data_6G5U
# 
_entry.id   6G5U 
# 
_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   6G5U         pdb_00006g5u 10.2210/pdb6g5u/pdb 
WWPDB D_1200009456 ?            ?                   
# 
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 2019-03-13 
2 'Structure model' 1 1 2024-01-17 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Data collection'        
2 2 'Structure model' 'Database references'    
3 2 'Structure model' 'Derived calculations'   
4 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' 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' '_struct_conn.pdbx_dist_value'        
4  2 'Structure model' '_struct_conn.ptnr1_auth_asym_id'     
5  2 'Structure model' '_struct_conn.ptnr1_auth_comp_id'     
6  2 'Structure model' '_struct_conn.ptnr1_auth_seq_id'      
7  2 'Structure model' '_struct_conn.ptnr1_label_asym_id'    
8  2 'Structure model' '_struct_conn.ptnr1_label_atom_id'    
9  2 'Structure model' '_struct_conn.ptnr1_label_comp_id'    
10 2 'Structure model' '_struct_conn.ptnr1_label_seq_id'     
11 2 'Structure model' '_struct_conn.ptnr2_auth_asym_id'     
12 2 'Structure model' '_struct_conn.ptnr2_auth_comp_id'     
13 2 'Structure model' '_struct_conn.ptnr2_auth_seq_id'      
14 2 'Structure model' '_struct_conn.ptnr2_label_asym_id'    
15 2 'Structure model' '_struct_conn.ptnr2_label_atom_id'    
16 2 'Structure model' '_struct_conn.ptnr2_label_comp_id'    
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        6G5U 
_pdbx_database_status.recvd_initial_deposition_date   2018-03-30 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_nmr_data            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Smirnov, A.'  1 ? 
'Manakova, E.' 2 ? 
'Grazulis, S.' 3 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   FR 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Eur J Med Chem' 
_citation.journal_id_ASTM           EJMCA5 
_citation.journal_id_CSD            0493 
_citation.journal_id_ISSN           1768-3254 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            156 
_citation.language                  ? 
_citation.page_first                61 
_citation.page_last                 78 
_citation.title                     
'Design of two-tail compounds with rotationally fixed benzenesulfonamide ring as inhibitors of carbonic anhydrases.' 
_citation.year                      2018 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.ejmech.2018.06.059 
_citation.pdbx_database_id_PubMed   30006175 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Zaksauskas, A.'   1 ? 
primary 'Capkauskaite, E.' 2 ? 
primary 'Jezepcikas, L.'   3 ? 
primary 'Linkuviene, V.'   4 ? 
primary 'Kisonaite, M.'    5 ? 
primary 'Smirnov, A.'      6 ? 
primary 'Manakova, E.'     7 ? 
primary 'Grazulis, S.'     8 ? 
primary 'Matulis, D.'      9 ? 
# 
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 13'                               29613.318 2   4.2.1.1 ? 'human carbonic anhydrase XIII' ? 
2 non-polymer syn 'ZINC ION'                                            65.409    2   ?       ? 
N-butyl-2,4-dichloro-5-sulfamoyl-benzamide ? 
3 non-polymer syn '~{N}-butyl-2,4-bis(chloranyl)-5-sulfamoyl-benzamide' 325.211   2   ?       ? ZN ? 
4 non-polymer syn 1,2-ETHANEDIOL                                        62.068    3   ?       ? 1,2-ETHANEDIOL ? 
5 non-polymer syn 'CITRIC ACID'                                         192.124   1   ?       ? 'CITRATE ANION' ? 
6 water       nat water                                                 18.015    607 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Carbonate dehydratase XIII,Carbonic anhydrase XIII,CA-XIII' 
# 
_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       
;MMSRLSWGYREHNGPIHWKEFFPIADGDQQSPIEIKTKEVKYDSSLRPLSIKYDPSSAKIISNSGHSFNVDFDDTENKSV
LRGGPLTGSYRLRQVHLHWGSADDHGSEHIVDGVSYAAELHVVHWNSDKYPSFVEAAHEPDGLAVLGVFLQIGEPNSQLQ
KITDTLDSIKEKGKQTRFTNFDLLSLLPPSWDYWTYPGSLTVPPLLESVTWIVLKQPINISSQQLAKFRSLLCTAEGEAA
AFLVSNHRPPQPLKGRKVRASFH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MMSRLSWGYREHNGPIHWKEFFPIADGDQQSPIEIKTKEVKYDSSLRPLSIKYDPSSAKIISNSGHSFNVDFDDTENKSV
LRGGPLTGSYRLRQVHLHWGSADDHGSEHIVDGVSYAAELHVVHWNSDKYPSFVEAAHEPDGLAVLGVFLQIGEPNSQLQ
KITDTLDSIKEKGKQTRFTNFDLLSLLPPSWDYWTYPGSLTVPPLLESVTWIVLKQPINISSQQLAKFRSLLCTAEGEAA
AFLVSNHRPPQPLKGRKVRASFH
;
_entity_poly.pdbx_strand_id                 B,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 '~{N}-butyl-2,4-bis(chloranyl)-5-sulfamoyl-benzamide' ENN 
4 1,2-ETHANEDIOL                                        EDO 
5 'CITRIC ACID'                                         CIT 
6 water                                                 HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   MET n 
1 3   SER n 
1 4   ARG n 
1 5   LEU n 
1 6   SER n 
1 7   TRP n 
1 8   GLY n 
1 9   TYR n 
1 10  ARG n 
1 11  GLU n 
1 12  HIS n 
1 13  ASN n 
1 14  GLY n 
1 15  PRO n 
1 16  ILE n 
1 17  HIS n 
1 18  TRP n 
1 19  LYS n 
1 20  GLU n 
1 21  PHE n 
1 22  PHE n 
1 23  PRO n 
1 24  ILE n 
1 25  ALA n 
1 26  ASP n 
1 27  GLY n 
1 28  ASP n 
1 29  GLN n 
1 30  GLN n 
1 31  SER n 
1 32  PRO n 
1 33  ILE n 
1 34  GLU n 
1 35  ILE n 
1 36  LYS n 
1 37  THR n 
1 38  LYS n 
1 39  GLU n 
1 40  VAL n 
1 41  LYS n 
1 42  TYR n 
1 43  ASP n 
1 44  SER n 
1 45  SER n 
1 46  LEU n 
1 47  ARG n 
1 48  PRO n 
1 49  LEU n 
1 50  SER n 
1 51  ILE n 
1 52  LYS n 
1 53  TYR n 
1 54  ASP n 
1 55  PRO n 
1 56  SER n 
1 57  SER n 
1 58  ALA n 
1 59  LYS n 
1 60  ILE n 
1 61  ILE n 
1 62  SER n 
1 63  ASN n 
1 64  SER n 
1 65  GLY n 
1 66  HIS n 
1 67  SER n 
1 68  PHE n 
1 69  ASN n 
1 70  VAL n 
1 71  ASP n 
1 72  PHE n 
1 73  ASP n 
1 74  ASP n 
1 75  THR n 
1 76  GLU n 
1 77  ASN n 
1 78  LYS n 
1 79  SER n 
1 80  VAL n 
1 81  LEU n 
1 82  ARG n 
1 83  GLY n 
1 84  GLY n 
1 85  PRO n 
1 86  LEU n 
1 87  THR n 
1 88  GLY n 
1 89  SER n 
1 90  TYR n 
1 91  ARG n 
1 92  LEU n 
1 93  ARG n 
1 94  GLN n 
1 95  VAL n 
1 96  HIS n 
1 97  LEU n 
1 98  HIS n 
1 99  TRP n 
1 100 GLY n 
1 101 SER n 
1 102 ALA n 
1 103 ASP n 
1 104 ASP n 
1 105 HIS n 
1 106 GLY n 
1 107 SER n 
1 108 GLU n 
1 109 HIS n 
1 110 ILE n 
1 111 VAL n 
1 112 ASP n 
1 113 GLY n 
1 114 VAL n 
1 115 SER n 
1 116 TYR n 
1 117 ALA n 
1 118 ALA n 
1 119 GLU n 
1 120 LEU n 
1 121 HIS n 
1 122 VAL n 
1 123 VAL n 
1 124 HIS n 
1 125 TRP n 
1 126 ASN n 
1 127 SER n 
1 128 ASP n 
1 129 LYS n 
1 130 TYR n 
1 131 PRO n 
1 132 SER n 
1 133 PHE n 
1 134 VAL n 
1 135 GLU n 
1 136 ALA n 
1 137 ALA n 
1 138 HIS n 
1 139 GLU n 
1 140 PRO n 
1 141 ASP n 
1 142 GLY n 
1 143 LEU n 
1 144 ALA n 
1 145 VAL n 
1 146 LEU n 
1 147 GLY n 
1 148 VAL n 
1 149 PHE n 
1 150 LEU n 
1 151 GLN n 
1 152 ILE n 
1 153 GLY n 
1 154 GLU n 
1 155 PRO n 
1 156 ASN n 
1 157 SER n 
1 158 GLN n 
1 159 LEU n 
1 160 GLN n 
1 161 LYS n 
1 162 ILE n 
1 163 THR n 
1 164 ASP n 
1 165 THR n 
1 166 LEU n 
1 167 ASP n 
1 168 SER n 
1 169 ILE n 
1 170 LYS n 
1 171 GLU n 
1 172 LYS n 
1 173 GLY n 
1 174 LYS n 
1 175 GLN n 
1 176 THR n 
1 177 ARG n 
1 178 PHE n 
1 179 THR n 
1 180 ASN n 
1 181 PHE n 
1 182 ASP n 
1 183 LEU n 
1 184 LEU n 
1 185 SER n 
1 186 LEU n 
1 187 LEU n 
1 188 PRO n 
1 189 PRO n 
1 190 SER n 
1 191 TRP n 
1 192 ASP n 
1 193 TYR n 
1 194 TRP n 
1 195 THR n 
1 196 TYR n 
1 197 PRO n 
1 198 GLY n 
1 199 SER n 
1 200 LEU n 
1 201 THR n 
1 202 VAL n 
1 203 PRO n 
1 204 PRO n 
1 205 LEU n 
1 206 LEU n 
1 207 GLU n 
1 208 SER n 
1 209 VAL n 
1 210 THR n 
1 211 TRP n 
1 212 ILE n 
1 213 VAL n 
1 214 LEU n 
1 215 LYS n 
1 216 GLN n 
1 217 PRO n 
1 218 ILE n 
1 219 ASN n 
1 220 ILE n 
1 221 SER n 
1 222 SER n 
1 223 GLN n 
1 224 GLN n 
1 225 LEU n 
1 226 ALA n 
1 227 LYS n 
1 228 PHE n 
1 229 ARG n 
1 230 SER n 
1 231 LEU n 
1 232 LEU n 
1 233 CYS n 
1 234 THR n 
1 235 ALA n 
1 236 GLU n 
1 237 GLY n 
1 238 GLU n 
1 239 ALA n 
1 240 ALA n 
1 241 ALA n 
1 242 PHE n 
1 243 LEU n 
1 244 VAL n 
1 245 SER n 
1 246 ASN n 
1 247 HIS n 
1 248 ARG n 
1 249 PRO n 
1 250 PRO n 
1 251 GLN n 
1 252 PRO n 
1 253 LEU n 
1 254 LYS n 
1 255 GLY n 
1 256 ARG n 
1 257 LYS n 
1 258 VAL n 
1 259 ARG n 
1 260 ALA n 
1 261 SER n 
1 262 PHE n 
1 263 HIS 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                   263 
_entity_src_gen.gene_src_common_name               Human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 CA13 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pET15b 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                               ?                 'C3 H7 N O2'          89.093  
ARG 'L-peptide linking' y ARGININE                                              ?                 'C6 H15 N4 O2 1'      175.209 
ASN 'L-peptide linking' y ASPARAGINE                                            ?                 'C4 H8 N2 O3'         132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                       ?                 'C4 H7 N O4'          133.103 
CIT non-polymer         . 'CITRIC ACID'                                         ?                 'C6 H8 O7'            192.124 
CYS 'L-peptide linking' y CYSTEINE                                              ?                 'C3 H7 N O2 S'        121.158 
EDO non-polymer         . 1,2-ETHANEDIOL                                        'ETHYLENE GLYCOL' 'C2 H6 O2'            62.068  
ENN non-polymer         . '~{N}-butyl-2,4-bis(chloranyl)-5-sulfamoyl-benzamide' ?                 'C11 H14 Cl2 N2 O3 S' 325.211 
GLN 'L-peptide linking' y GLUTAMINE                                             ?                 'C5 H10 N2 O3'        146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                       ?                 'C5 H9 N O4'          147.129 
GLY 'peptide linking'   y GLYCINE                                               ?                 'C2 H5 N O2'          75.067  
HIS 'L-peptide linking' y HISTIDINE                                             ?                 'C6 H10 N3 O2 1'      156.162 
HOH non-polymer         . WATER                                                 ?                 'H2 O'                18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                            ?                 'C6 H13 N O2'         131.173 
LEU 'L-peptide linking' y LEUCINE                                               ?                 'C6 H13 N O2'         131.173 
LYS 'L-peptide linking' y LYSINE                                                ?                 'C6 H15 N2 O2 1'      147.195 
MET 'L-peptide linking' y METHIONINE                                            ?                 'C5 H11 N O2 S'       149.211 
PHE 'L-peptide linking' y PHENYLALANINE                                         ?                 'C9 H11 N O2'         165.189 
PRO 'L-peptide linking' y PROLINE                                               ?                 'C5 H9 N O2'          115.130 
SER 'L-peptide linking' y SERINE                                                ?                 'C3 H7 N O3'          105.093 
THR 'L-peptide linking' y THREONINE                                             ?                 'C4 H9 N O3'          119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                            ?                 'C11 H12 N2 O2'       204.225 
TYR 'L-peptide linking' y TYROSINE                                              ?                 'C9 H11 N O3'         181.189 
VAL 'L-peptide linking' y VALINE                                                ?                 'C5 H11 N O2'         117.146 
ZN  non-polymer         . 'ZINC ION'                                            ?                 'Zn 2'                65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   B . n 
A 1 2   MET 2   2   ?   ?   ?   B . n 
A 1 3   SER 3   3   ?   ?   ?   B . n 
A 1 4   ARG 4   4   ?   ?   ?   B . n 
A 1 5   LEU 5   5   ?   ?   ?   B . n 
A 1 6   SER 6   6   6   SER SER B . n 
A 1 7   TRP 7   7   7   TRP TRP B . n 
A 1 8   GLY 8   8   8   GLY GLY B . n 
A 1 9   TYR 9   9   9   TYR TYR B . n 
A 1 10  ARG 10  10  10  ARG ARG B . n 
A 1 11  GLU 11  11  11  GLU GLU B . n 
A 1 12  HIS 12  12  12  HIS HIS B . n 
A 1 13  ASN 13  13  13  ASN ASN B . n 
A 1 14  GLY 14  14  14  GLY GLY B . n 
A 1 15  PRO 15  15  15  PRO PRO B . n 
A 1 16  ILE 16  16  16  ILE ILE B . n 
A 1 17  HIS 17  17  17  HIS HIS B . n 
A 1 18  TRP 18  18  18  TRP TRP B . n 
A 1 19  LYS 19  19  19  LYS LYS B . n 
A 1 20  GLU 20  20  20  GLU GLU B . n 
A 1 21  PHE 21  21  21  PHE PHE B . n 
A 1 22  PHE 22  22  22  PHE PHE B . n 
A 1 23  PRO 23  23  23  PRO PRO B . n 
A 1 24  ILE 24  24  24  ILE ILE B . n 
A 1 25  ALA 25  25  25  ALA ALA B . n 
A 1 26  ASP 26  26  26  ASP ASP B . n 
A 1 27  GLY 27  27  27  GLY GLY B . n 
A 1 28  ASP 28  28  28  ASP ASP B . n 
A 1 29  GLN 29  29  29  GLN GLN B . n 
A 1 30  GLN 30  30  30  GLN GLN B . n 
A 1 31  SER 31  31  31  SER SER B . n 
A 1 32  PRO 32  32  32  PRO PRO B . n 
A 1 33  ILE 33  33  33  ILE ILE B . n 
A 1 34  GLU 34  34  34  GLU GLU B . n 
A 1 35  ILE 35  35  35  ILE ILE B . n 
A 1 36  LYS 36  36  36  LYS LYS B . n 
A 1 37  THR 37  37  37  THR THR B . n 
A 1 38  LYS 38  38  38  LYS LYS B . n 
A 1 39  GLU 39  39  39  GLU GLU B . n 
A 1 40  VAL 40  40  40  VAL VAL B . n 
A 1 41  LYS 41  41  41  LYS LYS B . n 
A 1 42  TYR 42  42  42  TYR TYR B . n 
A 1 43  ASP 43  43  43  ASP ASP B . n 
A 1 44  SER 44  44  44  SER SER B . n 
A 1 45  SER 45  45  45  SER SER B . n 
A 1 46  LEU 46  46  46  LEU LEU B . n 
A 1 47  ARG 47  47  47  ARG ARG B . n 
A 1 48  PRO 48  48  48  PRO PRO B . n 
A 1 49  LEU 49  49  49  LEU LEU B . n 
A 1 50  SER 50  50  50  SER SER B . n 
A 1 51  ILE 51  51  51  ILE ILE B . n 
A 1 52  LYS 52  52  52  LYS LYS B . n 
A 1 53  TYR 53  53  53  TYR TYR B . n 
A 1 54  ASP 54  54  54  ASP ASP B . n 
A 1 55  PRO 55  55  55  PRO PRO B . n 
A 1 56  SER 56  56  56  SER SER B . n 
A 1 57  SER 57  57  57  SER SER B . n 
A 1 58  ALA 58  58  58  ALA ALA B . n 
A 1 59  LYS 59  59  59  LYS LYS B . n 
A 1 60  ILE 60  60  60  ILE ILE B . n 
A 1 61  ILE 61  61  61  ILE ILE B . n 
A 1 62  SER 62  62  62  SER SER B . n 
A 1 63  ASN 63  63  63  ASN ASN B . n 
A 1 64  SER 64  64  64  SER SER B . n 
A 1 65  GLY 65  65  65  GLY GLY B . n 
A 1 66  HIS 66  66  66  HIS HIS B . n 
A 1 67  SER 67  67  67  SER SER B . n 
A 1 68  PHE 68  68  68  PHE PHE B . n 
A 1 69  ASN 69  69  69  ASN ASN B . n 
A 1 70  VAL 70  70  70  VAL VAL B . n 
A 1 71  ASP 71  71  71  ASP ASP B . n 
A 1 72  PHE 72  72  72  PHE PHE B . n 
A 1 73  ASP 73  73  73  ASP ASP B . n 
A 1 74  ASP 74  74  74  ASP ASP B . n 
A 1 75  THR 75  75  75  THR THR B . n 
A 1 76  GLU 76  76  76  GLU GLU B . n 
A 1 77  ASN 77  77  77  ASN ASN B . n 
A 1 78  LYS 78  78  78  LYS LYS B . n 
A 1 79  SER 79  79  79  SER SER B . n 
A 1 80  VAL 80  80  80  VAL VAL B . n 
A 1 81  LEU 81  81  81  LEU LEU B . n 
A 1 82  ARG 82  82  82  ARG ARG B . n 
A 1 83  GLY 83  83  83  GLY GLY B . n 
A 1 84  GLY 84  84  84  GLY GLY B . n 
A 1 85  PRO 85  85  85  PRO PRO B . n 
A 1 86  LEU 86  86  86  LEU LEU B . n 
A 1 87  THR 87  87  87  THR THR B . n 
A 1 88  GLY 88  88  88  GLY GLY B . n 
A 1 89  SER 89  89  89  SER SER B . n 
A 1 90  TYR 90  90  90  TYR TYR B . n 
A 1 91  ARG 91  91  91  ARG ARG B . n 
A 1 92  LEU 92  92  92  LEU LEU B . n 
A 1 93  ARG 93  93  93  ARG ARG B . n 
A 1 94  GLN 94  94  94  GLN GLN B . n 
A 1 95  VAL 95  95  95  VAL VAL B . n 
A 1 96  HIS 96  96  96  HIS HIS B . n 
A 1 97  LEU 97  97  97  LEU LEU B . n 
A 1 98  HIS 98  98  98  HIS HIS B . n 
A 1 99  TRP 99  99  99  TRP TRP B . n 
A 1 100 GLY 100 100 100 GLY GLY B . n 
A 1 101 SER 101 101 101 SER SER B . n 
A 1 102 ALA 102 102 102 ALA ALA B . n 
A 1 103 ASP 103 103 103 ASP ASP B . n 
A 1 104 ASP 104 104 104 ASP ASP B . n 
A 1 105 HIS 105 105 105 HIS HIS B . n 
A 1 106 GLY 106 106 106 GLY GLY B . n 
A 1 107 SER 107 107 107 SER SER B . n 
A 1 108 GLU 108 108 108 GLU GLU B . n 
A 1 109 HIS 109 109 109 HIS HIS B . n 
A 1 110 ILE 110 110 110 ILE ILE B . n 
A 1 111 VAL 111 111 111 VAL VAL B . n 
A 1 112 ASP 112 112 112 ASP ASP B . n 
A 1 113 GLY 113 113 113 GLY GLY B . n 
A 1 114 VAL 114 114 114 VAL VAL B . n 
A 1 115 SER 115 115 115 SER SER B . n 
A 1 116 TYR 116 116 116 TYR TYR B . n 
A 1 117 ALA 117 117 117 ALA ALA B . n 
A 1 118 ALA 118 118 118 ALA ALA B . n 
A 1 119 GLU 119 119 119 GLU GLU B . n 
A 1 120 LEU 120 120 120 LEU LEU B . n 
A 1 121 HIS 121 121 121 HIS HIS B . n 
A 1 122 VAL 122 122 122 VAL VAL B . n 
A 1 123 VAL 123 123 123 VAL VAL B . n 
A 1 124 HIS 124 124 124 HIS HIS B . n 
A 1 125 TRP 125 125 125 TRP TRP B . n 
A 1 126 ASN 126 126 126 ASN ASN B . n 
A 1 127 SER 127 127 127 SER SER B . n 
A 1 128 ASP 128 128 128 ASP ASP B . n 
A 1 129 LYS 129 129 129 LYS LYS B . n 
A 1 130 TYR 130 130 130 TYR TYR B . n 
A 1 131 PRO 131 131 131 PRO PRO B . n 
A 1 132 SER 132 132 132 SER SER B . n 
A 1 133 PHE 133 133 133 PHE PHE B . n 
A 1 134 VAL 134 134 134 VAL VAL B . n 
A 1 135 GLU 135 135 135 GLU GLU B . n 
A 1 136 ALA 136 136 136 ALA ALA B . n 
A 1 137 ALA 137 137 137 ALA ALA B . n 
A 1 138 HIS 138 138 138 HIS HIS B . n 
A 1 139 GLU 139 139 139 GLU GLU B . n 
A 1 140 PRO 140 140 140 PRO PRO B . n 
A 1 141 ASP 141 141 141 ASP ASP B . n 
A 1 142 GLY 142 142 142 GLY GLY B . n 
A 1 143 LEU 143 143 143 LEU LEU B . n 
A 1 144 ALA 144 144 144 ALA ALA B . n 
A 1 145 VAL 145 145 145 VAL VAL B . n 
A 1 146 LEU 146 146 146 LEU LEU B . n 
A 1 147 GLY 147 147 147 GLY GLY B . n 
A 1 148 VAL 148 148 148 VAL VAL B . n 
A 1 149 PHE 149 149 149 PHE PHE B . n 
A 1 150 LEU 150 150 150 LEU LEU B . n 
A 1 151 GLN 151 151 151 GLN GLN B . n 
A 1 152 ILE 152 152 152 ILE ILE B . n 
A 1 153 GLY 153 153 153 GLY GLY B . n 
A 1 154 GLU 154 154 154 GLU GLU B . n 
A 1 155 PRO 155 155 155 PRO PRO B . n 
A 1 156 ASN 156 156 156 ASN ASN B . n 
A 1 157 SER 157 157 157 SER SER B . n 
A 1 158 GLN 158 158 158 GLN GLN B . n 
A 1 159 LEU 159 159 159 LEU LEU B . n 
A 1 160 GLN 160 160 160 GLN GLN B . n 
A 1 161 LYS 161 161 161 LYS LYS B . n 
A 1 162 ILE 162 162 162 ILE ILE B . n 
A 1 163 THR 163 163 163 THR THR B . n 
A 1 164 ASP 164 164 164 ASP ASP B . n 
A 1 165 THR 165 165 165 THR THR B . n 
A 1 166 LEU 166 166 166 LEU LEU B . n 
A 1 167 ASP 167 167 167 ASP ASP B . n 
A 1 168 SER 168 168 168 SER SER B . n 
A 1 169 ILE 169 169 169 ILE ILE B . n 
A 1 170 LYS 170 170 170 LYS LYS B . n 
A 1 171 GLU 171 171 171 GLU GLU B . n 
A 1 172 LYS 172 172 172 LYS LYS B . n 
A 1 173 GLY 173 173 173 GLY GLY B . n 
A 1 174 LYS 174 174 174 LYS LYS B . n 
A 1 175 GLN 175 175 175 GLN GLN B . n 
A 1 176 THR 176 176 176 THR THR B . n 
A 1 177 ARG 177 177 177 ARG ARG B . n 
A 1 178 PHE 178 178 178 PHE PHE B . n 
A 1 179 THR 179 179 179 THR THR B . n 
A 1 180 ASN 180 180 180 ASN ASN B . n 
A 1 181 PHE 181 181 181 PHE PHE B . n 
A 1 182 ASP 182 182 182 ASP ASP B . n 
A 1 183 LEU 183 183 183 LEU LEU B . n 
A 1 184 LEU 184 184 184 LEU LEU B . n 
A 1 185 SER 185 185 185 SER SER B . n 
A 1 186 LEU 186 186 186 LEU LEU B . n 
A 1 187 LEU 187 187 187 LEU LEU B . n 
A 1 188 PRO 188 188 188 PRO PRO B . n 
A 1 189 PRO 189 189 189 PRO PRO B . n 
A 1 190 SER 190 190 190 SER SER B . n 
A 1 191 TRP 191 191 191 TRP TRP B . n 
A 1 192 ASP 192 192 192 ASP ASP B . n 
A 1 193 TYR 193 193 193 TYR TYR B . n 
A 1 194 TRP 194 194 194 TRP TRP B . n 
A 1 195 THR 195 195 195 THR THR B . n 
A 1 196 TYR 196 196 196 TYR TYR B . n 
