
ATOM   698  N  N   . LEU A 1 87  ? -16.458 9.090   14.676  1.00 10.70 ? 90  LEU A N   1 
ATOM   699  C  CA  . LEU A 1 87  ? -15.877 8.027   13.875  1.00 10.82 ? 90  LEU A CA  1 
ATOM   700  C  C   . LEU A 1 87  ? -15.045 8.596   12.732  1.00 11.79 ? 90  LEU A C   1 
ATOM   701  O  O   . LEU A 1 87  ? -15.531 9.380   11.889  1.00 14.29 ? 90  LEU A O   1 
ATOM   702  C  CB  . LEU A 1 87  ? -16.989 7.121   13.326  1.00 11.57 ? 90  LEU A CB  1 
ATOM   703  C  CG  . LEU A 1 87  ? -16.512 5.984   12.423  1.00 11.63 ? 90  LEU A CG  1 
ATOM   704  C  CD1 . LEU A 1 87  ? -15.686 4.938   13.169  1.00 12.27 ? 90  LEU A CD1 1 
ATOM   705  C  CD2 . LEU A 1 87  ? -17.698 5.306   11.759  1.00 13.25 ? 90  LEU A CD2 1 
ATOM   706  N  N   . ILE A 1 88  ? -13.777 8.188   12.714  1.00 10.85 ? 91  ILE A N   1 
ATOM   707  C  CA  . ILE A 1 88  ? -12.859 8.561   11.632  1.00 11.09 ? 91  ILE A CA  1 
ATOM   708  C  C   . ILE A 1 88  ? -12.628 7.402   10.661  1.00 11.30 ? 91  ILE A C   1 
ATOM   709  O  O   . ILE A 1 88  ? -12.648 7.577   9.444   1.00 12.34 ? 91  ILE A O   1 
ATOM   710  C  CB  . ILE A 1 88  ? -11.559 9.225   12.140  1.00 11.72 ? 91  ILE A CB  1 
ATOM   711  C  CG1 . ILE A 1 88  ? -10.669 9.545   10.938  1.00 12.24 ? 91  ILE A CG1 1 
ATOM   712  C  CG2 . ILE A 1 88  ? -10.829 8.342   13.130  1.00 11.25 ? 91  ILE A CG2 1 
ATOM   713  C  CD1 . ILE A 1 88  ? -9.451  10.391  11.303  1.00 15.72 ? 91  ILE A CD1 1 
ATOM   714  N  N   . GLN A 1 89  ? -12.407 6.180   11.186  1.00 10.99 ? 92  GLN A N   1 
ATOM   715  C  CA  . GLN A 1 89  ? -12.166 5.056   10.293  1.00 11.15 ? 92  GLN A CA  1 
ATOM   716  C  C   . GLN A 1 89  ? -12.384 3.782   11.088  1.00 11.26 ? 92  GLN A C   1 
ATOM   717  O  O   . GLN A 1 89  ? -12.454 3.833   12.307  1.00 10.02 ? 92  GLN A O   1 
ATOM   718  C  CB  . GLN A 1 89  ? -10.738 5.023   9.744   1.00 11.57 ? 92  GLN A CB  1 
ATOM   719  C  CG  . GLN A 1 89  ? -9.696  5.080   10.864  1.00 10.58 ? 92  GLN A CG  1 
ATOM   720  C  CD  . GLN A 1 89  ? -8.945  3.776   10.952  1.00 15.04 ? 92  GLN A CD  1 
ATOM   721  O  OE1 . GLN A 1 89  ? -9.518  2.774   11.295  1.00 13.93 ? 92  GLN A OE1 1 
ATOM   722  N  NE2 . GLN A 1 89  ? -7.719  3.743   10.441  1.00 18.88 ? 92  GLN A NE2 1 
ATOM   723  N  N   . PHE A 1 90  ? -12.587 2.680   10.355  1.00 9.80  ? 93  PHE A N   1 
ATOM   724  C  CA  . PHE A 1 90  ? -12.443 1.371   10.976  1.00 9.08  ? 93  PHE A CA  1 
ATOM   725  C  C   . PHE A 1 90  ? -11.473 0.505   10.187  1.00 10.87 ? 93  PHE A C   1 
ATOM   726  O  O   . PHE A 1 90  ? -11.212 0.709   9.010   1.00 10.84 ? 93  PHE A O   1 
ATOM   727  C  CB  . PHE A 1 90  ? -13.805 0.673   11.153  1.00 9.27  ? 93  PHE A CB  1 
ATOM   728  C  CG  . PHE A 1 90  ? -14.519 0.220   9.904   1.00 10.47 ? 93  PHE A CG  1 
ATOM   729  C  CD1 . PHE A 1 90  ? -14.133 -0.942  9.252   1.00 10.90 ? 93  PHE A CD1 1 
ATOM   730  C  CD2 . PHE A 1 90  ? -15.638 0.928   9.479   1.00 10.59 ? 93  PHE A CD2 1 
ATOM   731  C  CE1 . PHE A 1 90  ? -14.822 -1.420  8.149   1.00 11.32 ? 93  PHE A CE1 1 
ATOM   732  C  CE2 . PHE A 1 90  ? -16.341 0.427   8.383   1.00 10.99 ? 93  PHE A CE2 1 
ATOM   733  C  CZ  . PHE A 1 90  ? -15.890 -0.672  7.697   1.00 11.35 ? 93  PHE A CZ  1 
ATOM   734  N  N   . HIS A 1 91  ? -10.918 -0.498  10.867  1.00 8.61  ? 94  HIS A N   1 
ATOM   735  C  CA  . HIS A 1 91  ? -10.037 -1.451  10.226  1.00 8.35  ? 94  HIS A CA  1 
ATOM   736  C  C   . HIS A 1 91  ? -10.122 -2.738  11.024  1.00 7.39  ? 94  HIS A C   1 
ATOM   737  O  O   . HIS A 1 91  ? -10.736 -2.755  12.093  1.00 7.66  ? 94  HIS A O   1 
ATOM   738  C  CB  . HIS A 1 91  ? -8.562  -0.942  10.197  1.00 8.51  ? 94  HIS A CB  1 
ATOM   739  C  CG  . HIS A 1 91  ? -8.049  -0.703  11.599  1.00 8.48  ? 94  HIS A CG  1 
ATOM   740  N  ND1 . HIS A 1 91  ? -8.259  0.485   12.264  1.00 9.29  ? 94  HIS A ND1 1 
ATOM   741  C  CD2 . HIS A 1 91  ? -7.413  -1.529  12.464  1.00 8.79  ? 94  HIS A CD2 1 
ATOM   742  C  CE1 . HIS A 1 91  ? -7.763  0.389   13.485  1.00 9.32  ? 94  HIS A CE1 1 
ATOM   743  N  NE2 . HIS A 1 91  ? -7.259  -0.863  13.639  1.00 7.44  ? 94  HIS A NE2 1 
ATOM   744  N  N   . PHE A 1 92  ? -9.460  -3.763  10.512  1.00 8.25  ? 95  PHE A N   1 
ATOM   745  C  CA  . PHE A 1 92  ? -9.416  -5.060  11.189  1.00 8.21  ? 95  PHE A CA  1 
ATOM   746  C  C   . PHE A 1 92  ? -7.980  -5.546  11.340  1.00 8.75  ? 95  PHE A C   1 
ATOM   747  O  O   . PHE A 1 92  ? -7.036  -5.071  10.697  1.00 8.28  ? 95  PHE A O   1 
ATOM   748  C  CB  . PHE A 1 92  ? -10.079 -6.132  10.308  1.00 8.50  ? 95  PHE A CB  1 
ATOM   749  C  CG  . PHE A 1 92  ? -11.540 -5.852  9.989   1.00 8.10  ? 95  PHE A CG  1 
ATOM   750  C  CD1 . PHE A 1 92  ? -11.893 -4.969  8.978   1.00 8.73  ? 95  PHE A CD1 1 
ATOM   751  C  CD2 . PHE A 1 92  ? -12.575 -6.492  10.695  1.00 8.53  ? 95  PHE A CD2 1 
ATOM   752  C  CE1 . PHE A 1 92  ? -13.226 -4.771  8.633   1.00 10.04 ? 95  PHE A CE1 1 
ATOM   753  C  CE2 . PHE A 1 92  ? -13.913 -6.289  10.354  1.00 9.16  ? 95  PHE A CE2 1 
ATOM   754  C  CZ  . PHE A 1 92  ? -14.240 -5.429  9.315   1.00 9.37  ? 95  PHE A CZ  1 
ATOM   755  N  N   . HIS A 1 93  ? -7.843  -6.487  12.261  1.00 9.33  ? 96  HIS A N   1 
ATOM   756  C  CA  . HIS A 1 93  ? -6.647  -7.300  12.417  1.00 8.99  ? 96  HIS A CA  1 
ATOM   757  C  C   . HIS A 1 93  ? -7.085  -8.744  12.310  1.00 9.41  ? 96  HIS A C   1 
ATOM   758  O  O   . HIS A 1 93  ? -8.150  -9.092  12.822  1.00 9.91  ? 96  HIS A O   1 
ATOM   759  C  CB  . HIS A 1 93  ? -6.009  -7.060  13.788  1.00 9.29  ? 96  HIS A CB  1 
ATOM   760  C  CG  . HIS A 1 93  ? -5.740  -5.621  14.114  1.00 8.95  ? 96  HIS A CG  1 
ATOM   761  N  ND1 . HIS A 1 93  ? -4.472  -5.103  13.914  1.00 9.32  ? 96  HIS A ND1 1 
ATOM   762  C  CD2 . HIS A 1 93  ? -6.544  -4.596  14.498  1.00 9.44  ? 96  HIS A CD2 1 
ATOM   763  C  CE1 . HIS A 1 93  ? -4.461  -3.816  14.307  1.00 9.42  ? 96  HIS A CE1 1 
ATOM   764  N  NE2 . HIS A 1 93  ? -5.741  -3.471  14.617  1.00 9.17  ? 96  HIS A NE2 1 
ATOM   765  N  N   . TRP A 1 94  ? -6.278  -9.567  11.616  1.00 8.49  ? 97  TRP A N   1 
ATOM   766  C  CA  . TRP A 1 94  ? -6.674  -10.967 11.437  1.00 8.30  ? 97  TRP A CA  1 
ATOM   767  C  C   . TRP A 1 94  ? -5.472  -11.891 11.316  1.00 8.51  ? 97  TRP A C   1 
ATOM   768  O  O   . TRP A 1 94  ? -4.302  -11.453 11.231  1.00 9.75  ? 97  TRP A O   1 
ATOM   769  C  CB  . TRP A 1 94  ? -7.589  -11.080 10.209  1.00 9.27  ? 97  TRP A CB  1 
ATOM   770  C  CG  . TRP A 1 94  ? -6.923  -10.683 8.926   1.00 9.73  ? 97  TRP A CG  1 
ATOM   771  C  CD1 . TRP A 1 94  ? -6.214  -11.501 8.086   1.00 10.34 ? 97  TRP A CD1 1 
ATOM   772  C  CD2 . TRP A 1 94  ? -6.876  -9.367  8.372   1.00 9.12  ? 97  TRP A CD2 1 
ATOM   773  N  NE1 . TRP A 1 94  ? -5.790  -10.779 6.982   1.00 11.72 ? 97  TRP A NE1 1 
ATOM   774  C  CE2 . TRP A 1 94  ? -6.134  -9.461  7.161   1.00 10.67 ? 97  TRP A CE2 1 
ATOM   775  C  CE3 . TRP A 1 94  ? -7.361  -8.116  8.775   1.00 9.88  ? 97  TRP A CE3 1 
ATOM   776  C  CZ2 . TRP A 1 94  ? -5.935  -8.357  6.340   1.00 10.69 ? 97  TRP A CZ2 1 
ATOM   777  C  CZ3 . TRP A 1 94  ? -7.115  -7.014  7.981   1.00 10.88 ? 97  TRP A CZ3 1 
ATOM   778  C  CH2 . TRP A 1 94  ? -6.424  -7.137  6.770   1.00 11.06 ? 97  TRP A CH2 1 
ATOM   779  N  N   . GLY A 1 95  ? -5.812  -13.186 11.326  1.00 9.14  ? 98  GLY A N   1 
ATOM   780  C  CA  . GLY A 1 95  ? -4.804  -14.236 11.400  1.00 9.96  ? 98  GLY A CA  1 
ATOM   781  C  C   . GLY A 1 95  ? -4.580  -14.969 10.073  1.00 11.13 ? 98  GLY A C   1 
ATOM   782  O  O   . GLY A 1 95  ? -5.256  -14.738 9.099   1.00 11.57 ? 98  GLY A O   1 
ATOM   783  N  N   . SER A 1 96  ? -3.599  -15.855 10.129  1.00 13.19 ? 99  SER A N   1 
ATOM   784  C  CA  . SER A 1 96  ? -3.344  -16.761 9.024   1.00 14.68 ? 99  SER A CA  1 
ATOM   785  C  C   . SER A 1 96  ? -4.236  -17.992 9.134   1.00 16.40 ? 99  SER A C   1 
ATOM   786  O  O   . SER A 1 96  ? -4.285  -18.773 8.186   1.00 16.27 ? 99  SER A O   1 
ATOM   787  C  CB  . SER A 1 96  ? -1.873  -17.110 9.046   1.00 15.06 ? 99  SER A CB  1 
ATOM   788  O  OG  . SER A 1 96  ? -1.388  -17.616 10.295  1.00 16.54 ? 99  SER A OG  1 
ATOM   789  N  N   . LEU A 1 97  ? -4.797  -18.230 10.333  1.00 15.65 ? 100 LEU A N   1 
ATOM   790  C  CA  . LEU A 1 97  ? -5.638  -19.357 10.704  1.00 15.92 ? 100 LEU A CA  1 
ATOM   791  C  C   . LEU A 1 97  ? -6.796  -18.839 11.533  1.00 16.59 ? 100 LEU A C   1 
ATOM   792  O  O   . LEU A 1 97  ? -6.670  -17.817 12.197  1.00 15.52 ? 100 LEU A O   1 
ATOM   793  C  CB  . LEU A 1 97  ? -4.831  -20.295 11.616  1.00 19.93 ? 100 LEU A CB  1 
ATOM   794  C  CG  . LEU A 1 97  ? -3.621  -20.963 10.975  1.00 24.36 ? 100 LEU A CG  1 
ATOM   795  C  CD1 . LEU A 1 97  ? -2.727  -21.555 12.045  1.00 30.88 ? 100 LEU A CD1 1 
ATOM   796  C  CD2 . LEU A 1 97  ? -4.102  -22.059 10.044  1.00 29.34 ? 100 LEU A CD2 1 
ATOM   797  N  N   . ASP A 1 98  ? -7.865  -19.622 11.566  1.00 14.10 ? 101 ASP A N   1 
ATOM   798  C  CA  . ASP A 1 98  ? -9.066  -19.111 12.225  1.00 15.53 ? 101 ASP A CA  1 
ATOM   799  C  C   . ASP A 1 98  ? -8.842  -19.040 13.735  1.00 15.80 ? 101 ASP A C   1 
ATOM   800  O  O   . ASP A 1 98  ? -9.582  -18.344 14.418  1.00 17.04 ? 101 ASP A O   1 
ATOM   801  C  CB  . ASP A 1 98  ? -10.274 -19.985 11.899  1.00 15.38 ? 101 ASP A CB  1 
ATOM   802  C  CG  . ASP A 1 98  ? -10.735 -20.028 10.453  1.00 18.54 ? 101 ASP A CG  1 
ATOM   803  O  OD1 . ASP A 1 98  ? -10.320 -19.222 9.620   1.00 15.56 ? 101 ASP A OD1 1 
ATOM   804  O  OD2 . ASP A 1 98  ? -11.551 -20.902 10.171  1.00 21.11 ? 101 ASP A OD2 1 
ATOM   805  N  N   . GLY A 1 99  ? -7.807  -19.725 14.264  1.00 15.77 ? 102 GLY A N   1 
ATOM   806  C  CA  . GLY A 1 99  ? -7.572  -19.707 15.702  1.00 15.68 ? 102 GLY A CA  1 
ATOM   807  C  C   . GLY A 1 99  ? -6.753  -18.534 16.257  1.00 14.22 ? 102 GLY A C   1 
ATOM   808  O  O   . GLY A 1 99  ? -6.352  -18.518 17.432  1.00 15.98 ? 102 GLY A O   1 
ATOM   809  N  N   . GLN A 1 100 ? -6.432  -17.585 15.392  1.00 12.43 ? 103 GLN A N   1 
ATOM   810  C  CA  . GLN A 1 100 ? -5.636  -16.447 15.857  1.00 11.47 ? 103 GLN A CA  1 
ATOM   811  C  C   . GLN A 1 100 ? -5.954  -15.281 14.961  1.00 10.61 ? 103 GLN A C   1 
ATOM   812  O  O   . GLN A 1 100 ? -6.536  -15.443 13.907  1.00 12.45 ? 103 GLN A O   1 
ATOM   813  C  CB  . GLN A 1 100 ? -4.133  -16.760 15.828  1.00 13.51 ? 103 GLN A CB  1 
ATOM   814  C  CG  . GLN A 1 100 ? -3.591  -16.916 14.409  1.00 15.33 ? 103 GLN A CG  1 
ATOM   815  C  CD  . GLN A 1 100 ? -2.250  -17.605 14.462  1.00 20.52 ? 103 GLN A CD  1 
ATOM   816  O  OE1 . GLN A 1 100 ? -2.121  -18.654 15.092  1.00 25.05 ? 103 GLN A OE1 1 
ATOM   817  N  NE2 . GLN A 1 100 ? -1.247  -17.037 13.811  1.00 18.34 ? 103 GLN A NE2 1 
ATOM   818  N  N   . GLY A 1 101 ? -5.642  -14.084 15.441  1.00 10.65 ? 104 GLY A N   1 
ATOM   819  C  CA  . GLY A 1 101 ? -5.928  -12.929 14.625  1.00 8.97  ? 104 GLY A CA  1 
ATOM   820  C  C   . GLY A 1 101 ? -6.381  -11.729 15.449  1.00 8.84  ? 104 GLY A C   1 
ATOM   821  O  O   . GLY A 1 101 ? -6.110  -10.585 15.097  1.00 10.40 ? 104 GLY A O   1 
ATOM   822  N  N   . SER A 1 102 ? -7.079  -12.000 16.562  1.00 8.74  ? 105 SER A N   1 
ATOM   823  C  CA  . SER A 1 102 ? -7.481  -10.845 17.373  1.00 8.94  ? 105 SER A CA  1 
ATOM   824  C  C   . SER A 1 102 ? -6.294  -10.315 18.177  1.00 9.28  ? 105 SER A C   1 
ATOM   825  O  O   . SER A 1 102 ? -5.275  -10.985 18.364  1.00 10.08 ? 105 SER A O   1 
ATOM   826  C  CB  . SER A 1 102 ? -8.631  -11.189 18.337  1.00 9.08  ? 105 SER A CB  1 
ATOM   827  O  OG  . SER A 1 102 ? -8.229  -12.150 19.312  1.00 9.30  ? 105 SER A OG  1 
ATOM   828  N  N   . GLU A 1 103 ? -6.437  -9.067  18.580  1.00 8.16  ? 106 GLU A N   1 
ATOM   829  C  CA  . GLU A 1 103 ? -5.460  -8.383  19.431  1.00 8.58  ? 106 GLU A CA  1 
ATOM   830  C  C   . GLU A 1 103 ? -5.788  -8.577  20.910  1.00 8.48  ? 106 GLU A C   1 
ATOM   831  O  O   . GLU A 1 103 ? -4.948  -9.145  21.647  1.00 7.96  ? 106 GLU A O   1 
ATOM   832  C  CB  . GLU A 1 103 ? -5.383  -6.910  19.050  1.00 8.87  ? 106 GLU A CB  1 
ATOM   833  C  CG  . GLU A 1 103 ? -5.042  -6.701  17.559  1.00 9.09  ? 106 GLU A CG  1 
ATOM   834  C  CD  . GLU A 1 103 ? -4.258  -5.444  17.326  1.00 9.02  ? 106 GLU A CD  1 
ATOM   835  O  OE1 . GLU A 1 103 ? -4.821  -4.336  17.501  1.00 8.52  ? 106 GLU A OE1 1 
ATOM   836  O  OE2 . GLU A 1 103 ? -3.061  -5.560  16.929  1.00 9.65  ? 106 GLU A OE2 1 
ATOM   837  N  N   . HIS A 1 104 ? -6.985  -8.131  21.333  1.00 9.26  ? 107 HIS A N   1 
ATOM   838  C  CA  . HIS A 1 104 ? -7.384  -8.499  22.675  1.00 7.77  ? 107 HIS A CA  1 
ATOM   839  C  C   . HIS A 1 104 ? -7.646  -10.004 22.694  1.00 8.21  ? 107 HIS A C   1 
ATOM   840  O  O   . HIS A 1 104 ? -7.947  -10.579 21.646  1.00 8.68  ? 107 HIS A O   1 
ATOM   841  C  CB  . HIS A 1 104 ? -8.639  -7.732  23.047  1.00 7.67  ? 107 HIS A CB  1 
ATOM   842  C  CG  . HIS A 1 104 ? -8.298  -6.288  23.206  1.00 7.31  ? 107 HIS A CG  1 
ATOM   843  N  ND1 . HIS A 1 104 ? -8.384  -5.385  22.130  1.00 7.68  ? 107 HIS A ND1 1 
ATOM   844  C  CD2 . HIS A 1 104 ? -7.842  -5.601  24.290  1.00 7.02  ? 107 HIS A CD2 1 
ATOM   845  C  CE1 . HIS A 1 104 ? -7.975  -4.184  22.556  1.00 7.44  ? 107 HIS A CE1 1 
ATOM   846  N  NE2 . HIS A 1 104 ? -7.588  -4.308  23.895  1.00 7.72  ? 107 HIS A NE2 1 
ATOM   847  N  N   . THR A 1 105 ? -7.477  -10.614 23.859  1.00 8.96  ? 108 THR A N   1 
ATOM   848  C  CA  . THR A 1 105 ? -7.903  -11.992 24.040  1.00 9.35  ? 108 THR A CA  1 
ATOM   849  C  C   . THR A 1 105 ? -8.854  -12.032 25.232  1.00 10.42 ? 108 THR A C   1 
ATOM   850  O  O   . THR A 1 105 ? -8.902  -11.104 26.021  1.00 10.23 ? 108 THR A O   1 
ATOM   851  C  CB  . THR A 1 105 ? -6.707  -12.897 24.308  1.00 8.81  ? 108 THR A CB  1 
ATOM   852  O  OG1 . THR A 1 105 ? -5.889  -12.383 25.378  1.00 9.82  ? 108 THR A OG1 1 
ATOM   853  C  CG2 . THR A 1 105 ? -5.874  -13.034 23.050  1.00 9.96  ? 108 THR A CG2 1 
ATOM   854  N  N   . VAL A 1 106 ? -9.614  -13.114 25.344  1.00 10.48 ? 109 VAL A N   1 
ATOM   855  C  CA  . VAL A 1 106 ? -10.593 -13.198 26.429  1.00 11.70 ? 109 VAL A CA  1 
ATOM   856  C  C   . VAL A 1 106 ? -10.281 -14.496 27.169  1.00 12.02 ? 109 VAL A C   1 
ATOM   857  O  O   . VAL A 1 106 ? -10.469 -15.572 26.597  1.00 13.18 ? 109 VAL A O   1 
ATOM   858  C  CB  . VAL A 1 106 ? -12.016 -13.223 25.833  1.00 14.01 ? 109 VAL A CB  1 
ATOM   859  C  CG1 . VAL A 1 106 ? -13.033 -13.368 26.949  1.00 15.03 ? 109 VAL A CG1 1 
ATOM   860  C  CG2 . VAL A 1 106 ? -12.291 -11.928 25.061  1.00 13.70 ? 109 VAL A CG2 1 
ATOM   861  N  N   . ASP A 1 107 ? -9.737  -14.404 28.375  1.00 11.77 ? 110 ASP A N   1 
ATOM   862  C  CA  . ASP A 1 107 ? -9.300  -15.609 29.093  1.00 13.89 ? 110 ASP A CA  1 
ATOM   863  C  C   . ASP A 1 107 ? -8.344  -16.415 28.221  1.00 15.35 ? 110 ASP A C   1 
ATOM   864  O  O   . ASP A 1 107 ? -8.399  -17.669 28.172  1.00 15.32 ? 110 ASP A O   1 
ATOM   865  C  CB  . ASP A 1 107 ? -10.486 -16.461 29.574  1.00 15.22 ? 110 ASP A CB  1 
ATOM   866  C  CG  . ASP A 1 107 ? -11.435 -15.706 30.497  1.00 15.77 ? 110 ASP A CG  1 
ATOM   867  O  OD1 . ASP A 1 107 ? -10.946 -14.962 31.327  1.00 16.88 ? 110 ASP A OD1 1 
ATOM   868  O  OD2 . ASP A 1 107 ? -12.628 -15.977 30.431  1.00 22.82 ? 110 ASP A OD2 1 
ATOM   869  N  N   . LYS A 1 108 ? -7.454  -15.678 27.554  1.00 13.02 ? 111 LYS A N   1 
ATOM   870  C  CA  . LYS A 1 108 ? -6.355  -16.193 26.742  1.00 14.38 ? 111 LYS A CA  1 
ATOM   871  C  C   . LYS A 1 108 ? -6.866  -16.695 25.391  1.00 12.71 ? 111 LYS A C   1 
ATOM   872  O  O   . LYS A 1 108 ? -6.050  -17.049 24.544  1.00 15.74 ? 111 LYS A O   1 
ATOM   873  C  CB  . LYS A 1 108 ? -5.507  -17.208 27.530  1.00 17.82 ? 111 LYS A CB  1 
ATOM   874  C  CG  . LYS A 1 108 ? -4.813  -16.698 28.792  1.00 20.84 ? 111 LYS A CG  1 
ATOM   875  C  CD  . LYS A 1 108 ? -3.838  -15.612 28.502  1.00 25.85 ? 111 LYS A CD  1 
ATOM   876  C  CE  . LYS A 1 108 ? -3.010  -15.166 29.693  1.00 32.34 ? 111 LYS A CE  1 
ATOM   877  N  NZ  . LYS A 1 108 ? -1.817  -16.021 29.865  1.00 36.89 ? 111 LYS A NZ  1 
ATOM   878  N  N   . LYS A 1 109 ? -8.186  -16.644 25.152  1.00 14.12 ? 112 LYS A N   1 
ATOM   879  C  CA  . LYS A 1 109 ? -8.729  -17.128 23.891  1.00 15.30 ? 112 LYS A CA  1 
ATOM   880  C  C   . LYS A 1 109 ? -8.560  -16.025 22.827  1.00 12.96 ? 112 LYS A C   1 
ATOM   881  O  O   . LYS A 1 109 ? -8.892  -14.864 23.052  1.00 13.23 ? 112 LYS A O   1 
ATOM   882  C  CB  . LYS A 1 109 ? -10.189 -17.519 24.053  1.00 19.59 ? 112 LYS A CB  1 
ATOM   883  C  CG  . LYS A 1 109 ? -11.015 -17.634 22.789  1.00 25.54 ? 112 LYS A CG  1 
ATOM   884  C  CD  . LYS A 1 109 ? -12.518 -17.670 23.127  1.00 30.93 ? 112 LYS A CD  1 
ATOM   885  C  CE  . LYS A 1 109 ? -13.469 -17.669 21.941  1.00 35.53 ? 112 LYS A CE  1 
ATOM   886  N  NZ  . LYS A 1 109 ? -12.999 -18.538 20.843  1.00 32.54 ? 112 LYS A NZ  1 
ATOM   887  N  N   A LYS A 1 110 ? -7.991  -16.420 21.688  0.50 13.47 ? 113 LYS A N   1 
ATOM   888  N  N   B LYS A 1 110 ? -8.031  -16.417 21.658  0.50 13.59 ? 113 LYS A N   1 
ATOM   889  C  CA  A LYS A 1 110 ? -7.903  -15.546 20.525  0.50 12.45 ? 113 LYS A CA  1 
ATOM   890  C  CA  B LYS A 1 110 ? -7.866  -15.524 20.507  0.50 12.53 ? 113 LYS A CA  1 
ATOM   891  C  C   A LYS A 1 110 ? -9.119  -15.797 19.636  0.50 12.21 ? 113 LYS A C   1 
ATOM   892  C  C   B LYS A 1 110 ? -8.941  -15.798 19.459  0.50 11.95 ? 113 LYS A C   1 
ATOM   893  O  O   A LYS A 1 110 ? -9.652  -16.916 19.570  0.50 11.82 ? 113 LYS A O   1 
ATOM   894  O  O   B LYS A 1 110 ? -9.174  -16.945 19.066  0.50 11.51 ? 113 LYS A O   1 
ATOM   895  C  CB  A LYS A 1 110 ? -6.599  -15.840 19.768  0.50 12.76 ? 113 LYS A CB  1 
ATOM   896  C  CB  B LYS A 1 110 ? -6.548  -15.812 19.775  0.50 13.14 ? 113 LYS A CB  1 
ATOM   897  C  CG  A LYS A 1 110 ? -5.348  -15.860 20.646  0.50 13.46 ? 113 LYS A CG  1 
ATOM   898  C  CG  B LYS A 1 110 ? -5.282  -15.434 20.535  0.50 14.07 ? 113 LYS A CG  1 
ATOM   899  C  CD  A LYS A 1 110 ? -4.120  -16.373 19.922  0.50 13.98 ? 113 LYS A CD  1 
ATOM   900  C  CD  B LYS A 1 110 ? -4.018  -15.927 19.867  0.50 14.97 ? 113 LYS A CD  1 
ATOM   901  C  CE  A LYS A 1 110 ? -2.844  -15.789 20.490  0.50 13.64 ? 113 LYS A CE  1 
ATOM   902  C  CE  B LYS A 1 110 ? -2.802  -15.424 20.609  0.50 15.43 ? 113 LYS A CE  1 
