data_6QL1
# 
_entry.id   6QL1 
# 
_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   6QL1         pdb_00006ql1 10.2210/pdb6ql1/pdb 
WWPDB D_1292100356 ?            ?                   
# 
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 2019-09-25 
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' 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_comp_id' 
7  2 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_seq_id'  
8  2 'Structure model' '_pdbx_struct_conn_angle.ptnr2_symmetry'      
9  2 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_comp_id'  
10 2 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_seq_id'   
11 2 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_asym_id' 
12 2 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_comp_id' 
13 2 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_seq_id'  
14 2 'Structure model' '_pdbx_struct_conn_angle.value'               
15 2 'Structure model' '_struct_conn.pdbx_dist_value'                
16 2 'Structure model' '_struct_conn.pdbx_ptnr2_label_alt_id'        
17 2 'Structure model' '_struct_conn.ptnr1_auth_comp_id'             
18 2 'Structure model' '_struct_conn.ptnr1_auth_seq_id'              
19 2 'Structure model' '_struct_conn.ptnr1_label_asym_id'            
20 2 'Structure model' '_struct_conn.ptnr1_label_atom_id'            
21 2 'Structure model' '_struct_conn.ptnr1_label_comp_id'            
22 2 'Structure model' '_struct_conn.ptnr1_label_seq_id'             
23 2 'Structure model' '_struct_conn.ptnr2_auth_comp_id'             
24 2 'Structure model' '_struct_conn.ptnr2_auth_seq_id'              
25 2 'Structure model' '_struct_conn.ptnr2_label_asym_id'            
26 2 'Structure model' '_struct_conn.ptnr2_label_atom_id'            
27 2 'Structure model' '_struct_conn.ptnr2_label_comp_id'            
28 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                        6QL1 
_pdbx_database_status.recvd_initial_deposition_date   2019-01-31 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_nmr_data            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Smirnov, A.'  1 ? 
'Manakova, E.' 2 ? 
'Grazulis, S.' 3 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Sci Rep' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2045-2322 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            9 
_citation.language                  ? 
_citation.page_first                12710 
_citation.page_last                 12710 
_citation.title                     
'Engineered Carbonic Anhydrase VI-Mimic Enzyme Switched the Structure and Affinities of Inhibitors.' 
_citation.year                      2019 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41598-019-49094-0 
_citation.pdbx_database_id_PubMed   31481705 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Kazokaite, J.'   1 ?                   
primary 'Kairys, V.'      2 ?                   
primary 'Smirnoviene, J.' 3 ?                   
primary 'Smirnov, A.'     4 ?                   
primary 'Manakova, E.'    5 ?                   
primary 'Tolvanen, M.'    6 ?                   
primary 'Parkkila, S.'    7 ?                   
primary 'Matulis, D.'     8 0000-0002-6178-6276 
# 
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'                                                       29366.055 1   4.2.1.1 
'A65T, N67Q, F130Y, V134Q, L203T' 'human carbonic anhydrase II'                                                ? 
2 non-polymer syn 'ZINC ION'                                                                   65.409    1   ?       ? 
'4-[(4,6-dimethylpyrimidin-2-yl)thio]-2,3,5,6-tetrafluorobenzenesulfonamide' ? 
3 non-polymer syn 'DIMETHYL SULFOXIDE'                                                         78.133    1   ?       ? Zn ? 
4 non-polymer syn 1,2-ETHANEDIOL                                                               62.068    1   ?       ? 
'Dimethyl sulfoxide'                                                         ? 
5 non-polymer syn BICINE                                                                       163.172   1   ?       ? 
'2-(Bis(2-hydroxyethyl)amino)acetic acid'                                    ? 
6 non-polymer syn '4-[(4,6-dimethylpyrimidin-2-yl)thio]-2,3,5,6-tetrafluorobenzenesulfonamide' 367.342   2   ?       ? 
ethane-1,2-diol                                                              ? 
7 non-polymer syn 'SODIUM ION'                                                                 22.990    1   ?       ? Na ? 
8 water       nat water                                                                        18.015    285 ?       ? ? ? 
# 
_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       
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHTFQVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDYGKAQQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLTECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHTFQVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDYGKAQQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLTECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION'                                                                   ZN  
3 'DIMETHYL SULFOXIDE'                                                         DMS 
4 1,2-ETHANEDIOL                                                               EDO 
5 BICINE                                                                       BCN 
6 '4-[(4,6-dimethylpyrimidin-2-yl)thio]-2,3,5,6-tetrafluorobenzenesulfonamide' V50 
7 'SODIUM ION'                                                                 NA  
8 water                                                                        HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   SER n 
1 3   HIS n 
1 4   HIS n 
1 5   TRP n 
1 6   GLY n 
1 7   TYR n 
1 8   GLY n 
1 9   LYS n 
1 10  HIS n 
1 11  ASN n 
1 12  GLY n 
1 13  PRO n 
1 14  GLU n 
1 15  HIS n 
1 16  TRP n 
1 17  HIS n 
1 18  LYS n 
1 19  ASP n 
1 20  PHE n 
1 21  PRO n 
1 22  ILE n 
1 23  ALA n 
1 24  LYS n 
1 25  GLY n 
1 26  GLU n 
1 27  ARG n 
1 28  GLN n 
1 29  SER n 
1 30  PRO n 
1 31  VAL n 
1 32  ASP n 
1 33  ILE n 
1 34  ASP n 
1 35  THR n 
1 36  HIS n 
1 37  THR n 
1 38  ALA n 
1 39  LYS n 
1 40  TYR n 
1 41  ASP n 
1 42  PRO n 
1 43  SER n 
1 44  LEU n 
1 45  LYS n 
1 46  PRO n 
1 47  LEU n 
1 48  SER n 
1 49  VAL n 
1 50  SER n 
1 51  TYR n 
1 52  ASP n 
1 53  GLN n 
1 54  ALA n 
1 55  THR n 
1 56  SER n 
1 57  LEU n 
1 58  ARG n 
1 59  ILE n 
1 60  LEU n 
1 61  ASN n 
1 62  ASN n 
1 63  GLY n 
1 64  HIS n 
1 65  THR n 
1 66  PHE n 
1 67  GLN n 
1 68  VAL n 
1 69  GLU n 
1 70  PHE n 
1 71  ASP n 
1 72  ASP n 
1 73  SER n 
1 74  GLN n 
1 75  ASP n 
1 76  LYS n 
1 77  ALA n 
1 78  VAL n 
1 79  LEU n 
1 80  LYS n 
1 81  GLY n 
1 82  GLY n 
1 83  PRO n 
1 84  LEU n 
1 85  ASP n 
1 86  GLY n 
1 87  THR n 
1 88  TYR n 
1 89  ARG n 
1 90  LEU n 
1 91  ILE n 
1 92  GLN n 
1 93  PHE n 
1 94  HIS n 
1 95  PHE n 
1 96  HIS n 
1 97  TRP n 
1 98  GLY n 
1 99  SER n 
1 100 LEU n 
1 101 ASP n 
1 102 GLY n 
1 103 GLN n 
1 104 GLY n 
1 105 SER n 
1 106 GLU n 
1 107 HIS n 
1 108 THR n 
1 109 VAL n 
1 110 ASP n 
1 111 LYS n 
1 112 LYS n 
1 113 LYS n 
1 114 TYR n 
1 115 ALA n 
1 116 ALA n 
1 117 GLU n 
1 118 LEU n 
1 119 HIS n 
1 120 LEU n 
1 121 VAL n 
1 122 HIS n 
1 123 TRP n 
1 124 ASN n 
1 125 THR n 
1 126 LYS n 
1 127 TYR n 
1 128 GLY n 
1 129 ASP n 
1 130 TYR n 
1 131 GLY n 
1 132 LYS n 
1 133 ALA n 
1 134 GLN n 
1 135 GLN n 
1 136 GLN n 
1 137 PRO n 
1 138 ASP n 
1 139 GLY n 
1 140 LEU n 
1 141 ALA n 
1 142 VAL n 
1 143 LEU n 
1 144 GLY n 
1 145 ILE n 
1 146 PHE n 
1 147 LEU n 
1 148 LYS n 
1 149 VAL n 
1 150 GLY n 
1 151 SER n 
1 152 ALA n 
1 153 LYS n 
1 154 PRO n 
1 155 GLY n 
1 156 LEU n 
1 157 GLN n 
1 158 LYS n 
1 159 VAL n 
1 160 VAL n 
1 161 ASP n 
1 162 VAL n 
1 163 LEU n 
1 164 ASP n 
1 165 SER n 
1 166 ILE n 
1 167 LYS n 
1 168 THR n 
1 169 LYS n 
1 170 GLY n 
1 171 LYS n 
1 172 SER n 
1 173 ALA n 
1 174 ASP n 
1 175 PHE n 
1 176 THR n 
1 177 ASN n 
1 178 PHE n 
1 179 ASP n 
1 180 PRO n 
1 181 ARG n 
1 182 GLY n 
1 183 LEU n 
1 184 LEU n 
1 185 PRO n 
1 186 GLU n 
1 187 SER n 
1 188 LEU n 
1 189 ASP n 
1 190 TYR n 
1 191 TRP n 
1 192 THR n 
1 193 TYR n 
1 194 PRO n 
1 195 GLY n 
1 196 SER n 
1 197 LEU n 
1 198 THR n 
1 199 THR n 
1 200 PRO n 
1 201 PRO n 
1 202 LEU n 
1 203 THR n 
1 204 GLU n 
1 205 CYS n 
1 206 VAL n 
1 207 THR n 
1 208 TRP n 
1 209 ILE n 
1 210 VAL n 
1 211 LEU n 
1 212 LYS n 
1 213 GLU n 
1 214 PRO n 
1 215 ILE n 
1 216 SER n 
1 217 VAL n 
1 218 SER n 
1 219 SER n 
1 220 GLU n 
1 221 GLN n 
1 222 VAL n 
1 223 LEU n 
1 224 LYS n 
1 225 PHE n 
1 226 ARG n 
1 227 LYS n 
1 228 LEU n 
1 229 ASN n 
1 230 PHE n 
1 231 ASN n 
1 232 GLY n 
1 233 GLU n 
1 234 GLY n 
1 235 GLU n 
1 236 PRO n 
1 237 GLU n 
1 238 GLU n 
1 239 LEU n 
1 240 MET n 
1 241 VAL n 
1 242 ASP n 
1 243 ASN n 
1 244 TRP n 
1 245 ARG n 
1 246 PRO n 
1 247 ALA n 
1 248 GLN n 
1 249 PRO n 
1 250 LEU n 
1 251 LYS n 
1 252 ASN n 
1 253 ARG n 
1 254 GLN n 
1 255 ILE n 
1 256 LYS n 
1 257 ALA n 
1 258 SER n 
1 259 PHE n 
1 260 LYS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   260 
_entity_src_gen.gene_src_common_name               Human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 CA2 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_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               'BL21(DE3)' 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pET15b 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                                                      ?                 
'C3 H7 N O2'         89.093  
ARG 'L-peptide linking' y ARGININE                                                                     ?                 
'C6 H15 N4 O2 1'     175.209 
ASN 'L-peptide linking' y ASPARAGINE                                                                   ?                 
'C4 H8 N2 O3'        132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                                              ?                 
'C4 H7 N O4'         133.103 
BCN non-polymer         . BICINE                                                                       ?                 
'C6 H13 N O4'        163.172 
CYS 'L-peptide linking' y CYSTEINE                                                                     ?                 
'C3 H7 N O2 S'       121.158 
DMS non-polymer         . 'DIMETHYL SULFOXIDE'                                                         ?                 
'C2 H6 O S'          78.133  
EDO non-polymer         . 1,2-ETHANEDIOL                                                               'ETHYLENE GLYCOL' 
'C2 H6 O2'           62.068  
GLN 'L-peptide linking' y GLUTAMINE                                                                    ?                 
'C5 H10 N2 O3'       146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                                              ?                 
'C5 H9 N O4'         147.129 
GLY 'peptide linking'   y GLYCINE                                                                      ?                 
'C2 H5 N O2'         75.067  
HIS 'L-peptide linking' y HISTIDINE                                                                    ?                 
'C6 H10 N3 O2 1'     156.162 
HOH non-polymer         . WATER                                                                        ?                 'H2 O' 
18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                                                   ?                 
'C6 H13 N O2'        131.173 
LEU 'L-peptide linking' y LEUCINE                                                                      ?                 
'C6 H13 N O2'        131.173 
LYS 'L-peptide linking' y LYSINE                                                                       ?                 
'C6 H15 N2 O2 1'     147.195 
MET 'L-peptide linking' y METHIONINE                                                                   ?                 
'C5 H11 N O2 S'      149.211 
NA  non-polymer         . 'SODIUM ION'                                                                 ?                 'Na 1' 
22.990  
PHE 'L-peptide linking' y PHENYLALANINE                                                                ?                 
'C9 H11 N O2'        165.189 
PRO 'L-peptide linking' y PROLINE                                                                      ?                 
'C5 H9 N O2'         115.130 
SER 'L-peptide linking' y SERINE                                                                       ?                 
'C3 H7 N O3'         105.093 
THR 'L-peptide linking' y THREONINE                                                                    ?                 
'C4 H9 N O3'         119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                                                   ?                 
'C11 H12 N2 O2'      204.225 
TYR 'L-peptide linking' y TYROSINE                                                                     ?                 
'C9 H11 N O3'        181.189 
V50 non-polymer         . '4-[(4,6-dimethylpyrimidin-2-yl)thio]-2,3,5,6-tetrafluorobenzenesulfonamide' ?                 
'C12 H9 F4 N3 O2 S2' 367.342 
VAL 'L-peptide linking' y VALINE                                                                       ?                 
'C5 H11 N O2'        117.146 
ZN  non-polymer         . 'ZINC ION'                                                                   ?                 'Zn 2' 
65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   SER 2   2   ?   ?   ?   A . n 
A 1 3   HIS 3   3   ?   ?   ?   A . n 
A 1 4   HIS 4   4   4   HIS HIS A . n 
A 1 5   TRP 5   5   5   TRP TRP A . n 
A 1 6   GLY 6   6   6   GLY GLY A . n 
A 1 7   TYR 7   7   7   TYR TYR A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   LYS 9   9   9   LYS LYS A . n 
A 1 10  HIS 10  10  10  HIS HIS A . n 
A 1 11  ASN 11  11  11  ASN ASN A . n 
A 1 12  GLY 12  12  12  GLY GLY A . n 
A 1 13  PRO 13  13  13  PRO PRO A . n 
A 1 14  GLU 14  14  14  GLU GLU A . n 
A 1 15  HIS 15  15  15  HIS HIS A . n 
A 1 16  TRP 16  16  16  TRP TRP A . n 
A 1 17  HIS 17  17  17  HIS HIS A . n 
A 1 18  LYS 18  18  18  LYS LYS A . n 
A 1 19  ASP 19  19  19  ASP ASP A . n 
A 1 20  PHE 20  20  20  PHE PHE A . n 
A 1 21  PRO 21  21  21  PRO PRO A . n 
A 1 22  ILE 22  22  22  ILE ILE A . n 
A 1 23  ALA 23  23  23  ALA ALA A . n 
A 1 24  LYS 24  24  24  LYS LYS A . n 
A 1 25  GLY 25  25  25  GLY GLY A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  ARG 27  27  27  ARG ARG A . n 
A 1 28  GLN 28  28  28  GLN GLN A . n 
A 1 29  SER 29  29  29  SER SER A . n 
A 1 30  PRO 30  30  30  PRO PRO A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  ASP 32  32  32  ASP ASP A . n 
A 1 33  ILE 33  33  33  ILE ILE A . n 
A 1 34  ASP 34  34  34  ASP ASP A . n 
A 1 35  THR 35  35  35  THR THR A . n 
A 1 36  HIS 36  36  36  HIS HIS A . n 
A 1 37  THR 37  37  37  THR THR A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  LYS 39  39  39  LYS LYS A . n 
A 1 40  TYR 40  40  40  TYR TYR A . n 
A 1 41  ASP 41  41  41  ASP ASP A . n 
A 1 42  PRO 42  42  42  PRO PRO A . n 
A 1 43  SER 43  43  43  SER SER A . n 
A 1 44  LEU 44  44  44  LEU LEU A . n 
A 1 45  LYS 45  45  45  LYS LYS A . n 
A 1 46  PRO 46  46  46  PRO PRO A . n 
A 1 47  LEU 47  47  47  LEU LEU A . n 
A 1 48  SER 48  48  48  SER SER A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  SER 50  50  50  SER SER A . n 
A 1 51  TYR 51  51  51  TYR TYR A . n 
A 1 52  ASP 52  52  52  ASP ASP A . n 
A 1 53  GLN 53  53  53  GLN GLN A . n 
A 1 54  ALA 54  54  54  ALA ALA A . n 
A 1 55  THR 55  55  55  THR THR A . n 
A 1 56  SER 56  56  56  SER SER A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  ARG 58  58  58  ARG ARG A . n 
A 1 59  ILE 59  59  59  ILE ILE A . n 
A 1 60  LEU 60  60  60  LEU LEU A . n 
A 1 61  ASN 61  61  61  ASN ASN A . n 
A 1 62  ASN 62  62  62  ASN ASN A . n 
A 1 63  GLY 63  63  63  GLY GLY A . n 
A 1 64  HIS 64  64  64  HIS HIS A . n 
A 1 65  THR 65  65  65  THR THR A . n 
A 1 66  PHE 66  66  66  PHE PHE A . n 
A 1 67  GLN 67  67  67  GLN GLN A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  GLU 69  69  69  GLU GLU A . n 
A 1 70  PHE 70  70  70  PHE PHE A . n 
A 1 71  ASP 71  71  71  ASP ASP A . n 
A 1 72  ASP 72  72  72  ASP ASP A . n 
A 1 73  SER 73  73  73  SER SER A . n 
A 1 74  GLN 74  74  74  GLN GLN A . n 
A 1 75  ASP 75  75  75  ASP ASP A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  ALA 77  77  77  ALA ALA A . n 
A 1 78  VAL 78  78  78  VAL VAL A . n 
A 1 79  LEU 79  79  79  LEU LEU A . n 
A 1 80  LYS 80  80  80  LYS LYS A . n 
A 1 81  GLY 81  81  81  GLY GLY A . n 
A 1 82  GLY 82  82  82  GLY GLY A . n 
A 1 83  PRO 83  83  83  PRO PRO A . n 
A 1 84  LEU 84  84  84  LEU LEU A . n 
A 1 85  ASP 85  85  85  ASP ASP A . n 
A 1 86  GLY 86  86  86  GLY GLY A . n 
A 1 87  THR 87  87  87  THR THR A . n 
A 1 88  TYR 88  88  88  TYR TYR A . n 
A 1 89  ARG 89  89  89  ARG ARG A . n 
A 1 90  LEU 90  90  90  LEU LEU A . n 
A 1 91  ILE 91  91  91  ILE ILE A . n 
A 1 92  GLN 92  92  92  GLN GLN A . n 
A 1 93  PHE 93  93  93  PHE PHE A . n 
A 1 94  HIS 94  94  94  HIS HIS A . n 
A 1 95  PHE 95  95  95  PHE PHE A . n 
A 1 96  HIS 96  96  96  HIS HIS A . n 
A 1 97  TRP 97  97  97  TRP TRP A . n 
A 1 98  GLY 98  98  98  GLY GLY A . n 
A 1 99  SER 99  99  99  SER SER A . n 
A 1 100 LEU 100 100 100 LEU LEU A . n 
A 1 101 ASP 101 101 101 ASP ASP A . n 
A 1 102 GLY 102 102 102 GLY GLY A . n 
A 1 103 GLN 103 103 103 GLN GLN A . n 
A 1 104 GLY 104 104 104 GLY GLY A . n 
A 1 105 SER 105 105 105 SER SER A . n 
A 1 106 GLU 106 106 106 GLU GLU A . n 
A 1 107 HIS 107 107 107 HIS HIS A . n 
A 1 108 THR 108 108 108 THR THR A . n 
A 1 109 VAL 109 109 109 VAL VAL A . n 
A 1 110 ASP 110 110 110 ASP ASP A . n 
A 1 111 LYS 111 111 111 LYS LYS A . n 
A 1 112 LYS 112 112 112 LYS LYS A . n 
A 1 113 LYS 113 113 113 LYS LYS A . n 
A 1 114 TYR 114 114 114 TYR TYR A . n 
A 1 115 ALA 115 115 115 ALA ALA A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 GLU 117 117 117 GLU GLU A . n 
A 1 118 LEU 118 118 118 LEU LEU A . n 
A 1 119 HIS 119 119 119 HIS HIS A . n 
A 1 120 LEU 120 120 120 LEU LEU A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 HIS 122 122 122 HIS HIS A . n 
A 1 123 TRP 123 123 123 TRP TRP A . n 
A 1 124 ASN 124 124 124 ASN ASN A . n 
A 1 125 THR 125 125 125 THR THR A . n 
A 1 126 LYS 126 127 127 LYS LYS A . n 
A 1 127 TYR 127 128 128 TYR TYR A . n 
A 1 128 GLY 128 129 129 GLY GLY A . n 
A 1 129 ASP 129 130 130 ASP ASP A . n 
A 1 130 TYR 130 131 131 TYR TYR A . n 
A 1 131 GLY 131 132 132 GLY GLY A . n 
A 1 132 LYS 132 133 133 LYS LYS A . n 
A 1 133 ALA 133 134 134 ALA ALA A . n 
A 1 134 GLN 134 135 135 GLN GLN A . n 
A 1 135 GLN 135 136 136 GLN GLN A . n 
A 1 136 GLN 136 137 137 GLN GLN A . n 
A 1 137 PRO 137 138 138 PRO PRO A . n 
A 1 138 ASP 138 139 139 ASP ASP A . n 
A 1 139 GLY 139 140 140 GLY GLY A . n 
A 1 140 LEU 140 141 141 LEU LEU A . n 
A 1 141 ALA 141 142 142 ALA ALA A . n 
A 1 142 VAL 142 143 143 VAL VAL A . n 
A 1 143 LEU 143 144 144 LEU LEU A . n 
A 1 144 GLY 144 145 145 GLY GLY A . n 
A 1 145 ILE 145 146 146 ILE ILE A . n 
A 1 146 PHE 146 147 147 PHE PHE A . n 
A 1 147 LEU 147 148 148 LEU LEU A . n 
A 1 148 LYS 148 149 149 LYS LYS A . n 
A 1 149 VAL 149 150 150 VAL VAL A . n 
A 1 150 GLY 150 151 151 GLY GLY A . n 
A 1 151 SER 151 152 152 SER SER A . n 
A 1 152 ALA 152 153 153 ALA ALA A . n 
A 1 153 LYS 153 154 154 LYS LYS A . n 
A 1 154 PRO 154 155 155 PRO PRO A . n 
A 1 155 GLY 155 156 156 GLY GLY A . n 
A 1 156 LEU 156 157 157 LEU LEU A . n 
A 1 157 GLN 157 158 158 GLN GLN A . n 
A 1 158 LYS 158 159 159 LYS LYS A . n 
A 1 159 VAL 159 160 160 VAL VAL A . n 
A 1 160 VAL 160 161 161 VAL VAL A . n 
A 1 161 ASP 161 162 162 ASP ASP A . n 
A 1 162 VAL 162 163 163 VAL VAL A . n 
A 1 163 LEU 163 164 164 LEU LEU A . n 
A 1 164 ASP 164 165 165 ASP ASP A . n 
A 1 165 SER 165 166 166 SER SER A . n 
A 1 166 ILE 166 167 167 ILE ILE A . n 
A 1 167 LYS 167 168 168 LYS LYS A . n 
A 1 168 THR 168 169 169 THR THR A . n 
A 1 169 LYS 169 170 170 LYS LYS A . n 
A 1 170 GLY 170 171 171 GLY GLY A . n 
A 1 171 LYS 171 172 172 LYS LYS A . n 
A 1 172 SER 172 173 173 SER SER A . n 
A 1 173 ALA 173 174 174 ALA ALA A . n 
A 1 174 ASP 174 175 175 ASP ASP A . n 
A 1 175 PHE 175 176 176 PHE PHE A . n 
A 1 176 THR 176 177 177 THR THR A . n 
A 1 177 ASN 177 178 178 ASN ASN A . n 
A 1 178 PHE 178 179 179 PHE PHE A . n 
A 1 179 ASP 179 180 180 ASP ASP A . n 
A 1 180 PRO 180 181 181 PRO PRO A . n 
A 1 181 ARG 181 182 182 ARG ARG A . n 
A 1 182 GLY 182 183 183 GLY GLY A . n 
A 1 183 LEU 183 184 184 LEU LEU A . n 
A 1 184 LEU 184 185 185 LEU LEU A . n 
A 1 185 PRO 185 186 186 PRO PRO A . n 
A 1 186 GLU 186 187 187 GLU GLU A . n 
A 1 187 SER 187 188 188 SER SER A . n 
A 1 188 LEU 188 189 189 LEU LEU A . n 
A 1 189 ASP 189 190 190 ASP ASP A . n 
A 1 190 TYR 190 191 191 TYR TYR A . n 
A 1 191 TRP 191 192 192 TRP TRP A . n 
A 1 192 THR 192 193 193 THR THR A . n 
A 1 193 TYR 193 194 194 TYR TYR A . n 
A 1 194 PRO 194 195 195 PRO PRO A . n 
A 1 195 GLY 195 196 196 GLY GLY A . n 
A 1 196 SER 196 197 197 SER SER A . n 
A 1 197 LEU 197 198 198 LEU LEU A . n 
A 1 198 THR 198 199 199 THR THR A . n 
A 1 199 THR 199 200 200 THR THR A . n 
A 1 200 PRO 200 201 201 PRO PRO A . n 
A 1 201 PRO 201 202 202 PRO PRO A . n 
A 1 202 LEU 202 203 203 LEU LEU A . n 
A 1 203 THR 203 204 204 THR THR A . n 
A 1 204 GLU 204 205 205 GLU GLU A . n 
A 1 205 CYS 205 206 206 CYS CYS A . n 
A 1 206 VAL 206 207 207 VAL VAL A . n 
A 1 207 THR 207 208 208 THR THR A . n 
A 1 208 TRP 208 209 209 TRP TRP A . n 
A 1 209 ILE 209 210 210 ILE ILE A . n 
A 1 210 VAL 210 211 211 VAL VAL A . n 
A 1 211 LEU 211 212 212 LEU LEU A . n 
A 1 212 LYS 212 213 213 LYS LYS A . n 
A 1 213 GLU 213 214 214 GLU GLU A . n 
A 1 214 PRO 214 215 215 PRO PRO A . n 
A 1 215 ILE 215 216 216 ILE ILE A . n 
A 1 216 SER 216 217 217 SER SER A . n 
A 1 217 VAL 217 218 218 VAL VAL A . n 
A 1 218 SER 218 219 219 SER SER A . n 
A 1 219 SER 219 220 220 SER SER A . n 
A 1 220 GLU 220 221 221 GLU GLU A . n 
A 1 221 GLN 221 222 222 GLN GLN A . n 
A 1 222 VAL 222 223 223 VAL VAL A . n 
A 1 223 LEU 223 224 224 LEU LEU A . n 
A 1 224 LYS 224 225 225 LYS LYS A . n 
A 1 225 PHE 225 226 226 PHE PHE A . n 
A 1 226 ARG 226 227 227 ARG ARG A . n 
A 1 227 LYS 227 228 228 LYS LYS A . n 
A 1 228 LEU 228 229 229 LEU LEU A . n 
A 1 229 ASN 229 230 230 ASN ASN A . n 
A 1 230 PHE 230 231 231 PHE PHE A . n 
A 1 231 ASN 231 232 232 ASN ASN A . n 
A 1 232 GLY 232 233 233 GLY GLY A . n 
A 1 233 GLU 233 234 234 GLU GLU A . n 
A 1 234 GLY 234 235 235 GLY GLY A . n 
A 1 235 GLU 235 236 236 GLU GLU A . n 
A 1 236 PRO 236 237 237 PRO PRO A . n 
A 1 237 GLU 237 238 238 GLU GLU A . n 
A 1 238 GLU 238 239 239 GLU GLU A . n 
A 1 239 LEU 239 240 240 LEU LEU A . n 
A 1 240 MET 240 241 241 MET MET A . n 
A 1 241 VAL 241 242 242 VAL VAL A . n 
A 1 242 ASP 242 243 243 ASP ASP A . n 
A 1 243 ASN 243 244 244 ASN ASN A . n 
A 1 244 TRP 244 245 245 TRP TRP A . n 
A 1 245 ARG 245 246 246 ARG ARG A . n 
A 1 246 PRO 246 247 247 PRO PRO A . n 
A 1 247 ALA 247 248 248 ALA ALA A . n 
A 1 248 GLN 248 249 249 GLN GLN A . n 
A 1 249 PRO 249 250 250 PRO PRO A . n 
A 1 250 LEU 250 251 251 LEU LEU A . n 
A 1 251 LYS 251 252 252 LYS LYS A . n 
A 1 252 ASN 252 253 253 ASN ASN A . n 
A 1 253 ARG 253 254 254 ARG ARG A . n 
A 1 254 GLN 254 255 255 GLN GLN A . n 
A 1 255 ILE 255 256 256 ILE ILE A . n 
A 1 256 LYS 256 257 257 LYS LYS A . n 
A 1 257 ALA 257 258 258 ALA ALA A . n 
A 1 258 SER 258 259 259 SER SER A . n 
A 1 259 PHE 259 260 260 PHE PHE A . n 
A 1 260 LYS 260 261 261 LYS LYS A . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 ZN  1   301 1   ZN  ZN  A . 
C 3 DMS 1   302 1   DMS DMS A . 
D 4 EDO 1   303 2   EDO EDO A . 
E 5 BCN 1   304 3   BCN BCN A . 
F 6 V50 1   305 1   V50 V50 A . 
G 6 V50 1   306 2   V50 V50 A . 
H 7 NA  1   307 1   NA  NA  A . 
I 8 HOH 1   401 148 HOH HOH A . 
I 8 HOH 2   402 199 HOH HOH A . 
I 8 HOH 3   403 240 HOH HOH A . 
I 8 HOH 4   404 170 HOH HOH A . 
I 8 HOH 5   405 201 HOH HOH A . 
I 8 HOH 6   406 283 HOH HOH A . 
I 8 HOH 7   407 109 HOH HOH A . 
I 8 HOH 8   408 280 HOH HOH A . 
I 8 HOH 9   409 218 HOH HOH A . 
I 8 HOH 10  410 278 HOH HOH A . 
I 8 HOH 11  411 273 HOH HOH A . 
I 8 HOH 12  412 210 HOH HOH A . 
I 8 HOH 13  413 225 HOH HOH A . 
I 8 HOH 14  414 236 HOH HOH A . 
I 8 HOH 15  415 143 HOH HOH A . 
I 8 HOH 16  416 98  HOH HOH A . 
I 8 HOH 17  417 281 HOH HOH A . 
I 8 HOH 18  418 191 HOH HOH A . 
I 8 HOH 19  419 223 HOH HOH A . 
I 8 HOH 20  420 284 HOH HOH A . 
I 8 HOH 21  421 192 HOH HOH A . 
I 8 HOH 22  422 220 HOH HOH A . 
I 8 HOH 23  423 23  HOH HOH A . 
I 8 HOH 24  424 6   HOH HOH A . 
I 8 HOH 25  425 72  HOH HOH A . 
I 8 HOH 26  426 172 HOH HOH A . 
I 8 HOH 27  427 53  HOH HOH A . 
I 8 HOH 28  428 27  HOH HOH A . 
I 8 HOH 29  429 127 HOH HOH A . 
I 8 HOH 30  430 257 HOH HOH A . 
I 8 HOH 31  431 78  HOH HOH A . 
I 8 HOH 32  432 117 HOH HOH A . 
I 8 HOH 33  433 2   HOH HOH A . 
I 8 HOH 34  434 118 HOH HOH A . 
I 8 HOH 35  435 111 HOH HOH A . 
I 8 HOH 36  436 260 HOH HOH A . 
I 8 HOH 37  437 221 HOH HOH A . 
I 8 HOH 38  438 84  HOH HOH A . 
I 8 HOH 39  439 13  HOH HOH A . 
I 8 HOH 40  440 7   HOH HOH A . 
I 8 HOH 41  441 263 HOH HOH A . 
I 8 HOH 42  442 141 HOH HOH A . 
I 8 HOH 43  443 24  HOH HOH A . 
I 8 HOH 44  444 94  HOH HOH A . 
I 8 HOH 45  445 267 HOH HOH A . 
I 8 HOH 46  446 54  HOH HOH A . 
I 8 HOH 47  447 41  HOH HOH A . 
I 8 HOH 48  448 59  HOH HOH A . 
I 8 HOH 49  449 18  HOH HOH A . 
I 8 HOH 50  450 55  HOH HOH A . 
I 8 HOH 51  451 95  HOH HOH A . 
I 8 HOH 52  452 198 HOH HOH A . 
I 8 HOH 53  453 244 HOH HOH A . 
I 8 HOH 54  454 211 HOH HOH A . 
I 8 HOH 55  455 121 HOH HOH A . 
I 8 HOH 56  456 120 HOH HOH A . 
I 8 HOH 57  457 256 HOH HOH A . 
I 8 HOH 58  458 231 HOH HOH A . 
I 8 HOH 59  459 44  HOH HOH A . 
I 8 HOH 60  460 258 HOH HOH A . 
I 8 HOH 61  461 138 HOH HOH A . 
I 8 HOH 62  462 119 HOH HOH A . 
I 8 HOH 63  463 43  HOH HOH A . 
I 8 HOH 64  464 156 HOH HOH A . 
I 8 HOH 65  465 113 HOH HOH A . 
I 8 HOH 66  466 75  HOH HOH A . 
I 8 HOH 67  467 115 HOH HOH A . 
I 8 HOH 68  468 31  HOH HOH A . 
I 8 HOH 69  469 38  HOH HOH A . 
I 8 HOH 70  470 102 HOH HOH A . 
I 8 HOH 71  471 183 HOH HOH A . 
I 8 HOH 72  472 47  HOH HOH A . 
I 8 HOH 73  473 145 HOH HOH A . 
I 8 HOH 74  474 105 HOH HOH A . 
I 8 HOH 75  475 17  HOH HOH A . 
I 8 HOH 76  476 65  HOH HOH A . 
I 8 HOH 77  477 154 HOH HOH A . 
I 8 HOH 78  478 36  HOH HOH A . 
I 8 HOH 79  479 129 HOH HOH A . 
I 8 HOH 80  480 190 HOH HOH A . 
I 8 HOH 81  481 19  HOH HOH A . 
I 8 HOH 82  482 133 HOH HOH A . 
I 8 HOH 83  483 67  HOH HOH A . 
I 8 HOH 84  484 25  HOH HOH A . 
I 8 HOH 85  485 14  HOH HOH A . 
I 8 HOH 86  486 88  HOH HOH A . 
I 8 HOH 87  487 106 HOH HOH A . 
I 8 HOH 88  488 261 HOH HOH A . 
I 8 HOH 89  489 48  HOH HOH A . 
I 8 HOH 90  490 146 HOH HOH A . 
I 8 HOH 91  491 254 HOH HOH A . 
I 8 HOH 92  492 85  HOH HOH A . 
I 8 HOH 93  493 46  HOH HOH A . 
I 8 HOH 94  494 122 HOH HOH A . 
I 8 HOH 95  495 103 HOH HOH A . 
I 8 HOH 96  496 5   HOH HOH A . 
I 8 HOH 97  497 8   HOH HOH A . 
I 8 HOH 98  498 50  HOH HOH A . 
I 8 HOH 99  499 73  HOH HOH A . 
I 8 HOH 100 500 32  HOH HOH A . 
I 8 HOH 101 501 222 HOH HOH A . 
I 8 HOH 102 502 205 HOH HOH A . 
I 8 HOH 103 503 164 HOH HOH A . 
I 8 HOH 104 504 12  HOH HOH A . 
I 8 HOH 105 505 28  HOH HOH A . 
I 8 HOH 106 506 247 HOH HOH A . 
I 8 HOH 107 507 11  HOH HOH A . 
I 8 HOH 108 508 197 HOH HOH A . 
I 8 HOH 109 509 159 HOH HOH A . 
I 8 HOH 110 510 79  HOH HOH A . 
I 8 HOH 111 511 130 HOH HOH A . 
I 8 HOH 112 512 10  HOH HOH A . 
I 8 HOH 113 513 1   HOH HOH A . 
I 8 HOH 114 514 200 HOH HOH A . 
I 8 HOH 115 515 57  HOH HOH A . 
I 8 HOH 116 516 29  HOH HOH A . 
I 8 HOH 117 517 66  HOH HOH A . 
I 8 HOH 118 518 87  HOH HOH A . 
I 8 HOH 119 519 49  HOH HOH A . 
I 8 HOH 120 520 136 HOH HOH A . 
I 8 HOH 121 521 251 HOH HOH A . 
I 8 HOH 122 522 203 HOH HOH A . 
I 8 HOH 123 523 224 HOH HOH A . 
I 8 HOH 124 524 83  HOH HOH A . 
I 8 HOH 125 525 86  HOH HOH A . 
I 8 HOH 126 526 63  HOH HOH A . 
I 8 HOH 127 527 30  HOH HOH A . 
I 8 HOH 128 528 9   HOH HOH A . 
I 8 HOH 129 529 150 HOH HOH A . 
I 8 HOH 130 530 125 HOH HOH A . 
I 8 HOH 131 531 45  HOH HOH A . 
I 8 HOH 132 532 104 HOH HOH A . 
I 8 HOH 133 533 108 HOH HOH A . 
I 8 HOH 134 534 206 HOH HOH A . 
I 8 HOH 135 535 246 HOH HOH A . 
I 8 HOH 136 536 39  HOH HOH A . 
I 8 HOH 137 537 155 HOH HOH A . 
I 8 HOH 138 538 34  HOH HOH A . 
I 8 HOH 139 539 91  HOH HOH A . 
I 8 HOH 140 540 61  HOH HOH A . 
I 8 HOH 141 541 76  HOH HOH A . 
I 8 HOH 142 542 226 HOH HOH A . 
I 8 HOH 143 543 230 HOH HOH A . 
I 8 HOH 144 544 42  HOH HOH A . 
I 8 HOH 145 545 140 HOH HOH A . 
I 8 HOH 146 546 97  HOH HOH A . 
I 8 HOH 147 547 80  HOH HOH A . 
I 8 HOH 148 548 142 HOH HOH A . 
I 8 HOH 149 549 253 HOH HOH A . 
I 8 HOH 150 550 69  HOH HOH A . 
I 8 HOH 151 551 168 HOH HOH A . 
I 8 HOH 152 552 15  HOH HOH A . 
I 8 HOH 153 553 182 HOH HOH A . 
I 8 HOH 154 554 241 HOH HOH A . 
I 8 HOH 155 555 100 HOH HOH A . 
I 8 HOH 156 556 282 HOH HOH A . 
I 8 HOH 157 557 144 HOH HOH A . 
I 8 HOH 158 558 185 HOH HOH A . 
I 8 HOH 159 559 40  HOH HOH A . 
I 8 HOH 160 560 90  HOH HOH A . 
I 8 HOH 161 561 70  HOH HOH A . 
I 8 HOH 162 562 81  HOH HOH A . 
I 8 HOH 163 563 235 HOH HOH A . 
I 8 HOH 164 564 124 HOH HOH A . 
I 8 HOH 165 565 101 HOH HOH A . 
I 8 HOH 166 566 22  HOH HOH A . 
I 8 HOH 167 567 128 HOH HOH A . 
I 8 HOH 168 568 135 HOH HOH A . 
I 8 HOH 169 569 96  HOH HOH A . 
I 8 HOH 170 570 149 HOH HOH A . 
I 8 HOH 171 571 186 HOH HOH A . 
I 8 HOH 172 572 77  HOH HOH A . 
I 8 HOH 173 573 202 HOH HOH A . 
I 8 HOH 174 574 52  HOH HOH A . 
I 8 HOH 175 575 165 HOH HOH A . 
I 8 HOH 176 576 74  HOH HOH A . 
I 8 HOH 177 577 160 HOH HOH A . 
I 8 HOH 178 578 21  HOH HOH A . 
I 8 HOH 179 579 276 HOH HOH A . 
I 8 HOH 180 580 116 HOH HOH A . 
I 8 HOH 181 581 64  HOH HOH A . 
I 8 HOH 182 582 3   HOH HOH A . 
I 8 HOH 183 583 271 HOH HOH A . 
I 8 HOH 184 584 153 HOH HOH A . 
I 8 HOH 185 585 68  HOH HOH A . 
I 8 HOH 186 586 35  HOH HOH A . 
I 8 HOH 187 587 60  HOH HOH A . 
I 8 HOH 188 588 51  HOH HOH A . 
I 8 HOH 189 589 174 HOH HOH A . 
I 8 HOH 190 590 194 HOH HOH A . 
I 8 HOH 191 591 139 HOH HOH A . 
I 8 HOH 192 592 37  HOH HOH A . 
I 8 HOH 193 593 147 HOH HOH A . 
I 8 HOH 194 594 92  HOH HOH A . 
I 8 HOH 195 595 33  HOH HOH A . 
I 8 HOH 196 596 152 HOH HOH A . 
I 8 HOH 197 597 187 HOH HOH A . 
I 8 HOH 198 598 4   HOH HOH A . 
I 8 HOH 199 599 16  HOH HOH A . 
I 8 HOH 200 600 269 HOH HOH A . 
I 8 HOH 201 601 20  HOH HOH A . 
I 8 HOH 202 602 213 HOH HOH A . 
I 8 HOH 203 603 243 HOH HOH A . 
I 8 HOH 204 604 137 HOH HOH A . 
I 8 HOH 205 605 209 HOH HOH A . 
I 8 HOH 206 606 229 HOH HOH A . 
I 8 HOH 207 607 114 HOH HOH A . 
I 8 HOH 208 608 195 HOH HOH A . 
I 8 HOH 209 609 26  HOH HOH A . 
I 8 HOH 210 610 107 HOH HOH A . 
I 8 HOH 211 611 58  HOH HOH A . 
I 8 HOH 212 612 233 HOH HOH A . 
I 8 HOH 213 613 232 HOH HOH A . 
I 8 HOH 214 614 277 HOH HOH A . 
I 8 HOH 215 615 82  HOH HOH A . 
I 8 HOH 216 616 89  HOH HOH A . 
I 8 HOH 217 617 151 HOH HOH A . 
I 8 HOH 218 618 167 HOH HOH A . 
I 8 HOH 219 619 112 HOH HOH A . 
I 8 HOH 220 620 219 HOH HOH A . 
I 8 HOH 221 621 207 HOH HOH A . 
I 8 HOH 222 622 275 HOH HOH A . 
I 8 HOH 223 623 234 HOH HOH A . 
I 8 HOH 224 624 217 HOH HOH A . 
I 8 HOH 225 625 93  HOH HOH A . 
I 8 HOH 226 626 238 HOH HOH A . 
I 8 HOH 227 627 132 HOH HOH A . 
I 8 HOH 228 628 239 HOH HOH A . 
I 8 HOH 229 629 188 HOH HOH A . 
I 8 HOH 230 630 162 HOH HOH A . 
I 8 HOH 231 631 215 HOH HOH A . 
I 8 HOH 232 632 245 HOH HOH A . 
I 8 HOH 233 633 62  HOH HOH A . 
I 8 HOH 234 634 176 HOH HOH A . 
I 8 HOH 235 635 131 HOH HOH A . 
I 8 HOH 236 636 71  HOH HOH A . 
I 8 HOH 237 637 285 HOH HOH A . 
I 8 HOH 238 638 237 HOH HOH A . 
I 8 HOH 239 639 279 HOH HOH A . 
I 8 HOH 240 640 249 HOH HOH A . 
I 8 HOH 241 641 274 HOH HOH A . 
I 8 HOH 242 642 255 HOH HOH A . 
I 8 HOH 243 643 270 HOH HOH A . 
I 8 HOH 244 644 157 HOH HOH A . 
I 8 HOH 245 645 178 HOH HOH A . 
I 8 HOH 246 646 208 HOH HOH A . 
I 8 HOH 247 647 216 HOH HOH A . 
I 8 HOH 248 648 123 HOH HOH A . 
I 8 HOH 249 649 161 HOH HOH A . 
I 8 HOH 250 650 265 HOH HOH A . 
I 8 HOH 251 651 242 HOH HOH A . 
I 8 HOH 252 652 252 HOH HOH A . 
I 8 HOH 253 653 196 HOH HOH A . 
I 8 HOH 254 654 189 HOH HOH A . 
I 8 HOH 255 655 214 HOH HOH A . 
I 8 HOH 256 656 259 HOH HOH A . 
I 8 HOH 257 657 169 HOH HOH A . 
I 8 HOH 258 658 171 HOH HOH A . 
I 8 HOH 259 659 262 HOH HOH A . 
I 8 HOH 260 660 163 HOH HOH A . 
I 8 HOH 261 661 228 HOH HOH A . 
I 8 HOH 262 662 184 HOH HOH A . 
I 8 HOH 263 663 99  HOH HOH A . 
I 8 HOH 264 664 180 HOH HOH A . 
I 8 HOH 265 665 250 HOH HOH A . 
I 8 HOH 266 666 204 HOH HOH A . 
I 8 HOH 267 667 134 HOH HOH A . 
I 8 HOH 268 668 193 HOH HOH A . 
I 8 HOH 269 669 110 HOH HOH A . 
I 8 HOH 270 670 212 HOH HOH A . 
I 8 HOH 271 671 268 HOH HOH A . 
I 8 HOH 272 672 272 HOH HOH A . 
I 8 HOH 273 673 173 HOH HOH A . 
I 8 HOH 274 674 126 HOH HOH A . 
I 8 HOH 275 675 264 HOH HOH A . 
I 8 HOH 276 676 166 HOH HOH A . 
I 8 HOH 277 677 175 HOH HOH A . 
I 8 HOH 278 678 56  HOH HOH A . 
I 8 HOH 279 679 181 HOH HOH A . 
I 8 HOH 280 680 266 HOH HOH A . 
I 8 HOH 281 681 248 HOH HOH A . 
I 8 HOH 282 682 179 HOH HOH A . 
I 8 HOH 283 683 227 HOH HOH A . 
I 8 HOH 284 684 177 HOH HOH A . 
I 8 HOH 285 685 158 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 9   CD  
2  1 Y 1 A LYS 9   ? CE  ? A LYS 9   CE  
3  1 Y 1 A LYS 9   ? NZ  ? A LYS 9   NZ  
4  1 Y 1 A LYS 159 ? CD  ? A LYS 158 CD  
5  1 Y 1 A LYS 159 ? CE  ? A LYS 158 CE  
6  1 Y 1 A LYS 159 ? NZ  ? A LYS 158 NZ  
7  1 Y 1 A LYS 228 ? NZ  ? A LYS 227 NZ  
8  1 Y 1 A LYS 261 ? CD  ? A LYS 260 CD  
9  1 Y 1 A LYS 261 ? CE  ? A LYS 260 CE  
10 1 Y 1 A LYS 261 ? NZ  ? A LYS 260 NZ  
11 1 N 0 A V50 305 ? C15 B F V50 ?   C15 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement        ? ? ? ? ? ? ? ? ? ? ? REFMAC      ? ? ? .    1 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.10 2 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? XDS         ? ? ? .    3 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? SCALA       ? ? ? .    4 
? phasing           ? ? ? ? ? ? ? ? ? ? ? MOLREP      ? ? ? .    5 
? 'model building'  ? ? ? ? ? ? ? ? ? ? ? Coot        ? ? ? .    6 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   104.310 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     6QL1 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     42.299 
_cell.length_a_esd                 ? 
_cell.length_b                     41.401 
_cell.length_b_esd                 ? 
_cell.length_c                     71.242 
_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                         6QL1 
_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                   6QL1 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                      ? 
_exptl_crystal.density_diffrn              ? 
_exptl_crystal.density_Matthews            2.06 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         40.24 
_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), 0.2M ammonium sulfate and 2M sodium malonate (pH 7)' 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2013-05-21 
_diffrn_detector.pdbx_frequency               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.976300 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'PETRA III, EMBL c/o DESY BEAMLINE P14 (MX2)' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.976300 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'P14 (MX2)' 
_diffrn_source.pdbx_synchrotron_site       'PETRA III, EMBL c/o DESY' 
# 
_reflns.B_iso_Wilson_estimate            ? 
_reflns.entry_id                         6QL1 
_reflns.data_reduction_details           ? 
_reflns.data_reduction_method            ? 
_reflns.d_resolution_high                1.418 
_reflns.d_resolution_low                 69.031 
_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                       42097 
_reflns.number_obs                       42097 
_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             92.800 
_reflns.R_free_details                   ? 
_reflns.Rmerge_F_all                     ? 
_reflns.Rmerge_F_obs                     ? 
_reflns.Friedel_coverage                 ? 
_reflns.number_gt                        ? 
_reflns.threshold_expression             ? 
_reflns.pdbx_redundancy                  7.000 
_reflns.pdbx_Rmerge_I_obs                ? 
_reflns.pdbx_Rmerge_I_all                ? 
_reflns.pdbx_Rsym_value                  0.042 
_reflns.pdbx_netI_over_av_sigmaI         9.804 
_reflns.pdbx_netI_over_sigmaI            22.700 
_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                  0.052 
_reflns.pdbx_Rpim_I_all                  0.019 
_reflns.pdbx_d_opt                       ? 
_reflns.pdbx_number_measured_all         293373 
_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 
1.420 1.500  ? 3.0  ? ? ? ? ? 74.100 ? ? ? ? 0.241 ? ? ? ? ? ? ? ? 6.600 0.241 ? ? ? 0.293 0.112 ? 1  1 ? ? 
1.500 1.590  ? 4.4  ? ? ? ? ? 95.000 ? ? ? ? 0.162 ? ? ? ? ? ? ? ? 7.100 0.162 ? ? ? 0.193 0.072 ? 2  1 ? ? 
1.590 1.700  ? 6.0  ? ? ? ? ? 94.200 ? ? ? ? 0.116 ? ? ? ? ? ? ? ? 6.900 0.116 ? ? ? 0.141 0.053 ? 3  1 ? ? 
1.700 1.830  ? 8.4  ? ? ? ? ? 96.400 ? ? ? ? 0.082 ? ? ? ? ? ? ? ? 7.200 0.082 ? ? ? 0.101 0.037 ? 4  1 ? ? 
1.830 2.010  ? 11.9 ? ? ? ? ? 95.100 ? ? ? ? 0.057 ? ? ? ? ? ? ? ? 6.900 0.057 ? ? ? 0.071 0.027 ? 5  1 ? ? 
2.010 2.240  ? 15.2 ? ? ? ? ? 97.400 ? ? ? ? 0.044 ? ? ? ? ? ? ? ? 7.200 0.044 ? ? ? 0.055 0.020 ? 6  1 ? ? 
2.240 2.590  ? 16.8 ? ? ? ? ? 96.200 ? ? ? ? 0.038 ? ? ? ? ? ? ? ? 6.900 0.038 ? ? ? 0.048 0.018 ? 7  1 ? ? 
2.590 3.170  ? 17.4 ? ? ? ? ? 98.600 ? ? ? ? 0.035 ? ? ? ? ? ? ? ? 7.200 0.035 ? ? ? 0.043 0.016 ? 8  1 ? ? 
3.170 4.490  ? 17.9 ? ? ? ? ? 96.700 ? ? ? ? 0.030 ? ? ? ? ? ? ? ? 6.800 0.030 ? ? ? 0.036 0.014 ? 9  1 ? ? 
4.490 69.031 ? 18.1 ? ? ? ? ? 97.800 ? ? ? ? 0.029 ? ? ? ? ? ? ? ? 6.800 0.029 ? ? ? 0.035 0.013 ? 10 1 ? ? 
# 
_refine.aniso_B[1][1]                            -0.0100 
_refine.aniso_B[1][2]                            0.0000 
_refine.aniso_B[1][3]                            0.2200 
_refine.aniso_B[2][2]                            -0.1200 
_refine.aniso_B[2][3]                            0.0000 
_refine.aniso_B[3][3]                            0.0200 
_refine.B_iso_max                                87.090 
_refine.B_iso_mean                               16.7794 
_refine.B_iso_min                                5.920 
_refine.correlation_coeff_Fo_to_Fc               0.9690 
_refine.correlation_coeff_Fo_to_Fc_free          0.9570 
_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                                 6QL1 
_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                            1.4200 
_refine.ls_d_res_low                             39.8600 
_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                     42082 
_refine.ls_number_reflns_R_free                  4219 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    92.4300 
_refine.ls_percent_reflns_R_free                 10.0000 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1611 
_refine.ls_R_factor_R_free                       0.1857 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1583 
_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                       0.0730 
_refine.pdbx_overall_ESU_R_Free                  0.0730 
_refine.pdbx_solvent_vdw_probe_radii             1.4000 
_refine.pdbx_solvent_ion_probe_radii             0.8000 
_refine.pdbx_solvent_shrinkage_radii             0.8000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_R_Cruickshank_DPI             0.0725 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        2044 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         67 
_refine_hist.number_atoms_solvent             285 
_refine_hist.number_atoms_total               2396 
_refine_hist.d_res_high                       1.4200 
_refine_hist.d_res_low                        39.8600 
# 
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  2341 ? r_bond_refined_d       ? ? 
'X-RAY DIFFRACTION' ? 1.992  1.682  3207 ? r_angle_refined_deg    ? ? 
'X-RAY DIFFRACTION' ? 7.079  5.000  289  ? r_dihedral_angle_1_deg ? ? 
'X-RAY DIFFRACTION' ? 36.118 23.772 114  ? r_dihedral_angle_2_deg ? ? 
'X-RAY DIFFRACTION' ? 14.124 15.000 377  ? r_dihedral_angle_3_deg ? ? 
'X-RAY DIFFRACTION' ? 18.978 15.000 8    ? r_dihedral_angle_4_deg ? ? 
'X-RAY DIFFRACTION' ? 0.137  0.200  279  ? r_chiral_restr         ? ? 
'X-RAY DIFFRACTION' ? 0.020  0.020  1873 ? r_gen_planes_refined   ? ? 
'X-RAY DIFFRACTION' ? 1.672  1.335  1111 ? r_mcbond_it            ? ? 
'X-RAY DIFFRACTION' ? 2.480  2.001  1415 ? r_mcangle_it           ? ? 
'X-RAY DIFFRACTION' ? 2.664  1.639  1230 ? r_scbond_it            ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.4180 
_refine_ls_shell.d_res_low                        1.4550 
_refine_ls_shell.number_reflns_all                1937 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             197 
_refine_ls_shell.number_reflns_R_work             1740 
_refine_ls_shell.percent_reflns_obs               57.7000 
_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                  0.2800 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.2150 
_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                     6QL1 
_struct.title                        
'Crystal structure of chimeric carbonic anhydrase VI with 4-[(4,6-dimethylpyrimidin-2-yl)thio]-2,3,5,6-tetrafluorobenzenesulfonamide' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        6QL1 
_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 6 ? 
H N N 7 ? 
I N N 8 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CAH2_HUMAN 
_struct_ref.pdbx_db_accession          P00918 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MSHHWGYGKHNGPEHWHKDFPIAKGERQSPVDIDTHTAKYDPSLKPLSVSYDQATSLRILNNGHAFNVEFDDSQDKAVLK
GGPLDGTYRLIQFHFHWGSLDGQGSEHTVDKKKYAAELHLVHWNTKYGDFGKAVQQPDGLAVLGIFLKVGSAKPGLQKVV
DVLDSIKTKGKSADFTNFDPRGLLPESLDYWTYPGSLTTPPLLECVTWIVLKEPISVSSEQVLKFRKLNFNGEGEPEELM
VDNWRPAQPLKNRQIKASFK
;
_struct_ref.pdbx_align_begin           1 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              6QL1 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 260 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P00918 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  260 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       261 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 6QL1 THR A 65  ? UNP P00918 ALA 65  'engineered mutation' 65  1 
1 6QL1 GLN A 67  ? UNP P00918 ASN 67  'engineered mutation' 67  2 
1 6QL1 TYR A 130 ? UNP P00918 PHE 130 'engineered mutation' 131 3 
1 6QL1 GLN A 134 ? UNP P00918 VAL 134 'engineered mutation' 135 4 
1 6QL1 THR A 203 ? UNP P00918 LEU 203 'engineered mutation' 204 5 
# 
_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)' 790   ? 
1 MORE         -2    ? 
1 'SSA (A^2)'  11360 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   homology 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 GLY A 12  ? ASP A 19  ? GLY A 12  ASP A 19  5 ? 8 
HELX_P HELX_P2 AA2 PHE A 20  ? GLY A 25  ? PHE A 20  GLY A 25  5 ? 6 
HELX_P HELX_P3 AA3 LYS A 126 ? GLY A 128 ? LYS A 127 GLY A 129 5 ? 3 
HELX_P HELX_P4 AA4 ASP A 129 ? GLN A 134 ? ASP A 130 GLN A 135 1 ? 6 
HELX_P HELX_P5 AA5 LYS A 153 ? GLY A 155 ? LYS A 154 GLY A 156 5 ? 3 
HELX_P HELX_P6 AA6 LEU A 156 ? LEU A 163 ? LEU A 157 LEU A 164 1 ? 8 
HELX_P HELX_P7 AA7 ASP A 164 ? LYS A 167 ? ASP A 165 LYS A 168 5 ? 4 
HELX_P HELX_P8 AA8 ASP A 179 ? LEU A 184 ? ASP A 180 LEU A 185 5 ? 6 
HELX_P HELX_P9 AA9 SER A 218 ? ARG A 226 ? SER A 219 ARG A 227 1 ? 9 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1  metalc ? ? A HIS 94  NE2 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 94  A ZN  301 1_555 ? ? ? ? ? ? ? 1.997 ? ? 
metalc2  metalc ? ? A HIS 96  NE2 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 96  A ZN  301 1_555 ? ? ? ? ? ? ? 2.021 ? ? 
metalc3  metalc ? ? A HIS 119 ND1 ? ? ? 1_555 B ZN  . ZN  ? ? A HIS 119 A ZN  301 1_555 ? ? ? ? ? ? ? 2.037 ? ? 
metalc4  metalc ? ? A GLY 234 O   ? ? ? 1_555 H NA  . NA  ? ? A GLY 235 A NA  307 2_645 ? ? ? ? ? ? ? 2.534 ? ? 
metalc5  metalc ? ? B ZN  .   ZN  ? ? ? 1_555 F V50 . N23 A ? A ZN  301 A V50 305 1_555 ? ? ? ? ? ? ? 1.939 ? ? 
metalc6  metalc ? ? B ZN  .   ZN  ? ? ? 1_555 F V50 . N23 B ? A ZN  301 A V50 305 1_555 ? ? ? ? ? ? ? 1.969 ? ? 
metalc7  metalc ? ? H NA  .   NA  ? ? ? 1_555 I HOH . O   ? ? A NA  307 A HOH 581 1_555 ? ? ? ? ? ? ? 2.551 ? ? 
metalc8  metalc ? ? H NA  .   NA  ? ? ? 1_555 I HOH . O   ? ? A NA  307 A HOH 583 1_555 ? ? ? ? ? ? ? 2.813 ? ? 
metalc9  metalc ? ? H NA  .   NA  ? ? ? 1_555 I HOH . O   ? ? A NA  307 A HOH 596 1_555 ? ? ? ? ? ? ? 2.297 ? ? 
metalc10 metalc ? ? H NA  .   NA  ? ? ? 1_555 I HOH . O   ? ? A NA  307 A HOH 614 1_555 ? ? ? ? ? ? ? 2.221 ? ? 
metalc11 metalc ? ? H NA  .   NA  ? ? ? 1_555 I HOH . O   ? ? A NA  307 A HOH 622 1_555 ? ? ? ? ? ? ? 2.362 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 NE2 ? A HIS 96  ? A HIS 96  ? 1_555 103.7 ? 