A 1 197 PRO 197 197 197 PRO PRO B . n 
A 1 198 GLY 198 198 198 GLY GLY B . n 
A 1 199 SER 199 199 199 SER SER B . n 
A 1 200 LEU 200 200 200 LEU LEU B . n 
A 1 201 THR 201 201 201 THR THR B . n 
A 1 202 VAL 202 202 202 VAL VAL B . n 
A 1 203 PRO 203 203 203 PRO PRO B . n 
A 1 204 PRO 204 204 204 PRO PRO B . n 
A 1 205 LEU 205 205 205 LEU LEU B . n 
A 1 206 LEU 206 206 206 LEU LEU B . n 
A 1 207 GLU 207 207 207 GLU GLU B . n 
A 1 208 SER 208 208 208 SER SER B . n 
A 1 209 VAL 209 209 209 VAL VAL B . n 
A 1 210 THR 210 210 210 THR THR B . n 
A 1 211 TRP 211 211 211 TRP TRP B . n 
A 1 212 ILE 212 212 212 ILE ILE B . n 
A 1 213 VAL 213 213 213 VAL VAL B . n 
A 1 214 LEU 214 214 214 LEU LEU B . n 
A 1 215 LYS 215 215 215 LYS LYS B . n 
A 1 216 GLN 216 216 216 GLN GLN B . n 
A 1 217 PRO 217 217 217 PRO PRO B . n 
A 1 218 ILE 218 218 218 ILE ILE B . n 
A 1 219 ASN 219 219 219 ASN ASN B . n 
A 1 220 ILE 220 220 220 ILE ILE B . n 
A 1 221 SER 221 221 221 SER SER B . n 
A 1 222 SER 222 222 222 SER SER B . n 
A 1 223 GLN 223 223 223 GLN GLN B . n 
A 1 224 GLN 224 224 224 GLN GLN B . n 
A 1 225 LEU 225 225 225 LEU LEU B . n 
A 1 226 ALA 226 226 226 ALA ALA B . n 
A 1 227 LYS 227 227 227 LYS LYS B . n 
A 1 228 PHE 228 228 228 PHE PHE B . n 
A 1 229 ARG 229 229 229 ARG ARG B . n 
A 1 230 SER 230 230 230 SER SER B . n 
A 1 231 LEU 231 231 231 LEU LEU B . n 
A 1 232 LEU 232 232 232 LEU LEU B . n 
A 1 233 CYS 233 233 233 CYS CYS B . n 
A 1 234 THR 234 234 234 THR THR B . n 
A 1 235 ALA 235 235 235 ALA ALA B . n 
A 1 236 GLU 236 236 236 GLU GLU B . n 
A 1 237 GLY 237 237 237 GLY GLY B . n 
A 1 238 GLU 238 238 238 GLU GLU B . n 
A 1 239 ALA 239 239 239 ALA ALA B . n 
A 1 240 ALA 240 240 240 ALA ALA B . n 
A 1 241 ALA 241 241 241 ALA ALA B . n 
A 1 242 PHE 242 242 242 PHE PHE B . n 
A 1 243 LEU 243 243 243 LEU LEU B . n 
A 1 244 VAL 244 244 244 VAL VAL B . n 
A 1 245 SER 245 245 245 SER SER B . n 
A 1 246 ASN 246 246 246 ASN ASN B . n 
A 1 247 HIS 247 247 247 HIS HIS B . n 
A 1 248 ARG 248 248 248 ARG ARG B . n 
A 1 249 PRO 249 249 249 PRO PRO B . n 
A 1 250 PRO 250 250 250 PRO PRO B . n 
A 1 251 GLN 251 251 251 GLN GLN B . n 
A 1 252 PRO 252 252 252 PRO PRO B . n 
A 1 253 LEU 253 253 253 LEU LEU B . n 
A 1 254 LYS 254 254 254 LYS LYS B . n 
A 1 255 GLY 255 255 255 GLY GLY B . n 
A 1 256 ARG 256 256 256 ARG ARG B . n 
A 1 257 LYS 257 257 257 LYS LYS B . n 
A 1 258 VAL 258 258 258 VAL VAL B . n 
A 1 259 ARG 259 259 259 ARG ARG B . n 
A 1 260 ALA 260 260 260 ALA ALA B . n 
A 1 261 SER 261 261 261 SER SER B . n 
A 1 262 PHE 262 262 262 PHE PHE B . n 
A 1 263 HIS 263 263 263 HIS HIS B . n 
B 1 1   MET 1   1   ?   ?   ?   A . n 
B 1 2   MET 2   2   ?   ?   ?   A . n 
B 1 3   SER 3   3   ?   ?   ?   A . n 
B 1 4   ARG 4   4   ?   ?   ?   A . n 
B 1 5   LEU 5   5   ?   ?   ?   A . n 
B 1 6   SER 6   6   6   SER SER A . n 
B 1 7   TRP 7   7   7   TRP TRP A . n 
B 1 8   GLY 8   8   8   GLY GLY A . n 
B 1 9   TYR 9   9   9   TYR TYR A . n 
B 1 10  ARG 10  10  10  ARG ARG A . n 
B 1 11  GLU 11  11  11  GLU GLU A . n 
B 1 12  HIS 12  12  12  HIS HIS A . n 
B 1 13  ASN 13  13  13  ASN ASN A . n 
B 1 14  GLY 14  14  14  GLY GLY A . n 
B 1 15  PRO 15  15  15  PRO PRO A . n 
B 1 16  ILE 16  16  16  ILE ILE A . n 
B 1 17  HIS 17  17  17  HIS HIS A . n 
B 1 18  TRP 18  18  18  TRP TRP A . n 
B 1 19  LYS 19  19  19  LYS LYS A . n 
B 1 20  GLU 20  20  20  GLU GLU A . n 
B 1 21  PHE 21  21  21  PHE PHE A . n 
B 1 22  PHE 22  22  22  PHE PHE A . n 
B 1 23  PRO 23  23  23  PRO PRO A . n 
B 1 24  ILE 24  24  24  ILE ILE A . n 
B 1 25  ALA 25  25  25  ALA ALA A . n 
B 1 26  ASP 26  26  26  ASP ASP A . n 
B 1 27  GLY 27  27  27  GLY GLY A . n 
B 1 28  ASP 28  28  28  ASP ASP A . n 
B 1 29  GLN 29  29  29  GLN GLN A . n 
B 1 30  GLN 30  30  30  GLN GLN A . n 
B 1 31  SER 31  31  31  SER SER A . n 
B 1 32  PRO 32  32  32  PRO PRO A . n 
B 1 33  ILE 33  33  33  ILE ILE A . n 
B 1 34  GLU 34  34  34  GLU GLU A . n 
B 1 35  ILE 35  35  35  ILE ILE A . n 
B 1 36  LYS 36  36  36  LYS LYS A . n 
B 1 37  THR 37  37  37  THR THR A . n 
B 1 38  LYS 38  38  38  LYS LYS A . n 
B 1 39  GLU 39  39  39  GLU GLU A . n 
B 1 40  VAL 40  40  40  VAL VAL A . n 
B 1 41  LYS 41  41  41  LYS LYS A . n 
B 1 42  TYR 42  42  42  TYR TYR A . n 
B 1 43  ASP 43  43  43  ASP ASP A . n 
B 1 44  SER 44  44  44  SER SER A . n 
B 1 45  SER 45  45  45  SER SER A . n 
B 1 46  LEU 46  46  46  LEU LEU A . n 
B 1 47  ARG 47  47  47  ARG ARG A . n 
B 1 48  PRO 48  48  48  PRO PRO A . n 
B 1 49  LEU 49  49  49  LEU LEU A . n 
B 1 50  SER 50  50  50  SER SER A . n 
B 1 51  ILE 51  51  51  ILE ILE A . n 
B 1 52  LYS 52  52  52  LYS LYS A . n 
B 1 53  TYR 53  53  53  TYR TYR A . n 
B 1 54  ASP 54  54  54  ASP ASP A . n 
B 1 55  PRO 55  55  55  PRO PRO A . n 
B 1 56  SER 56  56  56  SER SER A . n 
B 1 57  SER 57  57  57  SER SER A . n 
B 1 58  ALA 58  58  58  ALA ALA A . n 
B 1 59  LYS 59  59  59  LYS LYS A . n 
B 1 60  ILE 60  60  60  ILE ILE A . n 
B 1 61  ILE 61  61  61  ILE ILE A . n 
B 1 62  SER 62  62  62  SER SER A . n 
B 1 63  ASN 63  63  63  ASN ASN A . n 
B 1 64  SER 64  64  64  SER SER A . n 
B 1 65  GLY 65  65  65  GLY GLY A . n 
B 1 66  HIS 66  66  66  HIS HIS A . n 
B 1 67  SER 67  67  67  SER SER A . n 
B 1 68  PHE 68  68  68  PHE PHE A . n 
B 1 69  ASN 69  69  69  ASN ASN A . n 
B 1 70  VAL 70  70  70  VAL VAL A . n 
B 1 71  ASP 71  71  71  ASP ASP A . n 
B 1 72  PHE 72  72  72  PHE PHE A . n 
B 1 73  ASP 73  73  73  ASP ASP A . n 
B 1 74  ASP 74  74  74  ASP ASP A . n 
B 1 75  THR 75  75  75  THR THR A . n 
B 1 76  GLU 76  76  76  GLU GLU A . n 
B 1 77  ASN 77  77  77  ASN ASN A . n 
B 1 78  LYS 78  78  78  LYS LYS A . n 
B 1 79  SER 79  79  79  SER SER A . n 
B 1 80  VAL 80  80  80  VAL VAL A . n 
B 1 81  LEU 81  81  81  LEU LEU A . n 
B 1 82  ARG 82  82  82  ARG ARG A . n 
B 1 83  GLY 83  83  83  GLY GLY A . n 
B 1 84  GLY 84  84  84  GLY GLY A . n 
B 1 85  PRO 85  85  85  PRO PRO A . n 
B 1 86  LEU 86  86  86  LEU LEU A . n 
B 1 87  THR 87  87  87  THR THR A . n 
B 1 88  GLY 88  88  88  GLY GLY A . n 
B 1 89  SER 89  89  89  SER SER A . n 
B 1 90  TYR 90  90  90  TYR TYR A . n 
B 1 91  ARG 91  91  91  ARG ARG A . n 
B 1 92  LEU 92  92  92  LEU LEU A . n 
B 1 93  ARG 93  93  93  ARG ARG A . n 
B 1 94  GLN 94  94  94  GLN GLN A . n 
B 1 95  VAL 95  95  95  VAL VAL A . n 
B 1 96  HIS 96  96  96  HIS HIS A . n 
B 1 97  LEU 97  97  97  LEU LEU A . n 
B 1 98  HIS 98  98  98  HIS HIS A . n 
B 1 99  TRP 99  99  99  TRP TRP A . n 
B 1 100 GLY 100 100 100 GLY GLY A . n 
B 1 101 SER 101 101 101 SER SER A . n 
B 1 102 ALA 102 102 102 ALA ALA A . n 
B 1 103 ASP 103 103 103 ASP ASP A . n 
B 1 104 ASP 104 104 104 ASP ASP A . n 
B 1 105 HIS 105 105 105 HIS HIS A . n 
B 1 106 GLY 106 106 106 GLY GLY A . n 
B 1 107 SER 107 107 107 SER SER A . n 
B 1 108 GLU 108 108 108 GLU GLU A . n 
B 1 109 HIS 109 109 109 HIS HIS A . n 
B 1 110 ILE 110 110 110 ILE ILE A . n 
B 1 111 VAL 111 111 111 VAL VAL A . n 
B 1 112 ASP 112 112 112 ASP ASP A . n 
B 1 113 GLY 113 113 113 GLY GLY A . n 
B 1 114 VAL 114 114 114 VAL VAL A . n 
B 1 115 SER 115 115 115 SER SER A . n 
B 1 116 TYR 116 116 116 TYR TYR A . n 
B 1 117 ALA 117 117 117 ALA ALA A . n 
B 1 118 ALA 118 118 118 ALA ALA A . n 
B 1 119 GLU 119 119 119 GLU GLU A . n 
B 1 120 LEU 120 120 120 LEU LEU A . n 
B 1 121 HIS 121 121 121 HIS HIS A . n 
B 1 122 VAL 122 122 122 VAL VAL A . n 
B 1 123 VAL 123 123 123 VAL VAL A . n 
B 1 124 HIS 124 124 124 HIS HIS A . n 
B 1 125 TRP 125 125 125 TRP TRP A . n 
B 1 126 ASN 126 126 126 ASN ASN A . n 
B 1 127 SER 127 127 127 SER SER A . n 
B 1 128 ASP 128 128 128 ASP ASP A . n 
B 1 129 LYS 129 129 129 LYS LYS A . n 
B 1 130 TYR 130 130 130 TYR TYR A . n 
B 1 131 PRO 131 131 131 PRO PRO A . n 
B 1 132 SER 132 132 132 SER SER A . n 
B 1 133 PHE 133 133 133 PHE PHE A . n 
B 1 134 VAL 134 134 134 VAL VAL A . n 
B 1 135 GLU 135 135 135 GLU GLU A . n 
B 1 136 ALA 136 136 136 ALA ALA A . n 
B 1 137 ALA 137 137 137 ALA ALA A . n 
B 1 138 HIS 138 138 138 HIS HIS A . n 
B 1 139 GLU 139 139 139 GLU GLU A . n 
B 1 140 PRO 140 140 140 PRO PRO A . n 
B 1 141 ASP 141 141 141 ASP ASP A . n 
B 1 142 GLY 142 142 142 GLY GLY A . n 
B 1 143 LEU 143 143 143 LEU LEU A . n 
B 1 144 ALA 144 144 144 ALA ALA A . n 
B 1 145 VAL 145 145 145 VAL VAL A . n 
B 1 146 LEU 146 146 146 LEU LEU A . n 
B 1 147 GLY 147 147 147 GLY GLY A . n 
B 1 148 VAL 148 148 148 VAL VAL A . n 
B 1 149 PHE 149 149 149 PHE PHE A . n 
B 1 150 LEU 150 150 150 LEU LEU A . n 
B 1 151 GLN 151 151 151 GLN GLN A . n 
B 1 152 ILE 152 152 152 ILE ILE A . n 
B 1 153 GLY 153 153 153 GLY GLY A . n 
B 1 154 GLU 154 154 154 GLU GLU A . n 
B 1 155 PRO 155 155 155 PRO PRO A . n 
B 1 156 ASN 156 156 156 ASN ASN A . n 
B 1 157 SER 157 157 157 SER SER A . n 
B 1 158 GLN 158 158 158 GLN GLN A . n 
B 1 159 LEU 159 159 159 LEU LEU A . n 
B 1 160 GLN 160 160 160 GLN GLN A . n 
B 1 161 LYS 161 161 161 LYS LYS A . n 
B 1 162 ILE 162 162 162 ILE ILE A . n 
B 1 163 THR 163 163 163 THR THR A . n 
B 1 164 ASP 164 164 164 ASP ASP A . n 
B 1 165 THR 165 165 165 THR THR A . n 
B 1 166 LEU 166 166 166 LEU LEU A . n 
B 1 167 ASP 167 167 167 ASP ASP A . n 
B 1 168 SER 168 168 168 SER SER A . n 
B 1 169 ILE 169 169 169 ILE ILE A . n 
B 1 170 LYS 170 170 170 LYS LYS A . n 
B 1 171 GLU 171 171 171 GLU GLU A . n 
B 1 172 LYS 172 172 172 LYS LYS A . n 
B 1 173 GLY 173 173 173 GLY GLY A . n 
B 1 174 LYS 174 174 174 LYS LYS A . n 
B 1 175 GLN 175 175 175 GLN GLN A . n 
B 1 176 THR 176 176 176 THR THR A . n 
B 1 177 ARG 177 177 177 ARG ARG A . n 
B 1 178 PHE 178 178 178 PHE PHE A . n 
B 1 179 THR 179 179 179 THR THR A . n 
B 1 180 ASN 180 180 180 ASN ASN A . n 
B 1 181 PHE 181 181 181 PHE PHE A . n 
B 1 182 ASP 182 182 182 ASP ASP A . n 
B 1 183 LEU 183 183 183 LEU LEU A . n 
B 1 184 LEU 184 184 184 LEU LEU A . n 
B 1 185 SER 185 185 185 SER SER A . n 
B 1 186 LEU 186 186 186 LEU LEU A . n 
B 1 187 LEU 187 187 187 LEU LEU A . n 
B 1 188 PRO 188 188 188 PRO PRO A . n 
B 1 189 PRO 189 189 189 PRO PRO A . n 
B 1 190 SER 190 190 190 SER SER A . n 
B 1 191 TRP 191 191 191 TRP TRP A . n 
B 1 192 ASP 192 192 192 ASP ASP A . n 
B 1 193 TYR 193 193 193 TYR TYR A . n 
B 1 194 TRP 194 194 194 TRP TRP A . n 
B 1 195 THR 195 195 195 THR THR A . n 
B 1 196 TYR 196 196 196 TYR TYR A . n 
B 1 197 PRO 197 197 197 PRO PRO A . n 
B 1 198 GLY 198 198 198 GLY GLY A . n 
B 1 199 SER 199 199 199 SER SER A . n 
B 1 200 LEU 200 200 200 LEU LEU A . n 
B 1 201 THR 201 201 201 THR THR A . n 
B 1 202 VAL 202 202 202 VAL VAL A . n 
B 1 203 PRO 203 203 203 PRO PRO A . n 
B 1 204 PRO 204 204 204 PRO PRO A . n 
B 1 205 LEU 205 205 205 LEU LEU A . n 
B 1 206 LEU 206 206 206 LEU LEU A . n 
B 1 207 GLU 207 207 207 GLU GLU A . n 
B 1 208 SER 208 208 208 SER SER A . n 
B 1 209 VAL 209 209 209 VAL VAL A . n 
B 1 210 THR 210 210 210 THR THR A . n 
B 1 211 TRP 211 211 211 TRP TRP A . n 
B 1 212 ILE 212 212 212 ILE ILE A . n 
B 1 213 VAL 213 213 213 VAL VAL A . n 
B 1 214 LEU 214 214 214 LEU LEU A . n 
B 1 215 LYS 215 215 215 LYS LYS A . n 
B 1 216 GLN 216 216 216 GLN GLN A . n 
B 1 217 PRO 217 217 217 PRO PRO A . n 
B 1 218 ILE 218 218 218 ILE ILE A . n 
B 1 219 ASN 219 219 219 ASN ASN A . n 
B 1 220 ILE 220 220 220 ILE ILE A . n 
B 1 221 SER 221 221 221 SER SER A . n 
B 1 222 SER 222 222 222 SER SER A . n 
B 1 223 GLN 223 223 223 GLN GLN A . n 
B 1 224 GLN 224 224 224 GLN GLN A . n 
B 1 225 LEU 225 225 225 LEU LEU A . n 
B 1 226 ALA 226 226 226 ALA ALA A . n 
B 1 227 LYS 227 227 227 LYS LYS A . n 
B 1 228 PHE 228 228 228 PHE PHE A . n 
B 1 229 ARG 229 229 229 ARG ARG A . n 
B 1 230 SER 230 230 230 SER SER A . n 
B 1 231 LEU 231 231 231 LEU LEU A . n 
B 1 232 LEU 232 232 232 LEU LEU A . n 
B 1 233 CYS 233 233 233 CYS CYS A . n 
B 1 234 THR 234 234 234 THR THR A . n 
B 1 235 ALA 235 235 235 ALA ALA A . n 
B 1 236 GLU 236 236 236 GLU GLU A . n 
B 1 237 GLY 237 237 237 GLY GLY A . n 
B 1 238 GLU 238 238 238 GLU GLU A . n 
B 1 239 ALA 239 239 239 ALA ALA A . n 
B 1 240 ALA 240 240 240 ALA ALA A . n 
B 1 241 ALA 241 241 241 ALA ALA A . n 
B 1 242 PHE 242 242 242 PHE PHE A . n 
B 1 243 LEU 243 243 243 LEU LEU A . n 
B 1 244 VAL 244 244 244 VAL VAL A . n 
B 1 245 SER 245 245 245 SER SER A . n 
B 1 246 ASN 246 246 246 ASN ASN A . n 
B 1 247 HIS 247 247 247 HIS HIS A . n 
B 1 248 ARG 248 248 248 ARG ARG A . n 
B 1 249 PRO 249 249 249 PRO PRO A . n 
B 1 250 PRO 250 250 250 PRO PRO A . n 
B 1 251 GLN 251 251 251 GLN GLN A . n 
B 1 252 PRO 252 252 252 PRO PRO A . n 
B 1 253 LEU 253 253 253 LEU LEU A . n 
B 1 254 LYS 254 254 254 LYS LYS A . n 
B 1 255 GLY 255 255 255 GLY GLY A . n 
B 1 256 ARG 256 256 256 ARG ARG A . n 
B 1 257 LYS 257 257 257 LYS LYS A . n 
B 1 258 VAL 258 258 258 VAL VAL A . n 
B 1 259 ARG 259 259 259 ARG ARG A . n 
B 1 260 ALA 260 260 260 ALA ALA A . n 
B 1 261 SER 261 261 261 SER SER A . n 
B 1 262 PHE 262 262 262 PHE PHE A . n 
B 1 263 HIS 263 263 263 HIS HIS 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 
C 2 ZN  1   301 1   ZN  ZN  B . 
D 3 ENN 1   302 1   ENN EA1 B . 
E 4 EDO 1   303 1   EDO EDO B . 
F 4 EDO 1   304 3   EDO EDO B . 
G 2 ZN  1   301 2   ZN  ZN  A . 
H 3 ENN 1   302 2   ENN EA1 A . 
I 4 EDO 1   303 2   EDO EDO A . 
J 5 CIT 1   304 4   CIT CIT A . 
K 6 HOH 1   401 560 HOH HOH B . 
K 6 HOH 2   402 182 HOH HOH B . 
K 6 HOH 3   403 533 HOH HOH B . 
K 6 HOH 4   404 398 HOH HOH B . 
K 6 HOH 5   405 505 HOH HOH B . 
K 6 HOH 6   406 335 HOH HOH B . 
K 6 HOH 7   407 520 HOH HOH B . 
K 6 HOH 8   408 426 HOH HOH B . 
K 6 HOH 9   409 104 HOH HOH B . 
K 6 HOH 10  410 220 HOH HOH B . 
K 6 HOH 11  411 523 HOH HOH B . 
K 6 HOH 12  412 194 HOH HOH B . 
K 6 HOH 13  413 215 HOH HOH B . 
K 6 HOH 14  414 149 HOH HOH B . 
K 6 HOH 15  415 405 HOH HOH B . 
K 6 HOH 16  416 198 HOH HOH B . 
K 6 HOH 17  417 437 HOH HOH B . 
K 6 HOH 18  418 588 HOH HOH B . 
K 6 HOH 19  419 163 HOH HOH B . 
K 6 HOH 20  420 29  HOH HOH B . 
K 6 HOH 21  421 515 HOH HOH B . 
K 6 HOH 22  422 108 HOH HOH B . 
K 6 HOH 23  423 261 HOH HOH B . 
K 6 HOH 24  424 236 HOH HOH B . 
K 6 HOH 25  425 138 HOH HOH B . 
K 6 HOH 26  426 296 HOH HOH B . 
K 6 HOH 27  427 190 HOH HOH B . 
K 6 HOH 28  428 252 HOH HOH B . 
K 6 HOH 29  429 10  HOH HOH B . 
K 6 HOH 30  430 175 HOH HOH B . 
K 6 HOH 31  431 31  HOH HOH B . 
K 6 HOH 32  432 92  HOH HOH B . 
K 6 HOH 33  433 176 HOH HOH B . 
K 6 HOH 34  434 156 HOH HOH B . 
K 6 HOH 35  435 269 HOH HOH B . 
K 6 HOH 36  436 197 HOH HOH B . 
K 6 HOH 37  437 494 HOH HOH B . 
K 6 HOH 38  438 307 HOH HOH B . 
K 6 HOH 39  439 391 HOH HOH B . 
K 6 HOH 40  440 237 HOH HOH B . 
K 6 HOH 41  441 302 HOH HOH B . 
K 6 HOH 42  442 584 HOH HOH B . 
K 6 HOH 43  443 48  HOH HOH B . 
K 6 HOH 44  444 187 HOH HOH B . 
K 6 HOH 45  445 212 HOH HOH B . 
K 6 HOH 46  446 109 HOH HOH B . 
K 6 HOH 47  447 517 HOH HOH B . 
K 6 HOH 48  448 430 HOH HOH B . 
K 6 HOH 49  449 35  HOH HOH B . 
K 6 HOH 50  450 385 HOH HOH B . 
K 6 HOH 51  451 27  HOH HOH B . 
K 6 HOH 52  452 150 HOH HOH B . 
K 6 HOH 53  453 462 HOH HOH B . 
K 6 HOH 54  454 392 HOH HOH B . 
K 6 HOH 55  455 383 HOH HOH B . 
K 6 HOH 56  456 134 HOH HOH B . 
K 6 HOH 57  457 412 HOH HOH B . 
K 6 HOH 58  458 172 HOH HOH B . 
K 6 HOH 59  459 233 HOH HOH B . 
K 6 HOH 60  460 8   HOH HOH B . 
K 6 HOH 61  461 280 HOH HOH B . 
K 6 HOH 62  462 173 HOH HOH B . 
K 6 HOH 63  463 410 HOH HOH B . 
K 6 HOH 64  464 50  HOH HOH B . 
K 6 HOH 65  465 455 HOH HOH B . 
K 6 HOH 66  466 122 HOH HOH B . 
K 6 HOH 67  467 229 HOH HOH B . 
K 6 HOH 68  468 79  HOH HOH B . 
K 6 HOH 69  469 51  HOH HOH B . 
K 6 HOH 70  470 84  HOH HOH B . 
K 6 HOH 71  471 257 HOH HOH B . 
K 6 HOH 72  472 424 HOH HOH B . 
K 6 HOH 73  473 476 HOH HOH B . 
K 6 HOH 74  474 102 HOH HOH B . 
K 6 HOH 75  475 152 HOH HOH B . 
K 6 HOH 76  476 486 HOH HOH B . 
K 6 HOH 77  477 221 HOH HOH B . 
K 6 HOH 78  478 432 HOH HOH B . 
K 6 HOH 79  479 433 HOH HOH B . 
K 6 HOH 80  480 105 HOH HOH B . 
K 6 HOH 81  481 528 HOH HOH B . 
K 6 HOH 82  482 56  HOH HOH B . 
K 6 HOH 83  483 166 HOH HOH B . 
K 6 HOH 84  484 179 HOH HOH B . 
K 6 HOH 85  485 127 HOH HOH B . 
K 6 HOH 86  486 20  HOH HOH B . 
K 6 HOH 87  487 436 HOH HOH B . 
K 6 HOH 88  488 26  HOH HOH B . 
K 6 HOH 89  489 396 HOH HOH B . 
K 6 HOH 90  490 530 HOH HOH B . 
K 6 HOH 91  491 546 HOH HOH B . 
K 6 HOH 92  492 7   HOH HOH B . 
K 6 HOH 93  493 136 HOH HOH B . 
K 6 HOH 94  494 110 HOH HOH B . 
K 6 HOH 95  495 239 HOH HOH B . 
K 6 HOH 96  496 375 HOH HOH B . 
K 6 HOH 97  497 331 HOH HOH B . 
K 6 HOH 98  498 151 HOH HOH B . 
K 6 HOH 99  499 566 HOH HOH B . 
K 6 HOH 100 500 525 HOH HOH B . 
K 6 HOH 101 501 595 HOH HOH B . 
K 6 HOH 102 502 115 HOH HOH B . 
K 6 HOH 103 503 381 HOH HOH B . 
K 6 HOH 104 504 9   HOH HOH B . 
K 6 HOH 105 505 274 HOH HOH B . 
K 6 HOH 106 506 64  HOH HOH B . 
K 6 HOH 107 507 374 HOH HOH B . 
K 6 HOH 108 508 318 HOH HOH B . 
K 6 HOH 109 509 63  HOH HOH B . 
K 6 HOH 110 510 579 HOH HOH B . 
K 6 HOH 111 511 62  HOH HOH B . 
K 6 HOH 112 512 278 HOH HOH B . 
K 6 HOH 113 513 14  HOH HOH B . 
K 6 HOH 114 514 408 HOH HOH B . 
K 6 HOH 115 515 2   HOH HOH B . 
K 6 HOH 116 516 6   HOH HOH B . 
K 6 HOH 117 517 1   HOH HOH B . 
K 6 HOH 118 518 44  HOH HOH B . 
K 6 HOH 119 519 38  HOH HOH B . 
K 6 HOH 120 520 119 HOH HOH B . 
K 6 HOH 121 521 86  HOH HOH B . 
K 6 HOH 122 522 53  HOH HOH B . 
K 6 HOH 123 523 147 HOH HOH B . 
K 6 HOH 124 524 132 HOH HOH B . 
K 6 HOH 125 525 559 HOH HOH B . 
K 6 HOH 126 526 57  HOH HOH B . 
K 6 HOH 127 527 376 HOH HOH B . 
K 6 HOH 128 528 406 HOH HOH B . 
K 6 HOH 129 529 161 HOH HOH B . 
K 6 HOH 130 530 67  HOH HOH B . 
K 6 HOH 131 531 536 HOH HOH B . 
K 6 HOH 132 532 37  HOH HOH B . 
K 6 HOH 133 533 591 HOH HOH B . 
K 6 HOH 134 534 567 HOH HOH B . 
K 6 HOH 135 535 279 HOH HOH B . 
K 6 HOH 136 536 224 HOH HOH B . 
K 6 HOH 137 537 429 HOH HOH B . 
K 6 HOH 138 538 378 HOH HOH B . 
K 6 HOH 139 539 504 HOH HOH B . 
K 6 HOH 140 540 513 HOH HOH B . 
K 6 HOH 141 541 159 HOH HOH B . 
K 6 HOH 142 542 98  HOH HOH B . 
K 6 HOH 143 543 605 HOH HOH B . 
K 6 HOH 144 544 589 HOH HOH B . 
K 6 HOH 145 545 223 HOH HOH B . 
K 6 HOH 146 546 158 HOH HOH B . 
K 6 HOH 147 547 321 HOH HOH B . 
K 6 HOH 148 548 181 HOH HOH B . 
K 6 HOH 149 549 205 HOH HOH B . 
K 6 HOH 150 550 88  HOH HOH B . 
K 6 HOH 151 551 47  HOH HOH B . 
K 6 HOH 152 552 30  HOH HOH B . 
K 6 HOH 153 553 457 HOH HOH B . 
K 6 HOH 154 554 362 HOH HOH B . 
K 6 HOH 155 555 325 HOH HOH B . 
K 6 HOH 156 556 128 HOH HOH B . 
K 6 HOH 157 557 34  HOH HOH B . 
K 6 HOH 158 558 49  HOH HOH B . 
K 6 HOH 159 559 490 HOH HOH B . 
K 6 HOH 160 560 78  HOH HOH B . 
K 6 HOH 161 561 114 HOH HOH B . 
K 6 HOH 162 562 113 HOH HOH B . 
K 6 HOH 163 563 55  HOH HOH B . 
K 6 HOH 164 564 185 HOH HOH B . 
K 6 HOH 165 565 87  HOH HOH B . 
K 6 HOH 166 566 106 HOH HOH B . 
K 6 HOH 167 567 304 HOH HOH B . 
K 6 HOH 168 568 282 HOH HOH B . 
K 6 HOH 169 569 404 HOH HOH B . 
K 6 HOH 170 570 518 HOH HOH B . 
K 6 HOH 171 571 129 HOH HOH B . 
K 6 HOH 172 572 93  HOH HOH B . 
K 6 HOH 173 573 563 HOH HOH B . 
K 6 HOH 174 574 254 HOH HOH B . 
K 6 HOH 175 575 290 HOH HOH B . 
K 6 HOH 176 576 133 HOH HOH B . 
K 6 HOH 177 577 101 HOH HOH B . 
K 6 HOH 178 578 501 HOH HOH B . 
K 6 HOH 179 579 431 HOH HOH B . 
K 6 HOH 180 580 496 HOH HOH B . 
K 6 HOH 181 581 350 HOH HOH B . 
K 6 HOH 182 582 507 HOH HOH B . 
K 6 HOH 183 583 386 HOH HOH B . 