ATOM   903  N  NZ  A LYS A 1 110 ? -2.468  -16.382 21.799  0.50 13.74 ? 113 LYS A NZ  1 
ATOM   904  N  NZ  B LYS A 1 110 ? -1.732  -16.447 20.694  0.50 17.19 ? 113 LYS A NZ  1 
ATOM   905  N  N   . TYR A 1 111 ? -9.588  -14.733 18.974  1.00 10.71 ? 114 TYR A N   1 
ATOM   906  C  CA  . TYR A 1 111 ? -10.592 -14.827 17.940  1.00 10.46 ? 114 TYR A CA  1 
ATOM   907  C  C   . TYR A 1 111 ? -9.945  -14.735 16.557  1.00 10.19 ? 114 TYR A C   1 
ATOM   908  O  O   . TYR A 1 111 ? -8.764  -14.447 16.475  1.00 10.72 ? 114 TYR A O   1 
ATOM   909  C  CB  . TYR A 1 111 ? -11.636 -13.709 18.083  1.00 10.72 ? 114 TYR A CB  1 
ATOM   910  C  CG  . TYR A 1 111 ? -12.558 -13.945 19.253  1.00 11.16 ? 114 TYR A CG  1 
ATOM   911  C  CD1 . TYR A 1 111 ? -12.273 -13.470 20.517  1.00 12.22 ? 114 TYR A CD1 1 
ATOM   912  C  CD2 . TYR A 1 111 ? -13.721 -14.650 19.048  1.00 12.89 ? 114 TYR A CD2 1 
ATOM   913  C  CE1 . TYR A 1 111 ? -13.104 -13.747 21.594  1.00 14.53 ? 114 TYR A CE1 1 
ATOM   914  C  CE2 . TYR A 1 111 ? -14.589 -14.892 20.101  1.00 16.61 ? 114 TYR A CE2 1 
ATOM   915  C  CZ  . TYR A 1 111 ? -14.297 -14.386 21.349  1.00 15.31 ? 114 TYR A CZ  1 
ATOM   916  O  OH  . TYR A 1 111 ? -15.178 -14.598 22.392  1.00 20.10 ? 114 TYR A OH  1 
ATOM   917  N  N   . ALA A 1 112 ? -10.711 -14.997 15.489  1.00 9.42  ? 115 ALA A N   1 
ATOM   918  C  CA  . ALA A 1 112 ? -10.122 -15.003 14.145  1.00 9.56  ? 115 ALA A CA  1 
ATOM   919  C  C   . ALA A 1 112 ? -9.738  -13.611 13.643  1.00 9.41  ? 115 ALA A C   1 
ATOM   920  O  O   . ALA A 1 112 ? -8.920  -13.470 12.704  1.00 9.82  ? 115 ALA A O   1 
ATOM   921  C  CB  . ALA A 1 112 ? -11.132 -15.623 13.201  1.00 10.40 ? 115 ALA A CB  1 
ATOM   922  N  N   . ALA A 1 113 ? -10.380 -12.587 14.194  1.00 9.27  ? 116 ALA A N   1 
ATOM   923  C  CA  . ALA A 1 113 ? -10.047 -11.239 13.786  1.00 8.08  ? 116 ALA A CA  1 
ATOM   924  C  C   . ALA A 1 113 ? -10.636 -10.289 14.834  1.00 8.05  ? 116 ALA A C   1 
ATOM   925  O  O   . ALA A 1 113 ? -11.415 -10.688 15.725  1.00 8.26  ? 116 ALA A O   1 
ATOM   926  C  CB  . ALA A 1 113 ? -10.631 -10.972 12.398  1.00 7.82  ? 116 ALA A CB  1 
ATOM   927  N  N   . GLU A 1 114 ? -10.324 -9.006  14.666  1.00 7.81  ? 117 GLU A N   1 
ATOM   928  C  CA  . GLU A 1 114 ? -10.885 -8.004  15.559  1.00 7.26  ? 117 GLU A CA  1 
ATOM   929  C  C   . GLU A 1 114 ? -11.069 -6.734  14.737  1.00 8.51  ? 117 GLU A C   1 
ATOM   930  O  O   . GLU A 1 114 ? -10.179 -6.294  14.039  1.00 8.15  ? 117 GLU A O   1 
ATOM   931  C  CB  . GLU A 1 114 ? -9.930  -7.815  16.752  1.00 7.48  ? 117 GLU A CB  1 
ATOM   932  C  CG  . GLU A 1 114 ? -10.437 -6.854  17.850  1.00 7.51  ? 117 GLU A CG  1 
ATOM   933  C  CD  . GLU A 1 114 ? -9.507  -6.783  19.057  1.00 8.13  ? 117 GLU A CD  1 
ATOM   934  O  OE1 . GLU A 1 114 ? -8.864  -7.802  19.372  1.00 8.80  ? 117 GLU A OE1 1 
ATOM   935  O  OE2 . GLU A 1 114 ? -9.447  -5.701  19.699  1.00 8.48  ? 117 GLU A OE2 1 
ATOM   936  N  N   . LEU A 1 115 ? -12.256 -6.153  14.854  1.00 7.60  ? 118 LEU A N   1 
ATOM   937  C  CA  . LEU A 1 115 ? -12.600 -4.896  14.221  1.00 7.64  ? 118 LEU A CA  1 
ATOM   938  C  C   . LEU A 1 115 ? -12.352 -3.774  15.222  1.00 7.72  ? 118 LEU A C   1 
ATOM   939  O  O   . LEU A 1 115 ? -12.763 -3.832  16.387  1.00 8.35  ? 118 LEU A O   1 
ATOM   940  C  CB  . LEU A 1 115 ? -14.091 -5.019  13.817  1.00 7.78  ? 118 LEU A CB  1 
ATOM   941  C  CG  . LEU A 1 115 ? -14.875 -3.732  13.503  1.00 8.55  ? 118 LEU A CG  1 
ATOM   942  C  CD1 . LEU A 1 115 ? -14.320 -3.104  12.223  1.00 8.82  ? 118 LEU A CD1 1 
ATOM   943  C  CD2 . LEU A 1 115 ? -16.389 -4.073  13.319  1.00 9.17  ? 118 LEU A CD2 1 
ATOM   944  N  N   . HIS A 1 116 ? -11.762 -2.696  14.710  1.00 7.10  ? 119 HIS A N   1 
ATOM   945  C  CA  . HIS A 1 116 ? -11.526 -1.514  15.521  1.00 8.35  ? 119 HIS A CA  1 
ATOM   946  C  C   . HIS A 1 116 ? -12.241 -0.371  14.813  1.00 8.08  ? 119 HIS A C   1 
ATOM   947  O  O   . HIS A 1 116 ? -11.805 0.026   13.694  1.00 9.00  ? 119 HIS A O   1 
ATOM   948  C  CB  . HIS A 1 116 ? -10.032 -1.250  15.600  1.00 8.85  ? 119 HIS A CB  1 
ATOM   949  C  CG  . HIS A 1 116 ? -9.330  -2.224  16.479  1.00 8.22  ? 119 HIS A CG  1 
ATOM   950  N  ND1 . HIS A 1 116 ? -7.920  -2.424  16.486  1.00 8.80  ? 119 HIS A ND1 1 
ATOM   951  C  CD2 . HIS A 1 116 ? -9.841  -3.026  17.420  1.00 8.01  ? 119 HIS A CD2 1 
ATOM   952  C  CE1 . HIS A 1 116 ? -7.624  -3.332  17.368  1.00 8.74  ? 119 HIS A CE1 1 
ATOM   953  N  NE2 . HIS A 1 116 ? -8.785  -3.718  17.945  1.00 6.90  ? 119 HIS A NE2 1 
ATOM   954  N  N   . LEU A 1 117 ? -13.197 0.243   15.521  1.00 7.81  ? 120 LEU A N   1 
ATOM   955  C  CA  . LEU A 1 117 ? -13.846 1.461   15.049  1.00 8.68  ? 120 LEU A CA  1 
ATOM   956  C  C   . LEU A 1 117 ? -13.218 2.580   15.861  1.00 9.07  ? 120 LEU A C   1 
ATOM   957  O  O   . LEU A 1 117 ? -13.384 2.626   17.096  1.00 8.59  ? 120 LEU A O   1 
ATOM   958  C  CB  . LEU A 1 117 ? -15.361 1.386   15.274  1.00 8.67  ? 120 LEU A CB  1 
ATOM   959  C  CG  . LEU A 1 117 ? -16.007 0.328   14.374  1.00 9.60  ? 120 LEU A CG  1 
ATOM   960  C  CD1 . LEU A 1 117 ? -16.866 -0.579  15.237  1.00 12.20 ? 120 LEU A CD1 1 
ATOM   961  C  CD2 . LEU A 1 117 ? -16.912 0.969   13.319  1.00 11.02 ? 120 LEU A CD2 1 
ATOM   962  N  N   . VAL A 1 118 ? -12.504 3.459   15.138  1.00 8.12  ? 121 VAL A N   1 
ATOM   963  C  CA  . VAL A 1 118 ? -11.698 4.473   15.812  1.00 8.10  ? 121 VAL A CA  1 
ATOM   964  C  C   . VAL A 1 118 ? -12.409 5.820   15.838  1.00 8.90  ? 121 VAL A C   1 
ATOM   965  O  O   . VAL A 1 118 ? -12.866 6.297   14.785  1.00 8.39  ? 121 VAL A O   1 
ATOM   966  C  CB  . VAL A 1 118 ? -10.347 4.655   15.090  1.00 7.74  ? 121 VAL A CB  1 
ATOM   967  C  CG1 . VAL A 1 118 ? -9.479  5.706   15.773  1.00 8.63  ? 121 VAL A CG1 1 
ATOM   968  C  CG2 . VAL A 1 118 ? -9.581  3.330   14.923  1.00 8.15  ? 121 VAL A CG2 1 
ATOM   969  N  N   . HIS A 1 119 ? -12.549 6.408   17.056  1.00 8.09  ? 122 HIS A N   1 
ATOM   970  C  CA  . HIS A 1 119 ? -13.212 7.692   17.154  1.00 8.89  ? 122 HIS A CA  1 
ATOM   971  C  C   . HIS A 1 119 ? -12.347 8.676   17.940  1.00 8.95  ? 122 HIS A C   1 
ATOM   972  O  O   . HIS A 1 119 ? -11.546 8.261   18.777  1.00 9.92  ? 122 HIS A O   1 
ATOM   973  C  CB  . HIS A 1 119 ? -14.474 7.518   17.999  1.00 9.19  ? 122 HIS A CB  1 
ATOM   974  C  CG  . HIS A 1 119 ? -15.374 6.407   17.594  1.00 9.32  ? 122 HIS A CG  1 
ATOM   975  N  ND1 . HIS A 1 119 ? -15.052 5.074   17.868  1.00 10.28 ? 122 HIS A ND1 1 
ATOM   976  C  CD2 . HIS A 1 119 ? -16.608 6.384   16.987  1.00 10.85 ? 122 HIS A CD2 1 
ATOM   977  C  CE1 . HIS A 1 119 ? -16.044 4.300   17.432  1.00 11.26 ? 122 HIS A CE1 1 
ATOM   978  N  NE2 . HIS A 1 119 ? -17.004 5.052   16.878  1.00 10.38 ? 122 HIS A NE2 1 
ATOM   979  N  N   . TRP A 1 120 ? -12.524 9.994   17.703  1.00 10.22 ? 123 TRP A N   1 
ATOM   980  C  CA  . TRP A 1 120 ? -11.664 10.953  18.402  1.00 9.91  ? 123 TRP A CA  1 
ATOM   981  C  C   . TRP A 1 120 ? -12.529 11.987  19.099  1.00 11.13 ? 123 TRP A C   1 
ATOM   982  O  O   . TRP A 1 120 ? -13.631 12.313  18.624  1.00 12.04 ? 123 TRP A O   1 
ATOM   983  C  CB  . TRP A 1 120 ? -10.648 11.638  17.483  1.00 11.05 ? 123 TRP A CB  1 
ATOM   984  C  CG  . TRP A 1 120 ? -11.261 12.296  16.279  1.00 12.37 ? 123 TRP A CG  1 
ATOM   985  C  CD1 . TRP A 1 120 ? -11.485 11.701  15.056  1.00 14.71 ? 123 TRP A CD1 1 
ATOM   986  C  CD2 . TRP A 1 120 ? -11.657 13.674  16.143  1.00 12.83 ? 123 TRP A CD2 1 
ATOM   987  N  NE1 . TRP A 1 120 ? -12.036 12.593  14.180  1.00 14.93 ? 123 TRP A NE1 1 
ATOM   988  C  CE2 . TRP A 1 120 ? -12.150 13.810  14.816  1.00 14.07 ? 123 TRP A CE2 1 
ATOM   989  C  CE3 . TRP A 1 120 ? -11.690 14.790  17.003  1.00 14.21 ? 123 TRP A CE3 1 
ATOM   990  C  CZ2 . TRP A 1 120 ? -12.629 15.013  14.311  1.00 15.32 ? 123 TRP A CZ2 1 
ATOM   991  C  CZ3 . TRP A 1 120 ? -12.201 15.979  16.500  1.00 14.43 ? 123 TRP A CZ3 1 
ATOM   992  C  CH2 . TRP A 1 120 ? -12.667 16.071  15.181  1.00 14.99 ? 123 TRP A CH2 1 
ATOM   993  N  N   . ASN A 1 121 ? -12.014 12.480  20.224  1.00 10.46 ? 124 ASN A N   1 
ATOM   994  C  CA  . ASN A 1 121 ? -12.783 13.360  21.082  1.00 11.07 ? 124 ASN A CA  1 
ATOM   995  C  C   . ASN A 1 121 ? -12.929 14.756  20.465  1.00 11.88 ? 124 ASN A C   1 
ATOM   996  O  O   . ASN A 1 121 ? -11.926 15.407  20.236  1.00 11.11 ? 124 ASN A O   1 
ATOM   997  C  CB  . ASN A 1 121 ? -12.007 13.460  22.396  1.00 11.94 ? 124 ASN A CB  1 
ATOM   998  C  CG  . ASN A 1 121 ? -12.825 14.051  23.518  1.00 13.23 ? 124 ASN A CG  1 
ATOM   999  O  OD1 . ASN A 1 121 ? -13.654 14.910  23.259  1.00 15.15 ? 124 ASN A OD1 1 
ATOM   1000 N  ND2 . ASN A 1 121 ? -12.592 13.576  24.726  1.00 15.12 ? 124 ASN A ND2 1 
ATOM   1001 N  N   . THR A 1 122 ? -14.163 15.193  20.191  1.00 12.86 ? 125 THR A N   1 
ATOM   1002 C  CA  . THR A 1 122 ? -14.352 16.428  19.427  1.00 15.09 ? 125 THR A CA  1 
ATOM   1003 C  C   . THR A 1 122 ? -13.936 17.658  20.252  1.00 16.43 ? 125 THR A C   1 
ATOM   1004 O  O   . THR A 1 122 ? -13.580 18.628  19.561  1.00 17.45 ? 125 THR A O   1 
ATOM   1005 C  CB  . THR A 1 122 ? -15.822 16.613  19.030  1.00 15.73 ? 125 THR A CB  1 
ATOM   1006 O  OG1 . THR A 1 122 ? -16.582 16.628  20.232  1.00 16.46 ? 125 THR A OG1 1 
ATOM   1007 C  CG2 . THR A 1 122 ? -16.328 15.516  18.115  1.00 18.64 ? 125 THR A CG2 1 
ATOM   1008 N  N   . LYS A 1 123 ? -13.570 17.536  21.500  1.00 15.90 ? 127 LYS A N   1 
ATOM   1009 C  CA  . LYS A 1 123 ? -13.076 18.747  22.224  1.00 17.84 ? 127 LYS A CA  1 
ATOM   1010 C  C   . LYS A 1 123 ? -11.673 19.117  21.734  1.00 19.21 ? 127 LYS A C   1 
ATOM   1011 O  O   . LYS A 1 123 ? -11.254 20.272  21.864  1.00 19.03 ? 127 LYS A O   1 
ATOM   1012 C  CB  . LYS A 1 123 ? -13.242 18.511  23.719  1.00 20.84 ? 127 LYS A CB  1 
ATOM   1013 C  CG  . LYS A 1 123 ? -12.179 17.645  24.354  1.00 21.51 ? 127 LYS A CG  1 
ATOM   1014 C  CD  . LYS A 1 123 ? -12.521 17.454  25.836  1.00 25.91 ? 127 LYS A CD  1 
ATOM   1015 C  CE  . LYS A 1 123 ? -11.532 16.496  26.451  1.00 28.72 ? 127 LYS A CE  1 
ATOM   1016 N  NZ  . LYS A 1 123 ? -11.643 16.449  27.932  1.00 33.69 ? 127 LYS A NZ  1 
ATOM   1017 N  N   . TYR A 1 124 ? -10.996 18.177  21.076  1.00 16.22 ? 128 TYR A N   1 
ATOM   1018 C  CA  . TYR A 1 124 ? -9.647  18.450  20.603  1.00 16.94 ? 128 TYR A CA  1 
ATOM   1019 C  C   . TYR A 1 124 ? -9.578  18.904  19.155  1.00 21.26 ? 128 TYR A C   1 
ATOM   1020 O  O   . TYR A 1 124 ? -8.468  19.122  18.657  1.00 19.74 ? 128 TYR A O   1 
ATOM   1021 C  CB  . TYR A 1 124 ? -8.753  17.226  20.791  1.00 16.91 ? 128 TYR A CB  1 
ATOM   1022 C  CG  . TYR A 1 124 ? -8.631  16.921  22.248  1.00 16.64 ? 128 TYR A CG  1 
ATOM   1023 C  CD1 . TYR A 1 124 ? -8.166  17.904  23.114  1.00 20.00 ? 128 TYR A CD1 1 
ATOM   1024 C  CD2 . TYR A 1 124 ? -8.944  15.679  22.765  1.00 15.46 ? 128 TYR A CD2 1 
ATOM   1025 C  CE1 . TYR A 1 124 ? -8.048  17.636  24.464  1.00 19.10 ? 128 TYR A CE1 1 
ATOM   1026 C  CE2 . TYR A 1 124 ? -8.840  15.386  24.116  1.00 16.76 ? 128 TYR A CE2 1 
ATOM   1027 C  CZ  . TYR A 1 124 ? -8.396  16.395  24.967  1.00 20.06 ? 128 TYR A CZ  1 
ATOM   1028 O  OH  . TYR A 1 124 ? -8.280  16.123  26.296  1.00 21.19 ? 128 TYR A OH  1 
ATOM   1029 N  N   . GLY A 1 125 ? -10.719 18.896  18.467  1.00 18.23 ? 129 GLY A N   1 
ATOM   1030 C  CA  . GLY A 1 125 ? -10.818 19.596  17.183  1.00 18.76 ? 129 GLY A CA  1 
ATOM   1031 C  C   . GLY A 1 125 ? -10.344 18.797  15.969  1.00 16.93 ? 129 GLY A C   1 
ATOM   1032 O  O   . GLY A 1 125 ? -10.902 18.928  14.847  1.00 19.12 ? 129 GLY A O   1 
ATOM   1033 N  N   . ASP A 1 126 ? -9.332  17.936  16.157  1.00 15.77 ? 130 ASP A N   1 
ATOM   1034 C  CA  . ASP A 1 126 ? -8.997  17.008  15.082  1.00 18.76 ? 130 ASP A CA  1 
ATOM   1035 C  C   . ASP A 1 126 ? -8.278  15.791  15.625  1.00 17.93 ? 130 ASP A C   1 
ATOM   1036 O  O   . ASP A 1 126 ? -7.880  15.754  16.796  1.00 16.85 ? 130 ASP A O   1 
ATOM   1037 C  CB  . ASP A 1 126 ? -8.281  17.627  13.868  1.00 21.48 ? 130 ASP A CB  1 
ATOM   1038 C  CG  . ASP A 1 126 ? -6.858  18.105  14.019  1.00 26.75 ? 130 ASP A CG  1 
ATOM   1039 O  OD1 . ASP A 1 126 ? -6.098  17.608  14.885  1.00 24.03 ? 130 ASP A OD1 1 
ATOM   1040 O  OD2 . ASP A 1 126 ? -6.494  18.910  13.183  1.00 34.07 ? 130 ASP A OD2 1 
ATOM   1041 N  N   . PHE A 1 127 ? -8.179  14.783  14.761  1.00 17.94 ? 131 PHE A N   1 
ATOM   1042 C  CA  . PHE A 1 127 ? -7.604  13.519  15.156  1.00 19.70 ? 131 PHE A CA  1 
ATOM   1043 C  C   . PHE A 1 127 ? -6.148  13.689  15.578  1.00 16.72 ? 131 PHE A C   1 
ATOM   1044 O  O   . PHE A 1 127 ? -5.682  13.083  16.550  1.00 15.62 ? 131 PHE A O   1 
ATOM   1045 C  CB  . PHE A 1 127 ? -7.741  12.543  13.987  1.00 19.06 ? 131 PHE A CB  1 
ATOM   1046 C  CG  . PHE A 1 127 ? -7.074  11.244  14.306  1.00 21.75 ? 131 PHE A CG  1 
ATOM   1047 C  CD1 . PHE A 1 127 ? -7.770  10.274  15.017  1.00 20.25 ? 131 PHE A CD1 1 
ATOM   1048 C  CD2 . PHE A 1 127 ? -5.753  11.023  13.960  1.00 23.46 ? 131 PHE A CD2 1 
ATOM   1049 C  CE1 . PHE A 1 127 ? -7.164  9.087   15.362  1.00 19.80 ? 131 PHE A CE1 1 
ATOM   1050 C  CE2 . PHE A 1 127 ? -5.146  9.837   14.321  1.00 25.53 ? 131 PHE A CE2 1 
ATOM   1051 C  CZ  . PHE A 1 127 ? -5.850  8.875   15.020  1.00 23.32 ? 131 PHE A CZ  1 
ATOM   1052 N  N   . GLY A 1 128 ? -5.385  14.502  14.812  1.00 16.29 ? 132 GLY A N   1 
ATOM   1053 C  CA  . GLY A 1 128 ? -3.985  14.678  15.187  1.00 17.39 ? 132 GLY A CA  1 
ATOM   1054 C  C   . GLY A 1 128 ? -3.770  15.326  16.556  1.00 17.19 ? 132 GLY A C   1 
ATOM   1055 O  O   . GLY A 1 128 ? -2.792  14.993  17.203  1.00 19.82 ? 132 GLY A O   1 
ATOM   1056 N  N   . LYS A 1 129 ? -4.665  16.226  16.998  1.00 18.04 ? 133 LYS A N   1 
ATOM   1057 C  CA  . LYS A 1 129 ? -4.562  16.786  18.342  1.00 17.04 ? 133 LYS A CA  1 
ATOM   1058 C  C   . LYS A 1 129 ? -4.983  15.746  19.377  1.00 16.78 ? 133 LYS A C   1 
ATOM   1059 O  O   . LYS A 1 129 ? -4.365  15.611  20.438  1.00 15.32 ? 133 LYS A O   1 
ATOM   1060 C  CB  . LYS A 1 129 ? -5.414  18.035  18.506  1.00 21.63 ? 133 LYS A CB  1 
ATOM   1061 C  CG  . LYS A 1 129 ? -4.833  19.287  17.860  1.00 29.69 ? 133 LYS A CG  1 
ATOM   1062 C  CD  . LYS A 1 129 ? -3.442  19.592  18.361  1.00 36.27 ? 133 LYS A CD  1 
ATOM   1063 C  CE  . LYS A 1 129 ? -3.428  20.634  19.459  1.00 45.71 ? 133 LYS A CE  1 
ATOM   1064 N  NZ  . LYS A 1 129 ? -2.185  21.446  19.396  1.00 55.61 ? 133 LYS A NZ  1 
ATOM   1065 N  N   . ALA A 1 130 ? -6.063  15.017  19.048  1.00 14.73 ? 134 ALA A N   1 
ATOM   1066 C  CA  . ALA A 1 130 ? -6.611  14.060  19.990  1.00 14.27 ? 134 ALA A CA  1 
ATOM   1067 C  C   . ALA A 1 130 ? -5.595  12.970  20.372  1.00 13.40 ? 134 ALA A C   1 
ATOM   1068 O  O   . ALA A 1 130 ? -5.542  12.507  21.524  1.00 11.95 ? 134 ALA A O   1 
ATOM   1069 C  CB  . ALA A 1 130 ? -7.860  13.440  19.362  1.00 13.80 ? 134 ALA A CB  1 
ATOM   1070 N  N   . VAL A 1 131 ? -4.792  12.484  19.422  1.00 12.41 ? 135 VAL A N   1 
ATOM   1071 C  CA  . VAL A 1 131 ? -3.873  11.388  19.744  1.00 13.93 ? 135 VAL A CA  1 
ATOM   1072 C  C   . VAL A 1 131 ? -2.766  11.816  20.704  1.00 13.77 ? 135 VAL A C   1 
ATOM   1073 O  O   . VAL A 1 131 ? -2.051  10.988  21.246  1.00 15.37 ? 135 VAL A O   1 
ATOM   1074 C  CB  . VAL A 1 131 ? -3.271  10.688  18.499  1.00 16.37 ? 135 VAL A CB  1 
ATOM   1075 C  CG1 . VAL A 1 131 ? -4.299  9.995   17.645  1.00 17.32 ? 135 VAL A CG1 1 
ATOM   1076 C  CG2 . VAL A 1 131 ? -2.337  11.585  17.692  1.00 16.22 ? 135 VAL A CG2 1 
ATOM   1077 N  N   . GLN A 1 132 ? -2.600  13.136  20.923  1.00 15.02 ? 136 GLN A N   1 
ATOM   1078 C  CA  . GLN A 1 132 ? -1.616  13.635  21.862  1.00 18.60 ? 136 GLN A CA  1 
ATOM   1079 C  C   . GLN A 1 132 ? -2.207  13.741  23.273  1.00 18.01 ? 136 GLN A C   1 
ATOM   1080 O  O   . GLN A 1 132 ? -1.528  14.243  24.175  1.00 19.59 ? 136 GLN A O   1 
ATOM   1081 C  CB  . GLN A 1 132 ? -1.076  15.000  21.361  1.00 19.89 ? 136 GLN A CB  1 
ATOM   1082 C  CG  . GLN A 1 132 ? -0.419  14.915  19.984  1.00 26.32 ? 136 GLN A CG  1 
ATOM   1083 C  CD  . GLN A 1 132 ? 0.804   14.011  20.022  1.00 37.69 ? 136 GLN A CD  1 
ATOM   1084 O  OE1 . GLN A 1 132 ? 1.509   13.907  21.035  1.00 46.03 ? 136 GLN A OE1 1 
ATOM   1085 N  NE2 . GLN A 1 132 ? 1.070   13.322  18.913  1.00 38.30 ? 136 GLN A NE2 1 
ATOM   1086 N  N   . GLN A 1 133 ? -3.443  13.267  23.490  1.00 16.33 ? 137 GLN A N   1 
ATOM   1087 C  CA  . GLN A 1 133 ? -4.148  13.473  24.749  1.00 15.73 ? 137 GLN A CA  1 
ATOM   1088 C  C   . GLN A 1 133 ? -4.514  12.123  25.351  1.00 15.83 ? 137 GLN A C   1 
ATOM   1089 O  O   . GLN A 1 133 ? -4.847  11.168  24.632  1.00 13.63 ? 137 GLN A O   1 
ATOM   1090 C  CB  . GLN A 1 133 ? -5.418  14.326  24.602  1.00 18.34 ? 137 GLN A CB  1 
ATOM   1091 C  CG  . GLN A 1 133 ? -5.252  15.488  23.650  1.00 23.55 ? 137 GLN A CG  1 
ATOM   1092 C  CD  . GLN A 1 133 ? -4.289  16.513  24.186  1.00 26.15 ? 137 GLN A CD  1 
ATOM   1093 O  OE1 . GLN A 1 133 ? -4.138  16.650  25.400  1.00 24.76 ? 137 GLN A OE1 1 
ATOM   1094 N  NE2 . GLN A 1 133 ? -3.608  17.189  23.264  1.00 31.84 ? 137 GLN A NE2 1 
ATOM   1095 N  N   . PRO A 1 134 ? -4.440  11.967  26.692  1.00 16.43 ? 138 PRO A N   1 
ATOM   1096 C  CA  . PRO A 1 134 ? -4.752  10.702  27.345  1.00 16.33 ? 138 PRO A CA  1 
ATOM   1097 C  C   . PRO A 1 134 ? -6.203  10.252  27.167  1.00 15.54 ? 138 PRO A C   1 
ATOM   1098 O  O   . PRO A 1 134 ? -6.502  9.065   27.295  1.00 16.53 ? 138 PRO A O   1 
ATOM   1099 C  CB  . PRO A 1 134 ? -4.309  10.905  28.809  1.00 20.51 ? 138 PRO A CB  1 
ATOM   1100 C  CG  . PRO A 1 134 ? -4.392  12.387  28.981  1.00 21.06 ? 138 PRO A CG  1 
ATOM   1101 C  CD  . PRO A 1 134 ? -4.095  13.039  27.643  1.00 18.64 ? 138 PRO A CD  1 
ATOM   1102 N  N   . ASP A 1 135 ? -7.087  11.198  26.824  1.00 14.51 ? 139 ASP A N   1 
ATOM   1103 C  CA  . ASP A 1 135 ? -8.492  10.891  26.595  1.00 16.92 ? 139 ASP A CA  1 
ATOM   1104 C  C   . ASP A 1 135 ? -8.881  11.209  25.151  1.00 14.46 ? 139 ASP A C   1 
ATOM   1105 O  O   . ASP A 1 135 ? -10.020 11.608  24.861  1.00 14.67 ? 139 ASP A O   1 
ATOM   1106 C  CB  . ASP A 1 135 ? -9.374  11.641  27.594  1.00 16.67 ? 139 ASP A CB  1 