2  NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 112.8 ? 
3  NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 119 ? A HIS 119 ? 1_555 98.1  ? 
4  NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N23 A F V50 .   ? A V50 305 ? 1_555 120.7 ? 
5  NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N23 A F V50 .   ? A V50 305 ? 1_555 117.2 ? 
6  ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N23 A F V50 .   ? A V50 305 ? 1_555 102.3 ? 
7  NE2 ? A HIS 94  ? A HIS 94  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N23 B F V50 .   ? A V50 305 ? 1_555 103.3 ? 
8  NE2 ? A HIS 96  ? A HIS 96  ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N23 B F V50 .   ? A V50 305 ? 1_555 112.9 ? 
9  ND1 ? A HIS 119 ? A HIS 119 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N23 B F V50 .   ? A V50 305 ? 1_555 124.5 ? 
10 N23 A F V50 .   ? A V50 305 ? 1_555 ZN ? B ZN . ? A ZN 301 ? 1_555 N23 B F V50 .   ? A V50 305 ? 1_555 22.6  ? 
11 O   ? A GLY 234 ? A GLY 235 ? 1_555 NA ? H NA . ? A NA 307 ? 2_645 O   ? I HOH .   ? A HOH 581 ? 1_555 41.6  ? 
12 O   ? A GLY 234 ? A GLY 235 ? 1_555 NA ? H NA . ? A NA 307 ? 2_645 O   ? I HOH .   ? A HOH 583 ? 1_555 45.6  ? 
13 O   ? I HOH .   ? A HOH 581 ? 1_555 NA ? H NA . ? A NA 307 ? 2_645 O   ? I HOH .   ? A HOH 583 ? 1_555 5.2   ? 
14 O   ? A GLY 234 ? A GLY 235 ? 1_555 NA ? H NA . ? A NA 307 ? 2_645 O   ? I HOH .   ? A HOH 596 ? 1_555 40.9  ? 
15 O   ? I HOH .   ? A HOH 581 ? 1_555 NA ? H NA . ? A NA 307 ? 2_645 O   ? I HOH .   ? A HOH 596 ? 1_555 1.8   ? 
16 O   ? I HOH .   ? A HOH 583 ? 1_555 NA ? H NA . ? A NA 307 ? 2_645 O   ? I HOH .   ? A HOH 596 ? 1_555 4.9   ? 
17 O   ? A GLY 234 ? A GLY 235 ? 1_555 NA ? H NA . ? A NA 307 ? 2_645 O   ? I HOH .   ? A HOH 614 ? 1_555 46.1  ? 
18 O   ? I HOH .   ? A HOH 581 ? 1_555 NA ? H NA . ? A NA 307 ? 2_645 O   ? I HOH .   ? A HOH 614 ? 1_555 5.5   ? 
19 O   ? I HOH .   ? A HOH 583 ? 1_555 NA ? H NA . ? A NA 307 ? 2_645 O   ? I HOH .   ? A HOH 614 ? 1_555 6.7   ? 
20 O   ? I HOH .   ? A HOH 596 ? 1_555 NA ? H NA . ? A NA 307 ? 2_645 O   ? I HOH .   ? A HOH 614 ? 1_555 7.1   ? 
21 O   ? A GLY 234 ? A GLY 235 ? 1_555 NA ? H NA . ? A NA 307 ? 2_645 O   ? I HOH .   ? A HOH 622 ? 1_555 42.2  ? 
22 O   ? I HOH .   ? A HOH 581 ? 1_555 NA ? H NA . ? A NA 307 ? 2_645 O   ? I HOH .   ? A HOH 622 ? 1_555 4.5   ? 
23 O   ? I HOH .   ? A HOH 583 ? 1_555 NA ? H NA . ? A NA 307 ? 2_645 O   ? I HOH .   ? A HOH 622 ? 1_555 8.6   ? 
24 O   ? I HOH .   ? A HOH 596 ? 1_555 NA ? H NA . ? A NA 307 ? 2_645 O   ? I HOH .   ? A HOH 622 ? 1_555 6.2   ? 
25 O   ? I HOH .   ? A HOH 614 ? 1_555 NA ? H NA . ? A NA 307 ? 2_645 O   ? I HOH .   ? A HOH 622 ? 1_555 4.1   ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 SER 29  A . ? SER 29  A PRO 30  A ? PRO 30  A 1 -1.49 
2 PRO 200 A . ? PRO 201 A PRO 201 A ? PRO 202 A 1 9.34  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2  ? 
AA2 ? 10 ? 
AA3 ? 6  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2  ? parallel      
AA2 1 2  ? parallel      
AA2 2 3  ? anti-parallel 
AA2 3 4  ? anti-parallel 
AA2 4 5  ? parallel      
AA2 5 6  ? anti-parallel 
AA2 6 7  ? anti-parallel 
AA2 7 8  ? anti-parallel 
AA2 8 9  ? anti-parallel 
AA2 9 10 ? anti-parallel 
AA3 1 2  ? anti-parallel 
AA3 2 3  ? anti-parallel 
AA3 3 4  ? anti-parallel 
AA3 4 5  ? anti-parallel 
AA3 5 6  ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1  ASP A 32  ? ILE A 33  ? ASP A 32  ILE A 33  
AA1 2  THR A 108 ? VAL A 109 ? THR A 108 VAL A 109 
AA2 1  LYS A 39  ? TYR A 40  ? LYS A 39  TYR A 40  
AA2 2  LYS A 256 ? ALA A 257 ? LYS A 257 ALA A 258 
AA2 3  TYR A 190 ? GLY A 195 ? TYR A 191 GLY A 196 
AA2 4  VAL A 206 ? LEU A 211 ? VAL A 207 LEU A 212 
AA2 5  LEU A 140 ? VAL A 149 ? LEU A 141 VAL A 150 
AA2 6  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
AA2 7  THR A 87  ? TRP A 97  ? THR A 87  TRP A 97  
AA2 8  PHE A 66  ? PHE A 70  ? PHE A 66  PHE A 70  
AA2 9  SER A 56  ? ASN A 61  ? SER A 56  ASN A 61  
AA2 10 SER A 172 ? ASP A 174 ? SER A 173 ASP A 175 
AA3 1  LEU A 47  ? SER A 50  ? LEU A 47  SER A 50  
AA3 2  VAL A 78  ? GLY A 81  ? VAL A 78  GLY A 81  
AA3 3  THR A 87  ? TRP A 97  ? THR A 87  TRP A 97  
AA3 4  ALA A 116 ? ASN A 124 ? ALA A 116 ASN A 124 
AA3 5  LEU A 140 ? VAL A 149 ? LEU A 141 VAL A 150 
AA3 6  ILE A 215 ? VAL A 217 ? ILE A 216 VAL A 218 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2  N ILE A 33  ? N ILE A 33  O THR A 108 ? O THR A 108 
AA2 1 2  N LYS A 39  ? N LYS A 39  O ALA A 257 ? O ALA A 258 
AA2 2 3  O LYS A 256 ? O LYS A 257 N THR A 192 ? N THR A 193 
AA2 3 4  N GLY A 195 ? N GLY A 196 O VAL A 206 ? O VAL A 207 
AA2 4 5  O LEU A 211 ? O LEU A 212 N GLY A 144 ? N GLY A 145 
AA2 5 6  O ILE A 145 ? O ILE A 146 N LEU A 118 ? N LEU A 118 
AA2 6 7  O VAL A 121 ? O VAL A 121 N GLN A 92  ? N GLN A 92  
AA2 7 8  O ILE A 91  ? O ILE A 91  N PHE A 70  ? N PHE A 70  
AA2 8 9  O GLU A 69  ? O GLU A 69  N LEU A 57  ? N LEU A 57  
AA2 9 10 N ILE A 59  ? N ILE A 59  O ALA A 173 ? O ALA A 174 
AA3 1 2  N SER A 50  ? N SER A 50  O VAL A 78  ? O VAL A 78  
AA3 2 3  N LEU A 79  ? N LEU A 79  O TYR A 88  ? O TYR A 88  
AA3 3 4  N GLN A 92  ? N GLN A 92  O VAL A 121 ? O VAL A 121 
AA3 4 5  N LEU A 118 ? N LEU A 118 O ILE A 145 ? O ILE A 146 
AA3 5 6  N LYS A 148 ? N LYS A 149 O VAL A 217 ? 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 DMS 302 ? 4  'binding site for residue DMS A 302' 
AC3 Software A EDO 303 ? 4  'binding site for residue EDO A 303' 
AC4 Software A BCN 304 ? 5  'binding site for residue BCN A 304' 
AC5 Software A V50 305 ? 17 'binding site for residue V50 A 305' 
AC6 Software A V50 306 ? 12 'binding site for residue V50 A 306' 
AC7 Software A NA  307 ? 5  'binding site for residue NA A 307'  
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  AC1 4  HIS A 94  ? HIS A 94  . ? 1_555 ? 
2  AC1 4  HIS A 96  ? HIS A 96  . ? 1_555 ? 
3  AC1 4  HIS A 119 ? HIS A 119 . ? 1_555 ? 
4  AC1 4  V50 F .   ? V50 A 305 . ? 1_555 ? 
5  AC2 4  TYR A 7   ? TYR A 7   . ? 1_555 ? 
6  AC2 4  ASP A 242 ? ASP A 243 . ? 1_555 ? 
7  AC2 4  TRP A 244 ? TRP A 245 . ? 1_555 ? 
8  AC2 4  HOH I .   ? HOH A 554 . ? 1_555 ? 
9  AC3 4  GLN A 67  ? GLN A 67  . ? 1_555 ? 
10 AC3 4  ILE A 91  ? ILE A 91  . ? 1_555 ? 
11 AC3 4  HOH I .   ? HOH A 424 . ? 1_555 ? 
12 AC3 4  HOH I .   ? HOH A 472 . ? 1_555 ? 
13 AC4 5  LYS A 148 ? LYS A 149 . ? 1_555 ? 
14 AC4 5  LYS A 212 ? LYS A 213 . ? 1_555 ? 
15 AC4 5  PRO A 214 ? PRO A 215 . ? 1_555 ? 
16 AC4 5  HOH I .   ? HOH A 461 . ? 1_555 ? 
17 AC4 5  HOH I .   ? HOH A 476 . ? 1_555 ? 
18 AC5 17 HIS A 64  ? HIS A 64  . ? 1_555 ? 
19 AC5 17 GLN A 92  ? GLN A 92  . ? 1_555 ? 
20 AC5 17 HIS A 94  ? HIS A 94  . ? 1_555 ? 
21 AC5 17 HIS A 96  ? HIS A 96  . ? 1_555 ? 
22 AC5 17 HIS A 119 ? HIS A 119 . ? 1_555 ? 
23 AC5 17 VAL A 121 ? VAL A 121 . ? 1_555 ? 
24 AC5 17 TYR A 130 ? TYR A 131 . ? 1_555 ? 
25 AC5 17 GLN A 134 ? GLN A 135 . ? 1_555 ? 
26 AC5 17 VAL A 142 ? VAL A 143 . ? 1_555 ? 
27 AC5 17 LEU A 197 ? LEU A 198 . ? 1_555 ? 
28 AC5 17 THR A 198 ? THR A 199 . ? 1_555 ? 
29 AC5 17 THR A 199 ? THR A 200 . ? 1_555 ? 
30 AC5 17 PRO A 200 ? PRO A 201 . ? 1_555 ? 
31 AC5 17 PRO A 201 ? PRO A 202 . ? 1_555 ? 
32 AC5 17 TRP A 208 ? TRP A 209 . ? 1_555 ? 
33 AC5 17 ZN  B .   ? ZN  A 301 . ? 1_555 ? 
34 AC5 17 HOH I .   ? HOH A 424 . ? 1_555 ? 
35 AC6 12 HIS A 4   ? HIS A 4   . ? 1_555 ? 
36 AC6 12 TRP A 5   ? TRP A 5   . ? 1_555 ? 
37 AC6 12 HIS A 10  ? HIS A 10  . ? 1_555 ? 
38 AC6 12 ASN A 11  ? ASN A 11  . ? 1_555 ? 
39 AC6 12 HIS A 15  ? HIS A 15  . ? 1_555 ? 
40 AC6 12 TRP A 16  ? TRP A 16  . ? 1_555 ? 
41 AC6 12 ASP A 19  ? ASP A 19  . ? 1_555 ? 
42 AC6 12 ASP A 179 ? ASP A 180 . ? 1_655 ? 
43 AC6 12 ARG A 181 ? ARG A 182 . ? 1_655 ? 
44 AC6 12 GLY A 182 ? GLY A 183 . ? 1_655 ? 
45 AC6 12 HOH I .   ? HOH A 430 . ? 1_555 ? 
46 AC6 12 HOH I .   ? HOH A 508 . ? 1_655 ? 
47 AC7 5  HOH I .   ? HOH A 581 . ? 1_555 ? 
48 AC7 5  HOH I .   ? HOH A 583 . ? 1_555 ? 
49 AC7 5  HOH I .   ? HOH A 596 . ? 1_555 ? 
50 AC7 5  HOH I .   ? HOH A 614 . ? 1_555 ? 
51 AC7 5  HOH I .   ? HOH A 622 . ? 1_555 ? 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 NH1 A ARG 27 ? A O A HOH 401 ? ? 2.05 
2 1 OG  A SER 73 ? ? O A HOH 402 ? ? 2.18 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             CB 
_pdbx_validate_rmsd_angle.auth_asym_id_1             A 
_pdbx_validate_rmsd_angle.auth_comp_id_1             TYR 
_pdbx_validate_rmsd_angle.auth_seq_id_1              131 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CG 
_pdbx_validate_rmsd_angle.auth_asym_id_2             A 
_pdbx_validate_rmsd_angle.auth_comp_id_2             TYR 
_pdbx_validate_rmsd_angle.auth_seq_id_2              131 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             CD2 
_pdbx_validate_rmsd_angle.auth_asym_id_3             A 
_pdbx_validate_rmsd_angle.auth_comp_id_3             TYR 
_pdbx_validate_rmsd_angle.auth_seq_id_3              131 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                116.27 
_pdbx_validate_rmsd_angle.angle_target_value         121.00 
_pdbx_validate_rmsd_angle.angle_deviation            -4.73 
_pdbx_validate_rmsd_angle.angle_standard_deviation   0.60 
_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 ASN A 11  ? ? -140.76 19.97   
2 1 HIS A 64  ? B -145.23 -0.30   
3 1 LYS A 76  ? ? -115.26 -88.54  
4 1 LYS A 111 ? ? 74.44   -0.81   
5 1 PHE A 176 ? ? -150.93 71.09   
6 1 ASN A 244 ? ? -96.17  53.00   
7 1 LYS A 252 ? ? 59.99   -128.02 
# 
_phasing.method   MR 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A MET 1 ? A MET 1 
2 1 Y 1 A SER 2 ? A SER 2 
3 1 Y 1 A HIS 3 ? A HIS 3 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
BCN N1   N  N N 74  
BCN C1   C  N N 75  
BCN C2   C  N N 76  
BCN O21  O  N N 77  
BCN O22  O  N N 78  
BCN C3   C  N N 79  
BCN C4   C  N N 80  
BCN O4   O  N N 81  
BCN C5   C  N N 82  
BCN C6   C  N N 83  
BCN O6   O  N N 84  
BCN H11  H  N N 85  
BCN H12  H  N N 86  
BCN HO2  H  N N 87  
BCN H31  H  N N 88  
BCN H32  H  N N 89  
BCN H41  H  N N 90  
BCN H42  H  N N 91  
BCN HO4  H  N N 92  
BCN H51  H  N N 93  
BCN H52  H  N N 94  
BCN H61  H  N N 95  
BCN H62  H  N N 96  
BCN HO6  H  N N 97  
CYS N    N  N N 98  
CYS CA   C  N R 99  
CYS C    C  N N 100 
CYS O    O  N N 101 
CYS CB   C  N N 102 
CYS SG   S  N N 103 
CYS OXT  O  N N 104 
CYS H    H  N N 105 
CYS H2   H  N N 106 
CYS HA   H  N N 107 
CYS HB2  H  N N 108 
CYS HB3  H  N N 109 
CYS HG   H  N N 110 
CYS HXT  H  N N 111 
DMS S    S  N N 112 
DMS O    O  N N 113 
DMS C1   C  N N 114 
DMS C2   C  N N 115 
DMS H11  H  N N 116 
DMS H12  H  N N 117 
DMS H13  H  N N 118 
DMS H21  H  N N 119 
DMS H22  H  N N 120 
DMS H23  H  N N 121 
EDO C1   C  N N 122 
EDO O1   O  N N 123 
EDO C2   C  N N 124 
EDO O2   O  N N 125 
EDO H11  H  N N 126 
EDO H12  H  N N 127 
EDO HO1  H  N N 128 
EDO H21  H  N N 129 
EDO H22  H  N N 130 
EDO HO2  H  N N 131 
GLN N    N  N N 132 
GLN CA   C  N S 133 
GLN C    C  N N 134 
GLN O    O  N N 135 
GLN CB   C  N N 136 
GLN CG   C  N N 137 
GLN CD   C  N N 138 
GLN OE1  O  N N 139 
GLN NE2  N  N N 140 
GLN OXT  O  N N 141 
GLN H    H  N N 142 
GLN H2   H  N N 143 
GLN HA   H  N N 144 
GLN HB2  H  N N 145 
GLN HB3  H  N N 146 
GLN HG2  H  N N 147 
GLN HG3  H  N N 148 
GLN HE21 H  N N 149 
GLN HE22 H  N N 150 
GLN HXT  H  N N 151 
GLU N    N  N N 152 
GLU CA   C  N S 153 
GLU C    C  N N 154 
GLU O    O  N N 155 
GLU CB   C  N N 156 
GLU CG   C  N N 157 
GLU CD   C  N N 158 
GLU OE1  O  N N 159 
GLU OE2  O  N N 160 
GLU OXT  O  N N 161 
GLU H    H  N N 162 
GLU H2   H  N N 163 
GLU HA   H  N N 164 
GLU HB2  H  N N 165 
GLU HB3  H  N N 166 
GLU HG2  H  N N 167 
GLU HG3  H  N N 168 
GLU HE2  H  N N 169 
GLU HXT  H  N N 170 
GLY N    N  N N 171 
GLY CA   C  N N 172 
GLY C    C  N N 173 
GLY O    O  N N 174 
GLY OXT  O  N N 175 
GLY H    H  N N 176 
GLY H2   H  N N 177 
GLY HA2  H  N N 178 
GLY HA3  H  N N 179 
GLY HXT  H  N N 180 
HIS N    N  N N 181 
HIS CA   C  N S 182 
HIS C    C  N N 183 
HIS O    O  N N 184 
HIS CB   C  N N 185 
HIS CG   C  Y N 186 
HIS ND1  N  Y N 187 
HIS CD2  C  Y N 188 
HIS CE1  C  Y N 189 
HIS NE2  N  Y N 190 
HIS OXT  O  N N 191 
HIS H    H  N N 192 
HIS H2   H  N N 193 
HIS HA   H  N N 194 
HIS HB2  H  N N 195 
HIS HB3  H  N N 196 
HIS HD1  H  N N 197 
HIS HD2  H  N N 198 
HIS HE1  H  N N 199 
HIS HE2  H  N N 200 
HIS HXT  H  N N 201 
HOH O    O  N N 202 
HOH H1   H  N N 203 
HOH H2   H  N N 204 
ILE N    N  N N 205 
ILE CA   C  N S 206 
ILE C    C  N N 207 
ILE O    O  N N 208 
ILE CB   C  N S 209 
ILE CG1  C  N N 210 
ILE CG2  C  N N 211 
ILE CD1  C  N N 212 
ILE OXT  O  N N 213 
ILE H    H  N N 214 
ILE H2   H  N N 215 
ILE HA   H  N N 216 
ILE HB   H  N N 217 
ILE HG12 H  N N 218 
ILE HG13 H  N N 219 
ILE HG21 H  N N 220 
ILE HG22 H  N N 221 
ILE HG23 H  N N 222 
ILE HD11 H  N N 223 
ILE HD12 H  N N 224 
ILE HD13 H  N N 225 
ILE HXT  H  N N 226 
LEU N    N  N N 227 
LEU CA   C  N S 228 
LEU C    C  N N 229 
LEU O    O  N N 230 
LEU CB   C  N N 231 
LEU CG   C  N N 232 
LEU CD1  C  N N 233 
LEU CD2  C  N N 234 
LEU OXT  O  N N 235 
LEU H    H  N N 236 
LEU H2   H  N N 237 
LEU HA   H  N N 238 
LEU HB2  H  N N 239 
LEU HB3  H  N N 240 
LEU HG   H  N N 241 
LEU HD11 H  N N 242 
LEU HD12 H  N N 243 
LEU HD13 H  N N 244 
LEU HD21 H  N N 245 
LEU HD22 H  N N 246 
LEU HD23 H  N N 247 
LEU HXT  H  N N 248 
LYS N    N  N N 249 
LYS CA   C  N S 250 
LYS C    C  N N 251 
LYS O    O  N N 252 
LYS CB   C  N N 253 
LYS CG   C  N N 254 
LYS CD   C  N N 255 
LYS CE   C  N N 256 
LYS NZ   N  N N 257 
LYS OXT  O  N N 258 
LYS H    H  N N 259 
LYS H2   H  N N 260 
LYS HA   H  N N 261 
LYS HB2  H  N N 262 
LYS HB3  H  N N 263 
LYS HG2  H  N N 264 
LYS HG3  H  N N 265 
LYS HD2  H  N N 266 
LYS HD3  H  N N 267 
LYS HE2  H  N N 268 
LYS HE3  H  N N 269 
LYS HZ1  H  N N 270 
LYS HZ2  H  N N 271 
LYS HZ3  H  N N 272 
LYS HXT  H  N N 273 
MET N    N  N N 274 
MET CA   C  N S 275 
MET C    C  N N 276 
MET O    O  N N 277 
MET CB   C  N N 278 
MET CG   C  N N 279 
MET SD   S  N N 280 
MET CE   C  N N 281 
MET OXT  O  N N 282 
MET H    H  N N 283 
MET H2   H  N N 284 
MET HA   H  N N 285 
MET HB2  H  N N 286 
MET HB3  H  N N 287 
MET HG2  H  N N 288 
MET HG3  H  N N 289 
MET HE1  H  N N 290 
MET HE2  H  N N 291 
MET HE3  H  N N 292 
MET HXT  H  N N 293 
NA  NA   NA N N 294 
PHE N    N  N N 295 
PHE CA   C  N S 296 
PHE C    C  N N 297 
PHE O    O  N N 298 
PHE CB   C  N N 299 
PHE CG   C  Y N 300 
PHE CD1  C  Y N 301 
PHE CD2  C  Y N 302 
PHE CE1  C  Y N 303 
PHE CE2  C  Y N 304 
PHE CZ   C  Y N 305 
PHE OXT  O  N N 306 
PHE H    H  N N 307 
PHE H2   H  N N 308 
PHE HA   H  N N 309 
PHE HB2  H  N N 310 
PHE HB3  H  N N 311 
PHE HD1  H  N N 312 
PHE HD2  H  N N 313 
PHE HE1  H  N N 314 
PHE HE2  H  N N 315 
PHE HZ   H  N N 316 
PHE HXT  H  N N 317 
PRO N    N  N N 318 
PRO CA   C  N S 319 
PRO C    C  N N 320 
PRO O    O  N N 321 
PRO CB   C  N N 322 
PRO CG   C  N N 323 
PRO CD   C  N N 324 
PRO OXT  O  N N 325 
PRO H    H  N N 326 
PRO HA   H  N N 327 
PRO HB2  H  N N 328 
PRO HB3  H  N N 329 
PRO HG2  H  N N 330 
PRO HG3  H  N N 331 
PRO HD2  H  N N 332 
PRO HD3  H  N N 333 
PRO HXT  H  N N 334 
SER N    N  N N 335 
SER CA   C  N S 336 
SER C    C  N N 337 
SER O    O  N N 338 
SER CB   C  N N 339 
SER OG   O  N N 340 
SER OXT  O  N N 341 
SER H    H  N N 342 
SER H2   H  N N 343 
SER HA   H  N N 344 
SER HB2  H  N N 345 
SER HB3  H  N N 346 
SER HG   H  N N 347 
SER HXT  H  N N 348 
THR N    N  N N 349 
THR CA   C  N S 350 
THR C    C  N N 351 
THR O    O  N N 352 
THR CB   C  N R 353 
THR OG1  O  N N 354 
THR CG2  C  N N 355 
THR OXT  O  N N 356 
THR H    H  N N 357 
THR H2   H  N N 358 
THR HA   H  N N 359 
THR HB   H  N N 360 
THR HG1  H  N N 361 
THR HG21 H  N N 362 
THR HG22 H  N N 363 
THR HG23 H  N N 364 
THR HXT  H  N N 365 
TRP N    N  N N 366 
TRP CA   C  N S 367 
TRP C    C  N N 368 
TRP O    O  N N 369 
TRP CB   C  N N 370 
TRP CG   C  Y N 371 
TRP CD1  C  Y N 372 
TRP CD2  C  Y N 373 
TRP NE1  N  Y N 374 
TRP CE2  C  Y N 375 
TRP CE3  C  Y N 376 
TRP CZ2  C  Y N 377 
TRP CZ3  C  Y N 378 
TRP CH2  C  Y N 379 
TRP OXT  O  N N 380 
TRP H    H  N N 381 
TRP H2   H  N N 382 
TRP HA   H  N N 383 
TRP HB2  H  N N 384 
TRP HB3  H  N N 385 
TRP HD1  H  N N 386 
TRP HE1  H  N N 387 
TRP HE3  H  N N 388 
TRP HZ2  H  N N 389 
TRP HZ3  H  N N 390 
TRP HH2  H  N N 391 
TRP HXT  H  N N 392 
TYR N    N  N N 393 
TYR CA   C  N S 394 
TYR C    C  N N 395 
TYR O    O  N N 396 
TYR CB   C  N N 397 
TYR CG   C  Y N 398 
TYR CD1  C  Y N 399 
TYR CD2  C  Y N 400 
TYR CE1  C  Y N 401 
TYR CE2  C  Y N 402 
TYR CZ   C  Y N 403 
TYR OH   O  N N 404 
TYR OXT  O  N N 405 
TYR H    H  N N 406 
TYR H2   H  N N 407 
TYR HA   H  N N 408 
TYR HB2  H  N N 409 
TYR HB3  H  N N 410 
TYR HD1  H  N N 411 
TYR HD2  H  N N 412 
TYR HE1  H  N N 413 
TYR HE2  H  N N 414 
TYR HH   H  N N 415 
TYR HXT  H  N N 416 
V50 F13  F  N N 417 
V50 C4   C  Y N 418 
V50 C5   C  Y N 419 
V50 S7   S  N N 420 
V50 O9   O  N N 421 
V50 N23  N  N N 422 
V50 O8   O  N N 423 
V50 C6   C  Y N 424 
V50 F11  F  N N 425 
V50 C1   C  Y N 426 
V50 F10  F  N N 427 
V50 C3   C  Y N 428 
V50 F12  F  N N 429 
V50 C2   C  Y N 430 
V50 S14  S  N N 431 
V50 C15  C  Y N 432 
V50 N20  N  Y N 433 
V50 C19  C  Y N 434 
V50 C21  C  N N 435 
V50 C18  C  Y N 436 
V50 C17  C  Y N 437 
V50 N16  N  Y N 438 
V50 C22  C  N N 439 
V50 H1   H  N N 440 
V50 H2   H  N N 441 
V50 H3   H  N N 442 
V50 H4   H  N N 443 
V50 H5   H  N N 444 
V50 H6   H  N N 445 
V50 H7   H  N N 446 
V50 H8   H  N N 447 
V50 H9   H  N N 448 
VAL N    N  N N 449 
VAL CA   C  N S 450 
VAL C    C  N N 451 
VAL O    O  N N 452 
VAL CB   C  N N 453 
VAL CG1  C  N N 454 
VAL CG2  C  N N 455 
VAL OXT  O  N N 456 
VAL H    H  N N 457 
VAL H2   H  N N 458 
VAL HA   H  N N 459 
VAL HB   H  N N 460 
VAL HG11 H  N N 461 
VAL HG12 H  N N 462 
VAL HG13 H  N N 463 
VAL HG21 H  N N 464 
VAL HG22 H  N N 465 
VAL HG23 H  N N 466 
VAL HXT  H  N N 467 
ZN  ZN   ZN N N 468 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
BCN N1  C1   sing N N 70  
BCN N1  C3   sing N N 71  
BCN N1  C5   sing N N 72  
BCN C1  C2   sing N N 73  
BCN C1  H11  sing N N 74  
BCN C1  H12  sing N N 75  
BCN C2  O21  doub N N 76  
BCN C2  O22  sing N N 77  
BCN O22 HO2  sing N N 78  
BCN C3  C4   sing N N 79  
BCN C3  H31  sing N N 80  
BCN C3  H32  sing N N 81  
BCN C4  O4   sing N N 82  
BCN C4  H41  sing N N 83  
BCN C4  H42  sing N N 84  
BCN O4  HO4  sing N N 85  
BCN C5  C6   sing N N 86  
BCN C5  H51  sing N N 87  
BCN C5  H52  sing N N 88  
BCN C6  O6   sing N N 89  
BCN C6  H61  sing N N 90  
BCN C6  H62  sing N N 91  
BCN O6  HO6  sing N N 92  
CYS N   CA   sing N N 93  
CYS N   H    sing N N 94  
CYS N   H2   sing N N 95  
CYS CA  C    sing N N 96  
CYS CA  CB   sing N N 97  
CYS CA  HA   sing N N 98  
CYS C   O    doub N N 99  
CYS C   OXT  sing N N 100 
CYS CB  SG   sing N N 101 
CYS CB  HB2  sing N N 102 
CYS CB  HB3  sing N N 103 
CYS SG  HG   sing N N 104 
CYS OXT HXT  sing N N 105 
DMS S   O    doub N N 106 
DMS S   C1   sing N N 107 
DMS S   C2   sing N N 108 
DMS C1  H11  sing N N 109 
DMS C1  H12  sing N N 110 
DMS C1  H13  sing N N 111 
DMS C2  H21  sing N N 112 
DMS C2  H22  sing N N 113 
DMS C2  H23  sing N N 114 
EDO C1  O1   sing N N 115 
EDO C1  C2   sing N N 116 
EDO C1  H11  sing N N 117 
EDO C1  H12  sing N N 118 
EDO O1  HO1  sing N N 119 
EDO C2  O2   sing N N 120 
EDO C2  H21  sing N N 121 
EDO C2  H22  sing N N 122 
EDO O2  HO2  sing N N 123 
GLN N   CA   sing N N 124 
GLN N   H    sing N N 125 
GLN N   H2   sing N N 126 
GLN CA  C    sing N N 127 
GLN CA  CB   sing N N 128 
GLN CA  HA   sing N N 129 
GLN C   O    doub N N 130 
GLN C   OXT  sing N N 131 
GLN CB  CG   sing N N 132 
GLN CB  HB2  sing N N 133 
GLN CB  HB3  sing N N 134 
GLN CG  CD   sing N N 135 
GLN CG  HG2  sing N N 136 
GLN CG  HG3  sing N N 137 
GLN CD  OE1  doub N N 138 
GLN CD  NE2  sing N N 139 
GLN NE2 HE21 sing N N 140 
GLN NE2 HE22 sing N N 141 
GLN OXT HXT  sing N N 142 
GLU N   CA   sing N N 143 
GLU N   H    sing N N 144 
GLU N   H2   sing N N 145 
GLU CA  C    sing N N 146 
GLU CA  CB   sing N N 147 
GLU CA  HA   sing N N 148 
GLU C   O    doub N N 149 
GLU C   OXT  sing N N 150 
GLU CB  CG   sing N N 151 
GLU CB  HB2  sing N N 152 
GLU CB  HB3  sing N N 153 
GLU CG  CD   sing N N 154 
GLU CG  HG2  sing N N 155 
GLU CG  HG3  sing N N 156 
GLU CD  OE1  doub N N 157 
GLU CD  OE2  sing N N 158 
GLU OE2 HE2  sing N N 159 
GLU OXT HXT  sing N N 160 
GLY N   CA   sing N N 161 
GLY N   H    sing N N 162 
GLY N   H2   sing N N 163 
GLY CA  C    sing N N 164 
GLY CA  HA2  sing N N 165 
GLY CA  HA3  sing N N 166 
GLY C   O    doub N N 167 
GLY C   OXT  sing N N 168 
GLY OXT HXT  sing N N 169 
HIS N   CA   sing N N 170 
HIS N   H    sing N N 171 
HIS N   H2   sing N N 172 
HIS CA  C    sing N N 173 
HIS CA  CB   sing N N 174 
HIS CA  HA   sing N N 175 
HIS C   O    doub N N 176 
HIS C   OXT  sing N N 177 
HIS CB  CG   sing N N 178 
HIS CB  HB2  sing N N 179 
HIS CB  HB3  sing N N 180 
HIS CG  ND1  sing Y N 181 
HIS CG  CD2  doub Y N 182 
HIS ND1 CE1  doub Y N 183 
HIS ND1 HD1  sing N N 184 
HIS CD2 NE2  sing Y N 185 
HIS CD2 HD2  sing N N 186 
HIS CE1 NE2  sing Y N 187 
HIS CE1 HE1  sing N N 188 
HIS NE2 HE2  sing N N 189 
HIS OXT HXT  sing N N 190 
HOH O   H1   sing N N 191 
HOH O   H2   sing N N 192 
ILE N   CA   sing N N 193 
ILE N   H    sing N N 194 
ILE N   H2   sing N N 195 
ILE CA  C    sing N N 196 
ILE CA  CB   sing N N 197 
ILE CA  HA   sing N N 198 
ILE C   O    doub N N 199 
ILE C   OXT  sing N N 200 
ILE CB  CG1  sing N N 201 
ILE CB  CG2  sing N N 202 
ILE CB  HB   sing N N 203 
ILE CG1 CD1  sing N N 204 
ILE CG1 HG12 sing N N 205 
ILE CG1 HG13 sing N N 206 
ILE CG2 HG21 sing N N 207 
ILE CG2 HG22 sing N N 208 
ILE CG2 HG23 sing N N 209 
ILE CD1 HD11 sing N N 210 
ILE CD1 HD12 sing N N 211 
ILE CD1 HD13 sing N N 212 
ILE OXT HXT  sing N N 213 
LEU N   CA   sing N N 214 
LEU N   H    sing N N 215 
LEU N   H2   sing N N 216 
LEU CA  C    sing N N 217 
LEU CA  CB   sing N N 218 
LEU CA  HA   sing N N 219 
LEU C   O    doub N N 220 
LEU C   OXT  sing N N 221 
LEU CB  CG   sing N N 222 
LEU CB  HB2  sing N N 223 
LEU CB  HB3  sing N N 224 
LEU CG  CD1  sing N N 225 
LEU CG  CD2  sing N N 226 
LEU CG  HG   sing N N 227 
LEU CD1 HD11 sing N N 228 
LEU CD1 HD12 sing N N 229 
LEU CD1 HD13 sing N N 230 
LEU CD2 HD21 sing N N 231 
LEU CD2 HD22 sing N N 232 
LEU CD2 HD23 sing N N 233 
LEU OXT HXT  sing N N 234 
LYS N   CA   sing N N 235 
LYS N   H    sing N N 236 
LYS N   H2   sing N N 237 
LYS CA  C    sing N N 238 
LYS CA  CB   sing N N 239 
LYS CA  HA   sing N N 240 
LYS C   O    doub N N 241 
LYS C   OXT  sing N N 242 
LYS CB  CG   sing N N 243 
LYS CB  HB2  sing N N 244 
LYS CB  HB3  sing N N 245 
LYS CG  CD   sing N N 246 
LYS CG  HG2  sing N N 247 
LYS CG  HG3  sing N N 248 
LYS CD  CE   sing N N 249 
LYS CD  HD2  sing N N 250 
LYS CD  HD3  sing N N 251 
LYS CE  NZ   sing N N 252 
LYS CE  HE2  sing N N 253 
LYS CE  HE3  sing N N 254 
LYS NZ  HZ1  sing N N 255 
LYS NZ  HZ2  sing N N 256 
LYS NZ  HZ3  sing N N 257 
LYS OXT HXT  sing N N 258 
MET N   CA   sing N N 259 
MET N   H    sing N N 260 
MET N   H2   sing N N 261 
MET CA  C    sing N N 262 
MET CA  CB   sing N N 263 
MET CA  HA   sing N N 264 
MET C   O    doub N N 265 
MET C   OXT  sing N N 266 
MET CB  CG   sing N N 267 
MET CB  HB2  sing N N 268 
MET CB  HB3  sing N N 269 
MET CG  SD   sing N N 270 
MET CG  HG2  sing N N 271 
MET CG  HG3  sing N N 272 
MET SD  CE   sing N N 273 
MET CE  HE1  sing N N 274 
MET CE  HE2  sing N N 275 
MET CE  HE3  sing N N 276 
MET OXT HXT  sing N N 277 
PHE N   CA   sing N N 278 
PHE N   H    sing N N 279 
PHE N   H2   sing N N 280 
PHE CA  C    sing N N 281 
PHE CA  CB   sing N N 282 
PHE CA  HA   sing N N 283 
PHE C   O    doub N N 284 
PHE C   OXT  sing N N 285 
PHE CB  CG   sing N N 286 
PHE CB  HB2  sing N N 287 
PHE CB  HB3  sing N N 288 
PHE CG  CD1  doub Y N 289 
PHE CG  CD2  sing Y N 290 
PHE CD1 CE1  sing Y N 291 
PHE CD1 HD1  sing N N 292 
PHE CD2 CE2  doub Y N 293 
PHE CD2 HD2  sing N N 294 
PHE CE1 CZ   doub Y N 295 
PHE CE1 HE1  sing N N 296 
PHE CE2 CZ   sing Y N 297 
PHE CE2 HE2  sing N N 298 
PHE CZ  HZ   sing N N 299 
PHE OXT HXT  sing N N 300 
PRO N   CA   sing N N 301 
PRO N   CD   sing N N 302 
PRO N   H    sing N N 303 
PRO CA  C    sing N N 304 
PRO CA  CB   sing N N 305 
PRO CA  HA   sing N N 306 
PRO C   O    doub N N 307 
PRO C   OXT  sing N N 308 
PRO CB  CG   sing N N 309 
PRO CB  HB2  sing N N 310 
PRO CB  HB3  sing N N 311 
PRO CG  CD   sing N N 312 
PRO CG  HG2  sing N N 313 
PRO CG  HG3  sing N N 314 
PRO CD  HD2  sing N N 315 
PRO CD  HD3  sing N N 316 
PRO OXT HXT  sing N N 317 
SER N   CA   sing N N 318 
SER N   H    sing N N 319 
SER N   H2   sing N N 320 
SER CA  C    sing N N 321 
SER CA  CB   sing N N 322 
SER CA  HA   sing N N 323 
SER C   O    doub N N 324 
SER C   OXT  sing N N 325 
SER CB  OG   sing N N 326 
SER CB  HB2  sing N N 327 
SER CB  HB3  sing N N 328 
SER OG  HG   sing N N 329 
SER OXT HXT  sing N N 330 
THR N   CA   sing N N 331 
THR N   H    sing N N 332 
THR N   H2   sing N N 333 
THR CA  C    sing N N 334 
THR CA  CB   sing N N 335 
THR CA  HA   sing N N 336 
THR C   O    doub N N 337 
THR C   OXT  sing N N 338 
THR CB  OG1  sing N N 339 
THR CB  CG2  sing N N 340 
THR CB  HB   sing N N 341 
THR OG1 HG1  sing N N 342 
THR CG2 HG21 sing N N 343 
THR CG2 HG22 sing N N 344 
THR CG2 HG23 sing N N 345 
THR OXT HXT  sing N N 346 
TRP N   CA   sing N N 347 
TRP N   H    sing N N 348 
TRP N   H2   sing N N 349 
TRP CA  C    sing N N 350 
TRP CA  CB   sing N N 351 
TRP CA  HA   sing N N 352 
TRP C   O    doub N N 353 
TRP C   OXT  sing N N 354 
TRP CB  CG   sing N N 355 
TRP CB  HB2  sing N N 356 
TRP CB  HB3  sing N N 357 
TRP CG  CD1  doub Y N 358 
TRP CG  CD2  sing Y N 359 
TRP CD1 NE1  sing Y N 360 
TRP CD1 HD1  sing N N 361 
TRP CD2 CE2  doub Y N 362 
TRP CD2 CE3  sing Y N 363 
TRP NE1 CE2  sing Y N 364 
TRP NE1 HE1  sing N N 365 
TRP CE2 CZ2  sing Y N 366 
TRP CE3 CZ3  doub Y N 367 
TRP CE3 HE3  sing N N 368 
TRP CZ2 CH2  doub Y N 369 
TRP CZ2 HZ2  sing N N 370 
TRP CZ3 CH2  sing Y N 371 
TRP CZ3 HZ3  sing N N 372 
TRP CH2 HH2  sing N N 373 
TRP OXT HXT  sing N N 374 
TYR N   CA   sing N N 375 
TYR N   H    sing N N 376 
TYR N   H2   sing N N 377 
TYR CA  C    sing N N 378 
TYR CA  CB   sing N N 379 
TYR CA  HA   sing N N 380 
TYR C   O    doub N N 381 
TYR C   OXT  sing N N 382 
TYR CB  CG   sing N N 383 
TYR CB  HB2  sing N N 384 
TYR CB  HB3  sing N N 385 
TYR CG  CD1  doub Y N 386 
TYR CG  CD2  sing Y N 387 
TYR CD1 CE1  sing Y N 388 
TYR CD1 HD1  sing N N 389 
TYR CD2 CE2  doub Y N 390 
TYR CD2 HD2  sing N N 391 
TYR CE1 CZ   doub Y N 392 
TYR CE1 HE1  sing N N 393 
TYR CE2 CZ   sing Y N 394 
TYR CE2 HE2  sing N N 395 
TYR CZ  OH   sing N N 396 
TYR OH  HH   sing N N 397 
TYR OXT HXT  sing N N 398 
V50 C21 C19  sing N N 399 
V50 C19 N20  doub Y N 400 
V50 C19 C18  sing Y N 401 
V50 N20 C15  sing Y N 402 
V50 C18 C17  doub Y N 403 
V50 S14 C15  sing N N 404 
V50 S14 C2   sing N N 405 
V50 C15 N16  doub Y N 406 
V50 F10 C1   sing N N 407 
V50 C17 N16  sing Y N 408 
V50 C17 C22  sing N N 409 
V50 C1  C2   doub Y N 410 
V50 C1  C6   sing Y N 411 
V50 C2  C3   sing Y N 412 
V50 F12 C3   sing N N 413 
V50 C3  C4   doub Y N 414 
V50 C6  F11  sing N N 415 
V50 C6  C5   doub Y N 416 
V50 C4  C5   sing Y N 417 
V50 C4  F13  sing N N 418 
V50 C5  S7   sing N N 419 
V50 N23 S7   sing N N 420 
V50 O8  S7   doub N N 421 
V50 S7  O9   doub N N 422 
V50 N23 H1   sing N N 423 
V50 N23 H2   sing N N 424 
V50 C21 H3   sing N N 425 
V50 C21 H4   sing N N 426 
V50 C21 H5   sing N N 427 
V50 C18 H6   sing N N 428 
V50 C22 H7   sing N N 429 
V50 C22 H8   sing N N 430 
V50 C22 H9   sing N N 431 
VAL N   CA   sing N N 432 
VAL N   H    sing N N 433 
VAL N   H2   sing N N 434 
VAL CA  C    sing N N 435 
VAL CA  CB   sing N N 436 
VAL CA  HA   sing N N 437 
VAL C   O    doub N N 438 
VAL C   OXT  sing N N 439 
VAL CB  CG1  sing N N 440 
VAL CB  CG2  sing N N 441 
VAL CB  HB   sing N N 442 
VAL CG1 HG11 sing N N 443 
VAL CG1 HG12 sing N N 444 
VAL CG1 HG13 sing N N 445 
VAL CG2 HG21 sing N N 446 
VAL CG2 HG22 sing N N 447 
VAL CG2 HG23 sing N N 448 
VAL OXT HXT  sing N N 449 
# 
_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                    6QL1 
_atom_sites.fract_transf_matrix[1][1]   0.023641 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.006031 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.024154 
_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]   0.014486 
_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 4   ? 30.801  1.533   7.094   1.00 35.26 ? 4   HIS A N   1 
ATOM   2    C  CA  . HIS A 1 4   ? 30.994  1.786   8.570   1.00 34.06 ? 4   HIS A CA  1 
ATOM   3    C  C   . HIS A 1 4   ? 30.211  0.755   9.380   1.00 27.05 ? 4   HIS A C   1 
ATOM   4    O  O   . HIS A 1 4   ? 30.255  -0.430  9.059   1.00 27.19 ? 4   HIS A O   1 
ATOM   5    C  CB  . HIS A 1 4   ? 30.684  3.234   8.964   1.00 39.20 ? 4   HIS A CB  1 
ATOM   6    C  CG  . HIS A 1 4   ? 29.728  3.912   8.057   1.00 43.98 ? 4   HIS A CG  1 
ATOM   7    N  ND1 . HIS A 1 4   ? 29.225  5.166   8.343   1.00 54.72 ? 4   HIS A ND1 1 
ATOM   8    C  CD2 . HIS A 1 4   ? 29.182  3.529   6.881   1.00 52.90 ? 4   HIS A CD2 1 
ATOM   9    C  CE1 . HIS A 1 4   ? 28.419  5.544   7.368   1.00 62.01 ? 4   HIS A CE1 1 
ATOM   10   N  NE2 . HIS A 1 4   ? 28.381  4.553   6.451   1.00 61.57 ? 4   HIS A NE2 1 
ATOM   11   N  N   . TRP A 1 5   ? 29.467  1.225   10.387  1.00 20.72 ? 5   TRP A N   1 
ATOM   12   C  CA  . TRP A 1 5   ? 28.789  0.311   11.286  1.00 16.68 ? 5   TRP A CA  1 
ATOM   13   C  C   . TRP A 1 5   ? 27.768  -0.485  10.474  1.00 15.60 ? 5   TRP A C   1 
ATOM   14   O  O   . TRP A 1 5   ? 27.174  -0.018  9.494   1.00 17.35 ? 5   TRP A O   1 
ATOM   15   C  CB  . TRP A 1 5   ? 28.152  1.063   12.468  1.00 15.90 ? 5   TRP A CB  1 
ATOM   16   C  CG  . TRP A 1 5   ? 26.966  1.886   12.105  1.00 14.02 ? 5   TRP A CG  1 
ATOM   17   C  CD1 . TRP A 1 5   ? 26.929  3.216   11.766  1.00 16.18 ? 5   TRP A CD1 1 
ATOM   18   C  CD2 . TRP A 1 5   ? 25.615  1.415   12.020  1.00 13.56 ? 5   TRP A CD2 1 
ATOM   19   N  NE1 . TRP A 1 5   ? 25.651  3.592   11.478  1.00 15.90 ? 5   TRP A NE1 1 
ATOM   20   C  CE2 . TRP A 1 5   ? 24.816  2.516   11.646  1.00 15.68 ? 5   TRP A CE2 1 
ATOM   21   C  CE3 . TRP A 1 5   ? 25.016  0.177   12.309  1.00 12.97 ? 5   TRP A CE3 1 
ATOM   22   C  CZ2 . TRP A 1 5   ? 23.439  2.401   11.519  1.00 15.58 ? 5   TRP A CZ2 1 
ATOM   23   C  CZ3 . TRP A 1 5   ? 23.636  0.066   12.149  1.00 14.11 ? 5   TRP A CZ3 1 
ATOM   24   C  CH2 . TRP A 1 5   ? 22.865  1.178   11.794  1.00 14.95 ? 5   TRP A CH2 1 
ATOM   25   N  N   . GLY A 1 6   ? 27.519  -1.691  10.983  1.00 13.68 ? 6   GLY A N   1 
ATOM   26   C  CA  . GLY A 1 6   ? 26.465  -2.506  10.414  1.00 13.77 ? 6   GLY A CA  1 
ATOM   27   C  C   . GLY A 1 6   ? 26.165  -3.675  11.337  1.00 13.75 ? 6   GLY A C   1 
ATOM   28   O  O   . GLY A 1 6   ? 26.202  -3.528  12.568  1.00 14.31 ? 6   GLY A O   1 
ATOM   29   N  N   . TYR A 1 7   ? 25.869  -4.819  10.747  1.00 14.04 ? 7   TYR A N   1 
ATOM   30   C  CA  . TYR A 1 7   ? 25.481  -5.961  11.546  1.00 15.49 ? 7   TYR A CA  1 
ATOM   31   C  C   . TYR A 1 7   ? 26.316  -7.190  11.274  1.00 21.21 ? 7   TYR A C   1 
ATOM   32   O  O   . TYR A 1 7   ? 26.004  -8.250  11.815  1.00 26.79 ? 7   TYR A O   1 
ATOM   33   C  CB  . TYR A 1 7   ? 24.003  -6.284  11.312  1.00 13.92 ? 7   TYR A CB  1 
ATOM   34   C  CG  . TYR A 1 7   ? 23.075  -5.211  11.847  1.00 12.06 ? 7   TYR A CG  1 
ATOM   35   C  CD1 . TYR A 1 7   ? 22.674  -5.255  13.187  1.00 11.33 ? 7   TYR A CD1 1 
ATOM   36   C  CD2 . TYR A 1 7   ? 22.583  -4.189  11.034  1.00 11.65 ? 7   TYR A CD2 1 
ATOM   37   C  CE1 . TYR A 1 7   ? 21.884  -4.255  13.710  1.00 11.22 ? 7   TYR A CE1 1 
ATOM   38   C  CE2 . TYR A 1 7   ? 21.769  -3.194  11.545  1.00 10.86 ? 7   TYR A CE2 1 
ATOM   39   C  CZ  . TYR A 1 7   ? 21.397  -3.278  12.885  1.00 11.02 ? 7   TYR A CZ  1 
ATOM   40   O  OH  . TYR A 1 7   ? 20.555  -2.318  13.327  1.00 12.55 ? 7   TYR A OH  1 
ATOM   41   N  N   . GLY A 1 8   ? 27.406  -7.030  10.514  1.00 18.79 ? 8   GLY A N   1 
ATOM   42   C  CA  . GLY A 1 8   ? 28.281  -8.158  10.195  1.00 22.69 ? 8   GLY A CA  1 
ATOM   43   C  C   . GLY A 1 8   ? 29.257  -8.479  11.329  1.00 22.47 ? 8   GLY A C   1 
ATOM   44   O  O   . GLY A 1 8   ? 29.374  -7.764  12.340  1.00 24.38 ? 8   GLY A O   1 
ATOM   45   N  N   . LYS A 1 9   ? 30.090  -9.502  11.104  1.00 28.12 ? 9   LYS A N   1 
ATOM   46   C  CA  . LYS A 1 9   ? 31.090  -9.897  12.088  1.00 27.49 ? 9   LYS A CA  1 
ATOM   47   C  C   . LYS A 1 9   ? 32.109  -8.777  12.302  1.00 26.00 ? 9   LYS A C   1 
ATOM   48   O  O   . LYS A 1 9   ? 32.652  -8.630  13.397  1.00 25.40 ? 9   LYS A O   1 
ATOM   49   C  CB  . LYS A 1 9   ? 31.801  -11.181 11.637  1.00 30.51 ? 9   LYS A CB  1 
ATOM   50   C  CG  . LYS A 1 9   ? 32.865  -11.728 12.583  1.00 34.22 ? 9   LYS A CG  1 
ATOM   51   N  N   . HIS A 1 10  ? 32.339  -7.976  11.248  1.00 20.31 ? 10  HIS A N   1 
ATOM   52   C  CA  . HIS A 1 10  ? 33.415  -7.010  11.364  1.00 19.96 ? 10  HIS A CA  1 
ATOM   53   C  C   . HIS A 1 10  ? 32.954  -5.627  11.817  1.00 19.92 ? 10  HIS A C   1 
ATOM   54   O  O   . HIS A 1 10  ? 33.770  -4.823  12.256  1.00 19.90 ? 10  HIS A O   1 
ATOM   55   C  CB  . HIS A 1 10  ? 34.263  -6.999  10.076  1.00 18.34 ? 10  HIS A CB  1 
ATOM   56   C  CG  . HIS A 1 10  ? 34.704  -8.361  9.644   1.00 21.15 ? 10  HIS A CG  1 
ATOM   57   N  ND1 . HIS A 1 10  ? 35.670  -9.056  10.348  1.00 22.55 ? 10  HIS A ND1 1 
ATOM   58   C  CD2 . HIS A 1 10  ? 34.283  -9.168  8.638   1.00 24.70 ? 10  HIS A CD2 1 
ATOM   59   C  CE1 . HIS A 1 10  ? 35.851  -10.255 9.803   1.00 22.98 ? 10  HIS A CE1 1 
ATOM   60   N  NE2 . HIS A 1 10  ? 35.001  -10.348 8.737   1.00 23.98 ? 10  HIS A NE2 1 
ATOM   61   N  N   . ASN A 1 11  ? 31.639  -5.328  11.750  1.00 17.74 ? 11  ASN A N   1 
ATOM   62   C  CA  . ASN A 1 11  ? 31.199  -3.978  12.036  1.00 16.16 ? 11  ASN A CA  1 
ATOM   63   C  C   . ASN A 1 11  ? 29.886  -4.016  12.833  1.00 13.98 ? 11  ASN A C   1 
ATOM   64   O  O   . ASN A 1 11  ? 29.229  -2.976  12.900  1.00 14.19 ? 11  ASN A O   1 
ATOM   65   C  CB  . ASN A 1 11  ? 30.945  -3.173  10.756  1.00 16.82 ? 11  ASN A CB  1 
ATOM   66   C  CG  . ASN A 1 11  ? 29.912  -3.794  9.850   1.00 17.20 ? 11  ASN A CG  1 
ATOM   67   O  OD1 . ASN A 1 11  ? 29.428  -4.883  10.134  1.00 16.75 ? 11  ASN A OD1 1 
ATOM   68   N  ND2 . ASN A 1 11  ? 29.558  -3.104  8.776   1.00 20.43 ? 11  ASN A ND2 1 
ATOM   69   N  N   . GLY A 1 12  ? 29.617  -5.175  13.465  1.00 14.51 ? 12  GLY A N   1 
ATOM   70   C  CA  . GLY A 1 12  ? 28.338  -5.401  14.123  1.00 14.12 ? 12  GLY A CA  1 
ATOM   71   C  C   . GLY A 1 12  ? 28.295  -4.792  15.513  1.00 13.91 ? 12  GLY A C   1 
ATOM   72   O  O   . GLY A 1 12  ? 29.182  -4.075  15.970  1.00 13.19 ? 12  GLY A O   1 
ATOM   73   N  N   . PRO A 1 13  ? 27.216  -5.139  16.253  1.00 12.77 ? 13  PRO A N   1 
ATOM   74   C  CA  . PRO A 1 13  ? 27.011  -4.540  17.568  1.00 13.08 ? 13  PRO A CA  1 
ATOM   75   C  C   . PRO A 1 13  ? 28.159  -4.561  18.574  1.00 12.91 ? 13  PRO A C   1 
ATOM   76   O  O   . PRO A 1 13  ? 28.298  -3.598  19.315  1.00 12.72 ? 13  PRO A O   1 
ATOM   77   C  CB  . PRO A 1 13  ? 25.811  -5.337  18.101  1.00 14.46 ? 13  PRO A CB  1 
ATOM   78   C  CG  . PRO A 1 13  ? 25.026  -5.654  16.875  1.00 13.22 ? 13  PRO A CG  1 
ATOM   79   C  CD  . PRO A 1 13  ? 26.060  -5.926  15.780  1.00 12.03 ? 13  PRO A CD  1 
ATOM   80   N  N   . GLU A 1 14  ? 29.016  -5.588  18.552  1.00 14.96 ? 14  GLU A N   1 
ATOM   81   C  CA  . GLU A 1 14  ? 30.083  -5.576  19.542  1.00 15.38 ? 14  GLU A CA  1 
ATOM   82   C  C   . GLU A 1 14  ? 31.221  -4.635  19.142  1.00 15.13 ? 14  GLU A C   1 
ATOM   83   O  O   . GLU A 1 14  ? 32.119  -4.420  19.944  1.00 15.22 ? 14  GLU A O   1 
ATOM   84   C  CB  . GLU A 1 14  ? 30.652  -6.972  19.801  1.00 22.22 ? 14  GLU A CB  1 
ATOM   85   C  CG  . GLU A 1 14  ? 29.615  -8.065  20.061  1.00 29.87 ? 14  GLU A CG  1 
ATOM   86   C  CD  . GLU A 1 14  ? 28.697  -7.937  21.287  1.00 42.25 ? 14  GLU A CD  1 
ATOM   87   O  OE1 . GLU A 1 14  ? 29.219  -7.980  22.434  1.00 45.28 ? 14  GLU A OE1 1 
ATOM   88   O  OE2 . GLU A 1 14  ? 27.429  -7.810  21.102  1.00 43.82 ? 14  GLU A OE2 1 
ATOM   89   N  N   . HIS A 1 15  ? 31.159  -4.060  17.937  1.00 14.17 ? 15  HIS A N   1 