K 6 HOH 184 584 367 HOH HOH B . 
K 6 HOH 185 585 16  HOH HOH B . 
K 6 HOH 186 586 581 HOH HOH B . 
K 6 HOH 187 587 208 HOH HOH B . 
K 6 HOH 188 588 143 HOH HOH B . 
K 6 HOH 189 589 497 HOH HOH B . 
K 6 HOH 190 590 204 HOH HOH B . 
K 6 HOH 191 591 209 HOH HOH B . 
K 6 HOH 192 592 135 HOH HOH B . 
K 6 HOH 193 593 594 HOH HOH B . 
K 6 HOH 194 594 112 HOH HOH B . 
K 6 HOH 195 595 117 HOH HOH B . 
K 6 HOH 196 596 72  HOH HOH B . 
K 6 HOH 197 597 370 HOH HOH B . 
K 6 HOH 198 598 298 HOH HOH B . 
K 6 HOH 199 599 522 HOH HOH B . 
K 6 HOH 200 600 40  HOH HOH B . 
K 6 HOH 201 601 311 HOH HOH B . 
K 6 HOH 202 602 439 HOH HOH B . 
K 6 HOH 203 603 388 HOH HOH B . 
K 6 HOH 204 604 345 HOH HOH B . 
K 6 HOH 205 605 356 HOH HOH B . 
K 6 HOH 206 606 541 HOH HOH B . 
K 6 HOH 207 607 592 HOH HOH B . 
K 6 HOH 208 608 305 HOH HOH B . 
K 6 HOH 209 609 116 HOH HOH B . 
K 6 HOH 210 610 414 HOH HOH B . 
K 6 HOH 211 611 144 HOH HOH B . 
K 6 HOH 212 612 214 HOH HOH B . 
K 6 HOH 213 613 509 HOH HOH B . 
K 6 HOH 214 614 303 HOH HOH B . 
K 6 HOH 215 615 569 HOH HOH B . 
K 6 HOH 216 616 425 HOH HOH B . 
K 6 HOH 217 617 498 HOH HOH B . 
K 6 HOH 218 618 13  HOH HOH B . 
K 6 HOH 219 619 484 HOH HOH B . 
K 6 HOH 220 620 503 HOH HOH B . 
K 6 HOH 221 621 438 HOH HOH B . 
K 6 HOH 222 622 285 HOH HOH B . 
K 6 HOH 223 623 394 HOH HOH B . 
K 6 HOH 224 624 344 HOH HOH B . 
K 6 HOH 225 625 558 HOH HOH B . 
K 6 HOH 226 626 230 HOH HOH B . 
K 6 HOH 227 627 200 HOH HOH B . 
K 6 HOH 228 628 322 HOH HOH B . 
K 6 HOH 229 629 413 HOH HOH B . 
K 6 HOH 230 630 337 HOH HOH B . 
K 6 HOH 231 631 519 HOH HOH B . 
K 6 HOH 232 632 222 HOH HOH B . 
K 6 HOH 233 633 602 HOH HOH B . 
K 6 HOH 234 634 491 HOH HOH B . 
K 6 HOH 235 635 527 HOH HOH B . 
K 6 HOH 236 636 300 HOH HOH B . 
K 6 HOH 237 637 500 HOH HOH B . 
K 6 HOH 238 638 511 HOH HOH B . 
K 6 HOH 239 639 586 HOH HOH B . 
K 6 HOH 240 640 461 HOH HOH B . 
K 6 HOH 241 641 373 HOH HOH B . 
K 6 HOH 242 642 245 HOH HOH B . 
K 6 HOH 243 643 130 HOH HOH B . 
K 6 HOH 244 644 308 HOH HOH B . 
K 6 HOH 245 645 485 HOH HOH B . 
K 6 HOH 246 646 502 HOH HOH B . 
K 6 HOH 247 647 435 HOH HOH B . 
K 6 HOH 248 648 607 HOH HOH B . 
K 6 HOH 249 649 139 HOH HOH B . 
K 6 HOH 250 650 320 HOH HOH B . 
K 6 HOH 251 651 227 HOH HOH B . 
K 6 HOH 252 652 228 HOH HOH B . 
K 6 HOH 253 653 521 HOH HOH B . 
K 6 HOH 254 654 266 HOH HOH B . 
K 6 HOH 255 655 168 HOH HOH B . 
K 6 HOH 256 656 422 HOH HOH B . 
K 6 HOH 257 657 315 HOH HOH B . 
K 6 HOH 258 658 510 HOH HOH B . 
K 6 HOH 259 659 372 HOH HOH B . 
K 6 HOH 260 660 534 HOH HOH B . 
K 6 HOH 261 661 95  HOH HOH B . 
K 6 HOH 262 662 409 HOH HOH B . 
K 6 HOH 263 663 516 HOH HOH B . 
K 6 HOH 264 664 465 HOH HOH B . 
K 6 HOH 265 665 188 HOH HOH B . 
K 6 HOH 266 666 364 HOH HOH B . 
K 6 HOH 267 667 580 HOH HOH B . 
K 6 HOH 268 668 464 HOH HOH B . 
K 6 HOH 269 669 231 HOH HOH B . 
K 6 HOH 270 670 203 HOH HOH B . 
K 6 HOH 271 671 474 HOH HOH B . 
K 6 HOH 272 672 171 HOH HOH B . 
K 6 HOH 273 673 120 HOH HOH B . 
K 6 HOH 274 674 351 HOH HOH B . 
K 6 HOH 275 675 440 HOH HOH B . 
K 6 HOH 276 676 526 HOH HOH B . 
K 6 HOH 277 677 219 HOH HOH B . 
K 6 HOH 278 678 118 HOH HOH B . 
K 6 HOH 279 679 247 HOH HOH B . 
K 6 HOH 280 680 548 HOH HOH B . 
K 6 HOH 281 681 508 HOH HOH B . 
K 6 HOH 282 682 599 HOH HOH B . 
K 6 HOH 283 683 585 HOH HOH B . 
K 6 HOH 284 684 568 HOH HOH B . 
K 6 HOH 285 685 499 HOH HOH B . 
K 6 HOH 286 686 434 HOH HOH B . 
K 6 HOH 287 687 495 HOH HOH B . 
K 6 HOH 288 688 597 HOH HOH B . 
K 6 HOH 289 689 483 HOH HOH B . 
K 6 HOH 290 690 539 HOH HOH B . 
K 6 HOH 291 691 590 HOH HOH B . 
K 6 HOH 292 692 358 HOH HOH B . 
K 6 HOH 293 693 565 HOH HOH B . 
K 6 HOH 294 694 379 HOH HOH B . 
K 6 HOH 295 695 512 HOH HOH B . 
K 6 HOH 296 696 524 HOH HOH B . 
K 6 HOH 297 697 543 HOH HOH B . 
K 6 HOH 298 698 456 HOH HOH B . 
K 6 HOH 299 699 529 HOH HOH B . 
K 6 HOH 300 700 596 HOH HOH B . 
K 6 HOH 301 701 467 HOH HOH B . 
K 6 HOH 302 702 167 HOH HOH B . 
K 6 HOH 303 703 535 HOH HOH B . 
K 6 HOH 304 704 538 HOH HOH B . 
K 6 HOH 305 705 544 HOH HOH B . 
K 6 HOH 306 706 545 HOH HOH B . 
K 6 HOH 307 707 542 HOH HOH B . 
L 6 HOH 1   401 338 HOH HOH A . 
L 6 HOH 2   402 294 HOH HOH A . 
L 6 HOH 3   403 551 HOH HOH A . 
L 6 HOH 4   404 445 HOH HOH A . 
L 6 HOH 5   405 537 HOH HOH A . 
L 6 HOH 6   406 475 HOH HOH A . 
L 6 HOH 7   407 193 HOH HOH A . 
L 6 HOH 8   408 587 HOH HOH A . 
L 6 HOH 9   409 395 HOH HOH A . 
L 6 HOH 10  410 407 HOH HOH A . 
L 6 HOH 11  411 380 HOH HOH A . 
L 6 HOH 12  412 487 HOH HOH A . 
L 6 HOH 13  413 458 HOH HOH A . 
L 6 HOH 14  414 561 HOH HOH A . 
L 6 HOH 15  415 564 HOH HOH A . 
L 6 HOH 16  416 449 HOH HOH A . 
L 6 HOH 17  417 319 HOH HOH A . 
L 6 HOH 18  418 463 HOH HOH A . 
L 6 HOH 19  419 295 HOH HOH A . 
L 6 HOH 20  420 18  HOH HOH A . 
L 6 HOH 21  421 255 HOH HOH A . 
L 6 HOH 22  422 401 HOH HOH A . 
L 6 HOH 23  423 572 HOH HOH A . 
L 6 HOH 24  424 417 HOH HOH A . 
L 6 HOH 25  425 226 HOH HOH A . 
L 6 HOH 26  426 17  HOH HOH A . 
L 6 HOH 27  427 482 HOH HOH A . 
L 6 HOH 28  428 39  HOH HOH A . 
L 6 HOH 29  429 207 HOH HOH A . 
L 6 HOH 30  430 137 HOH HOH A . 
L 6 HOH 31  431 241 HOH HOH A . 
L 6 HOH 32  432 604 HOH HOH A . 
L 6 HOH 33  433 146 HOH HOH A . 
L 6 HOH 34  434 420 HOH HOH A . 
L 6 HOH 35  435 419 HOH HOH A . 
L 6 HOH 36  436 256 HOH HOH A . 
L 6 HOH 37  437 58  HOH HOH A . 
L 6 HOH 38  438 66  HOH HOH A . 
L 6 HOH 39  439 250 HOH HOH A . 
L 6 HOH 40  440 165 HOH HOH A . 
L 6 HOH 41  441 348 HOH HOH A . 
L 6 HOH 42  442 576 HOH HOH A . 
L 6 HOH 43  443 240 HOH HOH A . 
L 6 HOH 44  444 234 HOH HOH A . 
L 6 HOH 45  445 191 HOH HOH A . 
L 6 HOH 46  446 155 HOH HOH A . 
L 6 HOH 47  447 343 HOH HOH A . 
L 6 HOH 48  448 316 HOH HOH A . 
L 6 HOH 49  449 46  HOH HOH A . 
L 6 HOH 50  450 277 HOH HOH A . 
L 6 HOH 51  451 33  HOH HOH A . 
L 6 HOH 52  452 411 HOH HOH A . 
L 6 HOH 53  453 363 HOH HOH A . 
L 6 HOH 54  454 28  HOH HOH A . 
L 6 HOH 55  455 131 HOH HOH A . 
L 6 HOH 56  456 281 HOH HOH A . 
L 6 HOH 57  457 332 HOH HOH A . 
L 6 HOH 58  458 74  HOH HOH A . 
L 6 HOH 59  459 472 HOH HOH A . 
L 6 HOH 60  460 249 HOH HOH A . 
L 6 HOH 61  461 244 HOH HOH A . 
L 6 HOH 62  462 154 HOH HOH A . 
L 6 HOH 63  463 11  HOH HOH A . 
L 6 HOH 64  464 80  HOH HOH A . 
L 6 HOH 65  465 52  HOH HOH A . 
L 6 HOH 66  466 100 HOH HOH A . 
L 6 HOH 67  467 90  HOH HOH A . 
L 6 HOH 68  468 15  HOH HOH A . 
L 6 HOH 69  469 480 HOH HOH A . 
L 6 HOH 70  470 283 HOH HOH A . 
L 6 HOH 71  471 24  HOH HOH A . 
L 6 HOH 72  472 323 HOH HOH A . 
L 6 HOH 73  473 5   HOH HOH A . 
L 6 HOH 74  474 183 HOH HOH A . 
L 6 HOH 75  475 330 HOH HOH A . 
L 6 HOH 76  476 189 HOH HOH A . 
L 6 HOH 77  477 286 HOH HOH A . 
L 6 HOH 78  478 471 HOH HOH A . 
L 6 HOH 79  479 70  HOH HOH A . 
L 6 HOH 80  480 213 HOH HOH A . 
L 6 HOH 81  481 85  HOH HOH A . 
L 6 HOH 82  482 126 HOH HOH A . 
L 6 HOH 83  483 103 HOH HOH A . 
L 6 HOH 84  484 312 HOH HOH A . 
L 6 HOH 85  485 186 HOH HOH A . 
L 6 HOH 86  486 61  HOH HOH A . 
L 6 HOH 87  487 23  HOH HOH A . 
L 6 HOH 88  488 333 HOH HOH A . 
L 6 HOH 89  489 54  HOH HOH A . 
L 6 HOH 90  490 96  HOH HOH A . 
L 6 HOH 91  491 377 HOH HOH A . 
L 6 HOH 92  492 22  HOH HOH A . 
L 6 HOH 93  493 141 HOH HOH A . 
L 6 HOH 94  494 4   HOH HOH A . 
L 6 HOH 95  495 195 HOH HOH A . 
L 6 HOH 96  496 340 HOH HOH A . 
L 6 HOH 97  497 444 HOH HOH A . 
L 6 HOH 98  498 469 HOH HOH A . 
L 6 HOH 99  499 275 HOH HOH A . 
L 6 HOH 100 500 142 HOH HOH A . 
L 6 HOH 101 501 145 HOH HOH A . 
L 6 HOH 102 502 327 HOH HOH A . 
L 6 HOH 103 503 210 HOH HOH A . 
L 6 HOH 104 504 45  HOH HOH A . 
L 6 HOH 105 505 41  HOH HOH A . 
L 6 HOH 106 506 368 HOH HOH A . 
L 6 HOH 107 507 232 HOH HOH A . 
L 6 HOH 108 508 42  HOH HOH A . 
L 6 HOH 109 509 448 HOH HOH A . 
L 6 HOH 110 510 447 HOH HOH A . 
L 6 HOH 111 511 32  HOH HOH A . 
L 6 HOH 112 512 326 HOH HOH A . 
L 6 HOH 113 513 248 HOH HOH A . 
L 6 HOH 114 514 276 HOH HOH A . 
L 6 HOH 115 515 206 HOH HOH A . 
L 6 HOH 116 516 82  HOH HOH A . 
L 6 HOH 117 517 97  HOH HOH A . 
L 6 HOH 118 518 329 HOH HOH A . 
L 6 HOH 119 519 314 HOH HOH A . 
L 6 HOH 120 520 89  HOH HOH A . 
L 6 HOH 121 521 91  HOH HOH A . 
L 6 HOH 122 522 479 HOH HOH A . 
L 6 HOH 123 523 297 HOH HOH A . 
L 6 HOH 124 524 306 HOH HOH A . 
L 6 HOH 125 525 238 HOH HOH A . 
L 6 HOH 126 526 71  HOH HOH A . 
L 6 HOH 127 527 36  HOH HOH A . 
L 6 HOH 128 528 123 HOH HOH A . 
L 6 HOH 129 529 3   HOH HOH A . 
L 6 HOH 130 530 477 HOH HOH A . 
L 6 HOH 131 531 201 HOH HOH A . 
L 6 HOH 132 532 148 HOH HOH A . 
L 6 HOH 133 533 313 HOH HOH A . 
L 6 HOH 134 534 73  HOH HOH A . 
L 6 HOH 135 535 301 HOH HOH A . 
L 6 HOH 136 536 180 HOH HOH A . 
L 6 HOH 137 537 259 HOH HOH A . 
L 6 HOH 138 538 235 HOH HOH A . 
L 6 HOH 139 539 601 HOH HOH A . 
L 6 HOH 140 540 125 HOH HOH A . 
L 6 HOH 141 541 470 HOH HOH A . 
L 6 HOH 142 542 446 HOH HOH A . 
L 6 HOH 143 543 99  HOH HOH A . 
L 6 HOH 144 544 353 HOH HOH A . 
L 6 HOH 145 545 160 HOH HOH A . 
L 6 HOH 146 546 124 HOH HOH A . 
L 6 HOH 147 547 354 HOH HOH A . 
L 6 HOH 148 548 242 HOH HOH A . 
L 6 HOH 149 549 531 HOH HOH A . 
L 6 HOH 150 550 76  HOH HOH A . 
L 6 HOH 151 551 202 HOH HOH A . 
L 6 HOH 152 552 75  HOH HOH A . 
L 6 HOH 153 553 68  HOH HOH A . 
L 6 HOH 154 554 287 HOH HOH A . 
L 6 HOH 155 555 393 HOH HOH A . 
L 6 HOH 156 556 153 HOH HOH A . 
L 6 HOH 157 557 81  HOH HOH A . 
L 6 HOH 158 558 218 HOH HOH A . 
L 6 HOH 159 559 12  HOH HOH A . 
L 6 HOH 160 560 593 HOH HOH A . 
L 6 HOH 161 561 289 HOH HOH A . 
L 6 HOH 162 562 270 HOH HOH A . 
L 6 HOH 163 563 603 HOH HOH A . 
L 6 HOH 164 564 169 HOH HOH A . 
L 6 HOH 165 565 77  HOH HOH A . 
L 6 HOH 166 566 246 HOH HOH A . 
L 6 HOH 167 567 121 HOH HOH A . 
L 6 HOH 168 568 192 HOH HOH A . 
L 6 HOH 169 569 273 HOH HOH A . 
L 6 HOH 170 570 225 HOH HOH A . 
L 6 HOH 171 571 310 HOH HOH A . 
L 6 HOH 172 572 258 HOH HOH A . 
L 6 HOH 173 573 140 HOH HOH A . 
L 6 HOH 174 574 583 HOH HOH A . 
L 6 HOH 175 575 577 HOH HOH A . 
L 6 HOH 176 576 293 HOH HOH A . 
L 6 HOH 177 577 578 HOH HOH A . 
L 6 HOH 178 578 415 HOH HOH A . 
L 6 HOH 179 579 217 HOH HOH A . 
L 6 HOH 180 580 268 HOH HOH A . 
L 6 HOH 181 581 452 HOH HOH A . 
L 6 HOH 182 582 346 HOH HOH A . 
L 6 HOH 183 583 284 HOH HOH A . 
L 6 HOH 184 584 25  HOH HOH A . 
L 6 HOH 185 585 341 HOH HOH A . 
L 6 HOH 186 586 427 HOH HOH A . 
L 6 HOH 187 587 65  HOH HOH A . 
L 6 HOH 188 588 60  HOH HOH A . 
L 6 HOH 189 589 288 HOH HOH A . 
L 6 HOH 190 590 69  HOH HOH A . 
L 6 HOH 191 591 574 HOH HOH A . 
L 6 HOH 192 592 43  HOH HOH A . 
L 6 HOH 193 593 21  HOH HOH A . 
L 6 HOH 194 594 454 HOH HOH A . 
L 6 HOH 195 595 428 HOH HOH A . 
L 6 HOH 196 596 83  HOH HOH A . 
L 6 HOH 197 597 342 HOH HOH A . 
L 6 HOH 198 598 339 HOH HOH A . 
L 6 HOH 199 599 309 HOH HOH A . 
L 6 HOH 200 600 389 HOH HOH A . 
L 6 HOH 201 601 387 HOH HOH A . 
L 6 HOH 202 602 251 HOH HOH A . 
L 6 HOH 203 603 442 HOH HOH A . 
L 6 HOH 204 604 492 HOH HOH A . 
L 6 HOH 205 605 555 HOH HOH A . 
L 6 HOH 206 606 556 HOH HOH A . 
L 6 HOH 207 607 553 HOH HOH A . 
L 6 HOH 208 608 355 HOH HOH A . 
L 6 HOH 209 609 443 HOH HOH A . 
L 6 HOH 210 610 267 HOH HOH A . 
L 6 HOH 211 611 196 HOH HOH A . 
L 6 HOH 212 612 253 HOH HOH A . 
L 6 HOH 213 613 170 HOH HOH A . 
L 6 HOH 214 614 59  HOH HOH A . 
L 6 HOH 215 615 357 HOH HOH A . 
L 6 HOH 216 616 570 HOH HOH A . 
L 6 HOH 217 617 299 HOH HOH A . 
L 6 HOH 218 618 550 HOH HOH A . 
L 6 HOH 219 619 243 HOH HOH A . 
L 6 HOH 220 620 481 HOH HOH A . 
L 6 HOH 221 621 557 HOH HOH A . 
L 6 HOH 222 622 94  HOH HOH A . 
L 6 HOH 223 623 554 HOH HOH A . 
L 6 HOH 224 624 317 HOH HOH A . 
L 6 HOH 225 625 450 HOH HOH A . 
L 6 HOH 226 626 336 HOH HOH A . 
L 6 HOH 227 627 369 HOH HOH A . 
L 6 HOH 228 628 111 HOH HOH A . 
L 6 HOH 229 629 174 HOH HOH A . 
L 6 HOH 230 630 216 HOH HOH A . 
L 6 HOH 231 631 19  HOH HOH A . 
L 6 HOH 232 632 600 HOH HOH A . 
L 6 HOH 233 633 441 HOH HOH A . 
L 6 HOH 234 634 382 HOH HOH A . 
L 6 HOH 235 635 582 HOH HOH A . 
L 6 HOH 236 636 162 HOH HOH A . 
L 6 HOH 237 637 328 HOH HOH A . 
L 6 HOH 238 638 291 HOH HOH A . 
L 6 HOH 239 639 366 HOH HOH A . 
L 6 HOH 240 640 473 HOH HOH A . 
L 6 HOH 241 641 107 HOH HOH A . 
L 6 HOH 242 642 365 HOH HOH A . 
L 6 HOH 243 643 177 HOH HOH A . 
L 6 HOH 244 644 552 HOH HOH A . 
L 6 HOH 245 645 549 HOH HOH A . 
L 6 HOH 246 646 272 HOH HOH A . 
L 6 HOH 247 647 184 HOH HOH A . 
L 6 HOH 248 648 359 HOH HOH A . 
L 6 HOH 249 649 265 HOH HOH A . 
L 6 HOH 250 650 506 HOH HOH A . 
L 6 HOH 251 651 571 HOH HOH A . 
L 6 HOH 252 652 178 HOH HOH A . 
L 6 HOH 253 653 547 HOH HOH A . 
L 6 HOH 254 654 403 HOH HOH A . 
L 6 HOH 255 655 532 HOH HOH A . 
L 6 HOH 256 656 371 HOH HOH A . 
L 6 HOH 257 657 514 HOH HOH A . 
L 6 HOH 258 658 397 HOH HOH A . 
L 6 HOH 259 659 199 HOH HOH A . 
L 6 HOH 260 660 598 HOH HOH A . 
L 6 HOH 261 661 451 HOH HOH A . 
L 6 HOH 262 662 262 HOH HOH A . 
L 6 HOH 263 663 468 HOH HOH A . 
L 6 HOH 264 664 157 HOH HOH A . 
L 6 HOH 265 665 263 HOH HOH A . 
L 6 HOH 266 666 575 HOH HOH A . 
L 6 HOH 267 667 264 HOH HOH A . 
L 6 HOH 268 668 292 HOH HOH A . 
L 6 HOH 269 669 418 HOH HOH A . 
L 6 HOH 270 670 352 HOH HOH A . 
L 6 HOH 271 671 573 HOH HOH A . 
L 6 HOH 272 672 361 HOH HOH A . 
L 6 HOH 273 673 390 HOH HOH A . 
L 6 HOH 274 674 421 HOH HOH A . 
L 6 HOH 275 675 478 HOH HOH A . 
L 6 HOH 276 676 349 HOH HOH A . 
L 6 HOH 277 677 562 HOH HOH A . 
L 6 HOH 278 678 399 HOH HOH A . 
L 6 HOH 279 679 324 HOH HOH A . 
L 6 HOH 280 680 606 HOH HOH A . 
L 6 HOH 281 681 453 HOH HOH A . 
L 6 HOH 282 682 211 HOH HOH A . 
L 6 HOH 283 683 384 HOH HOH A . 
L 6 HOH 284 684 459 HOH HOH A . 
L 6 HOH 285 685 400 HOH HOH A . 
L 6 HOH 286 686 493 HOH HOH A . 
L 6 HOH 287 687 402 HOH HOH A . 
L 6 HOH 288 688 423 HOH HOH A . 
L 6 HOH 289 689 164 HOH HOH A . 
L 6 HOH 290 690 360 HOH HOH A . 
L 6 HOH 291 691 416 HOH HOH A . 
L 6 HOH 292 692 347 HOH HOH A . 
L 6 HOH 293 693 540 HOH HOH A . 
L 6 HOH 294 694 489 HOH HOH A . 
L 6 HOH 295 695 488 HOH HOH A . 
L 6 HOH 296 696 271 HOH HOH A . 
L 6 HOH 297 697 260 HOH HOH A . 
L 6 HOH 298 698 460 HOH HOH A . 
L 6 HOH 299 699 334 HOH HOH A . 
L 6 HOH 300 700 466 HOH HOH A . 
# 
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 reduction'  ? ? ? ? ? ? ? ? ? ? ? MOSFLM      ? ? ? .      2 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? SCALA       ? ? ? 3.3.20 3 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.10   4 
? 'model building'  ? ? ? ? ? ? ? ? ? ? ? Coot        ? ? ? .      5 
? phasing           ? ? ? ? ? ? ? ? ? ? ? MOLREP      ? ? ? .      6 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     6G5U 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     55.790 
_cell.length_a_esd                 ? 
_cell.length_b                     58.305 
_cell.length_b_esd                 ? 
_cell.length_c                     160.754 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_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                         6G5U 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_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                   6G5U 
_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            2.22 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         44.2 
_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              5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp            291 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;Crystallization buffer: 0.1M ammonium citrate (pH 5.0) and 18% PEG
4000
;
_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_detector.details                      ? 
_diffrn_detector.detector                     'IMAGE PLATE' 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'RIGAKU RAXIS IV++' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2014-02-19 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    'VARIMAX-HF MIRROR' 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.5418 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      'ROTATING ANODE' 
_diffrn_source.target                      ? 
_diffrn_source.type                        'RIGAKU MICROMAX-007 HF' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.5418 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ? 
_diffrn_source.pdbx_synchrotron_site       ? 
# 
_reflns.B_iso_Wilson_estimate            ? 
_reflns.entry_id                         6G5U 
_reflns.data_reduction_details           ? 
_reflns.data_reduction_method            ? 
_reflns.d_resolution_high                1.700 
_reflns.d_resolution_low                 40.309 
_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                       57444 
_reflns.number_obs                       57444 
_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             98.200 
_reflns.R_free_details                   ? 
_reflns.Rmerge_F_all                     ? 
_reflns.Rmerge_F_obs                     ? 
_reflns.Friedel_coverage                 ? 
_reflns.number_gt                        ? 
_reflns.threshold_expression             ? 
_reflns.pdbx_redundancy                  4.600 
_reflns.pdbx_Rmerge_I_obs                ? 
_reflns.pdbx_Rmerge_I_all                ? 
_reflns.pdbx_Rsym_value                  0.121 
_reflns.pdbx_netI_over_av_sigmaI         3.957 
_reflns.pdbx_netI_over_sigmaI            6.600 
_reflns.pdbx_res_netI_over_av_sigmaI_2   ? 
_reflns.pdbx_res_netI_over_sigmaI_2      ? 
_reflns.pdbx_chi_squared                 ? 
_reflns.pdbx_scaling_rejects             ? 
_reflns.pdbx_d_res_high_opt              ? 
_reflns.pdbx_d_res_low_opt               ? 
_reflns.pdbx_d_res_opt_method            ? 
_reflns.phase_calculation_details        ? 
_reflns.pdbx_Rrim_I_all                  0.145 
_reflns.pdbx_Rpim_I_all                  0.066 
_reflns.pdbx_d_opt                       ? 
_reflns.pdbx_number_measured_all         265748 
_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 
1.700 1.790  ? 1.4 ? ? ? ? ? 100.000 ? ? ? ? 0.444 ? ? ? ? ? ? ? ? 5.100 0.444 ? ? ? 0.539 0.230 ? 1  1 ? ? 
1.790 1.900  ? 1.7 ? ? ? ? ? 100.000 ? ? ? ? 0.355 ? ? ? ? ? ? ? ? 5.100 0.355 ? ? ? 0.439 0.188 ? 2  1 ? ? 
1.900 2.030  ? 2.2 ? ? ? ? ? 100.000 ? ? ? ? 0.261 ? ? ? ? ? ? ? ? 5.000 0.261 ? ? ? 0.331 0.145 ? 3  1 ? ? 
2.030 2.190  ? 6.0 ? ? ? ? ? 100.000 ? ? ? ? 0.111 ? ? ? ? ? ? ? ? 5.100 0.111 ? ? ? 0.138 0.060 ? 4  1 ? ? 
2.190 2.400  ? 3.0 ? ? ? ? ? 98.800  ? ? ? ? 0.157 ? ? ? ? ? ? ? ? 4.700 0.157 ? ? ? 0.200 0.091 ? 5  1 ? ? 
2.400 2.690  ? 7.3 ? ? ? ? ? 99.700  ? ? ? ? 0.081 ? ? ? ? ? ? ? ? 4.500 0.081 ? ? ? 0.098 0.045 ? 6  1 ? ? 
2.690 3.100  ? 7.8 ? ? ? ? ? 97.100  ? ? ? ? 0.071 ? ? ? ? ? ? ? ? 4.100 0.071 ? ? ? 0.084 0.039 ? 7  1 ? ? 
3.100 3.800  ? 6.9 ? ? ? ? ? 93.400  ? ? ? ? 0.076 ? ? ? ? ? ? ? ? 3.700 0.076 ? ? ? 0.091 0.045 ? 8  1 ? ? 