ATOM   1107 C  CG  . ASP A 1 135 ? -9.245  13.140  27.519  1.00 21.07 ? 139 ASP A CG  1 
ATOM   1108 O  OD1 . ASP A 1 135 ? -8.331  13.633  26.848  1.00 21.22 ? 139 ASP A OD1 1 
ATOM   1109 O  OD2 . ASP A 1 135 ? -10.103 13.829  28.162  1.00 24.15 ? 139 ASP A OD2 1 
ATOM   1110 N  N   . GLY A 1 136 ? -7.926  11.072  24.227  1.00 11.53 ? 140 GLY A N   1 
ATOM   1111 C  CA  . GLY A 1 136 ? -8.190  11.618  22.911  1.00 11.66 ? 140 GLY A CA  1 
ATOM   1112 C  C   . GLY A 1 136 ? -9.005  10.687  22.019  1.00 11.01 ? 140 GLY A C   1 
ATOM   1113 O  O   . GLY A 1 136 ? -9.723  11.186  21.152  1.00 10.61 ? 140 GLY A O   1 
ATOM   1114 N  N   . LEU A 1 137 ? -8.823  9.360   22.179  1.00 9.99  ? 141 LEU A N   1 
ATOM   1115 C  CA  . LEU A 1 137 ? -9.492  8.419   21.261  1.00 10.01 ? 141 LEU A CA  1 
ATOM   1116 C  C   . LEU A 1 137 ? -10.390 7.497   22.063  1.00 9.97  ? 141 LEU A C   1 
ATOM   1117 O  O   . LEU A 1 137 ? -10.113 7.225   23.221  1.00 10.51 ? 141 LEU A O   1 
ATOM   1118 C  CB  . LEU A 1 137 ? -8.493  7.547   20.492  1.00 10.14 ? 141 LEU A CB  1 
ATOM   1119 C  CG  . LEU A 1 137 ? -7.533  8.263   19.540  1.00 13.13 ? 141 LEU A CG  1 
ATOM   1120 C  CD1 . LEU A 1 137 ? -6.819  7.284   18.625  1.00 12.87 ? 141 LEU A CD1 1 
ATOM   1121 C  CD2 . LEU A 1 137 ? -8.162  9.357   18.713  1.00 13.95 ? 141 LEU A CD2 1 
ATOM   1122 N  N   . ALA A 1 138 ? -11.442 7.003   21.387  1.00 9.17  ? 142 ALA A N   1 
ATOM   1123 C  CA  . ALA A 1 138 ? -12.218 5.889   21.944  1.00 9.23  ? 142 ALA A CA  1 
ATOM   1124 C  C   . ALA A 1 138 ? -12.283 4.861   20.812  1.00 7.81  ? 142 ALA A C   1 
ATOM   1125 O  O   . ALA A 1 138 ? -12.648 5.221   19.712  1.00 8.68  ? 142 ALA A O   1 
ATOM   1126 C  CB  . ALA A 1 138 ? -13.595 6.329   22.326  1.00 10.56 ? 142 ALA A CB  1 
ATOM   1127 N  N   . VAL A 1 139 ? -11.778 3.635   21.060  1.00 8.16  ? 143 VAL A N   1 
ATOM   1128 C  CA  . VAL A 1 139 ? -11.770 2.625   20.004  1.00 8.64  ? 143 VAL A CA  1 
ATOM   1129 C  C   . VAL A 1 139 ? -12.726 1.521   20.454  1.00 8.66  ? 143 VAL A C   1 
ATOM   1130 O  O   . VAL A 1 139 ? -12.600 1.005   21.576  1.00 9.03  ? 143 VAL A O   1 
ATOM   1131 C  CB  . VAL A 1 139 ? -10.373 2.056   19.665  1.00 9.17  ? 143 VAL A CB  1 
ATOM   1132 C  CG1 . VAL A 1 139 ? -10.477 1.078   18.485  1.00 8.72  ? 143 VAL A CG1 1 
ATOM   1133 C  CG2 . VAL A 1 139 ? -9.475  3.235   19.244  1.00 9.59  ? 143 VAL A CG2 1 
ATOM   1134 N  N   . LEU A 1 140 ? -13.716 1.243   19.605  1.00 7.92  ? 144 LEU A N   1 
ATOM   1135 C  CA  . LEU A 1 140 ? -14.691 0.201   19.889  1.00 8.54  ? 144 LEU A CA  1 
ATOM   1136 C  C   . LEU A 1 140 ? -14.166 -1.058  19.207  1.00 8.65  ? 144 LEU A C   1 
ATOM   1137 O  O   . LEU A 1 140 ? -13.957 -1.058  18.001  1.00 9.49  ? 144 LEU A O   1 
ATOM   1138 C  CB  . LEU A 1 140 ? -16.052 0.636   19.325  1.00 9.27  ? 144 LEU A CB  1 
ATOM   1139 C  CG  . LEU A 1 140 ? -17.189 -0.369  19.476  1.00 9.57  ? 144 LEU A CG  1 
ATOM   1140 C  CD1 . LEU A 1 140 ? -17.357 -0.781  20.939  1.00 11.62 ? 144 LEU A CD1 1 
ATOM   1141 C  CD2 . LEU A 1 140 ? -18.465 0.220   18.857  1.00 10.93 ? 144 LEU A CD2 1 
ATOM   1142 N  N   . GLY A 1 141 ? -13.864 -2.079  20.022  1.00 8.35  ? 145 GLY A N   1 
ATOM   1143 C  CA  . GLY A 1 141 ? -13.289 -3.314  19.496  1.00 8.37  ? 145 GLY A CA  1 
ATOM   1144 C  C   . GLY A 1 141 ? -14.348 -4.422  19.490  1.00 7.93  ? 145 GLY A C   1 
ATOM   1145 O  O   . GLY A 1 141 ? -15.081 -4.594  20.467  1.00 8.95  ? 145 GLY A O   1 
ATOM   1146 N  N   . ILE A 1 142 ? -14.427 -5.146  18.369  1.00 7.44  ? 146 ILE A N   1 
ATOM   1147 C  CA  . ILE A 1 142 ? -15.458 -6.184  18.193  1.00 7.61  ? 146 ILE A CA  1 
ATOM   1148 C  C   . ILE A 1 142 ? -14.719 -7.412  17.695  1.00 8.16  ? 146 ILE A C   1 
ATOM   1149 O  O   . ILE A 1 142 ? -14.046 -7.370  16.674  1.00 9.00  ? 146 ILE A O   1 
ATOM   1150 C  CB  . ILE A 1 142 ? -16.553 -5.729  17.202  1.00 8.15  ? 146 ILE A CB  1 
ATOM   1151 C  CG1 . ILE A 1 142 ? -17.175 -4.439  17.721  1.00 7.66  ? 146 ILE A CG1 1 
ATOM   1152 C  CG2 . ILE A 1 142 ? -17.594 -6.821  17.011  1.00 9.63  ? 146 ILE A CG2 1 
ATOM   1153 C  CD1 . ILE A 1 142 ? -18.254 -3.837  16.772  1.00 8.29  ? 146 ILE A CD1 1 
ATOM   1154 N  N   . PHE A 1 143 ? -14.860 -8.510  18.404  1.00 8.56  ? 147 PHE A N   1 
ATOM   1155 C  CA  . PHE A 1 143 ? -14.236 -9.736  17.938  1.00 8.48  ? 147 PHE A CA  1 
ATOM   1156 C  C   . PHE A 1 143 ? -15.030 -10.403 16.816  1.00 9.15  ? 147 PHE A C   1 
ATOM   1157 O  O   . PHE A 1 143 ? -16.247 -10.284 16.742  1.00 10.11 ? 147 PHE A O   1 
ATOM   1158 C  CB  . PHE A 1 143 ? -14.249 -10.752 19.082  1.00 8.91  ? 147 PHE A CB  1 
ATOM   1159 C  CG  . PHE A 1 143 ? -13.411 -10.300 20.250  1.00 7.83  ? 147 PHE A CG  1 
ATOM   1160 C  CD1 . PHE A 1 143 ? -12.037 -10.132 20.094  1.00 7.71  ? 147 PHE A CD1 1 
ATOM   1161 C  CD2 . PHE A 1 143 ? -13.962 -10.068 21.496  1.00 8.71  ? 147 PHE A CD2 1 
ATOM   1162 C  CE1 . PHE A 1 143 ? -11.216 -9.703  21.132  1.00 7.89  ? 147 PHE A CE1 1 
ATOM   1163 C  CE2 . PHE A 1 143 ? -13.140 -9.714  22.564  1.00 9.56  ? 147 PHE A CE2 1 
ATOM   1164 C  CZ  . PHE A 1 143 ? -11.788 -9.508  22.387  1.00 8.23  ? 147 PHE A CZ  1 
ATOM   1165 N  N   . LEU A 1 144 ? -14.287 -11.051 15.901  1.00 8.41  ? 148 LEU A N   1 
ATOM   1166 C  CA  . LEU A 1 144 ? -14.920 -11.867 14.853  1.00 9.49  ? 148 LEU A CA  1 
ATOM   1167 C  C   . LEU A 1 144 ? -14.570 -13.334 15.119  1.00 10.55 ? 148 LEU A C   1 
ATOM   1168 O  O   . LEU A 1 144 ? -13.378 -13.679 15.258  1.00 9.72  ? 148 LEU A O   1 
ATOM   1169 C  CB  . LEU A 1 144 ? -14.327 -11.460 13.489  1.00 10.50 ? 148 LEU A CB  1 
ATOM   1170 C  CG  . LEU A 1 144 ? -14.927 -10.237 12.791  1.00 11.07 ? 148 LEU A CG  1 
ATOM   1171 C  CD1 . LEU A 1 144 ? -14.687 -8.950  13.597  1.00 12.24 ? 148 LEU A CD1 1 
ATOM   1172 C  CD2 . LEU A 1 144 ? -14.254 -10.058 11.425  1.00 10.62 ? 148 LEU A CD2 1 
ATOM   1173 N  N   . LYS A 1 145 ? -15.623 -14.178 15.084  1.00 10.65 ? 149 LYS A N   1 
ATOM   1174 C  CA  . LYS A 1 145 ? -15.427 -15.615 15.111  1.00 13.11 ? 149 LYS A CA  1 
ATOM   1175 C  C   . LYS A 1 145 ? -15.917 -16.144 13.771  1.00 13.78 ? 149 LYS A C   1 
ATOM   1176 O  O   . LYS A 1 145 ? -16.751 -15.517 13.098  1.00 14.31 ? 149 LYS A O   1 
ATOM   1177 C  CB  . LYS A 1 145 ? -16.192 -16.264 16.257  1.00 16.05 ? 149 LYS A CB  1 
ATOM   1178 C  CG  . LYS A 1 145 ? -17.697 -16.143 16.232  1.00 19.53 ? 149 LYS A CG  1 
ATOM   1179 C  CD  . LYS A 1 145 ? -18.230 -17.091 17.306  1.00 26.32 ? 149 LYS A CD  1 
ATOM   1180 C  CE  . LYS A 1 145 ? -19.736 -17.021 17.469  1.00 29.81 ? 149 LYS A CE  1 
ATOM   1181 N  NZ  . LYS A 1 145 ? -20.169 -17.561 18.784  1.00 39.23 ? 149 LYS A NZ  1 
ATOM   1182 N  N   . VAL A 1 146 ? -15.418 -17.317 13.388  1.00 13.09 ? 150 VAL A N   1 
ATOM   1183 C  CA  . VAL A 1 146 ? -15.809 -17.872 12.092  1.00 13.75 ? 150 VAL A CA  1 
ATOM   1184 C  C   . VAL A 1 146 ? -17.009 -18.800 12.344  1.00 13.94 ? 150 VAL A C   1 
ATOM   1185 O  O   . VAL A 1 146 ? -16.938 -19.716 13.193  1.00 16.08 ? 150 VAL A O   1 
ATOM   1186 C  CB  . VAL A 1 146 ? -14.625 -18.630 11.448  1.00 13.44 ? 150 VAL A CB  1 
ATOM   1187 C  CG1 . VAL A 1 146 ? -15.076 -19.434 10.237  1.00 15.14 ? 150 VAL A CG1 1 
ATOM   1188 C  CG2 . VAL A 1 146 ? -13.499 -17.693 10.996  1.00 15.52 ? 150 VAL A CG2 1 
ATOM   1189 N  N   . GLY A 1 147 ? -18.102 -18.553 11.595  1.00 12.48 ? 151 GLY A N   1 
ATOM   1190 C  CA  . GLY A 1 147 ? -19.306 -19.371 11.586  1.00 14.59 ? 151 GLY A CA  1 
ATOM   1191 C  C   . GLY A 1 147 ? -20.166 -18.951 10.402  1.00 12.68 ? 151 GLY A C   1 
ATOM   1192 O  O   . GLY A 1 147 ? -19.717 -19.057 9.259   1.00 13.97 ? 151 GLY A O   1 
ATOM   1193 N  N   A SER A 1 148 ? -21.381 -18.455 10.695  0.50 14.82 ? 152 SER A N   1 
ATOM   1194 N  N   B SER A 1 148 ? -21.368 -18.449 10.709  0.50 15.30 ? 152 SER A N   1 
ATOM   1195 C  CA  A SER A 1 148 ? -22.283 -17.909 9.679   0.50 15.69 ? 152 SER A CA  1 
ATOM   1196 C  CA  B SER A 1 148 ? -22.245 -17.853 9.708   0.50 16.57 ? 152 SER A CA  1 
ATOM   1197 C  C   A SER A 1 148 ? -21.747 -16.578 9.153   0.50 16.94 ? 152 SER A C   1 
ATOM   1198 C  C   B SER A 1 148 ? -21.579 -16.625 9.089   0.50 17.38 ? 152 SER A C   1 
ATOM   1199 O  O   A SER A 1 148 ? -21.145 -15.824 9.923   0.50 16.76 ? 152 SER A O   1 
ATOM   1200 O  O   B SER A 1 148 ? -20.757 -15.964 9.725   0.50 16.75 ? 152 SER A O   1 
ATOM   1201 C  CB  A SER A 1 148 ? -23.680 -17.741 10.212  0.50 17.87 ? 152 SER A CB  1 
ATOM   1202 C  CB  B SER A 1 148 ? -23.551 -17.472 10.320  0.50 19.58 ? 152 SER A CB  1 
ATOM   1203 O  OG  A SER A 1 148 ? -23.751 -16.701 11.190  0.50 16.31 ? 152 SER A OG  1 
ATOM   1204 O  OG  B SER A 1 148 ? -24.104 -18.561 11.046  0.50 20.83 ? 152 SER A OG  1 
ATOM   1205 N  N   . ALA A 1 149 ? -21.966 -16.311 7.851   1.00 15.97 ? 153 ALA A N   1 
ATOM   1206 C  CA  . ALA A 1 149 ? -21.561 -15.055 7.237   1.00 15.41 ? 153 ALA A CA  1 
ATOM   1207 C  C   . ALA A 1 149 ? -22.161 -13.870 7.988   1.00 14.46 ? 153 ALA A C   1 
ATOM   1208 O  O   . ALA A 1 149 ? -23.242 -13.948 8.579   1.00 15.58 ? 153 ALA A O   1 
ATOM   1209 C  CB  . ALA A 1 149 ? -21.973 -15.003 5.771   1.00 18.67 ? 153 ALA A CB  1 
ATOM   1210 N  N   . LYS A 1 150 ? -21.471 -12.722 7.901   1.00 14.10 ? 154 LYS A N   1 
ATOM   1211 C  CA  . LYS A 1 150 ? -22.004 -11.438 8.336   1.00 14.31 ? 154 LYS A CA  1 
ATOM   1212 C  C   . LYS A 1 150 ? -22.415 -10.649 7.104   1.00 14.16 ? 154 LYS A C   1 
ATOM   1213 O  O   . LYS A 1 150 ? -21.583 -10.198 6.336   1.00 14.64 ? 154 LYS A O   1 
ATOM   1214 C  CB  . LYS A 1 150 ? -20.944 -10.622 9.119   1.00 14.04 ? 154 LYS A CB  1 
ATOM   1215 C  CG  . LYS A 1 150 ? -21.520 -9.416  9.863   1.00 16.21 ? 154 LYS A CG  1 
ATOM   1216 C  CD  . LYS A 1 150 ? -22.360 -9.823  11.072  1.00 15.80 ? 154 LYS A CD  1 
ATOM   1217 C  CE  . LYS A 1 150 ? -22.644 -8.667  12.024  1.00 18.24 ? 154 LYS A CE  1 
ATOM   1218 N  NZ  . LYS A 1 150 ? -23.648 -9.031  13.047  1.00 21.94 ? 154 LYS A NZ  1 
ATOM   1219 N  N   . PRO A 1 151 ? -23.727 -10.511 6.810   1.00 17.08 ? 155 PRO A N   1 
ATOM   1220 C  CA  . PRO A 1 151 ? -24.123 -9.872  5.545   1.00 17.60 ? 155 PRO A CA  1 
ATOM   1221 C  C   . PRO A 1 151 ? -23.630 -8.428  5.435   1.00 16.13 ? 155 PRO A C   1 
ATOM   1222 O  O   . PRO A 1 151 ? -23.193 -8.012  4.363   1.00 15.97 ? 155 PRO A O   1 
ATOM   1223 C  CB  . PRO A 1 151 ? -25.658 -10.003 5.585   1.00 18.80 ? 155 PRO A CB  1 
ATOM   1224 C  CG  . PRO A 1 151 ? -25.894 -11.175 6.548   1.00 21.22 ? 155 PRO A CG  1 
ATOM   1225 C  CD  . PRO A 1 151 ? -24.861 -10.955 7.639   1.00 19.79 ? 155 PRO A CD  1 
ATOM   1226 N  N   . GLY A 1 152 ? -23.633 -7.715  6.572   1.00 14.89 ? 156 GLY A N   1 
ATOM   1227 C  CA  . GLY A 1 152 ? -23.166 -6.329  6.651   1.00 16.15 ? 156 GLY A CA  1 
ATOM   1228 C  C   . GLY A 1 152 ? -21.665 -6.166  6.353   1.00 16.03 ? 156 GLY A C   1 
ATOM   1229 O  O   . GLY A 1 152 ? -21.181 -5.043  6.137   1.00 17.24 ? 156 GLY A O   1 
ATOM   1230 N  N   . LEU A 1 153 ? -20.916 -7.283  6.323   1.00 13.99 ? 157 LEU A N   1 
ATOM   1231 C  CA  . LEU A 1 153 ? -19.497 -7.244  6.018   1.00 13.01 ? 157 LEU A CA  1 
ATOM   1232 C  C   . LEU A 1 153 ? -19.246 -7.435  4.540   1.00 12.10 ? 157 LEU A C   1 
ATOM   1233 O  O   . LEU A 1 153 ? -18.158 -7.161  4.027   1.00 12.29 ? 157 LEU A O   1 
ATOM   1234 C  CB  . LEU A 1 153 ? -18.740 -8.283  6.875   1.00 12.13 ? 157 LEU A CB  1 
ATOM   1235 C  CG  . LEU A 1 153 ? -17.243 -8.392  6.618   1.00 12.22 ? 157 LEU A CG  1 
ATOM   1236 C  CD1 . LEU A 1 153 ? -16.543 -7.081  7.058   1.00 13.15 ? 157 LEU A CD1 1 
ATOM   1237 C  CD2 . LEU A 1 153 ? -16.645 -9.552  7.428   1.00 11.93 ? 157 LEU A CD2 1 
ATOM   1238 N  N   . GLN A 1 154 ? -20.277 -7.928  3.804   1.00 14.46 ? 158 GLN A N   1 
ATOM   1239 C  CA  . GLN A 1 154 ? -19.954 -8.427  2.479   1.00 16.38 ? 158 GLN A CA  1 
ATOM   1240 C  C   . GLN A 1 154 ? -19.569 -7.326  1.491   1.00 13.18 ? 158 GLN A C   1 
ATOM   1241 O  O   . GLN A 1 154 ? -18.671 -7.542  0.671   1.00 14.11 ? 158 GLN A O   1 
ATOM   1242 C  CB  . GLN A 1 154 ? -21.087 -9.307  1.955   1.00 17.17 ? 158 GLN A CB  1 
ATOM   1243 C  CG  . GLN A 1 154 ? -20.703 -10.052 0.675   1.00 18.83 ? 158 GLN A CG  1 
ATOM   1244 C  CD  . GLN A 1 154 ? -19.585 -11.044 0.869   1.00 18.35 ? 158 GLN A CD  1 
ATOM   1245 O  OE1 . GLN A 1 154 ? -19.436 -11.663 1.934   1.00 18.71 ? 158 GLN A OE1 1 
ATOM   1246 N  NE2 . GLN A 1 154 ? -18.769 -11.219 -0.154  1.00 18.93 ? 158 GLN A NE2 1 
ATOM   1247 N  N   . LYS A 1 155 ? -20.111 -6.109  1.640   1.00 15.59 ? 159 LYS A N   1 
ATOM   1248 C  CA  . LYS A 1 155 ? -19.686 -5.034  0.752   1.00 15.03 ? 159 LYS A CA  1 
ATOM   1249 C  C   . LYS A 1 155 ? -18.192 -4.734  0.913   1.00 15.34 ? 159 LYS A C   1 
ATOM   1250 O  O   . LYS A 1 155 ? -17.508 -4.429  -0.064  1.00 14.50 ? 159 LYS A O   1 
ATOM   1251 C  CB  . LYS A 1 155 ? -20.492 -3.755  1.032   1.00 18.37 ? 159 LYS A CB  1 
ATOM   1252 C  CG  . LYS A 1 155 ? -21.939 -3.776  0.541   1.00 22.28 ? 159 LYS A CG  1 
ATOM   1253 C  CD  . LYS A 1 155 ? -22.512 -2.371  0.089   0.00 37.08 ? 159 LYS A CD  1 
ATOM   1254 C  CE  . LYS A 1 155 ? -21.336 -1.351  0.354   0.00 46.90 ? 159 LYS A CE  1 
ATOM   1255 N  NZ  . LYS A 1 155 ? -21.134 -0.090  -0.496  0.00 64.84 ? 159 LYS A NZ  1 
ATOM   1256 N  N   . VAL A 1 156 ? -17.683 -4.846  2.156   1.00 14.18 ? 160 VAL A N   1 
ATOM   1257 C  CA  . VAL A 1 156 ? -16.251 -4.710  2.388   1.00 14.15 ? 160 VAL A CA  1 
ATOM   1258 C  C   . VAL A 1 156 ? -15.441 -5.790  1.684   1.00 13.63 ? 160 VAL A C   1 
ATOM   1259 O  O   . VAL A 1 156 ? -14.470 -5.510  0.987   1.00 14.39 ? 160 VAL A O   1 
ATOM   1260 C  CB  . VAL A 1 156 ? -15.949 -4.666  3.899   1.00 13.66 ? 160 VAL A CB  1 
ATOM   1261 C  CG1 . VAL A 1 156 ? -14.444 -4.697  4.193   1.00 13.87 ? 160 VAL A CG1 1 
ATOM   1262 C  CG2 . VAL A 1 156 ? -16.563 -3.433  4.510   1.00 14.77 ? 160 VAL A CG2 1 
ATOM   1263 N  N   . VAL A 1 157 ? -15.814 -7.056  1.888   1.00 13.56 ? 161 VAL A N   1 
ATOM   1264 C  CA  . VAL A 1 157 ? -15.061 -8.178  1.363   1.00 15.21 ? 161 VAL A CA  1 
ATOM   1265 C  C   . VAL A 1 157 ? -15.061 -8.116  -0.168  1.00 14.96 ? 161 VAL A C   1 
ATOM   1266 O  O   . VAL A 1 157 ? -14.043 -8.345  -0.802  1.00 15.31 ? 161 VAL A O   1 
ATOM   1267 C  CB  . VAL A 1 157 ? -15.696 -9.466  1.937   1.00 16.86 ? 161 VAL A CB  1 
ATOM   1268 C  CG1 . VAL A 1 157 ? -15.524 -10.708 1.087   1.00 21.24 ? 161 VAL A CG1 1 
ATOM   1269 C  CG2 . VAL A 1 157 ? -15.235 -9.676  3.371   1.00 18.77 ? 161 VAL A CG2 1 
ATOM   1270 N  N   . ASP A 1 158 ? -16.176 -7.639  -0.726  1.00 17.74 ? 162 ASP A N   1 
ATOM   1271 C  CA  . ASP A 1 158 ? -16.286 -7.669  -2.183  1.00 20.25 ? 162 ASP A CA  1 
ATOM   1272 C  C   . ASP A 1 158 ? -15.358 -6.682  -2.904  1.00 20.78 ? 162 ASP A C   1 
ATOM   1273 O  O   . ASP A 1 158 ? -15.037 -6.919  -4.065  1.00 24.12 ? 162 ASP A O   1 
ATOM   1274 C  CB  . ASP A 1 158 ? -17.723 -7.509  -2.647  1.00 22.60 ? 162 ASP A CB  1 
ATOM   1275 C  CG  . ASP A 1 158 ? -18.432 -8.842  -2.689  1.00 25.46 ? 162 ASP A CG  1 
ATOM   1276 O  OD1 . ASP A 1 158 ? -17.729 -9.908  -2.699  1.00 29.29 ? 162 ASP A OD1 1 
ATOM   1277 O  OD2 . ASP A 1 158 ? -19.666 -8.812  -2.669  1.00 28.12 ? 162 ASP A OD2 1 
ATOM   1278 N  N   . VAL A 1 159 ? -14.946 -5.592  -2.232  1.00 17.00 ? 163 VAL A N   1 
ATOM   1279 C  CA  . VAL A 1 159 ? -14.128 -4.530  -2.821  1.00 17.72 ? 163 VAL A CA  1 
ATOM   1280 C  C   . VAL A 1 159 ? -12.631 -4.812  -2.623  1.00 15.53 ? 163 VAL A C   1 
ATOM   1281 O  O   . VAL A 1 159 ? -11.780 -4.119  -3.175  1.00 16.17 ? 163 VAL A O   1 
ATOM   1282 C  CB  . VAL A 1 159 ? -14.583 -3.169  -2.253  1.00 18.82 ? 163 VAL A CB  1 
ATOM   1283 C  CG1 . VAL A 1 159 ? -13.806 -2.815  -0.996  1.00 18.42 ? 163 VAL A CG1 1 
ATOM   1284 C  CG2 . VAL A 1 159 ? -14.483 -2.017  -3.255  1.00 22.91 ? 163 VAL A CG2 1 
ATOM   1285 N  N   . LEU A 1 160 ? -12.263 -5.809  -1.783  1.00 15.94 ? 164 LEU A N   1 
ATOM   1286 C  CA  . LEU A 1 160 ? -10.869 -6.021  -1.425  1.00 15.77 ? 164 LEU A CA  1 
ATOM   1287 C  C   . LEU A 1 160 ? -9.948  -6.313  -2.613  1.00 16.81 ? 164 LEU A C   1 
ATOM   1288 O  O   . LEU A 1 160 ? -8.819  -5.889  -2.585  1.00 17.47 ? 164 LEU A O   1 
ATOM   1289 C  CB  . LEU A 1 160 ? -10.727 -7.096  -0.363  1.00 14.00 ? 164 LEU A CB  1 
ATOM   1290 C  CG  . LEU A 1 160 ? -11.340 -6.748  0.997   1.00 13.87 ? 164 LEU A CG  1 
ATOM   1291 C  CD1 . LEU A 1 160 ? -11.149 -7.911  1.966   1.00 14.49 ? 164 LEU A CD1 1 
ATOM   1292 C  CD2 . LEU A 1 160 ? -10.714 -5.481  1.577   1.00 14.23 ? 164 LEU A CD2 1 
ATOM   1293 N  N   . ASP A 1 161 ? -10.425 -7.049  -3.628  1.00 20.01 ? 165 ASP A N   1 
ATOM   1294 C  CA  . ASP A 1 161 ? -9.553  -7.367  -4.749  1.00 23.38 ? 165 ASP A CA  1 
ATOM   1295 C  C   . ASP A 1 161 ? -9.159  -6.081  -5.500  1.00 24.68 ? 165 ASP A C   1 
ATOM   1296 O  O   . ASP A 1 161 ? -8.148  -6.068  -6.210  1.00 31.60 ? 165 ASP A O   1 
ATOM   1297 C  CB  . ASP A 1 161 ? -10.256 -8.375  -5.658  1.00 25.77 ? 165 ASP A CB  1 
ATOM   1298 C  CG  . ASP A 1 161 ? -11.258 -7.605  -6.474  1.00 27.95 ? 165 ASP A CG  1 
ATOM   1299 O  OD1 . ASP A 1 161 ? -12.279 -7.179  -5.924  1.00 31.08 ? 165 ASP A OD1 1 
ATOM   1300 O  OD2 . ASP A 1 161 ? -10.945 -7.333  -7.648  1.00 33.61 ? 165 ASP A OD2 1 
ATOM   1301 N  N   . SER A 1 162 ? -9.875  -4.969  -5.299  1.00 24.84 ? 166 SER A N   1 
ATOM   1302 C  CA  . SER A 1 162 ? -9.483  -3.710  -5.919  1.00 24.92 ? 166 SER A CA  1 
ATOM   1303 C  C   . SER A 1 162 ? -8.435  -2.923  -5.117  1.00 25.18 ? 166 SER A C   1 
ATOM   1304 O  O   . SER A 1 162 ? -7.880  -1.937  -5.631  1.00 21.22 ? 166 SER A O   1 
ATOM   1305 C  CB  . SER A 1 162 ? -10.680 -2.879  -6.272  1.00 29.33 ? 166 SER A CB  1 
ATOM   1306 O  OG  . SER A 1 162 ? -11.064 -2.072  -5.179  1.00 31.41 ? 166 SER A OG  1 
ATOM   1307 N  N   . ILE A 1 163 ? -8.140  -3.355  -3.876  1.00 18.68 ? 167 ILE A N   1 
ATOM   1308 C  CA  . ILE A 1 163 ? -7.101  -2.706  -3.075  1.00 16.94 ? 167 ILE A CA  1 
ATOM   1309 C  C   . ILE A 1 163 ? -6.100  -3.746  -2.586  1.00 16.49 ? 167 ILE A C   1 
ATOM   1310 O  O   . ILE A 1 163 ? -5.703  -3.793  -1.421  1.00 17.60 ? 167 ILE A O   1 
ATOM   1311 C  CB  . ILE A 1 163 ? -7.695  -1.901  -1.892  1.00 16.98 ? 167 ILE A CB  1 