ATOM   90   C  CA  . HIS A 1 15  ? 32.170  -3.107  17.508  1.00 13.82 ? 15  HIS A CA  1 
ATOM   91   C  C   . HIS A 1 15  ? 31.740  -1.653  17.718  1.00 13.85 ? 15  HIS A C   1 
ATOM   92   O  O   . HIS A 1 15  ? 32.538  -0.728  17.636  1.00 14.47 ? 15  HIS A O   1 
ATOM   93   C  CB  . HIS A 1 15  ? 32.484  -3.286  16.022  1.00 13.79 ? 15  HIS A CB  1 
ATOM   94   C  CG  . HIS A 1 15  ? 33.172  -4.584  15.749  1.00 16.22 ? 15  HIS A CG  1 
ATOM   95   N  ND1 . HIS A 1 15  ? 34.551  -4.675  15.864  1.00 22.03 ? 15  HIS A ND1 1 
ATOM   96   C  CD2 . HIS A 1 15  ? 32.687  -5.785  15.359  1.00 17.45 ? 15  HIS A CD2 1 
ATOM   97   C  CE1 . HIS A 1 15  ? 34.882  -5.935  15.589  1.00 21.54 ? 15  HIS A CE1 1 
ATOM   98   N  NE2 . HIS A 1 15  ? 33.788  -6.641  15.313  1.00 22.72 ? 15  HIS A NE2 1 
ATOM   99   N  N   . TRP A 1 16  ? 30.422  -1.435  17.891  1.00 11.94 ? 16  TRP A N   1 
ATOM   100  C  CA  . TRP A 1 16  ? 29.927  -0.067  17.795  1.00 11.27 ? 16  TRP A CA  1 
ATOM   101  C  C   . TRP A 1 16  ? 30.528  0.881   18.828  1.00 11.35 ? 16  TRP A C   1 
ATOM   102  O  O   . TRP A 1 16  ? 30.669  2.089   18.571  1.00 11.93 ? 16  TRP A O   1 
ATOM   103  C  CB  . TRP A 1 16  ? 28.391  -0.049  17.893  1.00 10.79 ? 16  TRP A CB  1 
ATOM   104  C  CG  . TRP A 1 16  ? 27.716  -0.799  16.800  1.00 11.35 ? 16  TRP A CG  1 
ATOM   105  C  CD1 . TRP A 1 16  ? 28.193  -1.211  15.597  1.00 11.16 ? 16  TRP A CD1 1 
ATOM   106  C  CD2 . TRP A 1 16  ? 26.325  -1.130  16.791  1.00 9.91  ? 16  TRP A CD2 1 
ATOM   107  N  NE1 . TRP A 1 16  ? 27.219  -1.801  14.860  1.00 11.48 ? 16  TRP A NE1 1 
ATOM   108  C  CE2 . TRP A 1 16  ? 26.049  -1.772  15.586  1.00 11.06 ? 16  TRP A CE2 1 
ATOM   109  C  CE3 . TRP A 1 16  ? 25.291  -0.914  17.719  1.00 9.84  ? 16  TRP A CE3 1 
ATOM   110  C  CZ2 . TRP A 1 16  ? 24.777  -2.205  15.232  1.00 10.55 ? 16  TRP A CZ2 1 
ATOM   111  C  CZ3 . TRP A 1 16  ? 24.042  -1.381  17.393  1.00 9.75  ? 16  TRP A CZ3 1 
ATOM   112  C  CH2 . TRP A 1 16  ? 23.786  -1.998  16.150  1.00 10.47 ? 16  TRP A CH2 1 
ATOM   113  N  N   . HIS A 1 17  ? 30.889  0.356   19.995  1.00 11.25 ? 17  HIS A N   1 
ATOM   114  C  CA  . HIS A 1 17  ? 31.347  1.218   21.064  1.00 12.39 ? 17  HIS A CA  1 
ATOM   115  C  C   . HIS A 1 17  ? 32.613  2.008   20.660  1.00 12.82 ? 17  HIS A C   1 
ATOM   116  O  O   . HIS A 1 17  ? 32.871  3.056   21.246  1.00 13.79 ? 17  HIS A O   1 
ATOM   117  C  CB  . HIS A 1 17  ? 31.625  0.413   22.349  1.00 13.00 ? 17  HIS A CB  1 
ATOM   118  C  CG  . HIS A 1 17  ? 32.832  -0.472  22.223  1.00 14.29 ? 17  HIS A CG  1 
ATOM   119  N  ND1 . HIS A 1 17  ? 34.056  -0.101  22.726  1.00 17.99 ? 17  HIS A ND1 1 
ATOM   120  C  CD2 . HIS A 1 17  ? 32.994  -1.630  21.565  1.00 13.60 ? 17  HIS A CD2 1 
ATOM   121  C  CE1 . HIS A 1 17  ? 34.923  -1.061  22.410  1.00 14.97 ? 17  HIS A CE1 1 
ATOM   122  N  NE2 . HIS A 1 17  ? 34.329  -2.007  21.693  1.00 15.89 ? 17  HIS A NE2 1 
ATOM   123  N  N   . LYS A 1 18  ? 33.357  1.485   19.675  1.00 15.10 ? 18  LYS A N   1 
ATOM   124  C  CA  . LYS A 1 18  ? 34.603  2.155   19.334  1.00 16.70 ? 18  LYS A CA  1 
ATOM   125  C  C   . LYS A 1 18  ? 34.296  3.486   18.655  1.00 17.98 ? 18  LYS A C   1 
ATOM   126  O  O   . LYS A 1 18  ? 35.072  4.431   18.787  1.00 22.87 ? 18  LYS A O   1 
ATOM   127  C  CB  . LYS A 1 18  ? 35.515  1.278   18.474  1.00 18.05 ? 18  LYS A CB  1 
ATOM   128  C  CG  . LYS A 1 18  ? 36.030  0.004   19.143  1.00 17.75 ? 18  LYS A CG  1 
ATOM   129  C  CD  . LYS A 1 18  ? 36.718  -0.910  18.173  1.00 17.32 ? 18  LYS A CD  1 
ATOM   130  C  CE  . LYS A 1 18  ? 35.781  -1.863  17.463  1.00 17.06 ? 18  LYS A CE  1 
ATOM   131  N  NZ  . LYS A 1 18  ? 36.410  -2.552  16.309  1.00 19.17 ? 18  LYS A NZ  1 
ATOM   132  N  N   . ASP A 1 19  ? 33.190  3.610   17.907  1.00 15.94 ? 19  ASP A N   1 
ATOM   133  C  CA  . ASP A 1 19  ? 32.829  4.905   17.332  1.00 16.07 ? 19  ASP A CA  1 
ATOM   134  C  C   . ASP A 1 19  ? 31.786  5.625   18.166  1.00 17.69 ? 19  ASP A C   1 
ATOM   135  O  O   . ASP A 1 19  ? 31.658  6.833   18.105  1.00 18.52 ? 19  ASP A O   1 
ATOM   136  C  CB  . ASP A 1 19  ? 32.466  4.777   15.856  1.00 17.40 ? 19  ASP A CB  1 
ATOM   137  C  CG  . ASP A 1 19  ? 33.705  4.443   15.030  1.00 22.17 ? 19  ASP A CG  1 
ATOM   138  O  OD1 . ASP A 1 19  ? 34.425  5.411   14.711  1.00 25.79 ? 19  ASP A OD1 1 
ATOM   139  O  OD2 . ASP A 1 19  ? 33.990  3.216   14.807  1.00 24.04 ? 19  ASP A OD2 1 
ATOM   140  N  N   . PHE A 1 20  ? 31.052  4.871   18.978  1.00 13.75 ? 20  PHE A N   1 
ATOM   141  C  CA  . PHE A 1 20  ? 29.926  5.423   19.686  1.00 15.45 ? 20  PHE A CA  1 
ATOM   142  C  C   . PHE A 1 20  ? 30.002  4.932   21.119  1.00 14.07 ? 20  PHE A C   1 
ATOM   143  O  O   . PHE A 1 20  ? 29.392  3.926   21.498  1.00 13.84 ? 20  PHE A O   1 
ATOM   144  C  CB  . PHE A 1 20  ? 28.638  4.940   19.005  1.00 13.14 ? 20  PHE A CB  1 
ATOM   145  C  CG  . PHE A 1 20  ? 28.583  5.245   17.537  1.00 11.74 ? 20  PHE A CG  1 
ATOM   146  C  CD1 . PHE A 1 20  ? 28.233  6.523   17.113  1.00 14.59 ? 20  PHE A CD1 1 
ATOM   147  C  CD2 . PHE A 1 20  ? 28.944  4.306   16.588  1.00 14.71 ? 20  PHE A CD2 1 
ATOM   148  C  CE1 . PHE A 1 20  ? 28.202  6.838   15.756  1.00 12.67 ? 20  PHE A CE1 1 
ATOM   149  C  CE2 . PHE A 1 20  ? 28.913  4.614   15.230  1.00 13.15 ? 20  PHE A CE2 1 
ATOM   150  C  CZ  . PHE A 1 20  ? 28.567  5.892   14.822  1.00 13.03 ? 20  PHE A CZ  1 
ATOM   151  N  N   . PRO A 1 21  ? 30.849  5.560   21.970  1.00 15.07 ? 21  PRO A N   1 
ATOM   152  C  CA  . PRO A 1 21  ? 31.074  5.048   23.317  1.00 14.47 ? 21  PRO A CA  1 
ATOM   153  C  C   . PRO A 1 21  ? 29.852  4.858   24.229  1.00 13.91 ? 21  PRO A C   1 
ATOM   154  O  O   . PRO A 1 21  ? 29.913  4.078   25.157  1.00 14.21 ? 21  PRO A O   1 
ATOM   155  C  CB  . PRO A 1 21  ? 32.120  6.013   23.928  1.00 16.63 ? 21  PRO A CB  1 
ATOM   156  C  CG  . PRO A 1 21  ? 32.153  7.160   22.974  1.00 18.10 ? 21  PRO A CG  1 
ATOM   157  C  CD  . PRO A 1 21  ? 31.758  6.671   21.599  1.00 16.08 ? 21  PRO A CD  1 
ATOM   158  N  N   . ILE A 1 22  ? 28.789  5.624   23.934  1.00 12.87 ? 22  ILE A N   1 
ATOM   159  C  CA  . ILE A 1 22  ? 27.562  5.508   24.728  1.00 12.06 ? 22  ILE A CA  1 
ATOM   160  C  C   . ILE A 1 22  ? 26.951  4.125   24.512  1.00 11.59 ? 22  ILE A C   1 
ATOM   161  O  O   . ILE A 1 22  ? 26.120  3.751   25.319  1.00 12.28 ? 22  ILE A O   1 
ATOM   162  C  CB  . ILE A 1 22  ? 26.583  6.608   24.278  1.00 12.87 ? 22  ILE A CB  1 
ATOM   163  C  CG1 . ILE A 1 22  ? 25.511  6.894   25.342  1.00 15.02 ? 22  ILE A CG1 1 
ATOM   164  C  CG2 . ILE A 1 22  ? 25.970  6.260   22.911  1.00 12.62 ? 22  ILE A CG2 1 
ATOM   165  C  CD1 . ILE A 1 22  ? 26.047  7.410   26.659  1.00 17.79 ? 22  ILE A CD1 1 
ATOM   166  N  N   . ALA A 1 23  ? 27.504  3.324   23.581  1.00 11.68 ? 23  ALA A N   1 
ATOM   167  C  CA  . ALA A 1 23  ? 27.107  1.927   23.476  1.00 12.18 ? 23  ALA A CA  1 
ATOM   168  C  C   . ALA A 1 23  ? 27.187  1.188   24.803  1.00 11.67 ? 23  ALA A C   1 
ATOM   169  O  O   . ALA A 1 23  ? 26.453  0.214   24.988  1.00 11.75 ? 23  ALA A O   1 
ATOM   170  C  CB  . ALA A 1 23  ? 27.955  1.208   22.426  1.00 11.05 ? 23  ALA A CB  1 
ATOM   171  N  N   . LYS A 1 24  ? 28.087  1.631   25.716  1.00 13.41 ? 24  LYS A N   1 
ATOM   172  C  CA  . LYS A 1 24  ? 28.283  0.996   27.009  1.00 14.24 ? 24  LYS A CA  1 
ATOM   173  C  C   . LYS A 1 24  ? 27.649  1.849   28.100  1.00 15.39 ? 24  LYS A C   1 
ATOM   174  O  O   . LYS A 1 24  ? 28.051  1.763   29.266  1.00 16.09 ? 24  LYS A O   1 
ATOM   175  C  CB  . LYS A 1 24  ? 29.782  0.843   27.307  1.00 15.60 ? 24  LYS A CB  1 
ATOM   176  C  CG  . LYS A 1 24  ? 30.445  -0.156  26.371  1.00 20.90 ? 24  LYS A CG  1 
ATOM   177  C  CD  . LYS A 1 24  ? 31.906  -0.318  26.731  1.00 21.03 ? 24  LYS A CD  1 
ATOM   178  C  CE  . LYS A 1 24  ? 32.651  -1.179  25.734  1.00 26.77 ? 24  LYS A CE  1 
ATOM   179  N  NZ  . LYS A 1 24  ? 32.318  -2.608  25.928  1.00 29.59 ? 24  LYS A NZ  1 
ATOM   180  N  N   . GLY A 1 25  ? 26.642  2.658   27.726  1.00 14.53 ? 25  GLY A N   1 
ATOM   181  C  CA  . GLY A 1 25  ? 26.017  3.575   28.672  1.00 14.99 ? 25  GLY A CA  1 
ATOM   182  C  C   . GLY A 1 25  ? 25.022  2.907   29.628  1.00 13.61 ? 25  GLY A C   1 
ATOM   183  O  O   . GLY A 1 25  ? 24.880  1.691   29.669  1.00 14.35 ? 25  GLY A O   1 
ATOM   184  N  N   . GLU A 1 26  ? 24.329  3.756   30.403  1.00 13.40 ? 26  GLU A N   1 
ATOM   185  C  CA  . GLU A 1 26  ? 23.476  3.269   31.478  1.00 13.67 ? 26  GLU A CA  1 
ATOM   186  C  C   . GLU A 1 26  ? 22.021  3.080   31.064  1.00 12.03 ? 26  GLU A C   1 
ATOM   187  O  O   . GLU A 1 26  ? 21.216  2.560   31.845  1.00 13.44 ? 26  GLU A O   1 
ATOM   188  C  CB  . GLU A 1 26  ? 23.467  4.272   32.643  1.00 17.88 ? 26  GLU A CB  1 
ATOM   189  C  CG  . GLU A 1 26  ? 24.861  4.606   33.213  1.00 22.41 ? 26  GLU A CG  1 
ATOM   190  C  CD  . GLU A 1 26  ? 25.571  3.393   33.790  1.00 25.06 ? 26  GLU A CD  1 
ATOM   191  O  OE1 . GLU A 1 26  ? 24.972  2.626   34.596  1.00 30.43 ? 26  GLU A OE1 1 
ATOM   192  O  OE2 . GLU A 1 26  ? 26.728  3.199   33.426  1.00 31.36 ? 26  GLU A OE2 1 
ATOM   193  N  N   A ARG A 1 27  ? 21.653  3.591   29.876  0.50 11.53 ? 27  ARG A N   1 
ATOM   194  N  N   B ARG A 1 27  ? 21.710  3.468   29.828  0.50 11.21 ? 27  ARG A N   1 
ATOM   195  C  CA  A ARG A 1 27  ? 20.264  3.437   29.429  0.50 10.12 ? 27  ARG A CA  1 
ATOM   196  C  CA  B ARG A 1 27  ? 20.285  3.424   29.424  0.50 9.93  ? 27  ARG A CA  1 
ATOM   197  C  C   A ARG A 1 27  ? 20.261  2.967   27.966  0.50 9.81  ? 27  ARG A C   1 
ATOM   198  C  C   B ARG A 1 27  ? 20.207  2.919   27.987  0.50 9.65  ? 27  ARG A C   1 
ATOM   199  O  O   A ARG A 1 27  ? 19.398  3.461   27.213  0.50 9.99  ? 27  ARG A O   1 
ATOM   200  O  O   B ARG A 1 27  ? 19.487  3.481   27.168  0.50 9.82  ? 27  ARG A O   1 
ATOM   201  C  CB  A ARG A 1 27  ? 19.384  4.658   29.761  0.50 11.31 ? 27  ARG A CB  1 
ATOM   202  C  CB  B ARG A 1 27  ? 19.705  4.833   29.546  0.50 10.80 ? 27  ARG A CB  1 
ATOM   203  C  CG  A ARG A 1 27  ? 19.721  5.943   29.013  0.50 11.97 ? 27  ARG A CG  1 
ATOM   204  C  CG  B ARG A 1 27  ? 20.184  5.649   30.738  0.50 11.36 ? 27  ARG A CG  1 
ATOM   205  C  CD  A ARG A 1 27  ? 18.908  7.251   29.085  0.50 13.00 ? 27  ARG A CD  1 
ATOM   206  C  CD  B ARG A 1 27  ? 19.502  6.998   30.602  0.50 12.28 ? 27  ARG A CD  1 
ATOM   207  N  NE  A ARG A 1 27  ? 17.579  7.109   28.511  0.50 12.72 ? 27  ARG A NE  1 
ATOM   208  N  NE  B ARG A 1 27  ? 19.742  7.859   31.752  0.50 14.14 ? 27  ARG A NE  1 
ATOM   209  C  CZ  A ARG A 1 27  ? 16.761  8.121   28.246  0.50 9.06  ? 27  ARG A CZ  1 
ATOM   210  C  CZ  B ARG A 1 27  ? 20.781  8.675   31.876  0.50 14.45 ? 27  ARG A CZ  1 
ATOM   211  N  NH1 A ARG A 1 27  ? 17.137  9.362   28.506  0.50 5.94  ? 27  ARG A NH1 1 
ATOM   212  N  NH1 B ARG A 1 27  ? 21.687  8.745   30.916  0.50 16.05 ? 27  ARG A NH1 1 
ATOM   213  N  NH2 A ARG A 1 27  ? 15.570  7.890   27.724  0.50 9.90  ? 27  ARG A NH2 1 
ATOM   214  N  NH2 B ARG A 1 27  ? 20.912  9.419   32.960  0.50 17.72 ? 27  ARG A NH2 1 
ATOM   215  N  N   . GLN A 1 28  ? 20.930  1.835   27.686  1.00 9.29  ? 28  GLN A N   1 
ATOM   216  C  CA  . GLN A 1 28  ? 20.956  1.336   26.318  1.00 8.79  ? 28  GLN A CA  1 
ATOM   217  C  C   . GLN A 1 28  ? 19.797  0.388   26.044  1.00 8.17  ? 28  GLN A C   1 
ATOM   218  O  O   . GLN A 1 28  ? 19.286  -0.314  26.910  1.00 9.29  ? 28  GLN A O   1 
ATOM   219  C  CB  . GLN A 1 28  ? 22.288  0.626   26.059  1.00 8.75  ? 28  GLN A CB  1 
ATOM   220  C  CG  . GLN A 1 28  ? 23.446  1.632   26.033  1.00 10.55 ? 28  GLN A CG  1 
ATOM   221  C  CD  . GLN A 1 28  ? 23.351  2.467   24.775  1.00 9.49  ? 28  GLN A CD  1 
ATOM   222  O  OE1 . GLN A 1 28  ? 23.554  1.987   23.653  1.00 10.13 ? 28  GLN A OE1 1 
ATOM   223  N  NE2 . GLN A 1 28  ? 23.010  3.742   24.879  1.00 9.47  ? 28  GLN A NE2 1 
ATOM   224  N  N   . SER A 1 29  ? 19.417  0.364   24.789  1.00 8.60  ? 29  SER A N   1 
ATOM   225  C  CA  . SER A 1 29  ? 18.342  -0.510  24.296  1.00 7.34  ? 29  SER A CA  1 
ATOM   226  C  C   . SER A 1 29  ? 18.841  -1.385  23.163  1.00 7.77  ? 29  SER A C   1 
ATOM   227  O  O   . SER A 1 29  ? 19.820  -1.064  22.463  1.00 7.61  ? 29  SER A O   1 
ATOM   228  C  CB  . SER A 1 29  ? 17.211  0.326   23.744  1.00 8.20  ? 29  SER A CB  1 
ATOM   229  O  OG  . SER A 1 29  ? 16.596  1.077   24.819  1.00 7.92  ? 29  SER A OG  1 
ATOM   230  N  N   . PRO A 1 30  ? 18.210  -2.522  22.854  1.00 7.54  ? 30  PRO A N   1 
ATOM   231  C  CA  . PRO A 1 30  ? 17.032  -3.050  23.564  1.00 7.03  ? 30  PRO A CA  1 
ATOM   232  C  C   . PRO A 1 30  ? 17.440  -3.716  24.862  1.00 6.69  ? 30  PRO A C   1 
ATOM   233  O  O   . PRO A 1 30  ? 18.613  -3.758  25.222  1.00 7.59  ? 30  PRO A O   1 
ATOM   234  C  CB  . PRO A 1 30  ? 16.477  -4.091  22.573  1.00 6.87  ? 30  PRO A CB  1 
ATOM   235  C  CG  . PRO A 1 30  ? 17.782  -4.648  21.980  1.00 7.13  ? 30  PRO A CG  1 
ATOM   236  C  CD  . PRO A 1 30  ? 18.673  -3.437  21.805  1.00 7.99  ? 30  PRO A CD  1 
ATOM   237  N  N   . VAL A 1 31  ? 16.438  -4.235  25.533  1.00 7.04  ? 31  VAL A N   1 
ATOM   238  C  CA  . VAL A 1 31  ? 16.615  -5.002  26.746  1.00 7.71  ? 31  VAL A CA  1 
ATOM   239  C  C   . VAL A 1 31  ? 15.723  -6.237  26.705  1.00 7.92  ? 31  VAL A C   1 
ATOM   240  O  O   . VAL A 1 31  ? 14.755  -6.316  25.949  1.00 8.16  ? 31  VAL A O   1 
ATOM   241  C  CB  . VAL A 1 31  ? 16.313  -4.193  28.032  1.00 8.98  ? 31  VAL A CB  1 
ATOM   242  C  CG1 . VAL A 1 31  ? 17.246  -2.983  28.123  1.00 9.75  ? 31  VAL A CG1 1 
ATOM   243  C  CG2 . VAL A 1 31  ? 14.846  -3.753  28.067  1.00 8.73  ? 31  VAL A CG2 1 
ATOM   244  N  N   . ASP A 1 32  ? 16.067  -7.206  27.561  1.00 8.21  ? 32  ASP A N   1 
ATOM   245  C  CA  . ASP A 1 32  ? 15.123  -8.255  27.863  1.00 9.14  ? 32  ASP A CA  1 
ATOM   246  C  C   . ASP A 1 32  ? 14.062  -7.718  28.817  1.00 9.01  ? 32  ASP A C   1 
ATOM   247  O  O   . ASP A 1 32  ? 14.399  -7.104  29.832  1.00 10.80 ? 32  ASP A O   1 
ATOM   248  C  CB  . ASP A 1 32  ? 15.855  -9.468  28.459  1.00 9.63  ? 32  ASP A CB  1 
ATOM   249  C  CG  . ASP A 1 32  ? 14.901  -10.607 28.742  1.00 11.45 ? 32  ASP A CG  1 
ATOM   250  O  OD1 . ASP A 1 32  ? 14.196  -11.098 27.841  1.00 10.86 ? 32  ASP A OD1 1 
ATOM   251  O  OD2 . ASP A 1 32  ? 14.888  -11.051 29.950  1.00 14.14 ? 32  ASP A OD2 1 
ATOM   252  N  N   . ILE A 1 33  ? 12.807  -8.012  28.498  1.00 9.19  ? 33  ILE A N   1 
ATOM   253  C  CA  . ILE A 1 33  ? 11.690  -7.682  29.385  1.00 10.45 ? 33  ILE A CA  1 
ATOM   254  C  C   . ILE A 1 33  ? 11.384  -8.910  30.228  1.00 11.32 ? 33  ILE A C   1 
ATOM   255  O  O   . ILE A 1 33  ? 10.816  -9.889  29.756  1.00 10.54 ? 33  ILE A O   1 
ATOM   256  C  CB  . ILE A 1 33  ? 10.494  -7.230  28.560  1.00 10.04 ? 33  ILE A CB  1 
ATOM   257  C  CG1 . ILE A 1 33  ? 10.837  -6.003  27.708  1.00 10.71 ? 33  ILE A CG1 1 
ATOM   258  C  CG2 . ILE A 1 33  ? 9.300   -6.951  29.467  1.00 11.06 ? 33  ILE A CG2 1 
ATOM   259  C  CD1 . ILE A 1 33  ? 9.873   -5.798  26.585  1.00 11.74 ? 33  ILE A CD1 1 
ATOM   260  N  N   . ASP A 1 34  ? 11.826  -8.849  31.483  1.00 11.82 ? 34  ASP A N   1 
ATOM   261  C  CA  . ASP A 1 34  ? 11.499  -9.882  32.471  1.00 12.48 ? 34  ASP A CA  1 
ATOM   262  C  C   . ASP A 1 34  ? 10.087  -9.571  32.991  1.00 12.69 ? 34  ASP A C   1 
ATOM   263  O  O   . ASP A 1 34  ? 9.882   -8.590  33.753  1.00 13.09 ? 34  ASP A O   1 
ATOM   264  C  CB  . ASP A 1 34  ? 12.579  -9.878  33.552  1.00 13.60 ? 34  ASP A CB  1 
ATOM   265  C  CG  . ASP A 1 34  ? 12.386  -10.909 34.644  1.00 17.56 ? 34  ASP A CG  1 
ATOM   266  O  OD1 . ASP A 1 34  ? 11.263  -11.349 34.833  1.00 17.84 ? 34  ASP A OD1 1 
ATOM   267  O  OD2 . ASP A 1 34  ? 13.393  -11.180 35.376  1.00 26.82 ? 34  ASP A OD2 1 
ATOM   268  N  N   . THR A 1 35  ? 9.119   -10.333 32.523  1.00 13.26 ? 35  THR A N   1 
ATOM   269  C  CA  . THR A 1 35  ? 7.727   -10.102 32.849  1.00 15.25 ? 35  THR A CA  1 
ATOM   270  C  C   . THR A 1 35  ? 7.417   -10.285 34.322  1.00 16.79 ? 35  THR A C   1 
ATOM   271  O  O   . THR A 1 35  ? 6.441   -9.689  34.772  1.00 18.48 ? 35  THR A O   1 
ATOM   272  C  CB  . THR A 1 35  ? 6.800   -10.970 31.996  1.00 18.69 ? 35  THR A CB  1 
ATOM   273  O  OG1 . THR A 1 35  ? 6.958   -12.312 32.462  1.00 17.07 ? 35  THR A OG1 1 
ATOM   274  C  CG2 . THR A 1 35  ? 7.091   -10.888 30.514  1.00 18.75 ? 35  THR A CG2 1 
ATOM   275  N  N   . HIS A 1 36  ? 8.249   -11.028 35.051  1.00 15.67 ? 36  HIS A N   1 
ATOM   276  C  CA  . HIS A 1 36  ? 8.005   -11.226 36.462  1.00 17.65 ? 36  HIS A CA  1 
ATOM   277  C  C   . HIS A 1 36  ? 8.419   -9.991  37.247  1.00 21.40 ? 36  HIS A C   1 
ATOM   278  O  O   . HIS A 1 36  ? 7.735   -9.658  38.221  1.00 29.18 ? 36  HIS A O   1 
ATOM   279  C  CB  . HIS A 1 36  ? 8.706   -12.539 36.842  1.00 18.92 ? 36  HIS A CB  1 
ATOM   280  C  CG  . HIS A 1 36  ? 8.194   -13.598 35.926  1.00 19.05 ? 36  HIS A CG  1 
ATOM   281  N  ND1 . HIS A 1 36  ? 8.964   -14.201 34.926  1.00 22.23 ? 36  HIS A ND1 1 
ATOM   282  C  CD2 . HIS A 1 36  ? 6.967   -14.150 35.827  1.00 17.86 ? 36  HIS A CD2 1 
ATOM   283  C  CE1 . HIS A 1 36  ? 8.239   -15.130 34.335  1.00 18.40 ? 36  HIS A CE1 1 
ATOM   284  N  NE2 . HIS A 1 36  ? 7.010   -15.103 34.841  1.00 21.16 ? 36  HIS A NE2 1 
ATOM   285  N  N   . THR A 1 37  ? 9.516   -9.336  36.845  1.00 17.04 ? 37  THR A N   1 
ATOM   286  C  CA  . THR A 1 37  ? 10.105  -8.200  37.524  1.00 16.15 ? 37  THR A CA  1 
ATOM   287  C  C   . THR A 1 37  ? 9.456   -6.876  37.089  1.00 16.86 ? 37  THR A C   1 
ATOM   288  O  O   . THR A 1 37  ? 9.558   -5.862  37.800  1.00 20.47 ? 37  THR A O   1 
ATOM   289  C  CB  . THR A 1 37  ? 11.618  -8.150  37.285  1.00 20.47 ? 37  THR A CB  1 
ATOM   290  O  OG1 . THR A 1 37  ? 12.186  -9.313  37.904  1.00 24.34 ? 37  THR A OG1 1 
ATOM   291  C  CG2 . THR A 1 37  ? 12.246  -6.878  37.811  1.00 23.07 ? 37  THR A CG2 1 
ATOM   292  N  N   . ALA A 1 38  ? 8.772   -6.863  35.942  1.00 16.23 ? 38  ALA A N   1 
ATOM   293  C  CA  . ALA A 1 38  ? 8.117   -5.618  35.533  1.00 17.68 ? 38  ALA A CA  1 
ATOM   294  C  C   . ALA A 1 38  ? 6.982   -5.322  36.523  1.00 19.45 ? 38  ALA A C   1 
ATOM   295  O  O   . ALA A 1 38  ? 6.328   -6.232  37.021  1.00 23.76 ? 38  ALA A O   1 
ATOM   296  C  CB  . ALA A 1 38  ? 7.641   -5.711  34.101  1.00 15.01 ? 38  ALA A CB  1 
ATOM   297  N  N   . LYS A 1 39  ? 6.804   -4.053  36.856  1.00 19.47 ? 39  LYS A N   1 
ATOM   298  C  CA  . LYS A 1 39  ? 5.805   -3.690  37.853  1.00 18.52 ? 39  LYS A CA  1 
ATOM   299  C  C   . LYS A 1 39  ? 4.604   -3.055  37.146  1.00 15.83 ? 39  LYS A C   1 
ATOM   300  O  O   . LYS A 1 39  ? 4.761   -2.075  36.412  1.00 13.25 ? 39  LYS A O   1 
ATOM   301  C  CB  . LYS A 1 39  ? 6.495   -2.652  38.738  1.00 25.06 ? 39  LYS A CB  1 
ATOM   302  C  CG  . LYS A 1 39  ? 5.656   -1.961  39.814  1.00 29.30 ? 39  LYS A CG  1 
ATOM   303  C  CD  . LYS A 1 39  ? 5.730   -2.630  41.161  1.00 27.13 ? 39  LYS A CD  1 
ATOM   304  C  CE  . LYS A 1 39  ? 4.521   -2.491  42.075  1.00 29.79 ? 39  LYS A CE  1 
ATOM   305  N  NZ  . LYS A 1 39  ? 4.839   -1.676  43.260  1.00 33.33 ? 39  LYS A NZ  1 
ATOM   306  N  N   . TYR A 1 40  ? 3.393   -3.516  37.471  1.00 16.30 ? 40  TYR A N   1 
ATOM   307  C  CA  . TYR A 1 40  ? 2.193   -2.830  37.073  1.00 18.46 ? 40  TYR A CA  1 
ATOM   308  C  C   . TYR A 1 40  ? 2.209   -1.446  37.697  1.00 16.40 ? 40  TYR A C   1 
ATOM   309  O  O   . TYR A 1 40  ? 2.464   -1.270  38.912  1.00 16.66 ? 40  TYR A O   1 
ATOM   310  C  CB  . TYR A 1 40  ? 0.936   -3.646  37.414  1.00 18.78 ? 40  TYR A CB  1 
ATOM   311  C  CG  . TYR A 1 40  ? -0.321  -2.839  37.290  1.00 24.52 ? 40  TYR A CG  1 
ATOM   312  C  CD1 . TYR A 1 40  ? -0.750  -2.328  36.075  1.00 23.65 ? 40  TYR A CD1 1 
ATOM   313  C  CD2 . TYR A 1 40  ? -1.146  -2.636  38.397  1.00 29.66 ? 40  TYR A CD2 1 
ATOM   314  C  CE1 . TYR A 1 40  ? -1.893  -1.559  35.970  1.00 30.42 ? 40  TYR A CE1 1 
ATOM   315  C  CE2 . TYR A 1 40  ? -2.307  -1.884  38.302  1.00 30.72 ? 40  TYR A CE2 1 
ATOM   316  C  CZ  . TYR A 1 40  ? -2.691  -1.355  37.085  1.00 31.81 ? 40  TYR A CZ  1 
ATOM   317  O  OH  . TYR A 1 40  ? -3.821  -0.595  36.984  1.00 36.92 ? 40  TYR A OH  1 
ATOM   318  N  N   . ASP A 1 41  ? 1.998   -0.448  36.848  1.00 16.24 ? 41  ASP A N   1 
ATOM   319  C  CA  . ASP A 1 41  ? 1.992   0.913   37.340  1.00 17.82 ? 41  ASP A CA  1 
ATOM   320  C  C   . ASP A 1 41  ? 0.581   1.428   37.125  1.00 24.83 ? 41  ASP A C   1 
ATOM   321  O  O   . ASP A 1 41  ? 0.231   1.779   36.008  1.00 21.75 ? 41  ASP A O   1 
ATOM   322  C  CB  . ASP A 1 41  ? 2.989   1.786   36.587  1.00 20.98 ? 41  ASP A CB  1 
ATOM   323  C  CG  . ASP A 1 41  ? 3.125   3.159   37.223  1.00 24.07 ? 41  ASP A CG  1 
ATOM   324  O  OD1 . ASP A 1 41  ? 2.205   3.551   37.955  1.00 24.26 ? 41  ASP A OD1 1 
ATOM   325  O  OD2 . ASP A 1 41  ? 4.164   3.806   36.962  1.00 28.13 ? 41  ASP A OD2 1 
ATOM   326  N  N   . PRO A 1 42  ? -0.276  1.440   38.168  1.00 26.25 ? 42  PRO A N   1 
ATOM   327  C  CA  . PRO A 1 42  ? -1.676  1.817   37.998  1.00 29.15 ? 42  PRO A CA  1 
ATOM   328  C  C   . PRO A 1 42  ? -1.790  3.297   37.664  1.00 26.31 ? 42  PRO A C   1 
ATOM   329  O  O   . PRO A 1 42  ? -2.867  3.733   37.260  1.00 30.68 ? 42  PRO A O   1 
ATOM   330  C  CB  . PRO A 1 42  ? -2.267  1.508   39.380  1.00 28.75 ? 42  PRO A CB  1 
ATOM   331  C  CG  . PRO A 1 42  ? -1.088  1.724   40.325  1.00 28.81 ? 42  PRO A CG  1 
ATOM   332  C  CD  . PRO A 1 42  ? 0.091   1.125   39.562  1.00 24.18 ? 42  PRO A CD  1 
ATOM   333  N  N   . SER A 1 43  ? -0.691  4.056   37.793  1.00 26.62 ? 43  SER A N   1 
ATOM   334  C  CA  . SER A 1 43  ? -0.706  5.466   37.423  1.00 29.82 ? 43  SER A CA  1 
ATOM   335  C  C   . SER A 1 43  ? -0.421  5.736   35.933  1.00 28.72 ? 43  SER A C   1 
ATOM   336  O  O   . SER A 1 43  ? -0.481  6.891   35.505  1.00 30.67 ? 43  SER A O   1 
ATOM   337  C  CB  . SER A 1 43  ? 0.197   6.282   38.300  1.00 33.12 ? 43  SER A CB  1 
ATOM   338  O  OG  . SER A 1 43  ? 1.551   6.105   37.931  1.00 33.90 ? 43  SER A OG  1 
ATOM   339  N  N   . LEU A 1 44  ? -0.061  4.714   35.134  1.00 28.77 ? 44  LEU A N   1 
ATOM   340  C  CA  . LEU A 1 44  ? 0.127   4.924   33.700  1.00 26.06 ? 44  LEU A CA  1 
ATOM   341  C  C   . LEU A 1 44  ? -1.250  5.126   33.070  1.00 30.68 ? 44  LEU A C   1 
ATOM   342  O  O   . LEU A 1 44  ? -2.179  4.437   33.469  1.00 29.84 ? 44  LEU A O   1 
ATOM   343  C  CB  . LEU A 1 44  ? 0.753   3.672   33.082  1.00 22.53 ? 44  LEU A CB  1 
ATOM   344  C  CG  . LEU A 1 44  ? 2.252   3.457   33.272  1.00 19.53 ? 44  LEU A CG  1 
ATOM   345  C  CD1 . LEU A 1 44  ? 2.629   2.058   32.823  1.00 21.55 ? 44  LEU A CD1 1 
ATOM   346  C  CD2 . LEU A 1 44  ? 3.082   4.486   32.506  1.00 18.99 ? 44  LEU A CD2 1 
ATOM   347  N  N   . LYS A 1 45  ? -1.347  5.995   32.054  1.00 32.70 ? 45  LYS A N   1 
ATOM   348  C  CA  . LYS A 1 45  ? -2.575  6.174   31.274  1.00 30.97 ? 45  LYS A CA  1 
ATOM   349  C  C   . LYS A 1 45  ? -2.606  5.225   30.082  1.00 29.72 ? 45  LYS A C   1 
ATOM   350  O  O   . LYS A 1 45  ? -1.573  4.729   29.659  1.00 30.73 ? 45  LYS A O   1 
ATOM   351  C  CB  . LYS A 1 45  ? -2.633  7.568   30.675  1.00 32.53 ? 45  LYS A CB  1 
ATOM   352  C  CG  . LYS A 1 45  ? -1.966  8.659   31.486  1.00 36.61 ? 45  LYS A CG  1 
ATOM   353  C  CD  . LYS A 1 45  ? -2.858  9.385   32.440  1.00 43.58 ? 45  LYS A CD  1 
ATOM   354  C  CE  . LYS A 1 45  ? -2.141  10.594  32.993  1.00 42.45 ? 45  LYS A CE  1 
ATOM   355  N  NZ  . LYS A 1 45  ? -1.267  11.207  31.963  1.00 47.56 ? 45  LYS A NZ  1 
ATOM   356  N  N   . PRO A 1 46  ? -3.787  4.944   29.467  1.00 27.79 ? 46  PRO A N   1 
ATOM   357  C  CA  . PRO A 1 46  ? -3.838  4.145   28.242  1.00 24.98 ? 46  PRO A CA  1 
ATOM   358  C  C   . PRO A 1 46  ? -3.071  5.004   27.252  1.00 19.57 ? 46  PRO A C   1 
ATOM   359  O  O   . PRO A 1 46  ? -3.048  6.217   27.362  1.00 23.23 ? 46  PRO A O   1 
ATOM   360  C  CB  . PRO A 1 46  ? -5.339  4.082   27.855  1.00 26.40 ? 46  PRO A CB  1 
ATOM   361  C  CG  . PRO A 1 46  ? -5.952  5.272   28.611  1.00 31.18 ? 46  PRO A CG  1 
ATOM   362  C  CD  . PRO A 1 46  ? -5.115  5.438   29.866  1.00 31.16 ? 46  PRO A CD  1 
ATOM   363  N  N   . LEU A 1 47  ? -2.403  4.311   26.363  1.00 25.61 ? 47  LEU A N   1 
ATOM   364  C  CA  . LEU A 1 47  ? -1.792  4.975   25.260  1.00 22.41 ? 47  LEU A CA  1 
ATOM   365  C  C   . LEU A 1 47  ? -2.902  5.618   24.432  1.00 21.40 ? 47  LEU A C   1 
ATOM   366  O  O   . LEU A 1 47  ? -4.011  5.095   24.366  1.00 19.86 ? 47  LEU A O   1 
ATOM   367  C  CB  . LEU A 1 47  ? -1.170  3.820   24.506  1.00 26.57 ? 47  LEU A CB  1 
ATOM   368  C  CG  . LEU A 1 47  ? 0.120   4.112   23.805  1.00 28.22 ? 47  LEU A CG  1 
ATOM   369  C  CD1 . LEU A 1 47  ? 1.001   4.944   24.720  1.00 24.97 ? 47  LEU A CD1 1 
ATOM   370  C  CD2 . LEU A 1 47  ? 0.755   2.784   23.394  1.00 25.96 ? 47  LEU A CD2 1 
ATOM   371  N  N   . SER A 1 48  ? -2.579  6.723   23.791  1.00 16.68 ? 48  SER A N   1 
ATOM   372  C  CA  . SER A 1 48  ? -3.387  7.317   22.748  1.00 16.00 ? 48  SER A CA  1 
ATOM   373  C  C   . SER A 1 48  ? -2.578  7.273   21.457  1.00 15.13 ? 48  SER A C   1 
ATOM   374  O  O   . SER A 1 48  ? -1.563  7.943   21.297  1.00 15.55 ? 48  SER A O   1 
ATOM   375  C  CB  . SER A 1 48  ? -3.758  8.712   23.139  1.00 15.66 ? 48  SER A CB  1 
ATOM   376  O  OG  . SER A 1 48  ? -4.423  9.337   22.071  1.00 18.93 ? 48  SER A OG  1 
ATOM   377  N  N   . VAL A 1 49  ? -2.955  6.387   20.591  1.00 15.23 ? 49  VAL A N   1 
ATOM   378  C  CA  . VAL A 1 49  ? -2.360  6.259   19.280  1.00 15.96 ? 49  VAL A CA  1 
ATOM   379  C  C   . VAL A 1 49  ? -3.359  6.862   18.318  1.00 18.48 ? 49  VAL A C   1 
ATOM   380  O  O   . VAL A 1 49  ? -4.433  6.274   18.120  1.00 21.23 ? 49  VAL A O   1 
ATOM   381  C  CB  . VAL A 1 49  ? -2.067  4.779   18.999  1.00 17.54 ? 49  VAL A CB  1 
ATOM   382  C  CG1 . VAL A 1 49  ? -1.390  4.579   17.646  1.00 22.90 ? 49  VAL A CG1 1 
ATOM   383  C  CG2 . VAL A 1 49  ? -1.325  4.097   20.137  1.00 19.04 ? 49  VAL A CG2 1 
ATOM   384  N  N   . SER A 1 50  ? -3.053  8.012   17.708  1.00 16.51 ? 50  SER A N   1 
ATOM   385  C  CA  . SER A 1 50  ? -3.999  8.721   16.843  1.00 17.68 ? 50  SER A CA  1 
ATOM   386  C  C   . SER A 1 50  ? -3.403  8.811   15.452  1.00 16.68 ? 50  SER A C   1 
ATOM   387  O  O   . SER A 1 50  ? -2.695  9.771   15.173  1.00 17.26 ? 50  SER A O   1 
ATOM   388  C  CB  . SER A 1 50  ? -4.286  10.112  17.330  1.00 21.79 ? 50  SER A CB  1 
ATOM   389  O  OG  . SER A 1 50  ? -5.014  10.070  18.537  1.00 25.73 ? 50  SER A OG  1 
ATOM   390  N  N   . TYR A 1 51  ? -3.649  7.815   14.616  1.00 15.41 ? 51  TYR A N   1 
ATOM   391  C  CA  . TYR A 1 51  ? -3.066  7.710   13.295  1.00 16.85 ? 51  TYR A CA  1 
ATOM   392  C  C   . TYR A 1 51  ? -4.073  7.945   12.165  1.00 19.06 ? 51  TYR A C   1 
ATOM   393  O  O   . TYR A 1 51  ? -3.739  7.661   11.013  1.00 20.27 ? 51  TYR A O   1 
ATOM   394  C  CB  . TYR A 1 51  ? -2.429  6.330   13.117  1.00 15.30 ? 51  TYR A CB  1 
ATOM   395  C  CG  . TYR A 1 51  ? -1.149  6.061   13.898  1.00 14.15 ? 51  TYR A CG  1 
ATOM   396  C  CD1 . TYR A 1 51  ? -0.453  7.059   14.596  1.00 14.21 ? 51  TYR A CD1 1 
ATOM   397  C  CD2 . TYR A 1 51  ? -0.662  4.767   13.987  1.00 13.36 ? 51  TYR A CD2 1 
ATOM   398  C  CE1 . TYR A 1 51  ? 0.742   6.768   15.268  1.00 13.06 ? 51  TYR A CE1 1 
ATOM   399  C  CE2 . TYR A 1 51  ? 0.502   4.453   14.660  1.00 13.76 ? 51  TYR A CE2 1 
ATOM   400  C  CZ  . TYR A 1 51  ? 1.215   5.460   15.311  1.00 12.48 ? 51  TYR A CZ  1 
ATOM   401  O  OH  . TYR A 1 51  ? 2.347   5.056   15.947  1.00 12.81 ? 51  TYR A OH  1 
ATOM   402  N  N   A ASP A 1 52  ? -5.268  8.451   12.514  0.50 21.04 ? 52  ASP A N   1 
ATOM   403  N  N   B ASP A 1 52  ? -5.291  8.428   12.491  0.50 21.06 ? 52  ASP A N   1 
ATOM   404  C  CA  A ASP A 1 52  ? -6.321  8.671   11.528  0.50 22.41 ? 52  ASP A CA  1 
ATOM   405  C  CA  B ASP A 1 52  ? -6.322  8.656   11.475  0.50 22.22 ? 52  ASP A CA  1 
ATOM   406  C  C   A ASP A 1 52  ? -5.866  9.571   10.378  0.50 22.70 ? 52  ASP A C   1 
ATOM   407  C  C   B ASP A 1 52  ? -5.815  9.544   10.341  0.50 22.56 ? 52  ASP A C   1 
ATOM   408  O  O   A ASP A 1 52  ? -6.227  9.332   9.226   0.50 23.81 ? 52  ASP A O   1 
ATOM   409  O  O   B ASP A 1 52  ? -6.099  9.277   9.171   0.50 23.29 ? 52  ASP A O   1 
ATOM   410  C  CB  A ASP A 1 52  ? -7.637  9.111   12.189  0.50 23.82 ? 52  ASP A CB  1 
ATOM   411  C  CB  B ASP A 1 52  ? -7.630  9.213   12.068  0.50 23.78 ? 52  ASP A CB  1 
ATOM   412  C  CG  A ASP A 1 52  ? -7.495  10.136  13.302  0.50 25.48 ? 52  ASP A CG  1 
ATOM   413  C  CG  B ASP A 1 52  ? -8.768  9.371   11.060  0.50 26.23 ? 52  ASP A CG  1 
ATOM   414  O  OD1 A ASP A 1 52  ? -6.805  9.843   14.311  0.50 26.23 ? 52  ASP A OD1 1 
ATOM   415  O  OD1 B ASP A 1 52  ? -9.160  8.358   10.431  0.50 25.91 ? 52  ASP A OD1 1 
ATOM   416  O  OD2 A ASP A 1 52  ? -8.106  11.210  13.174  0.50 31.93 ? 52  ASP A OD2 1 
ATOM   417  O  OD2 B ASP A 1 52  ? -9.259  10.518  10.902  0.50 30.59 ? 52  ASP A OD2 1 
ATOM   418  N  N   . GLN A 1 53  ? -5.068  10.598  10.683  1.00 22.34 ? 53  GLN A N   1 
ATOM   419  C  CA  . GLN A 1 53  ? -4.655  11.531  9.643   1.00 23.68 ? 53  GLN A CA  1 
ATOM   420  C  C   . GLN A 1 53  ? -3.220  11.299  9.163   1.00 21.40 ? 53  GLN A C   1 
ATOM   421  O  O   . GLN A 1 53  ? -2.629  12.205  8.564   1.00 21.37 ? 53  GLN A O   1 
ATOM   422  C  CB  . GLN A 1 53  ? -4.861  12.962  10.133  1.00 29.09 ? 53  GLN A CB  1 
ATOM   423  C  CG  . GLN A 1 53  ? -6.320  13.260  10.466  1.00 33.92 ? 53  GLN A CG  1 
ATOM   424  C  CD  . GLN A 1 53  ? -7.032  13.653  9.197   1.00 42.33 ? 53  GLN A CD  1 
ATOM   425  O  OE1 . GLN A 1 53  ? -6.874  14.770  8.692   1.00 50.39 ? 53  GLN A OE1 1 
ATOM   426  N  NE2 . GLN A 1 53  ? -7.790  12.712  8.651   1.00 37.42 ? 53  GLN A NE2 1 
ATOM   427  N  N   . ALA A 1 54  ? -2.619  10.146  9.488   1.00 19.08 ? 54  ALA A N   1 
ATOM   428  C  CA  . ALA A 1 54  ? -1.270  9.881   8.991   1.00 16.17 ? 54  ALA A CA  1 
ATOM   429  C  C   . ALA A 1 54  ? -1.167  10.060  7.478   1.00 19.19 ? 54  ALA A C   1 
ATOM   430  O  O   . ALA A 1 54  ? -2.056  9.638   6.727   1.00 23.39 ? 54  ALA A O   1 
ATOM   431  C  CB  . ALA A 1 54  ? -0.758  8.510   9.423   1.00 17.98 ? 54  ALA A CB  1 
ATOM   432  N  N   . THR A 1 55  ? -0.071  10.695  7.039   1.00 14.37 ? 55  THR A N   1 
ATOM   433  C  CA  . THR A 1 55  ? 0.239   10.882  5.630   1.00 15.67 ? 55  THR A CA  1 
ATOM   434  C  C   . THR A 1 55  ? 1.592   10.248  5.351   1.00 12.46 ? 55  THR A C   1 
ATOM   435  O  O   . THR A 1 55  ? 2.607   10.862  5.628   1.00 12.48 ? 55  THR A O   1 
ATOM   436  C  CB  . THR A 1 55  ? 0.412   12.373  5.298   1.00 19.98 ? 55  THR A CB  1 
ATOM   437  O  OG1 . THR A 1 55  ? -0.814  13.038  5.539   1.00 27.90 ? 55  THR A OG1 1 
ATOM   438  C  CG2 . THR A 1 55  ? 0.776   12.588  3.843   1.00 21.73 ? 55  THR A CG2 1 
ATOM   439  N  N   . SER A 1 56  ? 1.597   9.050   4.793   1.00 12.25 ? 56  SER A N   1 
ATOM   440  C  CA  . SER A 1 56  ? 2.846   8.417   4.391   1.00 12.19 ? 56  SER A CA  1 
ATOM   441  C  C   . SER A 1 56  ? 3.355   9.083   3.124   1.00 13.10 ? 56  SER A C   1 
ATOM   442  O  O   . SER A 1 56  ? 2.539   9.567   2.282   1.00 14.45 ? 56  SER A O   1 
ATOM   443  C  CB  . SER A 1 56  ? 2.772   6.916   4.214   1.00 13.43 ? 56  SER A CB  1 
ATOM   444  O  OG  . SER A 1 56  ? 1.848   6.578   3.152   1.00 13.55 ? 56  SER A OG  1 
ATOM   445  N  N   . LEU A 1 57  ? 4.671   9.070   2.946   1.00 13.06 ? 57  LEU A N   1 
ATOM   446  C  CA  . LEU A 1 57  ? 5.230   9.709   1.758   1.00 13.34 ? 57  LEU A CA  1 
ATOM   447  C  C   . LEU A 1 57  ? 6.072   8.772   0.914   1.00 14.23 ? 57  LEU A C   1 
ATOM   448  O  O   . LEU A 1 57  ? 5.993   8.765   -0.309  1.00 13.85 ? 57  LEU A O   1 
ATOM   449  C  CB  . LEU A 1 57  ? 6.085   10.887  2.210   1.00 16.12 ? 57  LEU A CB  1 
ATOM   450  C  CG  . LEU A 1 57  ? 5.292   12.054  2.789   1.00 17.76 ? 57  LEU A CG  1 
ATOM   451  C  CD1 . LEU A 1 57  ? 6.285   13.108  3.253   1.00 18.15 ? 57  LEU A CD1 1 
ATOM   452  C  CD2 . LEU A 1 57  ? 4.329   12.680  1.763   1.00 23.15 ? 57  LEU A CD2 1 
ATOM   453  N  N   . ARG A 1 58  ? 6.913   7.956   1.567   1.00 12.61 ? 58  ARG A N   1 
ATOM   454  C  CA  . ARG A 1 58  ? 8.016   7.347   0.860   1.00 12.46 ? 58  ARG A CA  1 
ATOM   455  C  C   . ARG A 1 58  ? 8.455   6.112   1.641   1.00 12.17 ? 58  ARG A C   1 
ATOM   456  O  O   . ARG A 1 58  ? 8.308   6.117   2.866   1.00 11.80 ? 58  ARG A O   1 
ATOM   457  C  CB  . ARG A 1 58  ? 9.186   8.350   0.800   1.00 14.63 ? 58  ARG A CB  1 
ATOM   458  C  CG  . ARG A 1 58  ? 10.255  7.979   -0.197  1.00 18.04 ? 58  ARG A CG  1 
ATOM   459  C  CD  . ARG A 1 58  ? 11.171  9.174   -0.220  1.00 18.79 ? 58  ARG A CD  1 
ATOM   460  N  NE  . ARG A 1 58  ? 12.029  9.180   0.952   1.00 17.37 ? 58  ARG A NE  1 
ATOM   461  C  CZ  . ARG A 1 58  ? 13.348  9.349   0.922   1.00 15.06 ? 58  ARG A CZ  1 
ATOM   462  N  NH1 . ARG A 1 58  ? 13.978  9.603   -0.211  1.00 16.48 ? 58  ARG A NH1 1 
ATOM   463  N  NH2 . ARG A 1 58  ? 14.045  9.348   2.048   1.00 16.25 ? 58  ARG A NH2 1 
ATOM   464  N  N   . ILE A 1 59  ? 9.038   5.159   0.955   1.00 11.30 ? 59  ILE A N   1 
ATOM   465  C  CA  . ILE A 1 59  ? 9.723   4.032   1.571   1.00 10.82 ? 59  ILE A CA  1 
ATOM   466  C  C   . ILE A 1 59  ? 11.176  4.042   1.109   1.00 10.78 ? 59  ILE A C   1 
ATOM   467  O  O   . ILE A 1 59  ? 11.470  4.273   -0.068  1.00 11.63 ? 59  ILE A O   1 
ATOM   468  C  CB  . ILE A 1 59  ? 8.960   2.731   1.323   1.00 10.27 ? 59  ILE A CB  1 
ATOM   469  C  CG1 . ILE A 1 59  ? 9.452   1.603   2.229   1.00 11.73 ? 59  ILE A CG1 1 
ATOM   470  C  CG2 . ILE A 1 59  ? 8.994   2.385   -0.172  1.00 11.28 ? 59  ILE A CG2 1 
ATOM   471  C  CD1 . ILE A 1 59  ? 8.571   0.334   2.118   1.00 11.60 ? 59  ILE A CD1 1 
ATOM   472  N  N   . LEU A 1 60  ? 12.139  3.740   1.994   1.00 12.25 ? 60  LEU A N   1 
ATOM   473  C  CA  . LEU A 1 60  ? 13.556  3.909   1.748   1.00 11.69 ? 60  LEU A CA  1 
ATOM   474  C  C   . LEU A 1 60  ? 14.290  2.684   2.299   1.00 11.64 ? 60  LEU A C   1 
ATOM   475  O  O   . LEU A 1 60  ? 14.058  2.326   3.468   1.00 11.33 ? 60  LEU A O   1 
ATOM   476  C  CB  . LEU A 1 60  ? 14.039  5.163   2.522   1.00 11.99 ? 60  LEU A CB  1 
ATOM   477  C  CG  . LEU A 1 60  ? 15.546  5.374   2.553   1.00 12.74 ? 60  LEU A CG  1 
ATOM   478  C  CD1 . LEU A 1 60  ? 16.129  5.649   1.155   1.00 13.79 ? 60  LEU A CD1 1 
ATOM   479  C  CD2 . LEU A 1 60  ? 15.931  6.485   3.538   1.00 12.87 ? 60  LEU A CD2 1 
ATOM   480  N  N   . ASN A 1 61  ? 15.202  2.124   1.522   1.00 9.71  ? 61  ASN A N   1 
ATOM   481  C  CA  . ASN A 1 61  ? 16.198  1.196   2.032   1.00 9.57  ? 61  ASN A CA  1 
ATOM   482  C  C   . ASN A 1 61  ? 17.407  2.014   2.462   1.00 10.75 ? 61  ASN A C   1 
ATOM   483  O  O   . ASN A 1 61  ? 18.048  2.625   1.597   1.00 12.35 ? 61  ASN A O   1 
ATOM   484  C  CB  . ASN A 1 61  ? 16.595  0.172   0.968   1.00 9.81  ? 61  ASN A CB  1 
ATOM   485  C  CG  . ASN A 1 61  ? 17.677  -0.788  1.406   1.00 10.27 ? 61  ASN A CG  1 
ATOM   486  O  OD1 . ASN A 1 61  ? 18.486  -0.483  2.293   1.00 11.88 ? 61  ASN A OD1 1 
ATOM   487  N  ND2 . ASN A 1 61  ? 17.703  -1.952  0.765   1.00 12.08 ? 61  ASN A ND2 1 
ATOM   488  N  N   . ASN A 1 62  ? 17.680  2.095   3.766   1.00 10.29 ? 62  ASN A N   1 
ATOM   489  C  CA  . ASN A 1 62  ? 18.724  3.003   4.233   1.00 12.06 ? 62  ASN A CA  1 
ATOM   490  C  C   . ASN A 1 62  ? 20.044  2.257   4.425   1.00 11.89 ? 62  ASN A C   1 
ATOM   491  O  O   . ASN A 1 62  ? 21.024  2.818   4.954   1.00 15.91 ? 62  ASN A O   1 
ATOM   492  C  CB  . ASN A 1 62  ? 18.303  3.798   5.453   1.00 11.41 ? 62  ASN A CB  1 
ATOM   493  C  CG  . ASN A 1 62  ? 18.271  2.957   6.715   1.00 12.75 ? 62  ASN A CG  1 
ATOM   494  O  OD1 . ASN A 1 62  ? 18.513  1.744   6.654   1.00 10.93 ? 62  ASN A OD1 1 
ATOM   495  N  ND2 . ASN A 1 62  ? 18.030  3.578   7.862   1.00 15.98 ? 62  ASN A ND2 1 
ATOM   496  N  N   . GLY A 1 63  ? 20.117  1.002   3.992   1.00 11.90 ? 63  GLY A N   1 
ATOM   497  C  CA  . GLY A 1 63  ? 21.317  0.228   4.124   1.00 11.25 ? 63  GLY A CA  1 
ATOM   498  C  C   . GLY A 1 63  ? 21.392  -0.603  5.391   1.00 12.24 ? 63  GLY A C   1 
ATOM   499  O  O   . GLY A 1 63  ? 22.299  -1.427  5.497   1.00 13.22 ? 63  GLY A O   1 
ATOM   500  N  N   A HIS A 1 64  ? 20.445  -0.351  6.315   0.50 11.22 ? 64  HIS A N   1 