3.800 5.380  ? 9.7 ? ? ? ? ? 89.000  ? ? ? ? 0.050 ? ? ? ? ? ? ? ? 3.000 0.050 ? ? ? 0.060 0.031 ? 9  1 ? ? 
5.380 40.309 ? 8.7 ? ? ? ? ? 92.000  ? ? ? ? 0.050 ? ? ? ? ? ? ? ? 3.300 0.050 ? ? ? 0.062 0.031 ? 10 1 ? ? 
# 
_refine.aniso_B[1][1]                            0.1900 
_refine.aniso_B[1][2]                            0.0000 
_refine.aniso_B[1][3]                            0.0000 
_refine.aniso_B[2][2]                            0.3900 
_refine.aniso_B[2][3]                            -0.0000 
_refine.aniso_B[3][3]                            -0.5800 
_refine.B_iso_max                                78.830 
_refine.B_iso_mean                               16.5456 
_refine.B_iso_min                                3.920 
_refine.correlation_coeff_Fo_to_Fc               0.9340 
_refine.correlation_coeff_Fo_to_Fc_free          0.9160 
_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                                 6G5U 
_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                            1.7000 
_refine.ls_d_res_low                             40.1900 
_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                     56867 
_refine.ls_number_reflns_R_free                  5727 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    97.0000 
_refine.ls_percent_reflns_R_free                 10.1000 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1961 
_refine.ls_R_factor_R_free                       0.2290 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1924 
_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                      5LLA 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.1330 
_refine.pdbx_overall_ESU_R_Free                  0.1250 
_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             0.1335 
_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        4108 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         65 
_refine_hist.number_atoms_solvent             607 
_refine_hist.number_atoms_total               4780 
_refine_hist.d_res_high                       1.7000 
_refine_hist.d_res_low                        40.1900 
# 
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' ? 0.020  0.019  4355 ? r_bond_refined_d       ? ? 
'X-RAY DIFFRACTION' ? 1.952  1.959  5935 ? r_angle_refined_deg    ? ? 
'X-RAY DIFFRACTION' ? 6.790  5.000  528  ? r_dihedral_angle_1_deg ? ? 
'X-RAY DIFFRACTION' ? 32.186 24.171 199  ? r_dihedral_angle_2_deg ? ? 
'X-RAY DIFFRACTION' ? 13.299 15.000 698  ? r_dihedral_angle_3_deg ? ? 
'X-RAY DIFFRACTION' ? 18.063 15.000 20   ? r_dihedral_angle_4_deg ? ? 
'X-RAY DIFFRACTION' ? 0.151  0.200  624  ? r_chiral_restr         ? ? 
'X-RAY DIFFRACTION' ? 0.012  0.021  3388 ? r_gen_planes_refined   ? ? 
'X-RAY DIFFRACTION' ? 1.404  1.366  2097 ? r_mcbond_it            ? ? 
'X-RAY DIFFRACTION' ? 2.129  2.043  2630 ? r_mcangle_it           ? ? 
'X-RAY DIFFRACTION' ? 2.539  1.621  2258 ? r_scbond_it            ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.7000 
_refine_ls_shell.d_res_low                        1.7440 
_refine_ls_shell.number_reflns_all                4275 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             428 
_refine_ls_shell.number_reflns_R_work             3847 
_refine_ls_shell.percent_reflns_obs               99.9300 
_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                  0.3490 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.2800 
_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                     6G5U 
_struct.title                        
'Crystal structure of human carbonic anhydrase isozyme XIII with N-butyl-2,4-dichloro-5-sulfamoyl-benzamide' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        6G5U 
_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 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 4 ? 
G N N 2 ? 
H N N 3 ? 
I N N 4 ? 
J N N 5 ? 
K N N 6 ? 
L N N 6 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CAH13_HUMAN 
_struct_ref.pdbx_db_accession          Q8N1Q1 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MSRLSWGYREHNGPIHWKEFFPIADGDQQSPIEIKTKEVKYDSSLRPLSIKYDPSSAKIISNSGHSFNVDFDDTENKSVL
RGGPLTGSYRLRQVHLHWGSADDHGSEHIVDGVSYAAELHVVHWNSDKYPSFVEAAHEPDGLAVLGVFLQIGEPNSQLQK
ITDTLDSIKEKGKQTRFTNFDLLSLLPPSWDYWTYPGSLTVPPLLESVTWIVLKQPINISSQQLAKFRSLLCTAEGEAAA
FLVSNHRPPQPLKGRKVRASFH
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 6G5U B 2 ? 263 ? Q8N1Q1 1 ? 262 ? 2 263 
2 1 6G5U A 2 ? 263 ? Q8N1Q1 1 ? 262 ? 2 263 
# 
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 6G5U MET B 1 ? UNP Q8N1Q1 ? ? 'initiating methionine' 1 1 
2 6G5U MET A 1 ? UNP Q8N1Q1 ? ? 'initiating methionine' 1 2 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,F,K 
2 1 B,G,H,I,J,L 
# 
loop_
_pdbx_struct_assembly_auth_evidence.id 
_pdbx_struct_assembly_auth_evidence.assembly_id 
_pdbx_struct_assembly_auth_evidence.experimental_support 
_pdbx_struct_assembly_auth_evidence.details 
1 1 none 'The protein is considered to be monomeric.' 
2 2 none ?                                            
# 
_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 
# 
_struct_biol.id        1 
_struct_biol.details   'biological unit is the same as asym.' 
# 
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 14  ? ILE A 16  ? GLY B 14  ILE B 16  5 ? 3 
HELX_P HELX_P2  AA2 HIS A 17  ? PHE A 22  ? HIS B 17  PHE B 22  1 ? 6 
HELX_P HELX_P3  AA3 PRO A 23  ? GLY A 27  ? PRO B 23  GLY B 27  5 ? 5 
HELX_P HELX_P4  AA4 LYS A 36  ? VAL A 40  ? LYS B 36  VAL B 40  5 ? 5 
HELX_P HELX_P5  AA5 SER A 132 ? ALA A 137 ? SER B 132 ALA B 137 1 ? 6 
HELX_P HELX_P6  AA6 ASN A 156 ? GLN A 158 ? ASN B 156 GLN B 158 5 ? 3 
HELX_P HELX_P7  AA7 LEU A 159 ? ASP A 164 ? LEU B 159 ASP B 164 1 ? 6 
HELX_P HELX_P8  AA8 THR A 165 ? LYS A 170 ? THR B 165 LYS B 170 5 ? 6 
HELX_P HELX_P9  AA9 ASP A 182 ? LEU A 187 ? ASP B 182 LEU B 187 5 ? 6 
HELX_P HELX_P10 AB1 SER A 221 ? ARG A 229 ? SER B 221 ARG B 229 1 ? 9 
HELX_P HELX_P11 AB2 GLY B 14  ? PHE B 21  ? GLY A 14  PHE A 21  5 ? 8 
HELX_P HELX_P12 AB3 PHE B 22  ? GLY B 27  ? PHE A 22  GLY A 27  5 ? 6 
HELX_P HELX_P13 AB4 SER B 132 ? ALA B 137 ? SER A 132 ALA A 137 1 ? 6 
HELX_P HELX_P14 AB5 ASN B 156 ? GLN B 158 ? ASN A 156 GLN A 158 5 ? 3 
HELX_P HELX_P15 AB6 LEU B 159 ? ASP B 164 ? LEU A 159 ASP A 164 1 ? 6 
HELX_P HELX_P16 AB7 THR B 165 ? LYS B 170 ? THR A 165 LYS A 170 5 ? 6 
HELX_P HELX_P17 AB8 ASP B 182 ? LEU B 187 ? ASP A 182 LEU A 187 5 ? 6 
HELX_P HELX_P18 AB9 SER B 221 ? ARG B 229 ? SER A 221 ARG A 229 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 96  NE2 ? ? ? 1_555 C ZN  . ZN ? ? B HIS 96  B ZN  301 1_555 ? ? ? ? ? ? ? 2.022 ? ? 
metalc2 metalc ? ? A HIS 98  NE2 ? ? ? 1_555 C ZN  . ZN ? ? B HIS 98  B ZN  301 1_555 ? ? ? ? ? ? ? 2.089 ? ? 
metalc3 metalc ? ? A HIS 121 ND1 ? ? ? 1_555 C ZN  . ZN ? ? B HIS 121 B ZN  301 1_555 ? ? ? ? ? ? ? 2.014 ? ? 
metalc4 metalc ? ? C ZN  .   ZN  ? ? ? 1_555 D ENN . S7 ? ? B ZN  301 B ENN 302 1_555 ? ? ? ? ? ? ? 2.988 ? ? 
metalc5 metalc ? ? C ZN  .   ZN  ? ? ? 1_555 D ENN . N8 ? ? B ZN  301 B ENN 302 1_555 ? ? ? ? ? ? ? 1.874 ? ? 
metalc6 metalc ? ? B HIS 96  NE2 ? ? ? 1_555 G ZN  . ZN ? ? A HIS 96  A ZN  301 1_555 ? ? ? ? ? ? ? 2.038 ? ? 
metalc7 metalc ? ? B HIS 98  NE2 ? ? ? 1_555 G ZN  . ZN ? ? A HIS 98  A ZN  301 1_555 ? ? ? ? ? ? ? 2.026 ? ? 
metalc8 metalc ? ? B HIS 121 ND1 ? ? ? 1_555 G ZN  . ZN ? ? A HIS 121 A ZN  301 1_555 ? ? ? ? ? ? ? 2.021 ? ? 
metalc9 metalc ? ? G ZN  .   ZN  ? ? ? 1_555 H ENN . N8 ? ? A ZN  301 A ENN 302 1_555 ? ? ? ? ? ? ? 1.980 ? ? 
# 
_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 96  ? B HIS 96  ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 NE2 ? A HIS 98  ? B HIS 98  ? 1_555 102.5 ? 
2  NE2 ? A HIS 96  ? B HIS 96  ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 ND1 ? A HIS 121 ? B HIS 121 ? 1_555 116.4 ? 
3  NE2 ? A HIS 98  ? B HIS 98  ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 ND1 ? A HIS 121 ? B HIS 121 ? 1_555 93.4  ? 
4  NE2 ? A HIS 96  ? B HIS 96  ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 S7  ? D ENN .   ? B ENN 302 ? 1_555 98.4  ? 
5  NE2 ? A HIS 98  ? B HIS 98  ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 S7  ? D ENN .   ? B ENN 302 ? 1_555 145.1 ? 
6  ND1 ? A HIS 121 ? B HIS 121 ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 S7  ? D ENN .   ? B ENN 302 ? 1_555 102.1 ? 
7  NE2 ? A HIS 96  ? B HIS 96  ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 N8  ? D ENN .   ? B ENN 302 ? 1_555 115.6 ? 
8  NE2 ? A HIS 98  ? B HIS 98  ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 N8  ? D ENN .   ? B ENN 302 ? 1_555 115.1 ? 
9  ND1 ? A HIS 121 ? B HIS 121 ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 N8  ? D ENN .   ? B ENN 302 ? 1_555 111.5 ? 
10 S7  ? D ENN .   ? B ENN 302 ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 N8  ? D ENN .   ? B ENN 302 ? 1_555 30.0  ? 
11 NE2 ? B HIS 96  ? A HIS 96  ? 1_555 ZN ? G ZN . ? A ZN 301 ? 1_555 NE2 ? B HIS 98  ? A HIS 98  ? 1_555 103.3 ? 
12 NE2 ? B HIS 96  ? A HIS 96  ? 1_555 ZN ? G ZN . ? A ZN 301 ? 1_555 ND1 ? B HIS 121 ? A HIS 121 ? 1_555 115.3 ? 
13 NE2 ? B HIS 98  ? A HIS 98  ? 1_555 ZN ? G ZN . ? A ZN 301 ? 1_555 ND1 ? B HIS 121 ? A HIS 121 ? 1_555 98.3  ? 
14 NE2 ? B HIS 96  ? A HIS 96  ? 1_555 ZN ? G ZN . ? A ZN 301 ? 1_555 N8  ? H ENN .   ? A ENN 302 ? 1_555 111.5 ? 
15 NE2 ? B HIS 98  ? A HIS 98  ? 1_555 ZN ? G ZN . ? A ZN 301 ? 1_555 N8  ? H ENN .   ? A ENN 302 ? 1_555 114.8 ? 
16 ND1 ? B HIS 121 ? A HIS 121 ? 1_555 ZN ? G ZN . ? A ZN 301 ? 1_555 N8  ? H ENN .   ? A ENN 302 ? 1_555 112.7 ? 
# 
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 31  A . ? SER 31  B PRO 32  A ? PRO 32  B 1 0.05  
2 PRO 203 A . ? PRO 203 B PRO 204 A ? PRO 204 B 1 7.81  
3 SER 31  B . ? SER 31  A PRO 32  B ? PRO 32  A 1 -3.78 
4 PRO 203 B . ? PRO 203 A PRO 204 B ? PRO 204 A 1 11.41 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2  ? 
AA2 ? 10 ? 
AA3 ? 6  ? 
AA4 ? 2  ? 
AA5 ? 10 ? 
AA6 ? 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      
AA4 1 2  ? parallel      
AA5 1 2  ? parallel      
AA5 2 3  ? anti-parallel 
AA5 3 4  ? anti-parallel 
AA5 4 5  ? parallel      
AA5 5 6  ? anti-parallel 
AA5 6 7  ? anti-parallel 
AA5 7 8  ? anti-parallel 
AA5 8 9  ? anti-parallel 
AA5 9 10 ? anti-parallel 
AA6 1 2  ? anti-parallel 
AA6 2 3  ? anti-parallel 
AA6 3 4  ? anti-parallel 
AA6 4 5  ? anti-parallel 
AA6 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  GLU A 34  ? ILE A 35  ? GLU B 34  ILE B 35  
AA1 2  ILE A 110 ? VAL A 111 ? ILE B 110 VAL B 111 
AA2 1  LYS A 41  ? TYR A 42  ? LYS B 41  TYR B 42  
AA2 2  ARG A 259 ? ALA A 260 ? ARG B 259 ALA B 260 
AA2 3  TYR A 193 ? GLY A 198 ? TYR B 193 GLY B 198 
AA2 4  VAL A 209 ? LEU A 214 ? VAL B 209 LEU B 214 
AA2 5  LEU A 143 ? ILE A 152 ? LEU B 143 ILE B 152 
AA2 6  ALA A 118 ? ASN A 126 ? ALA B 118 ASN B 126 
AA2 7  SER A 89  ? TRP A 99  ? SER B 89  TRP B 99  
AA2 8  PHE A 68  ? PHE A 72  ? PHE B 68  PHE B 72  
AA2 9  ALA A 58  ? ASN A 63  ? ALA B 58  ASN B 63  
AA2 10 GLN A 175 ? ARG A 177 ? GLN B 175 ARG B 177 
AA3 1  LEU A 49  ? LYS A 52  ? LEU B 49  LYS B 52  
AA3 2  VAL A 80  ? GLY A 83  ? VAL B 80  GLY B 83  
AA3 3  SER A 89  ? TRP A 99  ? SER B 89  TRP B 99  
AA3 4  ALA A 118 ? ASN A 126 ? ALA B 118 ASN B 126 
AA3 5  LEU A 143 ? ILE A 152 ? LEU B 143 ILE B 152 
AA3 6  ILE A 218 ? ILE A 220 ? ILE B 218 ILE B 220 
AA4 1  GLU B 34  ? ILE B 35  ? GLU A 34  ILE A 35  
AA4 2  ILE B 110 ? VAL B 111 ? ILE A 110 VAL A 111 
AA5 1  LYS B 41  ? TYR B 42  ? LYS A 41  TYR A 42  
AA5 2  ARG B 259 ? ALA B 260 ? ARG A 259 ALA A 260 
AA5 3  TYR B 193 ? GLY B 198 ? TYR A 193 GLY A 198 
AA5 4  VAL B 209 ? LEU B 214 ? VAL A 209 LEU A 214 
AA5 5  LEU B 143 ? ILE B 152 ? LEU A 143 ILE A 152 
AA5 6  ALA B 118 ? ASN B 126 ? ALA A 118 ASN A 126 
AA5 7  TYR B 90  ? TRP B 99  ? TYR A 90  TRP A 99  
AA5 8  PHE B 68  ? PHE B 72  ? PHE A 68  PHE A 72  
AA5 9  ALA B 58  ? ASN B 63  ? ALA A 58  ASN A 63  
AA5 10 GLN B 175 ? ARG B 177 ? GLN A 175 ARG A 177 
AA6 1  ARG B 47  ? LYS B 52  ? ARG A 47  LYS A 52  
AA6 2  VAL B 80  ? GLY B 84  ? VAL A 80  GLY A 84  
AA6 3  TYR B 90  ? TRP B 99  ? TYR A 90  TRP A 99  
AA6 4  ALA B 118 ? ASN B 126 ? ALA A 118 ASN A 126 
AA6 5  LEU B 143 ? ILE B 152 ? LEU A 143 ILE A 152 
AA6 6  ILE B 218 ? ILE B 220 ? ILE A 218 ILE A 220 
# 
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 35  ? N ILE B 35  O ILE A 110 ? O ILE B 110 
AA2 1 2  N LYS A 41  ? N LYS B 41  O ALA A 260 ? O ALA B 260 
AA2 2 3  O ARG A 259 ? O ARG B 259 N THR A 195 ? N THR B 195 
AA2 3 4  N GLY A 198 ? N GLY B 198 O VAL A 209 ? O VAL B 209 
AA2 4 5  O LEU A 214 ? O LEU B 214 N GLY A 147 ? N GLY B 147 
AA2 5 6  O VAL A 148 ? O VAL B 148 N LEU A 120 ? N LEU B 120 
AA2 6 7  O TRP A 125 ? O TRP B 125 N ARG A 91  ? N ARG B 91  
AA2 7 8  O VAL A 95  ? O VAL B 95  N VAL A 70  ? N VAL B 70  
AA2 8 9  O ASP A 71  ? O ASP B 71  N ILE A 60  ? N ILE B 60  
AA2 9 10 N ILE A 61  ? N ILE B 61  O THR A 176 ? O THR B 176 
AA3 1 2  N LYS A 52  ? N LYS B 52  O VAL A 80  ? O VAL B 80  
AA3 2 3  N LEU A 81  ? N LEU B 81  O TYR A 90  ? O TYR B 90  
AA3 3 4  N ARG A 91  ? N ARG B 91  O TRP A 125 ? O TRP B 125 
AA3 4 5  N LEU A 120 ? N LEU B 120 O VAL A 148 ? O VAL B 148 
AA3 5 6  N GLN A 151 ? N GLN B 151 O ILE A 218 ? O ILE B 218 
AA4 1 2  N ILE B 35  ? N ILE A 35  O ILE B 110 ? O ILE A 110 
AA5 1 2  N LYS B 41  ? N LYS A 41  O ALA B 260 ? O ALA A 260 
AA5 2 3  O ARG B 259 ? O ARG A 259 N THR B 195 ? N THR A 195 
AA5 3 4  N GLY B 198 ? N GLY A 198 O VAL B 209 ? O VAL A 209 
AA5 4 5  O LEU B 214 ? O LEU A 214 N GLY B 147 ? N GLY A 147 
AA5 5 6  O VAL B 148 ? O VAL A 148 N LEU B 120 ? N LEU A 120 
AA5 6 7  O TRP B 125 ? O TRP A 125 N ARG B 91  ? N ARG A 91  
AA5 7 8  O VAL B 95  ? O VAL A 95  N VAL B 70  ? N VAL A 70  
AA5 8 9  O ASP B 71  ? O ASP A 71  N ILE B 60  ? N ILE A 60  
AA5 9 10 N ILE B 61  ? N ILE A 61  O THR B 176 ? O THR A 176 
AA6 1 2  N SER B 50  ? N SER A 50  O ARG B 82  ? O ARG A 82  
AA6 2 3  N LEU B 81  ? N LEU A 81  O TYR B 90  ? O TYR A 90  
AA6 3 4  N ARG B 91  ? N ARG A 91  O TRP B 125 ? O TRP A 125 
AA6 4 5  N LEU B 120 ? N LEU A 120 O VAL B 148 ? O VAL A 148 
AA6 5 6  N PHE B 149 ? N PHE A 149 O ILE B 218 ? O ILE 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 B ZN  301 ? 4  'binding site for residue ZN B 301'  
AC2 Software B ENN 302 ? 13 'binding site for residue ENN B 302' 
AC3 Software B EDO 303 ? 4  'binding site for residue EDO B 303' 
AC4 Software B EDO 304 ? 7  'binding site for residue EDO B 304' 
AC5 Software A ZN  301 ? 4  'binding site for residue ZN A 301'  
AC6 Software A ENN 302 ? 14 'binding site for residue ENN A 302' 
AC7 Software A EDO 303 ? 5  'binding site for residue EDO A 303' 
AC8 Software A CIT 304 ? 11 'binding site for residue CIT A 304' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  AC1 4  HIS A 96  ? HIS B 96  . ? 1_555 ? 