ATOM   1312 C  CG1 . ILE A 1 163 ? -8.520  -2.803  -0.978  1.00 17.94 ? 167 ILE A CG1 1 
ATOM   1313 C  CG2 . ILE A 1 163 ? -8.479  -0.689  -2.388  1.00 19.76 ? 167 ILE A CG2 1 
ATOM   1314 C  CD1 . ILE A 1 163 ? -8.496  -2.329  0.462   1.00 17.61 ? 167 ILE A CD1 1 
ATOM   1315 N  N   . LYS A 1 164 ? -5.733  -4.669  -3.473  1.00 16.72 ? 168 LYS A N   1 
ATOM   1316 C  CA  . LYS A 1 164 ? -4.922  -5.785  -3.032  1.00 17.97 ? 168 LYS A CA  1 
ATOM   1317 C  C   . LYS A 1 164 ? -3.572  -5.407  -2.414  1.00 18.42 ? 168 LYS A C   1 
ATOM   1318 O  O   . LYS A 1 164 ? -3.137  -6.077  -1.487  1.00 16.98 ? 168 LYS A O   1 
ATOM   1319 C  CB  . LYS A 1 164 ? -4.671  -6.695  -4.236  1.00 18.00 ? 168 LYS A CB  1 
ATOM   1320 C  CG  . LYS A 1 164 ? -3.876  -7.935  -3.893  1.00 21.80 ? 168 LYS A CG  1 
ATOM   1321 C  CD  . LYS A 1 164 ? -3.423  -8.664  -5.154  1.00 24.33 ? 168 LYS A CD  1 
ATOM   1322 C  CE  . LYS A 1 164 ? -2.700  -9.962  -4.861  1.00 29.63 ? 168 LYS A CE  1 
ATOM   1323 N  NZ  . LYS A 1 164 ? -3.616  -11.005 -4.338  1.00 39.18 ? 168 LYS A NZ  1 
ATOM   1324 N  N   . THR A 1 165 ? -2.878  -4.385  -2.959  1.00 17.66 ? 169 THR A N   1 
ATOM   1325 C  CA  . THR A 1 165 ? -1.495  -4.076  -2.617  1.00 18.73 ? 169 THR A CA  1 
ATOM   1326 C  C   . THR A 1 165 ? -1.404  -2.724  -1.900  1.00 17.24 ? 169 THR A C   1 
ATOM   1327 O  O   . THR A 1 165 ? -2.271  -1.862  -2.037  1.00 18.63 ? 169 THR A O   1 
ATOM   1328 C  CB  . THR A 1 165 ? -0.610  -4.126  -3.891  1.00 18.72 ? 169 THR A CB  1 
ATOM   1329 O  OG1 . THR A 1 165 ? -1.266  -3.287  -4.838  1.00 21.01 ? 169 THR A OG1 1 
ATOM   1330 C  CG2 . THR A 1 165 ? -0.459  -5.543  -4.400  1.00 20.92 ? 169 THR A CG2 1 
ATOM   1331 N  N   . LYS A 1 166 ? -0.316  -2.552  -1.152  1.00 19.63 ? 170 LYS A N   1 
ATOM   1332 C  CA  . LYS A 1 166 ? 0.046   -1.335  -0.423  1.00 20.15 ? 170 LYS A CA  1 
ATOM   1333 C  C   . LYS A 1 166 ? -0.097  -0.093  -1.302  1.00 24.41 ? 170 LYS A C   1 
ATOM   1334 O  O   . LYS A 1 166 ? 0.406   -0.082  -2.434  1.00 27.94 ? 170 LYS A O   1 
ATOM   1335 C  CB  . LYS A 1 166 ? 1.444   -1.475  0.186   1.00 21.89 ? 170 LYS A CB  1 
ATOM   1336 C  CG  . LYS A 1 166 ? 1.912   -0.241  0.972   1.00 23.49 ? 170 LYS A CG  1 
ATOM   1337 C  CD  . LYS A 1 166 ? 3.325   -0.370  1.467   1.00 30.59 ? 170 LYS A CD  1 
ATOM   1338 C  CE  . LYS A 1 166 ? 3.740   0.863   2.254   1.00 37.65 ? 170 LYS A CE  1 
ATOM   1339 N  NZ  . LYS A 1 166 ? 5.212   1.029   2.347   1.00 42.97 ? 170 LYS A NZ  1 
ATOM   1340 N  N   . GLY A 1 167 ? -0.864  0.886   -0.813  1.00 22.35 ? 171 GLY A N   1 
ATOM   1341 C  CA  . GLY A 1 167 ? -1.126  2.170   -1.463  1.00 24.04 ? 171 GLY A CA  1 
ATOM   1342 C  C   . GLY A 1 167 ? -2.412  2.275   -2.288  1.00 27.17 ? 171 GLY A C   1 
ATOM   1343 O  O   . GLY A 1 167 ? -2.847  3.389   -2.614  1.00 32.25 ? 171 GLY A O   1 
ATOM   1344 N  N   . LYS A 1 168 ? -3.068  1.147   -2.614  1.00 21.36 ? 172 LYS A N   1 
ATOM   1345 C  CA  . LYS A 1 168 ? -4.294  1.209   -3.389  1.00 22.38 ? 172 LYS A CA  1 
ATOM   1346 C  C   . LYS A 1 168 ? -5.476  1.689   -2.550  1.00 21.70 ? 172 LYS A C   1 
ATOM   1347 O  O   . LYS A 1 168 ? -5.593  1.320   -1.377  1.00 22.35 ? 172 LYS A O   1 
ATOM   1348 C  CB  . LYS A 1 168 ? -4.581  -0.148  -4.044  1.00 22.53 ? 172 LYS A CB  1 
ATOM   1349 C  CG  . LYS A 1 168 ? -3.461  -0.660  -4.939  1.00 28.25 ? 172 LYS A CG  1 
ATOM   1350 C  CD  . LYS A 1 168 ? -3.878  -1.791  -5.858  1.00 35.76 ? 172 LYS A CD  1 
ATOM   1351 C  CE  . LYS A 1 168 ? -4.090  -1.354  -7.296  1.00 41.92 ? 172 LYS A CE  1 
ATOM   1352 N  NZ  . LYS A 1 168 ? -5.353  -1.893  -7.870  1.00 41.92 ? 172 LYS A NZ  1 
ATOM   1353 N  N   . SER A 1 169 ? -6.371  2.451   -3.183  1.00 22.17 ? 173 SER A N   1 
ATOM   1354 C  CA  . SER A 1 169 ? -7.619  2.897   -2.597  1.00 22.04 ? 173 SER A CA  1 
ATOM   1355 C  C   . SER A 1 169 ? -8.780  2.771   -3.581  1.00 23.26 ? 173 SER A C   1 
ATOM   1356 O  O   . SER A 1 169 ? -8.601  2.675   -4.809  1.00 22.42 ? 173 SER A O   1 
ATOM   1357 C  CB  . SER A 1 169 ? -7.500  4.300   -2.089  1.00 23.24 ? 173 SER A CB  1 
ATOM   1358 O  OG  . SER A 1 169 ? -7.501  5.193   -3.202  1.00 25.54 ? 173 SER A OG  1 
ATOM   1359 N  N   . ALA A 1 170 ? -9.984  2.767   -3.029  1.00 23.33 ? 174 ALA A N   1 
ATOM   1360 C  CA  . ALA A 1 170 ? -11.188 2.787   -3.835  1.00 25.12 ? 174 ALA A CA  1 
ATOM   1361 C  C   . ALA A 1 170 ? -12.272 3.598   -3.148  1.00 26.02 ? 174 ALA A C   1 
ATOM   1362 O  O   . ALA A 1 170 ? -12.396 3.616   -1.918  1.00 21.33 ? 174 ALA A O   1 
ATOM   1363 C  CB  . ALA A 1 170 ? -11.657 1.391   -4.098  1.00 23.75 ? 174 ALA A CB  1 
ATOM   1364 N  N   . ASP A 1 171 ? -13.112 4.218   -3.978  1.00 24.89 ? 175 ASP A N   1 
ATOM   1365 C  CA  . ASP A 1 171 ? -14.289 4.885   -3.462  1.00 27.51 ? 175 ASP A CA  1 
ATOM   1366 C  C   . ASP A 1 171 ? -15.061 3.851   -2.654  1.00 25.32 ? 175 ASP A C   1 
ATOM   1367 O  O   . ASP A 1 171 ? -15.141 2.677   -3.025  1.00 26.14 ? 175 ASP A O   1 
ATOM   1368 C  CB  . ASP A 1 171 ? -15.144 5.482   -4.589  1.00 32.27 ? 175 ASP A CB  1 
ATOM   1369 C  CG  . ASP A 1 171 ? -14.362 6.470   -5.447  1.00 39.84 ? 175 ASP A CG  1 
ATOM   1370 O  OD1 . ASP A 1 171 ? -13.523 7.204   -4.880  1.00 40.70 ? 175 ASP A OD1 1 
ATOM   1371 O  OD2 . ASP A 1 171 ? -14.587 6.497   -6.688  1.00 44.84 ? 175 ASP A OD2 1 
ATOM   1372 N  N   . PHE A 1 172 ? -15.611 4.294   -1.528  1.00 20.42 ? 176 PHE A N   1 
ATOM   1373 C  CA  . PHE A 1 172 ? -16.380 3.357   -0.720  1.00 19.15 ? 176 PHE A CA  1 
ATOM   1374 C  C   . PHE A 1 172 ? -17.443 4.154   -0.004  1.00 20.18 ? 176 PHE A C   1 
ATOM   1375 O  O   . PHE A 1 172 ? -17.293 4.466   1.162   1.00 22.83 ? 176 PHE A O   1 
ATOM   1376 C  CB  . PHE A 1 172 ? -15.437 2.560   0.201   1.00 17.80 ? 176 PHE A CB  1 
ATOM   1377 C  CG  . PHE A 1 172 ? -16.032 1.277   0.744   1.00 16.16 ? 176 PHE A CG  1 
ATOM   1378 C  CD1 . PHE A 1 172 ? -16.261 0.190   -0.089  1.00 16.88 ? 176 PHE A CD1 1 
ATOM   1379 C  CD2 . PHE A 1 172 ? -16.399 1.152   2.074   1.00 14.96 ? 176 PHE A CD2 1 
ATOM   1380 C  CE1 . PHE A 1 172 ? -16.812 -0.992  0.408   1.00 17.93 ? 176 PHE A CE1 1 
ATOM   1381 C  CE2 . PHE A 1 172 ? -16.959 -0.011  2.585   1.00 16.65 ? 176 PHE A CE2 1 
ATOM   1382 C  CZ  . PHE A 1 172 ? -17.137 -1.100  1.750   1.00 17.38 ? 176 PHE A CZ  1 
ATOM   1383 N  N   . THR A 1 173 ? -18.512 4.506   -0.732  1.00 17.52 ? 177 THR A N   1 
ATOM   1384 C  CA  . THR A 1 173 ? -19.578 5.344   -0.217  1.00 17.23 ? 177 THR A CA  1 
ATOM   1385 C  C   . THR A 1 173 ? -20.745 4.475   0.239   1.00 15.22 ? 177 THR A C   1 
ATOM   1386 O  O   . THR A 1 173 ? -20.907 3.330   -0.203  1.00 15.46 ? 177 THR A O   1 
ATOM   1387 C  CB  . THR A 1 173 ? -19.944 6.433   -1.243  1.00 19.68 ? 177 THR A CB  1 
ATOM   1388 O  OG1 . THR A 1 173 ? -20.475 5.763   -2.378  1.00 21.00 ? 177 THR A OG1 1 
ATOM   1389 C  CG2 . THR A 1 173 ? -18.764 7.279   -1.664  1.00 21.71 ? 177 THR A CG2 1 
ATOM   1390 N  N   . ASN A 1 174 ? -21.574 5.063   1.099   1.00 15.57 ? 178 ASN A N   1 
ATOM   1391 C  CA  . ASN A 1 174 ? -22.858 4.555   1.534   1.00 16.42 ? 178 ASN A CA  1 
ATOM   1392 C  C   . ASN A 1 174 ? -22.698 3.223   2.271   1.00 17.14 ? 178 ASN A C   1 
ATOM   1393 O  O   . ASN A 1 174 ? -23.615 2.418   2.263   1.00 17.96 ? 178 ASN A O   1 
ATOM   1394 C  CB  . ASN A 1 174 ? -23.832 4.442   0.366   1.00 15.95 ? 178 ASN A CB  1 
ATOM   1395 C  CG  . ASN A 1 174 ? -24.079 5.806   -0.264  1.00 18.51 ? 178 ASN A CG  1 
ATOM   1396 O  OD1 . ASN A 1 174 ? -24.749 6.630   0.339   1.00 19.62 ? 178 ASN A OD1 1 
ATOM   1397 N  ND2 . ASN A 1 174 ? -23.465 6.058   -1.418  1.00 18.08 ? 178 ASN A ND2 1 
ATOM   1398 N  N   . PHE A 1 175 ? -21.548 3.019   2.907   1.00 15.98 ? 179 PHE A N   1 
ATOM   1399 C  CA  . PHE A 1 175 ? -21.375 1.857   3.774   1.00 14.20 ? 179 PHE A CA  1 
ATOM   1400 C  C   . PHE A 1 175 ? -21.852 2.173   5.175   1.00 14.91 ? 179 PHE A C   1 
ATOM   1401 O  O   . PHE A 1 175 ? -21.459 3.197   5.742   1.00 17.17 ? 179 PHE A O   1 
ATOM   1402 C  CB  . PHE A 1 175 ? -19.933 1.397   3.838   1.00 13.35 ? 179 PHE A CB  1 
ATOM   1403 C  CG  . PHE A 1 175 ? -19.792 0.160   4.697   1.00 14.84 ? 179 PHE A CG  1 
ATOM   1404 C  CD1 . PHE A 1 175 ? -20.229 -1.067  4.230   1.00 15.62 ? 179 PHE A CD1 1 
ATOM   1405 C  CD2 . PHE A 1 175 ? -19.339 0.258   6.013   1.00 14.52 ? 179 PHE A CD2 1 
ATOM   1406 C  CE1 . PHE A 1 175 ? -20.125 -2.201  5.023   1.00 16.46 ? 179 PHE A CE1 1 
ATOM   1407 C  CE2 . PHE A 1 175 ? -19.240 -0.874  6.797   1.00 14.07 ? 179 PHE A CE2 1 
ATOM   1408 C  CZ  . PHE A 1 175 ? -19.663 -2.084  6.329   1.00 14.12 ? 179 PHE A CZ  1 
ATOM   1409 N  N   . ASP A 1 176 ? -22.707 1.287   5.691   1.00 14.65 ? 180 ASP A N   1 
ATOM   1410 C  CA  . ASP A 1 176 ? -23.319 1.529   6.980   1.00 14.91 ? 180 ASP A CA  1 
ATOM   1411 C  C   . ASP A 1 176 ? -22.647 0.667   8.044   1.00 14.78 ? 180 ASP A C   1 
ATOM   1412 O  O   . ASP A 1 176 ? -22.826 -0.546  8.066   1.00 14.59 ? 180 ASP A O   1 
ATOM   1413 C  CB  . ASP A 1 176 ? -24.786 1.128   6.922   1.00 17.74 ? 180 ASP A CB  1 
ATOM   1414 C  CG  . ASP A 1 176 ? -25.583 1.573   8.131   1.00 22.29 ? 180 ASP A CG  1 
ATOM   1415 O  OD1 . ASP A 1 176 ? -25.008 1.811   9.218   1.00 16.53 ? 180 ASP A OD1 1 
ATOM   1416 O  OD2 . ASP A 1 176 ? -26.796 1.777   7.957   1.00 25.81 ? 180 ASP A OD2 1 
ATOM   1417 N  N   . PRO A 1 177 ? -21.868 1.260   8.977   1.00 12.69 ? 181 PRO A N   1 
ATOM   1418 C  CA  . PRO A 1 177 ? -21.134 0.463   9.970   1.00 12.35 ? 181 PRO A CA  1 
ATOM   1419 C  C   . PRO A 1 177 ? -22.023 -0.207  11.000  1.00 12.57 ? 181 PRO A C   1 
ATOM   1420 O  O   . PRO A 1 177 ? -21.566 -1.120  11.696  1.00 11.45 ? 181 PRO A O   1 
ATOM   1421 C  CB  . PRO A 1 177 ? -20.104 1.490   10.485  1.00 12.06 ? 181 PRO A CB  1 
ATOM   1422 C  CG  . PRO A 1 177 ? -20.802 2.815   10.386  1.00 13.08 ? 181 PRO A CG  1 
ATOM   1423 C  CD  . PRO A 1 177 ? -21.631 2.716   9.122   1.00 12.92 ? 181 PRO A CD  1 
ATOM   1424 N  N   . ARG A 1 178 ? -23.309 0.158   11.054  1.00 11.98 ? 182 ARG A N   1 
ATOM   1425 C  CA  . ARG A 1 178 ? -24.185 -0.544  11.987  1.00 13.73 ? 182 ARG A CA  1 
ATOM   1426 C  C   . ARG A 1 178 ? -24.292 -2.023  11.597  1.00 12.83 ? 182 ARG A C   1 
ATOM   1427 O  O   . ARG A 1 178 ? -24.729 -2.835  12.421  1.00 13.11 ? 182 ARG A O   1 
ATOM   1428 C  CB  . ARG A 1 178 ? -25.563 0.136   12.006  1.00 14.11 ? 182 ARG A CB  1 
ATOM   1429 C  CG  . ARG A 1 178 ? -25.504 1.521   12.639  1.00 17.40 ? 182 ARG A CG  1 
ATOM   1430 C  CD  . ARG A 1 178 ? -26.791 2.305   12.501  1.00 18.21 ? 182 ARG A CD  1 
ATOM   1431 N  NE  . ARG A 1 178 ? -27.221 2.477   11.130  1.00 19.21 ? 182 ARG A NE  1 
ATOM   1432 C  CZ  . ARG A 1 178 ? -28.307 3.175   10.797  1.00 25.72 ? 182 ARG A CZ  1 
ATOM   1433 N  NH1 . ARG A 1 178 ? -29.013 3.767   11.746  1.00 22.85 ? 182 ARG A NH1 1 
ATOM   1434 N  NH2 . ARG A 1 178 ? -28.645 3.312   9.521   1.00 27.15 ? 182 ARG A NH2 1 
ATOM   1435 N  N   . GLY A 1 179 ? -23.939 -2.355  10.343  1.00 12.72 ? 183 GLY A N   1 
ATOM   1436 C  CA  . GLY A 1 179 ? -24.008 -3.710  9.806   1.00 13.38 ? 183 GLY A CA  1 
ATOM   1437 C  C   . GLY A 1 179 ? -22.954 -4.620  10.426  1.00 14.52 ? 183 GLY A C   1 
ATOM   1438 O  O   . GLY A 1 179 ? -22.997 -5.835  10.232  1.00 15.42 ? 183 GLY A O   1 
ATOM   1439 N  N   . LEU A 1 180 ? -22.005 -4.016  11.139  1.00 13.18 ? 184 LEU A N   1 
ATOM   1440 C  CA  . LEU A 1 180 ? -20.902 -4.793  11.716  1.00 13.03 ? 184 LEU A CA  1 
ATOM   1441 C  C   . LEU A 1 180 ? -21.091 -5.005  13.209  1.00 12.79 ? 184 LEU A C   1 
ATOM   1442 O  O   . LEU A 1 180 ? -20.190 -5.600  13.828  1.00 13.38 ? 184 LEU A O   1 
ATOM   1443 C  CB  . LEU A 1 180 ? -19.571 -4.061  11.475  1.00 13.53 ? 184 LEU A CB  1 
ATOM   1444 C  CG  . LEU A 1 180 ? -19.204 -3.823  10.005  1.00 13.94 ? 184 LEU A CG  1 
ATOM   1445 C  CD1 . LEU A 1 180 ? -17.999 -2.918  9.872   1.00 15.76 ? 184 LEU A CD1 1 
ATOM   1446 C  CD2 . LEU A 1 180 ? -19.021 -5.136  9.268   1.00 14.35 ? 184 LEU A CD2 1 
ATOM   1447 N  N   . LEU A 1 181 ? -22.183 -4.514  13.814  1.00 11.92 ? 185 LEU A N   1 
ATOM   1448 C  CA  . LEU A 1 181 ? -22.313 -4.588  15.274  1.00 12.13 ? 185 LEU A CA  1 
ATOM   1449 C  C   . LEU A 1 181 ? -22.959 -5.906  15.682  1.00 14.07 ? 185 LEU A C   1 
ATOM   1450 O  O   . LEU A 1 181 ? -23.797 -6.476  14.976  1.00 17.59 ? 185 LEU A O   1 
ATOM   1451 C  CB  . LEU A 1 181 ? -23.157 -3.431  15.813  1.00 12.23 ? 185 LEU A CB  1 
ATOM   1452 C  CG  . LEU A 1 181 ? -22.608 -2.056  15.461  1.00 12.86 ? 185 LEU A CG  1 
ATOM   1453 C  CD1 . LEU A 1 181 ? -23.506 -0.985  16.017  1.00 13.31 ? 185 LEU A CD1 1 
ATOM   1454 C  CD2 . LEU A 1 181 ? -21.164 -1.902  15.980  1.00 13.47 ? 185 LEU A CD2 1 
ATOM   1455 N  N   . PRO A 1 182 ? -22.657 -6.429  16.875  1.00 13.04 ? 186 PRO A N   1 
ATOM   1456 C  CA  . PRO A 1 182 ? -23.445 -7.555  17.368  1.00 12.87 ? 186 PRO A CA  1 
ATOM   1457 C  C   . PRO A 1 182 ? -24.736 -7.023  17.982  1.00 15.00 ? 186 PRO A C   1 
ATOM   1458 O  O   . PRO A 1 182 ? -24.953 -5.809  18.045  1.00 13.42 ? 186 PRO A O   1 
ATOM   1459 C  CB  . PRO A 1 182 ? -22.513 -8.134  18.437  1.00 12.03 ? 186 PRO A CB  1 
ATOM   1460 C  CG  . PRO A 1 182 ? -21.835 -6.918  18.994  1.00 11.68 ? 186 PRO A CG  1 
ATOM   1461 C  CD  . PRO A 1 182 ? -21.553 -6.046  17.760  1.00 11.76 ? 186 PRO A CD  1 
ATOM   1462 N  N   . GLU A 1 183 ? -25.538 -7.945  18.546  1.00 14.38 ? 187 GLU A N   1 
ATOM   1463 C  CA  . GLU A 1 183 ? -26.843 -7.615  19.107  1.00 15.81 ? 187 GLU A CA  1 
ATOM   1464 C  C   . GLU A 1 183 ? -26.657 -6.855  20.409  1.00 14.97 ? 187 GLU A C   1 
ATOM   1465 O  O   . GLU A 1 183 ? -27.270 -5.816  20.620  1.00 17.09 ? 187 GLU A O   1 
ATOM   1466 C  CB  . GLU A 1 183 ? -27.633 -8.927  19.259  1.00 16.03 ? 187 GLU A CB  1 
ATOM   1467 C  CG  . GLU A 1 183 ? -28.793 -8.810  20.196  1.00 21.70 ? 187 GLU A CG  1 
ATOM   1468 C  CD  . GLU A 1 183 ? -29.465 -10.153 20.477  1.00 22.50 ? 187 GLU A CD  1 
ATOM   1469 O  OE1 . GLU A 1 183 ? -29.301 -11.078 19.633  1.00 24.12 ? 187 GLU A OE1 1 
ATOM   1470 O  OE2 . GLU A 1 183 ? -30.145 -10.258 21.551  1.00 29.18 ? 187 GLU A OE2 1 
ATOM   1471 N  N   . SER A 1 184 ? -25.763 -7.336  21.295  1.00 13.47 ? 188 SER A N   1 
ATOM   1472 C  CA  . SER A 1 184 ? -25.531 -6.723  22.588  1.00 14.74 ? 188 SER A CA  1 
ATOM   1473 C  C   . SER A 1 184 ? -24.399 -5.707  22.514  1.00 14.39 ? 188 SER A C   1 
ATOM   1474 O  O   . SER A 1 184 ? -23.409 -5.942  21.836  1.00 14.70 ? 188 SER A O   1 
ATOM   1475 C  CB  . SER A 1 184 ? -25.108 -7.777  23.597  1.00 16.81 ? 188 SER A CB  1 
ATOM   1476 O  OG  . SER A 1 184 ? -24.879 -7.196  24.875  1.00 15.35 ? 188 SER A OG  1 
ATOM   1477 N  N   . LEU A 1 185 ? -24.567 -4.590  23.220  1.00 13.66 ? 189 LEU A N   1 
ATOM   1478 C  CA  . LEU A 1 185 ? -23.491 -3.620  23.425  1.00 15.73 ? 189 LEU A CA  1 
ATOM   1479 C  C   . LEU A 1 185 ? -22.856 -3.725  24.821  1.00 14.03 ? 189 LEU A C   1 
ATOM   1480 O  O   . LEU A 1 185 ? -22.161 -2.794  25.253  1.00 15.27 ? 189 LEU A O   1 
ATOM   1481 C  CB  . LEU A 1 185 ? -24.005 -2.195  23.164  1.00 14.99 ? 189 LEU A CB  1 
ATOM   1482 C  CG  . LEU A 1 185 ? -24.532 -1.919  21.763  1.00 16.73 ? 189 LEU A CG  1 
ATOM   1483 C  CD1 . LEU A 1 185 ? -25.074 -0.499  21.718  1.00 19.48 ? 189 LEU A CD1 1 
ATOM   1484 C  CD2 . LEU A 1 185 ? -23.392 -2.057  20.737  1.00 16.65 ? 189 LEU A CD2 1 
ATOM   1485 N  N   . ASP A 1 186 ? -23.031 -4.852  25.540  1.00 13.72 ? 190 ASP A N   1 
ATOM   1486 C  CA  . ASP A 1 186 ? -22.269 -5.046  26.776  1.00 14.48 ? 190 ASP A CA  1 
ATOM   1487 C  C   . ASP A 1 186 ? -20.763 -5.008  26.458  1.00 12.57 ? 190 ASP A C   1 
ATOM   1488 O  O   . ASP A 1 186 ? -20.328 -5.536  25.428  1.00 12.22 ? 190 ASP A O   1 
ATOM   1489 C  CB  . ASP A 1 186 ? -22.551 -6.413  27.398  1.00 16.56 ? 190 ASP A CB  1 
ATOM   1490 C  CG  . ASP A 1 186 ? -23.910 -6.532  28.092  1.00 19.99 ? 190 ASP A CG  1 
ATOM   1491 O  OD1 . ASP A 1 186 ? -24.498 -5.515  28.413  1.00 21.47 ? 190 ASP A OD1 1 
ATOM   1492 O  OD2 . ASP A 1 186 ? -24.338 -7.649  28.300  1.00 23.72 ? 190 ASP A OD2 1 
ATOM   1493 N  N   . TYR A 1 187 ? -19.997 -4.400  27.378  1.00 10.77 ? 191 TYR A N   1 
ATOM   1494 C  CA  . TYR A 1 187 ? -18.585 -4.168  27.050  1.00 10.66 ? 191 TYR A CA  1 
ATOM   1495 C  C   . TYR A 1 187 ? -17.669 -4.268  28.268  1.00 11.79 ? 191 TYR A C   1 
ATOM   1496 O  O   . TYR A 1 187 ? -18.113 -4.156  29.419  1.00 11.88 ? 191 TYR A O   1 
ATOM   1497 C  CB  . TYR A 1 187 ? -18.423 -2.782  26.406  1.00 11.23 ? 191 TYR A CB  1 
ATOM   1498 C  CG  . TYR A 1 187 ? -18.843 -1.625  27.286  1.00 10.63 ? 191 TYR A CG  1 
ATOM   1499 C  CD1 . TYR A 1 187 ? -17.928 -1.032  28.165  1.00 10.64 ? 191 TYR A CD1 1 
ATOM   1500 C  CD2 . TYR A 1 187 ? -20.151 -1.170  27.282  1.00 11.31 ? 191 TYR A CD2 1 
ATOM   1501 C  CE1 . TYR A 1 187 ? -18.294 0.002   29.017  1.00 13.79 ? 191 TYR A CE1 1 
ATOM   1502 C  CE2 . TYR A 1 187 ? -20.522 -0.099  28.089  1.00 13.25 ? 191 TYR A CE2 1 
ATOM   1503 C  CZ  . TYR A 1 187 ? -19.602 0.466   28.963  1.00 13.84 ? 191 TYR A CZ  1 
ATOM   1504 O  OH  . TYR A 1 187 ? -20.003 1.467   29.783  1.00 13.93 ? 191 TYR A OH  1 
ATOM   1505 N  N   . TRP A 1 188 ? -16.356 -4.442  27.983  1.00 9.65  ? 192 TRP A N   1 
ATOM   1506 C  CA  . TRP A 1 188 ? -15.271 -4.171  28.926  1.00 9.73  ? 192 TRP A CA  1 
ATOM   1507 C  C   . TRP A 1 188 ? -14.604 -2.854  28.555  1.00 10.62 ? 192 TRP A C   1 
ATOM   1508 O  O   . TRP A 1 188 ? -14.588 -2.489  27.381  1.00 10.91 ? 192 TRP A O   1 
ATOM   1509 C  CB  . TRP A 1 188 ? -14.225 -5.290  28.848  1.00 10.37 ? 192 TRP A CB  1 
ATOM   1510 C  CG  . TRP A 1 188 ? -14.730 -6.637  29.274  1.00 11.00 ? 192 TRP A CG  1 
ATOM   1511 C  CD1 . TRP A 1 188 ? -14.980 -7.079  30.565  1.00 10.26 ? 192 TRP A CD1 1 
ATOM   1512 C  CD2 . TRP A 1 188 ? -14.934 -7.762  28.403  1.00 12.18 ? 192 TRP A CD2 1 
ATOM   1513 N  NE1 . TRP A 1 188 ? -15.372 -8.389  30.508  1.00 12.31 ? 192 TRP A NE1 1 
ATOM   1514 C  CE2 . TRP A 1 188 ? -15.409 -8.823  29.204  1.00 13.48 ? 192 TRP A CE2 1 
ATOM   1515 C  CE3 . TRP A 1 188 ? -14.869 -7.934  26.996  1.00 13.59 ? 192 TRP A CE3 1 
ATOM   1516 C  CZ2 . TRP A 1 188 ? -15.690 -10.080 28.649  1.00 13.18 ? 192 TRP A CZ2 1 