ATOM   501  N  N   B HIS A 1 64  ? 20.423  -0.452  6.307   0.50 11.48 ? 64  HIS A N   1 
ATOM   502  C  CA  A HIS A 1 64  ? 20.403  -1.071  7.586   0.50 10.88 ? 64  HIS A CA  1 
ATOM   503  C  CA  B HIS A 1 64  ? 20.434  -1.345  7.467   0.50 10.98 ? 64  HIS A CA  1 
ATOM   504  C  C   A HIS A 1 64  ? 19.059  -1.795  7.745   0.50 10.33 ? 64  HIS A C   1 
ATOM   505  C  C   B HIS A 1 64  ? 19.008  -1.690  7.919   0.50 10.39 ? 64  HIS A C   1 
ATOM   506  O  O   A HIS A 1 64  ? 19.017  -2.899  8.313   0.50 9.22  ? 64  HIS A O   1 
ATOM   507  O  O   B HIS A 1 64  ? 18.827  -2.485  8.831   0.50 9.10  ? 64  HIS A O   1 
ATOM   508  C  CB  A HIS A 1 64  ? 20.712  -0.134  8.772   0.50 11.28 ? 64  HIS A CB  1 
ATOM   509  C  CB  B HIS A 1 64  ? 21.250  -0.775  8.632   0.50 12.29 ? 64  HIS A CB  1 
ATOM   510  C  CG  A HIS A 1 64  ? 21.927  0.705   8.552   0.50 12.78 ? 64  HIS A CG  1 
ATOM   511  C  CG  B HIS A 1 64  ? 20.554  0.357   9.290   0.50 13.18 ? 64  HIS A CG  1 
ATOM   512  N  ND1 A HIS A 1 64  ? 23.208  0.165   8.565   0.50 14.81 ? 64  HIS A ND1 1 
ATOM   513  N  ND1 B HIS A 1 64  ? 20.844  1.678   9.009   0.50 15.22 ? 64  HIS A ND1 1 
ATOM   514  C  CD2 A HIS A 1 64  ? 22.067  2.026   8.325   0.50 13.25 ? 64  HIS A CD2 1 
ATOM   515  C  CD2 B HIS A 1 64  ? 19.578  0.365   10.228  0.50 14.63 ? 64  HIS A CD2 1 
ATOM   516  C  CE1 A HIS A 1 64  ? 24.086  1.139   8.378   0.50 14.05 ? 64  HIS A CE1 1 
ATOM   517  C  CE1 B HIS A 1 64  ? 20.045  2.444   9.728   0.50 15.95 ? 64  HIS A CE1 1 
ATOM   518  N  NE2 A HIS A 1 64  ? 23.421  2.278   8.199   0.50 15.74 ? 64  HIS A NE2 1 
ATOM   519  N  NE2 B HIS A 1 64  ? 19.281  1.668   10.478  0.50 17.04 ? 64  HIS A NE2 1 
ATOM   520  N  N   . THR A 1 65  ? 17.992  -1.166  7.251   1.00 9.83  ? 65  THR A N   1 
ATOM   521  C  CA  . THR A 1 65  ? 16.590  -1.542  7.378   1.00 9.36  ? 65  THR A CA  1 
ATOM   522  C  C   . THR A 1 65  ? 15.859  -0.898  6.197   1.00 10.05 ? 65  THR A C   1 
ATOM   523  O  O   . THR A 1 65  ? 16.491  -0.224  5.364   1.00 10.83 ? 65  THR A O   1 
ATOM   524  C  CB  . THR A 1 65  ? 16.005  -1.104  8.739   1.00 9.75  ? 65  THR A CB  1 
ATOM   525  O  OG1 . THR A 1 65  ? 14.681  -1.656  8.857   1.00 12.81 ? 65  THR A OG1 1 
ATOM   526  C  CG2 . THR A 1 65  ? 15.924  0.391   8.907   1.00 11.12 ? 65  THR A CG2 1 
ATOM   527  N  N   . PHE A 1 66  ? 14.534  -1.044  6.163   1.00 9.85  ? 66  PHE A N   1 
ATOM   528  C  CA  . PHE A 1 66  ? 13.755  -0.147  5.344   1.00 10.07 ? 66  PHE A CA  1 
ATOM   529  C  C   . PHE A 1 66  ? 12.805  0.618   6.225   1.00 9.47  ? 66  PHE A C   1 
ATOM   530  O  O   . PHE A 1 66  ? 12.411  0.153   7.308   1.00 9.69  ? 66  PHE A O   1 
ATOM   531  C  CB  . PHE A 1 66  ? 12.994  -0.942  4.274   1.00 10.86 ? 66  PHE A CB  1 
ATOM   532  C  CG  . PHE A 1 66  ? 11.879  -1.791  4.815   1.00 10.72 ? 66  PHE A CG  1 
ATOM   533  C  CD1 . PHE A 1 66  ? 10.617  -1.256  4.959   1.00 11.94 ? 66  PHE A CD1 1 
ATOM   534  C  CD2 . PHE A 1 66  ? 12.093  -3.134  5.145   1.00 10.99 ? 66  PHE A CD2 1 
ATOM   535  C  CE1 . PHE A 1 66  ? 9.570   -2.042  5.450   1.00 13.59 ? 66  PHE A CE1 1 
ATOM   536  C  CE2 . PHE A 1 66  ? 11.042  -3.931  5.631   1.00 10.91 ? 66  PHE A CE2 1 
ATOM   537  C  CZ  . PHE A 1 66  ? 9.769   -3.373  5.783   1.00 11.94 ? 66  PHE A CZ  1 
ATOM   538  N  N   . GLN A 1 67  ? 12.482  1.851   5.806   1.00 9.90  ? 67  GLN A N   1 
ATOM   539  C  CA  . GLN A 1 67  ? 11.669  2.715   6.629   1.00 10.57 ? 67  GLN A CA  1 
ATOM   540  C  C   . GLN A 1 67  ? 10.610  3.358   5.759   1.00 10.03 ? 67  GLN A C   1 
ATOM   541  O  O   . GLN A 1 67  ? 10.889  3.777   4.607   1.00 10.71 ? 67  GLN A O   1 
ATOM   542  C  CB  . GLN A 1 67  ? 12.473  3.780   7.406   1.00 13.69 ? 67  GLN A CB  1 
ATOM   543  C  CG  . GLN A 1 67  ? 13.264  4.710   6.497   1.00 15.43 ? 67  GLN A CG  1 
ATOM   544  C  CD  . GLN A 1 67  ? 14.081  5.735   7.265   1.00 18.74 ? 67  GLN A CD  1 
ATOM   545  O  OE1 . GLN A 1 67  ? 13.951  6.938   7.023   1.00 21.72 ? 67  GLN A OE1 1 
ATOM   546  N  NE2 . GLN A 1 67  ? 14.897  5.264   8.193   1.00 17.97 ? 67  GLN A NE2 1 
ATOM   547  N  N   . VAL A 1 68  ? 9.418   3.441   6.312   1.00 9.55  ? 68  VAL A N   1 
ATOM   548  C  CA  . VAL A 1 68  ? 8.340   4.206   5.715   1.00 10.07 ? 68  VAL A CA  1 
ATOM   549  C  C   . VAL A 1 68  ? 8.279   5.538   6.417   1.00 10.44 ? 68  VAL A C   1 
ATOM   550  O  O   . VAL A 1 68  ? 8.134   5.545   7.655   1.00 10.61 ? 68  VAL A O   1 
ATOM   551  C  CB  . VAL A 1 68  ? 7.029   3.416   5.819   1.00 9.52  ? 68  VAL A CB  1 
ATOM   552  C  CG1 . VAL A 1 68  ? 5.801   4.261   5.423   1.00 10.55 ? 68  VAL A CG1 1 
ATOM   553  C  CG2 . VAL A 1 68  ? 7.062   2.168   4.952   1.00 9.86  ? 68  VAL A CG2 1 
ATOM   554  N  N   . GLU A 1 69  ? 8.258   6.643   5.639   1.00 10.94 ? 69  GLU A N   1 
ATOM   555  C  CA  . GLU A 1 69  ? 8.379   7.962   6.215   1.00 11.43 ? 69  GLU A CA  1 
ATOM   556  C  C   . GLU A 1 69  ? 7.055   8.680   6.032   1.00 12.21 ? 69  GLU A C   1 
ATOM   557  O  O   . GLU A 1 69  ? 6.340   8.398   5.060   1.00 11.71 ? 69  GLU A O   1 
ATOM   558  C  CB  . GLU A 1 69  ? 9.450   8.734   5.472   1.00 12.70 ? 69  GLU A CB  1 
ATOM   559  C  CG  . GLU A 1 69  ? 10.823  8.073   5.531   1.00 14.85 ? 69  GLU A CG  1 
ATOM   560  C  CD  . GLU A 1 69  ? 11.745  8.620   4.485   1.00 15.76 ? 69  GLU A CD  1 
ATOM   561  O  OE1 . GLU A 1 69  ? 11.232  9.320   3.565   1.00 19.17 ? 69  GLU A OE1 1 
ATOM   562  O  OE2 . GLU A 1 69  ? 12.946  8.323   4.602   1.00 19.28 ? 69  GLU A OE2 1 
ATOM   563  N  N   . PHE A 1 70  ? 6.771   9.535   7.014   1.00 10.66 ? 70  PHE A N   1 
ATOM   564  C  CA  . PHE A 1 70  ? 5.519   10.275  7.077   1.00 11.01 ? 70  PHE A CA  1 
ATOM   565  C  C   . PHE A 1 70  ? 5.780   11.770  7.008   1.00 12.15 ? 70  PHE A C   1 
ATOM   566  O  O   . PHE A 1 70  ? 6.858   12.263  7.311   1.00 12.15 ? 70  PHE A O   1 
ATOM   567  C  CB  . PHE A 1 70  ? 4.802   9.935   8.388   1.00 11.59 ? 70  PHE A CB  1 
ATOM   568  C  CG  . PHE A 1 70  ? 4.261   8.531   8.359   1.00 11.50 ? 70  PHE A CG  1 
ATOM   569  C  CD1 . PHE A 1 70  ? 5.081   7.450   8.628   1.00 11.87 ? 70  PHE A CD1 1 
ATOM   570  C  CD2 . PHE A 1 70  ? 2.952   8.273   8.005   1.00 10.72 ? 70  PHE A CD2 1 
ATOM   571  C  CE1 . PHE A 1 70  ? 4.640   6.147   8.470   1.00 12.33 ? 70  PHE A CE1 1 
ATOM   572  C  CE2 . PHE A 1 70  ? 2.487   6.956   7.901   1.00 12.13 ? 70  PHE A CE2 1 
ATOM   573  C  CZ  . PHE A 1 70  ? 3.337   5.907   8.151   1.00 11.93 ? 70  PHE A CZ  1 
ATOM   574  N  N   A ASP A 1 71  ? 4.751   12.507  6.573   0.50 14.57 ? 71  ASP A N   1 
ATOM   575  N  N   B ASP A 1 71  ? 4.742   12.491  6.581   0.50 15.34 ? 71  ASP A N   1 
ATOM   576  C  CA  A ASP A 1 71  ? 4.788   13.958  6.686   0.50 14.75 ? 71  ASP A CA  1 
ATOM   577  C  CA  B ASP A 1 71  ? 4.759   13.938  6.686   0.50 16.17 ? 71  ASP A CA  1 
ATOM   578  C  C   A ASP A 1 71  ? 4.567   14.353  8.140   0.50 15.81 ? 71  ASP A C   1 
ATOM   579  C  C   B ASP A 1 71  ? 4.562   14.347  8.142   0.50 16.69 ? 71  ASP A C   1 
ATOM   580  O  O   A ASP A 1 71  ? 3.486   14.134  8.681   0.50 19.83 ? 71  ASP A O   1 
ATOM   581  O  O   B ASP A 1 71  ? 3.480   14.141  8.686   0.50 20.77 ? 71  ASP A O   1 
ATOM   582  C  CB  A ASP A 1 71  ? 3.654   14.568  5.872   0.50 16.86 ? 71  ASP A CB  1 
ATOM   583  C  CB  B ASP A 1 71  ? 3.567   14.502  5.927   0.50 19.62 ? 71  ASP A CB  1 
ATOM   584  C  CG  A ASP A 1 71  ? 3.463   16.067  6.123   0.50 17.15 ? 71  ASP A CG  1 
ATOM   585  C  CG  B ASP A 1 71  ? 3.573   16.015  6.040   0.50 22.08 ? 71  ASP A CG  1 
ATOM   586  O  OD1 A ASP A 1 71  ? 4.332   16.707  6.754   0.50 14.79 ? 71  ASP A OD1 1 
ATOM   587  O  OD1 B ASP A 1 71  ? 4.610   16.583  5.721   0.50 23.19 ? 71  ASP A OD1 1 
ATOM   588  O  OD2 A ASP A 1 71  ? 2.415   16.590  5.666   0.50 20.02 ? 71  ASP A OD2 1 
ATOM   589  O  OD2 B ASP A 1 71  ? 2.544   16.592  6.478   0.50 25.03 ? 71  ASP A OD2 1 
ATOM   590  N  N   . ASP A 1 72  ? 5.582   14.950  8.762   1.00 17.05 ? 72  ASP A N   1 
ATOM   591  C  CA  . ASP A 1 72  ? 5.522   15.374  10.156  1.00 17.51 ? 72  ASP A CA  1 
ATOM   592  C  C   . ASP A 1 72  ? 5.574   16.903  10.263  1.00 20.14 ? 72  ASP A C   1 
ATOM   593  O  O   . ASP A 1 72  ? 6.038   17.395  11.304  1.00 23.55 ? 72  ASP A O   1 
ATOM   594  C  CB  . ASP A 1 72  ? 6.684   14.779  10.981  1.00 17.93 ? 72  ASP A CB  1 
ATOM   595  C  CG  . ASP A 1 72  ? 8.048   15.325  10.548  1.00 18.92 ? 72  ASP A CG  1 
ATOM   596  O  OD1 . ASP A 1 72  ? 8.132   15.912  9.413   1.00 20.46 ? 72  ASP A OD1 1 
ATOM   597  O  OD2 . ASP A 1 72  ? 9.043   15.163  11.263  1.00 19.03 ? 72  ASP A OD2 1 
ATOM   598  N  N   . SER A 1 73  ? 5.170   17.599  9.196   1.00 22.80 ? 73  SER A N   1 
ATOM   599  C  CA  . SER A 1 73  ? 5.186   19.076  9.184   1.00 23.93 ? 73  SER A CA  1 
ATOM   600  C  C   . SER A 1 73  ? 3.939   19.693  9.828   1.00 30.33 ? 73  SER A C   1 
ATOM   601  O  O   . SER A 1 73  ? 3.800   20.928  9.945   1.00 23.90 ? 73  SER A O   1 
ATOM   602  C  CB  . SER A 1 73  ? 5.349   19.583  7.773   1.00 22.12 ? 73  SER A CB  1 
ATOM   603  O  OG  . SER A 1 73  ? 4.179   19.339  7.000   1.00 23.24 ? 73  SER A OG  1 
ATOM   604  N  N   . GLN A 1 74  ? 2.983   18.840  10.193  1.00 26.37 ? 74  GLN A N   1 
ATOM   605  C  CA  . GLN A 1 74  ? 1.899   19.294  11.047  1.00 29.25 ? 74  GLN A CA  1 
ATOM   606  C  C   . GLN A 1 74  ? 1.546   18.160  11.985  1.00 28.72 ? 74  GLN A C   1 
ATOM   607  O  O   . GLN A 1 74  ? 2.023   17.048  11.786  1.00 22.08 ? 74  GLN A O   1 
ATOM   608  C  CB  . GLN A 1 74  ? 0.628   19.538  10.245  1.00 34.38 ? 74  GLN A CB  1 
ATOM   609  C  CG  . GLN A 1 74  ? 0.843   20.235  8.914   1.00 41.82 ? 74  GLN A CG  1 
ATOM   610  C  CD  . GLN A 1 74  ? -0.505  20.655  8.392   1.00 43.34 ? 74  GLN A CD  1 
ATOM   611  O  OE1 . GLN A 1 74  ? -1.261  21.342  9.092   1.00 42.64 ? 74  GLN A OE1 1 
ATOM   612  N  NE2 . GLN A 1 74  ? -0.830  20.188  7.195   1.00 43.23 ? 74  GLN A NE2 1 
ATOM   613  N  N   . ASP A 1 75  ? 0.708   18.483  12.983  1.00 31.87 ? 75  ASP A N   1 
ATOM   614  C  CA  . ASP A 1 75  ? 0.213   17.495  13.925  1.00 31.61 ? 75  ASP A CA  1 
ATOM   615  C  C   . ASP A 1 75  ? -0.859  16.689  13.204  1.00 31.77 ? 75  ASP A C   1 
ATOM   616  O  O   . ASP A 1 75  ? -1.996  17.138  13.055  1.00 34.22 ? 75  ASP A O   1 
ATOM   617  C  CB  . ASP A 1 75  ? -0.315  18.113  15.226  1.00 38.62 ? 75  ASP A CB  1 
ATOM   618  C  CG  . ASP A 1 75  ? 0.661   18.106  16.400  1.00 40.25 ? 75  ASP A CG  1 
ATOM   619  O  OD1 . ASP A 1 75  ? 1.601   17.286  16.396  1.00 37.95 ? 75  ASP A OD1 1 
ATOM   620  O  OD2 . ASP A 1 75  ? 0.454   18.920  17.343  1.00 44.52 ? 75  ASP A OD2 1 
ATOM   621  N  N   . LYS A 1 76  ? -0.434  15.522  12.715  1.00 27.34 ? 76  LYS A N   1 
ATOM   622  C  CA  . LYS A 1 76  ? -1.317  14.546  12.107  1.00 25.78 ? 76  LYS A CA  1 
ATOM   623  C  C   . LYS A 1 76  ? -1.311  13.292  12.980  1.00 26.30 ? 76  LYS A C   1 
ATOM   624  O  O   . LYS A 1 76  ? -2.097  13.191  13.927  1.00 31.69 ? 76  LYS A O   1 
ATOM   625  C  CB  . LYS A 1 76  ? -0.891  14.275  10.665  1.00 25.21 ? 76  LYS A CB  1 
ATOM   626  C  CG  . LYS A 1 76  ? -0.973  15.483  9.738   1.00 30.02 ? 76  LYS A CG  1 
ATOM   627  C  CD  . LYS A 1 76  ? -0.497  15.172  8.319   1.00 29.80 ? 76  LYS A CD  1 
ATOM   628  C  CE  . LYS A 1 76  ? -0.759  16.310  7.352   1.00 31.84 ? 76  LYS A CE  1 
ATOM   629  N  NZ  . LYS A 1 76  ? -0.392  15.993  5.950   1.00 29.86 ? 76  LYS A NZ  1 
ATOM   630  N  N   . ALA A 1 77  ? -0.377  12.395  12.702  1.00 24.42 ? 77  ALA A N   1 
ATOM   631  C  CA  . ALA A 1 77  ? -0.307  11.121  13.416  1.00 20.10 ? 77  ALA A CA  1 
ATOM   632  C  C   . ALA A 1 77  ? 0.504   11.294  14.701  1.00 20.01 ? 77  ALA A C   1 
ATOM   633  O  O   . ALA A 1 77  ? 1.673   11.675  14.589  1.00 22.65 ? 77  ALA A O   1 
ATOM   634  C  CB  . ALA A 1 77  ? 0.343   10.129  12.513  1.00 20.89 ? 77  ALA A CB  1 
ATOM   635  N  N   . VAL A 1 78  ? -0.110  11.124  15.876  1.00 14.77 ? 78  VAL A N   1 
ATOM   636  C  CA  . VAL A 1 78  ? 0.532   11.432  17.139  1.00 16.48 ? 78  VAL A CA  1 
ATOM   637  C  C   . VAL A 1 78  ? 0.314   10.319  18.153  1.00 15.53 ? 78  VAL A C   1 
ATOM   638  O  O   . VAL A 1 78  ? -0.744  9.624   18.181  1.00 16.86 ? 78  VAL A O   1 
ATOM   639  C  CB  . VAL A 1 78  ? 0.145   12.804  17.709  1.00 20.49 ? 78  VAL A CB  1 
ATOM   640  C  CG1 . VAL A 1 78  ? 0.447   13.912  16.694  1.00 19.37 ? 78  VAL A CG1 1 
ATOM   641  C  CG2 . VAL A 1 78  ? -1.307  12.802  18.046  1.00 22.18 ? 78  VAL A CG2 1 
ATOM   642  N  N   . LEU A 1 79  ? 1.347   10.153  18.986  1.00 13.16 ? 79  LEU A N   1 
ATOM   643  C  CA  . LEU A 1 79  ? 1.282   9.295   20.145  1.00 12.12 ? 79  LEU A CA  1 
ATOM   644  C  C   . LEU A 1 79  ? 1.321   10.171  21.370  1.00 13.64 ? 79  LEU A C   1 
ATOM   645  O  O   . LEU A 1 79  ? 2.155   11.064  21.472  1.00 12.50 ? 79  LEU A O   1 
ATOM   646  C  CB  . LEU A 1 79  ? 2.487   8.364   20.034  1.00 13.30 ? 79  LEU A CB  1 
ATOM   647  C  CG  . LEU A 1 79  ? 2.658   7.368   21.180  1.00 14.50 ? 79  LEU A CG  1 
ATOM   648  C  CD1 . LEU A 1 79  ? 1.564   6.292   21.129  1.00 17.25 ? 79  LEU A CD1 1 
ATOM   649  C  CD2 . LEU A 1 79  ? 4.026   6.716   21.014  1.00 14.70 ? 79  LEU A CD2 1 
ATOM   650  N  N   A LYS A 1 80  ? 0.425   9.907   22.319  0.50 13.12 ? 80  LYS A N   1 
ATOM   651  N  N   B LYS A 1 80  ? 0.416   9.858   22.298  0.50 13.48 ? 80  LYS A N   1 
ATOM   652  C  CA  A LYS A 1 80  ? 0.486   10.564  23.614  0.50 14.20 ? 80  LYS A CA  1 
ATOM   653  C  CA  B LYS A 1 80  ? 0.212   10.625  23.513  0.50 14.79 ? 80  LYS A CA  1 
ATOM   654  C  C   A LYS A 1 80  ? -0.069  9.637   24.686  0.50 13.43 ? 80  LYS A C   1 
ATOM   655  C  C   B LYS A 1 80  ? -0.185  9.684   24.650  0.50 14.05 ? 80  LYS A C   1 
ATOM   656  O  O   A LYS A 1 80  ? -0.421  8.490   24.406  0.50 13.78 ? 80  LYS A O   1 
ATOM   657  O  O   B LYS A 1 80  ? -0.483  8.521   24.378  0.50 14.47 ? 80  LYS A O   1 
ATOM   658  C  CB  A LYS A 1 80  ? -0.376  11.831  23.645  0.50 15.34 ? 80  LYS A CB  1 
ATOM   659  C  CB  B LYS A 1 80  ? -0.847  11.704  23.254  0.50 17.06 ? 80  LYS A CB  1 
ATOM   660  C  CG  A LYS A 1 80  ? -1.753  11.594  23.033  0.50 16.58 ? 80  LYS A CG  1 
ATOM   661  C  CG  B LYS A 1 80  ? -0.429  12.775  22.251  0.50 16.74 ? 80  LYS A CG  1 
ATOM   662  C  CD  A LYS A 1 80  ? -2.554  12.846  22.743  0.50 20.47 ? 80  LYS A CD  1 
ATOM   663  C  CD  B LYS A 1 80  ? -1.572  13.469  21.565  0.50 19.53 ? 80  LYS A CD  1 
ATOM   664  C  CE  A LYS A 1 80  ? -1.750  14.122  22.810  0.50 22.27 ? 80  LYS A CE  1 
ATOM   665  C  CE  B LYS A 1 80  ? -2.836  13.284  22.360  0.50 19.75 ? 80  LYS A CE  1 
ATOM   666  N  NZ  A LYS A 1 80  ? -1.934  14.934  21.585  0.50 25.78 ? 80  LYS A NZ  1 
ATOM   667  N  NZ  B LYS A 1 80  ? -2.529  13.428  23.803  0.50 18.75 ? 80  LYS A NZ  1 
ATOM   668  N  N   . GLY A 1 81  ? -0.133  10.183  25.893  1.00 15.14 ? 81  GLY A N   1 
ATOM   669  C  CA  . GLY A 1 81  ? -0.579  9.419   27.050  1.00 16.28 ? 81  GLY A CA  1 
ATOM   670  C  C   . GLY A 1 81  ? 0.424   8.354   27.460  1.00 18.08 ? 81  GLY A C   1 
ATOM   671  O  O   . GLY A 1 81  ? 1.624   8.440   27.181  1.00 16.22 ? 81  GLY A O   1 
ATOM   672  N  N   . GLY A 1 82  ? -0.055  7.349   28.197  1.00 19.83 ? 82  GLY A N   1 
ATOM   673  C  CA  . GLY A 1 82  ? 0.849   6.345   28.721  1.00 20.15 ? 82  GLY A CA  1 
ATOM   674  C  C   . GLY A 1 82  ? 1.868   6.988   29.635  1.00 20.35 ? 82  GLY A C   1 
ATOM   675  O  O   . GLY A 1 82  ? 1.513   7.774   30.521  1.00 19.64 ? 82  GLY A O   1 
ATOM   676  N  N   . PRO A 1 83  ? 3.182   6.721   29.441  1.00 14.89 ? 83  PRO A N   1 
ATOM   677  C  CA  . PRO A 1 83  ? 4.178   7.366   30.263  1.00 16.19 ? 83  PRO A CA  1 
ATOM   678  C  C   . PRO A 1 83  ? 4.596   8.736   29.758  1.00 14.80 ? 83  PRO A C   1 
ATOM   679  O  O   . PRO A 1 83  ? 5.398   9.410   30.420  1.00 17.90 ? 83  PRO A O   1 
ATOM   680  C  CB  . PRO A 1 83  ? 5.358   6.396   30.089  1.00 15.62 ? 83  PRO A CB  1 
ATOM   681  C  CG  . PRO A 1 83  ? 5.229   5.971   28.606  1.00 13.70 ? 83  PRO A CG  1 
ATOM   682  C  CD  . PRO A 1 83  ? 3.737   5.803   28.400  1.00 15.35 ? 83  PRO A CD  1 
ATOM   683  N  N   . LEU A 1 84  ? 4.022   9.153   28.629  1.00 14.53 ? 84  LEU A N   1 
ATOM   684  C  CA  . LEU A 1 84  ? 4.541   10.337  27.940  1.00 14.51 ? 84  LEU A CA  1 
ATOM   685  C  C   . LEU A 1 84  ? 3.919   11.612  28.539  1.00 15.52 ? 84  LEU A C   1 
ATOM   686  O  O   . LEU A 1 84  ? 2.718   11.615  28.872  1.00 16.99 ? 84  LEU A O   1 
ATOM   687  C  CB  . LEU A 1 84  ? 4.285   10.253  26.440  1.00 13.99 ? 84  LEU A CB  1 
ATOM   688  C  CG  . LEU A 1 84  ? 4.774   8.953   25.775  1.00 12.82 ? 84  LEU A CG  1 
ATOM   689  C  CD1 . LEU A 1 84  ? 4.279   8.934   24.369  1.00 13.22 ? 84  LEU A CD1 1 
ATOM   690  C  CD2 . LEU A 1 84  ? 6.311   8.894   25.823  1.00 13.20 ? 84  LEU A CD2 1 
ATOM   691  N  N   . ASP A 1 85  ? 4.744   12.664  28.563  1.00 16.73 ? 85  ASP A N   1 
ATOM   692  C  CA  . ASP A 1 85  ? 4.279   14.012  28.824  1.00 18.32 ? 85  ASP A CA  1 
ATOM   693  C  C   . ASP A 1 85  ? 4.252   14.676  27.462  1.00 19.78 ? 85  ASP A C   1 
ATOM   694  O  O   . ASP A 1 85  ? 5.218   14.575  26.697  1.00 23.95 ? 85  ASP A O   1 
ATOM   695  C  CB  . ASP A 1 85  ? 5.221   14.701  29.814  1.00 21.17 ? 85  ASP A CB  1 
ATOM   696  C  CG  . ASP A 1 85  ? 5.123   14.177  31.238  1.00 27.68 ? 85  ASP A CG  1 
ATOM   697  O  OD1 . ASP A 1 85  ? 4.036   13.711  31.626  1.00 30.99 ? 85  ASP A OD1 1 
ATOM   698  O  OD2 . ASP A 1 85  ? 6.150   14.196  31.929  1.00 26.56 ? 85  ASP A OD2 1 
ATOM   699  N  N   . GLY A 1 86  ? 3.167   15.362  27.135  1.00 22.61 ? 86  GLY A N   1 
ATOM   700  C  CA  . GLY A 1 86  ? 3.099   16.026  25.840  1.00 20.65 ? 86  GLY A CA  1 
ATOM   701  C  C   . GLY A 1 86  ? 2.792   15.087  24.672  1.00 21.75 ? 86  GLY A C   1 
ATOM   702  O  O   . GLY A 1 86  ? 2.212   14.016  24.826  1.00 24.31 ? 86  GLY A O   1 
ATOM   703  N  N   A THR A 1 87  ? 3.141   15.557  23.467  0.50 18.25 ? 87  THR A N   1 
ATOM   704  N  N   B THR A 1 87  ? 3.107   15.555  23.467  0.50 18.36 ? 87  THR A N   1 
ATOM   705  C  CA  A THR A 1 87  ? 2.673   15.024  22.206  0.50 16.31 ? 87  THR A CA  1 
ATOM   706  C  CA  B THR A 1 87  ? 2.666   14.863  22.283  0.50 16.49 ? 87  THR A CA  1 
ATOM   707  C  C   A THR A 1 87  ? 3.878   14.630  21.362  0.50 14.19 ? 87  THR A C   1 
ATOM   708  C  C   B THR A 1 87  ? 3.869   14.599  21.398  0.50 14.24 ? 87  THR A C   1 
ATOM   709  O  O   A THR A 1 87  ? 4.841   15.399  21.222  0.50 13.21 ? 87  THR A O   1 
ATOM   710  O  O   B THR A 1 87  ? 4.808   15.402  21.280  0.50 13.54 ? 87  THR A O   1 
ATOM   711  C  CB  A THR A 1 87  ? 1.926   16.096  21.397  0.50 17.91 ? 87  THR A CB  1 
ATOM   712  C  CB  B THR A 1 87  ? 1.602   15.660  21.530  0.50 18.46 ? 87  THR A CB  1 
ATOM   713  O  OG1 A THR A 1 87  ? 0.755   16.455  22.133  0.50 19.53 ? 87  THR A OG1 1 
ATOM   714  O  OG1 B THR A 1 87  ? 2.185   16.951  21.332  0.50 17.82 ? 87  THR A OG1 1 
ATOM   715  C  CG2 A THR A 1 87  ? 1.560   15.617  20.008  0.50 15.93 ? 87  THR A CG2 1 
ATOM   716  C  CG2 B THR A 1 87  ? 0.313   15.748  22.316  0.50 18.54 ? 87  THR A CG2 1 
ATOM   717  N  N   . TYR A 1 88  ? 3.833   13.421  20.797  1.00 11.43 ? 88  TYR A N   1 
ATOM   718  C  CA  . TYR A 1 88  ? 4.931   12.948  19.955  1.00 11.47 ? 88  TYR A CA  1 
ATOM   719  C  C   . TYR A 1 88  ? 4.420   12.643  18.566  1.00 11.09 ? 88  TYR A C   1 
ATOM   720  O  O   . TYR A 1 88  ? 3.424   11.924  18.413  1.00 14.79 ? 88  TYR A O   1 
ATOM   721  C  CB  . TYR A 1 88  ? 5.575   11.709  20.569  1.00 10.03 ? 88  TYR A CB  1 
ATOM   722  C  CG  . TYR A 1 88  ? 6.366   11.915  21.825  1.00 9.62  ? 88  TYR A CG  1 
ATOM   723  C  CD1 . TYR A 1 88  ? 5.761   12.316  23.029  1.00 10.19 ? 88  TYR A CD1 1 
ATOM   724  C  CD2 . TYR A 1 88  ? 7.750   11.709  21.836  1.00 8.57  ? 88  TYR A CD2 1 
ATOM   725  C  CE1 . TYR A 1 88  ? 6.509   12.421  24.209  1.00 9.71  ? 88  TYR A CE1 1 
ATOM   726  C  CE2 . TYR A 1 88  ? 8.500   11.822  23.000  1.00 8.20  ? 88  TYR A CE2 1 
ATOM   727  C  CZ  . TYR A 1 88  ? 7.890   12.156  24.212  1.00 8.41  ? 88  TYR A CZ  1 
ATOM   728  O  OH  . TYR A 1 88  ? 8.620   12.263  25.338  1.00 11.01 ? 88  TYR A OH  1 
ATOM   729  N  N   . ARG A 1 89  ? 5.102   13.147  17.535  1.00 10.37 ? 89  ARG A N   1 
ATOM   730  C  CA  . ARG A 1 89  ? 4.640   13.044  16.171  1.00 11.20 ? 89  ARG A CA  1 
ATOM   731  C  C   . ARG A 1 89  ? 5.290   11.867  15.444  1.00 9.50  ? 89  ARG A C   1 
ATOM   732  O  O   . ARG A 1 89  ? 6.529   11.738  15.483  1.00 9.57  ? 89  ARG A O   1 
ATOM   733  C  CB  . ARG A 1 89  ? 5.066   14.334  15.444  1.00 13.66 ? 89  ARG A CB  1 
ATOM   734  C  CG  . ARG A 1 89  ? 4.188   14.633  14.241  1.00 18.89 ? 89  ARG A CG  1 
ATOM   735  C  CD  . ARG A 1 89  ? 4.427   16.081  13.756  1.00 19.56 ? 89  ARG A CD  1 
ATOM   736  N  NE  . ARG A 1 89  ? 3.759   17.091  14.573  1.00 21.10 ? 89  ARG A NE  1 
ATOM   737  C  CZ  . ARG A 1 89  ? 3.945   18.428  14.417  1.00 22.15 ? 89  ARG A CZ  1 
ATOM   738  N  NH1 . ARG A 1 89  ? 4.787   18.874  13.501  1.00 19.81 ? 89  ARG A NH1 1 
ATOM   739  N  NH2 . ARG A 1 89  ? 3.301   19.311  15.164  1.00 22.48 ? 89  ARG A NH2 1 
ATOM   740  N  N   . LEU A 1 90  ? 4.488   11.070  14.713  1.00 9.56  ? 90  LEU A N   1 
ATOM   741  C  CA  . LEU A 1 90  ? 5.061   9.970   13.944  1.00 9.59  ? 90  LEU A CA  1 
ATOM   742  C  C   . LEU A 1 90  ? 5.873   10.503  12.780  1.00 9.08  ? 90  LEU A C   1 
ATOM   743  O  O   . LEU A 1 90  ? 5.402   11.372  12.022  1.00 12.27 ? 90  LEU A O   1 
ATOM   744  C  CB  . LEU A 1 90  ? 3.920   9.088   13.424  1.00 10.54 ? 90  LEU A CB  1 
ATOM   745  C  CG  . LEU A 1 90  ? 4.341   7.971   12.483  1.00 10.57 ? 90  LEU A CG  1 
ATOM   746  C  CD1 . LEU A 1 90  ? 5.064   6.859   13.232  1.00 11.64 ? 90  LEU A CD1 1 
ATOM   747  C  CD2 . LEU A 1 90  ? 3.080   7.364   11.883  1.00 11.69 ? 90  LEU A CD2 1 
ATOM   748  N  N   . ILE A 1 91  ? 7.118   10.029  12.680  1.00 8.61  ? 91  ILE A N   1 
ATOM   749  C  CA  . ILE A 1 91  ? 7.966   10.378  11.548  1.00 8.92  ? 91  ILE A CA  1 
ATOM   750  C  C   . ILE A 1 91  ? 8.248   9.198   10.625  1.00 9.50  ? 91  ILE A C   1 
ATOM   751  O  O   . ILE A 1 91  ? 8.301   9.333   9.400   1.00 9.18  ? 91  ILE A O   1 
ATOM   752  C  CB  . ILE A 1 91  ? 9.272   11.122  11.934  1.00 9.74  ? 91  ILE A CB  1 
ATOM   753  C  CG1 . ILE A 1 91  ? 10.182  11.400  10.728  1.00 12.28 ? 91  ILE A CG1 1 
ATOM   754  C  CG2 . ILE A 1 91  ? 10.090  10.360  12.973  1.00 10.78 ? 91  ILE A CG2 1 
ATOM   755  C  CD1 . ILE A 1 91  ? 9.549   12.256  9.654   1.00 15.12 ? 91  ILE A CD1 1 
ATOM   756  N  N   . GLN A 1 92  ? 8.415   7.998   11.177  1.00 8.80  ? 92  GLN A N   1 
ATOM   757  C  CA  . GLN A 1 92  ? 8.712   6.865   10.323  1.00 8.12  ? 92  GLN A CA  1 
ATOM   758  C  C   . GLN A 1 92  ? 8.509   5.573   11.092  1.00 8.33  ? 92  GLN A C   1 
ATOM   759  O  O   . GLN A 1 92  ? 8.416   5.624   12.306  1.00 8.91  ? 92  GLN A O   1 
ATOM   760  C  CB  . GLN A 1 92  ? 10.173  6.878   9.830   1.00 9.97  ? 92  GLN A CB  1 
ATOM   761  C  CG  . GLN A 1 92  ? 11.223  6.915   10.962  1.00 9.87  ? 92  GLN A CG  1 
ATOM   762  C  CD  . GLN A 1 92  ? 11.987  5.615   11.163  1.00 11.08 ? 92  GLN A CD  1 
ATOM   763  O  OE1 . GLN A 1 92  ? 11.419  4.553   11.224  1.00 10.32 ? 92  GLN A OE1 1 
ATOM   764  N  NE2 . GLN A 1 92  ? 13.302  5.697   11.307  1.00 14.25 ? 92  GLN A NE2 1 
ATOM   765  N  N   . PHE A 1 93  ? 8.343   4.495   10.374  1.00 7.78  ? 93  PHE A N   1 
ATOM   766  C  CA  . PHE A 1 93  ? 8.484   3.188   11.001  1.00 7.35  ? 93  PHE A CA  1 
ATOM   767  C  C   . PHE A 1 93  ? 9.447   2.351   10.195  1.00 7.50  ? 93  PHE A C   1 
ATOM   768  O  O   . PHE A 1 93  ? 9.644   2.536   9.015   1.00 7.81  ? 93  PHE A O   1 
ATOM   769  C  CB  . PHE A 1 93  ? 7.152   2.445   11.198  1.00 8.83  ? 93  PHE A CB  1 
ATOM   770  C  CG  . PHE A 1 93  ? 6.401   2.015   9.961   1.00 8.38  ? 93  PHE A CG  1 
ATOM   771  C  CD1 . PHE A 1 93  ? 6.796   0.941   9.203   1.00 8.75  ? 93  PHE A CD1 1 
ATOM   772  C  CD2 . PHE A 1 93  ? 5.236   2.707   9.588   1.00 9.19  ? 93  PHE A CD2 1 
ATOM   773  C  CE1 . PHE A 1 93  ? 6.121   0.525   8.058   1.00 9.64  ? 93  PHE A CE1 1 
ATOM   774  C  CE2 . PHE A 1 93  ? 4.547   2.288   8.454   1.00 10.18 ? 93  PHE A CE2 1 
ATOM   775  C  CZ  . PHE A 1 93  ? 4.993   1.235   7.689   1.00 9.86  ? 93  PHE A CZ  1 
ATOM   776  N  N   . HIS A 1 94  ? 10.046  1.351   10.849  1.00 6.82  ? 94  HIS A N   1 
ATOM   777  C  CA  . HIS A 1 94  ? 10.991  0.420   10.244  1.00 7.38  ? 94  HIS A CA  1 
ATOM   778  C  C   . HIS A 1 94  ? 10.958  -0.870  11.022  1.00 7.08  ? 94  HIS A C   1 
ATOM   779  O  O   . HIS A 1 94  ? 10.242  -0.983  12.010  1.00 7.68  ? 94  HIS A O   1 
ATOM   780  C  CB  . HIS A 1 94  ? 12.419  0.986   10.220  1.00 7.70  ? 94  HIS A CB  1 
ATOM   781  C  CG  . HIS A 1 94  ? 12.933  1.228   11.607  1.00 7.10  ? 94  HIS A CG  1 
ATOM   782  N  ND1 . HIS A 1 94  ? 12.661  2.383   12.323  1.00 7.24  ? 94  HIS A ND1 1 
ATOM   783  C  CD2 . HIS A 1 94  ? 13.597  0.386   12.447  1.00 7.32  ? 94  HIS A CD2 1 
ATOM   784  C  CE1 . HIS A 1 94  ? 13.137  2.266   13.554  1.00 7.32  ? 94  HIS A CE1 1 
ATOM   785  N  NE2 . HIS A 1 94  ? 13.743  1.028   13.672  1.00 7.18  ? 94  HIS A NE2 1 
ATOM   786  N  N   . PHE A 1 95  ? 11.690  -1.853  10.513  1.00 7.75  ? 95  PHE A N   1 
ATOM   787  C  CA  . PHE A 1 95  ? 11.675  -3.162  11.165  1.00 7.09  ? 95  PHE A CA  1 
ATOM   788  C  C   . PHE A 1 95  ? 13.084  -3.679  11.387  1.00 8.07  ? 95  PHE A C   1 
ATOM   789  O  O   . PHE A 1 95  ? 14.082  -3.224  10.827  1.00 8.49  ? 95  PHE A O   1 
ATOM   790  C  CB  . PHE A 1 95  ? 10.937  -4.209  10.293  1.00 7.74  ? 95  PHE A CB  1 
ATOM   791  C  CG  . PHE A 1 95  ? 9.498   -3.925  9.979   1.00 8.18  ? 95  PHE A CG  1 
ATOM   792  C  CD1 . PHE A 1 95  ? 9.128   -3.008  8.989   1.00 9.11  ? 95  PHE A CD1 1 
ATOM   793  C  CD2 . PHE A 1 95  ? 8.508   -4.659  10.611  1.00 8.97  ? 95  PHE A CD2 1 
ATOM   794  C  CE1 . PHE A 1 95  ? 7.807   -2.780  8.692   1.00 10.01 ? 95  PHE A CE1 1 
ATOM   795  C  CE2 . PHE A 1 95  ? 7.172   -4.434  10.307  1.00 9.96  ? 95  PHE A CE2 1 
ATOM   796  C  CZ  . PHE A 1 95  ? 6.833   -3.488  9.351   1.00 10.51 ? 95  PHE A CZ  1 
ATOM   797  N  N   . HIS A 1 96  ? 13.160  -4.659  12.299  1.00 7.80  ? 96  HIS A N   1 
ATOM   798  C  CA  . HIS A 1 96  ? 14.348  -5.477  12.502  1.00 6.96  ? 96  HIS A CA  1 
ATOM   799  C  C   . HIS A 1 96  ? 13.913  -6.923  12.390  1.00 8.56  ? 96  HIS A C   1 
ATOM   800  O  O   . HIS A 1 96  ? 12.830  -7.246  12.829  1.00 8.82  ? 96  HIS A O   1 
ATOM   801  C  CB  . HIS A 1 96  ? 14.993  -5.245  13.916  1.00 7.32  ? 96  HIS A CB  1 
ATOM   802  C  CG  . HIS A 1 96  ? 15.245  -3.787  14.157  1.00 7.90  ? 96  HIS A CG  1 
ATOM   803  N  ND1 . HIS A 1 96  ? 16.497  -3.211  13.992  1.00 8.22  ? 96  HIS A ND1 1 
ATOM   804  C  CD2 . HIS A 1 96  ? 14.419  -2.810  14.522  1.00 7.67  ? 96  HIS A CD2 1 
ATOM   805  C  CE1 . HIS A 1 96  ? 16.423  -1.888  14.310  1.00 8.41  ? 96  HIS A CE1 1 
ATOM   806  N  NE2 . HIS A 1 96  ? 15.154  -1.640  14.605  1.00 6.87  ? 96  HIS A NE2 1 
ATOM   807  N  N   . TRP A 1 97  ? 14.736  -7.747  11.747  1.00 7.72  ? 97  TRP A N   1 
ATOM   808  C  CA  . TRP A 1 97  ? 14.298  -9.121  11.549  1.00 7.98  ? 97  TRP A CA  1 
ATOM   809  C  C   . TRP A 1 97  ? 15.498  -10.035 11.401  1.00 7.67  ? 97  TRP A C   1 
ATOM   810  O  O   . TRP A 1 97  ? 16.651  -9.654  11.312  1.00 7.80  ? 97  TRP A O   1 
ATOM   811  C  CB  . TRP A 1 97  ? 13.411  -9.252  10.292  1.00 8.32  ? 97  TRP A CB  1 
ATOM   812  C  CG  . TRP A 1 97  ? 14.081  -8.865  9.001   1.00 8.31  ? 97  TRP A CG  1 
ATOM   813  C  CD1 . TRP A 1 97  ? 14.864  -9.686  8.219   1.00 9.39  ? 97  TRP A CD1 1 
ATOM   814  C  CD2 . TRP A 1 97  ? 14.151  -7.551  8.442   1.00 8.15  ? 97  TRP A CD2 1 
ATOM   815  N  NE1 . TRP A 1 97  ? 15.319  -8.980  7.136   1.00 9.89  ? 97  TRP A NE1 1 
ATOM   816  C  CE2 . TRP A 1 97  ? 14.921  -7.663  7.260   1.00 8.36  ? 97  TRP A CE2 1 
ATOM   817  C  CE3 . TRP A 1 97  ? 13.610  -6.295  8.793   1.00 8.51  ? 97  TRP A CE3 1 
ATOM   818  C  CZ2 . TRP A 1 97  ? 15.163  -6.575  6.439   1.00 9.42  ? 97  TRP A CZ2 1 
ATOM   819  C  CZ3 . TRP A 1 97  ? 13.852  -5.209  7.969   1.00 8.92  ? 97  TRP A CZ3 1 
ATOM   820  C  CH2 . TRP A 1 97  ? 14.646  -5.345  6.810   1.00 9.06  ? 97  TRP A CH2 1 
ATOM   821  N  N   . GLY A 1 98  ? 15.180  -11.341 11.401  1.00 8.22  ? 98  GLY A N   1 
ATOM   822  C  CA  . GLY A 1 98  ? 16.198  -12.386 11.470  1.00 8.92  ? 98  GLY A CA  1 
ATOM   823  C  C   . GLY A 1 98  ? 16.439  -13.111 10.140  1.00 9.45  ? 98  GLY A C   1 
ATOM   824  O  O   . GLY A 1 98  ? 15.752  -12.874 9.150   1.00 11.01 ? 98  GLY A O   1 
ATOM   825  N  N   . SER A 1 99  ? 17.471  -13.947 10.150  1.00 10.30 ? 99  SER A N   1 
ATOM   826  C  CA  . SER A 1 99  ? 17.684  -14.864 9.031   1.00 11.02 ? 99  SER A CA  1 
ATOM   827  C  C   . SER A 1 99  ? 16.824  -16.116 9.181   1.00 12.76 ? 99  SER A C   1 
ATOM   828  O  O   . SER A 1 99  ? 16.702  -16.865 8.209   1.00 15.51 ? 99  SER A O   1 
ATOM   829  C  CB  . SER A 1 99  ? 19.138  -15.192 8.995   1.00 12.28 ? 99  SER A CB  1 
ATOM   830  O  OG  . SER A 1 99  ? 19.548  -15.757 10.238  1.00 12.97 ? 99  SER A OG  1 
ATOM   831  N  N   . LEU A 1 100 ? 16.263  -16.340 10.369  1.00 12.85 ? 100 LEU A N   1 
ATOM   832  C  CA  . LEU A 1 100 ? 15.416  -17.472 10.679  1.00 15.00 ? 100 LEU A CA  1 
ATOM   833  C  C   . LEU A 1 100 ? 14.219  -16.943 11.465  1.00 13.93 ? 100 LEU A C   1 
ATOM   834  O  O   . LEU A 1 100 ? 14.327  -15.941 12.200  1.00 13.03 ? 100 LEU A O   1 
ATOM   835  C  CB  . LEU A 1 100 ? 16.217  -18.391 11.612  1.00 16.37 ? 100 LEU A CB  1 
ATOM   836  C  CG  . LEU A 1 100 ? 17.547  -18.855 11.052  1.00 18.20 ? 100 LEU A CG  1 
ATOM   837  C  CD1 . LEU A 1 100 ? 18.417  -19.469 12.154  1.00 21.36 ? 100 LEU A CD1 1 
ATOM   838  C  CD2 . LEU A 1 100 ? 17.276  -19.882 9.955   1.00 19.48 ? 100 LEU A CD2 1 
ATOM   839  N  N   . ASP A 1 101 ? 13.102  -17.665 11.443  1.00 14.11 ? 101 ASP A N   1 
ATOM   840  C  CA  . ASP A 1 101 ? 11.925  -17.238 12.193  1.00 12.91 ? 101 ASP A CA  1 
ATOM   841  C  C   . ASP A 1 101 ? 12.188  -17.139 13.705  1.00 12.05 ? 101 ASP A C   1 
ATOM   842  O  O   . ASP A 1 101 ? 11.479  -16.393 14.374  1.00 15.81 ? 101 ASP A O   1 
ATOM   843  C  CB  . ASP A 1 101 ? 10.753  -18.181 11.894  1.00 13.64 ? 101 ASP A CB  1 
ATOM   844  C  CG  . ASP A 1 101 ? 10.238  -18.136 10.466  1.00 15.99 ? 101 ASP A CG  1 
ATOM   845  O  OD1 . ASP A 1 101 ? 10.589  -17.240 9.677   1.00 14.71 ? 101 ASP A OD1 1 
ATOM   846  O  OD2 . ASP A 1 101 ? 9.409   -19.008 10.144  1.00 22.10 ? 101 ASP A OD2 1 
ATOM   847  N  N   . GLY A 1 102 ? 13.162  -17.899 14.261  1.00 14.32 ? 102 GLY A N   1 
ATOM   848  C  CA  . GLY A 1 102 ? 13.347  -17.877 15.705  1.00 14.24 ? 102 GLY A CA  1 
ATOM   849  C  C   . GLY A 1 102 ? 14.253  -16.760 16.229  1.00 15.62 ? 102 GLY A C   1 
ATOM   850  O  O   . GLY A 1 102 ? 14.618  -16.774 17.408  1.00 14.93 ? 102 GLY A O   1 
ATOM   851  N  N   . GLN A 1 103 ? 14.557  -15.776 15.376  1.00 12.89 ? 103 GLN A N   1 
ATOM   852  C  CA  . GLN A 1 103 ? 15.287  -14.632 15.887  1.00 11.68 ? 103 GLN A CA  1 
ATOM   853  C  C   . GLN A 1 103 ? 14.947  -13.450 15.002  1.00 9.85  ? 103 GLN A C   1 
ATOM   854  O  O   . GLN A 1 103 ? 14.387  -13.614 13.926  1.00 10.82 ? 103 GLN A O   1 
ATOM   855  C  CB  . GLN A 1 103 ? 16.792  -14.876 15.902  1.00 13.08 ? 103 GLN A CB  1 
ATOM   856  C  CG  . GLN A 1 103 ? 17.326  -15.064 14.479  1.00 13.37 ? 103 GLN A CG  1 
ATOM   857  C  CD  . GLN A 1 103 ? 18.650  -15.778 14.485  1.00 16.41 ? 103 GLN A CD  1 
ATOM   858  O  OE1 . GLN A 1 103 ? 18.715  -16.916 14.968  1.00 20.12 ? 103 GLN A OE1 1 
ATOM   859  N  NE2 . GLN A 1 103 ? 19.670  -15.195 13.865  1.00 15.75 ? 103 GLN A NE2 1 
ATOM   860  N  N   . GLY A 1 104 ? 15.301  -12.247 15.481  1.00 8.39  ? 104 GLY A N   1 
ATOM   861  C  CA  . GLY A 1 104 ? 15.058  -11.040 14.698  1.00 9.57  ? 104 GLY A CA  1 
ATOM   862  C  C   . GLY A 1 104 ? 14.589  -9.865  15.532  1.00 8.90  ? 104 GLY A C   1 
ATOM   863  O  O   . GLY A 1 104 ? 14.832  -8.711  15.166  1.00 9.27  ? 104 GLY A O   1 
ATOM   864  N  N   . SER A 1 105 ? 13.878  -10.111 16.616  1.00 8.01  ? 105 SER A N   1 
ATOM   865  C  CA  . SER A 1 105 ? 13.478  -8.989  17.443  1.00 7.85  ? 105 SER A CA  1 
ATOM   866  C  C   . SER A 1 105 ? 14.695  -8.468  18.212  1.00 7.83  ? 105 SER A C   1 
ATOM   867  O  O   . SER A 1 105 ? 15.684  -9.153  18.449  1.00 8.79  ? 105 SER A O   1 
ATOM   868  C  CB  . SER A 1 105 ? 12.367  -9.355  18.365  1.00 8.68  ? 105 SER A CB  1 
ATOM   869  O  OG  . SER A 1 105 ? 12.721  -10.353 19.346  1.00 8.20  ? 105 SER A OG  1 
ATOM   870  N  N   . GLU A 1 106 ? 14.538  -7.224  18.654  1.00 7.99  ? 106 GLU A N   1 
ATOM   871  C  CA  . GLU A 1 106 ? 15.575  -6.536  19.441  1.00 7.94  ? 106 GLU A CA  1 
ATOM   872  C  C   . GLU A 1 106 ? 15.214  -6.702  20.910  1.00 8.46  ? 106 GLU A C   1 
ATOM   873  O  O   . GLU A 1 106 ? 16.015  -7.259  21.643  1.00 8.56  ? 106 GLU A O   1 
ATOM   874  C  CB  . GLU A 1 106 ? 15.601  -5.060  19.038  1.00 7.32  ? 106 GLU A CB  1 
ATOM   875  C  CG  . GLU A 1 106 ? 16.017  -4.906  17.589  1.00 8.10  ? 106 GLU A CG  1 
ATOM   876  C  CD  . GLU A 1 106 ? 16.747  -3.634  17.315  1.00 9.12  ? 106 GLU A CD  1 
ATOM   877  O  OE1 . GLU A 1 106 ? 16.206  -2.557  17.513  1.00 8.15  ? 106 GLU A OE1 1 
ATOM   878  O  OE2 . GLU A 1 106 ? 17.922  -3.725  16.913  1.00 9.76  ? 106 GLU A OE2 1 
ATOM   879  N  N   . HIS A 1 107 ? 14.024  -6.294  21.336  1.00 7.88  ? 107 HIS A N   1 
ATOM   880  C  CA  . HIS A 1 107 ? 13.609  -6.653  22.678  1.00 8.13  ? 107 HIS A CA  1 
ATOM   881  C  C   . HIS A 1 107 ? 13.282  -8.126  22.686  1.00 8.16  ? 107 HIS A C   1 
ATOM   882  O  O   . HIS A 1 107 ? 12.948  -8.736  21.653  1.00 8.51  ? 107 HIS A O   1 
ATOM   883  C  CB  . HIS A 1 107 ? 12.369  -5.841  23.033  1.00 8.26  ? 107 HIS A CB  1 
ATOM   884  C  CG  . HIS A 1 107 ? 12.712  -4.395  23.184  1.00 7.47  ? 107 HIS A CG  1 
ATOM   885  N  ND1 . HIS A 1 107 ? 12.613  -3.490  22.164  1.00 7.73  ? 107 HIS A ND1 1 
ATOM   886  C  CD2 . HIS A 1 107 ? 13.135  -3.701  24.270  1.00 7.08  ? 107 HIS A CD2 1 
ATOM   887  C  CE1 . HIS A 1 107 ? 13.050  -2.295  22.594  1.00 7.33  ? 107 HIS A CE1 1 
ATOM   888  N  NE2 . HIS A 1 107 ? 13.352  -2.393  23.883  1.00 7.77  ? 107 HIS A NE2 1 
ATOM   889  N  N   . THR A 1 108 ? 13.415  -8.682  23.888  1.00 8.63  ? 108 THR A N   1 
ATOM   890  C  CA  . THR A 1 108 ? 12.981  -10.069 24.116  1.00 8.56  ? 108 THR A CA  1 
ATOM   891  C  C   . THR A 1 108 ? 12.022  -10.084 25.300  1.00 8.78  ? 108 THR A C   1 
ATOM   892  O  O   . THR A 1 108 ? 12.027  -9.123  26.062  1.00 8.94  ? 108 THR A O   1 
ATOM   893  C  CB  . THR A 1 108 ? 14.197  -10.975 24.324  1.00 9.43  ? 108 THR A CB  1 
ATOM   894  O  OG1 . THR A 1 108 ? 15.057  -10.514 25.377  1.00 10.13 ? 108 THR A OG1 1 
ATOM   895  C  CG2 . THR A 1 108 ? 15.045  -11.090 23.073  1.00 9.64  ? 108 THR A CG2 1 
ATOM   896  N  N   . VAL A 1 109 ? 11.223  -11.143 25.400  1.00 9.33  ? 109 VAL A N   1 
ATOM   897  C  CA  . VAL A 1 109 ? 10.291  -11.252 26.510  1.00 10.53 ? 109 VAL A CA  1 
ATOM   898  C  C   . VAL A 1 109 ? 10.621  -12.521 27.268  1.00 10.29 ? 109 VAL A C   1 
ATOM   899  O  O   . VAL A 1 109 ? 10.424  -13.599 26.694  1.00 11.08 ? 109 VAL A O   1 
ATOM   900  C  CB  . VAL A 1 109 ? 8.858   -11.274 25.980  1.00 10.36 ? 109 VAL A CB  1 
ATOM   901  C  CG1 . VAL A 1 109 ? 7.850   -11.405 27.113  1.00 13.22 ? 109 VAL A CG1 1 
ATOM   902  C  CG2 . VAL A 1 109 ? 8.567   -10.014 25.167  1.00 12.09 ? 109 VAL A CG2 1 
ATOM   903  N  N   . ASP A 1 110 ? 11.122  -12.381 28.499  1.00 11.12 ? 110 ASP A N   1 
ATOM   904  C  CA  . ASP A 1 110 ? 11.574  -13.573 29.231  1.00 11.97 ? 110 ASP A CA  1 
ATOM   905  C  C   . ASP A 1 110 ? 12.490  -14.418 28.346  1.00 12.00 ? 110 ASP A C   1 
ATOM   906  O  O   . ASP A 1 110 ? 12.374  -15.648 28.277  1.00 12.91 ? 110 ASP A O   1 
ATOM   907  C  CB  . ASP A 1 110 ? 10.366  -14.370 29.749  1.00 14.30 ? 110 ASP A CB  1 
ATOM   908  C  CG  . ASP A 1 110 ? 9.527   -13.599 30.749  1.00 12.62 ? 110 ASP A CG  1 
ATOM   909  O  OD1 . ASP A 1 110 ? 10.105  -12.802 31.457  1.00 15.72 ? 110 ASP A OD1 1 
ATOM   910  O  OD2 . ASP A 1 110 ? 8.298   -13.868 30.772  1.00 18.52 ? 110 ASP A OD2 1 