2  AC1 4  HIS A 98  ? HIS B 98  . ? 1_555 ? 
3  AC1 4  HIS A 121 ? HIS B 121 . ? 1_555 ? 
4  AC1 4  ENN D .   ? ENN B 302 . ? 1_555 ? 
5  AC2 13 GLN A 94  ? GLN B 94  . ? 1_555 ? 
6  AC2 13 HIS A 96  ? HIS B 96  . ? 1_555 ? 
7  AC2 13 HIS A 98  ? HIS B 98  . ? 1_555 ? 
8  AC2 13 HIS A 121 ? HIS B 121 . ? 1_555 ? 
9  AC2 13 VAL A 145 ? VAL B 145 . ? 1_555 ? 
10 AC2 13 LEU A 200 ? LEU B 200 . ? 1_555 ? 
11 AC2 13 THR A 201 ? THR B 201 . ? 1_555 ? 
12 AC2 13 VAL A 202 ? VAL B 202 . ? 1_555 ? 
13 AC2 13 TRP A 211 ? TRP B 211 . ? 1_555 ? 
14 AC2 13 ZN  C .   ? ZN  B 301 . ? 1_555 ? 
15 AC2 13 HOH K .   ? HOH B 465 . ? 1_555 ? 
16 AC2 13 HOH K .   ? HOH B 553 . ? 1_555 ? 
17 AC2 13 HOH K .   ? HOH B 698 . ? 1_555 ? 
18 AC3 4  SER A 56  ? SER B 56  . ? 1_555 ? 
19 AC3 4  ASN A 180 ? ASN B 180 . ? 1_555 ? 
20 AC3 4  HOH K .   ? HOH B 415 . ? 1_555 ? 
21 AC3 4  HOH K .   ? HOH B 538 . ? 1_555 ? 
22 AC4 7  LYS B 129 ? LYS A 129 . ? 4_555 ? 
23 AC4 7  HOH L .   ? HOH A 518 . ? 4_555 ? 
24 AC4 7  ARG A 10  ? ARG B 10  . ? 1_555 ? 
25 AC4 7  ALA A 241 ? ALA B 241 . ? 1_555 ? 
26 AC4 7  PHE A 242 ? PHE B 242 . ? 1_555 ? 
27 AC4 7  HOH K .   ? HOH B 462 . ? 1_555 ? 
28 AC4 7  HOH K .   ? HOH B 603 . ? 1_555 ? 
29 AC5 4  HIS B 96  ? HIS A 96  . ? 1_555 ? 
30 AC5 4  HIS B 98  ? HIS A 98  . ? 1_555 ? 
31 AC5 4  HIS B 121 ? HIS A 121 . ? 1_555 ? 
32 AC5 4  ENN H .   ? ENN A 302 . ? 1_555 ? 
33 AC6 14 GLN B 94  ? GLN A 94  . ? 1_555 ? 
34 AC6 14 HIS B 96  ? HIS A 96  . ? 1_555 ? 
35 AC6 14 HIS B 98  ? HIS A 98  . ? 1_555 ? 
36 AC6 14 HIS B 121 ? HIS A 121 . ? 1_555 ? 
37 AC6 14 VAL B 145 ? VAL A 145 . ? 1_555 ? 
38 AC6 14 LEU B 200 ? LEU A 200 . ? 1_555 ? 
39 AC6 14 THR B 201 ? THR A 201 . ? 1_555 ? 
40 AC6 14 VAL B 202 ? VAL A 202 . ? 1_555 ? 
41 AC6 14 TRP B 211 ? TRP A 211 . ? 1_555 ? 
42 AC6 14 ZN  G .   ? ZN  A 301 . ? 1_555 ? 
43 AC6 14 HOH L .   ? HOH A 413 . ? 1_555 ? 
44 AC6 14 HOH L .   ? HOH A 475 . ? 1_555 ? 
45 AC6 14 HOH L .   ? HOH A 537 . ? 1_555 ? 
46 AC6 14 HOH L .   ? HOH A 615 . ? 1_555 ? 
47 AC7 5  ASN B 180 ? ASN A 180 . ? 1_555 ? 
48 AC7 5  LYS A 52  ? LYS B 52  . ? 1_555 ? 
49 AC7 5  ASP A 54  ? ASP B 54  . ? 1_555 ? 
50 AC7 5  PRO A 55  ? PRO B 55  . ? 1_555 ? 
51 AC7 5  HOH K .   ? HOH B 402 . ? 1_555 ? 
52 AC8 11 GLY B 100 ? GLY A 100 . ? 1_555 ? 
53 AC8 11 SER B 101 ? SER A 101 . ? 1_555 ? 
54 AC8 11 HIS B 105 ? HIS A 105 . ? 1_555 ? 
55 AC8 11 SER B 245 ? SER A 245 . ? 1_555 ? 
56 AC8 11 HIS B 247 ? HIS A 247 . ? 1_555 ? 
57 AC8 11 HOH L .   ? HOH A 414 . ? 1_555 ? 
58 AC8 11 HOH L .   ? HOH A 415 . ? 1_555 ? 
59 AC8 11 HOH L .   ? HOH A 471 . ? 1_555 ? 
60 AC8 11 HOH L .   ? HOH A 538 . ? 1_555 ? 
61 AC8 11 HOH L .   ? HOH A 603 . ? 1_555 ? 
62 AC8 11 HOH K .   ? HOH B 536 . ? 3_554 ? 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   OG 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   SER 
_pdbx_validate_close_contact.auth_seq_id_1    230 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   B 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    401 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.06 
# 
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 SER B 67  ? ? -176.50 -174.93 
2 1 GLU B 76  ? ? -144.32 -154.81 
3 1 ASN B 77  ? ? -100.96 44.75   
4 1 HIS B 105 ? ? -151.95 66.39   
5 1 PHE B 178 ? ? -161.22 105.90  
6 1 ASN B 246 ? ? -145.39 45.75   
7 1 SER A 67  ? ? -177.95 -178.38 
8 1 ASN A 77  ? ? -97.29  35.53   
9 1 ASN A 246 ? ? -152.45 39.77   
# 
_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 B MET 1 ? A MET 1 
2  1 Y 1 B MET 2 ? A MET 2 
3  1 Y 1 B SER 3 ? A SER 3 
4  1 Y 1 B ARG 4 ? A ARG 4 
5  1 Y 1 B LEU 5 ? A LEU 5 
6  1 Y 1 A MET 1 ? B MET 1 
7  1 Y 1 A MET 2 ? B MET 2 
8  1 Y 1 A SER 3 ? B SER 3 
9  1 Y 1 A ARG 4 ? B ARG 4 
10 1 Y 1 A LEU 5 ? B LEU 5 
# 
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  
CIT C1   C  N N 74  
CIT O1   O  N N 75  
CIT O2   O  N N 76  
CIT C2   C  N N 77  
CIT C3   C  N N 78  
CIT O7   O  N N 79  
CIT C4   C  N N 80  
CIT C5   C  N N 81  
CIT O3   O  N N 82  
CIT O4   O  N N 83  
CIT C6   C  N N 84  
CIT O5   O  N N 85  
CIT O6   O  N N 86  
CIT HO2  H  N N 87  
CIT H21  H  N N 88  
CIT H22  H  N N 89  
CIT HO7  H  N N 90  
CIT H41  H  N N 91  
CIT H42  H  N N 92  
CIT HO4  H  N N 93  
CIT HO6  H  N N 94  
CYS N    N  N N 95  
CYS CA   C  N R 96  
CYS C    C  N N 97  
CYS O    O  N N 98  
CYS CB   C  N N 99  
CYS SG   S  N N 100 
CYS OXT  O  N N 101 
CYS H    H  N N 102 
CYS H2   H  N N 103 
CYS HA   H  N N 104 
CYS HB2  H  N N 105 
CYS HB3  H  N N 106 
CYS HG   H  N N 107 
CYS HXT  H  N N 108 
EDO C1   C  N N 109 
EDO O1   O  N N 110 
EDO C2   C  N N 111 
EDO O2   O  N N 112 
EDO H11  H  N N 113 
EDO H12  H  N N 114 
EDO HO1  H  N N 115 
EDO H21  H  N N 116 
EDO H22  H  N N 117 
EDO HO2  H  N N 118 
ENN C5   C  Y N 119 
ENN C4   C  Y N 120 
ENN C6   C  Y N 121 
ENN C2   C  Y N 122 
ENN O14  O  N N 123 
ENN C13  C  N N 124 
ENN N15  N  N N 125 
ENN C16  C  N N 126 
ENN C17  C  N N 127 
ENN C18  C  N N 128 
ENN C19  C  N N 129 
ENN C3   C  Y N 130 
ENN CL1  CL N N 131 
ENN C1   C  Y N 132 
ENN CL2  CL N N 133 
ENN S7   S  N N 134 
ENN O9   O  N N 135 
ENN O10  O  N N 136 
ENN N8   N  N N 137 
ENN H1   H  N N 138 
ENN H2   H  N N 139 
ENN H3   H  N N 140 
ENN H4   H  N N 141 
ENN H5   H  N N 142 
ENN H6   H  N N 143 
ENN H7   H  N N 144 
ENN H8   H  N N 145 
ENN H9   H  N N 146 
ENN H10  H  N N 147 
ENN H11  H  N N 148 
ENN H12  H  N N 149 
ENN H13  H  N N 150 
ENN H14  H  N N 151 
GLN N    N  N N 152 
GLN CA   C  N S 153 
GLN C    C  N N 154 
GLN O    O  N N 155 
GLN CB   C  N N 156 
GLN CG   C  N N 157 
GLN CD   C  N N 158 
GLN OE1  O  N N 159 
GLN NE2  N  N N 160 
GLN OXT  O  N N 161 
GLN H    H  N N 162 
GLN H2   H  N N 163 
GLN HA   H  N N 164 
GLN HB2  H  N N 165 
GLN HB3  H  N N 166 
GLN HG2  H  N N 167 
GLN HG3  H  N N 168 
GLN HE21 H  N N 169 
GLN HE22 H  N N 170 
GLN HXT  H  N N 171 
GLU N    N  N N 172 
GLU CA   C  N S 173 
GLU C    C  N N 174 
GLU O    O  N N 175 
GLU CB   C  N N 176 
GLU CG   C  N N 177 
GLU CD   C  N N 178 
GLU OE1  O  N N 179 
GLU OE2  O  N N 180 
GLU OXT  O  N N 181 
GLU H    H  N N 182 
GLU H2   H  N N 183 
GLU HA   H  N N 184 
GLU HB2  H  N N 185 
GLU HB3  H  N N 186 
GLU HG2  H  N N 187 
GLU HG3  H  N N 188 
GLU HE2  H  N N 189 
GLU HXT  H  N N 190 
GLY N    N  N N 191 
GLY CA   C  N N 192 
GLY C    C  N N 193 
GLY O    O  N N 194 
GLY OXT  O  N N 195 
GLY H    H  N N 196 
GLY H2   H  N N 197 
GLY HA2  H  N N 198 
GLY HA3  H  N N 199 
GLY HXT  H  N N 200 
HIS N    N  N N 201 
HIS CA   C  N S 202 
HIS C    C  N N 203 
HIS O    O  N N 204 
HIS CB   C  N N 205 
HIS CG   C  Y N 206 
HIS ND1  N  Y N 207 
HIS CD2  C  Y N 208 
HIS CE1  C  Y N 209 
HIS NE2  N  Y N 210 
HIS OXT  O  N N 211 
HIS H    H  N N 212 
HIS H2   H  N N 213 
HIS HA   H  N N 214 
HIS HB2  H  N N 215 
HIS HB3  H  N N 216 
HIS HD1  H  N N 217 
HIS HD2  H  N N 218 
HIS HE1  H  N N 219 
HIS HE2  H  N N 220 
HIS HXT  H  N N 221 
HOH O    O  N N 222 
HOH H1   H  N N 223 
HOH H2   H  N N 224 
ILE N    N  N N 225 
ILE CA   C  N S 226 
ILE C    C  N N 227 
ILE O    O  N N 228 
ILE CB   C  N S 229 
ILE CG1  C  N N 230 
ILE CG2  C  N N 231 
ILE CD1  C  N N 232 
ILE OXT  O  N N 233 
ILE H    H  N N 234 
ILE H2   H  N N 235 
ILE HA   H  N N 236 
ILE HB   H  N N 237 
ILE HG12 H  N N 238 
ILE HG13 H  N N 239 
ILE HG21 H  N N 240 
ILE HG22 H  N N 241 
ILE HG23 H  N N 242 
ILE HD11 H  N N 243 
ILE HD12 H  N N 244 
ILE HD13 H  N N 245 
ILE HXT  H  N N 246 
LEU N    N  N N 247 
LEU CA   C  N S 248 
LEU C    C  N N 249 
LEU O    O  N N 250 
LEU CB   C  N N 251 
LEU CG   C  N N 252 
LEU CD1  C  N N 253 
LEU CD2  C  N N 254 
LEU OXT  O  N N 255 
LEU H    H  N N 256 
LEU H2   H  N N 257 
LEU HA   H  N N 258 
LEU HB2  H  N N 259 
LEU HB3  H  N N 260 
LEU HG   H  N N 261 
LEU HD11 H  N N 262 
LEU HD12 H  N N 263 
LEU HD13 H  N N 264 
LEU HD21 H  N N 265 
LEU HD22 H  N N 266 
LEU HD23 H  N N 267 
LEU HXT  H  N N 268 
LYS N    N  N N 269 
LYS CA   C  N S 270 
LYS C    C  N N 271 
LYS O    O  N N 272 
LYS CB   C  N N 273 
LYS CG   C  N N 274 
LYS CD   C  N N 275 
LYS CE   C  N N 276 
LYS NZ   N  N N 277 
LYS OXT  O  N N 278 
LYS H    H  N N 279 
LYS H2   H  N N 280 
LYS HA   H  N N 281 
LYS HB2  H  N N 282 
LYS HB3  H  N N 283 
LYS HG2  H  N N 284 
LYS HG3  H  N N 285 
LYS HD2  H  N N 286 
LYS HD3  H  N N 287 
LYS HE2  H  N N 288 
LYS HE3  H  N N 289 
LYS HZ1  H  N N 290 
LYS HZ2  H  N N 291 
LYS HZ3  H  N N 292 
LYS HXT  H  N N 293 
MET N    N  N N 294 
MET CA   C  N S 295 
MET C    C  N N 296 
MET O    O  N N 297 
MET CB   C  N N 298 
MET CG   C  N N 299 
MET SD   S  N N 300 
MET CE   C  N N 301 
MET OXT  O  N N 302 
MET H    H  N N 303 
MET H2   H  N N 304 
MET HA   H  N N 305 
MET HB2  H  N N 306 
MET HB3  H  N N 307 
MET HG2  H  N N 308 
MET HG3  H  N N 309 
MET HE1  H  N N 310 
MET HE2  H  N N 311 
MET HE3  H  N N 312 
MET HXT  H  N N 313 
PHE N    N  N N 314 
PHE CA   C  N S 315 
PHE C    C  N N 316 
PHE O    O  N N 317 
PHE CB   C  N N 318 
PHE CG   C  Y N 319 
PHE CD1  C  Y N 320 
PHE CD2  C  Y N 321 
PHE CE1  C  Y N 322 
PHE CE2  C  Y N 323 
PHE CZ   C  Y N 324 
PHE OXT  O  N N 325 
PHE H    H  N N 326 
PHE H2   H  N N 327 
PHE HA   H  N N 328 
PHE HB2  H  N N 329 
PHE HB3  H  N N 330 
PHE HD1  H  N N 331 
PHE HD2  H  N N 332 
PHE HE1  H  N N 333 
PHE HE2  H  N N 334 
PHE HZ   H  N N 335 
PHE HXT  H  N N 336 
PRO N    N  N N 337 
PRO CA   C  N S 338 
PRO C    C  N N 339 
PRO O    O  N N 340 
PRO CB   C  N N 341 
PRO CG   C  N N 342 
PRO CD   C  N N 343 
PRO OXT  O  N N 344 
PRO H    H  N N 345 
PRO HA   H  N N 346 
PRO HB2  H  N N 347 
PRO HB3  H  N N 348 
PRO HG2  H  N N 349 
PRO HG3  H  N N 350 
PRO HD2  H  N N 351 
PRO HD3  H  N N 352 
PRO HXT  H  N N 353 
SER N    N  N N 354 
SER CA   C  N S 355 
SER C    C  N N 356 
SER O    O  N N 357 
SER CB   C  N N 358 
SER OG   O  N N 359 
SER OXT  O  N N 360 
SER H    H  N N 361 
SER H2   H  N N 362 
SER HA   H  N N 363 
SER HB2  H  N N 364 
SER HB3  H  N N 365 
SER HG   H  N N 366 
SER HXT  H  N N 367 
THR N    N  N N 368 
THR CA   C  N S 369 
THR C    C  N N 370 
THR O    O  N N 371 
THR CB   C  N R 372 
THR OG1  O  N N 373 
THR CG2  C  N N 374 
THR OXT  O  N N 375 
THR H    H  N N 376 
THR H2   H  N N 377 
THR HA   H  N N 378 
THR HB   H  N N 379 
THR HG1  H  N N 380 
THR HG21 H  N N 381 
THR HG22 H  N N 382 
THR HG23 H  N N 383 
THR HXT  H  N N 384 
TRP N    N  N N 385 
TRP CA   C  N S 386 
TRP C    C  N N 387 
TRP O    O  N N 388 
TRP CB   C  N N 389 
TRP CG   C  Y N 390 
TRP CD1  C  Y N 391 
TRP CD2  C  Y N 392 
TRP NE1  N  Y N 393 
TRP CE2  C  Y N 394 
TRP CE3  C  Y N 395 
TRP CZ2  C  Y N 396 
TRP CZ3  C  Y N 397 
TRP CH2  C  Y N 398 
TRP OXT  O  N N 399 
TRP H    H  N N 400 
TRP H2   H  N N 401 
TRP HA   H  N N 402 
TRP HB2  H  N N 403 
TRP HB3  H  N N 404 
TRP HD1  H  N N 405 
TRP HE1  H  N N 406 
TRP HE3  H  N N 407 
TRP HZ2  H  N N 408 
TRP HZ3  H  N N 409 
TRP HH2  H  N N 410 
TRP HXT  H  N N 411 
TYR N    N  N N 412 
TYR CA   C  N S 413 
TYR C    C  N N 414 
TYR O    O  N N 415 
TYR CB   C  N N 416 
TYR CG   C  Y N 417 
TYR CD1  C  Y N 418 
TYR CD2  C  Y N 419 
TYR CE1  C  Y N 420 
TYR CE2  C  Y N 421 
TYR CZ   C  Y N 422 
TYR OH   O  N N 423 
TYR OXT  O  N N 424 
TYR H    H  N N 425 
TYR H2   H  N N 426 
TYR HA   H  N N 427 
TYR HB2  H  N N 428 
TYR HB3  H  N N 429 
TYR HD1  H  N N 430 
TYR HD2  H  N N 431 
TYR HE1  H  N N 432 
TYR HE2  H  N N 433 
TYR HH   H  N N 434 
TYR HXT  H  N N 435 
VAL N    N  N N 436 
VAL CA   C  N S 437 
VAL C    C  N N 438 
VAL O    O  N N 439 
VAL CB   C  N N 440 
VAL CG1  C  N N 441 
VAL CG2  C  N N 442 
VAL OXT  O  N N 443 
VAL H    H  N N 444 
VAL H2   H  N N 445 
VAL HA   H  N N 446 
VAL HB   H  N N 447 
VAL HG11 H  N N 448 
VAL HG12 H  N N 449 
VAL HG13 H  N N 450 
VAL HG21 H  N N 451 
VAL HG22 H  N N 452 
VAL HG23 H  N N 453 
VAL HXT  H  N N 454 
ZN  ZN   ZN N N 455 
# 
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  
CIT C1  O1   doub N N 70  
CIT C1  O2   sing N N 71  
CIT C1  C2   sing N N 72  
CIT O2  HO2  sing N N 73  
CIT C2  C3   sing N N 74  
CIT C2  H21  sing N N 75  
CIT C2  H22  sing N N 76  
CIT C3  O7   sing N N 77  
CIT C3  C4   sing N N 78  
CIT C3  C6   sing N N 79  
CIT O7  HO7  sing N N 80  
CIT C4  C5   sing N N 81  
CIT C4  H41  sing N N 82  
CIT C4  H42  sing N N 83  
CIT C5  O3   doub N N 84  
CIT C5  O4   sing N N 85  
CIT O4  HO4  sing N N 86  
CIT C6  O5   doub N N 87  
CIT C6  O6   sing N N 88  
CIT O6  HO6  sing N N 89  
CYS N   CA   sing N N 90  
CYS N   H    sing N N 91  
CYS N   H2   sing N N 92  
CYS CA  C    sing N N 93  
CYS CA  CB   sing N N 94  
CYS CA  HA   sing N N 95  
CYS C   O    doub N N 96  
CYS C   OXT  sing N N 97  
CYS CB  SG   sing N N 98  
CYS CB  HB2  sing N N 99  
CYS CB  HB3  sing N N 100 
CYS SG  HG   sing N N 101 
CYS OXT HXT  sing N N 102 
EDO C1  O1   sing N N 103 
EDO C1  C2   sing N N 104 
EDO C1  H11  sing N N 105 
EDO C1  H12  sing N N 106 
EDO O1  HO1  sing N N 107 
EDO C2  O2   sing N N 108 
EDO C2  H21  sing N N 109 
EDO C2  H22  sing N N 110 
EDO O2  HO2  sing N N 111 
ENN CL2 C1   sing N N 112 
ENN CL1 C3   sing N N 113 
ENN C2  C1   doub Y N 114 
ENN C2  C3   sing Y N 115 
ENN C1  C6   sing Y N 116 
ENN C3  C4   doub Y N 117 
ENN C6  C5   doub Y N 118 
ENN C6  S7   sing N N 119 
ENN C4  C5   sing Y N 120 
ENN C4  C13  sing N N 121 
ENN C18 C17  sing N N 122 
ENN C18 C19  sing N N 123 
ENN O9  S7   doub N N 124 
ENN N15 C13  sing N N 125 
ENN N15 C16  sing N N 126 
ENN C17 C16  sing N N 127 
ENN C13 O14  doub N N 128 
ENN S7  O10  doub N N 129 
ENN S7  N8   sing N N 130 
ENN C5  H1   sing N N 131 
ENN C2  H2   sing N N 132 
ENN N15 H3   sing N N 133 
ENN C16 H4   sing N N 134 
ENN C16 H5   sing N N 135 
ENN C17 H6   sing N N 136 
ENN C17 H7   sing N N 137 
ENN C18 H8   sing N N 138 
ENN C18 H9   sing N N 139 
ENN C19 H10  sing N N 140 
ENN C19 H11  sing N N 141 
ENN C19 H12  sing N N 142 
ENN N8  H13  sing N N 143 
ENN N8  H14  sing N N 144 
GLN N   CA   sing N N 145 
GLN N   H    sing N N 146 
GLN N   H2   sing N N 147 
GLN CA  C    sing N N 148 
GLN CA  CB   sing N N 149 
GLN CA  HA   sing N N 150 
GLN C   O    doub N N 151 
GLN C   OXT  sing N N 152 
GLN CB  CG   sing N N 153 
GLN CB  HB2  sing N N 154 
GLN CB  HB3  sing N N 155 
GLN CG  CD   sing N N 156 
GLN CG  HG2  sing N N 157 
GLN CG  HG3  sing N N 158 
GLN CD  OE1  doub N N 159 
GLN CD  NE2  sing N N 160 
GLN NE2 HE21 sing N N 161 
GLN NE2 HE22 sing N N 162 
GLN OXT HXT  sing N N 163 
GLU N   CA   sing N N 164 
GLU N   H    sing N N 165 
GLU N   H2   sing N N 166 
GLU CA  C    sing N N 167 
GLU CA  CB   sing N N 168 
GLU CA  HA   sing N N 169 
GLU C   O    doub N N 170 
GLU C   OXT  sing N N 171 
GLU CB  CG   sing N N 172 
GLU CB  HB2  sing N N 173 
GLU CB  HB3  sing N N 174 
GLU CG  CD   sing N N 175 
GLU CG  HG2  sing N N 176 
GLU CG  HG3  sing N N 177 
GLU CD  OE1  doub N N 178 
GLU CD  OE2  sing N N 179 
GLU OE2 HE2  sing N N 180 
GLU OXT HXT  sing N N 181 
GLY N   CA   sing N N 182 
GLY N   H    sing N N 183 
GLY N   H2   sing N N 184 
GLY CA  C    sing N N 185 
GLY CA  HA2  sing N N 186 
GLY CA  HA3  sing N N 187 
GLY C   O    doub N N 188 
GLY C   OXT  sing N N 189 
GLY OXT HXT  sing N N 190 
HIS N   CA   sing N N 191 
HIS N   H    sing N N 192 
HIS N   H2   sing N N 193 
HIS CA  C    sing N N 194 
HIS CA  CB   sing N N 195 
HIS CA  HA   sing N N 196 
HIS C   O    doub N N 197 
HIS C   OXT  sing N N 198 
HIS CB  CG   sing N N 199 
HIS CB  HB2  sing N N 200 
HIS CB  HB3  sing N N 201 
HIS CG  ND1  sing Y N 202 
HIS CG  CD2  doub Y N 203 
HIS ND1 CE1  doub Y N 204 
HIS ND1 HD1  sing N N 205 
HIS CD2 NE2  sing Y N 206 
HIS CD2 HD2  sing N N 207 
HIS CE1 NE2  sing Y N 208 
HIS CE1 HE1  sing N N 209 
HIS NE2 HE2  sing N N 210 
HIS OXT HXT  sing N N 211 
HOH O   H1   sing N N 212 
HOH O   H2   sing N N 213 
ILE N   CA   sing N N 214 
ILE N   H    sing N N 215 
ILE N   H2   sing N N 216 
ILE CA  C    sing N N 217 
ILE CA  CB   sing N N 218 
ILE CA  HA   sing N N 219 
ILE C   O    doub N N 220 
ILE C   OXT  sing N N 221 
ILE CB  CG1  sing N N 222 
ILE CB  CG2  sing N N 223 
ILE CB  HB   sing N N 224 
ILE CG1 CD1  sing N N 225 
ILE CG1 HG12 sing N N 226 
ILE CG1 HG13 sing N N 227 
ILE CG2 HG21 sing N N 228 
ILE CG2 HG22 sing N N 229 
ILE CG2 HG23 sing N N 230 
ILE CD1 HD11 sing N N 231 
ILE CD1 HD12 sing N N 232 
ILE CD1 HD13 sing N N 233 
ILE OXT HXT  sing N N 234 
LEU N   CA   sing N N 235 
LEU N   H    sing N N 236 
LEU N   H2   sing N N 237 
LEU CA  C    sing N N 238 
LEU CA  CB   sing N N 239 
LEU CA  HA   sing N N 240 
LEU C   O    doub N N 241 
LEU C   OXT  sing N N 242 
LEU CB  CG   sing N N 243 
LEU CB  HB2  sing N N 244 
LEU CB  HB3  sing N N 245 
LEU CG  CD1  sing N N 246 
LEU CG  CD2  sing N N 247 
LEU CG  HG   sing N N 248 
LEU CD1 HD11 sing N N 249 
LEU CD1 HD12 sing N N 250 
LEU CD1 HD13 sing N N 251 
LEU CD2 HD21 sing N N 252 
LEU CD2 HD22 sing N N 253 
LEU CD2 HD23 sing N N 254 
LEU OXT HXT  sing N N 255 
LYS N   CA   sing N N 256 
LYS N   H    sing N N 257 
LYS N   H2   sing N N 258 
LYS CA  C    sing N N 259 
LYS CA  CB   sing N N 260 
LYS CA  HA   sing N N 261 
LYS C   O    doub N N 262 
LYS C   OXT  sing N N 263 
LYS CB  CG   sing N N 264 
LYS CB  HB2  sing N N 265 
LYS CB  HB3  sing N N 266 
LYS CG  CD   sing N N 267 
LYS CG  HG2  sing N N 268 
LYS CG  HG3  sing N N 269 
LYS CD  CE   sing N N 270 
LYS CD  HD2  sing N N 271 
LYS CD  HD3  sing N N 272 
LYS CE  NZ   sing N N 273 
LYS CE  HE2  sing N N 274 
LYS CE  HE3  sing N N 275 
LYS NZ  HZ1  sing N N 276 
LYS NZ  HZ2  sing N N 277 
LYS NZ  HZ3  sing N N 278 
LYS OXT HXT  sing N N 279 
MET N   CA   sing N N 280 
MET N   H    sing N N 281 
MET N   H2   sing N N 282 
MET CA  C    sing N N 283 
MET CA  CB   sing N N 284 
MET CA  HA   sing N N 285 
MET C   O    doub N N 286 
MET C   OXT  sing N N 287 
MET CB  CG   sing N N 288 
MET CB  HB2  sing N N 289 
MET CB  HB3  sing N N 290 
MET CG  SD   sing N N 291 
MET CG  HG2  sing N N 292 
MET CG  HG3  sing N N 293 
MET SD  CE   sing N N 294 
MET CE  HE1  sing N N 295 
MET CE  HE2  sing N N 296 
MET CE  HE3  sing N N 297 
MET OXT HXT  sing N N 298 
PHE N   CA   sing N N 299 
PHE N   H    sing N N 300 
PHE N   H2   sing N N 301 
PHE CA  C    sing N N 302 
PHE CA  CB   sing N N 303 
PHE CA  HA   sing N N 304 
PHE C   O    doub N N 305 
PHE C   OXT  sing N N 306 
PHE CB  CG   sing N N 307 
PHE CB  HB2  sing N N 308 
PHE CB  HB3  sing N N 309 
PHE CG  CD1  doub Y N 310 
PHE CG  CD2  sing Y N 311 
PHE CD1 CE1  sing Y N 312 
PHE CD1 HD1  sing N N 313 
PHE CD2 CE2  doub Y N 314 
PHE CD2 HD2  sing N N 315 
PHE CE1 CZ   doub Y N 316 
PHE CE1 HE1  sing N N 317 
PHE CE2 CZ   sing Y N 318 
PHE CE2 HE2  sing N N 319 
PHE CZ  HZ   sing N N 320 
PHE OXT HXT  sing N N 321 
PRO N   CA   sing N N 322 
PRO N   CD   sing N N 323 
PRO N   H    sing N N 324 
PRO CA  C    sing N N 325 
PRO CA  CB   sing N N 326 
PRO CA  HA   sing N N 327 
PRO C   O    doub N N 328 
PRO C   OXT  sing N N 329 
PRO CB  CG   sing N N 330 
PRO CB  HB2  sing N N 331 
PRO CB  HB3  sing N N 332 
PRO CG  CD   sing N N 333 
PRO CG  HG2  sing N N 334 
PRO CG  HG3  sing N N 335 
PRO CD  HD2  sing N N 336 
PRO CD  HD3  sing N N 337 
PRO OXT HXT  sing N N 338 
SER N   CA   sing N N 339 
SER N   H    sing N N 340 
SER N   H2   sing N N 341 