ATOM   1517 C  CZ3 . TRP A 1 188 ? -15.177 -9.163  26.456  1.00 12.59 ? 192 TRP A CZ3 1 
ATOM   1518 C  CH2 . TRP A 1 188 ? -15.551 -10.233 27.282  1.00 14.48 ? 192 TRP A CH2 1 
ATOM   1519 N  N   . THR A 1 189 ? -14.011 -2.150  29.530  1.00 9.50  ? 193 THR A N   1 
ATOM   1520 C  CA  . THR A 1 189 ? -13.296 -0.916  29.174  1.00 9.77  ? 193 THR A CA  1 
ATOM   1521 C  C   . THR A 1 189 ? -12.057 -0.737  30.053  1.00 10.81 ? 193 THR A C   1 
ATOM   1522 O  O   . THR A 1 189 ? -12.021 -1.161  31.218  1.00 10.64 ? 193 THR A O   1 
ATOM   1523 C  CB  . THR A 1 189 ? -14.248 0.296   29.245  1.00 9.88  ? 193 THR A CB  1 
ATOM   1524 O  OG1 . THR A 1 189 ? -13.543 1.456   28.810  1.00 11.38 ? 193 THR A OG1 1 
ATOM   1525 C  CG2 . THR A 1 189 ? -14.785 0.555   30.649  1.00 10.61 ? 193 THR A CG2 1 
ATOM   1526 N  N   . TYR A 1 190 ? -10.986 -0.201  29.448  1.00 10.29 ? 194 TYR A N   1 
ATOM   1527 C  CA  . TYR A 1 190 ? -9.752  0.061   30.162  1.00 8.97  ? 194 TYR A CA  1 
ATOM   1528 C  C   . TYR A 1 190 ? -8.981  1.118   29.389  1.00 10.08 ? 194 TYR A C   1 
ATOM   1529 O  O   . TYR A 1 190 ? -9.238  1.293   28.189  1.00 9.17  ? 194 TYR A O   1 
ATOM   1530 C  CB  . TYR A 1 190 ? -8.942  -1.242  30.337  1.00 8.72  ? 194 TYR A CB  1 
ATOM   1531 C  CG  . TYR A 1 190 ? -8.242  -1.699  29.072  1.00 8.89  ? 194 TYR A CG  1 
ATOM   1532 C  CD1 . TYR A 1 190 ? -8.943  -2.380  28.072  1.00 8.03  ? 194 TYR A CD1 1 
ATOM   1533 C  CD2 . TYR A 1 190 ? -6.924  -1.322  28.853  1.00 8.79  ? 194 TYR A CD2 1 
ATOM   1534 C  CE1 . TYR A 1 190 ? -8.319  -2.751  26.885  1.00 8.13  ? 194 TYR A CE1 1 
ATOM   1535 C  CE2 . TYR A 1 190 ? -6.265  -1.694  27.668  1.00 8.56  ? 194 TYR A CE2 1 
ATOM   1536 C  CZ  . TYR A 1 190 ? -6.987  -2.395  26.702  1.00 7.87  ? 194 TYR A CZ  1 
ATOM   1537 O  OH  . TYR A 1 190 ? -6.309  -2.657  25.546  1.00 9.01  ? 194 TYR A OH  1 
ATOM   1538 N  N   . PRO A 1 191 ? -8.054  1.856   30.040  1.00 9.27  ? 195 PRO A N   1 
ATOM   1539 C  CA  . PRO A 1 191 ? -7.223  2.832   29.353  1.00 8.75  ? 195 PRO A CA  1 
ATOM   1540 C  C   . PRO A 1 191 ? -6.032  2.155   28.692  1.00 9.26  ? 195 PRO A C   1 
ATOM   1541 O  O   . PRO A 1 191 ? -5.315  1.394   29.340  1.00 9.48  ? 195 PRO A O   1 
ATOM   1542 C  CB  . PRO A 1 191 ? -6.724  3.765   30.498  1.00 10.36 ? 195 PRO A CB  1 
ATOM   1543 C  CG  . PRO A 1 191 ? -6.772  2.887   31.712  1.00 10.93 ? 195 PRO A CG  1 
ATOM   1544 C  CD  . PRO A 1 191 ? -7.835  1.839   31.508  1.00 10.91 ? 195 PRO A CD  1 
ATOM   1545 N  N   . GLY A 1 192 ? -5.811  2.458   27.406  1.00 8.57  ? 196 GLY A N   1 
ATOM   1546 C  CA  . GLY A 1 192 ? -4.654  1.827   26.768  1.00 8.20  ? 196 GLY A CA  1 
ATOM   1547 C  C   . GLY A 1 192 ? -4.132  2.682   25.623  1.00 8.82  ? 196 GLY A C   1 
ATOM   1548 O  O   . GLY A 1 192 ? -4.054  3.921   25.751  1.00 8.96  ? 196 GLY A O   1 
ATOM   1549 N  N   . SER A 1 193 ? -3.777  2.030   24.521  1.00 8.54  ? 197 SER A N   1 
ATOM   1550 C  CA  . SER A 1 193 ? -2.940  2.699   23.526  1.00 8.26  ? 197 SER A CA  1 
ATOM   1551 C  C   . SER A 1 193 ? -3.347  2.330   22.104  1.00 8.46  ? 197 SER A C   1 
ATOM   1552 O  O   . SER A 1 193 ? -4.083  1.371   21.905  1.00 8.84  ? 197 SER A O   1 
ATOM   1553 C  CB  . SER A 1 193 ? -1.487  2.322   23.711  1.00 8.78  ? 197 SER A CB  1 
ATOM   1554 O  OG  . SER A 1 193 ? -1.243  0.956   23.293  1.00 8.76  ? 197 SER A OG  1 
ATOM   1555 N  N   . LEU A 1 194 ? -2.785  3.054   21.128  1.00 8.78  ? 198 LEU A N   1 
ATOM   1556 C  CA  . LEU A 1 194 ? -2.788  2.500   19.774  1.00 9.70  ? 198 LEU A CA  1 
ATOM   1557 C  C   . LEU A 1 194 ? -2.015  1.192   19.786  1.00 9.88  ? 198 LEU A C   1 
ATOM   1558 O  O   . LEU A 1 194 ? -1.088  0.998   20.589  1.00 9.73  ? 198 LEU A O   1 
ATOM   1559 C  CB  . LEU A 1 194 ? -2.081  3.484   18.835  1.00 10.48 ? 198 LEU A CB  1 
ATOM   1560 C  CG  . LEU A 1 194 ? -2.637  4.891   18.745  1.00 12.05 ? 198 LEU A CG  1 
ATOM   1561 C  CD1 . LEU A 1 194 ? -1.711  5.733   17.866  1.00 14.03 ? 198 LEU A CD1 1 
ATOM   1562 C  CD2 . LEU A 1 194 ? -4.052  4.906   18.194  1.00 11.98 ? 198 LEU A CD2 1 
ATOM   1563 N  N   . THR A 1 195 ? -2.386  0.269   18.869  1.00 8.56  ? 199 THR A N   1 
ATOM   1564 C  CA  . THR A 1 195 ? -1.745  -1.045  18.876  1.00 8.63  ? 199 THR A CA  1 
ATOM   1565 C  C   . THR A 1 195 ? -0.716  -1.164  17.754  1.00 9.10  ? 199 THR A C   1 
ATOM   1566 O  O   . THR A 1 195 ? -0.173  -2.243  17.532  1.00 10.45 ? 199 THR A O   1 
ATOM   1567 C  CB  . THR A 1 195 ? -2.759  -2.198  18.796  1.00 7.88  ? 199 THR A CB  1 
ATOM   1568 O  OG1 . THR A 1 195 ? -3.390  -2.186  17.510  1.00 8.44  ? 199 THR A OG1 1 
ATOM   1569 C  CG2 . THR A 1 195 ? -3.741  -2.236  19.962  1.00 8.82  ? 199 THR A CG2 1 
ATOM   1570 N  N   . VAL A 1 196 ? -0.489  -0.056  17.040  1.00 10.39 ? 200 VAL A N   1 
ATOM   1571 C  CA  . VAL A 1 196 ? 0.644   0.043   16.118  1.00 10.78 ? 200 VAL A CA  1 
ATOM   1572 C  C   . VAL A 1 196 ? 1.420   1.300   16.434  1.00 11.28 ? 200 VAL A C   1 
ATOM   1573 O  O   . VAL A 1 196 ? 0.854   2.264   16.943  1.00 11.78 ? 200 VAL A O   1 
ATOM   1574 C  CB  . VAL A 1 196 ? 0.139   0.131   14.670  1.00 12.21 ? 200 VAL A CB  1 
ATOM   1575 C  CG1 . VAL A 1 196 ? -0.454  -1.207  14.254  1.00 13.98 ? 200 VAL A CG1 1 
ATOM   1576 C  CG2 . VAL A 1 196 ? -0.851  1.276   14.454  1.00 13.99 ? 200 VAL A CG2 1 
ATOM   1577 N  N   . PRO A 1 197 ? 2.699   1.376   15.992  1.00 11.84 ? 201 PRO A N   1 
ATOM   1578 C  CA  . PRO A 1 197 ? 3.438   2.623   16.144  1.00 12.11 ? 201 PRO A CA  1 
ATOM   1579 C  C   . PRO A 1 197 ? 2.552   3.734   15.574  1.00 12.24 ? 201 PRO A C   1 
ATOM   1580 O  O   . PRO A 1 197 ? 1.961   3.626   14.462  1.00 14.20 ? 201 PRO A O   1 
ATOM   1581 C  CB  . PRO A 1 197 ? 4.595   2.348   15.157  1.00 13.47 ? 201 PRO A CB  1 
ATOM   1582 C  CG  . PRO A 1 197 ? 4.891   0.883   15.329  1.00 12.35 ? 201 PRO A CG  1 
ATOM   1583 C  CD  . PRO A 1 197 ? 3.485   0.284   15.382  1.00 12.10 ? 201 PRO A CD  1 
ATOM   1584 N  N   . PRO A 1 198 ? 2.507   4.924   16.209  1.00 11.82 ? 202 PRO A N   1 
ATOM   1585 C  CA  . PRO A 1 198 ? 3.352   5.295   17.360  1.00 12.40 ? 202 PRO A CA  1 
ATOM   1586 C  C   . PRO A 1 198 ? 3.006   4.852   18.782  1.00 11.43 ? 202 PRO A C   1 
ATOM   1587 O  O   . PRO A 1 198 ? 3.662   5.246   19.749  1.00 13.04 ? 202 PRO A O   1 
ATOM   1588 C  CB  . PRO A 1 198 ? 3.381   6.825   17.218  1.00 11.67 ? 202 PRO A CB  1 
ATOM   1589 C  CG  . PRO A 1 198 ? 2.068   7.169   16.630  1.00 12.75 ? 202 PRO A CG  1 
ATOM   1590 C  CD  . PRO A 1 198 ? 1.680   6.028   15.713  1.00 12.66 ? 202 PRO A CD  1 
ATOM   1591 N  N   . LEU A 1 199 ? 2.007   3.943   18.886  1.00 10.30 ? 203 LEU A N   1 
ATOM   1592 C  CA  . LEU A 1 199 ? 1.713   3.262   20.143  1.00 9.66  ? 203 LEU A CA  1 
ATOM   1593 C  C   . LEU A 1 199 ? 1.319   4.274   21.232  1.00 9.26  ? 203 LEU A C   1 
ATOM   1594 O  O   . LEU A 1 199 ? 1.487   4.009   22.408  1.00 10.81 ? 203 LEU A O   1 
ATOM   1595 C  CB  . LEU A 1 199 ? 2.903   2.380   20.570  1.00 11.20 ? 203 LEU A CB  1 
ATOM   1596 C  CG  . LEU A 1 199 ? 3.257   1.293   19.544  1.00 10.54 ? 203 LEU A CG  1 
ATOM   1597 C  CD1 . LEU A 1 199 ? 4.607   0.678   19.924  1.00 12.92 ? 203 LEU A CD1 1 
ATOM   1598 C  CD2 . LEU A 1 199 ? 2.141   0.219   19.514  1.00 11.12 ? 203 LEU A CD2 1 
ATOM   1599 N  N   . LEU A 1 200 ? 0.733   5.410   20.835  1.00 10.16 ? 204 LEU A N   1 
ATOM   1600 C  CA  . LEU A 1 200 ? 0.469   6.475   21.805  1.00 9.94  ? 204 LEU A CA  1 
ATOM   1601 C  C   . LEU A 1 200 ? -0.628  6.048   22.786  1.00 10.90 ? 204 LEU A C   1 
ATOM   1602 O  O   . LEU A 1 200 ? -1.576  5.348   22.396  1.00 10.36 ? 204 LEU A O   1 
ATOM   1603 C  CB  . LEU A 1 200 ? 0.051   7.746   21.048  1.00 12.69 ? 204 LEU A CB  1 
ATOM   1604 C  CG  . LEU A 1 200 ? 1.117   8.299   20.089  1.00 14.69 ? 204 LEU A CG  1 
ATOM   1605 C  CD1 . LEU A 1 200 ? 0.486   9.415   19.262  1.00 15.11 ? 204 LEU A CD1 1 
ATOM   1606 C  CD2 . LEU A 1 200 ? 2.289   8.848   20.919  1.00 18.80 ? 204 LEU A CD2 1 
ATOM   1607 N  N   . GLU A 1 201 ? -0.461  6.446   24.051  1.00 10.31 ? 205 GLU A N   1 
ATOM   1608 C  CA  . GLU A 1 201 ? -1.330  6.056   25.142  1.00 11.28 ? 205 GLU A CA  1 
ATOM   1609 C  C   . GLU A 1 201 ? -2.469  7.065   25.235  1.00 11.75 ? 205 GLU A C   1 
ATOM   1610 O  O   . GLU A 1 201 ? -2.546  7.845   26.180  1.00 11.78 ? 205 GLU A O   1 
ATOM   1611 C  CB  . GLU A 1 201 ? -0.441  5.949   26.390  1.00 11.91 ? 205 GLU A CB  1 
ATOM   1612 C  CG  . GLU A 1 201 ? 0.420   4.688   26.252  1.00 12.87 ? 205 GLU A CG  1 
ATOM   1613 C  CD  . GLU A 1 201 ? 1.429   4.454   27.361  1.00 14.52 ? 205 GLU A CD  1 
ATOM   1614 O  OE1 . GLU A 1 201 ? 1.735   5.414   28.097  1.00 16.85 ? 205 GLU A OE1 1 
ATOM   1615 O  OE2 . GLU A 1 201 ? 1.844   3.308   27.523  1.00 11.95 ? 205 GLU A OE2 1 
ATOM   1616 N  N   . CYS A 1 202 ? -3.380  7.035   24.253  1.00 10.19 ? 206 CYS A N   1 
ATOM   1617 C  CA  . CYS A 1 202 ? -4.430  8.045   24.055  1.00 10.02 ? 206 CYS A CA  1 
ATOM   1618 C  C   . CYS A 1 202 ? -5.818  7.417   23.920  1.00 9.81  ? 206 CYS A C   1 
ATOM   1619 O  O   . CYS A 1 202 ? -6.764  8.116   23.546  1.00 9.77  ? 206 CYS A O   1 
ATOM   1620 C  CB  . CYS A 1 202 ? -4.131  8.886   22.812  1.00 10.28 ? 206 CYS A CB  1 
ATOM   1621 S  SG  . CYS A 1 202 ? -4.059  7.884   21.286  1.00 11.46 ? 206 CYS A SG  1 
ATOM   1622 N  N   . VAL A 1 203 ? -5.915  6.109   24.181  1.00 8.69  ? 207 VAL A N   1 
ATOM   1623 C  CA  . VAL A 1 203 ? -7.113  5.320   23.854  1.00 8.48  ? 207 VAL A CA  1 
ATOM   1624 C  C   . VAL A 1 203 ? -7.914  4.901   25.079  1.00 8.58  ? 207 VAL A C   1 
ATOM   1625 O  O   . VAL A 1 203 ? -7.393  4.228   25.948  1.00 10.87 ? 207 VAL A O   1 
ATOM   1626 C  CB  . VAL A 1 203 ? -6.813  4.060   23.021  1.00 7.46  ? 207 VAL A CB  1 
ATOM   1627 C  CG1 . VAL A 1 203 ? -8.174  3.422   22.650  1.00 7.12  ? 207 VAL A CG1 1 
ATOM   1628 C  CG2 . VAL A 1 203 ? -6.081  4.474   21.708  1.00 8.83  ? 207 VAL A CG2 1 
ATOM   1629 N  N   . THR A 1 204 ? -9.195  5.263   25.107  1.00 8.11  ? 208 THR A N   1 
ATOM   1630 C  CA  . THR A 1 204 ? -10.131 4.541   25.943  1.00 8.09  ? 208 THR A CA  1 
ATOM   1631 C  C   . THR A 1 204 ? -10.622 3.353   25.148  1.00 8.12  ? 208 THR A C   1 
ATOM   1632 O  O   . THR A 1 204 ? -11.326 3.557   24.144  1.00 8.20  ? 208 THR A O   1 
ATOM   1633 C  CB  . THR A 1 204 ? -11.332 5.414   26.376  1.00 10.54 ? 208 THR A CB  1 
ATOM   1634 O  OG1 . THR A 1 204 ? -10.798 6.471   27.198  1.00 10.89 ? 208 THR A OG1 1 
ATOM   1635 C  CG2 . THR A 1 204 ? -12.292 4.634   27.247  1.00 10.87 ? 208 THR A CG2 1 
ATOM   1636 N  N   . TRP A 1 205 ? -10.242 2.142   25.555  1.00 8.32  ? 209 TRP A N   1 
ATOM   1637 C  CA  . TRP A 1 205 ? -10.716 0.961   24.843  1.00 7.62  ? 209 TRP A CA  1 
ATOM   1638 C  C   . TRP A 1 205 ? -12.077 0.509   25.368  1.00 8.17  ? 209 TRP A C   1 
ATOM   1639 O  O   . TRP A 1 205 ? -12.282 0.481   26.592  1.00 9.59  ? 209 TRP A O   1 
ATOM   1640 C  CB  . TRP A 1 205 ? -9.726  -0.200  25.041  1.00 7.64  ? 209 TRP A CB  1 
ATOM   1641 C  CG  . TRP A 1 205 ? -8.591  -0.067  24.070  1.00 7.02  ? 209 TRP A CG  1 
ATOM   1642 C  CD1 . TRP A 1 205 ? -7.348  0.484   24.265  1.00 6.76  ? 209 TRP A CD1 1 
ATOM   1643 C  CD2 . TRP A 1 205 ? -8.640  -0.484  22.696  1.00 7.50  ? 209 TRP A CD2 1 
ATOM   1644 N  NE1 . TRP A 1 205 ? -6.654  0.466   23.069  1.00 7.50  ? 209 TRP A NE1 1 
ATOM   1645 C  CE2 . TRP A 1 205 ? -7.399  -0.166  22.102  1.00 7.20  ? 209 TRP A CE2 1 
ATOM   1646 C  CE3 . TRP A 1 205 ? -9.636  -1.111  21.923  1.00 6.88  ? 209 TRP A CE3 1 
ATOM   1647 C  CZ2 . TRP A 1 205 ? -7.122  -0.428  20.774  1.00 8.12  ? 209 TRP A CZ2 1 
ATOM   1648 C  CZ3 . TRP A 1 205 ? -9.356  -1.407  20.616  1.00 7.46  ? 209 TRP A CZ3 1 
ATOM   1649 C  CH2 . TRP A 1 205 ? -8.115  -1.084  20.048  1.00 6.68  ? 209 TRP A CH2 1 
ATOM   1650 N  N   . ILE A 1 206 ? -12.971 0.212   24.409  1.00 8.45  ? 210 ILE A N   1 
ATOM   1651 C  CA  . ILE A 1 206 ? -14.288 -0.352  24.740  1.00 8.58  ? 210 ILE A CA  1 
ATOM   1652 C  C   . ILE A 1 206 ? -14.387 -1.629  23.904  1.00 8.90  ? 210 ILE A C   1 
ATOM   1653 O  O   . ILE A 1 206 ? -14.527 -1.515  22.684  1.00 9.24  ? 210 ILE A O   1 
ATOM   1654 C  CB  . ILE A 1 206 ? -15.377 0.675   24.365  1.00 9.78  ? 210 ILE A CB  1 
ATOM   1655 C  CG1 . ILE A 1 206 ? -15.176 1.927   25.238  1.00 10.27 ? 210 ILE A CG1 1 
ATOM   1656 C  CG2 . ILE A 1 206 ? -16.774 0.057   24.626  1.00 9.28  ? 210 ILE A CG2 1 
ATOM   1657 C  CD1 . ILE A 1 206 ? -15.914 3.159   24.705  1.00 12.51 ? 210 ILE A CD1 1 
ATOM   1658 N  N   . VAL A 1 207 ? -14.369 -2.798  24.560  1.00 8.49  ? 211 VAL A N   1 
ATOM   1659 C  CA  . VAL A 1 207 ? -14.335 -4.054  23.810  1.00 8.67  ? 211 VAL A CA  1 
ATOM   1660 C  C   . VAL A 1 207 ? -15.645 -4.782  24.059  1.00 9.45  ? 211 VAL A C   1 
ATOM   1661 O  O   . VAL A 1 207 ? -15.986 -4.987  25.228  1.00 11.09 ? 211 VAL A O   1 
ATOM   1662 C  CB  . VAL A 1 207 ? -13.134 -4.909  24.231  1.00 8.05  ? 211 VAL A CB  1 
ATOM   1663 C  CG1 . VAL A 1 207 ? -13.123 -6.314  23.583  1.00 7.62  ? 211 VAL A CG1 1 
ATOM   1664 C  CG2 . VAL A 1 207 ? -11.837 -4.131  23.960  1.00 7.86  ? 211 VAL A CG2 1 
ATOM   1665 N  N   . LEU A 1 208 ? -16.391 -5.046  22.975  1.00 9.98  ? 212 LEU A N   1 
ATOM   1666 C  CA  . LEU A 1 208 ? -17.686 -5.711  23.125  1.00 10.43 ? 212 LEU A CA  1 
ATOM   1667 C  C   . LEU A 1 208 ? -17.515 -7.153  23.541  1.00 10.81 ? 212 LEU A C   1 
ATOM   1668 O  O   . LEU A 1 208 ? -16.662 -7.887  23.068  1.00 10.85 ? 212 LEU A O   1 
ATOM   1669 C  CB  . LEU A 1 208 ? -18.481 -5.622  21.821  1.00 9.19  ? 212 LEU A CB  1 
ATOM   1670 C  CG  . LEU A 1 208 ? -18.853 -4.184  21.427  1.00 9.27  ? 212 LEU A CG  1 
ATOM   1671 C  CD1 . LEU A 1 208 ? -19.896 -4.227  20.300  1.00 11.40 ? 212 LEU A CD1 1 
ATOM   1672 C  CD2 . LEU A 1 208 ? -19.405 -3.332  22.619  1.00 8.98  ? 212 LEU A CD2 1 
ATOM   1673 N  N   . LYS A 1 209 ? -18.368 -7.553  24.494  1.00 11.33 ? 213 LYS A N   1 
ATOM   1674 C  CA  . LYS A 1 209 ? -18.374 -8.924  24.959  1.00 13.16 ? 213 LYS A CA  1 
ATOM   1675 C  C   . LYS A 1 209 ? -18.806 -9.893  23.854  1.00 11.34 ? 213 LYS A C   1 
ATOM   1676 O  O   . LYS A 1 209 ? -18.300 -11.041 23.796  1.00 13.38 ? 213 LYS A O   1 
ATOM   1677 C  CB  . LYS A 1 209 ? -19.405 -8.911  26.104  1.00 16.57 ? 213 LYS A CB  1 
ATOM   1678 C  CG  . LYS A 1 209 ? -19.928 -10.246 26.646  1.00 23.42 ? 213 LYS A CG  1 
ATOM   1679 C  CD  . LYS A 1 209 ? -21.324 -10.148 27.265  1.00 27.67 ? 213 LYS A CD  1 
ATOM   1680 C  CE  . LYS A 1 209 ? -22.423 -9.943  26.225  1.00 31.91 ? 213 LYS A CE  1 
ATOM   1681 N  NZ  . LYS A 1 209 ? -23.785 -9.925  26.820  1.00 39.49 ? 213 LYS A NZ  1 
ATOM   1682 N  N   . GLU A 1 210 ? -19.788 -9.498  23.037  1.00 10.52 ? 214 GLU A N   1 
ATOM   1683 C  CA  . GLU A 1 210 ? -20.361 -10.461 22.100  1.00 11.06 ? 214 GLU A CA  1 
ATOM   1684 C  C   . GLU A 1 210 ? -19.606 -10.372 20.769  1.00 10.15 ? 214 GLU A C   1 
ATOM   1685 O  O   . GLU A 1 210 ? -19.564 -9.278  20.186  1.00 10.93 ? 214 GLU A O   1 
ATOM   1686 C  CB  . GLU A 1 210 ? -21.830 -10.122 21.812  1.00 11.84 ? 214 GLU A CB  1 
ATOM   1687 C  CG  . GLU A 1 210 ? -22.452 -11.028 20.765  1.00 15.42 ? 214 GLU A CG  1 
ATOM   1688 C  CD  . GLU A 1 210 ? -23.978 -10.911 20.633  1.00 18.96 ? 214 GLU A CD  1 
ATOM   1689 O  OE1 . GLU A 1 210 ? -24.579 -10.053 21.270  1.00 16.98 ? 214 GLU A OE1 1 
ATOM   1690 O  OE2 . GLU A 1 210 ? -24.576 -11.790 19.943  1.00 27.84 ? 214 GLU A OE2 1 
ATOM   1691 N  N   A PRO A 1 211 ? -19.028 -11.476 20.246  0.50 10.42 ? 215 PRO A N   1 
ATOM   1692 N  N   B PRO A 1 211 ? -18.980 -11.453 20.264  0.50 10.71 ? 215 PRO A N   1 
ATOM   1693 C  CA  A PRO A 1 211 ? -18.376 -11.425 18.937  0.50 10.35 ? 215 PRO A CA  1 
ATOM   1694 C  CA  B PRO A 1 211 ? -18.356 -11.410 18.938  0.50 10.64 ? 215 PRO A CA  1 
ATOM   1695 C  C   A PRO A 1 211 ? -19.458 -11.295 17.868  0.50 11.03 ? 215 PRO A C   1 
ATOM   1696 C  C   B PRO A 1 211 ? -19.384 -11.507 17.813  0.50 11.18 ? 215 PRO A C   1 
ATOM   1697 O  O   A PRO A 1 211 ? -20.650 -11.485 18.150  0.50 11.05 ? 215 PRO A O   1 
ATOM   1698 O  O   B PRO A 1 211 ? -20.455 -12.120 17.978  0.50 10.97 ? 215 PRO A O   1 
ATOM   1699 C  CB  A PRO A 1 211 ? -17.676 -12.793 18.783  0.50 11.01 ? 215 PRO A CB  1 
ATOM   1700 C  CB  B PRO A 1 211 ? -17.514 -12.695 18.858  0.50 11.65 ? 215 PRO A CB  1 
ATOM   1701 C  CG  A PRO A 1 211 ? -18.435 -13.713 19.716  0.50 10.49 ? 215 PRO A CG  1 
ATOM   1702 C  CG  B PRO A 1 211 ? -17.484 -13.213 20.271  0.50 11.55 ? 215 PRO A CG  1 
ATOM   1703 C  CD  A PRO A 1 211 ? -18.992 -12.835 20.835  0.50 9.90  ? 215 PRO A CD  1 
ATOM   1704 C  CD  B PRO A 1 211 ? -18.776 -12.754 20.932  0.50 10.40 ? 215 PRO A CD  1 
ATOM   1705 N  N   . ILE A 1 212 ? -19.038 -10.934 16.648  1.00 10.41 ? 216 ILE A N   1 
ATOM   1706 C  CA  . ILE A 1 212 ? -19.854 -11.145 15.468  1.00 11.88 ? 216 ILE A CA  1 
ATOM   1707 C  C   . ILE A 1 212 ? -19.315 -12.384 14.767  1.00 11.66 ? 216 ILE A C   1 
ATOM   1708 O  O   . ILE A 1 212 ? -18.167 -12.765 14.965  1.00 12.50 ? 216 ILE A O   1 
ATOM   1709 C  CB  . ILE A 1 212 ? -19.875 -9.908  14.523  1.00 12.55 ? 216 ILE A CB  1 
ATOM   1710 C  CG1 . ILE A 1 212 ? -18.477 -9.547  13.986  1.00 11.03 ? 216 ILE A CG1 1 
ATOM   1711 C  CG2 . ILE A 1 212 ? -20.551 -8.699  15.230  1.00 12.54 ? 216 ILE A CG2 1 
ATOM   1712 C  CD1 . ILE A 1 212 ? -18.492 -8.533  12.777  1.00 9.62  ? 216 ILE A CD1 1 
ATOM   1713 N  N   . SER A 1 213 ? -20.195 -13.049 14.019  1.00 12.42 ? 217 SER A N   1 
ATOM   1714 C  CA  . SER A 1 213 ? -19.712 -14.205 13.289  1.00 12.29 ? 217 SER A CA  1 
ATOM   1715 C  C   . SER A 1 213 ? -19.606 -13.848 11.821  1.00 12.40 ? 217 SER A C   1 
ATOM   1716 O  O   . SER A 1 213 ? -20.475 -13.174 11.249  1.00 13.54 ? 217 SER A O   1 
ATOM   1717 C  CB  . SER A 1 213 ? -20.553 -15.437 13.560  1.00 16.46 ? 217 SER A CB  1 
ATOM   1718 O  OG  . SER A 1 213 ? -21.866 -15.243 13.095  1.00 18.99 ? 217 SER A OG  1 
ATOM   1719 N  N   . VAL A 1 214 ? -18.501 -14.288 11.241  1.00 12.16 ? 218 VAL A N   1 
ATOM   1720 C  CA  . VAL A 1 214 ? -18.258 -14.086 9.817   1.00 12.44 ? 218 VAL A CA  1 
ATOM   1721 C  C   . VAL A 1 214 ? -18.011 -15.441 9.197   1.00 12.33 ? 218 VAL A C   1 