ATOM   911  N  N   . LYS A 1 111 ? 13.376  -13.716 27.629  1.00 10.56 ? 111 LYS A N   1 
ATOM   912  C  CA  . LYS A 1 111 ? 14.442  -14.191 26.752  1.00 11.05 ? 111 LYS A CA  1 
ATOM   913  C  C   . LYS A 1 111 ? 13.914  -14.728 25.424  1.00 12.17 ? 111 LYS A C   1 
ATOM   914  O  O   . LYS A 1 111 ? 14.701  -15.079 24.561  1.00 13.01 ? 111 LYS A O   1 
ATOM   915  C  CB  . LYS A 1 111 ? 15.366  -15.251 27.392  1.00 13.63 ? 111 LYS A CB  1 
ATOM   916  C  CG  . LYS A 1 111 ? 16.055  -14.699 28.637  1.00 15.34 ? 111 LYS A CG  1 
ATOM   917  C  CD  . LYS A 1 111 ? 17.125  -13.588 28.337  1.00 17.98 ? 111 LYS A CD  1 
ATOM   918  C  CE  . LYS A 1 111 ? 17.845  -12.973 29.520  1.00 22.43 ? 111 LYS A CE  1 
ATOM   919  N  NZ  . LYS A 1 111 ? 18.356  -14.047 30.401  1.00 27.83 ? 111 LYS A NZ  1 
ATOM   920  N  N   . LYS A 1 112 ? 12.603  -14.733 25.199  1.00 9.61  ? 112 LYS A N   1 
ATOM   921  C  CA  . LYS A 1 112 ? 11.990  -15.114 23.945  1.00 9.95  ? 112 LYS A CA  1 
ATOM   922  C  C   . LYS A 1 112 ? 12.298  -14.072 22.863  1.00 10.64 ? 112 LYS A C   1 
ATOM   923  O  O   . LYS A 1 112 ? 12.053  -12.873 23.053  1.00 10.27 ? 112 LYS A O   1 
ATOM   924  C  CB  . LYS A 1 112 ? 10.480  -15.286 24.063  1.00 11.72 ? 112 LYS A CB  1 
ATOM   925  C  CG  . LYS A 1 112 ? 9.845   -15.748 22.750  1.00 13.46 ? 112 LYS A CG  1 
ATOM   926  C  CD  . LYS A 1 112 ? 8.328   -15.789 22.789  1.00 16.77 ? 112 LYS A CD  1 
ATOM   927  C  CE  . LYS A 1 112 ? 7.782   -15.897 21.377  1.00 19.31 ? 112 LYS A CE  1 
ATOM   928  N  NZ  . LYS A 1 112 ? 7.963   -17.252 20.804  1.00 20.64 ? 112 LYS A NZ  1 
ATOM   929  N  N   . LYS A 1 113 ? 12.797  -14.580 21.744  1.00 10.19 ? 113 LYS A N   1 
ATOM   930  C  CA  . LYS A 1 113 ? 13.020  -13.817 20.514  1.00 10.75 ? 113 LYS A CA  1 
ATOM   931  C  C   . LYS A 1 113 ? 11.873  -14.029 19.552  1.00 11.28 ? 113 LYS A C   1 
ATOM   932  O  O   . LYS A 1 113 ? 11.479  -15.153 19.248  1.00 13.86 ? 113 LYS A O   1 
ATOM   933  C  CB  . LYS A 1 113 ? 14.344  -14.225 19.872  1.00 12.66 ? 113 LYS A CB  1 
ATOM   934  C  CG  . LYS A 1 113 ? 15.561  -13.840 20.686  1.00 12.66 ? 113 LYS A CG  1 
ATOM   935  C  CD  . LYS A 1 113 ? 16.818  -14.475 20.103  1.00 15.14 ? 113 LYS A CD  1 
ATOM   936  C  CE  . LYS A 1 113 ? 18.020  -13.753 20.653  1.00 17.31 ? 113 LYS A CE  1 
ATOM   937  N  NZ  . LYS A 1 113 ? 18.860  -14.735 21.347  1.00 25.51 ? 113 LYS A NZ  1 
ATOM   938  N  N   . TYR A 1 114 ? 11.340  -12.932 19.031  1.00 9.80  ? 114 TYR A N   1 
ATOM   939  C  CA  . TYR A 1 114 ? 10.387  -12.978 17.938  1.00 8.61  ? 114 TYR A CA  1 
ATOM   940  C  C   . TYR A 1 114 ? 11.052  -12.876 16.572  1.00 9.18  ? 114 TYR A C   1 
ATOM   941  O  O   . TYR A 1 114 ? 12.248  -12.608 16.473  1.00 9.18  ? 114 TYR A O   1 
ATOM   942  C  CB  . TYR A 1 114 ? 9.334   -11.886 18.133  1.00 10.07 ? 114 TYR A CB  1 
ATOM   943  C  CG  . TYR A 1 114 ? 8.410   -12.126 19.292  1.00 9.27  ? 114 TYR A CG  1 
ATOM   944  C  CD1 . TYR A 1 114 ? 8.689   -11.680 20.581  1.00 9.75  ? 114 TYR A CD1 1 
ATOM   945  C  CD2 . TYR A 1 114 ? 7.214   -12.778 19.053  1.00 10.96 ? 114 TYR A CD2 1 
ATOM   946  C  CE1 . TYR A 1 114 ? 7.827   -11.894 21.640  1.00 11.86 ? 114 TYR A CE1 1 
ATOM   947  C  CE2 . TYR A 1 114 ? 6.321   -12.973 20.106  1.00 12.02 ? 114 TYR A CE2 1 
ATOM   948  C  CZ  . TYR A 1 114 ? 6.614   -12.480 21.368  1.00 13.28 ? 114 TYR A CZ  1 
ATOM   949  O  OH  . TYR A 1 114 ? 5.771   -12.683 22.437  1.00 18.04 ? 114 TYR A OH  1 
ATOM   950  N  N   . ALA A 1 115 ? 10.305  -13.217 15.512  1.00 9.63  ? 115 ALA A N   1 
ATOM   951  C  CA  . ALA A 1 115 ? 10.841  -13.206 14.158  1.00 9.12  ? 115 ALA A CA  1 
ATOM   952  C  C   . ALA A 1 115 ? 11.229  -11.806 13.702  1.00 9.28  ? 115 ALA A C   1 
ATOM   953  O  O   . ALA A 1 115 ? 12.083  -11.686 12.811  1.00 9.82  ? 115 ALA A O   1 
ATOM   954  C  CB  . ALA A 1 115 ? 9.805   -13.830 13.232  1.00 10.71 ? 115 ALA A CB  1 
ATOM   955  N  N   . ALA A 1 116 ? 10.558  -10.784 14.238  1.00 9.19  ? 116 ALA A N   1 
ATOM   956  C  CA  . ALA A 1 116 ? 10.864  -9.435  13.783  1.00 8.45  ? 116 ALA A CA  1 
ATOM   957  C  C   . ALA A 1 116 ? 10.304  -8.485  14.819  1.00 7.97  ? 116 ALA A C   1 
ATOM   958  O  O   . ALA A 1 116 ? 9.557   -8.879  15.747  1.00 8.61  ? 116 ALA A O   1 
ATOM   959  C  CB  . ALA A 1 116 ? 10.272  -9.150  12.398  1.00 9.30  ? 116 ALA A CB  1 
ATOM   960  N  N   . GLU A 1 117 ? 10.667  -7.202  14.662  1.00 7.55  ? 117 GLU A N   1 
ATOM   961  C  CA  . GLU A 1 117 ? 10.155  -6.150  15.537  1.00 7.57  ? 117 GLU A CA  1 
ATOM   962  C  C   . GLU A 1 117 ? 9.940   -4.894  14.694  1.00 7.55  ? 117 GLU A C   1 
ATOM   963  O  O   . GLU A 1 117 ? 10.837  -4.517  13.943  1.00 9.06  ? 117 GLU A O   1 
ATOM   964  C  CB  . GLU A 1 117 ? 11.070  -5.925  16.748  1.00 8.65  ? 117 GLU A CB  1 
ATOM   965  C  CG  . GLU A 1 117 ? 10.576  -4.955  17.802  1.00 9.72  ? 117 GLU A CG  1 
ATOM   966  C  CD  . GLU A 1 117 ? 11.487  -4.921  19.024  1.00 9.11  ? 117 GLU A CD  1 
ATOM   967  O  OE1 . GLU A 1 117 ? 12.145  -5.973  19.315  1.00 8.59  ? 117 GLU A OE1 1 
ATOM   968  O  OE2 . GLU A 1 117 ? 11.503  -3.866  19.720  1.00 9.44  ? 117 GLU A OE2 1 
ATOM   969  N  N   . LEU A 1 118 ? 8.755   -4.323  14.851  1.00 8.05  ? 118 LEU A N   1 
ATOM   970  C  CA  . LEU A 1 118 ? 8.356   -3.083  14.200  1.00 7.22  ? 118 LEU A CA  1 
ATOM   971  C  C   . LEU A 1 118 ? 8.565   -1.952  15.185  1.00 6.91  ? 118 LEU A C   1 
ATOM   972  O  O   . LEU A 1 118 ? 8.119   -2.018  16.311  1.00 7.46  ? 118 LEU A O   1 
ATOM   973  C  CB  . LEU A 1 118 ? 6.882   -3.219  13.780  1.00 8.03  ? 118 LEU A CB  1 
ATOM   974  C  CG  . LEU A 1 118 ? 6.135   -1.902  13.515  1.00 8.09  ? 118 LEU A CG  1 
ATOM   975  C  CD1 . LEU A 1 118 ? 6.687   -1.216  12.281  1.00 8.88  ? 118 LEU A CD1 1 
ATOM   976  C  CD2 . LEU A 1 118 ? 4.670   -2.266  13.239  1.00 9.77  ? 118 LEU A CD2 1 
ATOM   977  N  N   . HIS A 1 119 ? 9.174   -0.869  14.684  1.00 6.64  ? 119 HIS A N   1 
ATOM   978  C  CA  . HIS A 1 119 ? 9.397   0.329   15.486  1.00 6.74  ? 119 HIS A CA  1 
ATOM   979  C  C   . HIS A 1 119 ? 8.739   1.513   14.821  1.00 6.45  ? 119 HIS A C   1 
ATOM   980  O  O   . HIS A 1 119 ? 9.142   1.819   13.681  1.00 7.53  ? 119 HIS A O   1 
ATOM   981  C  CB  . HIS A 1 119 ? 10.907  0.611   15.627  1.00 6.88  ? 119 HIS A CB  1 
ATOM   982  C  CG  . HIS A 1 119 ? 11.574  -0.377  16.506  1.00 6.62  ? 119 HIS A CG  1 
ATOM   983  N  ND1 . HIS A 1 119 ? 12.949  -0.634  16.483  1.00 7.97  ? 119 HIS A ND1 1 
ATOM   984  C  CD2 . HIS A 1 119 ? 11.029  -1.194  17.440  1.00 7.25  ? 119 HIS A CD2 1 
ATOM   985  C  CE1 . HIS A 1 119 ? 13.245  -1.557  17.394  1.00 6.83  ? 119 HIS A CE1 1 
ATOM   986  N  NE2 . HIS A 1 119 ? 12.089  -1.910  17.965  1.00 6.84  ? 119 HIS A NE2 1 
ATOM   987  N  N   . LEU A 1 120 ? 7.746   2.131   15.513  1.00 7.45  ? 120 LEU A N   1 
ATOM   988  C  CA  . LEU A 1 120 ? 7.149   3.370   15.022  1.00 7.33  ? 120 LEU A CA  1 
ATOM   989  C  C   . LEU A 1 120 ? 7.759   4.498   15.832  1.00 7.55  ? 120 LEU A C   1 
ATOM   990  O  O   . LEU A 1 120 ? 7.646   4.565   17.060  1.00 7.00  ? 120 LEU A O   1 
ATOM   991  C  CB  . LEU A 1 120 ? 5.644   3.312   15.175  1.00 8.76  ? 120 LEU A CB  1 
ATOM   992  C  CG  . LEU A 1 120 ? 5.009   2.198   14.325  1.00 8.72  ? 120 LEU A CG  1 
ATOM   993  C  CD1 . LEU A 1 120 ? 4.263   1.216   15.257  1.00 11.98 ? 120 LEU A CD1 1 
ATOM   994  C  CD2 . LEU A 1 120 ? 4.016   2.839   13.331  1.00 10.45 ? 120 LEU A CD2 1 
ATOM   995  N  N   . VAL A 1 121 ? 8.506   5.352   15.128  1.00 7.87  ? 121 VAL A N   1 
ATOM   996  C  CA  . VAL A 1 121 ? 9.318   6.377   15.764  1.00 7.47  ? 121 VAL A CA  1 
ATOM   997  C  C   . VAL A 1 121 ? 8.585   7.711   15.753  1.00 8.35  ? 121 VAL A C   1 
ATOM   998  O  O   . VAL A 1 121 ? 8.088   8.167   14.715  1.00 8.74  ? 121 VAL A O   1 
ATOM   999  C  CB  . VAL A 1 121 ? 10.645  6.490   14.987  1.00 8.43  ? 121 VAL A CB  1 
ATOM   1000 C  CG1 . VAL A 1 121 ? 11.558  7.564   15.580  1.00 8.70  ? 121 VAL A CG1 1 
ATOM   1001 C  CG2 . VAL A 1 121 ? 11.349  5.144   14.827  1.00 8.88  ? 121 VAL A CG2 1 
ATOM   1002 N  N   . HIS A 1 122 ? 8.531   8.327   16.938  1.00 7.86  ? 122 HIS A N   1 
ATOM   1003 C  CA  . HIS A 1 122 ? 7.830   9.593   17.131  1.00 7.93  ? 122 HIS A CA  1 
ATOM   1004 C  C   . HIS A 1 122 ? 8.756   10.564  17.863  1.00 7.86  ? 122 HIS A C   1 
ATOM   1005 O  O   . HIS A 1 122 ? 9.550   10.165  18.705  1.00 9.44  ? 122 HIS A O   1 
ATOM   1006 C  CB  . HIS A 1 122 ? 6.533   9.420   17.957  1.00 8.09  ? 122 HIS A CB  1 
ATOM   1007 C  CG  . HIS A 1 122 ? 5.648   8.276   17.620  1.00 8.12  ? 122 HIS A CG  1 
ATOM   1008 N  ND1 . HIS A 1 122 ? 6.053   6.928   17.842  1.00 8.05  ? 122 HIS A ND1 1 
ATOM   1009 C  CD2 . HIS A 1 122 ? 4.441   8.219   16.995  1.00 8.43  ? 122 HIS A CD2 1 
ATOM   1010 C  CE1 . HIS A 1 122 ? 5.021   6.139   17.490  1.00 8.98  ? 122 HIS A CE1 1 
ATOM   1011 N  NE2 . HIS A 1 122 ? 4.051   6.893   16.911  1.00 9.44  ? 122 HIS A NE2 1 
ATOM   1012 N  N   . TRP A 1 123 ? 8.615   11.861  17.558  1.00 7.73  ? 123 TRP A N   1 
ATOM   1013 C  CA  . TRP A 1 123 ? 9.427   12.873  18.237  1.00 8.98  ? 123 TRP A CA  1 
ATOM   1014 C  C   . TRP A 1 123 ? 8.573   13.873  19.004  1.00 8.83  ? 123 TRP A C   1 
ATOM   1015 O  O   . TRP A 1 123 ? 7.445   14.223  18.615  1.00 9.39  ? 123 TRP A O   1 
ATOM   1016 C  CB  . TRP A 1 123 ? 10.343  13.569  17.225  1.00 9.80  ? 123 TRP A CB  1 
ATOM   1017 C  CG  . TRP A 1 123 ? 9.668   14.265  16.089  1.00 10.23 ? 123 TRP A CG  1 
ATOM   1018 C  CD1 . TRP A 1 123 ? 9.408   13.743  14.858  1.00 10.58 ? 123 TRP A CD1 1 
ATOM   1019 C  CD2 . TRP A 1 123 ? 9.290   15.652  16.007  1.00 10.67 ? 123 TRP A CD2 1 
ATOM   1020 N  NE1 . TRP A 1 123 ? 8.845   14.665  14.045  1.00 12.93 ? 123 TRP A NE1 1 
ATOM   1021 C  CE2 . TRP A 1 123 ? 8.743   15.851  14.725  1.00 11.93 ? 123 TRP A CE2 1 
ATOM   1022 C  CE3 . TRP A 1 123 ? 9.359   16.718  16.902  1.00 11.06 ? 123 TRP A CE3 1 
ATOM   1023 C  CZ2 . TRP A 1 123 ? 8.245   17.075  14.298  1.00 13.10 ? 123 TRP A CZ2 1 
ATOM   1024 C  CZ3 . TRP A 1 123 ? 8.864   17.924  16.469  1.00 12.62 ? 123 TRP A CZ3 1 
ATOM   1025 C  CH2 . TRP A 1 123 ? 8.316   18.101  15.215  1.00 12.71 ? 123 TRP A CH2 1 
ATOM   1026 N  N   . ASN A 1 124 ? 9.161   14.287  20.133  1.00 8.26  ? 124 ASN A N   1 
ATOM   1027 C  CA  . ASN A 1 124 ? 8.496   15.204  21.061  1.00 9.18  ? 124 ASN A CA  1 
ATOM   1028 C  C   . ASN A 1 124 ? 8.299   16.588  20.438  1.00 10.93 ? 124 ASN A C   1 
ATOM   1029 O  O   . ASN A 1 124 ? 9.298   17.268  20.165  1.00 10.82 ? 124 ASN A O   1 
ATOM   1030 C  CB  . ASN A 1 124 ? 9.307   15.233  22.353  1.00 9.92  ? 124 ASN A CB  1 
ATOM   1031 C  CG  . ASN A 1 124 ? 8.582   15.870  23.520  1.00 12.31 ? 124 ASN A CG  1 
ATOM   1032 O  OD1 . ASN A 1 124 ? 7.708   16.730  23.304  1.00 13.06 ? 124 ASN A OD1 1 
ATOM   1033 N  ND2 . ASN A 1 124 ? 8.950   15.423  24.726  1.00 13.12 ? 124 ASN A ND2 1 
ATOM   1034 N  N   . THR A 1 125 ? 7.042   17.036  20.222  1.00 11.85 ? 125 THR A N   1 
ATOM   1035 C  CA  . THR A 1 125 ? 6.792   18.293  19.480  1.00 12.73 ? 125 THR A CA  1 
ATOM   1036 C  C   . THR A 1 125 ? 7.352   19.448  20.322  1.00 12.97 ? 125 THR A C   1 
ATOM   1037 O  O   . THR A 1 125 ? 7.519   20.568  19.697  1.00 13.33 ? 125 THR A O   1 
ATOM   1038 C  CB  . THR A 1 125 ? 5.304   18.450  19.147  1.00 16.00 ? 125 THR A CB  1 
ATOM   1039 O  OG1 . THR A 1 125 ? 4.600   18.531  20.388  1.00 20.21 ? 125 THR A OG1 1 
ATOM   1040 C  CG2 . THR A 1 125 ? 4.826   17.332  18.258  1.00 18.86 ? 125 THR A CG2 1 
ATOM   1041 N  N   . LYS A 1 126 ? 7.609   19.365  21.627  1.00 12.12 ? 127 LYS A N   1 
ATOM   1042 C  CA  . LYS A 1 126 ? 8.185   20.514  22.353  1.00 11.87 ? 127 LYS A CA  1 
ATOM   1043 C  C   . LYS A 1 126 ? 9.565   20.893  21.826  1.00 12.55 ? 127 LYS A C   1 
ATOM   1044 O  O   . LYS A 1 126 ? 9.974   22.020  22.077  1.00 14.68 ? 127 LYS A O   1 
ATOM   1045 C  CB  . LYS A 1 126 ? 8.213   20.274  23.852  1.00 14.16 ? 127 LYS A CB  1 
ATOM   1046 C  CG  . LYS A 1 126 ? 9.294   19.350  24.349  1.00 15.49 ? 127 LYS A CG  1 
ATOM   1047 C  CD  . LYS A 1 126 ? 8.952   19.034  25.801  1.00 24.21 ? 127 LYS A CD  1 
ATOM   1048 C  CE  . LYS A 1 126 ? 10.162  18.723  26.621  1.00 28.72 ? 127 LYS A CE  1 
ATOM   1049 N  NZ  . LYS A 1 126 ? 10.073  19.393  27.952  1.00 35.37 ? 127 LYS A NZ  1 
ATOM   1050 N  N   . TYR A 1 127 ? 10.220  20.037  21.014  1.00 10.99 ? 128 TYR A N   1 
ATOM   1051 C  CA  . TYR A 1 127 ? 11.554  20.375  20.540  1.00 10.45 ? 128 TYR A CA  1 
ATOM   1052 C  C   . TYR A 1 127 ? 11.506  20.775  19.070  1.00 10.44 ? 128 TYR A C   1 
ATOM   1053 O  O   . TYR A 1 127 ? 12.609  21.002  18.523  1.00 11.11 ? 128 TYR A O   1 
ATOM   1054 C  CB  . TYR A 1 127 ? 12.512  19.173  20.693  1.00 11.40 ? 128 TYR A CB  1 
ATOM   1055 C  CG  . TYR A 1 127 ? 12.680  18.818  22.135  1.00 12.13 ? 128 TYR A CG  1 
ATOM   1056 C  CD1 . TYR A 1 127 ? 13.136  19.776  23.056  1.00 13.07 ? 128 TYR A CD1 1 
ATOM   1057 C  CD2 . TYR A 1 127 ? 12.361  17.558  22.633  1.00 11.54 ? 128 TYR A CD2 1 
ATOM   1058 C  CE1 . TYR A 1 127 ? 13.245  19.466  24.398  1.00 13.20 ? 128 TYR A CE1 1 
ATOM   1059 C  CE2 . TYR A 1 127 ? 12.470  17.245  23.967  1.00 13.13 ? 128 TYR A CE2 1 
ATOM   1060 C  CZ  . TYR A 1 127 ? 12.944  18.206  24.845  1.00 12.99 ? 128 TYR A CZ  1 
ATOM   1061 O  OH  . TYR A 1 127 ? 13.106  17.943  26.174  1.00 14.19 ? 128 TYR A OH  1 
ATOM   1062 N  N   . GLY A 1 128 ? 10.305  20.895  18.473  1.00 11.48 ? 129 GLY A N   1 
ATOM   1063 C  CA  . GLY A 1 128 ? 10.228  21.676  17.237  1.00 10.63 ? 129 GLY A CA  1 
ATOM   1064 C  C   . GLY A 1 128 ? 10.556  20.896  15.963  1.00 11.59 ? 129 GLY A C   1 
ATOM   1065 O  O   . GLY A 1 128 ? 9.863   21.051  14.953  1.00 11.72 ? 129 GLY A O   1 
ATOM   1066 N  N   A ASP A 1 129 ? 11.657  20.116  15.963  0.50 10.51 ? 130 ASP A N   1 
ATOM   1067 N  N   B ASP A 1 129 ? 11.543  20.006  16.025  0.50 11.42 ? 130 ASP A N   1 
ATOM   1068 C  CA  A ASP A 1 129 ? 12.004  19.257  14.828  0.50 10.42 ? 130 ASP A CA  1 
ATOM   1069 C  CA  B ASP A 1 129 ? 11.611  19.035  14.950  0.50 11.76 ? 130 ASP A CA  1 
ATOM   1070 C  C   A ASP A 1 129 ? 12.520  17.914  15.332  0.50 11.44 ? 130 ASP A C   1 
ATOM   1071 C  C   B ASP A 1 129 ? 12.490  17.871  15.357  0.50 12.31 ? 130 ASP A C   1 
ATOM   1072 O  O   A ASP A 1 129 ? 12.904  17.805  16.497  0.50 11.71 ? 130 ASP A O   1 
ATOM   1073 O  O   B ASP A 1 129 ? 13.171  17.882  16.392  0.50 11.97 ? 130 ASP A O   1 
ATOM   1074 C  CB  A ASP A 1 129 ? 12.897  19.957  13.788  0.50 10.61 ? 130 ASP A CB  1 
ATOM   1075 C  CB  B ASP A 1 129 ? 12.161  19.629  13.664  0.50 13.88 ? 130 ASP A CB  1 
ATOM   1076 C  CG  A ASP A 1 129 ? 14.337  20.241  14.159  0.50 10.96 ? 130 ASP A CG  1 
ATOM   1077 C  CG  B ASP A 1 129 ? 13.602  20.072  13.788  0.50 13.30 ? 130 ASP A CG  1 
ATOM   1078 O  OD1 A ASP A 1 129 ? 15.143  19.292  14.286  0.50 12.34 ? 130 ASP A OD1 1 
ATOM   1079 O  OD1 B ASP A 1 129 ? 14.234  19.735  14.804  0.50 15.60 ? 130 ASP A OD1 1 
ATOM   1080 O  OD2 A ASP A 1 129 ? 14.639  21.420  14.294  0.50 12.36 ? 130 ASP A OD2 1 
ATOM   1081 O  OD2 B ASP A 1 129 ? 14.084  20.747  12.859  0.50 16.99 ? 130 ASP A OD2 1 
ATOM   1082 N  N   . TYR A 1 130 ? 12.477  16.898  14.453  1.00 11.78 ? 131 TYR A N   1 
ATOM   1083 C  CA  . TYR A 1 130 ? 13.006  15.580  14.739  1.00 11.16 ? 131 TYR A CA  1 
ATOM   1084 C  C   . TYR A 1 130 ? 14.486  15.636  15.105  1.00 11.36 ? 131 TYR A C   1 
ATOM   1085 O  O   . TYR A 1 130 ? 14.937  14.964  16.003  1.00 10.61 ? 131 TYR A O   1 
ATOM   1086 C  CB  . TYR A 1 130 ? 12.730  14.722  13.509  1.00 12.45 ? 131 TYR A CB  1 
ATOM   1087 C  CG  . TYR A 1 130 ? 13.170  13.298  13.544  1.00 10.39 ? 131 TYR A CG  1 
ATOM   1088 C  CD1 . TYR A 1 130 ? 13.123  12.509  14.693  1.00 11.18 ? 131 TYR A CD1 1 
ATOM   1089 C  CD2 . TYR A 1 130 ? 13.454  12.707  12.308  1.00 11.86 ? 131 TYR A CD2 1 
ATOM   1090 C  CE1 . TYR A 1 130 ? 13.480  11.177  14.640  1.00 11.85 ? 131 TYR A CE1 1 
ATOM   1091 C  CE2 . TYR A 1 130 ? 13.850  11.379  12.260  1.00 13.05 ? 131 TYR A CE2 1 
ATOM   1092 C  CZ  . TYR A 1 130 ? 13.806  10.610  13.417  1.00 12.18 ? 131 TYR A CZ  1 
ATOM   1093 O  OH  . TYR A 1 130 ? 14.138  9.283   13.401  1.00 13.79 ? 131 TYR A OH  1 
ATOM   1094 N  N   . GLY A 1 131 ? 15.268  16.398  14.322  1.00 10.89 ? 132 GLY A N   1 
ATOM   1095 C  CA  . GLY A 1 131 ? 16.675  16.445  14.564  1.00 11.82 ? 132 GLY A CA  1 
ATOM   1096 C  C   . GLY A 1 131 ? 17.033  16.997  15.944  1.00 11.47 ? 132 GLY A C   1 
ATOM   1097 O  O   . GLY A 1 131 ? 17.929  16.442  16.624  1.00 14.21 ? 132 GLY A O   1 
ATOM   1098 N  N   A LYS A 1 132 ? 16.325  18.064  16.375  0.50 11.10 ? 133 LYS A N   1 
ATOM   1099 N  N   B LYS A 1 132 ? 16.332  18.050  16.377  0.50 11.00 ? 133 LYS A N   1 
ATOM   1100 C  CA  A LYS A 1 132 ? 16.488  18.627  17.712  0.50 12.92 ? 133 LYS A CA  1 
ATOM   1101 C  CA  B LYS A 1 132 ? 16.577  18.535  17.720  0.50 12.69 ? 133 LYS A CA  1 
ATOM   1102 C  C   A LYS A 1 132 ? 16.054  17.609  18.781  0.50 12.21 ? 133 LYS A C   1 
ATOM   1103 C  C   B LYS A 1 132 ? 16.120  17.499  18.755  0.50 11.91 ? 133 LYS A C   1 
ATOM   1104 O  O   A LYS A 1 132 ? 16.716  17.441  19.807  0.50 13.32 ? 133 LYS A O   1 
ATOM   1105 O  O   B LYS A 1 132 ? 16.824  17.218  19.726  0.50 12.43 ? 133 LYS A O   1 
ATOM   1106 C  CB  A LYS A 1 132 ? 15.719  19.947  17.862  0.50 13.12 ? 133 LYS A CB  1 
ATOM   1107 C  CB  B LYS A 1 132 ? 15.843  19.854  17.932  0.50 12.62 ? 133 LYS A CB  1 
ATOM   1108 C  CG  A LYS A 1 132 ? 16.393  21.212  17.334  0.50 15.90 ? 133 LYS A CG  1 
ATOM   1109 C  CG  B LYS A 1 132 ? 15.970  20.367  19.349  0.50 15.35 ? 133 LYS A CG  1 
ATOM   1110 C  CD  A LYS A 1 132 ? 17.695  21.530  18.073  0.50 18.25 ? 133 LYS A CD  1 
ATOM   1111 C  CD  B LYS A 1 132 ? 17.289  21.037  19.528  0.50 17.59 ? 133 LYS A CD  1 
ATOM   1112 C  CE  A LYS A 1 132 ? 17.589  22.560  19.195  0.50 18.71 ? 133 LYS A CE  1 
ATOM   1113 C  CE  B LYS A 1 132 ? 17.180  22.105  20.592  0.50 18.41 ? 133 LYS A CE  1 
ATOM   1114 N  NZ  A LYS A 1 132 ? 18.744  23.491  19.211  0.50 20.61 ? 133 LYS A NZ  1 
ATOM   1115 N  NZ  B LYS A 1 132 ? 17.849  21.624  21.824  0.50 24.34 ? 133 LYS A NZ  1 
ATOM   1116 N  N   . ALA A 1 133 ? 14.944  16.906  18.521  1.00 11.35 ? 134 ALA A N   1 
ATOM   1117 C  CA  . ALA A 1 133 ? 14.433  15.932  19.482  1.00 11.39 ? 134 ALA A CA  1 
ATOM   1118 C  C   . ALA A 1 133 ? 15.428  14.789  19.665  1.00 11.18 ? 134 ALA A C   1 
ATOM   1119 O  O   . ALA A 1 133 ? 15.535  14.238  20.761  1.00 11.81 ? 134 ALA A O   1 
ATOM   1120 C  CB  . ALA A 1 133 ? 13.092  15.406  19.008  1.00 10.29 ? 134 ALA A CB  1 
ATOM   1121 N  N   . GLN A 1 134 ? 16.187  14.407  18.615  1.00 11.90 ? 135 GLN A N   1 
ATOM   1122 C  CA  . GLN A 1 134 ? 17.137  13.295  18.693  1.00 12.45 ? 135 GLN A CA  1 
ATOM   1123 C  C   . GLN A 1 134 ? 18.270  13.584  19.680  1.00 13.47 ? 135 GLN A C   1 
ATOM   1124 O  O   . GLN A 1 134 ? 19.012  12.647  20.028  1.00 16.41 ? 135 GLN A O   1 
ATOM   1125 C  CB  . GLN A 1 134 ? 17.758  13.020  17.302  1.00 14.84 ? 135 GLN A CB  1 
ATOM   1126 C  CG  . GLN A 1 134 ? 16.811  12.388  16.263  1.00 14.05 ? 135 GLN A CG  1 
ATOM   1127 C  CD  . GLN A 1 134 ? 17.340  12.548  14.852  1.00 15.22 ? 135 GLN A CD  1 
ATOM   1128 O  OE1 . GLN A 1 134 ? 18.556  12.516  14.601  1.00 20.07 ? 135 GLN A OE1 1 
ATOM   1129 N  NE2 . GLN A 1 134 ? 16.424  12.786  13.926  1.00 14.96 ? 135 GLN A NE2 1 
ATOM   1130 N  N   . GLN A 1 135 ? 18.380  14.835  20.146  1.00 13.65 ? 136 GLN A N   1 
ATOM   1131 C  CA  . GLN A 1 135 ? 19.446  15.239  21.041  1.00 15.73 ? 136 GLN A CA  1 
ATOM   1132 C  C   . GLN A 1 135 ? 18.953  15.394  22.480  1.00 14.63 ? 136 GLN A C   1 
ATOM   1133 O  O   . GLN A 1 135 ? 19.661  15.926  23.333  1.00 19.08 ? 136 GLN A O   1 
ATOM   1134 C  CB  . GLN A 1 135 ? 20.135  16.506  20.526  1.00 20.20 ? 136 GLN A CB  1 
ATOM   1135 C  CG  . GLN A 1 135 ? 20.777  16.283  19.146  1.00 25.28 ? 136 GLN A CG  1 
ATOM   1136 C  CD  . GLN A 1 135 ? 21.712  15.090  19.130  1.00 32.55 ? 136 GLN A CD  1 
ATOM   1137 O  OE1 . GLN A 1 135 ? 22.450  14.817  20.092  1.00 36.90 ? 136 GLN A OE1 1 
ATOM   1138 N  NE2 . GLN A 1 135 ? 21.644  14.312  18.053  1.00 37.33 ? 136 GLN A NE2 1 
ATOM   1139 N  N   . GLN A 1 136 ? 17.687  15.045  22.771  1.00 11.95 ? 137 GLN A N   1 
ATOM   1140 C  CA  . GLN A 1 136 ? 17.178  15.342  24.103  1.00 12.71 ? 137 GLN A CA  1 
ATOM   1141 C  C   . GLN A 1 136 ? 16.832  14.049  24.814  1.00 13.61 ? 137 GLN A C   1 
ATOM   1142 O  O   . GLN A 1 136 ? 16.437  13.068  24.197  1.00 12.74 ? 137 GLN A O   1 
ATOM   1143 C  CB  . GLN A 1 136 ? 15.878  16.118  23.999  1.00 13.38 ? 137 GLN A CB  1 
ATOM   1144 C  CG  . GLN A 1 136 ? 15.978  17.351  23.115  1.00 17.95 ? 137 GLN A CG  1 
ATOM   1145 C  CD  . GLN A 1 136 ? 17.027  18.308  23.593  1.00 18.93 ? 137 GLN A CD  1 
ATOM   1146 O  OE1 . GLN A 1 136 ? 17.165  18.514  24.793  1.00 18.90 ? 137 GLN A OE1 1 
ATOM   1147 N  NE2 . GLN A 1 136 ? 17.715  18.938  22.639  1.00 26.13 ? 137 GLN A NE2 1 
ATOM   1148 N  N   . PRO A 1 137 ? 16.908  14.015  26.157  1.00 12.70 ? 138 PRO A N   1 
ATOM   1149 C  CA  . PRO A 1 137 ? 16.669  12.781  26.889  1.00 12.90 ? 138 PRO A CA  1 
ATOM   1150 C  C   . PRO A 1 137 ? 15.269  12.188  26.757  1.00 11.88 ? 138 PRO A C   1 
ATOM   1151 O  O   . PRO A 1 137 ? 15.095  10.969  26.863  1.00 14.10 ? 138 PRO A O   1 
ATOM   1152 C  CB  . PRO A 1 137 ? 17.044  13.106  28.342  1.00 15.24 ? 138 PRO A CB  1 
ATOM   1153 C  CG  . PRO A 1 137 ? 17.223  14.589  28.377  1.00 18.10 ? 138 PRO A CG  1 
ATOM   1154 C  CD  . PRO A 1 137 ? 17.374  15.148  26.974  1.00 15.57 ? 138 PRO A CD  1 
ATOM   1155 N  N   . ASP A 1 138 ? 14.271  13.049  26.509  1.00 11.18 ? 139 ASP A N   1 
ATOM   1156 C  CA  . ASP A 1 138 ? 12.870  12.681  26.238  1.00 11.15 ? 139 ASP A CA  1 
ATOM   1157 C  C   . ASP A 1 138 ? 12.432  13.132  24.847  1.00 9.18  ? 139 ASP A C   1 
ATOM   1158 O  O   . ASP A 1 138 ? 11.285  13.521  24.593  1.00 11.74 ? 139 ASP A O   1 
ATOM   1159 C  CB  . ASP A 1 138 ? 11.920  13.297  27.275  1.00 11.54 ? 139 ASP A CB  1 
ATOM   1160 C  CG  . ASP A 1 138 ? 12.005  14.818  27.287  1.00 12.38 ? 139 ASP A CG  1 
ATOM   1161 O  OD1 . ASP A 1 138 ? 12.964  15.386  26.752  1.00 13.49 ? 139 ASP A OD1 1 
ATOM   1162 O  OD2 . ASP A 1 138 ? 11.116  15.420  27.937  1.00 15.43 ? 139 ASP A OD2 1 
ATOM   1163 N  N   . GLY A 1 139 ? 13.386  13.040  23.932  1.00 9.29  ? 140 GLY A N   1 
ATOM   1164 C  CA  . GLY A 1 139 ? 13.116  13.501  22.590  1.00 8.70  ? 140 GLY A CA  1 
ATOM   1165 C  C   . GLY A 1 139 ? 12.229  12.565  21.737  1.00 7.97  ? 140 GLY A C   1 
ATOM   1166 O  O   . GLY A 1 139 ? 11.512  13.055  20.877  1.00 8.05  ? 140 GLY A O   1 
ATOM   1167 N  N   . LEU A 1 140 ? 12.403  11.240  21.900  1.00 7.99  ? 141 LEU A N   1 
ATOM   1168 C  CA  . LEU A 1 140 ? 11.710  10.318  21.031  1.00 8.36  ? 141 LEU A CA  1 
ATOM   1169 C  C   . LEU A 1 140 ? 10.903  9.340   21.862  1.00 7.82  ? 141 LEU A C   1 
ATOM   1170 O  O   . LEU A 1 140 ? 11.217  9.048   23.011  1.00 8.18  ? 141 LEU A O   1 
ATOM   1171 C  CB  . LEU A 1 140 ? 12.701  9.516   20.171  1.00 9.31  ? 141 LEU A CB  1 
ATOM   1172 C  CG  . LEU A 1 140 ? 13.683  10.295  19.306  1.00 10.44 ? 141 LEU A CG  1 
ATOM   1173 C  CD1 . LEU A 1 140 ? 14.481  9.300   18.424  1.00 11.72 ? 141 LEU A CD1 1 
ATOM   1174 C  CD2 . LEU A 1 140 ? 13.037  11.346  18.403  1.00 11.08 ? 141 LEU A CD2 1 
ATOM   1175 N  N   . ALA A 1 141 ? 9.843   8.859   21.229  1.00 8.08  ? 142 ALA A N   1 
ATOM   1176 C  CA  . ALA A 1 141 ? 9.096   7.749   21.775  1.00 7.72  ? 142 ALA A CA  1 
ATOM   1177 C  C   . ALA A 1 141 ? 8.955   6.756   20.649  1.00 7.07  ? 142 ALA A C   1 
ATOM   1178 O  O   . ALA A 1 141 ? 8.520   7.087   19.545  1.00 7.66  ? 142 ALA A O   1 
ATOM   1179 C  CB  . ALA A 1 141 ? 7.734   8.219   22.273  1.00 8.27  ? 142 ALA A CB  1 
ATOM   1180 N  N   . VAL A 1 142 ? 9.423   5.516   20.948  1.00 7.18  ? 143 VAL A N   1 
ATOM   1181 C  CA  . VAL A 1 142 ? 9.347   4.480   19.928  1.00 7.41  ? 143 VAL A CA  1 
ATOM   1182 C  C   . VAL A 1 142 ? 8.371   3.416   20.433  1.00 7.17  ? 143 VAL A C   1 
ATOM   1183 O  O   . VAL A 1 142 ? 8.517   2.864   21.539  1.00 8.25  ? 143 VAL A O   1 
ATOM   1184 C  CB  . VAL A 1 142 ? 10.705  3.829   19.559  1.00 7.04  ? 143 VAL A CB  1 
ATOM   1185 C  CG1 . VAL A 1 142 ? 10.527  2.815   18.422  1.00 7.95  ? 143 VAL A CG1 1 
ATOM   1186 C  CG2 . VAL A 1 142 ? 11.687  4.919   19.108  1.00 8.26  ? 143 VAL A CG2 1 
ATOM   1187 N  N   . LEU A 1 143 ? 7.361   3.175   19.596  1.00 7.16  ? 144 LEU A N   1 
ATOM   1188 C  CA  . LEU A 1 143 ? 6.380   2.125   19.839  1.00 7.53  ? 144 LEU A CA  1 
ATOM   1189 C  C   . LEU A 1 143 ? 6.877   0.855   19.145  1.00 8.12  ? 144 LEU A C   1 
ATOM   1190 O  O   . LEU A 1 143 ? 7.048   0.806   17.954  1.00 8.51  ? 144 LEU A O   1 
ATOM   1191 C  CB  . LEU A 1 143 ? 5.021   2.601   19.312  1.00 9.45  ? 144 LEU A CB  1 
ATOM   1192 C  CG  . LEU A 1 143 ? 3.846   1.637   19.492  1.00 10.00 ? 144 LEU A CG  1 
ATOM   1193 C  CD1 . LEU A 1 143 ? 3.550   1.366   20.935  1.00 11.93 ? 144 LEU A CD1 1 
ATOM   1194 C  CD2 . LEU A 1 143 ? 2.631   2.265   18.832  1.00 11.59 ? 144 LEU A CD2 1 
ATOM   1195 N  N   . GLY A 1 144 ? 7.141   -0.198  19.944  1.00 7.30  ? 145 GLY A N   1 
ATOM   1196 C  CA  . GLY A 1 144 ? 7.691   -1.462  19.477  1.00 7.40  ? 145 GLY A CA  1 
ATOM   1197 C  C   . GLY A 1 144 ? 6.617   -2.537  19.450  1.00 7.44  ? 145 GLY A C   1 
ATOM   1198 O  O   . GLY A 1 144 ? 5.876   -2.644  20.434  1.00 8.63  ? 145 GLY A O   1 
ATOM   1199 N  N   . ILE A 1 145 ? 6.574   -3.267  18.348  1.00 6.95  ? 146 ILE A N   1 
ATOM   1200 C  CA  . ILE A 1 145 ? 5.569   -4.307  18.196  1.00 7.92  ? 146 ILE A CA  1 
ATOM   1201 C  C   . ILE A 1 145 ? 6.282   -5.545  17.698  1.00 7.60  ? 146 ILE A C   1 
ATOM   1202 O  O   . ILE A 1 145 ? 6.964   -5.494  16.683  1.00 8.18  ? 146 ILE A O   1 
ATOM   1203 C  CB  . ILE A 1 145 ? 4.467   -3.819  17.236  1.00 7.78  ? 146 ILE A CB  1 
ATOM   1204 C  CG1 . ILE A 1 145 ? 3.853   -2.526  17.731  1.00 10.29 ? 146 ILE A CG1 1 
ATOM   1205 C  CG2 . ILE A 1 145 ? 3.408   -4.894  16.957  1.00 10.31 ? 146 ILE A CG2 1 
ATOM   1206 C  CD1 . ILE A 1 145 ? 2.735   -1.961  16.790  1.00 10.29 ? 146 ILE A CD1 1 
ATOM   1207 N  N   . PHE A 1 146 ? 6.112   -6.657  18.398  1.00 7.49  ? 147 PHE A N   1 
ATOM   1208 C  CA  . PHE A 1 146 ? 6.698   -7.916  17.968  1.00 7.45  ? 147 PHE A CA  1 
ATOM   1209 C  C   . PHE A 1 146 ? 5.928   -8.541  16.801  1.00 8.25  ? 147 PHE A C   1 
ATOM   1210 O  O   . PHE A 1 146 ? 4.712   -8.418  16.734  1.00 9.15  ? 147 PHE A O   1 
ATOM   1211 C  CB  . PHE A 1 146 ? 6.689   -8.890  19.140  1.00 8.24  ? 147 PHE A CB  1 
ATOM   1212 C  CG  . PHE A 1 146 ? 7.562   -8.429  20.274  1.00 7.10  ? 147 PHE A CG  1 
ATOM   1213 C  CD1 . PHE A 1 146 ? 8.930   -8.283  20.086  1.00 7.58  ? 147 PHE A CD1 1 
ATOM   1214 C  CD2 . PHE A 1 146 ? 7.033   -8.169  21.514  1.00 7.42  ? 147 PHE A CD2 1 
ATOM   1215 C  CE1 . PHE A 1 146 ? 9.713   -7.875  21.169  1.00 7.20  ? 147 PHE A CE1 1 
ATOM   1216 C  CE2 . PHE A 1 146 ? 7.807   -7.766  22.588  1.00 7.04  ? 147 PHE A CE2 1 
ATOM   1217 C  CZ  . PHE A 1 146 ? 9.166   -7.630  22.418  1.00 7.52  ? 147 PHE A CZ  1 
ATOM   1218 N  N   . LEU A 1 147 ? 6.643   -9.223  15.929  1.00 7.89  ? 148 LEU A N   1 
ATOM   1219 C  CA  . LEU A 1 147 ? 6.045   -10.016 14.838  1.00 9.01  ? 148 LEU A CA  1 
ATOM   1220 C  C   . LEU A 1 147 ? 6.374   -11.472 15.097  1.00 9.48  ? 148 LEU A C   1 
ATOM   1221 O  O   . LEU A 1 147 ? 7.517   -11.834 15.230  1.00 9.14  ? 148 LEU A O   1 
ATOM   1222 C  CB  . LEU A 1 147 ? 6.640   -9.604  13.478  1.00 8.87  ? 148 LEU A CB  1 
ATOM   1223 C  CG  . LEU A 1 147 ? 6.107   -8.322  12.822  1.00 8.69  ? 148 LEU A CG  1 
ATOM   1224 C  CD1 . LEU A 1 147 ? 6.414   -7.082  13.668  1.00 9.84  ? 148 LEU A CD1 1 
ATOM   1225 C  CD2 . LEU A 1 147 ? 6.768   -8.161  11.457  1.00 10.30 ? 148 LEU A CD2 1 
ATOM   1226 N  N   . LYS A 1 148 ? 5.308   -12.280 15.081  1.00 10.97 ? 149 LYS A N   1 
ATOM   1227 C  CA  . LYS A 1 148 ? 5.480   -13.731 15.053  1.00 12.35 ? 149 LYS A CA  1 
ATOM   1228 C  C   . LYS A 1 148 ? 4.959   -14.254 13.718  1.00 13.12 ? 149 LYS A C   1 
ATOM   1229 O  O   . LYS A 1 148 ? 4.126   -13.625 13.053  1.00 13.16 ? 149 LYS A O   1 
ATOM   1230 C  CB  . LYS A 1 148 ? 4.759   -14.363 16.240  1.00 14.83 ? 149 LYS A CB  1 
ATOM   1231 C  CG  . LYS A 1 148 ? 3.245   -14.317 16.192  1.00 16.67 ? 149 LYS A CG  1 
ATOM   1232 C  CD  . LYS A 1 148 ? 2.688   -15.018 17.440  1.00 22.43 ? 149 LYS A CD  1 
ATOM   1233 C  CE  . LYS A 1 148 ? 1.272   -15.498 17.249  1.00 29.94 ? 149 LYS A CE  1 
ATOM   1234 N  NZ  . LYS A 1 148 ? 0.606   -15.646 18.570  1.00 32.04 ? 149 LYS A NZ  1 
ATOM   1235 N  N   . VAL A 1 149 ? 5.477   -15.403 13.291  1.00 12.49 ? 150 VAL A N   1 
ATOM   1236 C  CA  . VAL A 1 149 ? 5.090   -16.026 12.043  1.00 13.36 ? 150 VAL A CA  1 
ATOM   1237 C  C   . VAL A 1 149 ? 3.891   -16.938 12.264  1.00 14.22 ? 150 VAL A C   1 
ATOM   1238 O  O   . VAL A 1 149 ? 3.944   -17.854 13.088  1.00 16.13 ? 150 VAL A O   1 
ATOM   1239 C  CB  . VAL A 1 149 ? 6.283   -16.795 11.440  1.00 13.33 ? 150 VAL A CB  1 
ATOM   1240 C  CG1 . VAL A 1 149 ? 5.933   -17.574 10.177  1.00 15.23 ? 150 VAL A CG1 1 
ATOM   1241 C  CG2 . VAL A 1 149 ? 7.432   -15.841 11.150  1.00 14.75 ? 150 VAL A CG2 1 
ATOM   1242 N  N   . GLY A 1 150 ? 2.825   -16.646 11.533  1.00 14.56 ? 151 GLY A N   1 
ATOM   1243 C  CA  . GLY A 1 150 ? 1.604   -17.429 11.571  1.00 14.45 ? 151 GLY A CA  1 
ATOM   1244 C  C   . GLY A 1 150 ? 0.744   -16.984 10.404  1.00 12.74 ? 151 GLY A C   1 
ATOM   1245 O  O   . GLY A 1 150 ? 1.142   -17.133 9.273   1.00 14.05 ? 151 GLY A O   1 
ATOM   1246 N  N   A SER A 1 151 ? -0.423  -16.418 10.711  0.50 13.51 ? 152 SER A N   1 
ATOM   1247 N  N   B SER A 1 151 ? -0.428  -16.437 10.712  0.50 13.46 ? 152 SER A N   1 
ATOM   1248 C  CA  A SER A 1 151 ? -1.345  -15.886 9.709   0.50 14.15 ? 152 SER A CA  1 
ATOM   1249 C  CA  B SER A 1 151 ? -1.281  -15.899 9.660   0.50 14.11 ? 152 SER A CA  1 
ATOM   1250 C  C   A SER A 1 151 ? -0.795  -14.574 9.162   0.50 13.91 ? 152 SER A C   1 
ATOM   1251 C  C   B SER A 1 151 ? -0.630  -14.647 9.085   0.50 13.88 ? 152 SER A C   1 
ATOM   1252 O  O   A SER A 1 151 ? -0.197  -13.809 9.931   0.50 14.13 ? 152 SER A O   1 
ATOM   1253 O  O   B SER A 1 151 ? 0.193   -13.989 9.730   0.50 14.34 ? 152 SER A O   1 
ATOM   1254 C  CB  A SER A 1 151 ? -2.678  -15.642 10.346  0.50 15.72 ? 152 SER A CB  1 
ATOM   1255 C  CB  B SER A 1 151 ? -2.677  -15.619 10.159  0.50 15.73 ? 152 SER A CB  1 
ATOM   1256 O  OG  A SER A 1 151 ? -3.224  -16.856 10.823  0.50 18.20 ? 152 SER A OG  1 
ATOM   1257 O  OG  B SER A 1 151 ? -2.669  -14.731 11.266  0.50 17.69 ? 152 SER A OG  1 
ATOM   1258 N  N   . ALA A 1 152 ? -1.021  -14.305 7.860   1.00 14.19 ? 153 ALA A N   1 
ATOM   1259 C  CA  . ALA A 1 152 ? -0.560  -13.067 7.245   1.00 13.30 ? 153 ALA A CA  1 
ATOM   1260 C  C   . ALA A 1 152 ? -1.214  -11.865 7.904   1.00 14.10 ? 153 ALA A C   1 
ATOM   1261 O  O   . ALA A 1 152 ? -2.330  -11.910 8.431   1.00 15.11 ? 153 ALA A O   1 
ATOM   1262 C  CB  . ALA A 1 152 ? -0.853  -13.064 5.757   1.00 15.47 ? 153 ALA A CB  1 
ATOM   1263 N  N   . LYS A 1 153 ? -0.472  -10.745 7.871   1.00 14.03 ? 154 LYS A N   1 
ATOM   1264 C  CA  . LYS A 1 153 ? -1.012  -9.482  8.354   1.00 14.60 ? 154 LYS A CA  1 
ATOM   1265 C  C   . LYS A 1 153 ? -1.472  -8.711  7.128   1.00 14.78 ? 154 LYS A C   1 
ATOM   1266 O  O   . LYS A 1 153 ? -0.649  -8.270  6.338   1.00 12.09 ? 154 LYS A O   1 
ATOM   1267 C  CB  . LYS A 1 153 ? 0.086   -8.692  9.076   1.00 13.68 ? 154 LYS A CB  1 
ATOM   1268 C  CG  . LYS A 1 153 ? -0.416  -7.464  9.833   1.00 14.73 ? 154 LYS A CG  1 
ATOM   1269 C  CD  . LYS A 1 153 ? -1.281  -7.855  10.994  1.00 13.84 ? 154 LYS A CD  1 
ATOM   1270 C  CE  . LYS A 1 153 ? -1.470  -6.681  11.941  1.00 15.28 ? 154 LYS A CE  1 
ATOM   1271 N  NZ  . LYS A 1 153 ? -2.488  -7.050  12.949  1.00 17.31 ? 154 LYS A NZ  1 
ATOM   1272 N  N   . PRO A 1 154 ? -2.799  -8.568  6.869   1.00 14.45 ? 155 PRO A N   1 
ATOM   1273 C  CA  . PRO A 1 154 ? -3.223  -7.962  5.586   1.00 16.41 ? 155 PRO A CA  1 
ATOM   1274 C  C   . PRO A 1 154 ? -2.695  -6.542  5.431   1.00 16.24 ? 155 PRO A C   1 
ATOM   1275 O  O   . PRO A 1 154 ? -2.218  -6.237  4.342   1.00 17.36 ? 155 PRO A O   1 
ATOM   1276 C  CB  . PRO A 1 154 ? -4.759  -7.960  5.701   1.00 19.14 ? 155 PRO A CB  1 
ATOM   1277 C  CG  . PRO A 1 154 ? -5.034  -9.084  6.678   1.00 20.86 ? 155 PRO A CG  1 
ATOM   1278 C  CD  . PRO A 1 154 ? -3.920  -9.061  7.692   1.00 18.13 ? 155 PRO A CD  1 
ATOM   1279 N  N   . GLY A 1 155 ? -2.589  -5.804  6.540   1.00 14.96 ? 156 GLY A N   1 
ATOM   1280 C  CA  . GLY A 1 155 ? -2.137  -4.419  6.542   1.00 15.54 ? 156 GLY A CA  1 
ATOM   1281 C  C   . GLY A 1 155 ? -0.649  -4.260  6.249   1.00 16.89 ? 156 GLY A C   1 
ATOM   1282 O  O   . GLY A 1 155 ? -0.201  -3.149  5.964   1.00 18.92 ? 156 GLY A O   1 
ATOM   1283 N  N   . LEU A 1 156 ? 0.101   -5.355  6.274   1.00 13.47 ? 157 LEU A N   1 
ATOM   1284 C  CA  . LEU A 1 156 ? 1.523   -5.344  5.925   1.00 13.79 ? 157 LEU A CA  1 
ATOM   1285 C  C   . LEU A 1 156 ? 1.800   -5.575  4.444   1.00 13.23 ? 157 LEU A C   1 
ATOM   1286 O  O   . LEU A 1 156 ? 2.882   -5.315  3.939   1.00 13.15 ? 157 LEU A O   1 
ATOM   1287 C  CB  . LEU A 1 156 ? 2.250   -6.406  6.773   1.00 13.24 ? 157 LEU A CB  1 
ATOM   1288 C  CG  . LEU A 1 156 ? 3.772   -6.512  6.649   1.00 13.24 ? 157 LEU A CG  1 
ATOM   1289 C  CD1 . LEU A 1 156 ? 4.521   -5.206  7.006   1.00 11.60 ? 157 LEU A CD1 1 
ATOM   1290 C  CD2 . LEU A 1 156 ? 4.337   -7.687  7.454   1.00 14.00 ? 157 LEU A CD2 1 
ATOM   1291 N  N   . GLN A 1 157 ? 0.840   -6.140  3.709   1.00 14.49 ? 158 GLN A N   1 
ATOM   1292 C  CA  . GLN A 1 157 ? 1.177   -6.625  2.393   1.00 14.59 ? 158 GLN A CA  1 
ATOM   1293 C  C   . GLN A 1 157 ? 1.578   -5.513  1.412   1.00 13.16 ? 158 GLN A C   1 
ATOM   1294 O  O   . GLN A 1 157 ? 2.466   -5.748  0.609   1.00 13.06 ? 158 GLN A O   1 
ATOM   1295 C  CB  . GLN A 1 157 ? 0.022   -7.465  1.831   1.00 14.72 ? 158 GLN A CB  1 
ATOM   1296 C  CG  . GLN A 1 157 ? 0.376   -8.232  0.547   1.00 16.00 ? 158 GLN A CG  1 
ATOM   1297 C  CD  . GLN A 1 157 ? 1.502   -9.196  0.788   1.00 13.27 ? 158 GLN A CD  1 
ATOM   1298 O  OE1 . GLN A 1 157 ? 1.597   -9.779  1.890   1.00 14.96 ? 158 GLN A OE1 1 
ATOM   1299 N  NE2 . GLN A 1 157 ? 2.350   -9.403  -0.221  1.00 14.83 ? 158 GLN A NE2 1 
ATOM   1300 N  N   A LYS A 1 158 ? 0.987   -4.318  1.523   0.50 14.95 ? 159 LYS A N   1 
ATOM   1301 N  N   B LYS A 1 158 ? 0.980   -4.322  1.526   0.50 14.84 ? 159 LYS A N   1 
ATOM   1302 C  CA  A LYS A 1 158 ? 1.346   -3.223  0.637   0.50 14.85 ? 159 LYS A CA  1 
ATOM   1303 C  CA  B LYS A 1 158 ? 1.326   -3.208  0.658   0.50 14.59 ? 159 LYS A CA  1 
ATOM   1304 C  C   A LYS A 1 158 ? 2.820   -2.871  0.836   0.50 14.78 ? 159 LYS A C   1 
ATOM   1305 C  C   B LYS A 1 158 ? 2.803   -2.860  0.844   0.50 14.69 ? 159 LYS A C   1 
ATOM   1306 O  O   A LYS A 1 158 ? 3.482   -2.462  -0.097  0.50 15.87 ? 159 LYS A O   1 
ATOM   1307 O  O   B LYS A 1 158 ? 3.465   -2.477  -0.101  0.50 15.73 ? 159 LYS A O   1 
ATOM   1308 C  CB  A LYS A 1 158 ? 0.506   -1.958  0.863   0.50 16.94 ? 159 LYS A CB  1 
ATOM   1309 C  CB  B LYS A 1 158 ? 0.411   -1.991  0.874   0.50 16.51 ? 159 LYS A CB  1 
ATOM   1310 C  CG  A LYS A 1 158 ? 0.838   -0.811  -0.079  0.50 19.11 ? 159 LYS A CG  1 
ATOM   1311 C  CG  B LYS A 1 158 ? -0.954  -2.092  0.200   0.50 17.28 ? 159 LYS A CG  1 
ATOM   1312 N  N   . VAL A 1 159 ? 3.313   -3.017  2.073   1.00 13.88 ? 160 VAL A N   1 
ATOM   1313 C  CA  . VAL A 1 159 ? 4.729   -2.773  2.322   1.00 12.96 ? 160 VAL A CA  1 
ATOM   1314 C  C   . VAL A 1 159 ? 5.576   -3.881  1.692   1.00 13.44 ? 160 VAL A C   1 
ATOM   1315 O  O   . VAL A 1 159 ? 6.540   -3.615  0.991   1.00 12.94 ? 160 VAL A O   1 
ATOM   1316 C  CB  . VAL A 1 159 ? 4.979   -2.759  3.825   1.00 13.13 ? 160 VAL A CB  1 
ATOM   1317 C  CG1 . VAL A 1 159 ? 6.473   -2.710  4.122   1.00 13.90 ? 160 VAL A CG1 1 
ATOM   1318 C  CG2 . VAL A 1 159 ? 4.233   -1.642  4.517   1.00 15.30 ? 160 VAL A CG2 1 
ATOM   1319 N  N   . VAL A 1 160 ? 5.186   -5.159  1.934   1.00 14.31 ? 161 VAL A N   1 
ATOM   1320 C  CA  . VAL A 1 160 ? 5.926   -6.306  1.417   1.00 15.58 ? 161 VAL A CA  1 
ATOM   1321 C  C   . VAL A 1 160 ? 6.000   -6.224  -0.114  1.00 14.99 ? 161 VAL A C   1 