SER CA  C    sing N N 342 
SER CA  CB   sing N N 343 
SER CA  HA   sing N N 344 
SER C   O    doub N N 345 
SER C   OXT  sing N N 346 
SER CB  OG   sing N N 347 
SER CB  HB2  sing N N 348 
SER CB  HB3  sing N N 349 
SER OG  HG   sing N N 350 
SER OXT HXT  sing N N 351 
THR N   CA   sing N N 352 
THR N   H    sing N N 353 
THR N   H2   sing N N 354 
THR CA  C    sing N N 355 
THR CA  CB   sing N N 356 
THR CA  HA   sing N N 357 
THR C   O    doub N N 358 
THR C   OXT  sing N N 359 
THR CB  OG1  sing N N 360 
THR CB  CG2  sing N N 361 
THR CB  HB   sing N N 362 
THR OG1 HG1  sing N N 363 
THR CG2 HG21 sing N N 364 
THR CG2 HG22 sing N N 365 
THR CG2 HG23 sing N N 366 
THR OXT HXT  sing N N 367 
TRP N   CA   sing N N 368 
TRP N   H    sing N N 369 
TRP N   H2   sing N N 370 
TRP CA  C    sing N N 371 
TRP CA  CB   sing N N 372 
TRP CA  HA   sing N N 373 
TRP C   O    doub N N 374 
TRP C   OXT  sing N N 375 
TRP CB  CG   sing N N 376 
TRP CB  HB2  sing N N 377 
TRP CB  HB3  sing N N 378 
TRP CG  CD1  doub Y N 379 
TRP CG  CD2  sing Y N 380 
TRP CD1 NE1  sing Y N 381 
TRP CD1 HD1  sing N N 382 
TRP CD2 CE2  doub Y N 383 
TRP CD2 CE3  sing Y N 384 
TRP NE1 CE2  sing Y N 385 
TRP NE1 HE1  sing N N 386 
TRP CE2 CZ2  sing Y N 387 
TRP CE3 CZ3  doub Y N 388 
TRP CE3 HE3  sing N N 389 
TRP CZ2 CH2  doub Y N 390 
TRP CZ2 HZ2  sing N N 391 
TRP CZ3 CH2  sing Y N 392 
TRP CZ3 HZ3  sing N N 393 
TRP CH2 HH2  sing N N 394 
TRP OXT HXT  sing N N 395 
TYR N   CA   sing N N 396 
TYR N   H    sing N N 397 
TYR N   H2   sing N N 398 
TYR CA  C    sing N N 399 
TYR CA  CB   sing N N 400 
TYR CA  HA   sing N N 401 
TYR C   O    doub N N 402 
TYR C   OXT  sing N N 403 
TYR CB  CG   sing N N 404 
TYR CB  HB2  sing N N 405 
TYR CB  HB3  sing N N 406 
TYR CG  CD1  doub Y N 407 
TYR CG  CD2  sing Y N 408 
TYR CD1 CE1  sing Y N 409 
TYR CD1 HD1  sing N N 410 
TYR CD2 CE2  doub Y N 411 
TYR CD2 HD2  sing N N 412 
TYR CE1 CZ   doub Y N 413 
TYR CE1 HE1  sing N N 414 
TYR CE2 CZ   sing Y N 415 
TYR CE2 HE2  sing N N 416 
TYR CZ  OH   sing N N 417 
TYR OH  HH   sing N N 418 
TYR OXT HXT  sing N N 419 
VAL N   CA   sing N N 420 
VAL N   H    sing N N 421 
VAL N   H2   sing N N 422 
VAL CA  C    sing N N 423 
VAL CA  CB   sing N N 424 
VAL CA  HA   sing N N 425 
VAL C   O    doub N N 426 
VAL C   OXT  sing N N 427 
VAL CB  CG1  sing N N 428 
VAL CB  CG2  sing N N 429 
VAL CB  HB   sing N N 430 
VAL CG1 HG11 sing N N 431 
VAL CG1 HG12 sing N N 432 
VAL CG1 HG13 sing N N 433 
VAL CG2 HG21 sing N N 434 
VAL CG2 HG22 sing N N 435 
VAL CG2 HG23 sing N N 436 
VAL OXT HXT  sing N N 437 
# 
_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   5LLA 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    6G5U 
_atom_sites.fract_transf_matrix[1][1]   0.017924 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.017151 
_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]   0.006221 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
# 
loop_
_atom_type.symbol 
C  
CL 
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . SER A 1 6   ? 28.181  -13.309 -11.968 1.00 32.98 ? 6   SER B N   1 
ATOM   2    C  CA  . SER A 1 6   ? 27.570  -12.168 -12.709 1.00 31.99 ? 6   SER B CA  1 
ATOM   3    C  C   . SER A 1 6   ? 27.698  -10.901 -11.831 1.00 29.67 ? 6   SER B C   1 
ATOM   4    O  O   . SER A 1 6   ? 27.773  -10.984 -10.575 1.00 29.58 ? 6   SER B O   1 
ATOM   5    C  CB  . SER A 1 6   ? 26.122  -12.480 -13.066 1.00 37.33 ? 6   SER B CB  1 
ATOM   6    O  OG  . SER A 1 6   ? 25.763  -11.868 -14.302 1.00 48.68 ? 6   SER B OG  1 
ATOM   7    N  N   . TRP A 1 7   ? 27.748  -9.745  -12.483 1.00 22.42 ? 7   TRP B N   1 
ATOM   8    C  CA  . TRP A 1 7   ? 27.992  -8.487  -11.801 1.00 19.19 ? 7   TRP B CA  1 
ATOM   9    C  C   . TRP A 1 7   ? 26.961  -8.103  -10.749 1.00 18.31 ? 7   TRP B C   1 
ATOM   10   O  O   . TRP A 1 7   ? 25.795  -8.503  -10.849 1.00 18.63 ? 7   TRP B O   1 
ATOM   11   C  CB  . TRP A 1 7   ? 28.097  -7.372  -12.835 1.00 16.56 ? 7   TRP B CB  1 
ATOM   12   C  CG  . TRP A 1 7   ? 26.770  -6.976  -13.453 1.00 16.78 ? 7   TRP B CG  1 
ATOM   13   C  CD1 . TRP A 1 7   ? 26.179  -7.508  -14.560 1.00 17.93 ? 7   TRP B CD1 1 
ATOM   14   C  CD2 . TRP A 1 7   ? 25.920  -5.928  -12.991 1.00 15.71 ? 7   TRP B CD2 1 
ATOM   15   N  NE1 . TRP A 1 7   ? 24.969  -6.853  -14.807 1.00 18.93 ? 7   TRP B NE1 1 
ATOM   16   C  CE2 . TRP A 1 7   ? 24.812  -5.871  -13.849 1.00 17.42 ? 7   TRP B CE2 1 
ATOM   17   C  CE3 . TRP A 1 7   ? 25.996  -5.030  -11.922 1.00 17.47 ? 7   TRP B CE3 1 
ATOM   18   C  CZ2 . TRP A 1 7   ? 23.760  -4.919  -13.668 1.00 16.31 ? 7   TRP B CZ2 1 
ATOM   19   C  CZ3 . TRP A 1 7   ? 24.986  -4.099  -11.742 1.00 18.73 ? 7   TRP B CZ3 1 
ATOM   20   C  CH2 . TRP A 1 7   ? 23.882  -4.054  -12.613 1.00 17.15 ? 7   TRP B CH2 1 
ATOM   21   N  N   . GLY A 1 8   ? 27.395  -7.275  -9.785  1.00 15.25 ? 8   GLY B N   1 
ATOM   22   C  CA  . GLY A 1 8   ? 26.485  -6.817  -8.727  1.00 15.79 ? 8   GLY B CA  1 
ATOM   23   C  C   . GLY A 1 8   ? 27.145  -5.664  -7.999  1.00 15.64 ? 8   GLY B C   1 
ATOM   24   O  O   . GLY A 1 8   ? 27.945  -4.896  -8.605  1.00 15.30 ? 8   GLY B O   1 
ATOM   25   N  N   . TYR A 1 9   ? 26.865  -5.564  -6.690  1.00 13.27 ? 9   TYR B N   1 
ATOM   26   C  CA  . TYR A 1 9   ? 27.417  -4.487  -5.879  1.00 14.44 ? 9   TYR B CA  1 
ATOM   27   C  C   . TYR A 1 9   ? 28.047  -5.042  -4.601  1.00 16.99 ? 9   TYR B C   1 
ATOM   28   O  O   . TYR A 1 9   ? 28.288  -4.267  -3.674  1.00 16.32 ? 9   TYR B O   1 
ATOM   29   C  CB  . TYR A 1 9   ? 26.306  -3.487  -5.496  1.00 13.33 ? 9   TYR B CB  1 
ATOM   30   C  CG  . TYR A 1 9   ? 25.747  -2.794  -6.701  1.00 12.35 ? 9   TYR B CG  1 
ATOM   31   C  CD1 . TYR A 1 9   ? 26.344  -1.602  -7.156  1.00 13.55 ? 9   TYR B CD1 1 
ATOM   32   C  CD2 . TYR A 1 9   ? 24.583  -3.272  -7.353  1.00 11.51 ? 9   TYR B CD2 1 
ATOM   33   C  CE1 . TYR A 1 9   ? 25.815  -0.899  -8.270  1.00 11.90 ? 9   TYR B CE1 1 
ATOM   34   C  CE2 . TYR A 1 9   ? 24.052  -2.576  -8.461  1.00 11.27 ? 9   TYR B CE2 1 
ATOM   35   C  CZ  . TYR A 1 9   ? 24.698  -1.401  -8.886  1.00 11.13 ? 9   TYR B CZ  1 
ATOM   36   O  OH  . TYR A 1 9   ? 24.173  -0.705  -9.928  1.00 11.97 ? 9   TYR B OH  1 
ATOM   37   N  N   . ARG A 1 10  ? 28.261  -6.375  -4.585  1.00 17.22 ? 10  ARG B N   1 
ATOM   38   C  CA  . ARG A 1 10  ? 28.866  -7.070  -3.440  1.00 19.39 ? 10  ARG B CA  1 
ATOM   39   C  C   . ARG A 1 10  ? 30.401  -6.956  -3.574  1.00 23.06 ? 10  ARG B C   1 
ATOM   40   O  O   . ARG A 1 10  ? 30.916  -6.414  -4.559  1.00 20.18 ? 10  ARG B O   1 
ATOM   41   C  CB  . ARG A 1 10  ? 28.354  -8.531  -3.378  1.00 18.82 ? 10  ARG B CB  1 
ATOM   42   C  CG  . ARG A 1 10  ? 26.835  -8.663  -3.224  1.00 19.36 ? 10  ARG B CG  1 
ATOM   43   C  CD  . ARG A 1 10  ? 26.363  -10.100 -3.346  1.00 21.57 ? 10  ARG B CD  1 
ATOM   44   N  NE  . ARG A 1 10  ? 26.680  -10.895 -2.154  1.00 24.18 ? 10  ARG B NE  1 
ATOM   45   C  CZ  . ARG A 1 10  ? 26.280  -12.161 -1.955  1.00 24.52 ? 10  ARG B CZ  1 
ATOM   46   N  NH1 . ARG A 1 10  ? 25.579  -12.800 -2.884  1.00 24.86 ? 10  ARG B NH1 1 
ATOM   47   N  NH2 . ARG A 1 10  ? 26.598  -12.791 -0.819  1.00 23.71 ? 10  ARG B NH2 1 
ATOM   48   N  N   . GLU A 1 11  ? 31.137  -7.446  -2.569  1.00 25.04 ? 11  GLU B N   1 
ATOM   49   C  CA  . GLU A 1 11  ? 32.605  -7.347  -2.582  1.00 26.62 ? 11  GLU B CA  1 
ATOM   50   C  C   . GLU A 1 11  ? 33.271  -7.844  -3.880  1.00 25.02 ? 11  GLU B C   1 
ATOM   51   O  O   . GLU A 1 11  ? 34.037  -7.128  -4.469  1.00 22.74 ? 11  GLU B O   1 
ATOM   52   C  CB  . GLU A 1 11  ? 33.170  -8.124  -1.378  1.00 31.03 ? 11  GLU B CB  1 
ATOM   53   C  CG  . GLU A 1 11  ? 34.695  -8.138  -1.287  1.00 35.05 ? 11  GLU B CG  1 
ATOM   54   C  CD  . GLU A 1 11  ? 35.211  -8.964  -0.091  1.00 44.53 ? 11  GLU B CD  1 
ATOM   55   O  OE1 . GLU A 1 11  ? 36.450  -9.022  0.088   1.00 44.61 ? 11  GLU B OE1 1 
ATOM   56   O  OE2 . GLU A 1 11  ? 34.393  -9.555  0.674   1.00 48.21 ? 11  GLU B OE2 1 
ATOM   57   N  N   . HIS A 1 12  ? 32.956  -9.064  -4.311  1.00 23.49 ? 12  HIS B N   1 
ATOM   58   C  CA  . HIS A 1 12  ? 33.710  -9.673  -5.405  1.00 24.46 ? 12  HIS B CA  1 
ATOM   59   C  C   . HIS A 1 12  ? 33.122  -9.371  -6.751  1.00 22.69 ? 12  HIS B C   1 
ATOM   60   O  O   . HIS A 1 12  ? 33.783  -9.608  -7.795  1.00 21.01 ? 12  HIS B O   1 
ATOM   61   C  CB  . HIS A 1 12  ? 33.778  -11.192 -5.218  1.00 31.85 ? 12  HIS B CB  1 
ATOM   62   C  CG  . HIS A 1 12  ? 34.352  -11.597 -3.896  1.00 33.00 ? 12  HIS B CG  1 
ATOM   63   N  ND1 . HIS A 1 12  ? 35.648  -11.289 -3.525  1.00 38.11 ? 12  HIS B ND1 1 
ATOM   64   C  CD2 . HIS A 1 12  ? 33.804  -12.271 -2.852  1.00 34.69 ? 12  HIS B CD2 1 
ATOM   65   C  CE1 . HIS A 1 12  ? 35.872  -11.758 -2.307  1.00 39.22 ? 12  HIS B CE1 1 
ATOM   66   N  NE2 . HIS A 1 12  ? 34.770  -12.358 -1.878  1.00 39.14 ? 12  HIS B NE2 1 
ATOM   67   N  N   . ASN A 1 13  ? 31.890  -8.857  -6.782  1.00 18.04 ? 13  ASN B N   1 
ATOM   68   C  CA  . ASN A 1 13  ? 31.318  -8.605  -8.101  1.00 17.20 ? 13  ASN B CA  1 
ATOM   69   C  C   . ASN A 1 13  ? 30.981  -7.152  -8.324  1.00 16.53 ? 13  ASN B C   1 
ATOM   70   O  O   . ASN A 1 13  ? 30.368  -6.809  -9.346  1.00 15.07 ? 13  ASN B O   1 
ATOM   71   C  CB  . ASN A 1 13  ? 30.119  -9.510  -8.390  1.00 18.62 ? 13  ASN B CB  1 
ATOM   72   C  CG  . ASN A 1 13  ? 28.906  -9.179  -7.511  1.00 21.24 ? 13  ASN B CG  1 
ATOM   73   O  OD1 . ASN A 1 13  ? 28.941  -8.260  -6.666  1.00 20.52 ? 13  ASN B OD1 1 
ATOM   74   N  ND2 . ASN A 1 13  ? 27.827  -9.922  -7.716  1.00 20.47 ? 13  ASN B ND2 1 
ATOM   75   N  N   . GLY A 1 14  ? 31.350  -6.309  -7.361  1.00 14.86 ? 14  GLY B N   1 
ATOM   76   C  CA  . GLY A 1 14  ? 30.956  -4.874  -7.428  1.00 15.90 ? 14  GLY B CA  1 
ATOM   77   C  C   . GLY A 1 14  ? 31.723  -3.998  -8.386  1.00 15.85 ? 14  GLY B C   1 
ATOM   78   O  O   . GLY A 1 14  ? 32.589  -4.462  -9.144  1.00 16.62 ? 14  GLY B O   1 
ATOM   79   N  N   . PRO A 1 15  ? 31.445  -2.670  -8.338  1.00 15.77 ? 15  PRO B N   1 
ATOM   80   C  CA  . PRO A 1 15  ? 31.952  -1.703  -9.314  1.00 15.01 ? 15  PRO B CA  1 
ATOM   81   C  C   . PRO A 1 15  ? 33.450  -1.770  -9.627  1.00 16.58 ? 15  PRO B C   1 
ATOM   82   O  O   . PRO A 1 15  ? 33.830  -1.687  -10.788 1.00 16.98 ? 15  PRO B O   1 
ATOM   83   C  CB  . PRO A 1 15  ? 31.537  -0.369  -8.687  1.00 14.04 ? 15  PRO B CB  1 
ATOM   84   C  CG  . PRO A 1 15  ? 30.192  -0.708  -8.106  1.00 14.27 ? 15  PRO B CG  1 
ATOM   85   C  CD  . PRO A 1 15  ? 30.476  -2.030  -7.404  1.00 14.42 ? 15  PRO B CD  1 
ATOM   86   N  N   . ILE A 1 16  ? 34.292  -1.935  -8.589  1.00 19.37 ? 16  ILE B N   1 
ATOM   87   C  CA  . ILE A 1 16  ? 35.726  -2.064  -8.786  1.00 21.04 ? 16  ILE B CA  1 
ATOM   88   C  C   . ILE A 1 16  ? 36.157  -3.211  -9.723  1.00 21.22 ? 16  ILE B C   1 
ATOM   89   O  O   . ILE A 1 16  ? 37.202  -3.138  -10.336 1.00 21.22 ? 16  ILE B O   1 
ATOM   90   C  CB  . ILE A 1 16  ? 36.512  -2.046  -7.401  1.00 24.61 ? 16  ILE B CB  1 
ATOM   91   C  CG1 . ILE A 1 16  ? 37.983  -1.644  -7.585  1.00 31.14 ? 16  ILE B CG1 1 
ATOM   92   C  CG2 . ILE A 1 16  ? 36.483  -3.398  -6.670  1.00 26.08 ? 16  ILE B CG2 1 
ATOM   93   C  CD1 . ILE A 1 16  ? 38.181  -0.172  -7.919  1.00 37.84 ? 16  ILE B CD1 1 
ATOM   94   N  N   . HIS A 1 17  ? 35.332  -4.255  -9.825  1.00 20.66 ? 17  HIS B N   1 
ATOM   95   C  CA  . HIS A 1 17  ? 35.623  -5.474  -10.596 1.00 20.56 ? 17  HIS B CA  1 
ATOM   96   C  C   . HIS A 1 17  ? 34.910  -5.453  -11.942 1.00 21.34 ? 17  HIS B C   1 
ATOM   97   O  O   . HIS A 1 17  ? 35.148  -6.341  -12.785 1.00 20.95 ? 17  HIS B O   1 
ATOM   98   C  CB  . HIS A 1 17  ? 35.200  -6.739  -9.836  1.00 21.39 ? 17  HIS B CB  1 
ATOM   99   C  CG  . HIS A 1 17  ? 35.874  -6.887  -8.520  1.00 25.84 ? 17  HIS B CG  1 
ATOM   100  N  ND1 . HIS A 1 17  ? 37.198  -7.257  -8.406  1.00 29.41 ? 17  HIS B ND1 1 
ATOM   101  C  CD2 . HIS A 1 17  ? 35.424  -6.684  -7.265  1.00 25.83 ? 17  HIS B CD2 1 
ATOM   102  C  CE1 . HIS A 1 17  ? 37.538  -7.266  -7.128  1.00 29.45 ? 17  HIS B CE1 1 
ATOM   103  N  NE2 . HIS A 1 17  ? 36.475  -6.934  -6.415  1.00 30.49 ? 17  HIS B NE2 1 
ATOM   104  N  N   . TRP A 1 18  ? 34.059  -4.440  -12.200 1.00 18.49 ? 18  TRP B N   1 
ATOM   105  C  CA  . TRP A 1 18  ? 33.349  -4.483  -13.471 1.00 17.58 ? 18  TRP B CA  1 
ATOM   106  C  C   . TRP A 1 18  ? 34.246  -4.469  -14.699 1.00 19.17 ? 18  TRP B C   1 
ATOM   107  O  O   . TRP A 1 18  ? 33.892  -5.092  -15.732 1.00 21.00 ? 18  TRP B O   1 
ATOM   108  C  CB  . TRP A 1 18  ? 32.251  -3.375  -13.587 1.00 15.87 ? 18  TRP B CB  1 
ATOM   109  C  CG  . TRP A 1 18  ? 31.137  -3.538  -12.590 1.00 14.59 ? 18  TRP B CG  1 
ATOM   110  C  CD1 . TRP A 1 18  ? 30.831  -4.629  -11.789 1.00 15.41 ? 18  TRP B CD1 1 
ATOM   111  C  CD2 . TRP A 1 18  ? 30.172  -2.546  -12.290 1.00 13.50 ? 18  TRP B CD2 1 
ATOM   112  N  NE1 . TRP A 1 18  ? 29.720  -4.342  -11.004 1.00 16.10 ? 18  TRP B NE1 1 
ATOM   113  C  CE2 . TRP A 1 18  ? 29.315  -3.064  -11.298 1.00 13.07 ? 18  TRP B CE2 1 
ATOM   114  C  CE3 . TRP A 1 18  ? 29.961  -1.217  -12.764 1.00 13.24 ? 18  TRP B CE3 1 
ATOM   115  C  CZ2 . TRP A 1 18  ? 28.197  -2.309  -10.778 1.00 13.40 ? 18  TRP B CZ2 1 
ATOM   116  C  CZ3 . TRP A 1 18  ? 28.881  -0.464  -12.235 1.00 13.62 ? 18  TRP B CZ3 1 
ATOM   117  C  CH2 . TRP A 1 18  ? 28.019  -1.010  -11.261 1.00 13.58 ? 18  TRP B CH2 1 
ATOM   118  N  N   . LYS A 1 19  ? 35.345  -3.736  -14.598 1.00 18.66 ? 19  LYS B N   1 
ATOM   119  C  CA  . LYS A 1 19  ? 36.358  -3.669  -15.688 1.00 20.54 ? 19  LYS B CA  1 
ATOM   120  C  C   . LYS A 1 19  ? 36.828  -5.090  -16.056 1.00 20.49 ? 19  LYS B C   1 
ATOM   121  O  O   . LYS A 1 19  ? 37.241  -5.308  -17.178 1.00 23.66 ? 19  LYS B O   1 
ATOM   122  C  CB  . LYS A 1 19  ? 37.550  -2.800  -15.304 1.00 23.59 ? 19  LYS B CB  1 
ATOM   123  C  CG  . LYS A 1 19  ? 38.347  -3.292  -14.091 1.00 24.97 ? 19  LYS B CG  1 
ATOM   124  C  CD  . LYS A 1 19  ? 39.768  -2.851  -14.232 1.00 31.36 ? 19  LYS B CD  1 
ATOM   125  C  CE  . LYS A 1 19  ? 40.060  -1.552  -13.517 1.00 38.69 ? 19  LYS B CE  1 
ATOM   126  N  NZ  . LYS A 1 19  ? 41.488  -1.180  -13.790 1.00 46.72 ? 19  LYS B NZ  1 
ATOM   127  N  N   . GLU A 1 20  ? 36.717  -6.051  -15.151 1.00 24.59 ? 20  GLU B N   1 
ATOM   128  C  CA  . GLU A 1 20  ? 37.200  -7.405  -15.458 1.00 27.68 ? 20  GLU B CA  1 
ATOM   129  C  C   . GLU A 1 20  ? 36.424  -8.014  -16.622 1.00 32.58 ? 20  GLU B C   1 
ATOM   130  O  O   . GLU A 1 20  ? 37.053  -8.489  -17.583 1.00 36.33 ? 20  GLU B O   1 
ATOM   131  C  CB  . GLU A 1 20  ? 37.281  -8.269  -14.208 1.00 26.70 ? 20  GLU B CB  1 
ATOM   132  C  CG  . GLU A 1 20  ? 38.307  -7.716  -13.183 1.00 28.27 ? 20  GLU B CG  1 
ATOM   133  C  CD  . GLU A 1 20  ? 38.074  -8.234  -11.782 1.00 27.72 ? 20  GLU B CD  1 
ATOM   134  O  OE1 . GLU A 1 20  ? 37.378  -9.272  -11.629 1.00 28.71 ? 20  GLU B OE1 1 
ATOM   135  O  OE2 . GLU A 1 20  ? 38.536  -7.589  -10.816 1.00 29.87 ? 20  GLU B OE2 1 
ATOM   136  N  N   . PHE A 1 21  ? 35.093  -7.892  -16.602 1.00 35.06 ? 21  PHE B N   1 
ATOM   137  C  CA  . PHE A 1 21  ? 34.241  -8.436  -17.671 1.00 35.47 ? 21  PHE B CA  1 
ATOM   138  C  C   . PHE A 1 21  ? 33.738  -7.382  -18.696 1.00 29.98 ? 21  PHE B C   1 
ATOM   139  O  O   . PHE A 1 21  ? 33.248  -7.755  -19.751 1.00 30.19 ? 21  PHE B O   1 
ATOM   140  C  CB  . PHE A 1 21  ? 33.045  -9.247  -17.128 1.00 45.84 ? 21  PHE B CB  1 
ATOM   141  C  CG  . PHE A 1 21  ? 33.100  -9.623  -15.636 1.00 64.53 ? 21  PHE B CG  1 
ATOM   142  C  CD1 . PHE A 1 21  ? 32.783  -8.672  -14.613 1.00 69.29 ? 21  PHE B CD1 1 
ATOM   143  C  CD2 . PHE A 1 21  ? 33.337  -10.959 -15.238 1.00 72.34 ? 21  PHE B CD2 1 
ATOM   144  C  CE1 . PHE A 1 21  ? 32.774  -9.031  -13.247 1.00 76.74 ? 21  PHE B CE1 1 
ATOM   145  C  CE2 . PHE A 1 21  ? 33.330  -11.316 -13.872 1.00 76.23 ? 21  PHE B CE2 1 
ATOM   146  C  CZ  . PHE A 1 21  ? 33.052  -10.353 -12.880 1.00 78.83 ? 21  PHE B CZ  1 
ATOM   147  N  N   . PHE A 1 22  ? 33.816  -6.085  -18.381 1.00 24.05 ? 22  PHE B N   1 
ATOM   148  C  CA  . PHE A 1 22  ? 33.378  -4.988  -19.316 1.00 23.18 ? 22  PHE B CA  1 
ATOM   149  C  C   . PHE A 1 22  ? 34.443  -3.920  -19.317 1.00 22.29 ? 22  PHE B C   1 
ATOM   150  O  O   . PHE A 1 22  ? 34.430  -3.003  -18.478 1.00 22.71 ? 22  PHE B O   1 
ATOM   151  C  CB  . PHE A 1 22  ? 32.008  -4.384  -18.965 1.00 23.50 ? 22  PHE B CB  1 
ATOM   152  C  CG  . PHE A 1 22  ? 30.981  -5.394  -18.641 1.00 22.43 ? 22  PHE B CG  1 
ATOM   153  C  CD1 . PHE A 1 22  ? 30.853  -5.908  -17.342 1.00 24.37 ? 22  PHE B CD1 1 
ATOM   154  C  CD2 . PHE A 1 22  ? 30.166  -5.888  -19.659 1.00 22.45 ? 22  PHE B CD2 1 
ATOM   155  C  CE1 . PHE A 1 22  ? 29.903  -6.901  -17.064 1.00 24.79 ? 22  PHE B CE1 1 
ATOM   156  C  CE2 . PHE A 1 22  ? 29.238  -6.860  -19.389 1.00 21.59 ? 22  PHE B CE2 1 
ATOM   157  C  CZ  . PHE A 1 22  ? 29.081  -7.352  -18.099 1.00 24.42 ? 22  PHE B CZ  1 
ATOM   158  N  N   . PRO A 1 23  ? 35.441  -4.050  -20.196 1.00 21.17 ? 23  PRO B N   1 
ATOM   159  C  CA  . PRO A 1 23  ? 36.598  -3.160  -20.252 1.00 20.51 ? 23  PRO B CA  1 
ATOM   160  C  C   . PRO A 1 23  ? 36.240  -1.720  -20.454 1.00 21.04 ? 23  PRO B C   1 
ATOM   161  O  O   . PRO A 1 23  ? 37.038  -0.841  -20.117 1.00 22.65 ? 23  PRO B O   1 
ATOM   162  C  CB  . PRO A 1 23  ? 37.330  -3.592  -21.532 1.00 21.30 ? 23  PRO B CB  1 
ATOM   163  C  CG  . PRO A 1 23  ? 36.893  -4.966  -21.750 1.00 23.13 ? 23  PRO B CG  1 
ATOM   164  C  CD  . PRO A 1 23  ? 35.621  -5.257  -21.036 1.00 23.16 ? 23  PRO B CD  1 
ATOM   165  N  N   . ILE A 1 24  ? 35.065  -1.471  -21.057 1.00 18.02 ? 24  ILE B N   1 
ATOM   166  C  CA  . ILE A 1 24  ? 34.653  -0.076  -21.254 1.00 16.90 ? 24  ILE B CA  1 
ATOM   167  C  C   . ILE A 1 24  ? 34.483  0.671   -19.893 1.00 16.33 ? 24  ILE B C   1 
ATOM   168  O  O   . ILE A 1 24  ? 34.426  1.895   -19.861 1.00 16.61 ? 24  ILE B O   1 
ATOM   169  C  CB  . ILE A 1 24  ? 33.411  0.052   -22.201 1.00 16.37 ? 24  ILE B CB  1 
ATOM   170  C  CG1 . ILE A 1 24  ? 33.289  1.471   -22.743 1.00 19.07 ? 24  ILE B CG1 1 
ATOM   171  C  CG2 . ILE A 1 24  ? 32.122  -0.319  -21.459 1.00 16.34 ? 24  ILE B CG2 1 
ATOM   172  C  CD1 . ILE A 1 24  ? 34.541  2.025   -23.392 1.00 21.41 ? 24  ILE B CD1 1 
ATOM   173  N  N   . ALA A 1 25  ? 34.440  -0.081  -18.780 1.00 17.57 ? 25  ALA B N   1 
ATOM   174  C  CA  . ALA A 1 25  ? 34.400  0.532   -17.467 1.00 17.81 ? 25  ALA B CA  1 
ATOM   175  C  C   . ALA A 1 25  ? 35.445  1.588   -17.231 1.00 20.59 ? 25  ALA B C   1 
ATOM   176  O  O   . ALA A 1 25  ? 35.193  2.496   -16.474 1.00 17.82 ? 25  ALA B O   1 
ATOM   177  C  CB  . ALA A 1 25  ? 34.481  -0.500  -16.366 1.00 17.15 ? 25  ALA B CB  1 
ATOM   178  N  N   . ASP A 1 26  ? 36.611  1.472   -17.904 1.00 21.21 ? 26  ASP B N   1 
ATOM   179  C  CA  . ASP A 1 26  ? 37.655  2.473   -17.818 1.00 22.42 ? 26  ASP B CA  1 
ATOM   180  C  C   . ASP A 1 26  ? 37.689  3.419   -18.986 1.00 20.69 ? 26  ASP B C   1 
ATOM   181  O  O   . ASP A 1 26  ? 38.708  4.024   -19.256 1.00 23.66 ? 26  ASP B O   1 
ATOM   182  C  CB  . ASP A 1 26  ? 39.007  1.749   -17.667 1.00 25.98 ? 26  ASP B CB  1 
ATOM   183  C  CG  . ASP A 1 26  ? 39.070  0.979   -16.392 1.00 30.45 ? 26  ASP B CG  1 