ATOM   1722 O  O   . VAL A 1 214 ? -17.591 -16.383 9.884   1.00 12.76 ? 218 VAL A O   1 
ATOM   1723 C  CB  . VAL A 1 214 ? -17.041 -13.177 9.563   1.00 12.54 ? 218 VAL A CB  1 
ATOM   1724 C  CG1 . VAL A 1 214 ? -17.295 -11.805 10.169  1.00 12.88 ? 218 VAL A CG1 1 
ATOM   1725 C  CG2 . VAL A 1 214 ? -15.705 -13.773 10.044  1.00 13.86 ? 218 VAL A CG2 1 
ATOM   1726 N  N   . SER A 1 215 ? -18.161 -15.543 7.881   1.00 12.53 ? 219 SER A N   1 
ATOM   1727 C  CA  . SER A 1 215 ? -17.938 -16.860 7.291   1.00 13.84 ? 219 SER A CA  1 
ATOM   1728 C  C   . SER A 1 215 ? -16.477 -17.136 6.968   1.00 13.76 ? 219 SER A C   1 
ATOM   1729 O  O   . SER A 1 215 ? -15.640 -16.236 6.855   1.00 11.14 ? 219 SER A O   1 
ATOM   1730 C  CB  . SER A 1 215 ? -18.788 -17.017 6.050   1.00 14.46 ? 219 SER A CB  1 
ATOM   1731 O  OG  . SER A 1 215 ? -18.268 -16.223 4.993   1.00 16.88 ? 219 SER A OG  1 
ATOM   1732 N  N   . SER A 1 216 ? -16.156 -18.426 6.800   1.00 13.23 ? 220 SER A N   1 
ATOM   1733 C  CA  . SER A 1 216 ? -14.800 -18.752 6.441   1.00 14.50 ? 220 SER A CA  1 
ATOM   1734 C  C   . SER A 1 216 ? -14.402 -18.075 5.127   1.00 15.38 ? 220 SER A C   1 
ATOM   1735 O  O   . SER A 1 216 ? -13.268 -17.608 5.016   1.00 14.93 ? 220 SER A O   1 
ATOM   1736 C  CB  . SER A 1 216 ? -14.563 -20.264 6.431   1.00 18.17 ? 220 SER A CB  1 
ATOM   1737 O  OG  . SER A 1 216 ? -15.500 -20.834 5.569   1.00 20.06 ? 220 SER A OG  1 
ATOM   1738 N  N   . GLU A 1 217 ? -15.354 -17.962 4.176   1.00 15.97 ? 221 GLU A N   1 
ATOM   1739 C  CA  . GLU A 1 217 ? -15.060 -17.349 2.894   1.00 15.79 ? 221 GLU A CA  1 
ATOM   1740 C  C   . GLU A 1 217 ? -14.791 -15.853 3.083   1.00 14.98 ? 221 GLU A C   1 
ATOM   1741 O  O   . GLU A 1 217 ? -13.951 -15.305 2.387   1.00 15.65 ? 221 GLU A O   1 
ATOM   1742 C  CB  . GLU A 1 217 ? -16.185 -17.503 1.877   1.00 19.19 ? 221 GLU A CB  1 
ATOM   1743 C  CG  . GLU A 1 217 ? -16.381 -18.960 1.459   1.00 23.07 ? 221 GLU A CG  1 
ATOM   1744 C  CD  . GLU A 1 217 ? -17.500 -19.636 2.242   1.00 26.67 ? 221 GLU A CD  1 
ATOM   1745 O  OE1 . GLU A 1 217 ? -17.833 -19.195 3.355   1.00 25.59 ? 221 GLU A OE1 1 
ATOM   1746 O  OE2 . GLU A 1 217 ? -18.051 -20.623 1.741   1.00 32.72 ? 221 GLU A OE2 1 
ATOM   1747 N  N   . GLN A 1 218 ? -15.482 -15.209 4.047   1.00 13.42 ? 222 GLN A N   1 
ATOM   1748 C  CA  . GLN A 1 218 ? -15.269 -13.769 4.226   1.00 11.75 ? 222 GLN A CA  1 
ATOM   1749 C  C   . GLN A 1 218 ? -13.838 -13.537 4.738   1.00 13.98 ? 222 GLN A C   1 
ATOM   1750 O  O   . GLN A 1 218 ? -13.115 -12.659 4.252   1.00 12.50 ? 222 GLN A O   1 
ATOM   1751 C  CB  . GLN A 1 218 ? -16.337 -13.268 5.200   1.00 11.98 ? 222 GLN A CB  1 
ATOM   1752 C  CG  . GLN A 1 218 ? -17.697 -13.197 4.520   1.00 12.46 ? 222 GLN A CG  1 
ATOM   1753 C  CD  . GLN A 1 218 ? -18.751 -12.556 5.378   1.00 12.47 ? 222 GLN A CD  1 
ATOM   1754 O  OE1 . GLN A 1 218 ? -18.920 -12.908 6.529   1.00 12.95 ? 222 GLN A OE1 1 
ATOM   1755 N  NE2 . GLN A 1 218 ? -19.528 -11.644 4.812   1.00 12.42 ? 222 GLN A NE2 1 
ATOM   1756 N  N   . VAL A 1 219 ? -13.412 -14.296 5.761   1.00 13.13 ? 223 VAL A N   1 
ATOM   1757 C  CA  . VAL A 1 219 ? -12.079 -14.090 6.341   1.00 15.14 ? 223 VAL A CA  1 
ATOM   1758 C  C   . VAL A 1 219 ? -10.979 -14.556 5.363   1.00 16.49 ? 223 VAL A C   1 
ATOM   1759 O  O   . VAL A 1 219 ? -9.905  -13.977 5.309   1.00 16.24 ? 223 VAL A O   1 
ATOM   1760 C  CB  . VAL A 1 219 ? -11.947 -14.735 7.734   1.00 17.09 ? 223 VAL A CB  1 
ATOM   1761 C  CG1 . VAL A 1 219 ? -11.846 -16.243 7.661   1.00 19.96 ? 223 VAL A CG1 1 
ATOM   1762 C  CG2 . VAL A 1 219 ? -10.713 -14.167 8.440   1.00 15.89 ? 223 VAL A CG2 1 
ATOM   1763 N  N   . LEU A 1 220 ? -11.261 -15.570 4.526   1.00 16.98 ? 224 LEU A N   1 
ATOM   1764 C  CA  . LEU A 1 220 ? -10.277 -16.008 3.546   1.00 18.46 ? 224 LEU A CA  1 
ATOM   1765 C  C   . LEU A 1 220 ? -9.947  -14.878 2.585   1.00 17.34 ? 224 LEU A C   1 
ATOM   1766 O  O   . LEU A 1 220 ? -8.804  -14.743 2.173   1.00 18.71 ? 224 LEU A O   1 
ATOM   1767 C  CB  . LEU A 1 220 ? -10.798 -17.223 2.764   1.00 21.66 ? 224 LEU A CB  1 
ATOM   1768 C  CG  . LEU A 1 220 ? -10.576 -18.579 3.442   1.00 29.31 ? 224 LEU A CG  1 
ATOM   1769 C  CD1 . LEU A 1 220 ? -11.369 -19.688 2.731   1.00 33.26 ? 224 LEU A CD1 1 
ATOM   1770 C  CD2 . LEU A 1 220 ? -9.096  -18.943 3.475   1.00 29.42 ? 224 LEU A CD2 1 
ATOM   1771 N  N   . LYS A 1 221 ? -10.953 -14.079 2.242   1.00 15.26 ? 225 LYS A N   1 
ATOM   1772 C  CA  . LYS A 1 221 ? -10.771 -12.932 1.353   1.00 16.03 ? 225 LYS A CA  1 
ATOM   1773 C  C   . LYS A 1 221 ? -9.878  -11.873 1.999   1.00 16.04 ? 225 LYS A C   1 
ATOM   1774 O  O   . LYS A 1 221 ? -9.075  -11.270 1.314   1.00 14.54 ? 225 LYS A O   1 
ATOM   1775 C  CB  . LYS A 1 221 ? -12.112 -12.399 0.835   1.00 18.50 ? 225 LYS A CB  1 
ATOM   1776 C  CG  . LYS A 1 221 ? -12.718 -13.375 -0.180  1.00 23.41 ? 225 LYS A CG  1 
ATOM   1777 C  CD  . LYS A 1 221 ? -13.998 -13.031 -0.884  1.00 32.01 ? 225 LYS A CD  1 
ATOM   1778 C  CE  . LYS A 1 221 ? -14.478 -14.252 -1.660  1.00 37.94 ? 225 LYS A CE  1 
ATOM   1779 N  NZ  . LYS A 1 221 ? -15.828 -14.082 -2.254  1.00 42.65 ? 225 LYS A NZ  1 
ATOM   1780 N  N   . PHE A 1 222 ? -9.962  -11.656 3.321   1.00 12.83 ? 226 PHE A N   1 
ATOM   1781 C  CA  . PHE A 1 222 ? -8.984  -10.791 3.983   1.00 13.54 ? 226 PHE A CA  1 
ATOM   1782 C  C   . PHE A 1 222 ? -7.547  -11.276 3.786   1.00 14.14 ? 226 PHE A C   1 
ATOM   1783 O  O   . PHE A 1 222 ? -6.646  -10.458 3.621   1.00 12.96 ? 226 PHE A O   1 
ATOM   1784 C  CB  . PHE A 1 222 ? -9.195  -10.778 5.513   1.00 13.08 ? 226 PHE A CB  1 
ATOM   1785 C  CG  . PHE A 1 222 ? -10.357 -10.007 6.110   1.00 13.46 ? 226 PHE A CG  1 
ATOM   1786 C  CD1 . PHE A 1 222 ? -11.453 -9.573  5.383   1.00 15.53 ? 226 PHE A CD1 1 
ATOM   1787 C  CD2 . PHE A 1 222 ? -10.396 -9.836  7.502   1.00 15.25 ? 226 PHE A CD2 1 
ATOM   1788 C  CE1 . PHE A 1 222 ? -12.460 -8.843  5.976   1.00 15.44 ? 226 PHE A CE1 1 
ATOM   1789 C  CE2 . PHE A 1 222 ? -11.448 -9.158  8.121   1.00 17.14 ? 226 PHE A CE2 1 
ATOM   1790 C  CZ  . PHE A 1 222 ? -12.490 -8.670  7.347   1.00 16.47 ? 226 PHE A CZ  1 
ATOM   1791 N  N   . ARG A 1 223 ? -7.314  -12.601 3.815   1.00 12.55 ? 227 ARG A N   1 
ATOM   1792 C  CA  . ARG A 1 223 ? -5.970  -13.171 3.780   1.00 13.85 ? 227 ARG A CA  1 
ATOM   1793 C  C   . ARG A 1 223 ? -5.423  -13.196 2.354   1.00 14.27 ? 227 ARG A C   1 
ATOM   1794 O  O   . ARG A 1 223 ? -4.276  -13.577 2.195   1.00 17.78 ? 227 ARG A O   1 
ATOM   1795 C  CB  . ARG A 1 223 ? -5.941  -14.606 4.313   1.00 13.74 ? 227 ARG A CB  1 
ATOM   1796 C  CG  . ARG A 1 223 ? -6.600  -14.791 5.688   1.00 11.95 ? 227 ARG A CG  1 
ATOM   1797 C  CD  . ARG A 1 223 ? -6.464  -16.221 6.207   1.00 14.32 ? 227 ARG A CD  1 
ATOM   1798 N  NE  . ARG A 1 223 ? -7.009  -16.376 7.562   1.00 15.05 ? 227 ARG A NE  1 
ATOM   1799 C  CZ  . ARG A 1 223 ? -7.969  -17.216 7.912   1.00 15.78 ? 227 ARG A CZ  1 
ATOM   1800 N  NH1 . ARG A 1 223 ? -8.405  -18.121 7.028   1.00 17.39 ? 227 ARG A NH1 1 
ATOM   1801 N  NH2 . ARG A 1 223 ? -8.410  -17.247 9.151   1.00 16.35 ? 227 ARG A NH2 1 
ATOM   1802 N  N   . LYS A 1 224 ? -6.216  -12.720 1.391   1.00 15.67 ? 228 LYS A N   1 
ATOM   1803 C  CA  . LYS A 1 224 ? -5.697  -12.592 0.020   1.00 16.44 ? 228 LYS A CA  1 
ATOM   1804 C  C   . LYS A 1 224 ? -5.073  -11.215 -0.204  1.00 18.16 ? 228 LYS A C   1 
ATOM   1805 O  O   . LYS A 1 224 ? -4.389  -10.986 -1.214  1.00 16.36 ? 228 LYS A O   1 
ATOM   1806 C  CB  . LYS A 1 224 ? -6.774  -12.882 -1.036  1.00 17.33 ? 228 LYS A CB  1 
ATOM   1807 C  CG  . LYS A 1 224 ? -7.269  -14.329 -0.990  1.00 19.48 ? 228 LYS A CG  1 
ATOM   1808 C  CD  . LYS A 1 224 ? -8.341  -14.636 -2.039  1.00 24.60 ? 228 LYS A CD  1 
ATOM   1809 N  N   . LEU A 1 225 ? -5.266  -10.278 0.738   1.00 15.99 ? 229 LEU A N   1 
ATOM   1810 C  CA  . LEU A 1 225 ? -4.600  -8.990  0.597   1.00 15.59 ? 229 LEU A CA  1 
ATOM   1811 C  C   . LEU A 1 225 ? -3.090  -9.154  0.753   1.00 15.76 ? 229 LEU A C   1 
ATOM   1812 O  O   . LEU A 1 225 ? -2.586  -10.155 1.253   1.00 15.04 ? 229 LEU A O   1 
ATOM   1813 C  CB  . LEU A 1 225 ? -5.131  -8.048  1.684   1.00 13.52 ? 229 LEU A CB  1 
ATOM   1814 C  CG  . LEU A 1 225 ? -6.602  -7.635  1.529   1.00 12.97 ? 229 LEU A CG  1 
ATOM   1815 C  CD1 . LEU A 1 225 ? -7.064  -7.030  2.834   1.00 14.58 ? 229 LEU A CD1 1 
ATOM   1816 C  CD2 . LEU A 1 225 ? -6.787  -6.570  0.461   1.00 13.60 ? 229 LEU A CD2 1 
ATOM   1817 N  N   . ASN A 1 226 ? -2.373  -8.083  0.420   1.00 17.99 ? 230 ASN A N   1 
ATOM   1818 C  CA  . ASN A 1 226 ? -0.923  -8.082  0.384   1.00 17.92 ? 230 ASN A CA  1 
ATOM   1819 C  C   . ASN A 1 226 ? -0.366  -6.906  1.196   1.00 16.42 ? 230 ASN A C   1 
ATOM   1820 O  O   . ASN A 1 226 ? -0.862  -5.790  1.101   1.00 18.30 ? 230 ASN A O   1 
ATOM   1821 C  CB  . ASN A 1 226 ? -0.413  -7.841  -1.049  1.00 17.86 ? 230 ASN A CB  1 
ATOM   1822 C  CG  . ASN A 1 226 ? -0.461  -9.036  -1.980  1.00 23.04 ? 230 ASN A CG  1 
ATOM   1823 O  OD1 . ASN A 1 226 ? -0.010  -8.903  -3.125  1.00 24.08 ? 230 ASN A OD1 1 
ATOM   1824 N  ND2 . ASN A 1 226 ? -0.993  -10.166 -1.543  1.00 22.53 ? 230 ASN A ND2 1 
ATOM   1825 N  N   . PHE A 1 227 ? 0.704   -7.186  1.945   1.00 16.64 ? 231 PHE A N   1 
ATOM   1826 C  CA  . PHE A 1 227 ? 1.424   -6.143  2.674   1.00 17.62 ? 231 PHE A CA  1 
ATOM   1827 C  C   . PHE A 1 227 ? 2.307   -5.323  1.726   1.00 20.67 ? 231 PHE A C   1 
ATOM   1828 O  O   . PHE A 1 227 ? 2.576   -4.160  2.006   1.00 19.76 ? 231 PHE A O   1 
ATOM   1829 C  CB  . PHE A 1 227 ? 2.411   -6.700  3.699   1.00 18.08 ? 231 PHE A CB  1 
ATOM   1830 C  CG  . PHE A 1 227 ? 1.875   -7.301  4.987   1.00 16.15 ? 231 PHE A CG  1 
ATOM   1831 C  CD1 . PHE A 1 227 ? 1.073   -6.557  5.832   1.00 17.20 ? 231 PHE A CD1 1 
ATOM   1832 C  CD2 . PHE A 1 227 ? 2.198   -8.609  5.340   1.00 16.97 ? 231 PHE A CD2 1 
ATOM   1833 C  CE1 . PHE A 1 227 ? 0.620   -7.111  7.029   1.00 15.44 ? 231 PHE A CE1 1 
ATOM   1834 C  CE2 . PHE A 1 227 ? 1.762   -9.160  6.550   1.00 17.74 ? 231 PHE A CE2 1 
ATOM   1835 C  CZ  . PHE A 1 227 ? 0.975   -8.398  7.386   1.00 16.76 ? 231 PHE A CZ  1 
ATOM   1836 N  N   . ASN A 1 228 ? 2.757   -5.949  0.639   1.00 21.86 ? 232 ASN A N   1 
ATOM   1837 C  CA  . ASN A 1 228 ? 3.656   -5.293  -0.316  1.00 25.26 ? 232 ASN A CA  1 
ATOM   1838 C  C   . ASN A 1 228 ? 2.892   -4.393  -1.286  1.00 27.94 ? 232 ASN A C   1 
ATOM   1839 O  O   . ASN A 1 228 ? 1.689   -4.550  -1.455  1.00 24.45 ? 232 ASN A O   1 
ATOM   1840 C  CB  . ASN A 1 228 ? 4.378   -6.363  -1.123  1.00 24.00 ? 232 ASN A CB  1 
ATOM   1841 C  CG  . ASN A 1 228 ? 3.397   -7.341  -1.729  1.00 24.19 ? 232 ASN A CG  1 
ATOM   1842 O  OD1 . ASN A 1 228 ? 2.952   -8.298  -1.078  1.00 24.40 ? 232 ASN A OD1 1 
ATOM   1843 N  ND2 . ASN A 1 228 ? 3.099   -7.136  -3.008  1.00 23.76 ? 232 ASN A ND2 1 
ATOM   1844 N  N   . GLY A 1 229 ? 3.609   -3.490  -1.982  1.00 23.95 ? 233 GLY A N   1 
ATOM   1845 C  CA  . GLY A 1 229 ? 2.999   -2.688  -3.042  1.00 23.59 ? 233 GLY A CA  1 
ATOM   1846 C  C   . GLY A 1 229 ? 2.977   -3.451  -4.370  1.00 24.90 ? 233 GLY A C   1 
ATOM   1847 O  O   . GLY A 1 229 ? 3.674   -4.435  -4.503  1.00 25.03 ? 233 GLY A O   1 
ATOM   1848 N  N   . GLU A 1 230 ? 2.171   -2.992  -5.342  1.00 24.92 ? 234 GLU A N   1 
ATOM   1849 C  CA  . GLU A 1 230 ? 2.116   -3.609  -6.660  1.00 28.94 ? 234 GLU A CA  1 
ATOM   1850 C  C   . GLU A 1 230 ? 3.516   -3.717  -7.259  1.00 28.57 ? 234 GLU A C   1 
ATOM   1851 O  O   . GLU A 1 230 ? 4.311   -2.789  -7.165  1.00 27.06 ? 234 GLU A O   1 
ATOM   1852 C  CB  . GLU A 1 230 ? 1.230   -2.770  -7.578  1.00 29.36 ? 234 GLU A CB  1 
ATOM   1853 C  CG  . GLU A 1 230 ? 0.971   -3.435  -8.918  1.00 32.86 ? 234 GLU A CG  1 
ATOM   1854 C  CD  . GLU A 1 230 ? 0.046   -2.629  -9.795  1.00 37.18 ? 234 GLU A CD  1 
ATOM   1855 O  OE1 . GLU A 1 230 ? -0.368  -1.512  -9.357  1.00 39.77 ? 234 GLU A OE1 1 
ATOM   1856 O  OE2 . GLU A 1 230 ? -0.211  -3.085  -10.933 1.00 37.50 ? 234 GLU A OE2 1 
ATOM   1857 N  N   . GLY A 1 231 ? 3.798   -4.873  -7.867  1.00 31.37 ? 235 GLY A N   1 
ATOM   1858 C  CA  . GLY A 1 231 ? 5.037   -5.105  -8.592  1.00 39.31 ? 235 GLY A CA  1 
ATOM   1859 C  C   . GLY A 1 231 ? 6.221   -5.305  -7.654  1.00 42.10 ? 235 GLY A C   1 
ATOM   1860 O  O   . GLY A 1 231 ? 7.370   -5.203  -8.082  1.00 38.45 ? 235 GLY A O   1 
ATOM   1861 N  N   . GLU A 1 232 ? 5.919   -5.548  -6.368  1.00 41.84 ? 236 GLU A N   1 
ATOM   1862 C  CA  . GLU A 1 232 ? 6.886   -6.070  -5.414  1.00 39.23 ? 236 GLU A CA  1 
ATOM   1863 C  C   . GLU A 1 232 ? 6.506   -7.517  -5.128  1.00 40.49 ? 236 GLU A C   1 
ATOM   1864 O  O   . GLU A 1 232 ? 5.395   -7.938  -5.466  1.00 40.12 ? 236 GLU A O   1 
ATOM   1865 C  CB  . GLU A 1 232 ? 6.891   -5.263  -4.113  1.00 48.01 ? 236 GLU A CB  1 
ATOM   1866 C  CG  . GLU A 1 232 ? 7.367   -3.832  -4.262  1.00 47.93 ? 236 GLU A CG  1 
ATOM   1867 C  CD  . GLU A 1 232 ? 7.005   -2.913  -3.105  1.00 53.36 ? 236 GLU A CD  1 
ATOM   1868 O  OE1 . GLU A 1 232 ? 6.443   -3.412  -2.092  1.00 57.38 ? 236 GLU A OE1 1 
ATOM   1869 O  OE2 . GLU A 1 232 ? 7.271   -1.693  -3.214  1.00 54.61 ? 236 GLU A OE2 1 
ATOM   1870 N  N   . PRO A 1 233 ? 7.408   -8.329  -4.522  1.00 34.96 ? 237 PRO A N   1 
ATOM   1871 C  CA  . PRO A 1 233 ? 7.127   -9.742  -4.273  1.00 33.92 ? 237 PRO A CA  1 
ATOM   1872 C  C   . PRO A 1 233 ? 6.011   -9.899  -3.236  1.00 29.93 ? 237 PRO A C   1 
ATOM   1873 O  O   . PRO A 1 233 ? 5.939   -9.105  -2.301  1.00 26.66 ? 237 PRO A O   1 
ATOM   1874 C  CB  . PRO A 1 233 ? 8.436   -10.297 -3.690  1.00 37.61 ? 237 PRO A CB  1 
ATOM   1875 C  CG  . PRO A 1 233 ? 9.490   -9.254  -4.002  1.00 38.30 ? 237 PRO A CG  1 
ATOM   1876 C  CD  . PRO A 1 233 ? 8.754   -7.934  -4.069  1.00 40.09 ? 237 PRO A CD  1 
ATOM   1877 N  N   . GLU A 1 234 ? 5.187   -10.937 -3.425  1.00 27.99 ? 238 GLU A N   1 
ATOM   1878 C  CA  . GLU A 1 234 ? 3.946   -11.108 -2.693  1.00 28.68 ? 238 GLU A CA  1 
ATOM   1879 C  C   . GLU A 1 234 ? 4.223   -11.525 -1.252  1.00 24.25 ? 238 GLU A C   1 
ATOM   1880 O  O   . GLU A 1 234 ? 4.782   -12.573 -0.986  1.00 24.63 ? 238 GLU A O   1 
ATOM   1881 C  CB  . GLU A 1 234 ? 3.013   -12.100 -3.401  1.00 29.28 ? 238 GLU A CB  1 
ATOM   1882 C  CG  . GLU A 1 234 ? 1.683   -12.215 -2.688  1.00 32.70 ? 238 GLU A CG  1 
ATOM   1883 C  CD  . GLU A 1 234 ? 0.551   -12.929 -3.385  1.00 35.08 ? 238 GLU A CD  1 
ATOM   1884 O  OE1 . GLU A 1 234 ? 0.804   -14.045 -3.929  1.00 40.12 ? 238 GLU A OE1 1 
ATOM   1885 O  OE2 . GLU A 1 234 ? -0.580  -12.366 -3.364  1.00 27.00 ? 238 GLU A OE2 1 
ATOM   1886 N  N   . GLU A 1 235 ? 3.641   -10.765 -0.321  1.00 23.48 ? 239 GLU A N   1 
ATOM   1887 C  CA  . GLU A 1 235 ? 3.692   -11.130 1.073   1.00 22.42 ? 239 GLU A CA  1 
ATOM   1888 C  C   . GLU A 1 235 ? 2.255   -11.032 1.580   1.00 16.97 ? 239 GLU A C   1 
ATOM   1889 O  O   . GLU A 1 235 ? 1.710   -9.944  1.541   1.00 19.37 ? 239 GLU A O   1 
ATOM   1890 C  CB  . GLU A 1 235 ? 4.563   -10.110 1.792   1.00 20.45 ? 239 GLU A CB  1 
ATOM   1891 N  N   . LEU A 1 236 ? 1.631   -12.173 1.915   1.00 17.03 ? 240 LEU A N   1 
ATOM   1892 C  CA  . LEU A 1 236 ? 0.193   -12.098 2.202   1.00 15.89 ? 240 LEU A CA  1 
ATOM   1893 C  C   . LEU A 1 236 ? 0.011   -11.272 3.484   1.00 14.75 ? 240 LEU A C   1 
ATOM   1894 O  O   . LEU A 1 236 ? 0.793   -11.429 4.434   1.00 18.19 ? 240 LEU A O   1 
ATOM   1895 C  CB  . LEU A 1 236 ? -0.346  -13.510 2.423   1.00 16.52 ? 240 LEU A CB  1 
ATOM   1896 C  CG  . LEU A 1 236 ? -0.443  -14.376 1.169   1.00 16.71 ? 240 LEU A CG  1 
ATOM   1897 C  CD1 . LEU A 1 236 ? -1.121  -15.695 1.482   1.00 21.62 ? 240 LEU A CD1 1 
ATOM   1898 C  CD2 . LEU A 1 236 ? -1.215  -13.634 0.099   1.00 17.64 ? 240 LEU A CD2 1 
ATOM   1899 N  N   . MET A 1 237 ? -1.022  -10.416 3.501   1.00 14.59 ? 241 MET A N   1 
ATOM   1900 C  CA  . MET A 1 237 ? -1.359  -9.611  4.685   1.00 14.30 ? 241 MET A CA  1 
ATOM   1901 C  C   . MET A 1 237 ? -2.166  -10.505 5.640   1.00 13.83 ? 241 MET A C   1 
ATOM   1902 O  O   . MET A 1 237 ? -3.386  -10.648 5.483   1.00 14.10 ? 241 MET A O   1 
ATOM   1903 C  CB  . MET A 1 237 ? -2.197  -8.384  4.291   1.00 13.78 ? 241 MET A CB  1 
ATOM   1904 C  CG  . MET A 1 237 ? -2.652  -7.438  5.482   1.00 14.16 ? 241 MET A CG  1 
ATOM   1905 S  SD  . MET A 1 237 ? -3.550  -6.037  4.931   1.00 16.92 ? 241 MET A SD  1 
ATOM   1906 C  CE  . MET A 1 237 ? -2.167  -5.027  4.351   1.00 13.10 ? 241 MET A CE  1 
ATOM   1907 N  N   . VAL A 1 238 ? -1.429  -11.206 6.508   1.00 13.69 ? 242 VAL A N   1 
ATOM   1908 C  CA  . VAL A 1 238 ? -2.013  -12.051 7.546   1.00 13.95 ? 242 VAL A CA  1 
ATOM   1909 C  C   . VAL A 1 238 ? -1.234  -11.810 8.834   1.00 14.60 ? 242 VAL A C   1 
ATOM   1910 O  O   . VAL A 1 238 ? -0.087  -11.349 8.828   1.00 15.52 ? 242 VAL A O   1 
ATOM   1911 C  CB  . VAL A 1 238 ? -2.037  -13.552 7.208   1.00 13.16 ? 242 VAL A CB  1 
ATOM   1912 C  CG1 . VAL A 1 238 ? -2.959  -13.848 6.010   1.00 14.33 ? 242 VAL A CG1 1 
ATOM   1913 C  CG2 . VAL A 1 238 ? -0.621  -14.111 7.014   1.00 15.20 ? 242 VAL A CG2 1 
ATOM   1914 N  N   . ASP A 1 239 ? -1.871  -12.126 9.969   1.00 11.47 ? 243 ASP A N   1 
ATOM   1915 C  CA  . ASP A 1 239 ? -1.163  -11.976 11.232  1.00 11.14 ? 243 ASP A CA  1 
ATOM   1916 C  C   . ASP A 1 239 ? -0.681  -10.550 11.427  1.00 10.53 ? 243 ASP A C   1 
ATOM   1917 O  O   . ASP A 1 239 ? 0.377   -10.345 12.009  1.00 13.54 ? 243 ASP A O   1 
ATOM   1918 C  CB  . ASP A 1 239 ? -0.102  -13.063 11.521  1.00 12.46 ? 243 ASP A CB  1 
ATOM   1919 C  CG  . ASP A 1 239 ? -0.694  -14.451 11.594  1.00 14.31 ? 243 ASP A CG  1 
ATOM   1920 O  OD1 . ASP A 1 239 ? -1.731  -14.620 12.228  1.00 12.73 ? 243 ASP A OD1 1 
ATOM   1921 O  OD2 . ASP A 1 239 ? -0.125  -15.376 10.924  1.00 15.39 ? 243 ASP A OD2 1 
ATOM   1922 N  N   . ASN A 1 240 ? -1.602  -9.603  11.233  1.00 10.76 ? 244 ASN A N   1 
ATOM   1923 C  CA  . ASN A 1 240 ? -1.261  -8.197  11.452  1.00 10.59 ? 244 ASN A CA  1 
ATOM   1924 C  C   . ASN A 1 240 ? -1.857  -7.779  12.803  1.00 10.16 ? 244 ASN A C   1 
ATOM   1925 O  O   . ASN A 1 240 ? -2.604  -6.790  12.861  1.00 11.16 ? 244 ASN A O   1 
ATOM   1926 C  CB  . ASN A 1 240 ? -1.851  -7.288  10.376  1.00 11.08 ? 244 ASN A CB  1 