ATOM   1322 O  O   . VAL A 1 160 ? 7.043   -6.462  -0.690  1.00 15.46 ? 161 VAL A O   1 
ATOM   1323 C  CB  . VAL A 1 160 ? 5.292   -7.644  1.907   1.00 17.02 ? 161 VAL A CB  1 
ATOM   1324 C  CG1 . VAL A 1 160 ? 5.657   -8.834  1.020   1.00 20.55 ? 161 VAL A CG1 1 
ATOM   1325 C  CG2 . VAL A 1 160 ? 5.565   -7.908  3.393   1.00 20.03 ? 161 VAL A CG2 1 
ATOM   1326 N  N   . ASP A 1 161 ? 4.917   -5.785  -0.744  1.00 15.85 ? 162 ASP A N   1 
ATOM   1327 C  CA  . ASP A 1 161 ? 4.911   -5.838  -2.207  1.00 17.20 ? 162 ASP A CA  1 
ATOM   1328 C  C   . ASP A 1 161 ? 5.794   -4.785  -2.869  1.00 17.88 ? 162 ASP A C   1 
ATOM   1329 O  O   . ASP A 1 161 ? 6.157   -4.961  -4.035  1.00 21.82 ? 162 ASP A O   1 
ATOM   1330 C  CB  . ASP A 1 161 ? 3.483   -5.764  -2.703  1.00 18.77 ? 162 ASP A CB  1 
ATOM   1331 C  CG  . ASP A 1 161 ? 2.840   -7.138  -2.607  1.00 21.11 ? 162 ASP A CG  1 
ATOM   1332 O  OD1 . ASP A 1 161 ? 3.575   -8.163  -2.662  1.00 23.67 ? 162 ASP A OD1 1 
ATOM   1333 O  OD2 . ASP A 1 161 ? 1.623   -7.158  -2.456  1.00 23.37 ? 162 ASP A OD2 1 
ATOM   1334 N  N   . VAL A 1 162 ? 6.155   -3.687  -2.165  1.00 14.79 ? 163 VAL A N   1 
ATOM   1335 C  CA  . VAL A 1 162 ? 6.963   -2.642  -2.779  1.00 15.34 ? 163 VAL A CA  1 
ATOM   1336 C  C   . VAL A 1 162 ? 8.458   -2.915  -2.558  1.00 13.98 ? 163 VAL A C   1 
ATOM   1337 O  O   . VAL A 1 162 ? 9.298   -2.202  -3.087  1.00 14.69 ? 163 VAL A O   1 
ATOM   1338 C  CB  . VAL A 1 162 ? 6.567   -1.247  -2.238  1.00 16.48 ? 163 VAL A CB  1 
ATOM   1339 C  CG1 . VAL A 1 162 ? 7.077   -1.036  -0.830  1.00 16.02 ? 163 VAL A CG1 1 
ATOM   1340 C  CG2 . VAL A 1 162 ? 6.908   -0.034  -3.100  1.00 18.05 ? 163 VAL A CG2 1 
ATOM   1341 N  N   . LEU A 1 163 ? 8.817   -3.913  -1.706  1.00 13.51 ? 164 LEU A N   1 
ATOM   1342 C  CA  . LEU A 1 163 ? 10.220  -4.078  -1.320  1.00 12.08 ? 164 LEU A CA  1 
ATOM   1343 C  C   . LEU A 1 163 ? 11.135  -4.428  -2.487  1.00 13.80 ? 164 LEU A C   1 
ATOM   1344 O  O   . LEU A 1 163 ? 12.309  -4.016  -2.518  1.00 14.17 ? 164 LEU A O   1 
ATOM   1345 C  CB  . LEU A 1 163 ? 10.386  -5.132  -0.216  1.00 12.62 ? 164 LEU A CB  1 
ATOM   1346 C  CG  . LEU A 1 163 ? 9.739   -4.790  1.113   1.00 13.40 ? 164 LEU A CG  1 
ATOM   1347 C  CD1 . LEU A 1 163 ? 10.005  -5.968  2.048   1.00 13.86 ? 164 LEU A CD1 1 
ATOM   1348 C  CD2 . LEU A 1 163 ? 10.255  -3.475  1.671   1.00 13.47 ? 164 LEU A CD2 1 
ATOM   1349 N  N   . ASP A 1 164 ? 10.573  -5.132  -3.484  1.00 15.86 ? 165 ASP A N   1 
ATOM   1350 C  CA  . ASP A 1 164 ? 11.409  -5.404  -4.653  1.00 19.35 ? 165 ASP A CA  1 
ATOM   1351 C  C   . ASP A 1 164 ? 11.846  -4.110  -5.368  1.00 19.62 ? 165 ASP A C   1 
ATOM   1352 O  O   . ASP A 1 164 ? 12.898  -4.136  -6.024  1.00 22.39 ? 165 ASP A O   1 
ATOM   1353 C  CB  . ASP A 1 164 ? 10.754  -6.423  -5.588  1.00 24.05 ? 165 ASP A CB  1 
ATOM   1354 C  CG  . ASP A 1 164 ? 9.729   -5.714  -6.429  1.00 27.51 ? 165 ASP A CG  1 
ATOM   1355 O  OD1 . ASP A 1 164 ? 8.762   -5.224  -5.841  1.00 28.61 ? 165 ASP A OD1 1 
ATOM   1356 O  OD2 . ASP A 1 164 ? 9.953   -5.592  -7.675  1.00 34.92 ? 165 ASP A OD2 1 
ATOM   1357 N  N   . SER A 1 165 ? 11.149  -2.975  -5.181  1.00 15.74 ? 166 SER A N   1 
ATOM   1358 C  CA  . SER A 1 165 ? 11.538  -1.716  -5.819  1.00 15.19 ? 166 SER A CA  1 
ATOM   1359 C  C   . SER A 1 165 ? 12.599  -0.953  -5.036  1.00 16.02 ? 166 SER A C   1 
ATOM   1360 O  O   . SER A 1 165 ? 13.113  0.066   -5.492  1.00 15.52 ? 166 SER A O   1 
ATOM   1361 C  CB  . SER A 1 165 ? 10.336  -0.855  -6.078  1.00 18.48 ? 166 SER A CB  1 
ATOM   1362 O  OG  . SER A 1 165 ? 9.831   -0.343  -4.877  1.00 19.14 ? 166 SER A OG  1 
ATOM   1363 N  N   . ILE A 1 166 ? 12.918  -1.438  -3.815  1.00 14.21 ? 167 ILE A N   1 
ATOM   1364 C  CA  . ILE A 1 166 ? 13.927  -0.789  -2.982  1.00 12.90 ? 167 ILE A CA  1 
ATOM   1365 C  C   . ILE A 1 166 ? 14.954  -1.818  -2.503  1.00 13.03 ? 167 ILE A C   1 
ATOM   1366 O  O   . ILE A 1 166 ? 15.363  -1.849  -1.316  1.00 12.37 ? 167 ILE A O   1 
ATOM   1367 C  CB  . ILE A 1 166 ? 13.291  0.051   -1.830  1.00 11.95 ? 167 ILE A CB  1 
ATOM   1368 C  CG1 . ILE A 1 166 ? 12.434  -0.838  -0.921  1.00 10.94 ? 167 ILE A CG1 1 
ATOM   1369 C  CG2 . ILE A 1 166 ? 12.499  1.253   -2.380  1.00 12.96 ? 167 ILE A CG2 1 
ATOM   1370 C  CD1 . ILE A 1 166 ? 12.251  -0.227  0.457   1.00 13.32 ? 167 ILE A CD1 1 
ATOM   1371 N  N   . LYS A 1 167 ? 15.387  -2.688  -3.401  1.00 14.05 ? 168 LYS A N   1 
ATOM   1372 C  CA  . LYS A 1 167 ? 16.174  -3.829  -2.982  1.00 13.10 ? 168 LYS A CA  1 
ATOM   1373 C  C   . LYS A 1 167 ? 17.474  -3.421  -2.287  1.00 14.03 ? 168 LYS A C   1 
ATOM   1374 O  O   . LYS A 1 167 ? 17.942  -4.096  -1.365  1.00 13.93 ? 168 LYS A O   1 
ATOM   1375 C  CB  . LYS A 1 167 ? 16.442  -4.785  -4.167  1.00 14.96 ? 168 LYS A CB  1 
ATOM   1376 C  CG  . LYS A 1 167 ? 17.171  -6.055  -3.745  1.00 15.77 ? 168 LYS A CG  1 
ATOM   1377 C  CD  . LYS A 1 167 ? 17.398  -6.984  -4.932  1.00 18.18 ? 168 LYS A CD  1 
ATOM   1378 C  CE  . LYS A 1 167 ? 18.295  -8.163  -4.616  1.00 23.78 ? 168 LYS A CE  1 
ATOM   1379 N  NZ  . LYS A 1 167 ? 18.488  -9.073  -5.780  1.00 31.45 ? 168 LYS A NZ  1 
ATOM   1380 N  N   . THR A 1 168 ? 18.070  -2.329  -2.730  1.00 11.56 ? 169 THR A N   1 
ATOM   1381 C  CA  . THR A 1 168 ? 19.432  -2.016  -2.365  1.00 12.04 ? 169 THR A CA  1 
ATOM   1382 C  C   . THR A 1 168 ? 19.484  -0.661  -1.644  1.00 10.48 ? 169 THR A C   1 
ATOM   1383 O  O   . THR A 1 168 ? 18.586  0.189   -1.760  1.00 12.29 ? 169 THR A O   1 
ATOM   1384 C  CB  . THR A 1 168 ? 20.402  -2.070  -3.569  1.00 13.22 ? 169 THR A CB  1 
ATOM   1385 O  OG1 . THR A 1 168 ? 19.809  -1.310  -4.615  1.00 14.19 ? 169 THR A OG1 1 
ATOM   1386 C  CG2 . THR A 1 168 ? 20.610  -3.486  -4.067  1.00 14.38 ? 169 THR A CG2 1 
ATOM   1387 N  N   . LYS A 1 169 ? 20.567  -0.495  -0.904  1.00 11.97 ? 170 LYS A N   1 
ATOM   1388 C  CA  . LYS A 1 169 ? 20.858  0.683   -0.111  1.00 12.79 ? 170 LYS A CA  1 
ATOM   1389 C  C   . LYS A 1 169 ? 20.690  1.975   -0.907  1.00 13.35 ? 170 LYS A C   1 
ATOM   1390 O  O   . LYS A 1 169 ? 21.293  2.045   -1.987  1.00 16.33 ? 170 LYS A O   1 
ATOM   1391 C  CB  . LYS A 1 169 ? 22.252  0.550   0.484   1.00 14.60 ? 170 LYS A CB  1 
ATOM   1392 C  CG  . LYS A 1 169 ? 22.689  1.772   1.302   1.00 15.29 ? 170 LYS A CG  1 
ATOM   1393 C  CD  . LYS A 1 169 ? 24.035  1.571   1.972   1.00 18.46 ? 170 LYS A CD  1 
ATOM   1394 C  CE  . LYS A 1 169 ? 25.142  1.113   1.036   1.00 24.61 ? 170 LYS A CE  1 
ATOM   1395 N  NZ  . LYS A 1 169 ? 26.463  1.055   1.724   1.00 33.26 ? 170 LYS A NZ  1 
ATOM   1396 N  N   . GLY A 1 170 ? 19.914  2.931   -0.397  1.00 14.66 ? 171 GLY A N   1 
ATOM   1397 C  CA  . GLY A 1 170 ? 19.777  4.236   -1.072  1.00 14.34 ? 171 GLY A CA  1 
ATOM   1398 C  C   . GLY A 1 170 ? 18.601  4.290   -2.037  1.00 15.51 ? 171 GLY A C   1 
ATOM   1399 O  O   . GLY A 1 170 ? 18.268  5.366   -2.585  1.00 17.52 ? 171 GLY A O   1 
ATOM   1400 N  N   . LYS A 1 171 ? 18.000  3.154   -2.323  1.00 12.51 ? 172 LYS A N   1 
ATOM   1401 C  CA  . LYS A 1 171 ? 16.785  3.183   -3.128  1.00 12.89 ? 172 LYS A CA  1 
ATOM   1402 C  C   . LYS A 1 171 ? 15.559  3.633   -2.357  1.00 12.80 ? 172 LYS A C   1 
ATOM   1403 O  O   . LYS A 1 171 ? 15.334  3.187   -1.223  1.00 12.19 ? 172 LYS A O   1 
ATOM   1404 C  CB  . LYS A 1 171 ? 16.496  1.849   -3.812  1.00 13.01 ? 172 LYS A CB  1 
ATOM   1405 C  CG  . LYS A 1 171 ? 17.561  1.431   -4.834  1.00 16.00 ? 172 LYS A CG  1 
ATOM   1406 C  CD  . LYS A 1 171 ? 17.058  0.415   -5.913  1.00 20.52 ? 172 LYS A CD  1 
ATOM   1407 C  CE  . LYS A 1 171 ? 15.896  0.873   -6.796  1.00 25.17 ? 172 LYS A CE  1 
ATOM   1408 N  NZ  . LYS A 1 171 ? 15.393  -0.197  -7.703  1.00 26.20 ? 172 LYS A NZ  1 
ATOM   1409 N  N   . SER A 1 172 ? 14.747  4.474   -2.979  1.00 14.34 ? 173 SER A N   1 
ATOM   1410 C  CA  . SER A 1 172 ? 13.481  4.867   -2.397  1.00 13.70 ? 173 SER A CA  1 
ATOM   1411 C  C   . SER A 1 172 ? 12.336  4.722   -3.419  1.00 12.52 ? 173 SER A C   1 
ATOM   1412 O  O   . SER A 1 172 ? 12.535  4.693   -4.647  1.00 14.20 ? 173 SER A O   1 
ATOM   1413 C  CB  . SER A 1 172 ? 13.543  6.244   -1.777  1.00 13.75 ? 173 SER A CB  1 
ATOM   1414 O  OG  . SER A 1 172 ? 13.630  7.235   -2.802  1.00 16.85 ? 173 SER A OG  1 
ATOM   1415 N  N   . ALA A 1 173 ? 11.103  4.686   -2.927  1.00 12.67 ? 174 ALA A N   1 
ATOM   1416 C  CA  . ALA A 1 173 ? 9.916   4.660   -3.785  1.00 13.65 ? 174 ALA A CA  1 
ATOM   1417 C  C   . ALA A 1 173 ? 8.808   5.485   -3.155  1.00 15.72 ? 174 ALA A C   1 
ATOM   1418 O  O   . ALA A 1 173 ? 8.667   5.553   -1.932  1.00 13.28 ? 174 ALA A O   1 
ATOM   1419 C  CB  . ALA A 1 173 ? 9.428   3.231   -3.995  1.00 14.61 ? 174 ALA A CB  1 
ATOM   1420 N  N   . ASP A 1 174 ? 7.942   6.067   -3.986  1.00 16.95 ? 175 ASP A N   1 
ATOM   1421 C  CA  . ASP A 1 174 ? 6.785   6.743   -3.447  1.00 17.53 ? 175 ASP A CA  1 
ATOM   1422 C  C   . ASP A 1 174 ? 5.971   5.722   -2.665  1.00 15.93 ? 175 ASP A C   1 
ATOM   1423 O  O   . ASP A 1 174 ? 5.827   4.561   -3.072  1.00 19.08 ? 175 ASP A O   1 
ATOM   1424 C  CB  . ASP A 1 174 ? 6.018   7.460   -4.580  1.00 22.04 ? 175 ASP A CB  1 
ATOM   1425 C  CG  . ASP A 1 174 ? 6.808   8.555   -5.303  1.00 31.09 ? 175 ASP A CG  1 
ATOM   1426 O  OD1 . ASP A 1 174 ? 7.284   9.528   -4.629  1.00 31.08 ? 175 ASP A OD1 1 
ATOM   1427 O  OD2 . ASP A 1 174 ? 6.925   8.454   -6.568  1.00 34.03 ? 175 ASP A OD2 1 
ATOM   1428 N  N   . PHE A 1 175 ? 5.392   6.181   -1.544  1.00 14.40 ? 176 PHE A N   1 
ATOM   1429 C  CA  . PHE A 1 175 ? 4.595   5.274   -0.738  1.00 13.29 ? 176 PHE A CA  1 
ATOM   1430 C  C   . PHE A 1 175 ? 3.529   6.058   -0.023  1.00 17.02 ? 176 PHE A C   1 
ATOM   1431 O  O   . PHE A 1 175 ? 3.562   6.242   1.176   1.00 17.80 ? 176 PHE A O   1 
ATOM   1432 C  CB  . PHE A 1 175 ? 5.474   4.487   0.241   1.00 13.67 ? 176 PHE A CB  1 
ATOM   1433 C  CG  . PHE A 1 175 ? 4.872   3.203   0.720   1.00 13.91 ? 176 PHE A CG  1 
ATOM   1434 C  CD1 . PHE A 1 175 ? 4.709   2.149   -0.158  1.00 14.27 ? 176 PHE A CD1 1 
ATOM   1435 C  CD2 . PHE A 1 175 ? 4.464   3.040   2.042   1.00 13.45 ? 176 PHE A CD2 1 
ATOM   1436 C  CE1 . PHE A 1 175 ? 4.138   0.973   0.279   1.00 14.54 ? 176 PHE A CE1 1 
ATOM   1437 C  CE2 . PHE A 1 175 ? 3.941   1.825   2.509   1.00 13.05 ? 176 PHE A CE2 1 
ATOM   1438 C  CZ  . PHE A 1 175 ? 3.795   0.800   1.610   1.00 13.64 ? 176 PHE A CZ  1 
ATOM   1439 N  N   . THR A 1 176 ? 2.546   6.530   -0.772  1.00 15.74 ? 177 THR A N   1 
ATOM   1440 C  CA  . THR A 1 176 ? 1.470   7.328   -0.227  1.00 14.26 ? 177 THR A CA  1 
ATOM   1441 C  C   . THR A 1 176 ? 0.265   6.500   0.207   1.00 12.05 ? 177 THR A C   1 
ATOM   1442 O  O   . THR A 1 176 ? 0.072   5.391   -0.228  1.00 12.11 ? 177 THR A O   1 
ATOM   1443 C  CB  . THR A 1 176 ? 1.068   8.422   -1.228  1.00 14.69 ? 177 THR A CB  1 
ATOM   1444 O  OG1 . THR A 1 176 ? 0.719   7.733   -2.428  1.00 18.88 ? 177 THR A OG1 1 
ATOM   1445 C  CG2 . THR A 1 176 ? 2.184   9.405   -1.466  1.00 18.24 ? 177 THR A CG2 1 
ATOM   1446 N  N   . ASN A 1 177 ? -0.527  7.101   1.087   1.00 14.06 ? 178 ASN A N   1 
ATOM   1447 C  CA  . ASN A 1 177 ? -1.792  6.551   1.516   1.00 14.41 ? 178 ASN A CA  1 
ATOM   1448 C  C   . ASN A 1 177 ? -1.649  5.205   2.229   1.00 14.18 ? 178 ASN A C   1 
ATOM   1449 O  O   . ASN A 1 177 ? -2.579  4.406   2.210   1.00 17.21 ? 178 ASN A O   1 
ATOM   1450 C  CB  . ASN A 1 177 ? -2.778  6.477   0.348   1.00 14.90 ? 178 ASN A CB  1 
ATOM   1451 C  CG  . ASN A 1 177 ? -3.001  7.837   -0.280  1.00 15.94 ? 178 ASN A CG  1 
ATOM   1452 O  OD1 . ASN A 1 177 ? -3.682  8.680   0.302   1.00 17.44 ? 178 ASN A OD1 1 
ATOM   1453 N  ND2 . ASN A 1 177 ? -2.379  8.055   -1.427  1.00 15.11 ? 178 ASN A ND2 1 
ATOM   1454 N  N   . PHE A 1 178 ? -0.534  4.977   2.901   1.00 12.97 ? 179 PHE A N   1 
ATOM   1455 C  CA  . PHE A 1 178 ? -0.422  3.767   3.716   1.00 12.55 ? 179 PHE A CA  1 
ATOM   1456 C  C   . PHE A 1 178 ? -0.885  4.078   5.125   1.00 12.77 ? 179 PHE A C   1 
ATOM   1457 O  O   . PHE A 1 178 ? -0.447  5.044   5.723   1.00 14.99 ? 179 PHE A O   1 
ATOM   1458 C  CB  . PHE A 1 178 ? 1.024   3.330   3.802   1.00 12.25 ? 179 PHE A CB  1 
ATOM   1459 C  CG  . PHE A 1 178 ? 1.111   2.094   4.652   1.00 12.64 ? 179 PHE A CG  1 
ATOM   1460 C  CD1 . PHE A 1 178 ? 0.768   0.883   4.104   1.00 12.46 ? 179 PHE A CD1 1 
ATOM   1461 C  CD2 . PHE A 1 178 ? 1.549   2.175   5.965   1.00 11.67 ? 179 PHE A CD2 1 
ATOM   1462 C  CE1 . PHE A 1 178 ? 0.799   -0.269  4.877   1.00 12.99 ? 179 PHE A CE1 1 
ATOM   1463 C  CE2 . PHE A 1 178 ? 1.572   1.022   6.735   1.00 12.75 ? 179 PHE A CE2 1 
ATOM   1464 C  CZ  . PHE A 1 178 ? 1.253   -0.194  6.174   1.00 13.49 ? 179 PHE A CZ  1 
ATOM   1465 N  N   . ASP A 1 179 ? -1.791  3.237   5.653   1.00 13.74 ? 180 ASP A N   1 
ATOM   1466 C  CA  . ASP A 1 179 ? -2.400  3.454   6.956   1.00 13.67 ? 180 ASP A CA  1 
ATOM   1467 C  C   . ASP A 1 179 ? -1.684  2.585   7.986   1.00 12.71 ? 180 ASP A C   1 
ATOM   1468 O  O   . ASP A 1 179 ? -1.817  1.360   8.013   1.00 14.07 ? 180 ASP A O   1 
ATOM   1469 C  CB  . ASP A 1 179 ? -3.858  2.973   6.943   1.00 15.02 ? 180 ASP A CB  1 
ATOM   1470 C  CG  . ASP A 1 179 ? -4.663  3.416   8.161   1.00 19.96 ? 180 ASP A CG  1 
ATOM   1471 O  OD1 . ASP A 1 179 ? -4.085  3.714   9.210   1.00 16.89 ? 180 ASP A OD1 1 
ATOM   1472 O  OD2 . ASP A 1 179 ? -5.911  3.457   8.046   1.00 25.76 ? 180 ASP A OD2 1 
ATOM   1473 N  N   . PRO A 1 180 ? -0.902  3.164   8.907   1.00 12.07 ? 181 PRO A N   1 
ATOM   1474 C  CA  . PRO A 1 180 ? -0.144  2.305   9.836   1.00 11.90 ? 181 PRO A CA  1 
ATOM   1475 C  C   . PRO A 1 180 ? -1.038  1.680   10.905  1.00 12.73 ? 181 PRO A C   1 
ATOM   1476 O  O   . PRO A 1 180 ? -0.566  0.794   11.630  1.00 12.07 ? 181 PRO A O   1 
ATOM   1477 C  CB  . PRO A 1 180 ? 0.839   3.286   10.472  1.00 13.15 ? 181 PRO A CB  1 
ATOM   1478 C  CG  . PRO A 1 180 ? 0.198   4.666   10.348  1.00 12.96 ? 181 PRO A CG  1 
ATOM   1479 C  CD  . PRO A 1 180 ? -0.602  4.597   9.059   1.00 12.10 ? 181 PRO A CD  1 
ATOM   1480 N  N   . ARG A 1 181 ? -2.308  2.088   10.982  1.00 12.24 ? 182 ARG A N   1 
ATOM   1481 C  CA  . ARG A 1 181 ? -3.213  1.416   11.900  1.00 13.90 ? 182 ARG A CA  1 
ATOM   1482 C  C   . ARG A 1 181 ? -3.329  -0.059  11.566  1.00 14.56 ? 182 ARG A C   1 
ATOM   1483 O  O   . ARG A 1 181 ? -3.714  -0.831  12.428  1.00 14.70 ? 182 ARG A O   1 
ATOM   1484 C  CB  . ARG A 1 181 ? -4.575  2.109   11.868  1.00 14.85 ? 182 ARG A CB  1 
ATOM   1485 C  CG  . ARG A 1 181 ? -4.451  3.518   12.448  1.00 15.32 ? 182 ARG A CG  1 
ATOM   1486 C  CD  . ARG A 1 181 ? -5.787  4.194   12.471  1.00 16.53 ? 182 ARG A CD  1 
ATOM   1487 N  NE  . ARG A 1 181 ? -6.262  4.415   11.132  1.00 17.64 ? 182 ARG A NE  1 
ATOM   1488 C  CZ  . ARG A 1 181 ? -7.330  5.137   10.835  1.00 20.32 ? 182 ARG A CZ  1 
ATOM   1489 N  NH1 . ARG A 1 181 ? -8.048  5.687   11.811  1.00 21.53 ? 182 ARG A NH1 1 
ATOM   1490 N  NH2 . ARG A 1 181 ? -7.640  5.284   9.570   1.00 21.22 ? 182 ARG A NH2 1 
ATOM   1491 N  N   . GLY A 1 182 ? -3.075  -0.441  10.323  1.00 14.40 ? 183 GLY A N   1 
ATOM   1492 C  CA  . GLY A 1 182 ? -3.209  -1.834  9.932   1.00 14.52 ? 183 GLY A CA  1 
ATOM   1493 C  C   . GLY A 1 182 ? -2.045  -2.695  10.429  1.00 14.84 ? 183 GLY A C   1 
ATOM   1494 O  O   . GLY A 1 182 ? -1.988  -3.877  10.078  1.00 15.82 ? 183 GLY A O   1 
ATOM   1495 N  N   . LEU A 1 183 ? -1.056  -2.103  11.144  1.00 12.19 ? 184 LEU A N   1 
ATOM   1496 C  CA  . LEU A 1 183 ? 0.063   -2.895  11.662  1.00 12.44 ? 184 LEU A CA  1 
ATOM   1497 C  C   . LEU A 1 183 ? -0.074  -3.112  13.156  1.00 11.54 ? 184 LEU A C   1 
ATOM   1498 O  O   . LEU A 1 183 ? 0.872   -3.704  13.726  1.00 13.63 ? 184 LEU A O   1 
ATOM   1499 C  CB  . LEU A 1 183 ? 1.404   -2.181  11.380  1.00 12.40 ? 184 LEU A CB  1 
ATOM   1500 C  CG  . LEU A 1 183 ? 1.724   -2.026  9.890   1.00 13.43 ? 184 LEU A CG  1 
ATOM   1501 C  CD1 . LEU A 1 183 ? 2.940   -1.130  9.685   1.00 14.35 ? 184 LEU A CD1 1 
ATOM   1502 C  CD2 . LEU A 1 183 ? 1.885   -3.357  9.164   1.00 17.78 ? 184 LEU A CD2 1 
ATOM   1503 N  N   . LEU A 1 184 ? -1.147  -2.638  13.797  1.00 10.94 ? 185 LEU A N   1 
ATOM   1504 C  CA  . LEU A 1 184 ? -1.279  -2.718  15.243  1.00 11.91 ? 185 LEU A CA  1 
ATOM   1505 C  C   . LEU A 1 184 ? -1.978  -4.010  15.615  1.00 14.73 ? 185 LEU A C   1 
ATOM   1506 O  O   . LEU A 1 184 ? -2.701  -4.599  14.813  1.00 17.58 ? 185 LEU A O   1 
ATOM   1507 C  CB  . LEU A 1 184 ? -2.094  -1.543  15.776  1.00 12.12 ? 185 LEU A CB  1 
ATOM   1508 C  CG  . LEU A 1 184 ? -1.517  -0.167  15.411  1.00 14.23 ? 185 LEU A CG  1 
ATOM   1509 C  CD1 . LEU A 1 184 ? -2.436  0.972   15.837  1.00 13.48 ? 185 LEU A CD1 1 
ATOM   1510 C  CD2 . LEU A 1 184 ? -0.097  0.038   15.958  1.00 17.77 ? 185 LEU A CD2 1 
ATOM   1511 N  N   . PRO A 1 185 ? -1.664  -4.568  16.793  1.00 12.72 ? 186 PRO A N   1 
ATOM   1512 C  CA  . PRO A 1 185 ? -2.426  -5.698  17.325  1.00 12.56 ? 186 PRO A CA  1 
ATOM   1513 C  C   . PRO A 1 185 ? -3.718  -5.162  17.922  1.00 13.79 ? 186 PRO A C   1 
ATOM   1514 O  O   . PRO A 1 185 ? -3.948  -3.946  17.955  1.00 14.24 ? 186 PRO A O   1 
ATOM   1515 C  CB  . PRO A 1 185 ? -1.441  -6.250  18.384  1.00 12.01 ? 186 PRO A CB  1 
ATOM   1516 C  CG  . PRO A 1 185 ? -0.746  -4.991  18.932  1.00 11.34 ? 186 PRO A CG  1 
ATOM   1517 C  CD  . PRO A 1 185 ? -0.570  -4.123  17.689  1.00 11.09 ? 186 PRO A CD  1 
ATOM   1518 N  N   A GLU A 1 186 ? -4.524  -6.123  18.391  0.50 14.30 ? 187 GLU A N   1 
ATOM   1519 N  N   B GLU A 1 186 ? -4.583  -6.040  18.480  0.50 14.11 ? 187 GLU A N   1 
ATOM   1520 C  CA  A GLU A 1 186 ? -5.794  -5.782  18.992  0.50 14.40 ? 187 GLU A CA  1 
ATOM   1521 C  CA  B GLU A 1 186 ? -5.836  -5.556  19.063  0.50 13.77 ? 187 GLU A CA  1 
ATOM   1522 C  C   A GLU A 1 186 ? -5.590  -4.934  20.243  0.50 13.68 ? 187 GLU A C   1 
ATOM   1523 C  C   B GLU A 1 186 ? -5.613  -4.822  20.371  0.50 13.73 ? 187 GLU A C   1 
ATOM   1524 O  O   A GLU A 1 186 ? -6.143  -3.842  20.291  0.50 16.42 ? 187 GLU A O   1 
ATOM   1525 O  O   B GLU A 1 186 ? -6.282  -3.839  20.694  0.50 16.00 ? 187 GLU A O   1 
ATOM   1526 C  CB  A GLU A 1 186 ? -6.646  -7.046  19.120  0.50 16.07 ? 187 GLU A CB  1 
ATOM   1527 C  CB  B GLU A 1 186 ? -6.767  -6.689  19.490  0.50 15.90 ? 187 GLU A CB  1 
ATOM   1528 C  CG  A GLU A 1 186 ? -7.663  -6.946  20.229  0.50 18.40 ? 187 GLU A CG  1 
ATOM   1529 C  CG  B GLU A 1 186 ? -7.215  -7.537  18.342  0.50 16.42 ? 187 GLU A CG  1 
ATOM   1530 C  CD  A GLU A 1 186 ? -8.365  -8.267  20.480  0.50 20.00 ? 187 GLU A CD  1 
ATOM   1531 C  CD  B GLU A 1 186 ? -8.136  -8.674  18.762  0.50 16.97 ? 187 GLU A CD  1 
ATOM   1532 O  OE1 A GLU A 1 186 ? -8.229  -9.193  19.640  0.50 20.98 ? 187 GLU A OE1 1 
ATOM   1533 O  OE1 B GLU A 1 186 ? -8.314  -8.893  19.990  0.50 17.96 ? 187 GLU A OE1 1 
ATOM   1534 O  OE2 A GLU A 1 186 ? -9.035  -8.352  21.497  0.50 23.44 ? 187 GLU A OE2 1 
ATOM   1535 O  OE2 B GLU A 1 186 ? -8.643  -9.348  17.865  0.50 19.53 ? 187 GLU A OE2 1 
ATOM   1536 N  N   . SER A 1 187 ? -4.739  -5.387  21.198  1.00 13.21 ? 188 SER A N   1 
ATOM   1537 C  CA  . SER A 1 187 ? -4.560  -4.797  22.509  1.00 13.65 ? 188 SER A CA  1 
ATOM   1538 C  C   . SER A 1 187 ? -3.441  -3.765  22.501  1.00 13.59 ? 188 SER A C   1 
ATOM   1539 O  O   . SER A 1 187 ? -2.447  -4.016  21.818  1.00 15.56 ? 188 SER A O   1 
ATOM   1540 C  CB  . SER A 1 187 ? -4.151  -5.882  23.468  1.00 14.01 ? 188 SER A CB  1 
ATOM   1541 O  OG  . SER A 1 187 ? -3.975  -5.315  24.761  1.00 14.98 ? 188 SER A OG  1 
ATOM   1542 N  N   . LEU A 1 188 ? -3.580  -2.692  23.297  1.00 12.55 ? 189 LEU A N   1 
ATOM   1543 C  CA  . LEU A 1 188 ? -2.520  -1.685  23.460  1.00 14.53 ? 189 LEU A CA  1 
ATOM   1544 C  C   . LEU A 1 188 ? -1.866  -1.818  24.841  1.00 12.99 ? 189 LEU A C   1 
ATOM   1545 O  O   . LEU A 1 188 ? -1.238  -0.869  25.326  1.00 15.38 ? 189 LEU A O   1 
ATOM   1546 C  CB  . LEU A 1 188 ? -3.077  -0.270  23.242  1.00 16.25 ? 189 LEU A CB  1 
ATOM   1547 C  CG  . LEU A 1 188 ? -3.483  0.071   21.817  1.00 17.23 ? 189 LEU A CG  1 
ATOM   1548 C  CD1 . LEU A 1 188 ? -3.936  1.526   21.725  1.00 19.30 ? 189 LEU A CD1 1 
ATOM   1549 C  CD2 . LEU A 1 188 ? -2.342  -0.184  20.831  1.00 17.37 ? 189 LEU A CD2 1 
ATOM   1550 N  N   . ASP A 1 189 ? -1.975  -2.975  25.485  1.00 13.59 ? 190 ASP A N   1 
ATOM   1551 C  CA  . ASP A 1 189 ? -1.258  -3.256  26.714  1.00 13.51 ? 190 ASP A CA  1 
ATOM   1552 C  C   . ASP A 1 189 ? 0.244   -3.183  26.405  1.00 10.82 ? 190 ASP A C   1 
ATOM   1553 O  O   . ASP A 1 189 ? 0.659   -3.666  25.348  1.00 11.81 ? 190 ASP A O   1 
ATOM   1554 C  CB  . ASP A 1 189 ? -1.630  -4.659  27.234  1.00 15.04 ? 190 ASP A CB  1 
ATOM   1555 C  CG  . ASP A 1 189 ? -2.945  -4.761  27.994  1.00 19.22 ? 190 ASP A CG  1 
ATOM   1556 O  OD1 . ASP A 1 189 ? -3.569  -3.739  28.158  1.00 21.93 ? 190 ASP A OD1 1 
ATOM   1557 O  OD2 . ASP A 1 189 ? -3.322  -5.908  28.315  1.00 23.29 ? 190 ASP A OD2 1 
ATOM   1558 N  N   . TYR A 1 190 ? 1.027   -2.652  27.332  1.00 10.29 ? 191 TYR A N   1 
ATOM   1559 C  CA  . TYR A 1 190 ? 2.413   -2.378  26.969  1.00 9.62  ? 191 TYR A CA  1 
ATOM   1560 C  C   . TYR A 1 190 ? 3.298   -2.386  28.202  1.00 10.10 ? 191 TYR A C   1 
ATOM   1561 O  O   . TYR A 1 190 ? 2.878   -2.301  29.364  1.00 10.28 ? 191 TYR A O   1 
ATOM   1562 C  CB  . TYR A 1 190 ? 2.537   -1.005  26.278  1.00 10.81 ? 191 TYR A CB  1 
ATOM   1563 C  CG  . TYR A 1 190 ? 2.193   0.171   27.148  1.00 10.28 ? 191 TYR A CG  1 
ATOM   1564 C  CD1 . TYR A 1 190 ? 3.123   0.798   27.975  1.00 10.90 ? 191 TYR A CD1 1 
ATOM   1565 C  CD2 . TYR A 1 190 ? 0.905   0.728   27.135  1.00 9.76  ? 191 TYR A CD2 1 
ATOM   1566 C  CE1 . TYR A 1 190 ? 2.784   1.843   28.819  1.00 10.71 ? 191 TYR A CE1 1 
ATOM   1567 C  CE2 . TYR A 1 190 ? 0.541   1.777   27.954  1.00 10.89 ? 191 TYR A CE2 1 
ATOM   1568 C  CZ  . TYR A 1 190 ? 1.485   2.361   28.797  1.00 11.67 ? 191 TYR A CZ  1 
ATOM   1569 O  OH  . TYR A 1 190 ? 1.131   3.403   29.619  1.00 13.72 ? 191 TYR A OH  1 
ATOM   1570 N  N   . TRP A 1 191 ? 4.602   -2.509  27.937  1.00 9.37  ? 192 TRP A N   1 
ATOM   1571 C  CA  . TRP A 1 191 ? 5.710   -2.251  28.857  1.00 8.87  ? 192 TRP A CA  1 
ATOM   1572 C  C   . TRP A 1 191 ? 6.400   -0.962  28.456  1.00 8.57  ? 192 TRP A C   1 
ATOM   1573 O  O   . TRP A 1 191 ? 6.429   -0.649  27.262  1.00 9.65  ? 192 TRP A O   1 
ATOM   1574 C  CB  . TRP A 1 191 ? 6.707   -3.400  28.833  1.00 9.13  ? 192 TRP A CB  1 
ATOM   1575 C  CG  . TRP A 1 191 ? 6.177   -4.717  29.285  1.00 8.45  ? 192 TRP A CG  1 
ATOM   1576 C  CD1 . TRP A 1 191 ? 5.948   -5.142  30.567  1.00 10.55 ? 192 TRP A CD1 1 
ATOM   1577 C  CD2 . TRP A 1 191 ? 5.930   -5.841  28.431  1.00 9.32  ? 192 TRP A CD2 1 
ATOM   1578 N  NE1 . TRP A 1 191 ? 5.513   -6.441  30.520  1.00 11.06 ? 192 TRP A NE1 1 
ATOM   1579 C  CE2 . TRP A 1 191 ? 5.510   -6.912  29.234  1.00 10.26 ? 192 TRP A CE2 1 
ATOM   1580 C  CE3 . TRP A 1 191 ? 6.063   -6.060  27.052  1.00 8.90  ? 192 TRP A CE3 1 
ATOM   1581 C  CZ2 . TRP A 1 191 ? 5.210   -8.171  28.689  1.00 11.55 ? 192 TRP A CZ2 1 
ATOM   1582 C  CZ3 . TRP A 1 191 ? 5.758   -7.284  26.515  1.00 10.57 ? 192 TRP A CZ3 1 
ATOM   1583 C  CH2 . TRP A 1 191 ? 5.341   -8.325  27.331  1.00 10.87 ? 192 TRP A CH2 1 
ATOM   1584 N  N   . THR A 1 192 ? 6.958   -0.254  29.411  1.00 8.16  ? 193 THR A N   1 
ATOM   1585 C  CA  . THR A 1 192 ? 7.658   0.958   29.075  1.00 8.71  ? 193 THR A CA  1 
ATOM   1586 C  C   . THR A 1 192 ? 8.899   1.092   29.948  1.00 8.11  ? 193 THR A C   1 
ATOM   1587 O  O   . THR A 1 192 ? 8.944   0.696   31.127  1.00 8.83  ? 193 THR A O   1 
ATOM   1588 C  CB  . THR A 1 192 ? 6.727   2.166   29.106  1.00 7.93  ? 193 THR A CB  1 
ATOM   1589 O  OG1 . THR A 1 192 ? 7.486   3.315   28.734  1.00 9.83  ? 193 THR A OG1 1 
ATOM   1590 C  CG2 . THR A 1 192 ? 6.164   2.427   30.495  1.00 8.79  ? 193 THR A CG2 1 
ATOM   1591 N  N   . TYR A 1 193 ? 9.963   1.662   29.377  1.00 8.47  ? 194 TYR A N   1 
ATOM   1592 C  CA  . TYR A 1 193 ? 11.205  1.903   30.119  1.00 8.47  ? 194 TYR A CA  1 
ATOM   1593 C  C   . TYR A 1 193 ? 12.016  2.929   29.353  1.00 8.46  ? 194 TYR A C   1 
ATOM   1594 O  O   . TYR A 1 193 ? 11.763  3.177   28.152  1.00 7.77  ? 194 TYR A O   1 
ATOM   1595 C  CB  . TYR A 1 193 ? 12.022  0.607   30.296  1.00 8.52  ? 194 TYR A CB  1 
ATOM   1596 C  CG  . TYR A 1 193 ? 12.709  0.149   29.037  1.00 7.11  ? 194 TYR A CG  1 
ATOM   1597 C  CD1 . TYR A 1 193 ? 12.052  -0.585  28.062  1.00 7.36  ? 194 TYR A CD1 1 
ATOM   1598 C  CD2 . TYR A 1 193 ? 14.045  0.496   28.834  1.00 7.65  ? 194 TYR A CD2 1 
ATOM   1599 C  CE1 . TYR A 1 193 ? 12.681  -0.861  26.851  1.00 6.68  ? 194 TYR A CE1 1 
ATOM   1600 C  CE2 . TYR A 1 193 ? 14.687  0.189   27.636  1.00 7.62  ? 194 TYR A CE2 1 
ATOM   1601 C  CZ  . TYR A 1 193 ? 14.017  -0.502  26.662  1.00 6.80  ? 194 TYR A CZ  1 
ATOM   1602 O  OH  . TYR A 1 193 ? 14.700  -0.795  25.511  1.00 6.94  ? 194 TYR A OH  1 
ATOM   1603 N  N   . PRO A 1 194 ? 12.945  3.644   30.009  1.00 9.10  ? 195 PRO A N   1 
ATOM   1604 C  CA  . PRO A 1 194 ? 13.786  4.630   29.355  1.00 10.00 ? 195 PRO A CA  1 
ATOM   1605 C  C   . PRO A 1 194 ? 15.002  3.985   28.718  1.00 9.70  ? 195 PRO A C   1 
ATOM   1606 O  O   . PRO A 1 194 ? 15.660  3.200   29.363  1.00 9.79  ? 195 PRO A O   1 
ATOM   1607 C  CB  . PRO A 1 194 ? 14.198  5.533   30.540  1.00 10.27 ? 195 PRO A CB  1 
ATOM   1608 C  CG  . PRO A 1 194 ? 14.267  4.616   31.719  1.00 10.78 ? 195 PRO A CG  1 
ATOM   1609 C  CD  . PRO A 1 194 ? 13.145  3.604   31.479  1.00 11.01 ? 195 PRO A CD  1 
ATOM   1610 N  N   . GLY A 1 195 ? 15.242  4.358   27.477  1.00 8.15  ? 196 GLY A N   1 
ATOM   1611 C  CA  . GLY A 1 195 ? 16.351  3.735   26.798  1.00 9.22  ? 196 GLY A CA  1 
ATOM   1612 C  C   . GLY A 1 195 ? 16.909  4.627   25.695  1.00 7.93  ? 196 GLY A C   1 
ATOM   1613 O  O   . GLY A 1 195 ? 17.044  5.847   25.822  1.00 8.43  ? 196 GLY A O   1 
ATOM   1614 N  N   . SER A 1 196 ? 17.319  3.930   24.625  1.00 7.46  ? 197 SER A N   1 
ATOM   1615 C  CA  . SER A 1 196 ? 18.174  4.539   23.622  1.00 7.84  ? 197 SER A CA  1 
ATOM   1616 C  C   . SER A 1 196 ? 17.711  4.164   22.229  1.00 8.21  ? 197 SER A C   1 
ATOM   1617 O  O   . SER A 1 196 ? 16.943  3.208   22.033  1.00 8.08  ? 197 SER A O   1 
ATOM   1618 C  CB  . SER A 1 196 ? 19.634  4.121   23.805  1.00 8.60  ? 197 SER A CB  1 
ATOM   1619 O  OG  . SER A 1 196 ? 19.861  2.775   23.353  1.00 7.78  ? 197 SER A OG  1 
ATOM   1620 N  N   . LEU A 1 197 ? 18.320  4.805   21.217  1.00 8.51  ? 198 LEU A N   1 
ATOM   1621 C  CA  . LEU A 1 197 ? 18.327  4.284   19.856  1.00 8.18  ? 198 LEU A CA  1 
ATOM   1622 C  C   . LEU A 1 197 ? 19.031  2.944   19.893  1.00 7.57  ? 198 LEU A C   1 
ATOM   1623 O  O   . LEU A 1 197 ? 20.024  2.767   20.596  1.00 7.91  ? 198 LEU A O   1 
ATOM   1624 C  CB  . LEU A 1 197 ? 19.141  5.227   18.954  1.00 9.50  ? 198 LEU A CB  1 
ATOM   1625 C  CG  . LEU A 1 197 ? 18.554  6.622   18.840  1.00 9.62  ? 198 LEU A CG  1 
ATOM   1626 C  CD1 . LEU A 1 197 ? 19.492  7.533   18.064  1.00 11.91 ? 198 LEU A CD1 1 
ATOM   1627 C  CD2 . LEU A 1 197 ? 17.156  6.638   18.236  1.00 12.47 ? 198 LEU A CD2 1 
ATOM   1628 N  N   . THR A 1 198 ? 18.533  1.994   19.106  1.00 7.34  ? 199 THR A N   1 
ATOM   1629 C  CA  . THR A 1 198 ? 19.209  0.708   19.068  1.00 7.98  ? 199 THR A CA  1 
ATOM   1630 C  C   . THR A 1 198 ? 20.239  0.624   17.937  1.00 7.95  ? 199 THR A C   1 
ATOM   1631 O  O   . THR A 1 198 ? 20.857  -0.457  17.777  1.00 8.04  ? 199 THR A O   1 
ATOM   1632 C  CB  . THR A 1 198 ? 18.169  -0.405  18.894  1.00 8.07  ? 199 THR A CB  1 
ATOM   1633 O  OG1 . THR A 1 198 ? 17.644  -0.369  17.552  1.00 7.73  ? 199 THR A OG1 1 
ATOM   1634 C  CG2 . THR A 1 198 ? 17.131  -0.420  19.996  1.00 8.13  ? 199 THR A CG2 1 
ATOM   1635 N  N   . THR A 1 199 ? 20.428  1.730   17.181  1.00 9.60  ? 200 THR A N   1 
ATOM   1636 C  CA  . THR A 1 199 ? 21.472  1.756   16.164  1.00 10.83 ? 200 THR A CA  1 
ATOM   1637 C  C   . THR A 1 199 ? 22.305  2.989   16.475  1.00 10.63 ? 200 THR A C   1 
ATOM   1638 O  O   . THR A 1 199 ? 21.848  3.927   17.132  1.00 10.46 ? 200 THR A O   1 
ATOM   1639 C  CB  . THR A 1 199 ? 20.909  1.982   14.752  1.00 12.00 ? 200 THR A CB  1 
ATOM   1640 O  OG1 . THR A 1 199 ? 20.073  3.121   14.815  1.00 19.10 ? 200 THR A OG1 1 
ATOM   1641 C  CG2 . THR A 1 199 ? 20.034  0.819   14.340  1.00 11.88 ? 200 THR A CG2 1 
ATOM   1642 N  N   . PRO A 1 200 ? 23.576  3.016   16.007  1.00 9.96  ? 201 PRO A N   1 
ATOM   1643 C  CA  . PRO A 1 200 ? 24.334  4.263   16.122  1.00 10.35 ? 201 PRO A CA  1 
ATOM   1644 C  C   . PRO A 1 200 ? 23.502  5.445   15.628  1.00 9.43  ? 201 PRO A C   1 
ATOM   1645 O  O   . PRO A 1 200 ? 22.763  5.329   14.639  1.00 12.08 ? 201 PRO A O   1 
ATOM   1646 C  CB  . PRO A 1 200 ? 25.482  3.915   15.148  1.00 10.68 ? 201 PRO A CB  1 
ATOM   1647 C  CG  . PRO A 1 200 ? 25.735  2.450   15.440  1.00 10.87 ? 201 PRO A CG  1 
ATOM   1648 C  CD  . PRO A 1 200 ? 24.325  1.880   15.408  1.00 11.37 ? 201 PRO A CD  1 
ATOM   1649 N  N   . PRO A 1 201 ? 23.565  6.604   16.289  1.00 10.43 ? 202 PRO A N   1 
ATOM   1650 C  CA  . PRO A 1 201 ? 24.534  6.889   17.355  1.00 10.92 ? 202 PRO A CA  1 
ATOM   1651 C  C   . PRO A 1 201 ? 24.210  6.454   18.783  1.00 10.41 ? 202 PRO A C   1 
ATOM   1652 O  O   . PRO A 1 201 ? 24.934  6.791   19.713  1.00 11.40 ? 202 PRO A O   1 
ATOM   1653 C  CB  . PRO A 1 201 ? 24.553  8.428   17.288  1.00 11.60 ? 202 PRO A CB  1 
ATOM   1654 C  CG  . PRO A 1 201 ? 23.168  8.831   16.863  1.00 12.18 ? 202 PRO A CG  1 
ATOM   1655 C  CD  . PRO A 1 201 ? 22.784  7.779   15.867  1.00 10.83 ? 202 PRO A CD  1 
ATOM   1656 N  N   . LEU A 1 202 ? 23.158  5.647   18.969  1.00 9.39  ? 203 LEU A N   1 
ATOM   1657 C  CA  . LEU A 1 202 ? 22.882  4.991   20.262  1.00 9.26  ? 203 LEU A CA  1 
ATOM   1658 C  C   . LEU A 1 202 ? 22.515  5.969   21.371  1.00 7.88  ? 203 LEU A C   1 
ATOM   1659 O  O   . LEU A 1 202 ? 22.539  5.620   22.553  1.00 9.39  ? 203 LEU A O   1 
ATOM   1660 C  CB  . LEU A 1 202 ? 24.016  4.069   20.708  1.00 8.86  ? 203 LEU A CB  1 
ATOM   1661 C  CG  . LEU A 1 202 ? 24.334  2.973   19.694  1.00 9.02  ? 203 LEU A CG  1 
ATOM   1662 C  CD1 . LEU A 1 202 ? 25.624  2.314   20.152  1.00 10.13 ? 203 LEU A CD1 1 
ATOM   1663 C  CD2 . LEU A 1 202 ? 23.232  1.935   19.624  1.00 10.17 ? 203 LEU A CD2 1 
ATOM   1664 N  N   . THR A 1 203 ? 22.051  7.155   20.940  1.00 8.77  ? 204 THR A N   1 
ATOM   1665 C  CA  . THR A 1 203 ? 21.751  8.237   21.856  1.00 9.27  ? 204 THR A CA  1 
ATOM   1666 C  C   . THR A 1 203 ? 20.646  7.796   22.821  1.00 9.80  ? 204 THR A C   1 
ATOM   1667 O  O   . THR A 1 203 ? 19.667  7.129   22.436  1.00 9.42  ? 204 THR A O   1 
ATOM   1668 C  CB  . THR A 1 203 ? 21.193  9.422   21.060  1.00 10.73 ? 204 THR A CB  1 
ATOM   1669 O  OG1 . THR A 1 203 ? 22.128  9.646   20.000  1.00 13.47 ? 204 THR A OG1 1 
ATOM   1670 C  CG2 . THR A 1 203 ? 21.051  10.685  21.882  1.00 13.11 ? 204 THR A CG2 1 
ATOM   1671 N  N   . GLU A 1 204 ? 20.734  8.251   24.073  1.00 10.90 ? 205 GLU A N   1 
ATOM   1672 C  CA  . GLU A 1 204 ? 19.839  7.863   25.145  1.00 11.31 ? 205 GLU A CA  1 
ATOM   1673 C  C   . GLU A 1 204 ? 18.660  8.841   25.182  1.00 11.77 ? 205 GLU A C   1 
ATOM   1674 O  O   . GLU A 1 204 ? 18.459  9.564   26.169  1.00 13.74 ? 205 GLU A O   1 
ATOM   1675 C  CB  . GLU A 1 204 ? 20.601  7.711   26.475  1.00 10.39 ? 205 GLU A CB  1 
ATOM   1676 C  CG  . GLU A 1 204 ? 21.603  6.564   26.330  1.00 12.01 ? 205 GLU A CG  1 
ATOM   1677 C  CD  . GLU A 1 204 ? 22.449  6.213   27.530  1.00 11.96 ? 205 GLU A CD  1 
ATOM   1678 O  OE1 . GLU A 1 204 ? 22.624  7.086   28.447  1.00 14.02 ? 205 GLU A OE1 1 
ATOM   1679 O  OE2 . GLU A 1 204 ? 22.863  5.063   27.646  1.00 10.98 ? 205 GLU A OE2 1 
ATOM   1680 N  N   . CYS A 1 205 ? 17.845  8.845   24.114  1.00 8.97  ? 206 CYS A N   1 
ATOM   1681 C  CA  . CYS A 1 205 ? 16.802  9.829   23.912  1.00 9.25  ? 206 CYS A CA  1 
ATOM   1682 C  C   . CYS A 1 205 ? 15.426  9.214   23.730  1.00 7.93  ? 206 CYS A C   1 
ATOM   1683 O  O   . CYS A 1 205 ? 14.542  9.933   23.265  1.00 9.03  ? 206 CYS A O   1 
ATOM   1684 C  CB  . CYS A 1 205 ? 17.132  10.655  22.656  1.00 8.81  ? 206 CYS A CB  1 
ATOM   1685 S  SG  . CYS A 1 205 ? 17.290  9.684   21.122  1.00 11.12 ? 206 CYS A SG  1 
ATOM   1686 N  N   . VAL A 1 206 ? 15.272  7.946   24.101  1.00 7.64  ? 207 VAL A N   1 
ATOM   1687 C  CA  . VAL A 1 206 ? 14.045  7.209   23.713  1.00 8.02  ? 207 VAL A CA  1 
ATOM   1688 C  C   . VAL A 1 206 ? 13.271  6.765   24.949  1.00 8.04  ? 207 VAL A C   1 
ATOM   1689 O  O   . VAL A 1 206 ? 13.824  6.122   25.847  1.00 9.47  ? 207 VAL A O   1 
ATOM   1690 C  CB  . VAL A 1 206 ? 14.346  5.975   22.869  1.00 8.34  ? 207 VAL A CB  1 
ATOM   1691 C  CG1 . VAL A 1 206 ? 13.017  5.289   22.509  1.00 8.31  ? 207 VAL A CG1 1 
ATOM   1692 C  CG2 . VAL A 1 206 ? 15.099  6.363   21.613  1.00 9.28  ? 207 VAL A CG2 1 
ATOM   1693 N  N   . THR A 1 207 ? 11.982  7.091   24.961  1.00 7.71  ? 208 THR A N   1 
ATOM   1694 C  CA  . THR A 1 207 ? 11.026  6.404   25.825  1.00 7.67  ? 208 THR A CA  1 
ATOM   1695 C  C   . THR A 1 207 ? 10.476  5.233   25.035  1.00 7.59  ? 208 THR A C   1 
ATOM   1696 O  O   . THR A 1 207 ? 9.863   5.442   23.977  1.00 7.86  ? 208 THR A O   1 
ATOM   1697 C  CB  . THR A 1 207 ? 9.843   7.282   26.285  1.00 8.09  ? 208 THR A CB  1 
ATOM   1698 O  OG1 . THR A 1 207 ? 10.392  8.344   27.069  1.00 9.44  ? 208 THR A OG1 1 
ATOM   1699 C  CG2 . THR A 1 207 ? 8.913   6.479   27.184  1.00 8.85  ? 208 THR A CG2 1 
ATOM   1700 N  N   . TRP A 1 208 ? 10.786  4.014   25.490  1.00 7.32  ? 209 TRP A N   1 
ATOM   1701 C  CA  . TRP A 1 208 ? 10.315  2.832   24.768  1.00 7.04  ? 209 TRP A CA  1 
ATOM   1702 C  C   . TRP A 1 208 ? 8.935   2.424   25.272  1.00 7.03  ? 209 TRP A C   1 
ATOM   1703 O  O   . TRP A 1 208 ? 8.772   2.336   26.493  1.00 7.37  ? 209 TRP A O   1 
ATOM   1704 C  CB  . TRP A 1 208 ? 11.314  1.682   24.985  1.00 7.16  ? 209 TRP A CB  1 
ATOM   1705 C  CG  . TRP A 1 208 ? 12.470  1.763   24.041  1.00 6.68  ? 209 TRP A CG  1 
ATOM   1706 C  CD1 . TRP A 1 208 ? 13.689  2.356   24.253  1.00 7.50  ? 209 TRP A CD1 1 
ATOM   1707 C  CD2 . TRP A 1 208 ? 12.429  1.361   22.675  1.00 6.89  ? 209 TRP A CD2 1 
ATOM   1708 N  NE1 . TRP A 1 208 ? 14.408  2.339   23.073  1.00 8.07  ? 209 TRP A NE1 1 
ATOM   1709 C  CE2 . TRP A 1 208 ? 13.656  1.743   22.100  1.00 7.09  ? 209 TRP A CE2 1 
ATOM   1710 C  CE3 . TRP A 1 208 ? 11.440  0.760   21.888  1.00 7.27  ? 209 TRP A CE3 1 
ATOM   1711 C  CZ2 . TRP A 1 208 ? 13.934  1.535   20.758  1.00 7.04  ? 209 TRP A CZ2 1 
ATOM   1712 C  CZ3 . TRP A 1 208 ? 11.762  0.483   20.569  1.00 7.27  ? 209 TRP A CZ3 1 
ATOM   1713 C  CH2 . TRP A 1 208 ? 12.992  0.866   20.003  1.00 8.70  ? 209 TRP A CH2 1 
ATOM   1714 N  N   . ILE A 1 209 ? 8.042   2.098   24.330  1.00 7.02  ? 210 ILE A N   1 
ATOM   1715 C  CA  . ILE A 1 209 ? 6.714   1.561   24.664  1.00 7.41  ? 210 ILE A CA  1 
ATOM   1716 C  C   . ILE A 1 209 ? 6.609   0.286   23.849  1.00 7.67  ? 210 ILE A C   1 
ATOM   1717 O  O   . ILE A 1 209 ? 6.563   0.390   22.625  1.00 7.51  ? 210 ILE A O   1 
ATOM   1718 C  CB  . ILE A 1 209 ? 5.622   2.595   24.355  1.00 7.87  ? 210 ILE A CB  1 
ATOM   1719 C  CG1 . ILE A 1 209 ? 5.855   3.873   25.155  1.00 8.61  ? 210 ILE A CG1 1 
ATOM   1720 C  CG2 . ILE A 1 209 ? 4.233   2.008   24.610  1.00 9.15  ? 210 ILE A CG2 1 
ATOM   1721 C  CD1 . ILE A 1 209 ? 5.030   5.088   24.686  1.00 11.39 ? 210 ILE A CD1 1 
ATOM   1722 N  N   . VAL A 1 210 ? 6.656   -0.905  24.491  1.00 7.69  ? 211 VAL A N   1 
ATOM   1723 C  CA  . VAL A 1 210 ? 6.660   -2.165  23.774  1.00 8.11  ? 211 VAL A CA  1 
ATOM   1724 C  C   . VAL A 1 210 ? 5.321   -2.861  23.991  1.00 8.07  ? 211 VAL A C   1 
ATOM   1725 O  O   . VAL A 1 210 ? 5.002   -3.159  25.143  1.00 9.05  ? 211 VAL A O   1 
ATOM   1726 C  CB  . VAL A 1 210 ? 7.856   -3.032  24.214  1.00 7.88  ? 211 VAL A CB  1 
ATOM   1727 C  CG1 . VAL A 1 210 ? 7.811   -4.337  23.435  1.00 8.14  ? 211 VAL A CG1 1 
ATOM   1728 C  CG2 . VAL A 1 210 ? 9.178   -2.299  23.918  1.00 9.07  ? 211 VAL A CG2 1 
ATOM   1729 N  N   . LEU A 1 211 ? 4.589   -3.141  22.907  1.00 8.51  ? 212 LEU A N   1 
ATOM   1730 C  CA  . LEU A 1 211 ? 3.256   -3.739  23.126  1.00 9.10  ? 212 LEU A CA  1 
ATOM   1731 C  C   . LEU A 1 211 ? 3.421   -5.203  23.490  1.00 9.20  ? 212 LEU A C   1 
ATOM   1732 O  O   . LEU A 1 211 ? 4.287   -5.874  22.995  1.00 9.13  ? 212 LEU A O   1 