ATOM   184  O  OD1 . ASP A 1 26  ? 38.710  1.568   -15.344 1.00 27.82 ? 26  ASP B OD1 1 
ATOM   185  O  OD2 . ASP A 1 26  ? 39.420  -0.217  -16.451 1.00 32.88 ? 26  ASP B OD2 1 
ATOM   186  N  N   . GLY A 1 27  ? 36.568  3.583   -19.684 1.00 19.79 ? 27  GLY B N   1 
ATOM   187  C  CA  . GLY A 1 27  ? 36.519  4.504   -20.835 1.00 18.40 ? 27  GLY B CA  1 
ATOM   188  C  C   . GLY A 1 27  ? 36.547  5.976   -20.523 1.00 19.00 ? 27  GLY B C   1 
ATOM   189  O  O   . GLY A 1 27  ? 36.578  6.339   -19.349 1.00 19.70 ? 27  GLY B O   1 
ATOM   190  N  N   . ASP A 1 28  ? 36.459  6.810   -21.571 1.00 19.46 ? 28  ASP B N   1 
ATOM   191  C  CA  . ASP A 1 28  ? 36.588  8.240   -21.428 1.00 20.22 ? 28  ASP B CA  1 
ATOM   192  C  C   . ASP A 1 28  ? 35.224  8.884   -21.309 1.00 16.87 ? 28  ASP B C   1 
ATOM   193  O  O   . ASP A 1 28  ? 35.162  10.100  -21.151 1.00 15.61 ? 28  ASP B O   1 
ATOM   194  C  CB  . ASP A 1 28  ? 37.251  8.916   -22.654 1.00 27.71 ? 28  ASP B CB  1 
ATOM   195  C  CG  . ASP A 1 28  ? 38.776  8.616   -22.800 1.00 34.86 ? 28  ASP B CG  1 
ATOM   196  O  OD1 . ASP A 1 28  ? 39.473  8.421   -21.779 1.00 29.88 ? 28  ASP B OD1 1 
ATOM   197  O  OD2 . ASP A 1 28  ? 39.259  8.635   -23.972 1.00 39.08 ? 28  ASP B OD2 1 
ATOM   198  N  N   . GLN A 1 29  ? 34.132  8.107   -21.439 1.00 15.24 ? 29  GLN B N   1 
ATOM   199  C  CA  . GLN A 1 29  ? 32.814  8.776   -21.303 1.00 15.71 ? 29  GLN B CA  1 
ATOM   200  C  C   . GLN A 1 29  ? 31.954  8.013   -20.297 1.00 13.56 ? 29  GLN B C   1 
ATOM   201  O  O   . GLN A 1 29  ? 30.829  7.650   -20.577 1.00 13.96 ? 29  GLN B O   1 
ATOM   202  C  CB  . GLN A 1 29  ? 32.077  8.943   -22.652 1.00 17.74 ? 29  GLN B CB  1 
ATOM   203  C  CG  . GLN A 1 29  ? 32.924  9.770   -23.648 1.00 23.10 ? 29  GLN B CG  1 
ATOM   204  C  CD  . GLN A 1 29  ? 32.108  10.777  -24.443 1.00 27.20 ? 29  GLN B CD  1 
ATOM   205  O  OE1 . GLN A 1 29  ? 31.019  10.433  -24.960 1.00 24.63 ? 29  GLN B OE1 1 
ATOM   206  N  NE2 . GLN A 1 29  ? 32.611  12.056  -24.520 1.00 27.47 ? 29  GLN B NE2 1 
ATOM   207  N  N   . GLN A 1 30  ? 32.505  7.755   -19.113 1.00 12.19 ? 30  GLN B N   1 
ATOM   208  C  CA  . GLN A 1 30  ? 31.797  6.929   -18.105 1.00 10.93 ? 30  GLN B CA  1 
ATOM   209  C  C   . GLN A 1 30  ? 31.007  7.774   -17.109 1.00 10.19 ? 30  GLN B C   1 
ATOM   210  O  O   . GLN A 1 30  ? 31.285  8.972   -16.911 1.00 10.86 ? 30  GLN B O   1 
ATOM   211  C  CB  . GLN A 1 30  ? 32.805  6.007   -17.364 1.00 11.34 ? 30  GLN B CB  1 
ATOM   212  C  CG  . GLN A 1 30  ? 33.368  4.851   -18.214 1.00 11.65 ? 30  GLN B CG  1 
ATOM   213  C  CD  . GLN A 1 30  ? 32.328  3.865   -18.530 1.00 11.38 ? 30  GLN B CD  1 
ATOM   214  O  OE1 . GLN A 1 30  ? 31.791  3.174   -17.636 1.00 11.26 ? 30  GLN B OE1 1 
ATOM   215  N  NE2 . GLN A 1 30  ? 31.968  3.788   -19.800 1.00 11.13 ? 30  GLN B NE2 1 
ATOM   216  N  N   . SER A 1 31  ? 29.957  7.141   -16.579 1.00 10.01 ? 31  SER B N   1 
ATOM   217  C  CA  . SER A 1 31  ? 29.018  7.762   -15.640 1.00 9.09  ? 31  SER B CA  1 
ATOM   218  C  C   . SER A 1 31  ? 28.875  6.891   -14.398 1.00 9.29  ? 31  SER B C   1 
ATOM   219  O  O   . SER A 1 31  ? 29.096  5.694   -14.437 1.00 11.65 ? 31  SER B O   1 
ATOM   220  C  CB  . SER A 1 31  ? 27.627  7.895   -16.381 1.00 9.13  ? 31  SER B CB  1 
ATOM   221  O  OG  . SER A 1 31  ? 27.781  8.858   -17.432 1.00 9.26  ? 31  SER B OG  1 
ATOM   222  N  N   . PRO A 1 32  ? 28.477  7.481   -13.272 1.00 9.22  ? 32  PRO B N   1 
ATOM   223  C  CA  . PRO A 1 32  ? 28.159  8.847   -13.068 1.00 9.13  ? 32  PRO B CA  1 
ATOM   224  C  C   . PRO A 1 32  ? 29.391  9.717   -12.764 1.00 9.00  ? 32  PRO B C   1 
ATOM   225  O  O   . PRO A 1 32  ? 30.549  9.247   -12.830 1.00 9.27  ? 32  PRO B O   1 
ATOM   226  C  CB  . PRO A 1 32  ? 27.280  8.768   -11.822 1.00 9.23  ? 32  PRO B CB  1 
ATOM   227  C  CG  . PRO A 1 32  ? 28.040  7.724   -10.976 1.00 8.79  ? 32  PRO B CG  1 
ATOM   228  C  CD  . PRO A 1 32  ? 28.309  6.673   -12.050 1.00 9.51  ? 32  PRO B CD  1 
ATOM   229  N  N   . ILE A 1 33  ? 29.141  10.986  -12.473 1.00 9.60  ? 33  ILE B N   1 
ATOM   230  C  CA  . ILE A 1 33  ? 30.204  11.968  -12.245 1.00 9.95  ? 33  ILE B CA  1 
ATOM   231  C  C   . ILE A 1 33  ? 29.889  12.918  -11.080 1.00 10.49 ? 33  ILE B C   1 
ATOM   232  O  O   . ILE A 1 33  ? 28.705  13.062  -10.618 1.00 10.07 ? 33  ILE B O   1 
ATOM   233  C  CB  . ILE A 1 33  ? 30.527  12.912  -13.452 1.00 10.28 ? 33  ILE B CB  1 
ATOM   234  C  CG1 . ILE A 1 33  ? 29.282  13.716  -13.866 1.00 10.09 ? 33  ILE B CG1 1 
ATOM   235  C  CG2 . ILE A 1 33  ? 31.034  12.099  -14.668 1.00 9.88  ? 33  ILE B CG2 1 
ATOM   236  C  CD1 . ILE A 1 33  ? 29.574  14.899  -14.712 1.00 10.61 ? 33  ILE B CD1 1 
ATOM   237  N  N   A GLU A 1 34  ? 30.974  13.529  -10.609 0.50 11.00 ? 34  GLU B N   1 
ATOM   238  N  N   B GLU A 1 34  ? 30.953  13.538  -10.575 0.50 10.00 ? 34  GLU B N   1 
ATOM   239  C  CA  A GLU A 1 34  ? 30.983  14.737  -9.805  0.50 11.81 ? 34  GLU B CA  1 
ATOM   240  C  CA  B GLU A 1 34  ? 30.852  14.700  -9.705  0.50 10.17 ? 34  GLU B CA  1 
ATOM   241  C  C   A GLU A 1 34  ? 30.585  15.965  -10.618 0.50 11.60 ? 34  GLU B C   1 
ATOM   242  C  C   B GLU A 1 34  ? 30.586  15.942  -10.552 0.50 10.62 ? 34  GLU B C   1 
ATOM   243  O  O   A GLU A 1 34  ? 31.207  16.250  -11.643 0.50 12.34 ? 34  GLU B O   1 
ATOM   244  O  O   B GLU A 1 34  ? 31.269  16.187  -11.543 0.50 11.53 ? 34  GLU B O   1 
ATOM   245  C  CB  A GLU A 1 34  ? 32.420  14.914  -9.283  0.50 13.38 ? 34  GLU B CB  1 
ATOM   246  C  CB  B GLU A 1 34  ? 32.158  14.825  -8.902  0.50 10.17 ? 34  GLU B CB  1 
ATOM   247  C  CG  A GLU A 1 34  ? 32.720  14.106  -8.038  0.50 16.30 ? 34  GLU B CG  1 
ATOM   248  C  CG  B GLU A 1 34  ? 32.346  16.127  -8.132  0.50 9.79  ? 34  GLU B CG  1 
ATOM   249  C  CD  A GLU A 1 34  ? 32.065  14.642  -6.755  0.50 16.16 ? 34  GLU B CD  1 
ATOM   250  C  CD  B GLU A 1 34  ? 31.457  16.226  -6.904  0.50 10.64 ? 34  GLU B CD  1 
ATOM   251  O  OE1 A GLU A 1 34  ? 31.304  15.671  -6.741  0.50 20.50 ? 34  GLU B OE1 1 
ATOM   252  O  OE1 B GLU A 1 34  ? 31.507  15.289  -6.042  0.50 12.19 ? 34  GLU B OE1 1 
ATOM   253  O  OE2 A GLU A 1 34  ? 32.302  13.991  -5.749  0.50 15.48 ? 34  GLU B OE2 1 
ATOM   254  O  OE2 B GLU A 1 34  ? 30.749  17.215  -6.829  0.50 9.19  ? 34  GLU B OE2 1 
ATOM   255  N  N   . ILE A 1 35  ? 29.539  16.678  -10.180 1.00 11.70 ? 35  ILE B N   1 
ATOM   256  C  CA  . ILE A 1 35  ? 29.152  17.922  -10.876 1.00 12.51 ? 35  ILE B CA  1 
ATOM   257  C  C   . ILE A 1 35  ? 29.629  19.056  -10.001 1.00 13.92 ? 35  ILE B C   1 
ATOM   258  O  O   . ILE A 1 35  ? 29.078  19.310  -8.918  1.00 12.85 ? 35  ILE B O   1 
ATOM   259  C  CB  . ILE A 1 35  ? 27.610  18.005  -11.103 1.00 13.59 ? 35  ILE B CB  1 
ATOM   260  C  CG1 . ILE A 1 35  ? 27.161  16.821  -12.014 1.00 14.03 ? 35  ILE B CG1 1 
ATOM   261  C  CG2 . ILE A 1 35  ? 27.246  19.379  -11.663 1.00 15.47 ? 35  ILE B CG2 1 
ATOM   262  C  CD1 . ILE A 1 35  ? 25.644  16.579  -12.046 1.00 12.74 ? 35  ILE B CD1 1 
ATOM   263  N  N   . LYS A 1 36  ? 30.719  19.705  -10.462 1.00 15.17 ? 36  LYS B N   1 
ATOM   264  C  CA  . LYS A 1 36  ? 31.252  20.861  -9.717  1.00 16.36 ? 36  LYS B CA  1 
ATOM   265  C  C   . LYS A 1 36  ? 30.690  22.090  -10.396 1.00 16.17 ? 36  LYS B C   1 
ATOM   266  O  O   . LYS A 1 36  ? 31.089  22.426  -11.497 1.00 16.77 ? 36  LYS B O   1 
ATOM   267  C  CB  . LYS A 1 36  ? 32.769  20.844  -9.711  1.00 18.05 ? 36  LYS B CB  1 
ATOM   268  C  CG  . LYS A 1 36  ? 33.371  19.629  -8.976  1.00 18.59 ? 36  LYS B CG  1 
ATOM   269  C  CD  . LYS A 1 36  ? 34.790  19.414  -9.546  1.00 21.86 ? 36  LYS B CD  1 
ATOM   270  C  CE  . LYS A 1 36  ? 35.789  19.345  -8.404  1.00 20.38 ? 36  LYS B CE  1 
ATOM   271  N  NZ  . LYS A 1 36  ? 37.207  19.179  -8.828  1.00 18.01 ? 36  LYS B NZ  1 
ATOM   272  N  N   . THR A 1 37  ? 29.695  22.677  -9.765  1.00 17.42 ? 37  THR B N   1 
ATOM   273  C  CA  . THR A 1 37  ? 28.906  23.774  -10.364 1.00 21.77 ? 37  THR B CA  1 
ATOM   274  C  C   . THR A 1 37  ? 29.730  24.969  -10.846 1.00 23.74 ? 37  THR B C   1 
ATOM   275  O  O   . THR A 1 37  ? 29.396  25.578  -11.865 1.00 24.20 ? 37  THR B O   1 
ATOM   276  C  CB  . THR A 1 37  ? 27.784  24.212  -9.467  1.00 22.13 ? 37  THR B CB  1 
ATOM   277  O  OG1 . THR A 1 37  ? 28.344  24.729  -8.266  1.00 24.06 ? 37  THR B OG1 1 
ATOM   278  C  CG2 . THR A 1 37  ? 26.821  22.995  -9.163  1.00 20.98 ? 37  THR B CG2 1 
ATOM   279  N  N   A LYS A 1 38  ? 30.825  25.282  -10.155 0.50 24.73 ? 38  LYS B N   1 
ATOM   280  N  N   B LYS A 1 38  ? 30.829  25.272  -10.158 0.50 25.21 ? 38  LYS B N   1 
ATOM   281  C  CA  A LYS A 1 38  ? 31.666  26.394  -10.610 0.50 26.43 ? 38  LYS B CA  1 
ATOM   282  C  CA  B LYS A 1 38  ? 31.681  26.378  -10.603 0.50 27.30 ? 38  LYS B CA  1 
ATOM   283  C  C   A LYS A 1 38  ? 32.320  26.103  -11.973 0.50 26.07 ? 38  LYS B C   1 
ATOM   284  C  C   B LYS A 1 38  ? 32.325  26.100  -11.970 0.50 26.59 ? 38  LYS B C   1 
ATOM   285  O  O   A LYS A 1 38  ? 32.685  27.047  -12.686 0.50 24.69 ? 38  LYS B O   1 
ATOM   286  O  O   B LYS A 1 38  ? 32.681  27.048  -12.683 0.50 25.15 ? 38  LYS B O   1 
ATOM   287  C  CB  A LYS A 1 38  ? 32.705  26.799  -9.554  0.50 29.39 ? 38  LYS B CB  1 
ATOM   288  C  CB  B LYS A 1 38  ? 32.726  26.751  -9.541  0.50 31.31 ? 38  LYS B CB  1 
ATOM   289  C  CG  A LYS A 1 38  ? 32.164  27.652  -8.410  0.50 29.98 ? 38  LYS B CG  1 
ATOM   290  C  CG  B LYS A 1 38  ? 32.127  27.427  -8.314  0.50 32.89 ? 38  LYS B CG  1 
ATOM   291  C  CD  A LYS A 1 38  ? 31.830  29.067  -8.863  0.50 30.85 ? 38  LYS B CD  1 
ATOM   292  C  CD  B LYS A 1 38  ? 33.132  27.538  -7.176  0.50 34.50 ? 38  LYS B CD  1 
ATOM   293  C  CE  A LYS A 1 38  ? 30.334  29.343  -8.818  0.50 30.60 ? 38  LYS B CE  1 
ATOM   294  C  CE  B LYS A 1 38  ? 32.610  28.447  -6.072  0.50 35.59 ? 38  LYS B CE  1 
ATOM   295  N  NZ  A LYS A 1 38  ? 30.027  30.252  -7.662  0.50 30.59 ? 38  LYS B NZ  1 
ATOM   296  N  NZ  B LYS A 1 38  ? 33.649  28.720  -5.048  0.50 42.43 ? 38  LYS B NZ  1 
ATOM   297  N  N   . GLU A 1 39  ? 32.430  24.819  -12.352 1.00 22.48 ? 39  GLU B N   1 
ATOM   298  C  CA  . GLU A 1 39  ? 33.016  24.421  -13.643 1.00 23.56 ? 39  GLU B CA  1 
ATOM   299  C  C   . GLU A 1 39  ? 31.969  24.085  -14.666 1.00 19.81 ? 39  GLU B C   1 
ATOM   300  O  O   . GLU A 1 39  ? 32.290  23.678  -15.776 1.00 23.06 ? 39  GLU B O   1 
ATOM   301  C  CB  . GLU A 1 39  ? 33.981  23.207  -13.534 1.00 28.52 ? 39  GLU B CB  1 
ATOM   302  C  CG  . GLU A 1 39  ? 35.383  23.614  -13.057 1.00 35.65 ? 39  GLU B CG  1 
ATOM   303  C  CD  . GLU A 1 39  ? 35.352  23.994  -11.582 1.00 40.21 ? 39  GLU B CD  1 
ATOM   304  O  OE1 . GLU A 1 39  ? 35.056  23.096  -10.770 1.00 42.11 ? 39  GLU B OE1 1 
ATOM   305  O  OE2 . GLU A 1 39  ? 35.571  25.182  -11.228 1.00 41.92 ? 39  GLU B OE2 1 
ATOM   306  N  N   . VAL A 1 40  ? 30.715  24.255  -14.303 1.00 19.95 ? 40  VAL B N   1 
ATOM   307  C  CA  . VAL A 1 40  ? 29.631  23.988  -15.290 1.00 18.61 ? 40  VAL B CA  1 
ATOM   308  C  C   . VAL A 1 40  ? 29.491  25.180  -16.190 1.00 19.83 ? 40  VAL B C   1 
ATOM   309  O  O   . VAL A 1 40  ? 29.614  26.295  -15.728 1.00 21.99 ? 40  VAL B O   1 
ATOM   310  C  CB  . VAL A 1 40  ? 28.277  23.669  -14.569 1.00 17.42 ? 40  VAL B CB  1 
ATOM   311  C  CG1 . VAL A 1 40  ? 27.126  23.750  -15.533 1.00 16.36 ? 40  VAL B CG1 1 
ATOM   312  C  CG2 . VAL A 1 40  ? 28.350  22.274  -13.966 1.00 16.21 ? 40  VAL B CG2 1 
ATOM   313  N  N   . LYS A 1 41  ? 29.250  24.950  -17.482 1.00 21.08 ? 41  LYS B N   1 
ATOM   314  C  CA  . LYS A 1 41  ? 29.080  26.087  -18.394 1.00 23.01 ? 41  LYS B CA  1 
ATOM   315  C  C   . LYS A 1 41  ? 27.590  26.256  -18.704 1.00 22.33 ? 41  LYS B C   1 
ATOM   316  O  O   . LYS A 1 41  ? 26.983  25.329  -19.256 1.00 18.39 ? 41  LYS B O   1 
ATOM   317  C  CB  . LYS A 1 41  ? 29.909  25.832  -19.669 1.00 26.77 ? 41  LYS B CB  1 
ATOM   318  C  CG  . LYS A 1 41  ? 31.314  26.419  -19.616 1.00 34.04 ? 41  LYS B CG  1 
ATOM   319  C  CD  . LYS A 1 41  ? 32.358  25.531  -18.953 1.00 42.05 ? 41  LYS B CD  1 
ATOM   320  C  CE  . LYS A 1 41  ? 33.296  26.419  -18.093 1.00 47.33 ? 41  LYS B CE  1 
ATOM   321  N  NZ  . LYS A 1 41  ? 34.122  25.720  -17.053 1.00 45.44 ? 41  LYS B NZ  1 
ATOM   322  N  N   . TYR A 1 42  ? 27.006  27.409  -18.334 1.00 20.90 ? 42  TYR B N   1 
ATOM   323  C  CA  . TYR A 1 42  ? 25.665  27.743  -18.833 1.00 20.10 ? 42  TYR B CA  1 
ATOM   324  C  C   . TYR A 1 42  ? 25.642  27.762  -20.387 1.00 18.88 ? 42  TYR B C   1 
ATOM   325  O  O   . TYR A 1 42  ? 26.536  28.337  -20.983 1.00 17.46 ? 42  TYR B O   1 
ATOM   326  C  CB  . TYR A 1 42  ? 25.179  29.083  -18.224 1.00 23.85 ? 42  TYR B CB  1 
ATOM   327  C  CG  . TYR A 1 42  ? 23.948  29.625  -18.920 1.00 25.80 ? 42  TYR B CG  1 
ATOM   328  C  CD1 . TYR A 1 42  ? 22.707  28.954  -18.852 1.00 24.59 ? 42  TYR B CD1 1 
ATOM   329  C  CD2 . TYR A 1 42  ? 24.026  30.818  -19.686 1.00 28.16 ? 42  TYR B CD2 1 
ATOM   330  C  CE1 . TYR A 1 42  ? 21.588  29.447  -19.494 1.00 26.49 ? 42  TYR B CE1 1 
ATOM   331  C  CE2 . TYR A 1 42  ? 22.901  31.329  -20.324 1.00 28.79 ? 42  TYR B CE2 1 
ATOM   332  C  CZ  . TYR A 1 42  ? 21.691  30.653  -20.230 1.00 32.49 ? 42  TYR B CZ  1 
ATOM   333  O  OH  . TYR A 1 42  ? 20.584  31.183  -20.888 1.00 30.51 ? 42  TYR B OH  1 
ATOM   334  N  N   . ASP A 1 43  ? 24.650  27.137  -21.042 1.00 15.74 ? 43  ASP B N   1 
ATOM   335  C  CA  . ASP A 1 43  ? 24.627  27.177  -22.503 1.00 17.80 ? 43  ASP B CA  1 
ATOM   336  C  C   . ASP A 1 43  ? 23.243  27.575  -22.942 1.00 20.16 ? 43  ASP B C   1 
ATOM   337  O  O   . ASP A 1 43  ? 22.299  26.772  -22.909 1.00 17.65 ? 43  ASP B O   1 
ATOM   338  C  CB  . ASP A 1 43  ? 25.058  25.823  -23.083 1.00 19.26 ? 43  ASP B CB  1 
ATOM   339  C  CG  . ASP A 1 43  ? 25.138  25.806  -24.561 1.00 22.93 ? 43  ASP B CG  1 
ATOM   340  O  OD1 . ASP A 1 43  ? 24.688  26.775  -25.235 1.00 22.63 ? 43  ASP B OD1 1 
ATOM   341  O  OD2 . ASP A 1 43  ? 25.688  24.806  -25.089 1.00 24.74 ? 43  ASP B OD2 1 
ATOM   342  N  N   . SER A 1 44  ? 23.148  28.819  -23.431 1.00 21.57 ? 44  SER B N   1 
ATOM   343  C  CA  . SER A 1 44  ? 21.868  29.423  -23.834 1.00 23.19 ? 44  SER B CA  1 
ATOM   344  C  C   . SER A 1 44  ? 21.207  28.716  -25.044 1.00 22.92 ? 44  SER B C   1 
ATOM   345  O  O   . SER A 1 44  ? 19.987  28.870  -25.278 1.00 26.00 ? 44  SER B O   1 
ATOM   346  C  CB  . SER A 1 44  ? 22.057  30.944  -24.038 1.00 22.20 ? 44  SER B CB  1 
ATOM   347  O  OG  . SER A 1 44  ? 22.673  31.082  -25.282 1.00 28.45 ? 44  SER B OG  1 
ATOM   348  N  N   . SER A 1 45  ? 21.963  27.883  -25.759 1.00 21.77 ? 45  SER B N   1 
ATOM   349  C  CA  . SER A 1 45  ? 21.460  27.168  -26.903 1.00 20.86 ? 45  SER B CA  1 
ATOM   350  C  C   . SER A 1 45  ? 20.763  25.860  -26.483 1.00 21.30 ? 45  SER B C   1 
ATOM   351  O  O   . SER A 1 45  ? 20.133  25.214  -27.321 1.00 21.81 ? 45  SER B O   1 
ATOM   352  C  CB  . SER A 1 45  ? 22.609  26.828  -27.872 1.00 22.89 ? 45  SER B CB  1 
ATOM   353  O  OG  . SER A 1 45  ? 23.481  25.831  -27.335 1.00 28.12 ? 45  SER B OG  1 
ATOM   354  N  N   . LEU A 1 46  ? 20.935  25.434  -25.219 1.00 16.41 ? 46  LEU B N   1 
ATOM   355  C  CA  . LEU A 1 46  ? 20.204  24.232  -24.718 1.00 14.65 ? 46  LEU B CA  1 
ATOM   356  C  C   . LEU A 1 46  ? 18.705  24.580  -24.783 1.00 15.14 ? 46  LEU B C   1 
ATOM   357  O  O   . LEU A 1 46  ? 18.359  25.740  -24.665 1.00 16.95 ? 46  LEU B O   1 
ATOM   358  C  CB  . LEU A 1 46  ? 20.569  23.951  -23.269 1.00 12.33 ? 46  LEU B CB  1 
ATOM   359  C  CG  . LEU A 1 46  ? 21.931  23.209  -23.199 1.00 11.84 ? 46  LEU B CG  1 
ATOM   360  C  CD1 . LEU A 1 46  ? 22.436  23.173  -21.720 1.00 11.57 ? 46  LEU B CD1 1 
ATOM   361  C  CD2 . LEU A 1 46  ? 21.781  21.806  -23.782 1.00 11.45 ? 46  LEU B CD2 1 
ATOM   362  N  N   . ARG A 1 47  ? 17.829  23.577  -24.909 1.00 12.96 ? 47  ARG B N   1 
ATOM   363  C  CA  . ARG A 1 47  ? 16.387  23.898  -24.946 1.00 13.75 ? 47  ARG B CA  1 
ATOM   364  C  C   . ARG A 1 47  ? 15.711  23.364  -23.720 1.00 11.89 ? 47  ARG B C   1 
ATOM   365  O  O   . ARG A 1 47  ? 16.234  22.446  -23.046 1.00 11.04 ? 47  ARG B O   1 
ATOM   366  C  CB  . ARG A 1 47  ? 15.747  23.329  -26.198 1.00 16.29 ? 47  ARG B CB  1 
ATOM   367  C  CG  . ARG A 1 47  ? 16.102  24.261  -27.335 1.00 24.28 ? 47  ARG B CG  1 
ATOM   368  C  CD  . ARG A 1 47  ? 16.169  23.516  -28.600 1.00 32.16 ? 47  ARG B CD  1 
ATOM   369  N  NE  . ARG A 1 47  ? 16.465  24.512  -29.607 1.00 35.74 ? 47  ARG B NE  1 
ATOM   370  C  CZ  . ARG A 1 47  ? 16.449  24.244  -30.903 1.00 44.18 ? 47  ARG B CZ  1 
ATOM   371  N  NH1 . ARG A 1 47  ? 16.157  23.011  -31.336 1.00 35.14 ? 47  ARG B NH1 1 
ATOM   372  N  NH2 . ARG A 1 47  ? 16.740  25.224  -31.761 1.00 54.75 ? 47  ARG B NH2 1 
ATOM   373  N  N   . PRO A 1 48  ? 14.512  23.878  -23.470 1.00 10.52 ? 48  PRO B N   1 
ATOM   374  C  CA  . PRO A 1 48  ? 13.805  23.332  -22.357 1.00 10.68 ? 48  PRO B CA  1 
ATOM   375  C  C   . PRO A 1 48  ? 13.395  21.898  -22.588 1.00 10.66 ? 48  PRO B C   1 
ATOM   376  O  O   . PRO A 1 48  ? 13.179  21.487  -23.727 1.00 10.96 ? 48  PRO B O   1 
ATOM   377  C  CB  . PRO A 1 48  ? 12.561  24.231  -22.231 1.00 11.36 ? 48  PRO B CB  1 
ATOM   378  C  CG  . PRO A 1 48  ? 12.879  25.470  -23.039 1.00 12.51 ? 48  PRO B CG  1 
ATOM   379  C  CD  . PRO A 1 48  ? 13.877  25.071  -24.088 1.00 11.37 ? 48  PRO B CD  1 
ATOM   380  N  N   . LEU A 1 49  ? 13.343  21.130  -21.497 1.00 9.10  ? 49  LEU B N   1 
ATOM   381  C  CA  . LEU A 1 49  ? 12.774  19.771  -21.588 1.00 9.93  ? 49  LEU B CA  1 
ATOM   382  C  C   . LEU A 1 49  ? 11.264  19.852  -21.871 1.00 10.73 ? 49  LEU B C   1 
ATOM   383  O  O   . LEU A 1 49  ? 10.543  20.700  -21.337 1.00 11.93 ? 49  LEU B O   1 
ATOM   384  C  CB  . LEU A 1 49  ? 12.999  19.010  -20.269 1.00 9.26  ? 49  LEU B CB  1 
ATOM   385  C  CG  . LEU A 1 49  ? 14.521  18.824  -19.934 1.00 10.52 ? 49  LEU B CG  1 
ATOM   386  C  CD1 . LEU A 1 49  ? 14.599  18.213  -18.565 1.00 10.45 ? 49  LEU B CD1 1 
ATOM   387  C  CD2 . LEU A 1 49  ? 15.257  17.893  -20.911 1.00 9.32  ? 49  LEU B CD2 1 
ATOM   388  N  N   . SER A 1 50  ? 10.803  18.898  -22.684 1.00 11.60 ? 50  SER B N   1 
ATOM   389  C  CA  . SER A 1 50  ? 9.373   18.785  -22.977 1.00 11.90 ? 50  SER B CA  1 
ATOM   390  C  C   . SER A 1 50  ? 8.981   17.295  -22.833 1.00 14.00 ? 50  SER B C   1 
ATOM   391  O  O   . SER A 1 50  ? 9.506   16.481  -23.561 1.00 12.14 ? 50  SER B O   1 
ATOM   392  C  CB  . SER A 1 50  ? 9.191   19.195  -24.430 1.00 13.49 ? 50  SER B CB  1 
ATOM   393  O  OG  . SER A 1 50  ? 7.821   19.064  -24.704 1.00 13.75 ? 50  SER B OG  1 
ATOM   394  N  N   . ILE A 1 51  ? 8.101   16.984  -21.868 1.00 12.40 ? 51  ILE B N   1 
ATOM   395  C  CA  . ILE A 1 51  ? 7.852   15.636  -21.450 1.00 14.47 ? 51  ILE B CA  1 
ATOM   396  C  C   . ILE A 1 51  ? 6.396   15.247  -21.641 1.00 14.98 ? 51  ILE B C   1 
ATOM   397  O  O   . ILE A 1 51  ? 5.450   15.959  -21.270 1.00 14.01 ? 51  ILE B O   1 
ATOM   398  C  CB  . ILE A 1 51  ? 8.207   15.510  -19.938 1.00 15.44 ? 51  ILE B CB  1 
ATOM   399  C  CG1 . ILE A 1 51  ? 9.703   15.586  -19.738 1.00 18.46 ? 51  ILE B CG1 1 