ATOM   1927 C  CG  . ASN A 1 240 ? -3.319  -7.499  10.038  1.00 11.99 ? 244 ASN A CG  1 
ATOM   1928 O  OD1 . ASN A 1 240 ? -3.989  -8.379  10.621  1.00 12.06 ? 244 ASN A OD1 1 
ATOM   1929 N  ND2 . ASN A 1 240 ? -3.849  -6.622  9.193   1.00 11.77 ? 244 ASN A ND2 1 
ATOM   1930 N  N   . TRP A 1 241 ? -1.540  -8.560  13.832  1.00 9.14  ? 245 TRP A N   1 
ATOM   1931 C  CA  . TRP A 1 241 ? -1.965  -8.288  15.196  1.00 9.89  ? 245 TRP A CA  1 
ATOM   1932 C  C   . TRP A 1 241 ? -0.744  -8.185  16.108  1.00 10.07 ? 245 TRP A C   1 
ATOM   1933 O  O   . TRP A 1 241 ? 0.257   -8.895  15.959  1.00 10.48 ? 245 TRP A O   1 
ATOM   1934 C  CB  . TRP A 1 241 ? -2.912  -9.398  15.691  1.00 10.23 ? 245 TRP A CB  1 
ATOM   1935 C  CG  . TRP A 1 241 ? -2.462  -10.817 15.462  1.00 9.78  ? 245 TRP A CG  1 
ATOM   1936 C  CD1 . TRP A 1 241 ? -2.655  -11.580 14.342  1.00 10.03 ? 245 TRP A CD1 1 
ATOM   1937 C  CD2 . TRP A 1 241 ? -1.883  -11.690 16.441  1.00 10.86 ? 245 TRP A CD2 1 
ATOM   1938 N  NE1 . TRP A 1 241 ? -2.176  -12.860 14.549  1.00 10.45 ? 245 TRP A NE1 1 
ATOM   1939 C  CE2 . TRP A 1 241 ? -1.669  -12.946 15.823  1.00 11.42 ? 245 TRP A CE2 1 
ATOM   1940 C  CE3 . TRP A 1 241 ? -1.487  -11.526 17.770  1.00 12.23 ? 245 TRP A CE3 1 
ATOM   1941 C  CZ2 . TRP A 1 241 ? -1.073  -14.013 16.504  1.00 11.60 ? 245 TRP A CZ2 1 
ATOM   1942 C  CZ3 . TRP A 1 241 ? -0.921  -12.585 18.464  1.00 11.84 ? 245 TRP A CZ3 1 
ATOM   1943 C  CH2 . TRP A 1 241 ? -0.696  -13.810 17.819  1.00 12.58 ? 245 TRP A CH2 1 
ATOM   1944 N  N   . ARG A 1 242 ? -0.902  -7.342  17.153  1.00 9.26  ? 246 ARG A N   1 
ATOM   1945 C  CA  . ARG A 1 242 ? 0.080   -7.213  18.221  1.00 9.60  ? 246 ARG A CA  1 
ATOM   1946 C  C   . ARG A 1 242 ? -0.359  -8.112  19.372  1.00 11.03 ? 246 ARG A C   1 
ATOM   1947 O  O   . ARG A 1 242 ? -1.529  -8.183  19.674  1.00 12.82 ? 246 ARG A O   1 
ATOM   1948 C  CB  . ARG A 1 242 ? 0.026   -5.759  18.735  1.00 9.19  ? 246 ARG A CB  1 
ATOM   1949 C  CG  . ARG A 1 242 ? 1.175   -5.508  19.716  1.00 9.76  ? 246 ARG A CG  1 
ATOM   1950 C  CD  . ARG A 1 242 ? 1.108   -4.125  20.332  1.00 10.21 ? 246 ARG A CD  1 
ATOM   1951 N  NE  . ARG A 1 242 ? 2.354   -3.825  21.082  1.00 10.28 ? 246 ARG A NE  1 
ATOM   1952 C  CZ  . ARG A 1 242 ? 2.493   -2.819  21.937  1.00 12.75 ? 246 ARG A CZ  1 
ATOM   1953 N  NH1 . ARG A 1 242 ? 1.480   -2.002  22.169  1.00 10.62 ? 246 ARG A NH1 1 
ATOM   1954 N  NH2 . ARG A 1 242 ? 3.645   -2.633  22.558  1.00 12.84 ? 246 ARG A NH2 1 
ATOM   1955 N  N   . PRO A 1 243 ? 0.550   -8.895  19.991  1.00 11.23 ? 247 PRO A N   1 
ATOM   1956 C  CA  . PRO A 1 243 ? 0.176   -9.740  21.123  1.00 13.03 ? 247 PRO A CA  1 
ATOM   1957 C  C   . PRO A 1 243 ? -0.224  -8.916  22.346  1.00 11.92 ? 247 PRO A C   1 
ATOM   1958 O  O   . PRO A 1 243 ? 0.118   -7.726  22.471  1.00 12.58 ? 247 PRO A O   1 
ATOM   1959 C  CB  . PRO A 1 243 ? 1.475   -10.479 21.441  1.00 14.33 ? 247 PRO A CB  1 
ATOM   1960 C  CG  . PRO A 1 243 ? 2.277   -10.370 20.159  1.00 15.96 ? 247 PRO A CG  1 
ATOM   1961 C  CD  . PRO A 1 243 ? 1.960   -9.015  19.570  1.00 13.05 ? 247 PRO A CD  1 
ATOM   1962 N  N   . ALA A 1 244 ? -0.866  -9.602  23.277  1.00 11.66 ? 248 ALA A N   1 
ATOM   1963 C  CA  . ALA A 1 244 ? -1.253  -8.979  24.529  1.00 10.78 ? 248 ALA A CA  1 
ATOM   1964 C  C   . ALA A 1 244 ? -0.029  -8.446  25.265  1.00 11.78 ? 248 ALA A C   1 
ATOM   1965 O  O   . ALA A 1 244 ? 1.012   -9.104  25.361  1.00 14.06 ? 248 ALA A O   1 
ATOM   1966 C  CB  . ALA A 1 244 ? -2.005  -9.982  25.378  1.00 12.47 ? 248 ALA A CB  1 
ATOM   1967 N  N   . GLN A 1 245 ? -0.221  -7.280  25.891  1.00 10.81 ? 249 GLN A N   1 
ATOM   1968 C  CA  . GLN A 1 245 ? 0.802   -6.554  26.639  1.00 11.88 ? 249 GLN A CA  1 
ATOM   1969 C  C   . GLN A 1 245 ? 0.443   -6.611  28.117  1.00 12.91 ? 249 GLN A C   1 
ATOM   1970 O  O   . GLN A 1 245 ? -0.715  -6.832  28.508  1.00 11.70 ? 249 GLN A O   1 
ATOM   1971 C  CB  . GLN A 1 245 ? 0.824   -5.105  26.181  1.00 14.12 ? 249 GLN A CB  1 
ATOM   1972 C  CG  . GLN A 1 245 ? 1.117   -4.994  24.674  1.00 14.63 ? 249 GLN A CG  1 
ATOM   1973 C  CD  . GLN A 1 245 ? 2.452   -5.614  24.321  1.00 16.59 ? 249 GLN A CD  1 
ATOM   1974 O  OE1 . GLN A 1 245 ? 3.481   -5.341  24.949  1.00 18.76 ? 249 GLN A OE1 1 
ATOM   1975 N  NE2 . GLN A 1 245 ? 2.430   -6.536  23.391  1.00 16.70 ? 249 GLN A NE2 1 
ATOM   1976 N  N   . PRO A 1 246 ? 1.428   -6.413  29.026  1.00 15.24 ? 250 PRO A N   1 
ATOM   1977 C  CA  . PRO A 1 246 ? 1.089   -6.492  30.450  1.00 16.40 ? 250 PRO A CA  1 
ATOM   1978 C  C   . PRO A 1 246 ? 0.149   -5.376  30.904  1.00 14.95 ? 250 PRO A C   1 
ATOM   1979 O  O   . PRO A 1 246 ? 0.264   -4.217  30.490  1.00 16.32 ? 250 PRO A O   1 
ATOM   1980 C  CB  . PRO A 1 246 ? 2.444   -6.390  31.148  1.00 17.49 ? 250 PRO A CB  1 
ATOM   1981 C  CG  . PRO A 1 246 ? 3.351   -5.779  30.138  1.00 19.27 ? 250 PRO A CG  1 
ATOM   1982 C  CD  . PRO A 1 246 ? 2.844   -6.160  28.745  1.00 16.88 ? 250 PRO A CD  1 
ATOM   1983 N  N   . LEU A 1 247 ? -0.780  -5.781  31.779  1.00 16.22 ? 251 LEU A N   1 
ATOM   1984 C  CA  . LEU A 1 247 ? -1.856  -4.919  32.221  1.00 17.85 ? 251 LEU A CA  1 
ATOM   1985 C  C   . LEU A 1 247 ? -1.290  -3.861  33.173  1.00 17.48 ? 251 LEU A C   1 
ATOM   1986 O  O   . LEU A 1 247 ? -1.783  -2.735  33.213  1.00 15.17 ? 251 LEU A O   1 
ATOM   1987 C  CB  . LEU A 1 247 ? -2.905  -5.790  32.918  1.00 18.76 ? 251 LEU A CB  1 
ATOM   1988 C  CG  . LEU A 1 247 ? -4.221  -5.105  33.281  1.00 19.35 ? 251 LEU A CG  1 
ATOM   1989 C  CD1 . LEU A 1 247 ? -4.908  -4.531  32.025  1.00 15.99 ? 251 LEU A CD1 1 
ATOM   1990 C  CD2 . LEU A 1 247 ? -5.121  -6.128  33.961  1.00 21.71 ? 251 LEU A CD2 1 
ATOM   1991 N  N   . LYS A 1 248 ? -0.208  -4.207  33.894  1.00 17.04 ? 252 LYS A N   1 
ATOM   1992 C  CA  . LYS A 1 248 ? 0.468   -3.251  34.778  1.00 17.15 ? 252 LYS A CA  1 
ATOM   1993 C  C   . LYS A 1 248 ? -0.547  -2.760  35.803  1.00 18.13 ? 252 LYS A C   1 
ATOM   1994 O  O   . LYS A 1 248 ? -1.371  -3.548  36.291  1.00 20.75 ? 252 LYS A O   1 
ATOM   1995 C  CB  . LYS A 1 248 ? 1.272   -2.199  34.001  1.00 18.77 ? 252 LYS A CB  1 
ATOM   1996 C  CG  . LYS A 1 248 ? 2.467   -2.827  33.300  1.00 19.53 ? 252 LYS A CG  1 
ATOM   1997 C  CD  . LYS A 1 248 ? 3.362   -1.880  32.565  1.00 20.82 ? 252 LYS A CD  1 
ATOM   1998 C  CE  . LYS A 1 248 ? 4.652   -2.548  32.130  1.00 24.92 ? 252 LYS A CE  1 
ATOM   1999 N  NZ  . LYS A 1 248 ? 5.436   -1.669  31.238  1.00 23.63 ? 252 LYS A NZ  1 
ATOM   2000 N  N   . ASN A 1 249 ? -0.508  -1.462  36.093  1.00 17.79 ? 253 ASN A N   1 
ATOM   2001 C  CA  . ASN A 1 249 ? -1.354  -0.892  37.129  1.00 23.87 ? 253 ASN A CA  1 
ATOM   2002 C  C   . ASN A 1 249 ? -2.697  -0.432  36.552  1.00 22.21 ? 253 ASN A C   1 
ATOM   2003 O  O   . ASN A 1 249 ? -2.988  0.777   36.606  1.00 24.84 ? 253 ASN A O   1 
ATOM   2004 C  CB  . ASN A 1 249 ? -0.648  0.280   37.820  1.00 31.93 ? 253 ASN A CB  1 
ATOM   2005 C  CG  . ASN A 1 249 ? -1.427  0.785   39.019  1.00 41.83 ? 253 ASN A CG  1 
ATOM   2006 O  OD1 . ASN A 1 249 ? -1.759  0.013   39.924  1.00 48.84 ? 253 ASN A OD1 1 
ATOM   2007 N  ND2 . ASN A 1 249 ? -1.761  2.070   39.017  1.00 47.99 ? 253 ASN A ND2 1 
ATOM   2008 N  N   . ARG A 1 250 ? -3.470  -1.378  35.956  1.00 15.98 ? 254 ARG A N   1 
ATOM   2009 C  CA  . ARG A 1 250 ? -4.737  -1.036  35.343  1.00 14.96 ? 254 ARG A CA  1 
ATOM   2010 C  C   . ARG A 1 250 ? -5.766  -2.075  35.757  1.00 15.94 ? 254 ARG A C   1 
ATOM   2011 O  O   . ARG A 1 250 ? -5.441  -3.238  35.936  1.00 19.17 ? 254 ARG A O   1 
ATOM   2012 C  CB  . ARG A 1 250 ? -4.664  -1.018  33.800  1.00 13.81 ? 254 ARG A CB  1 
ATOM   2013 C  CG  . ARG A 1 250 ? -3.822  0.125   33.250  1.00 12.99 ? 254 ARG A CG  1 
ATOM   2014 C  CD  . ARG A 1 250 ? -3.786  0.097   31.720  1.00 14.13 ? 254 ARG A CD  1 
ATOM   2015 N  NE  . ARG A 1 250 ? -2.904  -0.997  31.319  1.00 12.92 ? 254 ARG A NE  1 
ATOM   2016 C  CZ  . ARG A 1 250 ? -2.648  -1.264  30.036  1.00 11.38 ? 254 ARG A CZ  1 
ATOM   2017 N  NH1 . ARG A 1 250 ? -3.291  -0.576  29.090  1.00 11.66 ? 254 ARG A NH1 1 
ATOM   2018 N  NH2 . ARG A 1 250 ? -1.812  -2.240  29.718  1.00 9.95  ? 254 ARG A NH2 1 
ATOM   2019 N  N   . GLN A 1 251 ? -7.038  -1.668  35.804  1.00 16.62 ? 255 GLN A N   1 
ATOM   2020 C  CA  . GLN A 1 251 ? -8.128  -2.606  36.046  1.00 19.44 ? 255 GLN A CA  1 
ATOM   2021 C  C   . GLN A 1 251 ? -9.087  -2.541  34.860  1.00 18.67 ? 255 GLN A C   1 
ATOM   2022 O  O   . GLN A 1 251 ? -9.397  -1.456  34.367  1.00 21.86 ? 255 GLN A O   1 
ATOM   2023 C  CB  . GLN A 1 251 ? -8.954  -2.042  37.200  1.00 25.72 ? 255 GLN A CB  1 
ATOM   2024 C  CG  . GLN A 1 251 ? -8.854  -2.842  38.488  1.00 36.57 ? 255 GLN A CG  1 
ATOM   2025 C  CD  . GLN A 1 251 ? -10.114 -3.655  38.676  1.00 42.51 ? 255 GLN A CD  1 
ATOM   2026 O  OE1 . GLN A 1 251 ? -10.274 -4.738  38.103  1.00 53.59 ? 255 GLN A OE1 1 
ATOM   2027 N  NE2 . GLN A 1 251 ? -11.034 -3.124  39.476  1.00 43.05 ? 255 GLN A NE2 1 
ATOM   2028 N  N   . ILE A 1 252 ? -9.484  -3.701  34.356  1.00 14.87 ? 256 ILE A N   1 
ATOM   2029 C  CA  . ILE A 1 252 ? -10.513 -3.712  33.319  1.00 13.92 ? 256 ILE A CA  1 
ATOM   2030 C  C   . ILE A 1 252 ? -11.869 -3.666  34.008  1.00 13.94 ? 256 ILE A C   1 
ATOM   2031 O  O   . ILE A 1 252 ? -12.027 -4.373  34.982  1.00 14.50 ? 256 ILE A O   1 
ATOM   2032 C  CB  . ILE A 1 252 ? -10.351 -4.971  32.458  1.00 12.36 ? 256 ILE A CB  1 
ATOM   2033 C  CG1 . ILE A 1 252 ? -8.951  -4.990  31.820  1.00 15.01 ? 256 ILE A CG1 1 
ATOM   2034 C  CG2 . ILE A 1 252 ? -11.484 -5.112  31.411  1.00 13.09 ? 256 ILE A CG2 1 
ATOM   2035 C  CD1 . ILE A 1 252 ? -8.663  -6.299  31.117  1.00 16.27 ? 256 ILE A CD1 1 
ATOM   2036 N  N   . LYS A 1 253 ? -12.802 -2.838  33.520  1.00 13.81 ? 257 LYS A N   1 
ATOM   2037 C  CA  . LYS A 1 253 ? -14.126 -2.678  34.112  1.00 13.69 ? 257 LYS A CA  1 
ATOM   2038 C  C   . LYS A 1 253 ? -15.123 -3.307  33.152  1.00 15.15 ? 257 LYS A C   1 
ATOM   2039 O  O   . LYS A 1 253 ? -14.928 -3.304  31.931  1.00 13.85 ? 257 LYS A O   1 
ATOM   2040 C  CB  . LYS A 1 253 ? -14.417 -1.190  34.374  1.00 14.98 ? 257 LYS A CB  1 
ATOM   2041 C  CG  . LYS A 1 253 ? -13.528 -0.519  35.442  1.00 19.12 ? 257 LYS A CG  1 
ATOM   2042 C  CD  . LYS A 1 253 ? -14.074 -1.213  36.819  0.00 13.84 ? 257 LYS A CD  1 
ATOM   2043 C  CE  . LYS A 1 253 ? -13.099 -0.783  37.908  0.00 11.88 ? 257 LYS A CE  1 
ATOM   2044 N  NZ  . LYS A 1 253 ? -13.381 0.575   38.434  0.00 12.86 ? 257 LYS A NZ  1 
ATOM   2045 N  N   . ALA A 1 254 ? -16.143 -3.949  33.710  1.00 13.91 ? 258 ALA A N   1 
ATOM   2046 C  CA  . ALA A 1 254 ? -17.181 -4.554  32.884  1.00 14.84 ? 258 ALA A CA  1 
ATOM   2047 C  C   . ALA A 1 254 ? -18.491 -3.821  33.103  1.00 15.67 ? 258 ALA A C   1 
ATOM   2048 O  O   . ALA A 1 254 ? -18.783 -3.369  34.225  1.00 16.51 ? 258 ALA A O   1 
ATOM   2049 C  CB  . ALA A 1 254 ? -17.360 -6.032  33.157  1.00 14.26 ? 258 ALA A CB  1 
ATOM   2050 N  N   . SER A 1 255 ? -19.288 -3.717  32.032  1.00 13.17 ? 259 SER A N   1 
ATOM   2051 C  CA  . SER A 1 255 ? -20.537 -2.973  32.071  1.00 15.55 ? 259 SER A CA  1 
ATOM   2052 C  C   . SER A 1 255 ? -21.655 -3.942  32.427  1.00 16.76 ? 259 SER A C   1 
ATOM   2053 O  O   . SER A 1 255 ? -22.820 -3.535  32.532  1.00 20.61 ? 259 SER A O   1 
ATOM   2054 C  CB  . SER A 1 255 ? -20.824 -2.345  30.697  1.00 13.69 ? 259 SER A CB  1 
ATOM   2055 O  OG  . SER A 1 255 ? -21.298 -3.328  29.774  1.00 14.74 ? 259 SER A OG  1 
ATOM   2056 N  N   . PHE A 1 256 ? -21.301 -5.205  32.654  1.00 17.04 ? 260 PHE A N   1 
ATOM   2057 C  CA  . PHE A 1 256 ? -22.293 -6.265  32.800  1.00 19.24 ? 260 PHE A CA  1 
ATOM   2058 C  C   . PHE A 1 256 ? -21.799 -7.258  33.844  1.00 23.00 ? 260 PHE A C   1 
ATOM   2059 O  O   . PHE A 1 256 ? -20.598 -7.334  34.118  1.00 22.52 ? 260 PHE A O   1 
ATOM   2060 C  CB  . PHE A 1 256 ? -22.545 -6.997  31.473  1.00 21.00 ? 260 PHE A CB  1 
ATOM   2061 C  CG  . PHE A 1 256 ? -21.318 -7.698  30.930  1.00 18.04 ? 260 PHE A CG  1 
ATOM   2062 C  CD1 . PHE A 1 256 ? -20.329 -6.966  30.282  1.00 18.45 ? 260 PHE A CD1 1 
ATOM   2063 C  CD2 . PHE A 1 256 ? -21.091 -9.050  31.169  1.00 18.90 ? 260 PHE A CD2 1 
ATOM   2064 C  CE1 . PHE A 1 256 ? -19.180 -7.598  29.830  1.00 18.06 ? 260 PHE A CE1 1 
ATOM   2065 C  CE2 . PHE A 1 256 ? -19.922 -9.665  30.746  1.00 19.41 ? 260 PHE A CE2 1 
ATOM   2066 C  CZ  . PHE A 1 256 ? -18.971 -8.935  30.055  1.00 18.38 ? 260 PHE A CZ  1 
ATOM   2067 N  N   . LYS A 1 257 ? -22.775 -8.044  34.337  1.00 29.08 ? 261 LYS A N   1 
ATOM   2068 C  CA  . LYS A 1 257 ? -22.741 -9.094  35.353  1.00 40.71 ? 261 LYS A CA  1 
ATOM   2069 C  C   . LYS A 1 257 ? -21.919 -8.713  36.585  1.00 46.66 ? 261 LYS A C   1 
ATOM   2070 O  O   . LYS A 1 257 ? -20.698 -8.571  36.552  0.01 47.44 ? 261 LYS A O   1 
ATOM   2071 C  CB  . LYS A 1 257 ? -22.381 -10.458 34.763  1.00 40.65 ? 261 LYS A CB  1 
ATOM   2072 C  CG  . LYS A 1 257 ? -23.243 -10.891 33.581  1.00 42.58 ? 261 LYS A CG  1 
ATOM   2073 C  CD  . LYS A 1 257 ? -22.626 -12.080 32.836  1.00 51.05 ? 261 LYS A CD  1 
ATOM   2074 C  CE  . LYS A 1 257 ? -21.113 -12.135 32.992  1.00 53.38 ? 261 LYS A CE  1 
ATOM   2075 N  NZ  . LYS A 1 257 ? -20.529 -13.421 32.544  1.00 59.26 ? 261 LYS A NZ  1 
ATOM   2076 O  OXT . LYS A 1 257 ? -22.508 -8.563  37.663  1.00 57.77 ? 261 LYS A OXT 1 
HETATM 2077 ZN ZN  . ZN  B 2 .   ? -6.516  -1.705  15.303  1.00 8.96  ? 301 ZN  A ZN  1 
HETATM 2078 NA NA  . NA  C 3 .   ? -17.848 -22.047 6.160   1.00 22.46 ? 302 NA  A NA  1 
HETATM 2079 F  F13 . 5DU D 4 .   ? -4.895  3.163   11.290  1.00 33.71 ? 303 5DU A F13 1 
HETATM 2080 C  C9  . 5DU D 4 .   ? -4.564  2.079   12.064  1.00 27.16 ? 303 5DU A C9  1 
HETATM 2081 C  C8  . 5DU D 4 .   ? -3.879  0.960   11.573  1.00 25.19 ? 303 5DU A C8  1 
HETATM 2082 S  S24 . 5DU D 4 .   ? -3.318  0.730   9.874   1.00 32.17 ? 303 5DU A S24 1 
HETATM 2083 C  C25 . 5DU D 4 .   ? -2.434  2.329   9.643   1.00 32.48 ? 303 5DU A C25 1 
HETATM 2084 C  C26 . 5DU D 4 .   ? -1.149  2.151   10.427  1.00 32.78 ? 303 5DU A C26 1 
HETATM 2085 O  O27 . 5DU D 4 .   ? -0.330  3.291   10.276  1.00 30.51 ? 303 5DU A O27 1 
HETATM 2086 C  C7  . 5DU D 4 .   ? -3.603  -0.112  12.384  1.00 24.02 ? 303 5DU A C7  1 
HETATM 2087 F  F12 . 5DU D 4 .   ? -2.899  -1.181  11.921  1.00 24.72 ? 303 5DU A F12 1 
HETATM 2088 C  C6  . 5DU D 4 .   ? -3.974  -0.069  13.715  1.00 20.02 ? 303 5DU A C6  1 
HETATM 2089 F  F11 . 5DU D 4 .   ? -3.624  -1.099  14.539  1.00 21.30 ? 303 5DU A F11 1 
HETATM 2090 C  C10 . 5DU D 4 .   ? -4.926  2.144   13.432  1.00 22.00 ? 303 5DU A C10 1 
HETATM 2091 C  C5  . 5DU D 4 .   ? -4.589  1.029   14.262  1.00 19.32 ? 303 5DU A C5  1 
HETATM 2092 S  S1  . 5DU D 4 .   ? -5.092  0.938   16.016  1.00 18.39 ? 303 5DU A S1  1 
HETATM 2093 O  O3  . 5DU D 4 .   ? -3.947  1.428   16.908  1.00 18.56 ? 303 5DU A O3  1 
HETATM 2094 N  N4  . 5DU D 4 .   ? -5.298  -0.697  16.360  1.00 16.12 ? 303 5DU A N4  1 
HETATM 2095 O  O2  . 5DU D 4 .   ? -6.336  1.636   16.295  1.00 20.21 ? 303 5DU A O2  1 
HETATM 2096 N  N14 . 5DU D 4 .   ? -5.616  3.274   13.925  1.00 28.92 ? 303 5DU A N14 1 
HETATM 2097 C  C15 . 5DU D 4 .   ? -5.366  4.616   13.463  1.00 33.92 ? 303 5DU A C15 1 
HETATM 2098 C  C19 . 5DU D 4 .   ? -3.966  5.076   13.704  1.00 33.49 ? 303 5DU A C19 1 
HETATM 2099 C  C20 . 5DU D 4 .   ? -2.780  4.375   13.820  1.00 30.93 ? 303 5DU A C20 1 
HETATM 2100 C  C21 . 5DU D 4 .   ? -1.579  5.095   14.025  1.00 30.75 ? 303 5DU A C21 1 
HETATM 2101 C  C22 . 5DU D 4 .   ? -1.563  6.505   14.115  1.00 32.62 ? 303 5DU A C22 1 
HETATM 2102 C  C23 . 5DU D 4 .   ? -2.783  7.185   14.001  1.00 38.39 ? 303 5DU A C23 1 
HETATM 2103 C  C18 . 5DU D 4 .   ? -3.952  6.439   13.780  1.00 37.70 ? 303 5DU A C18 1 
HETATM 2104 C  C17 . 5DU D 4 .   ? -5.357  6.900   13.607  1.00 43.13 ? 303 5DU A C17 1 
HETATM 2105 C  C16 . 5DU D 4 .   ? -6.056  5.697   14.282  1.00 37.49 ? 303 5DU A C16 1 
HETATM 2106 S  S   . DMS E 5 .   ? 1.782   -11.688 14.967  1.00 57.65 ? 304 DMS A S   1 
HETATM 2107 O  O   . DMS E 5 .   ? 2.400   -13.021 14.551  1.00 55.06 ? 304 DMS A O   1 
HETATM 2108 C  C1  . DMS E 5 .   ? 2.890   -10.436 14.362  1.00 50.39 ? 304 DMS A C1  1 
HETATM 2109 C  C2  . DMS E 5 .   ? 2.117   -11.524 16.705  1.00 45.26 ? 304 DMS A C2  1 
HETATM 2110 C  C   . BEZ F 6 .   ? -10.663 -11.856 -3.730  1.00 35.27 ? 305 BEZ A C   1 
HETATM 2111 O  O1  . BEZ F 6 .   ? -10.461 -12.870 -4.453  1.00 41.79 ? 305 BEZ A O1  1 
HETATM 2112 O  O2  . BEZ F 6 .   ? -11.779 -11.499 -3.300  1.00 35.36 ? 305 BEZ A O2  1 
HETATM 2113 C  C1  . BEZ F 6 .   ? -9.469  -11.018 -3.364  1.00 34.01 ? 305 BEZ A C1  1 
HETATM 2114 C  C2  . BEZ F 6 .   ? -9.423  -10.349 -2.147  1.00 27.32 ? 305 BEZ A C2  1 
HETATM 2115 C  C3  . BEZ F 6 .   ? -8.328  -9.566  -1.826  1.00 29.17 ? 305 BEZ A C3  1 
HETATM 2116 C  C4  . BEZ F 6 .   ? -7.260  -9.467  -2.691  1.00 30.91 ? 305 BEZ A C4  1 
HETATM 2117 C  C5  . BEZ F 6 .   ? -7.301  -10.127 -3.905  1.00 28.76 ? 305 BEZ A C5  1 
HETATM 2118 C  C6  . BEZ F 6 .   ? -8.395  -10.909 -4.239  1.00 31.10 ? 305 BEZ A C6  1 
HETATM 2119 O  O   . HOH G 7 .   ? -7.344  6.165   6.321   1.00 36.70 ? 401 HOH A O   1 
HETATM 2120 O  O   . HOH G 7 .   ? -22.580 -14.398 11.146  1.00 18.60 ? 402 HOH A O   1 
HETATM 2121 O  O   . HOH G 7 .   ? -14.239 -18.390 18.946  1.00 34.26 ? 403 HOH A O   1 
HETATM 2122 O  O   . HOH G 7 .   ? -14.127 -16.707 28.779  1.00 32.86 ? 404 HOH A O   1 
HETATM 2123 O  O   . HOH G 7 .   ? 11.236  -12.354 15.383  1.00 34.36 ? 405 HOH A O   1 
HETATM 2124 O  O   . HOH G 7 .   ? -13.804 -8.865  -5.265  1.00 19.25 ? 406 HOH A O   1 
HETATM 2125 O  O   . HOH G 7 .   ? -10.549 -15.682 33.797  1.00 41.22 ? 407 HOH A O   1 
HETATM 2126 O  O   . HOH G 7 .   ? -7.661  -19.403 19.221  1.00 35.24 ? 408 HOH A O   1 
HETATM 2127 O  O   . HOH G 7 .   ? -18.351 -20.643 14.999  1.00 39.72 ? 409 HOH A O   1 
HETATM 2128 O  O   . HOH G 7 .   ? 4.754   -3.573  26.308  1.00 18.59 ? 410 HOH A O   1 
HETATM 2129 O  O   . HOH G 7 .   ? -8.445  -3.839  7.792   1.00 18.13 ? 411 HOH A O   1 
HETATM 2130 O  O   . HOH G 7 .   ? 2.717   -12.925 5.126   1.00 39.05 ? 412 HOH A O   1 