ATOM   1733 C  CB  . LEU A 1 211 ? 2.498   -3.626  21.811  1.00 9.13  ? 212 LEU A CB  1 
ATOM   1734 C  CG  . LEU A 1 211 ? 2.083   -2.203  21.405  1.00 9.83  ? 212 LEU A CG  1 
ATOM   1735 C  CD1 . LEU A 1 211 ? 1.041   -2.232  20.268  1.00 11.88 ? 212 LEU A CD1 1 
ATOM   1736 C  CD2 . LEU A 1 211 ? 1.625   -1.395  22.611  1.00 10.83 ? 212 LEU A CD2 1 
ATOM   1737 N  N   A LYS A 1 212 ? 2.530   -5.666  24.387  0.50 9.22  ? 213 LYS A N   1 
ATOM   1738 N  N   B LYS A 1 212 ? 2.555   -5.714  24.384  0.50 8.96  ? 213 LYS A N   1 
ATOM   1739 C  CA  A LYS A 1 212 ? 2.494   -7.028  24.893  0.50 10.67 ? 213 LYS A CA  1 
ATOM   1740 C  CA  B LYS A 1 212 ? 2.696   -7.110  24.777  0.50 10.22 ? 213 LYS A CA  1 
ATOM   1741 C  C   A LYS A 1 212 ? 2.102   -8.015  23.796  0.50 10.76 ? 213 LYS A C   1 
ATOM   1742 C  C   B LYS A 1 212 ? 2.161   -8.059  23.709  0.50 10.46 ? 213 LYS A C   1 
ATOM   1743 O  O   A LYS A 1 212 ? 2.668   -9.091  23.690  0.50 12.55 ? 213 LYS A O   1 
ATOM   1744 O  O   B LYS A 1 212 ? 2.700   -9.142  23.528  0.50 12.57 ? 213 LYS A O   1 
ATOM   1745 C  CB  A LYS A 1 212 ? 1.501   -7.045  26.059  0.50 12.78 ? 213 LYS A CB  1 
ATOM   1746 C  CB  B LYS A 1 212 ? 2.044   -7.368  26.134  0.50 11.21 ? 213 LYS A CB  1 
ATOM   1747 C  CG  A LYS A 1 212 ? 1.037   -8.418  26.514  0.50 14.49 ? 213 LYS A CG  1 
ATOM   1748 C  CG  B LYS A 1 212 ? 1.812   -8.828  26.507  0.50 13.07 ? 213 LYS A CG  1 
ATOM   1749 C  CD  A LYS A 1 212 ? -0.192  -8.310  27.404  0.50 15.17 ? 213 LYS A CD  1 
ATOM   1750 C  CD  B LYS A 1 212 ? 1.093   -8.936  27.850  0.50 15.07 ? 213 LYS A CD  1 
ATOM   1751 C  CE  A LYS A 1 212 ? -1.485  -8.520  26.645  0.50 16.06 ? 213 LYS A CE  1 
ATOM   1752 C  CE  B LYS A 1 212 ? 0.777   -10.348 28.303  0.50 17.03 ? 213 LYS A CE  1 
ATOM   1753 N  NZ  A LYS A 1 212 ? -1.561  -7.755  25.369  0.50 15.03 ? 213 LYS A NZ  1 
ATOM   1754 N  NZ  B LYS A 1 212 ? -0.045  -10.339 29.533  0.50 20.30 ? 213 LYS A NZ  1 
ATOM   1755 N  N   . GLU A 1 213 ? 1.140   -7.635  22.957  1.00 10.51 ? 214 GLU A N   1 
ATOM   1756 C  CA  . GLU A 1 213 ? 0.576   -8.569  21.995  1.00 11.45 ? 214 GLU A CA  1 
ATOM   1757 C  C   . GLU A 1 213 ? 1.375   -8.478  20.705  1.00 10.73 ? 214 GLU A C   1 
ATOM   1758 O  O   . GLU A 1 213 ? 1.409   -7.423  20.061  1.00 10.25 ? 214 GLU A O   1 
ATOM   1759 C  CB  . GLU A 1 213 ? -0.886  -8.214  21.728  1.00 12.32 ? 214 GLU A CB  1 
ATOM   1760 C  CG  . GLU A 1 213 ? -1.542  -9.187  20.777  1.00 15.42 ? 214 GLU A CG  1 
ATOM   1761 C  CD  . GLU A 1 213 ? -3.034  -9.017  20.568  1.00 20.09 ? 214 GLU A CD  1 
ATOM   1762 O  OE1 . GLU A 1 213 ? -3.624  -8.068  21.076  1.00 17.10 ? 214 GLU A OE1 1 
ATOM   1763 O  OE2 . GLU A 1 213 ? -3.608  -9.964  19.940  1.00 30.34 ? 214 GLU A OE2 1 
ATOM   1764 N  N   . PRO A 1 214 ? 1.939   -9.577  20.220  1.00 10.60 ? 215 PRO A N   1 
ATOM   1765 C  CA  . PRO A 1 214 ? 2.567   -9.508  18.921  1.00 10.53 ? 215 PRO A CA  1 
ATOM   1766 C  C   . PRO A 1 214 ? 1.515   -9.467  17.819  1.00 11.08 ? 215 PRO A C   1 
ATOM   1767 O  O   . PRO A 1 214 ? 0.379   -9.879  18.013  1.00 12.78 ? 215 PRO A O   1 
ATOM   1768 C  CB  . PRO A 1 214 ? 3.325   -10.831 18.801  1.00 11.65 ? 215 PRO A CB  1 
ATOM   1769 C  CG  . PRO A 1 214 ? 2.460   -11.763 19.627  1.00 17.78 ? 215 PRO A CG  1 
ATOM   1770 C  CD  . PRO A 1 214 ? 2.016   -10.928 20.844  1.00 11.83 ? 215 PRO A CD  1 
ATOM   1771 N  N   . ILE A 1 215 ? 1.918   -8.989  16.640  1.00 10.74 ? 216 ILE A N   1 
ATOM   1772 C  CA  . ILE A 1 215 ? 1.144   -9.237  15.436  1.00 11.02 ? 216 ILE A CA  1 
ATOM   1773 C  C   . ILE A 1 215 ? 1.673   -10.470 14.746  1.00 10.37 ? 216 ILE A C   1 
ATOM   1774 O  O   . ILE A 1 215 ? 2.846   -10.878 14.858  1.00 11.26 ? 216 ILE A O   1 
ATOM   1775 C  CB  . ILE A 1 215 ? 1.168   -8.020  14.502  1.00 10.50 ? 216 ILE A CB  1 
ATOM   1776 C  CG1 . ILE A 1 215 ? 2.568   -7.663  13.977  1.00 11.12 ? 216 ILE A CG1 1 
ATOM   1777 C  CG2 . ILE A 1 215 ? 0.493   -6.832  15.175  1.00 11.48 ? 216 ILE A CG2 1 
ATOM   1778 C  CD1 . ILE A 1 215 ? 2.474   -6.694  12.780  1.00 11.68 ? 216 ILE A CD1 1 
ATOM   1779 N  N   A SER A 1 216 ? 0.737   -11.072 14.015  0.50 11.39 ? 217 SER A N   1 
ATOM   1780 N  N   B SER A 1 216 ? 0.759   -11.178 14.086  0.50 12.25 ? 217 SER A N   1 
ATOM   1781 C  CA  A SER A 1 216 ? 1.022   -12.240 13.200  0.50 11.54 ? 217 SER A CA  1 
ATOM   1782 C  CA  B SER A 1 216 ? 1.219   -12.320 13.305  0.50 13.00 ? 217 SER A CA  1 
ATOM   1783 C  C   A SER A 1 216 ? 1.311   -11.831 11.762  0.50 11.01 ? 217 SER A C   1 
ATOM   1784 C  C   B SER A 1 216 ? 1.339   -11.882 11.857  0.50 11.85 ? 217 SER A C   1 
ATOM   1785 O  O   A SER A 1 216 ? 0.575   -11.053 11.160  0.50 12.61 ? 217 SER A O   1 
ATOM   1786 O  O   B SER A 1 216 ? 0.490   -11.144 11.365  0.50 13.64 ? 217 SER A O   1 
ATOM   1787 C  CB  A SER A 1 216 ? -0.114  -13.229 13.301  0.50 12.58 ? 217 SER A CB  1 
ATOM   1788 C  CB  B SER A 1 216 ? 0.280   -13.479 13.404  0.50 15.11 ? 217 SER A CB  1 
ATOM   1789 O  OG  A SER A 1 216 ? -0.024  -13.941 14.519  0.50 13.46 ? 217 SER A OG  1 
ATOM   1790 O  OG  B SER A 1 216 ? -0.992  -13.004 13.026  0.50 18.58 ? 217 SER A OG  1 
ATOM   1791 N  N   . VAL A 1 217 ? 2.429   -12.320 11.237  1.00 11.39 ? 218 VAL A N   1 
ATOM   1792 C  CA  . VAL A 1 217 ? 2.702   -12.147 9.825   1.00 11.74 ? 218 VAL A CA  1 
ATOM   1793 C  C   . VAL A 1 217 ? 2.968   -13.508 9.204   1.00 12.53 ? 218 VAL A C   1 
ATOM   1794 O  O   . VAL A 1 217 ? 3.267   -14.445 9.933   1.00 11.11 ? 218 VAL A O   1 
ATOM   1795 C  CB  . VAL A 1 217 ? 3.883   -11.177 9.578   1.00 12.63 ? 218 VAL A CB  1 
ATOM   1796 C  CG1 . VAL A 1 217 ? 3.639   -9.858  10.324  1.00 13.06 ? 218 VAL A CG1 1 
ATOM   1797 C  CG2 . VAL A 1 217 ? 5.180   -11.798 10.061  1.00 13.46 ? 218 VAL A CG2 1 
ATOM   1798 N  N   . SER A 1 218 ? 2.825   -13.616 7.899   1.00 11.73 ? 219 SER A N   1 
ATOM   1799 C  CA  . SER A 1 218 ? 3.028   -14.945 7.351   1.00 13.06 ? 219 SER A CA  1 
ATOM   1800 C  C   . SER A 1 218 ? 4.501   -15.197 7.083   1.00 13.92 ? 219 SER A C   1 
ATOM   1801 O  O   . SER A 1 218 ? 5.352   -14.277 6.953   1.00 13.07 ? 219 SER A O   1 
ATOM   1802 C  CB  . SER A 1 218 ? 2.244   -15.168 6.109   1.00 13.51 ? 219 SER A CB  1 
ATOM   1803 O  OG  . SER A 1 218 ? 2.749   -14.292 5.087   1.00 14.97 ? 219 SER A OG  1 
ATOM   1804 N  N   A SER A 1 219 ? 4.864   -16.472 6.899   0.50 13.45 ? 220 SER A N   1 
ATOM   1805 N  N   B SER A 1 219 ? 4.808   -16.493 6.956   0.50 13.64 ? 220 SER A N   1 
ATOM   1806 C  CA  A SER A 1 219 ? 6.249   -16.789 6.604   0.50 14.38 ? 220 SER A CA  1 
ATOM   1807 C  CA  B SER A 1 219 ? 6.145   -16.908 6.604   0.50 14.76 ? 220 SER A CA  1 
ATOM   1808 C  C   A SER A 1 219 ? 6.664   -16.114 5.296   0.50 14.84 ? 220 SER A C   1 
ATOM   1809 C  C   B SER A 1 219 ? 6.602   -16.138 5.371   0.50 14.62 ? 220 SER A C   1 
ATOM   1810 O  O   A SER A 1 219 ? 7.821   -15.709 5.092   0.50 14.45 ? 220 SER A O   1 
ATOM   1811 O  O   B SER A 1 219 ? 7.742   -15.671 5.339   0.50 14.59 ? 220 SER A O   1 
ATOM   1812 C  CB  A SER A 1 219 ? 6.412   -18.289 6.571   0.50 15.07 ? 220 SER A CB  1 
ATOM   1813 C  CB  B SER A 1 219 ? 6.214   -18.414 6.424   0.50 14.90 ? 220 SER A CB  1 
ATOM   1814 O  OG  A SER A 1 219 ? 5.444   -18.847 5.711   0.50 17.81 ? 220 SER A OG  1 
ATOM   1815 O  OG  B SER A 1 219 ? 7.557   -18.813 6.159   0.50 18.97 ? 220 SER A OG  1 
ATOM   1816 N  N   . GLU A 1 220 ? 5.703   -16.013 4.379   1.00 13.64 ? 221 GLU A N   1 
ATOM   1817 C  CA  . GLU A 1 220 ? 6.005   -15.430 3.084   1.00 14.71 ? 221 GLU A CA  1 
ATOM   1818 C  C   . GLU A 1 220 ? 6.283   -13.935 3.226   1.00 14.19 ? 221 GLU A C   1 
ATOM   1819 O  O   . GLU A 1 220 ? 7.171   -13.419 2.555   1.00 15.51 ? 221 GLU A O   1 
ATOM   1820 C  CB  . GLU A 1 220 ? 4.834   -15.572 2.092   1.00 15.90 ? 221 GLU A CB  1 
ATOM   1821 C  CG  . GLU A 1 220 ? 4.663   -17.025 1.581   1.00 21.06 ? 221 GLU A CG  1 
ATOM   1822 C  CD  . GLU A 1 220 ? 3.970   -17.935 2.570   1.00 22.48 ? 221 GLU A CD  1 
ATOM   1823 O  OE1 . GLU A 1 220 ? 3.353   -17.447 3.592   1.00 20.91 ? 221 GLU A OE1 1 
ATOM   1824 O  OE2 . GLU A 1 220 ? 4.084   -19.192 2.367   1.00 28.56 ? 221 GLU A OE2 1 
ATOM   1825 N  N   . GLN A 1 221 ? 5.549   -13.263 4.115   1.00 13.63 ? 222 GLN A N   1 
ATOM   1826 C  CA  . GLN A 1 221 ? 5.816   -11.852 4.339   1.00 11.98 ? 222 GLN A CA  1 
ATOM   1827 C  C   . GLN A 1 221 ? 7.230   -11.617 4.856   1.00 13.97 ? 222 GLN A C   1 
ATOM   1828 O  O   . GLN A 1 221 ? 7.957   -10.748 4.343   1.00 12.38 ? 222 GLN A O   1 
ATOM   1829 C  CB  . GLN A 1 221 ? 4.765   -11.265 5.261   1.00 12.78 ? 222 GLN A CB  1 
ATOM   1830 C  CG  . GLN A 1 221 ? 3.460   -11.130 4.496   1.00 12.90 ? 222 GLN A CG  1 
ATOM   1831 C  CD  . GLN A 1 221 ? 2.319   -10.621 5.336   1.00 11.38 ? 222 GLN A CD  1 
ATOM   1832 O  OE1 . GLN A 1 221 ? 2.184   -11.000 6.500   1.00 11.93 ? 222 GLN A OE1 1 
ATOM   1833 N  NE2 . GLN A 1 221 ? 1.459   -9.755  4.803   1.00 11.42 ? 222 GLN A NE2 1 
ATOM   1834 N  N   . VAL A 1 222 ? 7.632   -12.375 5.882   1.00 12.56 ? 223 VAL A N   1 
ATOM   1835 C  CA  . VAL A 1 222 ? 8.970   -12.133 6.435   1.00 13.95 ? 223 VAL A CA  1 
ATOM   1836 C  C   . VAL A 1 222 ? 10.068  -12.589 5.463   1.00 14.02 ? 223 VAL A C   1 
ATOM   1837 O  O   . VAL A 1 222 ? 11.156  -12.004 5.377   1.00 13.97 ? 223 VAL A O   1 
ATOM   1838 C  CB  . VAL A 1 222 ? 9.102   -12.757 7.844   1.00 14.98 ? 223 VAL A CB  1 
ATOM   1839 C  CG1 . VAL A 1 222 ? 9.059   -14.264 7.800   1.00 18.83 ? 223 VAL A CG1 1 
ATOM   1840 C  CG2 . VAL A 1 222 ? 10.367  -12.280 8.558   1.00 18.18 ? 223 VAL A CG2 1 
ATOM   1841 N  N   A LEU A 1 223 ? 9.789   -13.612 4.652   0.50 14.00 ? 224 LEU A N   1 
ATOM   1842 N  N   B LEU A 1 223 ? 9.751   -13.620 4.674   0.50 14.51 ? 224 LEU A N   1 
ATOM   1843 C  CA  A LEU A 1 223 ? 10.783  -14.029 3.680   0.50 14.94 ? 224 LEU A CA  1 
ATOM   1844 C  CA  B LEU A 1 223 ? 10.662  -14.104 3.657   0.50 15.86 ? 224 LEU A CA  1 
ATOM   1845 C  C   A LEU A 1 223 ? 11.112  -12.882 2.736   0.50 14.75 ? 224 LEU A C   1 
ATOM   1846 C  C   B LEU A 1 223 ? 11.060  -12.960 2.729   0.50 15.18 ? 224 LEU A C   1 
ATOM   1847 O  O   A LEU A 1 223 ? 12.253  -12.730 2.297   0.50 15.95 ? 224 LEU A O   1 
ATOM   1848 O  O   B LEU A 1 223 ? 12.217  -12.878 2.316   0.50 16.56 ? 224 LEU A O   1 
ATOM   1849 C  CB  A LEU A 1 223 ? 10.190  -15.180 2.876   0.50 15.94 ? 224 LEU A CB  1 
ATOM   1850 C  CB  B LEU A 1 223 ? 9.925   -15.194 2.877   0.50 17.07 ? 224 LEU A CB  1 
ATOM   1851 C  CG  A LEU A 1 223 ? 10.174  -16.493 3.629   0.50 17.90 ? 224 LEU A CG  1 
ATOM   1852 C  CG  B LEU A 1 223 ? 10.807  -16.096 2.022   0.50 19.57 ? 224 LEU A CG  1 
ATOM   1853 C  CD1 A LEU A 1 223 ? 9.273   -17.488 2.918   0.50 17.04 ? 224 LEU A CD1 1 
ATOM   1854 C  CD1 B LEU A 1 223 ? 11.925  -16.658 2.881   0.50 18.89 ? 224 LEU A CD1 1 
ATOM   1855 C  CD2 A LEU A 1 223 ? 11.582  -17.017 3.755   0.50 17.16 ? 224 LEU A CD2 1 
ATOM   1856 C  CD2 B LEU A 1 223 ? 9.969   -17.265 1.512   0.50 17.69 ? 224 LEU A CD2 1 
ATOM   1857 N  N   . LYS A 1 224 ? 10.095  -12.088 2.414   1.00 14.34 ? 225 LYS A N   1 
ATOM   1858 C  CA  . LYS A 1 224 ? 10.314  -10.962 1.523   1.00 14.68 ? 225 LYS A CA  1 
ATOM   1859 C  C   . LYS A 1 224 ? 11.207  -9.902  2.165   1.00 13.56 ? 225 LYS A C   1 
ATOM   1860 O  O   . LYS A 1 224 ? 11.983  -9.268  1.475   1.00 13.47 ? 225 LYS A O   1 
ATOM   1861 C  CB  . LYS A 1 224 ? 8.991   -10.469 0.914   1.00 18.35 ? 225 LYS A CB  1 
ATOM   1862 C  CG  . LYS A 1 224 ? 8.373   -11.516 -0.041  1.00 21.46 ? 225 LYS A CG  1 
ATOM   1863 C  CD  . LYS A 1 224 ? 7.097   -11.185 -0.835  1.00 27.30 ? 225 LYS A CD  1 
ATOM   1864 C  CE  . LYS A 1 224 ? 6.643   -12.281 -1.801  1.00 27.93 ? 225 LYS A CE  1 
ATOM   1865 N  NZ  . LYS A 1 224 ? 5.379   -11.931 -2.505  1.00 31.57 ? 225 LYS A NZ  1 
ATOM   1866 N  N   . PHE A 1 225 ? 11.103  -9.708  3.482   1.00 11.93 ? 226 PHE A N   1 
ATOM   1867 C  CA  . PHE A 1 225 ? 12.059  -8.804  4.118   1.00 12.06 ? 226 PHE A CA  1 
ATOM   1868 C  C   . PHE A 1 225 ? 13.496  -9.268  3.898   1.00 11.23 ? 226 PHE A C   1 
ATOM   1869 O  O   . PHE A 1 225 ? 14.412  -8.471  3.706   1.00 12.13 ? 226 PHE A O   1 
ATOM   1870 C  CB  . PHE A 1 225 ? 11.875  -8.819  5.643   1.00 11.07 ? 226 PHE A CB  1 
ATOM   1871 C  CG  . PHE A 1 225 ? 10.650  -8.146  6.239   1.00 11.60 ? 226 PHE A CG  1 
ATOM   1872 C  CD1 . PHE A 1 225 ? 9.578   -7.660  5.493   1.00 13.29 ? 226 PHE A CD1 1 
ATOM   1873 C  CD2 . PHE A 1 225 ? 10.574  -8.017  7.614   1.00 12.13 ? 226 PHE A CD2 1 
ATOM   1874 C  CE1 . PHE A 1 225 ? 8.488   -7.055  6.109   1.00 15.63 ? 226 PHE A CE1 1 
ATOM   1875 C  CE2 . PHE A 1 225 ? 9.489   -7.430  8.242   1.00 15.09 ? 226 PHE A CE2 1 
ATOM   1876 C  CZ  . PHE A 1 225 ? 8.469   -6.918  7.485   1.00 13.79 ? 226 PHE A CZ  1 
ATOM   1877 N  N   . ARG A 1 226 ? 13.663  -10.608 3.925   1.00 11.49 ? 227 ARG A N   1 
ATOM   1878 C  CA  . ARG A 1 226 ? 14.990  -11.211 3.845   1.00 11.86 ? 227 ARG A CA  1 
ATOM   1879 C  C   . ARG A 1 226 ? 15.586  -11.156 2.425   1.00 12.62 ? 227 ARG A C   1 
ATOM   1880 O  O   . ARG A 1 226 ? 16.745  -11.516 2.250   1.00 14.29 ? 227 ARG A O   1 
ATOM   1881 C  CB  . ARG A 1 226 ? 14.957  -12.663 4.378   1.00 11.72 ? 227 ARG A CB  1 
ATOM   1882 C  CG  . ARG A 1 226 ? 14.460  -12.780 5.816   1.00 10.85 ? 227 ARG A CG  1 
ATOM   1883 C  CD  . ARG A 1 226 ? 14.578  -14.244 6.205   1.00 12.11 ? 227 ARG A CD  1 
ATOM   1884 N  NE  . ARG A 1 226 ? 14.014  -14.419 7.562   1.00 13.06 ? 227 ARG A NE  1 
ATOM   1885 C  CZ  . ARG A 1 226 ? 12.982  -15.204 7.837   1.00 14.08 ? 227 ARG A CZ  1 
ATOM   1886 N  NH1 . ARG A 1 226 ? 12.518  -15.995 6.888   1.00 16.77 ? 227 ARG A NH1 1 
ATOM   1887 N  NH2 . ARG A 1 226 ? 12.462  -15.271 9.053   1.00 14.50 ? 227 ARG A NH2 1 
ATOM   1888 N  N   A LYS A 1 227 ? 14.817  -10.659 1.450   0.50 12.45 ? 228 LYS A N   1 
ATOM   1889 N  N   B LYS A 1 227 ? 14.815  -10.659 1.451   0.50 12.54 ? 228 LYS A N   1 
ATOM   1890 C  CA  A LYS A 1 227 ? 15.330  -10.559 0.097   0.50 13.28 ? 228 LYS A CA  1 
ATOM   1891 C  CA  B LYS A 1 227 ? 15.322  -10.559 0.096   0.50 13.41 ? 228 LYS A CA  1 
ATOM   1892 C  C   A LYS A 1 227 ? 15.935  -9.186  -0.116  0.50 12.11 ? 228 LYS A C   1 
ATOM   1893 C  C   B LYS A 1 227 ? 15.927  -9.185  -0.120  0.50 12.24 ? 228 LYS A C   1 
ATOM   1894 O  O   A LYS A 1 227 ? 16.593  -8.975  -1.128  0.50 14.90 ? 228 LYS A O   1 
ATOM   1895 O  O   B LYS A 1 227 ? 16.591  -8.977  -1.129  0.50 15.21 ? 228 LYS A O   1 
ATOM   1896 C  CB  A LYS A 1 227 ? 14.208  -10.823 -0.906  0.50 14.41 ? 228 LYS A CB  1 
ATOM   1897 C  CB  B LYS A 1 227 ? 14.213  -10.883 -0.906  0.50 14.61 ? 228 LYS A CB  1 
ATOM   1898 C  CG  A LYS A 1 227 ? 13.734  -12.269 -0.886  0.50 17.11 ? 228 LYS A CG  1 
ATOM   1899 C  CG  B LYS A 1 227 ? 13.897  -12.375 -0.941  0.50 17.16 ? 228 LYS A CG  1 
ATOM   1900 C  CD  A LYS A 1 227 ? 12.645  -12.518 -1.905  0.50 20.50 ? 228 LYS A CD  1 
ATOM   1901 C  CD  B LYS A 1 227 ? 13.029  -12.792 -2.116  0.50 20.52 ? 228 LYS A CD  1 
ATOM   1902 C  CE  A LYS A 1 227 ? 13.161  -12.320 -3.316  0.50 21.54 ? 228 LYS A CE  1 
ATOM   1903 C  CE  B LYS A 1 227 ? 12.717  -14.270 -2.128  0.50 21.81 ? 228 LYS A CE  1 
ATOM   1904 N  N   . LEU A 1 228 ? 15.695  -8.240  0.799   1.00 11.04 ? 229 LEU A N   1 
ATOM   1905 C  CA  . LEU A 1 228 ? 16.394  -6.972  0.720   1.00 10.90 ? 229 LEU A CA  1 
ATOM   1906 C  C   . LEU A 1 228 ? 17.887  -7.161  0.878   1.00 11.41 ? 229 LEU A C   1 
ATOM   1907 O  O   . LEU A 1 228 ? 18.398  -8.201  1.274   1.00 12.21 ? 229 LEU A O   1 
ATOM   1908 C  CB  . LEU A 1 228 ? 15.906  -6.015  1.811   1.00 10.52 ? 229 LEU A CB  1 
ATOM   1909 C  CG  . LEU A 1 228 ? 14.460  -5.595  1.622   1.00 11.24 ? 229 LEU A CG  1 
ATOM   1910 C  CD1 . LEU A 1 228 ? 13.968  -4.946  2.929   1.00 12.25 ? 229 LEU A CD1 1 
ATOM   1911 C  CD2 . LEU A 1 228 ? 14.393  -4.554  0.480   1.00 12.52 ? 229 LEU A CD2 1 
ATOM   1912 N  N   . ASN A 1 229 ? 18.608  -6.096  0.524   1.00 12.06 ? 230 ASN A N   1 
ATOM   1913 C  CA  . ASN A 1 229 ? 20.076  -6.131  0.509   1.00 11.46 ? 230 ASN A CA  1 
ATOM   1914 C  C   . ASN A 1 229 ? 20.629  -5.006  1.384   1.00 12.13 ? 230 ASN A C   1 
ATOM   1915 O  O   . ASN A 1 229 ? 20.172  -3.859  1.302   1.00 13.42 ? 230 ASN A O   1 
ATOM   1916 C  CB  . ASN A 1 229 ? 20.665  -5.903  -0.897  1.00 12.33 ? 230 ASN A CB  1 
ATOM   1917 C  CG  . ASN A 1 229 ? 20.597  -7.084  -1.825  1.00 15.38 ? 230 ASN A CG  1 
ATOM   1918 O  OD1 . ASN A 1 229 ? 21.156  -6.961  -2.937  1.00 18.26 ? 230 ASN A OD1 1 
ATOM   1919 N  ND2 . ASN A 1 229 ? 19.992  -8.188  -1.425  1.00 15.37 ? 230 ASN A ND2 1 
ATOM   1920 N  N   . PHE A 1 230 ? 21.708  -5.314  2.114   1.00 11.66 ? 231 PHE A N   1 
ATOM   1921 C  CA  . PHE A 1 230 ? 22.445  -4.265  2.826   1.00 12.07 ? 231 PHE A CA  1 
ATOM   1922 C  C   . PHE A 1 230 ? 23.232  -3.367  1.879   1.00 13.30 ? 231 PHE A C   1 
ATOM   1923 O  O   . PHE A 1 230 ? 23.447  -2.174  2.122   1.00 13.86 ? 231 PHE A O   1 
ATOM   1924 C  CB  . PHE A 1 230 ? 23.466  -4.851  3.809   1.00 12.31 ? 231 PHE A CB  1 
ATOM   1925 C  CG  . PHE A 1 230 ? 22.940  -5.417  5.114   1.00 12.15 ? 231 PHE A CG  1 
ATOM   1926 C  CD1 . PHE A 1 230 ? 22.156  -4.667  5.996   1.00 11.86 ? 231 PHE A CD1 1 
ATOM   1927 C  CD2 . PHE A 1 230 ? 23.255  -6.722  5.462   1.00 12.90 ? 231 PHE A CD2 1 
ATOM   1928 C  CE1 . PHE A 1 230 ? 21.692  -5.225  7.197   1.00 12.20 ? 231 PHE A CE1 1 
ATOM   1929 C  CE2 . PHE A 1 230 ? 22.782  -7.286  6.648   1.00 12.22 ? 231 PHE A CE2 1 
ATOM   1930 C  CZ  . PHE A 1 230 ? 22.046  -6.528  7.543   1.00 12.07 ? 231 PHE A CZ  1 
ATOM   1931 N  N   . ASN A 1 231 ? 23.724  -3.990  0.807   1.00 13.26 ? 232 ASN A N   1 
ATOM   1932 C  CA  . ASN A 1 231 ? 24.614  -3.308  -0.130  1.00 13.30 ? 232 ASN A CA  1 
ATOM   1933 C  C   . ASN A 1 231 ? 23.863  -2.413  -1.110  1.00 13.26 ? 232 ASN A C   1 
ATOM   1934 O  O   . ASN A 1 231 ? 22.656  -2.520  -1.290  1.00 13.97 ? 232 ASN A O   1 
ATOM   1935 C  CB  . ASN A 1 231 ? 25.329  -4.381  -0.954  1.00 14.03 ? 232 ASN A CB  1 
ATOM   1936 C  CG  . ASN A 1 231 ? 24.348  -5.328  -1.623  1.00 13.96 ? 232 ASN A CG  1 
ATOM   1937 O  OD1 . ASN A 1 231 ? 23.822  -6.246  -0.991  1.00 15.00 ? 232 ASN A OD1 1 
ATOM   1938 N  ND2 . ASN A 1 231 ? 24.044  -5.131  -2.909  1.00 14.83 ? 232 ASN A ND2 1 
ATOM   1939 N  N   . GLY A 1 232 ? 24.647  -1.497  -1.718  1.00 13.53 ? 233 GLY A N   1 
ATOM   1940 C  CA  . GLY A 1 232 ? 24.148  -0.705  -2.835  1.00 13.22 ? 233 GLY A CA  1 
ATOM   1941 C  C   . GLY A 1 232 ? 24.116  -1.496  -4.143  1.00 13.20 ? 233 GLY A C   1 
ATOM   1942 O  O   . GLY A 1 232 ? 24.711  -2.561  -4.248  1.00 13.95 ? 233 GLY A O   1 
ATOM   1943 N  N   . GLU A 1 233 ? 23.339  -0.988  -5.123  1.00 15.16 ? 234 GLU A N   1 
ATOM   1944 C  CA  . GLU A 1 233 ? 23.307  -1.604  -6.446  1.00 14.80 ? 234 GLU A CA  1 
ATOM   1945 C  C   . GLU A 1 233 ? 24.705  -1.690  -7.050  1.00 14.27 ? 234 GLU A C   1 
ATOM   1946 O  O   . GLU A 1 233 ? 25.500  -0.788  -6.909  1.00 16.04 ? 234 GLU A O   1 
ATOM   1947 C  CB  . GLU A 1 233 ? 22.416  -0.740  -7.357  1.00 17.08 ? 234 GLU A CB  1 
ATOM   1948 C  CG  . GLU A 1 233 ? 22.229  -1.325  -8.751  1.00 17.09 ? 234 GLU A CG  1 
ATOM   1949 C  CD  . GLU A 1 233 ? 21.317  -0.523  -9.654  1.00 26.87 ? 234 GLU A CD  1 
ATOM   1950 O  OE1 . GLU A 1 233 ? 20.933  0.643   -9.279  1.00 25.11 ? 234 GLU A OE1 1 
ATOM   1951 O  OE2 . GLU A 1 233 ? 21.080  -1.029  -10.778 1.00 27.77 ? 234 GLU A OE2 1 
ATOM   1952 N  N   . GLY A 1 234 ? 24.988  -2.861  -7.604  1.00 17.62 ? 235 GLY A N   1 
ATOM   1953 C  CA  . GLY A 1 234 ? 26.258  -3.029  -8.284  1.00 20.15 ? 235 GLY A CA  1 
ATOM   1954 C  C   . GLY A 1 234 ? 27.356  -3.519  -7.356  1.00 22.34 ? 235 GLY A C   1 
ATOM   1955 O  O   . GLY A 1 234 ? 28.479  -3.740  -7.808  1.00 22.84 ? 235 GLY A O   1 
ATOM   1956 N  N   . GLU A 1 235 ? 27.020  -3.720  -6.067  1.00 19.48 ? 236 GLU A N   1 
ATOM   1957 C  CA  . GLU A 1 235 ? 28.003  -4.171  -5.091  1.00 18.36 ? 236 GLU A CA  1 
ATOM   1958 C  C   . GLU A 1 235 ? 27.679  -5.627  -4.791  1.00 18.16 ? 236 GLU A C   1 
ATOM   1959 O  O   . GLU A 1 235 ? 26.597  -6.121  -5.131  1.00 19.60 ? 236 GLU A O   1 
ATOM   1960 C  CB  . GLU A 1 235 ? 27.929  -3.344  -3.799  1.00 16.56 ? 236 GLU A CB  1 
ATOM   1961 C  CG  . GLU A 1 235 ? 28.363  -1.896  -3.962  1.00 20.48 ? 236 GLU A CG  1 
ATOM   1962 C  CD  . GLU A 1 235 ? 28.120  -1.098  -2.694  1.00 27.36 ? 236 GLU A CD  1 
ATOM   1963 O  OE1 . GLU A 1 235 ? 27.461  -1.633  -1.786  1.00 25.50 ? 236 GLU A OE1 1 
ATOM   1964 O  OE2 . GLU A 1 235 ? 28.618  0.045   -2.580  1.00 32.70 ? 236 GLU A OE2 1 
ATOM   1965 N  N   . PRO A 1 236 ? 28.615  -6.364  -4.156  1.00 17.65 ? 237 PRO A N   1 
ATOM   1966 C  CA  . PRO A 1 236 ? 28.393  -7.777  -3.850  1.00 16.36 ? 237 PRO A CA  1 
ATOM   1967 C  C   . PRO A 1 236 ? 27.121  -7.885  -3.002  1.00 17.14 ? 237 PRO A C   1 
ATOM   1968 O  O   . PRO A 1 236 ? 26.903  -7.081  -2.077  1.00 17.73 ? 237 PRO A O   1 
ATOM   1969 C  CB  . PRO A 1 236 ? 29.650  -8.171  -3.063  1.00 18.61 ? 237 PRO A CB  1 
ATOM   1970 C  CG  . PRO A 1 236 ? 30.704  -7.179  -3.535  1.00 20.00 ? 237 PRO A CG  1 
ATOM   1971 C  CD  . PRO A 1 236 ? 29.939  -5.885  -3.749  1.00 19.76 ? 237 PRO A CD  1 
ATOM   1972 N  N   . GLU A 1 237 ? 26.330  -8.903  -3.291  1.00 16.32 ? 238 GLU A N   1 
ATOM   1973 C  CA  . GLU A 1 237 ? 25.008  -9.013  -2.684  1.00 16.55 ? 238 GLU A CA  1 
ATOM   1974 C  C   . GLU A 1 237 ? 25.158  -9.578  -1.273  1.00 16.72 ? 238 GLU A C   1 
ATOM   1975 O  O   . GLU A 1 237 ? 25.682  -10.667 -1.053  1.00 16.41 ? 238 GLU A O   1 
ATOM   1976 C  CB  . GLU A 1 237 ? 24.071  -9.848  -3.542  1.00 19.66 ? 238 GLU A CB  1 
ATOM   1977 C  CG  . GLU A 1 237 ? 22.729  -10.007 -2.878  1.00 21.96 ? 238 GLU A CG  1 
ATOM   1978 C  CD  . GLU A 1 237 ? 21.570  -10.525 -3.704  1.00 26.00 ? 238 GLU A CD  1 
ATOM   1979 O  OE1 . GLU A 1 237 ? 21.819  -11.026 -4.838  1.00 30.13 ? 238 GLU A OE1 1 
ATOM   1980 O  OE2 . GLU A 1 237 ? 20.425  -10.429 -3.214  1.00 20.76 ? 238 GLU A OE2 1 
ATOM   1981 N  N   A GLU A 1 238 ? 24.681  -8.807  -0.295  0.50 15.09 ? 239 GLU A N   1 
ATOM   1982 N  N   B GLU A 1 238 ? 24.657  -8.779  -0.326  0.50 14.59 ? 239 GLU A N   1 
ATOM   1983 C  CA  A GLU A 1 238 ? 24.638  -9.315  1.070   0.50 15.62 ? 239 GLU A CA  1 
ATOM   1984 C  CA  B GLU A 1 238 ? 24.591  -9.115  1.089   0.50 15.10 ? 239 GLU A CA  1 
ATOM   1985 C  C   A GLU A 1 238 ? 23.239  -9.094  1.628   0.50 13.15 ? 239 GLU A C   1 
ATOM   1986 C  C   B GLU A 1 238 ? 23.127  -9.064  1.505   0.50 12.62 ? 239 GLU A C   1 
ATOM   1987 O  O   A GLU A 1 238 ? 22.798  -7.962  1.786   0.50 13.59 ? 239 GLU A O   1 
ATOM   1988 O  O   B GLU A 1 238 ? 22.526  -7.996  1.463   0.50 13.20 ? 239 GLU A O   1 
ATOM   1989 C  CB  A GLU A 1 238 ? 25.771  -8.748  1.929   0.50 16.33 ? 239 GLU A CB  1 
ATOM   1990 C  CB  B GLU A 1 238 ? 25.252  -8.011  1.910   0.50 14.71 ? 239 GLU A CB  1 
ATOM   1991 C  CG  A GLU A 1 238 ? 25.845  -9.326  3.341   0.50 17.77 ? 239 GLU A CG  1 
ATOM   1992 C  CG  B GLU A 1 238 ? 26.758  -7.835  1.760   0.50 18.14 ? 239 GLU A CG  1 
ATOM   1993 C  CD  A GLU A 1 238 ? 26.170  -10.807 3.564   0.50 18.05 ? 239 GLU A CD  1 
ATOM   1994 C  CD  B GLU A 1 238 ? 27.257  -6.706  2.657   0.50 21.72 ? 239 GLU A CD  1 
ATOM   1995 O  OE1 A GLU A 1 238 ? 26.489  -11.559 2.575   0.50 17.60 ? 239 GLU A OE1 1 
ATOM   1996 O  OE1 B GLU A 1 238 ? 27.464  -6.952  3.874   0.50 23.98 ? 239 GLU A OE1 1 
ATOM   1997 O  OE2 A GLU A 1 238 ? 26.089  -11.243 4.733   0.50 20.12 ? 239 GLU A OE2 1 
ATOM   1998 O  OE2 B GLU A 1 238 ? 27.362  -5.566  2.161   0.50 22.13 ? 239 GLU A OE2 1 
ATOM   1999 N  N   . LEU A 1 239 ? 22.554  -10.211 1.890   1.00 13.16 ? 240 LEU A N   1 
ATOM   2000 C  CA  . LEU A 1 239 ? 21.152  -10.198 2.285   1.00 11.73 ? 240 LEU A CA  1 
ATOM   2001 C  C   . LEU A 1 239 ? 20.972  -9.401  3.584   1.00 11.56 ? 240 LEU A C   1 
ATOM   2002 O  O   . LEU A 1 239 ? 21.744  -9.570  4.523   1.00 12.76 ? 240 LEU A O   1 
ATOM   2003 C  CB  . LEU A 1 239 ? 20.607  -11.608 2.493   1.00 12.45 ? 240 LEU A CB  1 
ATOM   2004 C  CG  . LEU A 1 239 ? 20.568  -12.459 1.206   1.00 13.99 ? 240 LEU A CG  1 
ATOM   2005 C  CD1 . LEU A 1 239 ? 20.125  -13.868 1.528   1.00 15.74 ? 240 LEU A CD1 1 
ATOM   2006 C  CD2 . LEU A 1 239 ? 19.621  -11.880 0.145   1.00 14.69 ? 240 LEU A CD2 1 
ATOM   2007 N  N   . MET A 1 240 ? 19.956  -8.534  3.573   1.00 10.70 ? 241 MET A N   1 
ATOM   2008 C  CA  . MET A 1 240 ? 19.626  -7.802  4.796   1.00 10.31 ? 241 MET A CA  1 
ATOM   2009 C  C   . MET A 1 240 ? 18.804  -8.728  5.692   1.00 10.91 ? 241 MET A C   1 
ATOM   2010 O  O   . MET A 1 240 ? 17.600  -8.893  5.574   1.00 11.01 ? 241 MET A O   1 
ATOM   2011 C  CB  . MET A 1 240 ? 18.833  -6.551  4.403   1.00 11.21 ? 241 MET A CB  1 
ATOM   2012 C  CG  . MET A 1 240 ? 18.463  -5.671  5.626   1.00 10.41 ? 241 MET A CG  1 
ATOM   2013 S  SD  . MET A 1 240 ? 17.507  -4.219  5.146   1.00 11.73 ? 241 MET A SD  1 
ATOM   2014 C  CE  . MET A 1 240 ? 18.796  -3.200  4.411   1.00 10.92 ? 241 MET A CE  1 
ATOM   2015 N  N   . VAL A 1 241 ? 19.542  -9.341  6.600   1.00 9.28  ? 242 VAL A N   1 
ATOM   2016 C  CA  . VAL A 1 241 ? 19.001  -10.223 7.610   1.00 10.19 ? 242 VAL A CA  1 
ATOM   2017 C  C   . VAL A 1 241 ? 19.796  -9.990  8.895   1.00 10.98 ? 242 VAL A C   1 
ATOM   2018 O  O   . VAL A 1 241 ? 20.964  -9.564  8.883   1.00 10.14 ? 242 VAL A O   1 
ATOM   2019 C  CB  . VAL A 1 241 ? 19.088  -11.714 7.208   1.00 12.01 ? 242 VAL A CB  1 
ATOM   2020 C  CG1 . VAL A 1 241 ? 18.203  -12.013 6.000   1.00 11.80 ? 242 VAL A CG1 1 
ATOM   2021 C  CG2 . VAL A 1 241 ? 20.513  -12.215 7.056   1.00 12.39 ? 242 VAL A CG2 1 
ATOM   2022 N  N   . ASP A 1 242 ? 19.148  -10.308 10.034  1.00 9.13  ? 243 ASP A N   1 
ATOM   2023 C  CA  . ASP A 1 242 ? 19.805  -10.191 11.358  1.00 10.00 ? 243 ASP A CA  1 
ATOM   2024 C  C   . ASP A 1 242 ? 20.287  -8.778  11.642  1.00 9.05  ? 243 ASP A C   1 
ATOM   2025 O  O   . ASP A 1 242 ? 21.384  -8.545  12.138  1.00 9.66  ? 243 ASP A O   1 
ATOM   2026 C  CB  . ASP A 1 242 ? 20.909  -11.247 11.597  1.00 10.10 ? 243 ASP A CB  1 
ATOM   2027 C  CG  . ASP A 1 242 ? 20.305  -12.624 11.654  1.00 11.69 ? 243 ASP A CG  1 
ATOM   2028 O  OD1 . ASP A 1 242 ? 19.236  -12.793 12.277  1.00 9.82  ? 243 ASP A OD1 1 
ATOM   2029 O  OD2 . ASP A 1 242 ? 20.957  -13.558 11.067  1.00 14.25 ? 243 ASP A OD2 1 
ATOM   2030 N  N   . ASN A 1 243 ? 19.410  -7.828  11.313  1.00 8.03  ? 244 ASN A N   1 
ATOM   2031 C  CA  . ASN A 1 243 ? 19.716  -6.417  11.574  1.00 7.80  ? 244 ASN A CA  1 
ATOM   2032 C  C   . ASN A 1 243 ? 19.092  -5.979  12.891  1.00 8.44  ? 244 ASN A C   1 
ATOM   2033 O  O   . ASN A 1 243 ? 18.404  -4.958  12.952  1.00 9.36  ? 244 ASN A O   1 
ATOM   2034 C  CB  . ASN A 1 243 ? 19.182  -5.572  10.394  1.00 8.72  ? 244 ASN A CB  1 
ATOM   2035 C  CG  . ASN A 1 243 ? 17.680  -5.697  10.152  1.00 9.08  ? 244 ASN A CG  1 
ATOM   2036 O  OD1 . ASN A 1 243 ? 17.057  -6.626  10.660  1.00 10.16 ? 244 ASN A OD1 1 
ATOM   2037 N  ND2 . ASN A 1 243 ? 17.097  -4.825  9.343   1.00 11.13 ? 244 ASN A ND2 1 
ATOM   2038 N  N   . TRP A 1 244 ? 19.405  -6.755  13.917  1.00 8.07  ? 245 TRP A N   1 
ATOM   2039 C  CA  . TRP A 1 244 ? 18.977  -6.482  15.282  1.00 8.11  ? 245 TRP A CA  1 
ATOM   2040 C  C   . TRP A 1 244 ? 20.163  -6.385  16.220  1.00 8.35  ? 245 TRP A C   1 
ATOM   2041 O  O   . TRP A 1 244 ? 21.144  -7.116  16.056  1.00 9.37  ? 245 TRP A O   1 
ATOM   2042 C  CB  . TRP A 1 244 ? 18.004  -7.571  15.751  1.00 8.22  ? 245 TRP A CB  1 
ATOM   2043 C  CG  . TRP A 1 244 ? 18.463  -8.995  15.565  1.00 8.27  ? 245 TRP A CG  1 
ATOM   2044 C  CD1 . TRP A 1 244 ? 18.347  -9.726  14.425  1.00 8.97  ? 245 TRP A CD1 1 
ATOM   2045 C  CD2 . TRP A 1 244 ? 19.032  -9.868  16.558  1.00 8.25  ? 245 TRP A CD2 1 
ATOM   2046 N  NE1 . TRP A 1 244 ? 18.842  -10.982 14.636  1.00 8.23  ? 245 TRP A NE1 1 
ATOM   2047 C  CE2 . TRP A 1 244 ? 19.260  -11.110 15.947  1.00 8.34  ? 245 TRP A CE2 1 
ATOM   2048 C  CE3 . TRP A 1 244 ? 19.304  -9.727  17.923  1.00 10.16 ? 245 TRP A CE3 1 
ATOM   2049 C  CZ2 . TRP A 1 244 ? 19.797  -12.214 16.633  1.00 8.75  ? 245 TRP A CZ2 1 
ATOM   2050 C  CZ3 . TRP A 1 244 ? 19.823  -10.798 18.615  1.00 10.65 ? 245 TRP A CZ3 1 
ATOM   2051 C  CH2 . TRP A 1 244 ? 20.051  -12.013 17.970  1.00 9.66  ? 245 TRP A CH2 1 
ATOM   2052 N  N   . ARG A 1 245 ? 20.059  -5.499  17.201  1.00 8.68  ? 246 ARG A N   1 
ATOM   2053 C  CA  . ARG A 1 245 ? 21.015  -5.447  18.297  1.00 8.84  ? 246 ARG A CA  1 
ATOM   2054 C  C   . ARG A 1 245 ? 20.539  -6.356  19.418  1.00 8.81  ? 246 ARG A C   1 
ATOM   2055 O  O   . ARG A 1 245 ? 19.349  -6.376  19.710  1.00 9.65  ? 246 ARG A O   1 
ATOM   2056 C  CB  . ARG A 1 245 ? 21.069  -4.013  18.833  1.00 9.04  ? 246 ARG A CB  1 
ATOM   2057 C  CG  . ARG A 1 245 ? 22.204  -3.770  19.810  1.00 9.10  ? 246 ARG A CG  1 
ATOM   2058 C  CD  . ARG A 1 245 ? 22.117  -2.424  20.486  1.00 8.98  ? 246 ARG A CD  1 
ATOM   2059 N  NE  . ARG A 1 245 ? 23.377  -2.135  21.179  1.00 9.76  ? 246 ARG A NE  1 
ATOM   2060 C  CZ  . ARG A 1 245 ? 23.556  -1.093  22.001  1.00 9.51  ? 246 ARG A CZ  1 
ATOM   2061 N  NH1 . ARG A 1 245 ? 22.564  -0.272  22.342  1.00 9.79  ? 246 ARG A NH1 1 
ATOM   2062 N  NH2 . ARG A 1 245 ? 24.787  -0.844  22.457  1.00 11.27 ? 246 ARG A NH2 1 
ATOM   2063 N  N   . PRO A 1 246 ? 21.414  -7.166  20.048  1.00 9.91  ? 247 PRO A N   1 
ATOM   2064 C  CA  . PRO A 1 246 ? 20.978  -7.985  21.178  1.00 10.00 ? 247 PRO A CA  1 
ATOM   2065 C  C   . PRO A 1 246 ? 20.617  -7.131  22.385  1.00 9.98  ? 247 PRO A C   1 
ATOM   2066 O  O   . PRO A 1 246 ? 20.997  -5.954  22.510  1.00 10.34 ? 247 PRO A O   1 
ATOM   2067 C  CB  . PRO A 1 246 ? 22.246  -8.782  21.535  1.00 11.98 ? 247 PRO A CB  1 
ATOM   2068 C  CG  . PRO A 1 246 ? 23.147  -8.690  20.319  1.00 15.67 ? 247 PRO A CG  1 
ATOM   2069 C  CD  . PRO A 1 246 ? 22.809  -7.384  19.639  1.00 11.61 ? 247 PRO A CD  1 
ATOM   2070 N  N   . ALA A 1 247 ? 19.975  -7.802  23.342  1.00 10.18 ? 248 ALA A N   1 
ATOM   2071 C  CA  . ALA A 1 247 ? 19.623  -7.162  24.585  1.00 9.45  ? 248 ALA A CA  1 
ATOM   2072 C  C   . ALA A 1 247 ? 20.871  -6.692  25.324  1.00 9.68  ? 248 ALA A C   1 
ATOM   2073 O  O   . ALA A 1 247 ? 21.903  -7.361  25.382  1.00 11.29 ? 248 ALA A O   1 
ATOM   2074 C  CB  . ALA A 1 247 ? 18.809  -8.132  25.423  1.00 11.60 ? 248 ALA A CB  1 
ATOM   2075 N  N   . GLN A 1 248 ? 20.721  -5.511  25.892  1.00 8.79  ? 249 GLN A N   1 
ATOM   2076 C  CA  . GLN A 1 248 ? 21.731  -4.762  26.607  1.00 9.64  ? 249 GLN A CA  1 
ATOM   2077 C  C   . GLN A 1 248 ? 21.454  -4.793  28.103  1.00 10.47 ? 249 GLN A C   1 
ATOM   2078 O  O   . GLN A 1 248 ? 20.323  -4.971  28.507  1.00 11.18 ? 249 GLN A O   1 
ATOM   2079 C  CB  . GLN A 1 248 ? 21.812  -3.328  26.079  1.00 10.55 ? 249 GLN A CB  1 
ATOM   2080 C  CG  . GLN A 1 248 ? 22.135  -3.288  24.582  1.00 9.74  ? 249 GLN A CG  1 
ATOM   2081 C  CD  . GLN A 1 248 ? 23.484  -3.926  24.273  1.00 11.33 ? 249 GLN A CD  1 
ATOM   2082 O  OE1 . GLN A 1 248 ? 24.521  -3.613  24.895  1.00 14.61 ? 249 GLN A OE1 1 
ATOM   2083 N  NE2 . GLN A 1 248 ? 23.446  -4.881  23.362  1.00 11.62 ? 249 GLN A NE2 1 
ATOM   2084 N  N   . PRO A 1 249 ? 22.458  -4.505  28.984  1.00 12.37 ? 250 PRO A N   1 
ATOM   2085 C  CA  . PRO A 1 249 ? 22.216  -4.565  30.434  1.00 12.99 ? 250 PRO A CA  1 
ATOM   2086 C  C   . PRO A 1 249 ? 21.131  -3.564  30.850  1.00 11.48 ? 250 PRO A C   1 
ATOM   2087 O  O   . PRO A 1 249 ? 21.174  -2.395  30.473  1.00 12.26 ? 250 PRO A O   1 
ATOM   2088 C  CB  . PRO A 1 249 ? 23.614  -4.191  30.982  1.00 15.72 ? 250 PRO A CB  1 
ATOM   2089 C  CG  . PRO A 1 249 ? 24.567  -4.592  29.880  1.00 16.07 ? 250 PRO A CG  1 
ATOM   2090 C  CD  . PRO A 1 249 ? 23.840  -4.168  28.610  1.00 14.91 ? 250 PRO A CD  1 
ATOM   2091 N  N   . LEU A 1 250 ? 20.225  -4.034  31.717  1.00 13.59 ? 251 LEU A N   1 
ATOM   2092 C  CA  . LEU A 1 250 ? 19.172  -3.171  32.241  1.00 12.76 ? 251 LEU A CA  1 
ATOM   2093 C  C   . LEU A 1 250 ? 19.731  -2.091  33.163  1.00 12.71 ? 251 LEU A C   1 
ATOM   2094 O  O   . LEU A 1 250 ? 19.194  -0.993  33.263  1.00 12.46 ? 251 LEU A O   1 
ATOM   2095 C  CB  . LEU A 1 250 ? 18.099  -4.028  32.908  1.00 13.64 ? 251 LEU A CB  1 
ATOM   2096 C  CG  . LEU A 1 250 ? 16.816  -3.317  33.310  1.00 13.60 ? 251 LEU A CG  1 
ATOM   2097 C  CD1 . LEU A 1 250 ? 16.120  -2.712  32.116  1.00 13.90 ? 251 LEU A CD1 1 
ATOM   2098 C  CD2 . LEU A 1 250 ? 15.874  -4.285  34.005  1.00 15.66 ? 251 LEU A CD2 1 
ATOM   2099 N  N   . LYS A 1 251 ? 20.808  -2.446  33.861  1.00 14.89 ? 252 LYS A N   1 
ATOM   2100 C  CA  . LYS A 1 251 ? 21.468  -1.509  34.806  1.00 16.58 ? 252 LYS A CA  1 
ATOM   2101 C  C   . LYS A 1 251 ? 20.488  -1.083  35.899  1.00 17.39 ? 252 LYS A C   1 
ATOM   2102 O  O   . LYS A 1 251 ? 19.853  -1.980  36.448  1.00 22.57 ? 252 LYS A O   1 
ATOM   2103 C  CB  . LYS A 1 251 ? 22.248  -0.434  34.052  1.00 18.21 ? 252 LYS A CB  1 
ATOM   2104 C  CG  . LYS A 1 251 ? 23.450  -1.056  33.367  1.00 21.05 ? 252 LYS A CG  1 
ATOM   2105 C  CD  . LYS A 1 251 ? 24.348  -0.152  32.648  1.00 26.02 ? 252 LYS A CD  1 
ATOM   2106 C  CE  . LYS A 1 251 ? 25.617  -0.888  32.305  1.00 25.20 ? 252 LYS A CE  1 
ATOM   2107 N  NZ  . LYS A 1 251 ? 26.406  -0.052  31.369  1.00 27.18 ? 252 LYS A NZ  1 
ATOM   2108 N  N   . ASN A 1 252 ? 20.295  0.211   36.164  1.00 18.78 ? 253 ASN A N   1 
ATOM   2109 C  CA  . ASN A 1 252 ? 19.461  0.468   37.340  1.00 23.54 ? 253 ASN A CA  1 
ATOM   2110 C  C   . ASN A 1 252 ? 17.939  0.419   37.024  1.00 24.23 ? 253 ASN A C   1 
ATOM   2111 O  O   . ASN A 1 252 ? 17.092  0.551   37.914  1.00 25.36 ? 253 ASN A O   1 
ATOM   2112 C  CB  . ASN A 1 252 ? 20.056  1.664   38.100  1.00 30.09 ? 253 ASN A CB  1 
ATOM   2113 C  CG  . ASN A 1 252 ? 19.386  2.000   39.420  1.00 43.63 ? 253 ASN A CG  1 
ATOM   2114 O  OD1 . ASN A 1 252 ? 19.064  1.113   40.220  1.00 48.85 ? 253 ASN A OD1 1 
ATOM   2115 N  ND2 . ASN A 1 252 ? 19.206  3.289   39.669  1.00 46.30 ? 253 ASN A ND2 1 
ATOM   2116 N  N   . ARG A 1 253 ? 17.556  0.200   35.759  1.00 15.02 ? 254 ARG A N   1 
ATOM   2117 C  CA  . ARG A 1 253 ? 16.280  0.720   35.286  1.00 14.07 ? 254 ARG A CA  1 
ATOM   2118 C  C   . ARG A 1 253 ? 15.143  -0.209  35.689  1.00 14.55 ? 254 ARG A C   1 
ATOM   2119 O  O   . ARG A 1 253 ? 15.343  -1.391  35.947  1.00 17.64 ? 254 ARG A O   1 
ATOM   2120 C  CB  . ARG A 1 253 ? 16.289  0.814   33.752  1.00 11.25 ? 254 ARG A CB  1 
ATOM   2121 C  CG  . ARG A 1 253 ? 17.184  1.919   33.238  1.00 11.41 ? 254 ARG A CG  1 
ATOM   2122 C  CD  . ARG A 1 253 ? 17.257  1.889   31.736  1.00 11.36 ? 254 ARG A CD  1 
ATOM   2123 N  NE  . ARG A 1 253 ? 18.111  0.778   31.316  1.00 10.75 ? 254 ARG A NE  1 
ATOM   2124 C  CZ  . ARG A 1 253 ? 18.323  0.464   30.031  1.00 9.42  ? 254 ARG A CZ  1 
ATOM   2125 N  NH1 . ARG A 1 253 ? 17.712  1.153   29.064  1.00 9.66  ? 254 ARG A NH1 1 
ATOM   2126 N  NH2 . ARG A 1 253 ? 19.196  -0.501  29.731  1.00 8.91  ? 254 ARG A NH2 1 
ATOM   2127 N  N   . GLN A 1 254 ? 13.923  0.335   35.754  1.00 12.52 ? 255 GLN A N   1 
ATOM   2128 C  CA  . GLN A 1 254 ? 12.734  -0.465  35.988  1.00 14.00 ? 255 GLN A CA  1 
ATOM   2129 C  C   . GLN A 1 254 ? 11.891  -0.427  34.715  1.00 12.29 ? 255 GLN A C   1 
ATOM   2130 O  O   . GLN A 1 254 ? 11.716  0.640   34.078  1.00 15.91 ? 255 GLN A O   1 
ATOM   2131 C  CB  . GLN A 1 254 ? 11.895  0.153   37.112  1.00 18.01 ? 255 GLN A CB  1 
ATOM   2132 C  CG  . GLN A 1 254 ? 12.615  0.145   38.455  1.00 26.21 ? 255 GLN A CG  1 
ATOM   2133 C  CD  . GLN A 1 254 ? 11.794  -0.327  39.644  1.00 32.55 ? 255 GLN A CD  1 
ATOM   2134 O  OE1 . GLN A 1 254 ? 11.952  0.175   40.761  1.00 40.51 ? 255 GLN A OE1 1 
ATOM   2135 N  NE2 . GLN A 1 254 ? 10.943  -1.330  39.444  1.00 35.44 ? 255 GLN A NE2 1 
ATOM   2136 N  N   . ILE A 1 255 ? 11.351  -1.581  34.358  1.00 10.99 ? 256 ILE A N   1 
ATOM   2137 C  CA  . ILE A 1 255 ? 10.346  -1.673  33.317  1.00 11.71 ? 256 ILE A CA  1 
ATOM   2138 C  C   . ILE A 1 255 ? 8.968   -1.674  33.985  1.00 11.34 ? 256 ILE A C   1 
ATOM   2139 O  O   . ILE A 1 255 ? 8.762   -2.401  34.969  1.00 13.25 ? 256 ILE A O   1 
ATOM   2140 C  CB  . ILE A 1 255 ? 10.573  -2.927  32.477  1.00 9.52  ? 256 ILE A CB  1 
ATOM   2141 C  CG1 . ILE A 1 255 ? 12.017  -2.965  31.949  1.00 10.09 ? 256 ILE A CG1 1 
ATOM   2142 C  CG2 . ILE A 1 255 ? 9.506   -3.044  31.378  1.00 12.01 ? 256 ILE A CG2 1 
ATOM   2143 C  CD1 . ILE A 1 255 ? 12.302  -4.173  31.092  1.00 12.54 ? 256 ILE A CD1 1 
ATOM   2144 N  N   . LYS A 1 256 ? 8.081   -0.821  33.487  1.00 10.77 ? 257 LYS A N   1 
ATOM   2145 C  CA  . LYS A 1 256 ? 6.731   -0.719  34.019  1.00 11.39 ? 257 LYS A CA  1 
ATOM   2146 C  C   . LYS A 1 256 ? 5.756   -1.336  33.045  1.00 12.20 ? 257 LYS A C   1 
ATOM   2147 O  O   . LYS A 1 256 ? 5.908   -1.242  31.827  1.00 12.64 ? 257 LYS A O   1 
ATOM   2148 C  CB  . LYS A 1 256 ? 6.420   0.759   34.272  1.00 12.63 ? 257 LYS A CB  1 
ATOM   2149 C  CG  . LYS A 1 256 ? 7.247   1.331   35.408  1.00 16.92 ? 257 LYS A CG  1 
ATOM   2150 C  CD  . LYS A 1 256 ? 7.081   2.815   35.575  1.00 26.17 ? 257 LYS A CD  1 
ATOM   2151 C  CE  . LYS A 1 256 ? 8.012   3.405   36.622  1.00 34.19 ? 257 LYS A CE  1 
ATOM   2152 N  NZ  . LYS A 1 256 ? 8.239   4.866   36.437  1.00 35.56 ? 257 LYS A NZ  1 
ATOM   2153 N  N   . ALA A 1 257 ? 4.718   -1.981  33.552  1.00 11.30 ? 258 ALA A N   1 
ATOM   2154 C  CA  . ALA A 1 257 ? 3.633   -2.599  32.800  1.00 11.32 ? 258 ALA A CA  1 
ATOM   2155 C  C   . ALA A 1 257 ? 2.373   -1.760  32.943  1.00 11.78 ? 258 ALA A C   1 
ATOM   2156 O  O   . ALA A 1 257 ? 2.042   -1.280  34.053  1.00 13.28 ? 258 ALA A O   1 
ATOM   2157 C  CB  . ALA A 1 257 ? 3.394   -4.034  33.213  1.00 12.44 ? 258 ALA A CB  1 
ATOM   2158 N  N   . SER A 1 258 ? 1.663   -1.617  31.829  1.00 12.26 ? 259 SER A N   1 
ATOM   2159 C  CA  . SER A 1 258 ? 0.387   -0.926  31.845  1.00 12.86 ? 259 SER A CA  1 
ATOM   2160 C  C   . SER A 1 258 ? -0.744  -1.808  32.360  1.00 13.57 ? 259 SER A C   1 
ATOM   2161 O  O   . SER A 1 258 ? -1.860  -1.269  32.447  1.00 17.38 ? 259 SER A O   1 
ATOM   2162 C  CB  . SER A 1 258 ? 0.068   -0.383  30.472  1.00 12.39 ? 259 SER A CB  1 
ATOM   2163 O  OG  . SER A 1 258 ? -0.354  -1.429  29.617  1.00 13.14 ? 259 SER A OG  1 
ATOM   2164 N  N   . PHE A 1 259 ? -0.482  -3.075  32.640  1.00 13.93 ? 260 PHE A N   1 
ATOM   2165 C  CA  . PHE A 1 259 ? -1.565  -4.038  32.789  1.00 16.97 ? 260 PHE A CA  1 
ATOM   2166 C  C   . PHE A 1 259 ? -1.199  -5.013  33.896  1.00 22.87 ? 260 PHE A C   1 
ATOM   2167 O  O   . PHE A 1 259 ? -0.015  -5.202  34.226  1.00 21.36 ? 260 PHE A O   1 
ATOM   2168 C  CB  . PHE A 1 259 ? -1.731  -4.836  31.499  1.00 16.82 ? 260 PHE A CB  1 
ATOM   2169 C  CG  . PHE A 1 259 ? -0.484  -5.589  31.094  1.00 17.38 ? 260 PHE A CG  1 
ATOM   2170 C  CD1 . PHE A 1 259 ? 0.506   -4.953  30.376  1.00 15.72 ? 260 PHE A CD1 1 
ATOM   2171 C  CD2 . PHE A 1 259 ? -0.265  -6.902  31.506  1.00 18.75 ? 260 PHE A CD2 1 
ATOM   2172 C  CE1 . PHE A 1 259 ? 1.658   -5.627  30.017  1.00 17.34 ? 260 PHE A CE1 1 
ATOM   2173 C  CE2 . PHE A 1 259 ? 0.908   -7.574  31.169  1.00 20.97 ? 260 PHE A CE2 1 
ATOM   2174 C  CZ  . PHE A 1 259 ? 1.871   -6.923  30.423  1.00 21.38 ? 260 PHE A CZ  1 
ATOM   2175 N  N   . LYS A 1 260 ? -2.292  -5.625  34.418  1.00 30.82 ? 261 LYS A N   1 
ATOM   2176 C  CA  . LYS A 1 260 ? -2.410  -6.838  35.233  1.00 43.02 ? 261 LYS A CA  1 
ATOM   2177 C  C   . LYS A 1 260 ? -2.197  -6.564  36.727  1.00 51.64 ? 261 LYS A C   1 
ATOM   2178 O  O   . LYS A 1 260 ? -1.215  -7.032  37.303  1.00 61.97 ? 261 LYS A O   1 
ATOM   2179 C  CB  . LYS A 1 260 ? -1.652  -8.053  34.682  1.00 39.54 ? 261 LYS A CB  1 
ATOM   2180 C  CG  . LYS A 1 260 ? -2.415  -8.853  33.631  1.00 39.81 ? 261 LYS A CG  1 
ATOM   2181 O  OXT . LYS A 1 260 ? -3.025  -5.892  37.371  1.00 56.47 ? 261 LYS A OXT 1 
HETATM 2182 ZN ZN  . ZN  B 2 .   ? 14.435  0.114   15.307  1.00 7.70  ? 301 ZN  A ZN  1 
HETATM 2183 S  S   . DMS C 3 .   ? 22.419  -9.940  14.949  1.00 23.33 ? 302 DMS A S   1 
HETATM 2184 O  O   . DMS C 3 .   ? 23.190  -11.264 14.704  1.00 29.07 ? 302 DMS A O   1 
HETATM 2185 C  C1  . DMS C 3 .   ? 22.602  -9.678  16.693  1.00 21.94 ? 302 DMS A C1  1 
HETATM 2186 C  C2  . DMS C 3 .   ? 23.583  -8.685  14.482  1.00 26.64 ? 302 DMS A C2  1 
HETATM 2187 C  C1  A EDO D 4 .   ? 13.180  11.133  8.511   0.50 18.73 ? 303 EDO A C1  1 
HETATM 2188 C  C1  B EDO D 4 .   ? 13.205  11.693  8.434   0.50 29.49 ? 303 EDO A C1  1 
HETATM 2189 O  O1  A EDO D 4 .   ? 13.704  9.853   8.807   0.50 20.81 ? 303 EDO A O1  1 
HETATM 2190 O  O1  B EDO D 4 .   ? 14.214  12.421  7.751   0.50 31.35 ? 303 EDO A O1  1 
HETATM 2191 C  C2  A EDO D 4 .   ? 12.214  11.029  7.374   0.50 24.32 ? 303 EDO A C2  1 
HETATM 2192 C  C2  B EDO D 4 .   ? 12.249  11.041  7.497   0.50 34.70 ? 303 EDO A C2  1 
HETATM 2193 O  O2  A EDO D 4 .   ? 11.861  12.291  6.839   0.50 25.94 ? 303 EDO A O2  1 
HETATM 2194 O  O2  B EDO D 4 .   ? 11.704  11.949  6.555   0.50 34.11 ? 303 EDO A O2  1 
HETATM 2195 N  N1  . BCN E 5 .   ? 0.541   -12.661 23.206  1.00 59.66 ? 304 BCN A N1  1 
HETATM 2196 C  C1  . BCN E 5 .   ? -0.764  -11.967 23.173  1.00 57.98 ? 304 BCN A C1  1 
HETATM 2197 C  C2  . BCN E 5 .   ? -1.416  -11.634 24.521  1.00 65.95 ? 304 BCN A C2  1 
HETATM 2198 O  O21 . BCN E 5 .   ? -1.734  -10.448 24.701  1.00 61.08 ? 304 BCN A O21 1 
HETATM 2199 O  O22 . BCN E 5 .   ? -1.593  -12.565 25.343  1.00 68.11 ? 304 BCN A O22 1 
HETATM 2200 C  C3  . BCN E 5 .   ? 0.407   -14.083 22.855  1.00 59.25 ? 304 BCN A C3  1 
HETATM 2201 C  C4  . BCN E 5 .   ? 1.362   -14.536 21.790  1.00 54.27 ? 304 BCN A C4  1 
HETATM 2202 O  O4  . BCN E 5 .   ? 0.687   -14.667 20.554  1.00 53.43 ? 304 BCN A O4  1 
HETATM 2203 C  C5  . BCN E 5 .   ? 1.311   -12.449 24.447  1.00 52.42 ? 304 BCN A C5  1 
HETATM 2204 C  C6  . BCN E 5 .   ? 1.320   -13.688 25.321  1.00 48.46 ? 304 BCN A C6  1 
HETATM 2205 O  O6  . BCN E 5 .   ? 1.807   -13.402 26.617  1.00 45.24 ? 304 BCN A O6  1 
HETATM 2206 F  F13 A V50 F 6 .   ? 14.801  5.481   16.208  0.50 8.25  ? 305 V50 A F13 1 
HETATM 2207 F  F13 B V50 F 6 .   ? 13.985  5.083   15.514  0.50 19.97 ? 305 V50 A F13 1 
HETATM 2208 C  C4  A V50 F 6 .   ? 15.439  4.875   15.211  0.50 8.80  ? 305 V50 A C4  1 
HETATM 2209 C  C4  B V50 F 6 .   ? 15.306  5.132   15.505  0.50 15.49 ? 305 V50 A C4  1 
HETATM 2210 C  C5  A V50 F 6 .   ? 15.800  3.529   15.361  0.50 7.45  ? 305 V50 A C5  1 
HETATM 2211 C  C5  B V50 F 6 .   ? 16.050  4.064   15.986  0.50 13.18 ? 305 V50 A C5  1 
HETATM 2212 S  S7  A V50 F 6 .   ? 15.306  2.639   16.799  0.50 6.69  ? 305 V50 A S7  1 
HETATM 2213 S  S7  B V50 F 6 .   ? 15.338  2.644   16.746  0.50 10.68 ? 305 V50 A S7  1 
HETATM 2214 O  O9  A V50 F 6 .   ? 13.868  2.812   16.838  0.50 6.90  ? 305 V50 A O9  1 
HETATM 2215 O  O9  B V50 F 6 .   ? 13.942  2.850   16.532  0.50 11.13 ? 305 V50 A O9  1 
HETATM 2216 N  N23 A V50 F 6 .   ? 15.531  1.073   16.587  0.50 6.35  ? 305 V50 A N23 1 
HETATM 2217 N  N23 B V50 F 6 .   ? 15.853  1.326   15.938  0.50 9.69  ? 305 V50 A N23 1 
HETATM 2218 O  O8  A V50 F 6 .   ? 16.032  3.155   17.912  0.50 5.92  ? 305 V50 A O8  1 
HETATM 2219 O  O8  B V50 F 6 .   ? 15.870  2.656   18.101  0.50 10.56 ? 305 V50 A O8  1 
HETATM 2220 C  C6  A V50 F 6 .   ? 16.511  2.947   14.278  0.50 8.61  ? 305 V50 A C6  1 
HETATM 2221 C  C6  B V50 F 6 .   ? 17.442  4.222   15.909  0.50 12.94 ? 305 V50 A C6  1 
HETATM 2222 F  F11 A V50 F 6 .   ? 16.868  1.685   14.237  0.50 9.84  ? 305 V50 A F11 1 
HETATM 2223 F  F11 B V50 F 6 .   ? 18.211  3.239   16.389  0.50 13.12 ? 305 V50 A F11 1 
HETATM 2224 C  C1  A V50 F 6 .   ? 16.825  3.661   13.142  0.50 9.87  ? 305 V50 A C1  1 
HETATM 2225 C  C1  B V50 F 6 .   ? 18.103  5.329   15.382  0.50 16.13 ? 305 V50 A C1  1 
HETATM 2226 F  F10 A V50 F 6 .   ? 17.491  3.061   12.151  0.50 11.00 ? 305 V50 A F10 1 
HETATM 2227 F  F10 B V50 F 6 .   ? 19.466  5.345   15.411  0.50 14.31 ? 305 V50 A F10 1 
HETATM 2228 C  C3  A V50 F 6 .   ? 15.816  5.572   14.061  0.50 9.39  ? 305 V50 A C3  1 
HETATM 2229 C  C3  B V50 F 6 .   ? 15.921  6.232   14.939  0.50 17.49 ? 305 V50 A C3  1 
HETATM 2230 F  F12 A V50 F 6 .   ? 15.449  6.835   13.846  0.50 9.15  ? 305 V50 A F12 1 
HETATM 2231 F  F12 B V50 F 6 .   ? 15.079  7.190   14.516  0.50 19.25 ? 305 V50 A F12 1 
HETATM 2232 C  C2  A V50 F 6 .   ? 16.426  4.960   13.020  0.50 9.58  ? 305 V50 A C2  1 
HETATM 2233 C  C2  B V50 F 6 .   ? 17.321  6.373   14.865  0.50 17.12 ? 305 V50 A C2  1 
HETATM 2234 S  S14 A V50 F 6 .   ? 16.819  5.822   11.532  0.50 12.13 ? 305 V50 A S14 1 
HETATM 2235 S  S14 B V50 F 6 .   ? 18.089  7.858   14.236  0.50 22.99 ? 305 V50 A S14 1 
HETATM 2236 C  C15 A V50 F 6 .   ? 17.479  7.365   12.073  0.50 12.37 ? 305 V50 A C15 1 
HETATM 2237 C  C15 B V50 F 6 .   ? 17.953  7.514   12.426  0.00 20.61 ? 305 V50 A C15 1 
HETATM 2238 N  N20 . V50 F 6 .   ? 17.164  8.327   11.230  1.00 12.94 ? 305 V50 A N20 1 
HETATM 2239 C  C19 . V50 F 6 .   ? 17.678  9.542   11.524  1.00 13.48 ? 305 V50 A C19 1 
HETATM 2240 C  C21 . V50 F 6 .   ? 17.330  10.665  10.601  1.00 14.90 ? 305 V50 A C21 1 
HETATM 2241 C  C18 . V50 F 6 .   ? 18.425  9.835   12.613  1.00 15.19 ? 305 V50 A C18 1 
HETATM 2242 C  C17 . V50 F 6 .   ? 18.703  8.760   13.375  1.00 15.23 ? 305 V50 A C17 1 
HETATM 2243 N  N16 . V50 F 6 .   ? 18.267  7.496   13.135  1.00 13.20 ? 305 V50 A N16 1 
HETATM 2244 C  C22 . V50 F 6 .   ? 19.547  8.995   14.591  1.00 15.29 ? 305 V50 A C22 1 
HETATM 2245 F  F13 . V50 G 6 .   ? 33.917  -1.777  13.493  1.00 29.31 ? 306 V50 A F13 1 
HETATM 2246 C  C4  . V50 G 6 .   ? 33.900  -0.901  12.480  1.00 34.25 ? 306 V50 A C4  1 
HETATM 2247 C  C5  . V50 G 6 .   ? 33.073  0.243   12.432  1.00 34.44 ? 306 V50 A C5  1 
HETATM 2248 S  S7  . V50 G 6 .   ? 31.903  0.553   13.725  1.00 30.02 ? 306 V50 A S7  1 
HETATM 2249 O  O9  . V50 G 6 .   ? 31.280  -0.733  13.853  1.00 23.84 ? 306 V50 A O9  1 
HETATM 2250 N  N23 . V50 G 6 .   ? 32.575  0.869   15.228  1.00 27.25 ? 306 V50 A N23 1 
HETATM 2251 O  O8  . V50 G 6 .   ? 31.198  1.832   13.529  1.00 29.78 ? 306 V50 A O8  1 
HETATM 2252 C  C6  . V50 G 6 .   ? 33.169  1.091   11.312  1.00 41.48 ? 306 V50 A C6  1 
HETATM 2253 F  F11 . V50 G 6 .   ? 32.424  2.208   11.178  1.00 47.92 ? 306 V50 A F11 1 
HETATM 2254 C  C1  . V50 G 6 .   ? 34.064  0.808   10.287  1.00 44.31 ? 306 V50 A C1  1 
HETATM 2255 F  F10 . V50 G 6 .   ? 34.099  1.658   9.253   1.00 48.84 ? 306 V50 A F10 1 
HETATM 2256 C  C3  . V50 G 6 .   ? 34.802  -1.165  11.445  1.00 38.56 ? 306 V50 A C3  1 
HETATM 2257 F  F12 . V50 G 6 .   ? 35.547  -2.280  11.552  1.00 35.32 ? 306 V50 A F12 1 
HETATM 2258 C  C2  . V50 G 6 .   ? 34.893  -0.314  10.332  1.00 42.72 ? 306 V50 A C2  1 
HETATM 2259 S  S14 . V50 G 6 .   ? 36.033  -0.610  8.997   1.00 48.92 ? 306 V50 A S14 1 
HETATM 2260 C  C15 . V50 G 6 .   ? 35.097  -1.614  7.835   1.00 68.13 ? 306 V50 A C15 1 
HETATM 2261 N  N20 . V50 G 6 .   ? 34.591  -2.791  8.245   1.00 69.33 ? 306 V50 A N20 1 
HETATM 2262 C  C19 . V50 G 6 .   ? 33.896  -3.493  7.307   1.00 78.42 ? 306 V50 A C19 1 
HETATM 2263 C  C21 . V50 G 6 .   ? 33.313  -4.809  7.735   1.00 70.72 ? 306 V50 A C21 1 
HETATM 2264 C  C18 . V50 G 6 .   ? 33.670  -3.115  6.003   1.00 87.09 ? 306 V50 A C18 1 
HETATM 2265 C  C17 . V50 G 6 .   ? 34.234  -1.901  5.699   1.00 85.43 ? 306 V50 A C17 1 
HETATM 2266 N  N16 . V50 G 6 .   ? 34.943  -1.141  6.577   1.00 82.90 ? 306 V50 A N16 1 
HETATM 2267 C  C22 . V50 G 6 .   ? 34.055  -1.394  4.297   1.00 78.38 ? 306 V50 A C22 1 
HETATM 2268 NA NA  . NA  H 7 .   ? 12.666  17.130  10.058  1.00 25.18 ? 307 NA  A NA  1 
HETATM 2269 O  O   . HOH I 8 .   ? 18.837  10.264  29.221  1.00 22.85 ? 401 HOH A O   1 
HETATM 2270 O  O   . HOH I 8 .   ? 3.384   21.140  6.058   1.00 28.29 ? 402 HOH A O   1 
HETATM 2271 O  O   . HOH I 8 .   ? 8.377   20.439  28.889  1.00 35.79 ? 403 HOH A O   1 
HETATM 2272 O  O   . HOH I 8 .   ? 27.985  2.141   31.955  1.00 41.04 ? 404 HOH A O   1 
HETATM 2273 O  O   . HOH I 8 .   ? 2.017   19.490  18.817  1.00 38.05 ? 405 HOH A O   1 
HETATM 2274 O  O   . HOH I 8 .   ? 27.159  -3.791  3.549   1.00 45.02 ? 406 HOH A O   1 
HETATM 2275 O  O   . HOH I 8 .   ? 5.761   -8.622  37.337  1.00 23.67 ? 407 HOH A O   1 
HETATM 2276 O  O   . HOH I 8 .   ? 7.356   -3.354  -6.505  1.00 37.51 ? 408 HOH A O   1 
HETATM 2277 O  O   . HOH I 8 .   ? 23.032  2.841   36.053  1.00 40.09 ? 409 HOH A O   1 
HETATM 2278 O  O   . HOH I 8 .   ? 4.132   11.583  32.830  1.00 37.30 ? 410 HOH A O   1 
HETATM 2279 O  O   . HOH I 8 .   ? 1.619   14.099  31.437  1.00 38.06 ? 411 HOH A O   1 
HETATM 2280 O  O   . HOH I 8 .   ? -1.935  2.212   34.518  1.00 36.63 ? 412 HOH A O   1 
HETATM 2281 O  O   . HOH I 8 .   ? -5.747  -11.220 19.752  1.00 36.93 ? 413 HOH A O   1 
HETATM 2282 O  O   . HOH I 8 .   ? 7.964   -20.194 8.467   1.00 30.66 ? 414 HOH A O   1 
HETATM 2283 O  O   . HOH I 8 .   ? 17.709  24.134  22.100  1.00 36.29 ? 415 HOH A O   1 
HETATM 2284 O  O   . HOH I 8 .   ? 6.992   -6.982  -5.378  1.00 34.33 ? 416 HOH A O   1 
HETATM 2285 O  O   . HOH I 8 .   ? 5.727   2.463   -4.511  1.00 34.46 ? 417 HOH A O   1 
HETATM 2286 O  O   . HOH I 8 .   ? -4.705  8.049   26.718  1.00 31.05 ? 418 HOH A O   1 
HETATM 2287 O  O   . HOH I 8 .   ? 22.258  -6.427  -5.181  1.00 29.10 ? 419 HOH A O   1 
HETATM 2288 O  O   . HOH I 8 .   ? 20.137  -3.413  -10.632 1.00 39.94 ? 420 HOH A O   1 
HETATM 2289 O  O   . HOH I 8 .   ? 0.787   10.463  30.115  1.00 30.05 ? 421 HOH A O   1 
HETATM 2290 O  O   . HOH I 8 .   ? 27.166  1.676   -1.223  1.00 39.89 ? 422 HOH A O   1 
HETATM 2291 O  O   . HOH I 8 .   ? 14.925  -2.582  -6.343  1.00 21.86 ? 423 HOH A O   1 
HETATM 2292 O  O   . HOH I 8 .   ? 14.480  8.381   10.785  1.00 16.75 ? 424 HOH A O   1 
HETATM 2293 O  O   . HOH I 8 .   ? 6.754   -14.721 28.869  1.00 28.57 ? 425 HOH A O   1 
HETATM 2294 O  O   . HOH I 8 .   ? -2.965  -1.554  29.447  1.00 27.19 ? 426 HOH A O   1 
HETATM 2295 O  O   . HOH I 8 .   ? 25.424  -1.770  26.504  1.00 21.07 ? 427 HOH A O   1 
HETATM 2296 O  O   . HOH I 8 .   ? 14.360  -18.497 19.351  1.00 17.70 ? 428 HOH A O   1 
HETATM 2297 O  O   . HOH I 8 .   ? 19.794  25.521  17.950  1.00 34.14 ? 429 HOH A O   1 
HETATM 2298 O  O   . HOH I 8 .   ? 30.621  3.923   12.073  1.00 29.63 ? 430 HOH A O   1 
HETATM 2299 O  O   . HOH I 8 .   ? 25.757  -0.916  28.987  1.00 24.97 ? 431 HOH A O   1 
HETATM 2300 O  O   . HOH I 8 .   ? 12.213  7.761   28.862  1.00 22.06 ? 432 HOH A O   1 
HETATM 2301 O  O   . HOH I 8 .   ? 19.907  -2.334  15.909  1.00 9.42  ? 433 HOH A O   1 
HETATM 2302 O  O   . HOH I 8 .   ? 23.533  -11.436 5.297   1.00 23.18 ? 434 HOH A O   1 
HETATM 2303 O  O   . HOH I 8 .   ? 10.333  2.869   33.964  1.00 31.43 ? 435 HOH A O   1 
HETATM 2304 O  O   . HOH I 8 .   ? 4.464   -12.888 33.048  1.00 37.53 ? 436 HOH A O   1 
HETATM 2305 O  O   . HOH I 8 .   ? 22.622  4.902   4.958   1.00 35.21 ? 437 HOH A O   1 
HETATM 2306 O  O   . HOH I 8 .   ? 9.103   14.199  29.108  1.00 18.46 ? 438 HOH A O   1 
HETATM 2307 O  O   . HOH I 8 .   ? 24.526  6.592   30.196  1.00 18.98 ? 439 HOH A O   1 
HETATM 2308 O  O   . HOH I 8 .   ? 21.136  0.966   -4.562  1.00 16.88 ? 440 HOH A O   1 
HETATM 2309 O  O   . HOH I 8 .   ? -2.739  -12.444 19.744  1.00 37.52 ? 441 HOH A O   1 
HETATM 2310 O  O   . HOH I 8 .   ? 4.088   -21.210 4.062   1.00 34.71 ? 442 HOH A O   1 
HETATM 2311 O  O   . HOH I 8 .   ? -2.934  10.595  20.295  1.00 21.63 ? 443 HOH A O   1 
HETATM 2312 O  O   . HOH I 8 .   ? 1.319   -15.029 2.995   1.00 23.23 ? 444 HOH A O   1 
HETATM 2313 O  O   . HOH I 8 .   ? 8.920   11.189  -5.875  1.00 37.08 ? 445 HOH A O   1 
HETATM 2314 O  O   . HOH I 8 .   ? 1.804   -18.840 5.222   1.00 25.39 ? 446 HOH A O   1 
HETATM 2315 O  O   . HOH I 8 .   ? 20.821  11.177  18.284  1.00 22.17 ? 447 HOH A O   1 
HETATM 2316 O  O   . HOH I 8 .   ? 20.502  -18.864 14.848  1.00 34.34 ? 448 HOH A O   1 
HETATM 2317 O  O   . HOH I 8 .   ? 0.990   12.621  26.720  1.00 17.55 ? 449 HOH A O   1 
HETATM 2318 O  O   . HOH I 8 .   ? 11.584  17.638  29.317  1.00 22.83 ? 450 HOH A O   1 
HETATM 2319 O  O   . HOH I 8 .   ? 5.572   -19.949 13.181  1.00 21.02 ? 451 HOH A O   1 
HETATM 2320 O  O   . HOH I 8 .   ? -2.037  -9.610  16.944  1.00 25.84 ? 452 HOH A O   1 
HETATM 2321 O  O   . HOH I 8 .   ? 20.815  11.831  15.829  1.00 31.14 ? 453 HOH A O   1 
HETATM 2322 O  O   . HOH I 8 .   ? 36.366  2.048   15.112  1.00 31.51 ? 454 HOH A O   1 
HETATM 2323 O  O   . HOH I 8 .   ? 20.671  2.645   34.453  1.00 28.14 ? 455 HOH A O   1 
HETATM 2324 O  O   . HOH I 8 .   ? 2.415   -19.190 14.818  1.00 26.01 ? 456 HOH A O   1 
HETATM 2325 O  O   . HOH I 8 .   ? -6.157  -3.472  27.549  1.00 39.93 ? 457 HOH A O   1 
HETATM 2326 O  O   . HOH I 8 .   ? -6.751  8.065   21.730  1.00 30.15 ? 458 HOH A O   1 
HETATM 2327 O  O   . HOH I 8 .   ? 14.166  -13.099 31.517  1.00 20.83 ? 459 HOH A O   1 
HETATM 2328 O  O   . HOH I 8 .   ? 36.417  -5.229  12.342  1.00 36.81 ? 460 HOH A O   1 
HETATM 2329 O  O   . HOH I 8 .   ? 4.142   -12.168 26.157  1.00 26.81 ? 461 HOH A O   1 
HETATM 2330 O  O   . HOH I 8 .   ? 22.997  -13.768 9.339   1.00 23.18 ? 462 HOH A O   1 
HETATM 2331 O  O   . HOH I 8 .   ? 10.667  -16.463 16.931  1.00 19.85 ? 463 HOH A O   1 
HETATM 2332 O  O   . HOH I 8 .   ? 25.656  1.333   -5.272  1.00 39.04 ? 464 HOH A O   1 
HETATM 2333 O  O   . HOH I 8 .   ? 32.837  -5.237  22.400  1.00 32.00 ? 465 HOH A O   1 
HETATM 2334 O  O   . HOH I 8 .   ? 3.079   12.541  11.349  1.00 23.12 ? 466 HOH A O   1 
HETATM 2335 O  O   . HOH I 8 .   ? 23.233  9.611   27.761  1.00 17.32 ? 467 HOH A O   1 
HETATM 2336 O  O   . HOH I 8 .   ? 16.302  -10.137 32.044  1.00 20.54 ? 468 HOH A O   1 
HETATM 2337 O  O   . HOH I 8 .   ? 26.679  8.718   20.396  1.00 20.68 ? 469 HOH A O   1 
HETATM 2338 O  O   . HOH I 8 .   ? 34.698  1.873   24.434  1.00 23.29 ? 470 HOH A O   1 
HETATM 2339 O  O   . HOH I 8 .   ? 2.686   -2.137  -2.655  1.00 28.06 ? 471 HOH A O   1 
HETATM 2340 O  O   . HOH I 8 .   ? 9.064   12.620  5.810   1.00 21.29 ? 472 HOH A O   1 
HETATM 2341 O  O   . HOH I 8 .   ? 24.522  10.522  20.875  1.00 23.45 ? 473 HOH A O   1 
HETATM 2342 O  O   . HOH I 8 .   ? 14.040  -14.766 1.690   1.00 21.27 ? 474 HOH A O   1 
HETATM 2343 O  O   . HOH I 8 .   ? 13.114  -13.613 11.227  1.00 10.11 ? 475 HOH A O   1 
HETATM 2344 O  O   . HOH I 8 .   ? 3.864   -14.531 21.953  1.00 26.07 ? 476 HOH A O   1 
HETATM 2345 O  O   . HOH I 8 .   ? 16.812  22.489  15.492  1.00 28.29 ? 477 HOH A O   1 
HETATM 2346 O  O   . HOH I 8 .   ? 7.573   12.232  27.833  1.00 15.19 ? 478 HOH A O   1 
HETATM 2347 O  O   . HOH I 8 .   ? 7.051   11.375  31.278  1.00 32.34 ? 479 HOH A O   1 
HETATM 2348 O  O   . HOH I 8 .   ? 2.522   -10.524 -3.469  1.00 24.18 ? 480 HOH A O   1 
HETATM 2349 O  O   . HOH I 8 .   ? 17.523  -9.356  20.819  1.00 10.13 ? 481 HOH A O   1 
HETATM 2350 O  O   . HOH I 8 .   ? 17.293  -10.906 -2.903  1.00 27.29 ? 482 HOH A O   1 
HETATM 2351 O  O   . HOH I 8 .   ? 18.560  -1.697  11.596  1.00 20.91 ? 483 HOH A O   1 
HETATM 2352 O  O   . HOH I 8 .   ? 15.030  3.435   10.197  1.00 19.42 ? 484 HOH A O   1 
HETATM 2353 O  O   . HOH I 8 .   ? 17.225  -14.100 24.326  1.00 15.52 ? 485 HOH A O   1 
HETATM 2354 O  O   . HOH I 8 .   ? 6.449   -16.966 18.565  1.00 21.39 ? 486 HOH A O   1 
HETATM 2355 O  O   . HOH I 8 .   ? 22.149  -10.056 25.109  1.00 21.83 ? 487 HOH A O   1 
HETATM 2356 O  O   . HOH I 8 .   ? 2.004   3.711   40.665  1.00 40.68 ? 488 HOH A O   1 
HETATM 2357 O  O   . HOH I 8 .   ? 12.332  2.623   -6.406  1.00 23.47 ? 489 HOH A O   1 
HETATM 2358 O  O   . HOH I 8 .   ? 7.317   22.023  15.065  1.00 19.99 ? 490 HOH A O   1 
HETATM 2359 O  O   . HOH I 8 .   ? 24.528  -7.226  26.119  1.00 32.91 ? 491 HOH A O   1 
HETATM 2360 O  O   . HOH I 8 .   ? 19.195  -2.477  -7.007  1.00 26.01 ? 492 HOH A O   1 
HETATM 2361 O  O   . HOH I 8 .   ? 8.821   14.711  31.681  1.00 21.30 ? 493 HOH A O   1 
HETATM 2362 O  O   . HOH I 8 .   ? 21.482  -17.620 10.738  1.00 26.49 ? 494 HOH A O   1 
HETATM 2363 O  O   . HOH I 8 .   ? 15.138  9.794   5.314   1.00 20.35 ? 495 HOH A O   1 
HETATM 2364 O  O   . HOH I 8 .   ? 16.519  -11.711 17.964  1.00 9.01  ? 496 HOH A O   1 
HETATM 2365 O  O   . HOH I 8 .   ? -0.498  -5.339  23.520  1.00 14.34 ? 497 HOH A O   1 
HETATM 2366 O  O   . HOH I 8 .   ? -1.718  -4.088  2.725   1.00 21.22 ? 498 HOH A O   1 
HETATM 2367 O  O   . HOH I 8 .   ? 23.764  -2.406  7.801   1.00 22.10 ? 499 HOH A O   1 
HETATM 2368 O  O   . HOH I 8 .   ? -0.169  9.735   1.905   1.00 16.70 ? 500 HOH A O   1 
HETATM 2369 O  O   . HOH I 8 .   ? 15.479  18.704  27.313  1.00 44.13 ? 501 HOH A O   1 
HETATM 2370 O  O   . HOH I 8 .   ? 17.340  6.489   7.995   1.00 30.42 ? 502 HOH A O   1 
HETATM 2371 O  O   . HOH I 8 .   ? -3.678  -18.694 8.835   1.00 36.21 ? 503 HOH A O   1 
HETATM 2372 O  O   . HOH I 8 .   ? 10.777  10.489  25.390  1.00 11.09 ? 504 HOH A O   1 
HETATM 2373 O  O   . HOH I 8 .   ? 10.608  -17.651 20.016  1.00 18.99 ? 505 HOH A O   1 
HETATM 2374 O  O   . HOH I 8 .   ? 14.000  -6.468  -6.992  1.00 33.92 ? 506 HOH A O   1 
HETATM 2375 O  O   . HOH I 8 .   ? 18.531  -6.976  29.108  1.00 12.57 ? 507 HOH A O   1 
HETATM 2376 O  O   . HOH I 8 .   ? -4.635  -3.337  13.306  1.00 29.44 ? 508 HOH A O   1 
HETATM 2377 O  O   . HOH I 8 .   ? -4.757  9.938   6.239   1.00 31.21 ? 509 HOH A O   1 
HETATM 2378 O  O   . HOH I 8 .   ? -3.686  -5.839  9.128   1.00 18.90 ? 510 HOH A O   1 
HETATM 2379 O  O   . HOH I 8 .   ? 18.225  7.978   -1.681  1.00 25.27 ? 511 HOH A O   1 
HETATM 2380 O  O   . HOH I 8 .   ? 17.633  -11.483 25.105  1.00 12.68 ? 512 HOH A O   1 
HETATM 2381 O  O   . HOH I 8 .   ? 4.036   -6.536  20.319  1.00 9.50  ? 513 HOH A O   1 
HETATM 2382 O  O   . HOH I 8 .   ? -4.615  -13.357 7.833   1.00 25.39 ? 514 HOH A O   1 
HETATM 2383 O  O   . HOH I 8 .   ? 16.817  -6.842  31.161  1.00 21.36 ? 515 HOH A O   1 
HETATM 2384 O  O   . HOH I 8 .   ? 3.137   -18.588 8.010   1.00 16.91 ? 516 HOH A O   1 
HETATM 2385 O  O   . HOH I 8 .   ? 6.246   22.004  17.690  1.00 22.50 ? 517 HOH A O   1 
HETATM 2386 O  O   . HOH I 8 .   ? 4.998   -10.499 24.299  1.00 17.54 ? 518 HOH A O   1 
HETATM 2387 O  O   . HOH I 8 .   ? 36.633  -0.534  14.409  1.00 20.35 ? 519 HOH A O   1 
HETATM 2388 O  O   . HOH I 8 .   ? -2.281  -11.337 11.198  1.00 23.59 ? 520 HOH A O   1 
HETATM 2389 O  O   . HOH I 8 .   ? 26.262  -1.519  2.765   1.00 38.06 ? 521 HOH A O   1 
HETATM 2390 O  O   . HOH I 8 .   ? 12.322  -13.653 32.912  1.00 28.51 ? 522 HOH A O   1 
HETATM 2391 O  O   . HOH I 8 .   ? 28.036  -1.875  30.028  1.00 34.41 ? 523 HOH A O   1 
HETATM 2392 O  O   . HOH I 8 .   ? -5.121  4.654   20.884  1.00 22.04 ? 524 HOH A O   1 
HETATM 2393 O  O   . HOH I 8 .   ? 37.113  5.357   15.466  1.00 24.60 ? 525 HOH A O   1 
HETATM 2394 O  O   . HOH I 8 .   ? 1.234   -2.245  41.222  1.00 27.02 ? 526 HOH A O   1 
HETATM 2395 O  O   . HOH I 8 .   ? 29.777  -2.056  21.114  1.00 14.29 ? 527 HOH A O   1 
HETATM 2396 O  O   . HOH I 8 .   ? -0.927  7.642   4.807   1.00 17.41 ? 528 HOH A O   1 
HETATM 2397 O  O   . HOH I 8 .   ? 12.895  -13.827 36.132  1.00 28.59 ? 529 HOH A O   1 
HETATM 2398 O  O   . HOH I 8 .   ? 0.961   15.607  28.841  1.00 29.86 ? 530 HOH A O   1 
HETATM 2399 O  O   . HOH I 8 .   ? 8.017   -15.026 26.591  1.00 18.55 ? 531 HOH A O   1 
HETATM 2400 O  O   . HOH I 8 .   ? 7.399   -20.375 11.535  1.00 35.54 ? 532 HOH A O   1 
HETATM 2401 O  O   . HOH I 8 .   ? 9.181   11.208  3.288   1.00 21.88 ? 533 HOH A O   1 
HETATM 2402 O  O   . HOH I 8 .   ? -5.229  -5.689  30.362  1.00 31.24 ? 534 HOH A O   1 
HETATM 2403 O  O   . HOH I 8 .   ? -4.755  -7.057  11.293  1.00 25.83 ? 535 HOH A O   1 
HETATM 2404 O  O   . HOH I 8 .   ? -0.569  -12.458 18.589  1.00 34.03 ? 536 HOH A O   1 
HETATM 2405 O  O   . HOH I 8 .   ? 28.708  -5.856  -0.287  1.00 23.21 ? 537 HOH A O   1 
HETATM 2406 O  O   . HOH I 8 .   ? 23.696  -9.513  9.553   1.00 18.93 ? 538 HOH A O   1 
HETATM 2407 O  O   . HOH I 8 .   ? 5.440   10.934  -2.014  1.00 22.40 ? 539 HOH A O   1 
HETATM 2408 O  O   . HOH I 8 .   ? -2.038  -1.201  6.834   1.00 26.25 ? 540 HOH A O   1 
HETATM 2409 O  O   . HOH I 8 .   ? 9.164   4.591   30.604  1.00 20.52 ? 541 HOH A O   1 
HETATM 2410 O  O   . HOH I 8 .   ? -10.834 -8.979  16.131  1.00 24.42 ? 542 HOH A O   1 
HETATM 2411 O  O   . HOH I 8 .   ? -6.566  6.280   24.252  1.00 25.53 ? 543 HOH A O   1 
HETATM 2412 O  O   . HOH I 8 .   ? 1.724   11.947  8.928   1.00 15.84 ? 544 HOH A O   1 
HETATM 2413 O  O   . HOH I 8 .   ? 7.081   -19.342 3.423   1.00 46.41 ? 545 HOH A O   1 
HETATM 2414 O  O   . HOH I 8 .   ? 9.540   19.940  12.372  1.00 20.83 ? 546 HOH A O   1 
HETATM 2415 O  O   . HOH I 8 .   ? 5.097   17.791  23.555  1.00 20.23 ? 547 HOH A O   1 
HETATM 2416 O  O   . HOH I 8 .   ? 26.216  -5.567  22.329  1.00 26.64 ? 548 HOH A O   1 
HETATM 2417 O  O   . HOH I 8 .   ? 0.017   -17.767 6.752   1.00 32.54 ? 549 HOH A O   1 
HETATM 2418 O  O   . HOH I 8 .   ? 14.236  -3.646  37.263  1.00 17.20 ? 550 HOH A O   1 
HETATM 2419 O  O   . HOH I 8 .   ? 19.552  6.387   -4.899  1.00 29.02 ? 551 HOH A O   1 
HETATM 2420 O  O   . HOH I 8 .   ? 26.032  -3.139  21.069  1.00 13.30 ? 552 HOH A O   1 
HETATM 2421 O  O   . HOH I 8 .   ? 29.222  -7.600  16.554  1.00 24.22 ? 553 HOH A O   1 
HETATM 2422 O  O   . HOH I 8 .   ? 24.579  -11.829 12.287  1.00 33.93 ? 554 HOH A O   1 
HETATM 2423 O  O   . HOH I 8 .   ? -2.955  1.148   26.373  1.00 26.38 ? 555 HOH A O   1 
HETATM 2424 O  O   . HOH I 8 .   ? -4.414  -7.819  14.902  1.00 30.27 ? 556 HOH A O   1 
HETATM 2425 O  O   . HOH I 8 .   ? 7.641   15.948  27.298  1.00 20.64 ? 557 HOH A O   1 
HETATM 2426 O  O   . HOH I 8 .   ? 35.090  3.872   22.836  1.00 22.81 ? 558 HOH A O   1 
HETATM 2427 O  O   . HOH I 8 .   ? 32.431  3.033   26.002  1.00 24.86 ? 559 HOH A O   1 
HETATM 2428 O  O   . HOH I 8 .   ? 16.458  -14.115 1.101   1.00 28.55 ? 560 HOH A O   1 
HETATM 2429 O  O   . HOH I 8 .   ? 13.707  -6.879  32.594  1.00 17.90 ? 561 HOH A O   1 
HETATM 2430 O  O   . HOH I 8 .   ? 2.286   5.404   -3.385  1.00 29.24 ? 562 HOH A O   1 
HETATM 2431 O  O   . HOH I 8 .   ? 9.631   9.976   -3.062  1.00 38.81 ? 563 HOH A O   1 
HETATM 2432 O  O   . HOH I 8 .   ? 22.890  -13.662 -4.569  1.00 29.00 ? 564 HOH A O   1 
HETATM 2433 O  O   . HOH I 8 .   ? 7.638   -16.660 14.676  1.00 20.46 ? 565 HOH A O   1 
HETATM 2434 O  O   . HOH I 8 .   ? 9.944   -17.402 6.855   1.00 22.22 ? 566 HOH A O   1 
HETATM 2435 O  O   . HOH I 8 .   ? 6.298   13.140  34.586  1.00 27.45 ? 567 HOH A O   1 
HETATM 2436 O  O   . HOH I 8 .   ? 8.545   9.706   28.797  1.00 23.70 ? 568 HOH A O   1 
HETATM 2437 O  O   . HOH I 8 .   ? 22.897  9.921   24.960  1.00 16.05 ? 569 HOH A O   1 
HETATM 2438 O  O   . HOH I 8 .   ? -0.956  21.423  17.218  1.00 33.01 ? 570 HOH A O   1 
HETATM 2439 O  O   . HOH I 8 .   ? 8.452   -7.109  -3.116  1.00 24.30 ? 571 HOH A O   1 
HETATM 2440 O  O   . HOH I 8 .   ? 25.387  -4.700  7.907   1.00 21.54 ? 572 HOH A O   1 
HETATM 2441 O  O   . HOH I 8 .   ? -2.794  -15.969 6.308   1.00 29.05 ? 573 HOH A O   1 
HETATM 2442 O  O   . HOH I 8 .   ? -4.427  11.463  13.364  1.00 30.32 ? 574 HOH A O   1 
HETATM 2443 O  O   . HOH I 8 .   ? 7.603   1.111   -6.018  1.00 24.98 ? 575 HOH A O   1 
HETATM 2444 O  O   . HOH I 8 .   ? 34.187  -4.181  24.372  1.00 25.80 ? 576 HOH A O   1 
HETATM 2445 O  O   . HOH I 8 .   ? 17.344  -2.889  37.574  1.00 39.34 ? 577 HOH A O   1 
HETATM 2446 O  O   . HOH I 8 .   ? 11.927  -8.051  -1.156  1.00 22.20 ? 578 HOH A O   1 
HETATM 2447 O  O   . HOH I 8 .   ? 25.280  4.501   8.369   1.00 39.50 ? 579 HOH A O   1 
HETATM 2448 O  O   . HOH I 8 .   ? -5.856  -2.172  25.033  1.00 22.41 ? 580 HOH A O   1 
HETATM 2449 O  O   . HOH I 8 .   ? 10.995  17.312  11.977  1.00 19.34 ? 581 HOH A O   1 
HETATM 2450 O  O   . HOH I 8 .   ? 22.418  0.095   29.497  1.00 13.25 ? 582 HOH A O   1 
HETATM 2451 O  O   . HOH I 8 .   ? 10.332  17.646  8.575   1.00 31.64 ? 583 HOH A O   1 
HETATM 2452 O  O   . HOH I 8 .   ? -3.031  1.702   1.184   1.00 30.55 ? 584 HOH A O   1 
HETATM 2453 O  O   . HOH I 8 .   ? 11.855  -4.064  35.826  1.00 16.95 ? 585 HOH A O   1 
HETATM 2454 O  O   . HOH I 8 .   ? 20.487  -6.819  32.584  1.00 23.56 ? 586 HOH A O   1 
HETATM 2455 O  O   . HOH I 8 .   ? 23.481  -12.605 -0.872  1.00 29.32 ? 587 HOH A O   1 
HETATM 2456 O  O   . HOH I 8 .   ? -1.933  -9.711  14.073  1.00 18.76 ? 588 HOH A O   1 
HETATM 2457 O  O   . HOH I 8 .   ? 24.962  6.263   10.445  1.00 30.97 ? 589 HOH A O   1 
HETATM 2458 O  O   . HOH I 8 .   ? 22.702  -4.673  34.228  1.00 23.50 ? 590 HOH A O   1 
HETATM 2459 O  O   . HOH I 8 .   ? -1.189  -16.493 13.617  1.00 25.41 ? 591 HOH A O   1 
HETATM 2460 O  O   . HOH I 8 .   ? -2.909  1.134   3.917   1.00 24.18 ? 592 HOH A O   1 
HETATM 2461 O  O   . HOH I 8 .   ? 5.859   -18.531 22.426  1.00 35.07 ? 593 HOH A O   1 
HETATM 2462 O  O   . HOH I 8 .   ? 8.343   5.513   -6.855  1.00 24.83 ? 594 HOH A O   1 
HETATM 2463 O  O   . HOH I 8 .   ? 11.510  -6.139  33.959  1.00 18.49 ? 595 HOH A O   1 
HETATM 2464 O  O   . HOH I 8 .   ? 11.695  15.050  9.970   1.00 24.24 ? 596 HOH A O   1 
HETATM 2465 O  O   . HOH I 8 .   ? -10.548 7.025   12.675  1.00 32.50 ? 597 HOH A O   1 
HETATM 2466 O  O   . HOH I 8 .   ? 18.970  -10.540 22.797  1.00 11.13 ? 598 HOH A O   1 
HETATM 2467 O  O   . HOH I 8 .   ? 13.139  -17.527 21.647  1.00 15.28 ? 599 HOH A O   1 
HETATM 2468 O  O   . HOH I 8 .   ? 21.471  -0.386  39.324  1.00 35.73 ? 600 HOH A O   1 
HETATM 2469 O  O   . HOH I 8 .   ? 4.759   -8.134  32.869  1.00 18.02 ? 601 HOH A O   1 
HETATM 2470 O  O   . HOH I 8 .   ? 29.561  5.036   27.957  1.00 39.63 ? 602 HOH A O   1 
HETATM 2471 O  O   . HOH I 8 .   ? 16.671  14.176  11.294  1.00 35.45 ? 603 HOH A O   1 
HETATM 2472 O  O   . HOH I 8 .   ? -4.840  -4.387  33.457  1.00 46.67 ? 604 HOH A O   1 
HETATM 2473 O  O   . HOH I 8 .   ? 10.638  22.767  24.900  1.00 24.78 ? 605 HOH A O   1 
HETATM 2474 O  O   . HOH I 8 .   ? 3.153   -5.922  39.252  1.00 33.48 ? 606 HOH A O   1 
HETATM 2475 O  O   . HOH I 8 .   ? 13.987  3.294   35.236  1.00 28.24 ? 607 HOH A O   1 
HETATM 2476 O  O   . HOH I 8 .   ? 12.683  -18.071 26.518  1.00 25.17 ? 608 HOH A O   1 
HETATM 2477 O  O   . HOH I 8 .   ? 24.118  3.078   -1.805  1.00 29.11 ? 609 HOH A O   1 
HETATM 2478 O  O   . HOH I 8 .   ? -3.452  -7.696  2.001   1.00 21.84 ? 610 HOH A O   1 
HETATM 2479 O  O   . HOH I 8 .   ? 28.777  7.983   22.045  1.00 18.20 ? 611 HOH A O   1 
HETATM 2480 O  O   . HOH I 8 .   ? 4.302   -14.157 -4.245  1.00 35.71 ? 612 HOH A O   1 
HETATM 2481 O  O   . HOH I 8 .   ? -3.628  6.845   8.101   1.00 43.16 ? 613 HOH A O   1 
HETATM 2482 O  O   . HOH I 8 .   ? 13.630  19.110  10.344  1.00 28.24 ? 614 HOH A O   1 
HETATM 2483 O  O   . HOH I 8 .   ? 14.746  -18.047 23.924  1.00 26.07 ? 615 HOH A O   1 
HETATM 2484 O  O   . HOH I 8 .   ? 8.344   -16.755 31.765  1.00 28.89 ? 616 HOH A O   1 
HETATM 2485 O  O   . HOH I 8 .   ? -2.530  1.674   31.965  1.00 25.92 ? 617 HOH A O   1 
HETATM 2486 O  O   . HOH I 8 .   ? 15.666  5.321   -5.776  1.00 32.42 ? 618 HOH A O   1 
HETATM 2487 O  O   . HOH I 8 .   ? 4.291   21.292  21.689  1.00 35.20 ? 619 HOH A O   1 
HETATM 2488 O  O   . HOH I 8 .   ? 31.290  -7.060  8.511   1.00 31.21 ? 620 HOH A O   1 
HETATM 2489 O  O   . HOH I 8 .   ? 6.123   -17.247 32.812  1.00 36.37 ? 621 HOH A O   1 
HETATM 2490 O  O   . HOH I 8 .   ? 14.616  16.626  11.291  1.00 28.09 ? 622 HOH A O   1 
HETATM 2491 O  O   . HOH I 8 .   ? 10.733  7.908   -3.754  1.00 40.66 ? 623 HOH A O   1 
HETATM 2492 O  O   . HOH I 8 .   ? -7.058  7.523   19.299  1.00 36.47 ? 624 HOH A O   1 
HETATM 2493 O  O   . HOH I 8 .   ? 13.709  -6.832  -2.321  1.00 31.03 ? 625 HOH A O   1 
HETATM 2494 O  O   . HOH I 8 .   ? 6.936   8.057   32.820  1.00 34.98 ? 626 HOH A O   1 
HETATM 2495 O  O   . HOH I 8 .   ? 20.910  -12.476 22.170  1.00 22.82 ? 627 HOH A O   1 
HETATM 2496 O  O   . HOH I 8 .   ? 7.348   17.999  28.924  1.00 28.66 ? 628 HOH A O   1 
HETATM 2497 O  O   . HOH I 8 .   ? 20.261  4.701   10.923  1.00 27.61 ? 629 HOH A O   1 
HETATM 2498 O  O   . HOH I 8 .   ? 27.418  -4.046  6.559   1.00 30.00 ? 630 HOH A O   1 
HETATM 2499 O  O   . HOH I 8 .   ? 25.779  -7.932  7.818   1.00 36.67 ? 631 HOH A O   1 
HETATM 2500 O  O   . HOH I 8 .   ? 20.866  13.734  25.477  1.00 35.21 ? 632 HOH A O   1 
HETATM 2501 O  O   . HOH I 8 .   ? 8.220   -15.419 16.824  1.00 17.10 ? 633 HOH A O   1 
HETATM 2502 O  O   . HOH I 8 .   ? 3.333   21.676  17.485  1.00 29.32 ? 634 HOH A O   1 
HETATM 2503 O  O   . HOH I 8 .   ? 31.455  8.413   15.198  1.00 32.75 ? 635 HOH A O   1 
HETATM 2504 O  O   . HOH I 8 .   ? 29.799  -2.968  23.772  1.00 27.57 ? 636 HOH A O   1 
HETATM 2505 O  O   . HOH I 8 .   ? 22.751  -7.901  28.607  1.00 40.74 ? 637 HOH A O   1 
HETATM 2506 O  O   . HOH I 8 .   ? -4.160  13.191  19.697  1.00 38.32 ? 638 HOH A O   1 
HETATM 2507 O  O   . HOH I 8 .   ? 2.172   16.455  30.797  1.00 36.23 ? 639 HOH A O   1 
HETATM 2508 O  O   . HOH I 8 .   ? 15.395  -10.526 -5.191  1.00 36.31 ? 640 HOH A O   1 
HETATM 2509 O  O   . HOH I 8 .   ? 20.832  -16.375 23.770  1.00 40.77 ? 641 HOH A O   1 
HETATM 2510 O  O   . HOH I 8 .   ? 25.513  -9.887  23.244  1.00 33.58 ? 642 HOH A O   1 
HETATM 2511 O  O   . HOH I 8 .   ? 31.553  -3.341  -5.983  1.00 42.15 ? 643 HOH A O   1 
HETATM 2512 O  O   . HOH I 8 .   ? -2.730  -1.637  3.866   1.00 29.39 ? 644 HOH A O   1 
HETATM 2513 O  O   . HOH I 8 .   ? 21.585  2.876   -6.501  1.00 25.72 ? 645 HOH A O   1 
HETATM 2514 O  O   . HOH I 8 .   ? -3.797  10.873  26.052  1.00 39.96 ? 646 HOH A O   1 
HETATM 2515 O  O   . HOH I 8 .   ? 3.334   -6.977  35.025  1.00 30.53 ? 647 HOH A O   1 
HETATM 2516 O  O   . HOH I 8 .   ? 24.972  -12.324 -6.218  1.00 27.07 ? 648 HOH A O   1 
HETATM 2517 O  O   . HOH I 8 .   ? 3.047   -10.141 31.519  1.00 28.76 ? 649 HOH A O   1 
HETATM 2518 O  O   . HOH I 8 .   ? 16.895  -3.599  -7.842  1.00 35.69 ? 650 HOH A O   1 
HETATM 2519 O  O   . HOH I 8 .   ? 5.372   -14.647 25.579  1.00 32.26 ? 651 HOH A O   1 
HETATM 2520 O  O   . HOH I 8 .   ? 8.350   13.126  -4.730  1.00 34.76 ? 652 HOH A O   1 
HETATM 2521 O  O   . HOH I 8 .   ? 23.953  -11.734 8.135   1.00 33.73 ? 653 HOH A O   1 
HETATM 2522 O  O   . HOH I 8 .   ? 18.766  -10.414 31.447  1.00 32.72 ? 654 HOH A O   1 
HETATM 2523 O  O   . HOH I 8 .   ? 8.032   11.850  -1.467  1.00 27.85 ? 655 HOH A O   1 
HETATM 2524 O  O   . HOH I 8 .   ? 27.569  -3.987  27.268  1.00 33.35 ? 656 HOH A O   1 
HETATM 2525 O  O   . HOH I 8 .   ? 4.258   -16.231 20.068  1.00 27.90 ? 657 HOH A O   1 
HETATM 2526 O  O   . HOH I 8 .   ? 19.566  -1.434  43.196  1.00 33.72 ? 658 HOH A O   1 
HETATM 2527 O  O   . HOH I 8 .   ? 11.696  12.877  -0.501  1.00 33.24 ? 659 HOH A O   1 
HETATM 2528 O  O   . HOH I 8 .   ? -3.167  -5.236  0.526   1.00 29.13 ? 660 HOH A O   1 
HETATM 2529 O  O   . HOH I 8 .   ? 11.970  4.860   34.746  1.00 26.43 ? 661 HOH A O   1 
HETATM 2530 O  O   . HOH I 8 .   ? 16.463  2.996   42.824  1.00 25.39 ? 662 HOH A O   1 
HETATM 2531 O  O   . HOH I 8 .   ? 18.933  -15.762 25.387  1.00 29.22 ? 663 HOH A O   1 
HETATM 2532 O  O   . HOH I 8 .   ? 22.312  5.659   2.180   1.00 31.60 ? 664 HOH A O   1 
HETATM 2533 O  O   . HOH I 8 .   ? 9.201   2.769   -7.594  1.00 31.93 ? 665 HOH A O   1 
HETATM 2534 O  O   . HOH I 8 .   ? 36.678  0.631   25.915  1.00 32.99 ? 666 HOH A O   1 
HETATM 2535 O  O   . HOH I 8 .   ? 15.943  -8.103  33.693  1.00 30.76 ? 667 HOH A O   1 
HETATM 2536 O  O   . HOH I 8 .   ? 13.945  -8.188  -4.412  1.00 29.64 ? 668 HOH A O   1 
HETATM 2537 O  O   . HOH I 8 .   ? 9.316   12.606  0.879   1.00 22.50 ? 669 HOH A O   1 
HETATM 2538 O  O   . HOH I 8 .   ? 8.778   15.561  4.815   1.00 26.92 ? 670 HOH A O   1 
HETATM 2539 O  O   . HOH I 8 .   ? 24.984  -11.450 21.571  1.00 40.32 ? 671 HOH A O   1 
HETATM 2540 O  O   . HOH I 8 .   ? 17.726  -15.603 3.589   1.00 34.44 ? 672 HOH A O   1 
HETATM 2541 O  O   . HOH I 8 .   ? 27.163  7.132   30.006  1.00 30.87 ? 673 HOH A O   1 
HETATM 2542 O  O   . HOH I 8 .   ? 19.531  -11.304 27.132  1.00 24.92 ? 674 HOH A O   1 
HETATM 2543 O  O   . HOH I 8 .   ? 9.974   -9.467  -2.820  1.00 33.86 ? 675 HOH A O   1 
HETATM 2544 O  O   . HOH I 8 .   ? 21.142  -5.028  -7.177  1.00 35.36 ? 676 HOH A O   1 
HETATM 2545 O  O   . HOH I 8 .   ? 22.755  -15.849 7.140   1.00 29.17 ? 677 HOH A O   1 
HETATM 2546 O  O   . HOH I 8 .   ? 19.930  -9.397  28.939  1.00 19.49 ? 678 HOH A O   1 
HETATM 2547 O  O   . HOH I 8 .   ? 22.206  5.456   -5.040  1.00 33.12 ? 679 HOH A O   1 
HETATM 2548 O  O   . HOH I 8 .   ? 24.634  5.016   0.113   1.00 35.65 ? 680 HOH A O   1 
HETATM 2549 O  O   . HOH I 8 .   ? 16.893  -13.504 -2.155  1.00 36.03 ? 681 HOH A O   1 
HETATM 2550 O  O   . HOH I 8 .   ? 25.022  10.686  23.581  1.00 33.35 ? 682 HOH A O   1 
HETATM 2551 O  O   . HOH I 8 .   ? 27.962  10.264  18.209  1.00 30.87 ? 683 HOH A O   1 
HETATM 2552 O  O   . HOH I 8 .   ? 23.132  -12.482 20.298  1.00 31.14 ? 684 HOH A O   1 
HETATM 2553 O  O   . HOH I 8 .   ? 33.406  -5.362  -1.767  1.00 30.75 ? 685 HOH A O   1 
# 