HETATM 2131 O  O   . HOH G 7 .   ? -0.505  14.159  16.448  1.00 32.83 ? 413 HOH A O   1 
HETATM 2132 O  O   . HOH G 7 .   ? -18.927 -12.055 -3.386  1.00 26.23 ? 414 HOH A O   1 
HETATM 2133 O  O   . HOH G 7 .   ? -15.126 19.455  13.438  1.00 29.51 ? 415 HOH A O   1 
HETATM 2134 O  O   . HOH G 7 .   ? -1.099  23.239  17.933  1.00 33.06 ? 416 HOH A O   1 
HETATM 2135 O  O   . HOH G 7 .   ? -6.030  -4.681  -6.574  1.00 26.82 ? 417 HOH A O   1 
HETATM 2136 O  O   . HOH G 7 .   ? -19.055 17.534  18.703  1.00 33.22 ? 418 HOH A O   1 
HETATM 2137 O  O   . HOH G 7 .   ? -24.062 8.714   20.372  1.00 31.05 ? 419 HOH A O   1 
HETATM 2138 O  O   . HOH G 7 .   ? -25.221 -3.407  31.638  1.00 30.14 ? 420 HOH A O   1 
HETATM 2139 O  O   . HOH G 7 .   ? -3.595  -13.138 -2.904  1.00 28.57 ? 421 HOH A O   1 
HETATM 2140 O  O   . HOH G 7 .   ? -4.668  -12.040 31.970  1.00 25.47 ? 422 HOH A O   1 
HETATM 2141 O  O   . HOH G 7 .   ? -9.862  1.081   34.282  1.00 38.78 ? 423 HOH A O   1 
HETATM 2142 O  O   . HOH G 7 .   ? -19.535 17.374  6.178   1.00 22.11 ? 424 HOH A O   1 
HETATM 2143 O  O   . HOH G 7 .   ? -19.738 -17.035 3.016   1.00 27.43 ? 425 HOH A O   1 
HETATM 2144 O  O   . HOH G 7 .   ? -29.479 9.670   6.519   1.00 40.89 ? 426 HOH A O   1 
HETATM 2145 O  O   . HOH G 7 .   ? 2.137   7.985   27.914  1.00 31.85 ? 427 HOH A O   1 
HETATM 2146 O  O   . HOH G 7 .   ? 0.312   -1.204  -4.898  1.00 25.86 ? 428 HOH A O   1 
HETATM 2147 O  O   . HOH G 7 .   ? -8.452  -15.293 36.989  1.00 27.16 ? 429 HOH A O   1 
HETATM 2148 O  O   . HOH G 7 .   ? 1.908   12.271  23.053  1.00 33.55 ? 430 HOH A O   1 
HETATM 2149 O  O   . HOH G 7 .   ? 6.648   -10.800 14.867  1.00 36.56 ? 431 HOH A O   1 
HETATM 2150 O  O   . HOH G 7 .   ? 15.900  3.916   15.376  1.00 30.08 ? 432 HOH A O   1 
HETATM 2151 O  O   . HOH G 7 .   ? -6.758  -14.936 31.498  1.00 21.72 ? 433 HOH A O   1 
HETATM 2152 O  O   . HOH G 7 .   ? 0.287   -19.559 10.916  1.00 35.13 ? 434 HOH A O   1 
HETATM 2153 O  O   . HOH G 7 .   ? -21.104 -6.683  -2.054  1.00 30.48 ? 435 HOH A O   1 
HETATM 2154 O  O   . HOH G 7 .   ? 9.925   -4.531  -8.086  1.00 36.42 ? 436 HOH A O   1 
HETATM 2155 O  O   . HOH G 7 .   ? -19.215 -20.790 4.946   1.00 23.82 ? 437 HOH A O   1 
HETATM 2156 O  O   . HOH G 7 .   ? -10.513 8.617   25.675  1.00 16.60 ? 438 HOH A O   1 
HETATM 2157 O  O   . HOH G 7 .   ? -10.304 -18.209 16.962  1.00 27.19 ? 439 HOH A O   1 
HETATM 2158 O  O   . HOH G 7 .   ? 11.382  -7.071  22.463  1.00 30.62 ? 440 HOH A O   1 
HETATM 2159 O  O   . HOH G 7 .   ? -7.782  -15.399 11.272  1.00 10.80 ? 441 HOH A O   1 
HETATM 2160 O  O   . HOH G 7 .   ? -12.358 16.334  8.987   1.00 41.02 ? 442 HOH A O   1 
HETATM 2161 O  O   . HOH G 7 .   ? 16.030  2.758   20.819  1.00 37.65 ? 443 HOH A O   1 
HETATM 2162 O  O   . HOH G 7 .   ? -16.108 15.877  23.616  1.00 24.85 ? 444 HOH A O   1 
HETATM 2163 O  O   . HOH G 7 .   ? 7.944   -5.771  -10.622 1.00 32.40 ? 445 HOH A O   1 
HETATM 2164 O  O   . HOH G 7 .   ? -19.157 10.080  8.957   1.00 17.38 ? 446 HOH A O   1 
HETATM 2165 O  O   . HOH G 7 .   ? -25.693 9.701   13.531  1.00 37.57 ? 447 HOH A O   1 
HETATM 2166 O  O   . HOH G 7 .   ? -21.796 5.664   4.742   1.00 16.34 ? 448 HOH A O   1 
HETATM 2167 O  O   . HOH G 7 .   ? -23.075 -0.884  34.426  1.00 29.09 ? 449 HOH A O   1 
HETATM 2168 O  O   . HOH G 7 .   ? -12.998 -9.030  -3.177  1.00 24.34 ? 450 HOH A O   1 
HETATM 2169 O  O   . HOH G 7 .   ? -4.349  -13.453 17.854  1.00 12.42 ? 451 HOH A O   1 
HETATM 2170 O  O   . HOH G 7 .   ? 15.521  -2.732  14.431  1.00 23.70 ? 452 HOH A O   1 
HETATM 2171 O  O   . HOH G 7 .   ? 3.869   5.015   29.686  1.00 19.81 ? 453 HOH A O   1 
HETATM 2172 O  O   . HOH G 7 .   ? -25.534 -10.595 17.731  1.00 30.06 ? 454 HOH A O   1 
HETATM 2173 O  O   . HOH G 7 .   ? -16.422 -15.400 32.776  1.00 36.20 ? 455 HOH A O   1 
HETATM 2174 O  O   . HOH G 7 .   ? 2.919   -4.215  7.931   1.00 22.29 ? 456 HOH A O   1 
HETATM 2175 O  O   . HOH G 7 .   ? -1.139  -4.143  15.684  1.00 10.84 ? 457 HOH A O   1 
HETATM 2176 O  O   . HOH G 7 .   ? 10.740  -9.124  8.972   1.00 40.81 ? 458 HOH A O   1 
HETATM 2177 O  O   . HOH G 7 .   ? -3.603  -15.932 24.205  1.00 16.56 ? 459 HOH A O   1 
HETATM 2178 O  O   . HOH G 7 .   ? 0.152   0.945   34.514  1.00 25.71 ? 460 HOH A O   1 
HETATM 2179 O  O   . HOH G 7 .   ? 8.728   -3.922  21.016  1.00 17.11 ? 461 HOH A O   1 
HETATM 2180 O  O   . HOH G 7 .   ? -22.447 -5.717  3.128   1.00 22.45 ? 462 HOH A O   1 
HETATM 2181 O  O   . HOH G 7 .   ? -21.066 7.741   1.845   1.00 17.21 ? 463 HOH A O   1 
HETATM 2182 O  O   . HOH G 7 .   ? -26.008 5.905   26.986  1.00 32.34 ? 464 HOH A O   1 
HETATM 2183 O  O   . HOH G 7 .   ? -1.238  8.900   28.323  1.00 35.63 ? 465 HOH A O   1 
HETATM 2184 O  O   . HOH G 7 .   ? 4.774   -6.556  7.975   1.00 32.75 ? 466 HOH A O   1 
HETATM 2185 O  O   . HOH G 7 .   ? -23.130 -2.923  6.762   1.00 23.53 ? 467 HOH A O   1 
HETATM 2186 O  O   . HOH G 7 .   ? 1.630   -11.726 24.927  1.00 25.77 ? 468 HOH A O   1 
HETATM 2187 O  O   . HOH G 7 .   ? -16.877 -8.444  20.405  1.00 9.85  ? 469 HOH A O   1 
HETATM 2188 O  O   . HOH G 7 .   ? -4.233  -8.930  31.210  1.00 31.94 ? 470 HOH A O   1 
HETATM 2189 O  O   . HOH G 7 .   ? 13.815  -0.791  7.133   1.00 35.64 ? 471 HOH A O   1 
HETATM 2190 O  O   . HOH G 7 .   ? -27.031 -12.923 20.374  1.00 37.05 ? 472 HOH A O   1 
HETATM 2191 O  O   . HOH G 7 .   ? -24.868 20.329  8.563   1.00 52.42 ? 473 HOH A O   1 
HETATM 2192 O  O   . HOH G 7 .   ? 5.531   7.174   20.292  1.00 19.28 ? 474 HOH A O   1 
HETATM 2193 O  O   . HOH G 7 .   ? 3.728   -8.963  25.700  1.00 29.81 ? 475 HOH A O   1 
HETATM 2194 O  O   . HOH G 7 .   ? -14.762 9.114   31.925  1.00 38.19 ? 476 HOH A O   1 
HETATM 2195 O  O   . HOH G 7 .   ? -16.022 -12.466 24.366  1.00 21.19 ? 477 HOH A O   1 
HETATM 2196 O  O   . HOH G 7 .   ? -11.525 -3.145  42.181  1.00 51.41 ? 478 HOH A O   1 
HETATM 2197 O  O   . HOH G 7 .   ? -17.782 -20.622 8.082   1.00 14.98 ? 479 HOH A O   1 
HETATM 2198 O  O   . HOH G 7 .   ? -20.904 8.142   30.136  1.00 38.07 ? 480 HOH A O   1 
HETATM 2199 O  O   . HOH G 7 .   ? -2.447  -8.880  29.165  1.00 14.40 ? 481 HOH A O   1 
HETATM 2200 O  O   . HOH G 7 .   ? 8.483   3.203   27.820  1.00 31.22 ? 482 HOH A O   1 
HETATM 2201 O  O   . HOH G 7 .   ? -13.319 -22.359 11.716  1.00 26.22 ? 483 HOH A O   1 
HETATM 2202 O  O   . HOH G 7 .   ? -25.908 -6.083  13.235  1.00 36.63 ? 484 HOH A O   1 
HETATM 2203 O  O   . HOH G 7 .   ? -3.272  -13.253 25.159  1.00 15.37 ? 485 HOH A O   1 
HETATM 2204 O  O   . HOH G 7 .   ? -14.824 20.039  17.529  1.00 33.58 ? 486 HOH A O   1 
HETATM 2205 O  O   . HOH G 7 .   ? -23.108 15.960  4.658   1.00 29.95 ? 487 HOH A O   1 
HETATM 2206 O  O   . HOH G 7 .   ? -13.891 -4.983  -6.444  1.00 31.58 ? 488 HOH A O   1 
HETATM 2207 O  O   . HOH G 7 .   ? 2.148   -15.695 9.362   1.00 31.46 ? 489 HOH A O   1 
HETATM 2208 O  O   . HOH G 7 .   ? -8.639  0.676   -6.737  1.00 32.07 ? 490 HOH A O   1 
HETATM 2209 O  O   . HOH G 7 .   ? 0.165   -14.413 30.967  1.00 43.62 ? 491 HOH A O   1 
HETATM 2210 O  O   . HOH G 7 .   ? -18.472 -3.639  -2.549  1.00 32.12 ? 492 HOH A O   1 
HETATM 2211 O  O   . HOH G 7 .   ? -21.452 -7.236  23.531  1.00 13.72 ? 493 HOH A O   1 
HETATM 2212 O  O   . HOH G 7 .   ? -3.253  -11.186 20.783  1.00 14.08 ? 494 HOH A O   1 
HETATM 2213 O  O   . HOH G 7 .   ? -18.104 10.363  11.422  1.00 20.01 ? 495 HOH A O   1 
HETATM 2214 O  O   . HOH G 7 .   ? 4.273   4.560   10.768  1.00 36.49 ? 496 HOH A O   1 
HETATM 2215 O  O   . HOH G 7 .   ? 4.190   -2.478  28.658  1.00 30.62 ? 497 HOH A O   1 
HETATM 2216 O  O   . HOH G 7 .   ? -20.358 10.806  26.519  1.00 20.98 ? 498 HOH A O   1 
HETATM 2217 O  O   . HOH G 7 .   ? -7.222  -8.916  32.534  1.00 19.81 ? 499 HOH A O   1 
HETATM 2218 O  O   . HOH G 7 .   ? -14.155 10.527  27.818  1.00 22.86 ? 500 HOH A O   1 
HETATM 2219 O  O   . HOH G 7 .   ? -23.853 -0.417  31.633  1.00 33.72 ? 501 HOH A O   1 
HETATM 2220 O  O   . HOH G 7 .   ? -25.577 -15.410 8.040   1.00 27.66 ? 502 HOH A O   1 
HETATM 2221 O  O   . HOH G 7 .   ? -26.827 -10.919 22.713  1.00 31.92 ? 503 HOH A O   1 
HETATM 2222 O  O   . HOH G 7 .   ? -24.841 -7.769  9.110   1.00 18.90 ? 504 HOH A O   1 
HETATM 2223 O  O   . HOH G 7 .   ? -11.041 -19.568 6.918   1.00 31.49 ? 505 HOH A O   1 
HETATM 2224 O  O   . HOH G 7 .   ? 13.606  0.219   24.372  1.00 26.37 ? 506 HOH A O   1 
HETATM 2225 O  O   . HOH G 7 .   ? -15.759 9.115   -1.976  1.00 31.09 ? 507 HOH A O   1 
HETATM 2226 O  O   . HOH G 7 .   ? -13.459 20.122  14.914  1.00 27.23 ? 508 HOH A O   1 
HETATM 2227 O  O   . HOH G 7 .   ? 3.988   2.848   8.194   1.00 35.06 ? 509 HOH A O   1 
HETATM 2228 O  O   . HOH G 7 .   ? -23.880 -2.515  28.937  1.00 31.16 ? 510 HOH A O   1 
HETATM 2229 O  O   . HOH G 7 .   ? 4.959   -4.935  20.898  1.00 13.54 ? 511 HOH A O   1 
HETATM 2230 O  O   . HOH G 7 .   ? -3.874  -20.840 15.545  1.00 45.05 ? 512 HOH A O   1 
HETATM 2231 O  O   . HOH G 7 .   ? -13.610 13.465  31.390  1.00 42.11 ? 513 HOH A O   1 
HETATM 2232 O  O   . HOH G 7 .   ? 1.291   -6.528  34.554  1.00 29.13 ? 514 HOH A O   1 
HETATM 2233 O  O   . HOH G 7 .   ? -17.065 -7.424  39.778  1.00 33.34 ? 515 HOH A O   1 
HETATM 2234 O  O   . HOH G 7 .   ? -18.502 -9.236  34.393  1.00 32.13 ? 516 HOH A O   1 
HETATM 2235 O  O   . HOH G 7 .   ? -23.893 -0.837  26.386  1.00 19.51 ? 517 HOH A O   1 
HETATM 2236 O  O   . HOH G 7 .   ? -24.806 12.078  6.287   1.00 29.97 ? 518 HOH A O   1 
HETATM 2237 O  O   . HOH G 7 .   ? -18.638 12.117  12.865  1.00 31.38 ? 519 HOH A O   1 
HETATM 2238 O  O   . HOH G 7 .   ? -4.537  -15.912 0.571   1.00 30.14 ? 520 HOH A O   1 
HETATM 2239 O  O   . HOH G 7 .   ? 13.247  -5.894  24.574  1.00 31.83 ? 521 HOH A O   1 
HETATM 2240 O  O   . HOH G 7 .   ? -16.302 -10.093 32.800  1.00 19.53 ? 522 HOH A O   1 
HETATM 2241 O  O   . HOH G 7 .   ? -12.599 12.869  29.184  1.00 35.10 ? 523 HOH A O   1 
HETATM 2242 O  O   . HOH G 7 .   ? -14.117 -21.514 3.154   1.00 41.56 ? 524 HOH A O   1 
HETATM 2243 O  O   . HOH G 7 .   ? -11.276 9.860   7.513   1.00 35.45 ? 525 HOH A O   1 
HETATM 2244 O  O   . HOH G 7 .   ? -5.847  -11.480 36.360  1.00 36.27 ? 526 HOH A O   1 
HETATM 2245 O  O   . HOH G 7 .   ? 14.775  -0.240  15.193  1.00 32.97 ? 527 HOH A O   1 
HETATM 2246 O  O   . HOH G 7 .   ? -12.748 7.907   28.761  1.00 34.66 ? 528 HOH A O   1 
HETATM 2247 O  O   . HOH G 7 .   ? -25.110 4.772   8.375   1.00 31.10 ? 529 HOH A O   1 
HETATM 2248 O  O   . HOH G 7 .   ? -12.956 -17.014 26.284  1.00 35.65 ? 530 HOH A O   1 
HETATM 2249 O  O   . HOH G 7 .   ? -26.834 -4.287  24.999  1.00 22.12 ? 531 HOH A O   1 
HETATM 2250 O  O   . HOH G 7 .   ? 1.346   -1.731  29.382  1.00 16.06 ? 532 HOH A O   1 
HETATM 2251 O  O   . HOH G 7 .   ? -11.835 2.834   30.709  1.00 26.06 ? 533 HOH A O   1 
HETATM 2252 O  O   . HOH G 7 .   ? 2.690   -11.237 9.665   1.00 24.48 ? 534 HOH A O   1 
HETATM 2253 O  O   . HOH G 7 .   ? -9.866  13.537  9.168   1.00 42.30 ? 535 HOH A O   1 
HETATM 2254 O  O   . HOH G 7 .   ? -28.019 5.621   18.945  1.00 40.87 ? 536 HOH A O   1 
HETATM 2255 O  O   . HOH G 7 .   ? -17.206 -16.570 21.719  1.00 35.39 ? 537 HOH A O   1 
HETATM 2256 O  O   . HOH G 7 .   ? -0.297  10.850  23.566  1.00 21.43 ? 538 HOH A O   1 
HETATM 2257 O  O   . HOH G 7 .   ? 1.259   8.733   24.623  1.00 19.89 ? 539 HOH A O   1 
HETATM 2258 O  O   . HOH G 7 .   ? 11.512  1.262   25.982  1.00 35.28 ? 540 HOH A O   1 
HETATM 2259 O  O   . HOH G 7 .   ? -8.888  -6.190  35.778  1.00 18.97 ? 541 HOH A O   1 
HETATM 2260 O  O   . HOH G 7 .   ? -7.973  -22.218 10.195  1.00 25.09 ? 542 HOH A O   1 
HETATM 2261 O  O   . HOH G 7 .   ? -27.804 2.338   23.389  1.00 42.85 ? 543 HOH A O   1 
HETATM 2262 O  O   . HOH G 7 .   ? -1.852  -12.337 22.798  1.00 15.23 ? 544 HOH A O   1 
HETATM 2263 O  O   . HOH G 7 .   ? -7.138  -17.031 1.352   1.00 26.51 ? 545 HOH A O   1 
HETATM 2264 O  O   . HOH G 7 .   ? -9.831  14.801  12.205  1.00 23.06 ? 546 HOH A O   1 
HETATM 2265 O  O   . HOH G 7 .   ? 7.794   -7.208  -0.969  1.00 38.61 ? 547 HOH A O   1 
HETATM 2266 O  O   . HOH G 7 .   ? -13.853 14.110  27.362  1.00 34.36 ? 548 HOH A O   1 
HETATM 2267 O  O   . HOH G 7 .   ? -25.916 8.141   6.185   1.00 36.13 ? 549 HOH A O   1 
HETATM 2268 O  O   . HOH G 7 .   ? -24.208 -17.784 6.561   1.00 34.33 ? 550 HOH A O   1 
HETATM 2269 O  O   . HOH G 7 .   ? -0.851  -8.687  32.432  1.00 31.00 ? 551 HOH A O   1 
HETATM 2270 O  O   . HOH G 7 .   ? -6.397  -19.387 5.227   1.00 33.85 ? 552 HOH A O   1 
HETATM 2271 O  O   . HOH G 7 .   ? -5.509  15.892  12.172  1.00 39.54 ? 553 HOH A O   1 
HETATM 2272 O  O   . HOH G 7 .   ? -7.713  -19.681 30.270  1.00 36.78 ? 554 HOH A O   1 
HETATM 2273 O  O   . HOH G 7 .   ? -23.809 -0.930  4.016   1.00 22.24 ? 555 HOH A O   1 
HETATM 2274 O  O   . HOH G 7 .   ? -9.523  -8.271  33.820  1.00 25.51 ? 556 HOH A O   1 
HETATM 2275 O  O   . HOH G 7 .   ? -8.149  -19.408 21.601  1.00 30.56 ? 557 HOH A O   1 
HETATM 2276 O  O   . HOH G 7 .   ? -13.021 -18.516 14.741  1.00 23.61 ? 558 HOH A O   1 
HETATM 2277 O  O   . HOH G 7 .   ? 0.051   -14.363 21.988  1.00 31.19 ? 559 HOH A O   1 
HETATM 2278 O  O   . HOH G 7 .   ? -21.103 18.926  13.688  1.00 33.29 ? 560 HOH A O   1 
HETATM 2279 O  O   . HOH G 7 .   ? -17.822 -12.288 31.765  1.00 37.22 ? 561 HOH A O   1 
HETATM 2280 O  O   . HOH G 7 .   ? -6.260  -5.409  37.904  1.00 36.55 ? 562 HOH A O   1 
HETATM 2281 O  O   . HOH G 7 .   ? 7.827   6.105   21.857  1.00 16.78 ? 563 HOH A O   1 
HETATM 2282 O  O   . HOH G 7 .   ? -6.466  6.544   10.552  1.00 40.69 ? 564 HOH A O   1 
HETATM 2283 O  O   . HOH G 7 .   ? 5.371   -7.058  22.607  1.00 31.34 ? 565 HOH A O   1 
HETATM 2284 O  O   . HOH G 7 .   ? -7.348  1.310   35.032  1.00 27.46 ? 566 HOH A O   1 
HETATM 2285 O  O   . HOH G 7 .   ? -22.026 -18.496 13.747  1.00 27.26 ? 567 HOH A O   1 
HETATM 2286 O  O   . HOH G 7 .   ? 9.332   7.612   18.839  1.00 36.29 ? 568 HOH A O   1 
HETATM 2287 O  O   . HOH G 7 .   ? -17.176 -9.694  36.512  1.00 37.02 ? 569 HOH A O   1 
HETATM 2288 O  O   . HOH G 7 .   ? -5.719  3.741   -5.976  1.00 38.97 ? 570 HOH A O   1 
HETATM 2289 O  O   . HOH G 7 .   ? -17.991 4.036   -3.810  1.00 41.12 ? 571 HOH A O   1 
HETATM 2290 O  O   . HOH G 7 .   ? -3.566  4.882   7.041   1.00 41.41 ? 572 HOH A O   1 
HETATM 2291 O  O   . HOH G 7 .   ? -8.273  -17.344 34.892  1.00 31.06 ? 573 HOH A O   1 
HETATM 2292 O  O   . HOH G 7 .   ? -24.987 -9.278  2.010   1.00 35.56 ? 574 HOH A O   1 
HETATM 2293 O  O   . HOH G 7 .   ? -21.150 -19.604 6.417   1.00 34.86 ? 575 HOH A O   1 
HETATM 2294 O  O   . HOH G 7 .   ? -6.784  1.242   37.204  1.00 35.31 ? 576 HOH A O   1 
HETATM 2295 O  O   . HOH G 7 .   ? -12.714 10.126  -6.103  1.00 42.61 ? 577 HOH A O   1 
HETATM 2296 O  O   . HOH G 7 .   ? -25.732 -6.725  33.873  1.00 42.82 ? 578 HOH A O   1 
HETATM 2297 O  O   . HOH G 7 .   ? -1.405  10.955  25.989  1.00 31.29 ? 579 HOH A O   1 
HETATM 2298 O  O   . HOH G 7 .   ? 0.149   0.633   -6.935  1.00 40.05 ? 580 HOH A O   1 
HETATM 2299 O  O   . HOH G 7 .   ? 8.820   -4.883  23.773  1.00 26.49 ? 581 HOH A O   1 
HETATM 2300 O  O   . HOH G 7 .   ? 10.589  -2.658  13.748  1.00 36.37 ? 582 HOH A O   1 
HETATM 2301 O  O   . HOH G 7 .   ? -12.576 -17.372 16.789  1.00 25.84 ? 583 HOH A O   1 
HETATM 2302 O  O   . HOH G 7 .   ? -17.790 19.772  17.640  1.00 33.65 ? 584 HOH A O   1 
HETATM 2303 O  O   . HOH G 7 .   ? -26.925 4.865   6.728   1.00 36.07 ? 585 HOH A O   1 
HETATM 2304 O  O   . HOH G 7 .   ? -17.404 -23.158 4.139   1.00 32.76 ? 586 HOH A O   1 
HETATM 2305 O  O   . HOH G 7 .   ? -18.772 14.234  2.712   1.00 43.23 ? 587 HOH A O   1 
HETATM 2306 O  O   . HOH G 7 .   ? -31.666 5.453   12.967  1.00 38.56 ? 588 HOH A O   1 
HETATM 2307 O  O   . HOH G 7 .   ? -5.142  -0.229  39.895  1.00 42.79 ? 589 HOH A O   1 
HETATM 2308 O  O   . HOH G 7 .   ? 4.790   -13.254 -5.915  1.00 37.89 ? 590 HOH A O   1 
HETATM 2309 O  O   . HOH G 7 .   ? 1.056   -10.005 28.705  1.00 35.97 ? 591 HOH A O   1 
HETATM 2310 O  O   . HOH G 7 .   ? 0.713   3.234   2.162   1.00 41.22 ? 592 HOH A O   1 
HETATM 2311 O  O   . HOH G 7 .   ? -1.667  -13.437 27.431  1.00 28.37 ? 593 HOH A O   1 
HETATM 2312 O  O   . HOH G 7 .   ? -8.401  -1.519  41.295  1.00 38.00 ? 594 HOH A O   1 
HETATM 2313 O  O   . HOH G 7 .   ? -10.125 5.079   30.450  1.00 31.92 ? 595 HOH A O   1 
HETATM 2314 O  O   . HOH G 7 .   ? -1.689  -17.553 25.154  1.00 34.21 ? 596 HOH A O   1 
HETATM 2315 O  O   . HOH G 7 .   ? -27.838 4.701   25.314  1.00 37.14 ? 597 HOH A O   1 
HETATM 2316 O  O   . HOH G 7 .   ? -2.907  -17.782 4.908   1.00 35.34 ? 598 HOH A O   1 
HETATM 2317 O  O   . HOH G 7 .   ? -16.658 19.843  22.192  1.00 40.60 ? 599 HOH A O   1 
HETATM 2318 O  O   . HOH G 7 .   ? -20.280 -23.039 3.832   1.00 34.54 ? 600 HOH A O   1 
HETATM 2319 O  O   . HOH G 7 .   ? -23.542 -6.923  -0.170  1.00 33.35 ? 601 HOH A O   1 
HETATM 2320 O  O   . HOH G 7 .   ? -1.928  -12.275 31.229  1.00 33.46 ? 602 HOH A O   1 
HETATM 2321 O  O   . HOH G 7 .   ? -5.461  -9.763  34.608  1.00 38.11 ? 603 HOH A O   1 
HETATM 2322 O  O   . HOH G 7 .   ? -16.938 -14.095 37.349  1.00 38.45 ? 604 HOH A O   1 
HETATM 2323 O  O   . HOH G 7 .   ? 15.772  -1.466  25.813  1.00 30.44 ? 605 HOH A O   1 
HETATM 2324 O  O   . HOH G 7 .   ? -16.825 -13.923 26.666  1.00 36.30 ? 606 HOH A O   1 
HETATM 2325 O  O   . HOH G 7 .   ? 4.333   12.345  23.931  1.00 43.29 ? 607 HOH A O   1 
HETATM 2326 O  O   . HOH G 7 .   ? -1.732  3.230   -6.804  1.00 34.51 ? 608 HOH A O   1 
HETATM 2327 O  O   . HOH G 7 .   ? -20.023 -15.494 22.612  1.00 39.43 ? 609 HOH A O   1 
HETATM 2328 O  O   . HOH G 7 .   ? 2.103   -14.372 20.589  1.00 36.76 ? 610 HOH A O   1 
HETATM 2329 O  O   . HOH G 7 .   ? -12.620 -19.377 26.477  1.00 41.58 ? 611 HOH A O   1 
HETATM 2330 O  O   . HOH G 7 .   ? -22.148 -13.257 23.888  1.00 38.59 ? 612 HOH A O   1 
HETATM 2331 O  O   . HOH G 7 .   ? -14.325 10.605  36.154  1.00 44.96 ? 613 HOH A O   1 
HETATM 2332 O  O   . HOH G 7 .   ? -1.013  -11.351 28.801  1.00 24.83 ? 614 HOH A O   1 
HETATM 2333 O  O   . HOH G 7 .   ? 6.623   5.284   28.513  1.00 36.70 ? 615 HOH A O   1 
HETATM 2334 O  O   . HOH G 7 .   ? 3.747   9.836   24.095  1.00 28.03 ? 616 HOH A O   1 
HETATM 2335 O  O   . HOH G 7 .   ? -1.333  10.712  13.901  1.00 44.84 ? 617 HOH A O   1 
# 