ATOM   400  C  CG2 . ILE A 1 51  ? 7.607   14.220  -19.324 1.00 19.34 ? 51  ILE B CG2 1 
ATOM   401  C  CD1 . ILE A 1 51  ? 10.116  15.923  -18.307 1.00 19.72 ? 51  ILE B CD1 1 
ATOM   402  N  N   . LYS A 1 52  ? 6.190   14.050  -22.170 1.00 14.62 ? 52  LYS B N   1 
ATOM   403  C  CA  . LYS A 1 52  ? 4.814   13.505  -22.211 1.00 15.96 ? 52  LYS B CA  1 
ATOM   404  C  C   . LYS A 1 52  ? 4.921   12.084  -21.732 1.00 14.64 ? 52  LYS B C   1 
ATOM   405  O  O   . LYS A 1 52  ? 5.465   11.243  -22.452 1.00 12.83 ? 52  LYS B O   1 
ATOM   406  C  CB  . LYS A 1 52  ? 4.293   13.539  -23.631 1.00 18.47 ? 52  LYS B CB  1 
ATOM   407  C  CG  . LYS A 1 52  ? 2.923   12.872  -23.844 1.00 22.39 ? 52  LYS B CG  1 
ATOM   408  C  CD  . LYS A 1 52  ? 2.786   12.506  -25.321 1.00 25.18 ? 52  LYS B CD  1 
ATOM   409  C  CE  . LYS A 1 52  ? 1.363   12.066  -25.610 1.00 29.51 ? 52  LYS B CE  1 
ATOM   410  N  NZ  . LYS A 1 52  ? 0.925   10.717  -25.089 1.00 26.19 ? 52  LYS B NZ  1 
ATOM   411  N  N   . TYR A 1 53  ? 4.391   11.817  -20.533 1.00 12.59 ? 53  TYR B N   1 
ATOM   412  C  CA  . TYR A 1 53  ? 4.388   10.472  -19.948 1.00 11.50 ? 53  TYR B CA  1 
ATOM   413  C  C   . TYR A 1 53  ? 2.992   9.985   -19.741 1.00 12.99 ? 53  TYR B C   1 
ATOM   414  O  O   . TYR A 1 53  ? 2.304   10.508  -18.836 1.00 13.94 ? 53  TYR B O   1 
ATOM   415  C  CB  . TYR A 1 53  ? 5.185   10.369  -18.696 1.00 11.92 ? 53  TYR B CB  1 
ATOM   416  C  CG  . TYR A 1 53  ? 6.710   10.615  -18.769 1.00 11.63 ? 53  TYR B CG  1 
ATOM   417  C  CD1 . TYR A 1 53  ? 7.460   10.318  -19.911 1.00 11.84 ? 53  TYR B CD1 1 
ATOM   418  C  CD2 . TYR A 1 53  ? 7.417   11.117  -17.631 1.00 11.17 ? 53  TYR B CD2 1 
ATOM   419  C  CE1 . TYR A 1 53  ? 8.828   10.500  -19.907 1.00 10.75 ? 53  TYR B CE1 1 
ATOM   420  C  CE2 . TYR A 1 53  ? 8.776   11.315  -17.640 1.00 11.19 ? 53  TYR B CE2 1 
ATOM   421  C  CZ  . TYR A 1 53  ? 9.476   11.005  -18.786 1.00 11.20 ? 53  TYR B CZ  1 
ATOM   422  O  OH  . TYR A 1 53  ? 10.805  11.197  -18.835 1.00 11.30 ? 53  TYR B OH  1 
ATOM   423  N  N   . ASP A 1 54  ? 2.602   8.954   -20.542 1.00 12.44 ? 54  ASP B N   1 
ATOM   424  C  CA  . ASP A 1 54  ? 1.197   8.389   -20.483 1.00 11.53 ? 54  ASP B CA  1 
ATOM   425  C  C   . ASP A 1 54  ? 1.160   7.420   -19.290 1.00 12.44 ? 54  ASP B C   1 
ATOM   426  O  O   . ASP A 1 54  ? 1.960   6.524   -19.243 1.00 10.62 ? 54  ASP B O   1 
ATOM   427  C  CB  . ASP A 1 54  ? 0.955   7.598   -21.774 1.00 11.57 ? 54  ASP B CB  1 
ATOM   428  C  CG  . ASP A 1 54  ? -0.473  7.157   -21.935 1.00 12.49 ? 54  ASP B CG  1 
ATOM   429  O  OD1 . ASP A 1 54  ? -1.176  6.853   -20.952 1.00 13.29 ? 54  ASP B OD1 1 
ATOM   430  O  OD2 . ASP A 1 54  ? -0.913  7.082   -23.085 1.00 15.26 ? 54  ASP B OD2 1 
ATOM   431  N  N   . PRO A 1 55  ? 0.252   7.615   -18.316 1.00 12.64 ? 55  PRO B N   1 
ATOM   432  C  CA  . PRO A 1 55  ? 0.257   6.749   -17.148 1.00 13.14 ? 55  PRO B CA  1 
ATOM   433  C  C   . PRO A 1 55  ? -0.104  5.300   -17.532 1.00 12.54 ? 55  PRO B C   1 
ATOM   434  O  O   . PRO A 1 55  ? 0.166   4.364   -16.761 1.00 13.13 ? 55  PRO B O   1 
ATOM   435  C  CB  . PRO A 1 55  ? -0.859  7.328   -16.260 1.00 14.01 ? 55  PRO B CB  1 
ATOM   436  C  CG  . PRO A 1 55  ? -1.194  8.691   -16.791 1.00 16.62 ? 55  PRO B CG  1 
ATOM   437  C  CD  . PRO A 1 55  ? -0.815  8.648   -18.268 1.00 15.23 ? 55  PRO B CD  1 
ATOM   438  N  N   . SER A 1 56  ? -0.715  5.103   -18.721 1.00 11.93 ? 56  SER B N   1 
ATOM   439  C  CA  . SER A 1 56  ? -0.959  3.717   -19.149 1.00 12.83 ? 56  SER B CA  1 
ATOM   440  C  C   . SER A 1 56  ? 0.278   2.989   -19.701 1.00 12.64 ? 56  SER B C   1 
ATOM   441  O  O   . SER A 1 56  ? 0.229   1.768   -19.892 1.00 13.42 ? 56  SER B O   1 
ATOM   442  C  CB  . SER A 1 56  ? -2.105  3.682   -20.179 1.00 14.68 ? 56  SER B CB  1 
ATOM   443  O  OG  . SER A 1 56  ? -1.591  3.959   -21.477 1.00 17.75 ? 56  SER B OG  1 
ATOM   444  N  N   . SER A 1 57  ? 1.409   3.707   -19.866 1.00 11.35 ? 57  SER B N   1 
ATOM   445  C  CA  . SER A 1 57  ? 2.561   3.135   -20.470 1.00 10.99 ? 57  SER B CA  1 
ATOM   446  C  C   . SER A 1 57  ? 3.222   2.109   -19.543 1.00 12.16 ? 57  SER B C   1 
ATOM   447  O  O   . SER A 1 57  ? 3.716   1.114   -20.045 1.00 11.49 ? 57  SER B O   1 
ATOM   448  C  CB  . SER A 1 57  ? 3.599   4.179   -20.846 1.00 11.35 ? 57  SER B CB  1 
ATOM   449  O  OG  . SER A 1 57  ? 3.093   4.912   -21.976 1.00 11.87 ? 57  SER B OG  1 
ATOM   450  N  N   . ALA A 1 58  ? 3.204   2.327   -18.240 1.00 10.26 ? 58  ALA B N   1 
ATOM   451  C  CA  . ALA A 1 58  ? 3.812   1.352   -17.323 1.00 10.79 ? 58  ALA B CA  1 
ATOM   452  C  C   . ALA A 1 58  ? 3.043   0.025   -17.381 1.00 10.34 ? 58  ALA B C   1 
ATOM   453  O  O   . ALA A 1 58  ? 1.808   0.057   -17.426 1.00 10.81 ? 58  ALA B O   1 
ATOM   454  C  CB  . ALA A 1 58  ? 3.759   1.859   -15.892 1.00 10.21 ? 58  ALA B CB  1 
ATOM   455  N  N   . LYS A 1 59  ? 3.770   -1.094  -17.417 1.00 10.69 ? 59  LYS B N   1 
ATOM   456  C  CA  . LYS A 1 59  ? 3.122   -2.420  -17.467 1.00 10.36 ? 59  LYS B CA  1 
ATOM   457  C  C   . LYS A 1 59  ? 3.529   -3.322  -16.316 1.00 11.14 ? 59  LYS B C   1 
ATOM   458  O  O   . LYS A 1 59  ? 2.675   -3.998  -15.802 1.00 11.85 ? 59  LYS B O   1 
ATOM   459  C  CB  . LYS A 1 59  ? 3.490   -3.097  -18.807 1.00 10.49 ? 59  LYS B CB  1 
ATOM   460  C  CG  . LYS A 1 59  ? 2.967   -2.211  -19.968 1.00 10.57 ? 59  LYS B CG  1 
ATOM   461  C  CD  . LYS A 1 59  ? 1.460   -2.135  -20.039 1.00 10.38 ? 59  LYS B CD  1 
ATOM   462  C  CE  . LYS A 1 59  ? 1.048   -1.167  -21.164 1.00 12.77 ? 59  LYS B CE  1 
ATOM   463  N  NZ  . LYS A 1 59  ? -0.372  -0.693  -21.173 1.00 12.16 ? 59  LYS B NZ  1 
ATOM   464  N  N   . ILE A 1 60  ? 4.808   -3.316  -15.898 1.00 11.61 ? 60  ILE B N   1 
ATOM   465  C  CA  . ILE A 1 60  ? 5.306   -4.372  -14.985 1.00 15.20 ? 60  ILE B CA  1 
ATOM   466  C  C   . ILE A 1 60  ? 6.357   -3.761  -14.108 1.00 14.25 ? 60  ILE B C   1 
ATOM   467  O  O   . ILE A 1 60  ? 7.138   -2.935  -14.579 1.00 16.19 ? 60  ILE B O   1 
ATOM   468  C  CB  . ILE A 1 60  ? 5.936   -5.605  -15.768 1.00 17.17 ? 60  ILE B CB  1 
ATOM   469  C  CG1 . ILE A 1 60  ? 4.856   -6.423  -16.496 1.00 23.85 ? 60  ILE B CG1 1 
ATOM   470  C  CG2 . ILE A 1 60  ? 6.480   -6.632  -14.787 1.00 21.35 ? 60  ILE B CG2 1 
ATOM   471  C  CD1 . ILE A 1 60  ? 5.318   -6.978  -17.845 1.00 25.72 ? 60  ILE B CD1 1 
ATOM   472  N  N   . ILE A 1 61  ? 6.347   -4.102  -12.820 1.00 13.31 ? 61  ILE B N   1 
ATOM   473  C  CA  . ILE A 1 61  ? 7.460   -3.764  -11.959 1.00 12.38 ? 61  ILE B CA  1 
ATOM   474  C  C   . ILE A 1 61  ? 8.112   -5.076  -11.532 1.00 13.26 ? 61  ILE B C   1 
ATOM   475  O  O   . ILE A 1 61  ? 7.439   -6.058  -11.231 1.00 12.42 ? 61  ILE B O   1 
ATOM   476  C  CB  . ILE A 1 61  ? 7.031   -2.906  -10.730 1.00 12.27 ? 61  ILE B CB  1 
ATOM   477  C  CG1 . ILE A 1 61  ? 8.257   -2.301  -10.022 1.00 13.18 ? 61  ILE B CG1 1 
ATOM   478  C  CG2 . ILE A 1 61  ? 6.236   -3.717  -9.680  1.00 11.98 ? 61  ILE B CG2 1 
ATOM   479  C  CD1 . ILE A 1 61  ? 7.919   -1.231  -9.013  1.00 12.54 ? 61  ILE B CD1 1 
ATOM   480  N  N   . SER A 1 62  ? 9.419   -5.076  -11.513 1.00 12.94 ? 62  SER B N   1 
ATOM   481  C  CA  . SER A 1 62  ? 10.176  -6.330  -11.223 1.00 12.25 ? 62  SER B CA  1 
ATOM   482  C  C   . SER A 1 62  ? 11.395  -6.028  -10.426 1.00 13.05 ? 62  SER B C   1 
ATOM   483  O  O   . SER A 1 62  ? 11.861  -4.887  -10.362 1.00 13.40 ? 62  SER B O   1 
ATOM   484  C  CB  . SER A 1 62  ? 10.556  -7.060  -12.498 1.00 14.21 ? 62  SER B CB  1 
ATOM   485  O  OG  . SER A 1 62  ? 11.344  -6.227  -13.343 1.00 16.27 ? 62  SER B OG  1 
ATOM   486  N  N   . ASN A 1 63  ? 11.878  -7.052  -9.761  1.00 12.76 ? 63  ASN B N   1 
ATOM   487  C  CA  . ASN A 1 63  ? 13.227  -7.033  -9.151  1.00 12.62 ? 63  ASN B CA  1 
ATOM   488  C  C   . ASN A 1 63  ? 14.229  -7.662  -10.102 1.00 11.73 ? 63  ASN B C   1 
ATOM   489  O  O   . ASN A 1 63  ? 14.178  -8.898  -10.358 1.00 12.82 ? 63  ASN B O   1 
ATOM   490  C  CB  . ASN A 1 63  ? 13.196  -7.803  -7.851  1.00 11.89 ? 63  ASN B CB  1 
ATOM   491  C  CG  . ASN A 1 63  ? 14.495  -7.723  -7.107  1.00 11.69 ? 63  ASN B CG  1 
ATOM   492  O  OD1 . ASN A 1 63  ? 15.485  -7.313  -7.652  1.00 13.96 ? 63  ASN B OD1 1 
ATOM   493  N  ND2 . ASN A 1 63  ? 14.507  -8.135  -5.852  1.00 12.01 ? 63  ASN B ND2 1 
ATOM   494  N  N   . SER A 1 64  ? 15.131  -6.808  -10.656 1.00 12.03 ? 64  SER B N   1 
ATOM   495  C  CA  . SER A 1 64  ? 16.170  -7.288  -11.591 1.00 11.60 ? 64  SER B CA  1 
ATOM   496  C  C   . SER A 1 64  ? 17.315  -8.014  -10.894 1.00 11.25 ? 64  SER B C   1 
ATOM   497  O  O   . SER A 1 64  ? 18.198  -8.522  -11.561 1.00 13.15 ? 64  SER B O   1 
ATOM   498  C  CB  . SER A 1 64  ? 16.745  -6.150  -12.374 1.00 12.49 ? 64  SER B CB  1 
ATOM   499  O  OG  . SER A 1 64  ? 17.443  -5.256  -11.473 1.00 11.69 ? 64  SER B OG  1 
ATOM   500  N  N   . GLY A 1 65  ? 17.329  -7.923  -9.575  1.00 12.15 ? 65  GLY B N   1 
ATOM   501  C  CA  . GLY A 1 65  ? 18.475  -8.297  -8.733  1.00 12.58 ? 65  GLY B CA  1 
ATOM   502  C  C   . GLY A 1 65  ? 19.399  -7.105  -8.504  1.00 12.26 ? 65  GLY B C   1 
ATOM   503  O  O   . GLY A 1 65  ? 20.311  -7.207  -7.685  1.00 14.03 ? 65  GLY B O   1 
ATOM   504  N  N   . HIS A 1 66  ? 19.187  -5.975  -9.218  1.00 11.41 ? 66  HIS B N   1 
ATOM   505  C  CA  . HIS A 1 66  ? 20.073  -4.787  -9.173  1.00 12.24 ? 66  HIS B CA  1 
ATOM   506  C  C   . HIS A 1 66  ? 19.344  -3.498  -8.737  1.00 11.42 ? 66  HIS B C   1 
ATOM   507  O  O   . HIS A 1 66  ? 20.008  -2.522  -8.405  1.00 11.78 ? 66  HIS B O   1 
ATOM   508  C  CB  . HIS A 1 66  ? 20.776  -4.477  -10.517 1.00 14.65 ? 66  HIS B CB  1 
ATOM   509  C  CG  . HIS A 1 66  ? 21.324  -5.689  -11.190 1.00 15.44 ? 66  HIS B CG  1 
ATOM   510  N  ND1 . HIS A 1 66  ? 22.417  -6.368  -10.686 1.00 15.42 ? 66  HIS B ND1 1 
ATOM   511  C  CD2 . HIS A 1 66  ? 20.901  -6.397  -12.261 1.00 15.93 ? 66  HIS B CD2 1 
ATOM   512  C  CE1 . HIS A 1 66  ? 22.668  -7.424  -11.449 1.00 17.65 ? 66  HIS B CE1 1 
ATOM   513  N  NE2 . HIS A 1 66  ? 21.770  -7.460  -12.415 1.00 17.47 ? 66  HIS B NE2 1 
ATOM   514  N  N   . SER A 1 67  ? 18.011  -3.477  -8.837  1.00 12.54 ? 67  SER B N   1 
ATOM   515  C  CA  . SER A 1 67  ? 17.088  -2.406  -8.402  1.00 11.93 ? 67  SER B CA  1 
ATOM   516  C  C   . SER A 1 67  ? 15.702  -2.978  -8.689  1.00 12.82 ? 67  SER B C   1 
ATOM   517  O  O   . SER A 1 67  ? 15.600  -4.189  -9.100  1.00 13.60 ? 67  SER B O   1 
ATOM   518  C  CB  . SER A 1 67  ? 17.315  -1.071  -9.221  1.00 12.34 ? 67  SER B CB  1 
ATOM   519  O  OG  . SER A 1 67  ? 16.462  -0.030  -8.740  1.00 10.60 ? 67  SER B OG  1 
ATOM   520  N  N   . PHE A 1 68  ? 14.651  -2.164  -8.484  1.00 11.50 ? 68  PHE B N   1 
ATOM   521  C  CA  . PHE A 1 68  ? 13.352  -2.456  -9.115  1.00 11.92 ? 68  PHE B CA  1 
ATOM   522  C  C   . PHE A 1 68  ? 13.420  -1.882  -10.527 1.00 13.11 ? 68  PHE B C   1 
ATOM   523  O  O   . PHE A 1 68  ? 14.251  -0.980  -10.802 1.00 12.90 ? 68  PHE B O   1 
ATOM   524  C  CB  . PHE A 1 68  ? 12.138  -1.885  -8.337  1.00 11.87 ? 68  PHE B CB  1 
ATOM   525  C  CG  . PHE A 1 68  ? 12.034  -0.373  -8.389  1.00 12.06 ? 68  PHE B CG  1 
ATOM   526  C  CD1 . PHE A 1 68  ? 11.401  0.282   -9.464  1.00 12.79 ? 68  PHE B CD1 1 
ATOM   527  C  CD2 . PHE A 1 68  ? 12.596  0.443   -7.362  1.00 11.58 ? 68  PHE B CD2 1 
ATOM   528  C  CE1 . PHE A 1 68  ? 11.310  1.665   -9.477  1.00 13.64 ? 68  PHE B CE1 1 
ATOM   529  C  CE2 . PHE A 1 68  ? 12.491  1.815   -7.417  1.00 11.27 ? 68  PHE B CE2 1 
ATOM   530  C  CZ  . PHE A 1 68  ? 11.875  2.432   -8.470  1.00 12.79 ? 68  PHE B CZ  1 
ATOM   531  N  N   . ASN A 1 69  ? 12.617  -2.423  -11.441 1.00 12.19 ? 69  ASN B N   1 
ATOM   532  C  CA  . ASN A 1 69  ? 12.593  -1.952  -12.819 1.00 14.65 ? 69  ASN B CA  1 
ATOM   533  C  C   . ASN A 1 69  ? 11.128  -1.831  -13.179 1.00 13.55 ? 69  ASN B C   1 
ATOM   534  O  O   . ASN A 1 69  ? 10.411  -2.845  -13.070 1.00 12.18 ? 69  ASN B O   1 
ATOM   535  C  CB  . ASN A 1 69  ? 13.078  -3.106  -13.643 1.00 18.43 ? 69  ASN B CB  1 
ATOM   536  C  CG  . ASN A 1 69  ? 14.095  -2.739  -14.600 1.00 31.51 ? 69  ASN B CG  1 
ATOM   537  O  OD1 . ASN A 1 69  ? 15.259  -2.462  -14.248 1.00 45.02 ? 69  ASN B OD1 1 
ATOM   538  N  ND2 . ASN A 1 69  ? 13.711  -2.745  -15.830 1.00 28.53 ? 69  ASN B ND2 1 
ATOM   539  N  N   . VAL A 1 70  ? 10.666  -0.631  -13.541 1.00 11.96 ? 70  VAL B N   1 
ATOM   540  C  CA  . VAL A 1 70  ? 9.324   -0.473  -14.069 1.00 11.90 ? 70  VAL B CA  1 
ATOM   541  C  C   . VAL A 1 70  ? 9.572   -0.487  -15.572 1.00 11.87 ? 70  VAL B C   1 
ATOM   542  O  O   . VAL A 1 70  ? 10.342  0.334   -16.123 1.00 11.15 ? 70  VAL B O   1 
ATOM   543  C  CB  . VAL A 1 70  ? 8.574   0.848   -13.639 1.00 12.24 ? 70  VAL B CB  1 
ATOM   544  C  CG1 . VAL A 1 70  ? 7.206   0.983   -14.364 1.00 11.87 ? 70  VAL B CG1 1 
ATOM   545  C  CG2 . VAL A 1 70  ? 8.448   0.923   -12.101 1.00 11.88 ? 70  VAL B CG2 1 
ATOM   546  N  N   . ASP A 1 71  ? 8.942   -1.456  -16.245 1.00 12.23 ? 71  ASP B N   1 
ATOM   547  C  CA  . ASP A 1 71  ? 9.010   -1.533  -17.716 1.00 14.29 ? 71  ASP B CA  1 
ATOM   548  C  C   . ASP A 1 71  ? 7.790   -0.884  -18.329 1.00 12.64 ? 71  ASP B C   1 
ATOM   549  O  O   . ASP A 1 71  ? 6.690   -1.002  -17.785 1.00 12.48 ? 71  ASP B O   1 
ATOM   550  C  CB  . ASP A 1 71  ? 9.082   -2.983  -18.145 1.00 17.69 ? 71  ASP B CB  1 
ATOM   551  C  CG  . ASP A 1 71  ? 10.540  -3.495  -18.220 1.00 25.36 ? 71  ASP B CG  1 
ATOM   552  O  OD1 . ASP A 1 71  ? 11.430  -2.805  -18.842 1.00 32.16 ? 71  ASP B OD1 1 
ATOM   553  O  OD2 . ASP A 1 71  ? 10.764  -4.601  -17.719 1.00 32.58 ? 71  ASP B OD2 1 
ATOM   554  N  N   . PHE A 1 72  ? 7.997   -0.144  -19.405 1.00 10.92 ? 72  PHE B N   1 
ATOM   555  C  CA  . PHE A 1 72  ? 6.933   0.608   -20.064 1.00 11.41 ? 72  PHE B CA  1 
ATOM   556  C  C   . PHE A 1 72  ? 6.808   -0.002  -21.448 1.00 11.82 ? 72  PHE B C   1 
ATOM   557  O  O   . PHE A 1 72  ? 7.797   -0.434  -22.077 1.00 12.85 ? 72  PHE B O   1 
ATOM   558  C  CB  . PHE A 1 72  ? 7.316   2.089   -20.237 1.00 11.43 ? 72  PHE B CB  1 
ATOM   559  C  CG  . PHE A 1 72  ? 7.474   2.789   -18.894 1.00 11.86 ? 72  PHE B CG  1 
ATOM   560  C  CD1 . PHE A 1 72  ? 8.661   2.636   -18.136 1.00 11.20 ? 72  PHE B CD1 1 
ATOM   561  C  CD2 . PHE A 1 72  ? 6.402   3.553   -18.343 1.00 11.28 ? 72  PHE B CD2 1 
ATOM   562  C  CE1 . PHE A 1 72  ? 8.755   3.270   -16.859 1.00 11.33 ? 72  PHE B CE1 1 
ATOM   563  C  CE2 . PHE A 1 72  ? 6.508   4.193   -17.083 1.00 11.91 ? 72  PHE B CE2 1 
ATOM   564  C  CZ  . PHE A 1 72  ? 7.680   4.030   -16.318 1.00 11.33 ? 72  PHE B CZ  1 
ATOM   565  N  N   . ASP A 1 73  ? 5.571   -0.025  -21.917 1.00 11.06 ? 73  ASP B N   1 
ATOM   566  C  CA  . ASP A 1 73  ? 5.350   -0.461  -23.303 1.00 10.62 ? 73  ASP B CA  1 
ATOM   567  C  C   . ASP A 1 73  ? 5.895   0.650   -24.235 1.00 11.21 ? 73  ASP B C   1 
ATOM   568  O  O   . ASP A 1 73  ? 5.451   1.806   -24.179 1.00 11.89 ? 73  ASP B O   1 
ATOM   569  C  CB  . ASP A 1 73  ? 3.829   -0.527  -23.488 1.00 11.45 ? 73  ASP B CB  1 
ATOM   570  C  CG  . ASP A 1 73  ? 3.414   -0.759  -24.932 1.00 12.56 ? 73  ASP B CG  1 
ATOM   571  O  OD1 . ASP A 1 73  ? 4.255   -1.059  -25.757 1.00 11.65 ? 73  ASP B OD1 1 
ATOM   572  O  OD2 . ASP A 1 73  ? 2.217   -0.670  -25.211 1.00 15.25 ? 73  ASP B OD2 1 
ATOM   573  N  N   . ASP A 1 74  ? 6.866   0.281   -25.076 1.00 10.70 ? 74  ASP B N   1 
ATOM   574  C  CA  . ASP A 1 74  ? 7.520   1.244   -25.934 1.00 10.89 ? 74  ASP B CA  1 
ATOM   575  C  C   . ASP A 1 74  ? 7.192   0.873   -27.381 1.00 10.69 ? 74  ASP B C   1 
ATOM   576  O  O   . ASP A 1 74  ? 8.032   1.105   -28.289 1.00 9.93  ? 74  ASP B O   1 
ATOM   577  C  CB  . ASP A 1 74  ? 9.023   1.362   -25.686 1.00 11.68 ? 74  ASP B CB  1 
ATOM   578  C  CG  . ASP A 1 74  ? 9.823   0.107   -26.001 1.00 14.49 ? 74  ASP B CG  1 
ATOM   579  O  OD1 . ASP A 1 74  ? 9.253   -0.992  -26.272 1.00 15.55 ? 74  ASP B OD1 1 
ATOM   580  O  OD2 . ASP A 1 74  ? 11.057  0.225   -26.075 1.00 13.17 ? 74  ASP B OD2 1 
ATOM   581  N  N   . THR A 1 75  ? 5.949   0.389   -27.585 1.00 10.96 ? 75  THR B N   1 
ATOM   582  C  CA  . THR A 1 75  ? 5.531   0.044   -29.002 1.00 11.33 ? 75  THR B CA  1 
ATOM   583  C  C   . THR A 1 75  ? 5.493   1.293   -29.917 1.00 12.85 ? 75  THR B C   1 
ATOM   584  O  O   . THR A 1 75  ? 5.905   1.231   -31.106 1.00 13.67 ? 75  THR B O   1 
ATOM   585  C  CB  . THR A 1 75  ? 4.105   -0.578  -28.989 1.00 12.54 ? 75  THR B CB  1 
ATOM   586  O  OG1 . THR A 1 75  ? 4.166   -1.805  -28.241 1.00 12.40 ? 75  THR B OG1 1 
ATOM   587  C  CG2 . THR A 1 75  ? 3.586   -0.883  -30.433 1.00 11.31 ? 75  THR B CG2 1 
ATOM   588  N  N   . GLU A 1 76  ? 5.031   2.420   -29.370 1.00 13.09 ? 76  GLU B N   1 
ATOM   589  C  CA  . GLU A 1 76  ? 5.079   3.667   -30.156 1.00 13.84 ? 76  GLU B CA  1 
ATOM   590  C  C   . GLU A 1 76  ? 5.374   4.866   -29.263 1.00 12.84 ? 76  GLU B C   1 
ATOM   591  O  O   . GLU A 1 76  ? 6.018   4.693   -28.219 1.00 12.53 ? 76  GLU B O   1 
ATOM   592  C  CB  . GLU A 1 76  ? 3.772   3.758   -31.004 1.00 14.33 ? 76  GLU B CB  1 
ATOM   593  C  CG  . GLU A 1 76  ? 2.517   3.925   -30.107 1.00 16.99 ? 76  GLU B CG  1 
ATOM   594  C  CD  . GLU A 1 76  ? 1.231   3.921   -30.931 1.00 21.34 ? 76  GLU B CD  1 
ATOM   595  O  OE1 . GLU A 1 76  ? 1.128   4.712   -31.860 1.00 23.70 ? 76  GLU B OE1 1 
ATOM   596  O  OE2 . GLU A 1 76  ? 0.368   3.041   -30.723 1.00 28.07 ? 76  GLU B OE2 1 
ATOM   597  N  N   . ASN A 1 77  ? 4.964   6.076   -29.664 1.00 13.06 ? 77  ASN B N   1 
ATOM   598  C  CA  . ASN A 1 77  ? 5.402   7.277   -28.945 1.00 11.96 ? 77  ASN B CA  1 
ATOM   599  C  C   . ASN A 1 77  ? 4.367   7.824   -28.001 1.00 11.61 ? 77  ASN B C   1 
ATOM   600  O  O   . ASN A 1 77  ? 4.223   9.067   -27.930 1.00 12.97 ? 77  ASN B O   1 
ATOM   601  C  CB  . ASN A 1 77  ? 5.790   8.390   -29.925 1.00 12.76 ? 77  ASN B CB  1 
ATOM   602  C  CG  . ASN A 1 77  ? 7.179   8.223   -30.504 1.00 11.11 ? 77  ASN B CG  1 
ATOM   603  O  OD1 . ASN A 1 77  ? 8.033   7.531   -29.944 1.00 11.09 ? 77  ASN B OD1 1 
ATOM   604  N  ND2 . ASN A 1 77  ? 7.421   8.837   -31.643 1.00 13.03 ? 77  ASN B ND2 1 
ATOM   605  N  N   . LYS A 1 78  ? 3.711   6.969   -27.214 1.00 11.33 ? 78  LYS B N   1 
ATOM   606  C  CA  . LYS A 1 78  ? 2.802   7.456   -26.220 1.00 11.48 ? 78  LYS B CA  1 
ATOM   607  C  C   . LYS A 1 78  ? 3.530   8.260   -25.098 1.00 11.47 ? 78  LYS B C   1 
ATOM   608  O  O   . LYS A 1 78  ? 2.970   9.192   -24.508 1.00 10.36 ? 78  LYS B O   1 
ATOM   609  C  CB  . LYS A 1 78  ? 1.982   6.304   -25.597 1.00 12.98 ? 78  LYS B CB  1 
ATOM   610  C  CG  . LYS A 1 78  ? 0.946   5.722   -26.553 1.00 14.26 ? 78  LYS B CG  1 
ATOM   611  C  CD  . LYS A 1 78  ? 0.247   4.539   -25.932 1.00 16.89 ? 78  LYS B CD  1 
ATOM   612  C  CE  . LYS A 1 78  ? -0.649  3.859   -26.979 1.00 20.40 ? 78  LYS B CE  1 
ATOM   613  N  NZ  . LYS A 1 78  ? -1.091  2.542   -26.402 1.00 19.32 ? 78  LYS B NZ  1 
ATOM   614  N  N   . SER A 1 79  ? 4.733   7.838   -24.763 1.00 10.18 ? 79  SER B N   1 
ATOM   615  C  CA  . SER A 1 79  ? 5.496   8.484   -23.702 1.00 10.36 ? 79  SER B CA  1 
ATOM   616  C  C   . SER A 1 79  ? 6.899   8.782   -24.244 1.00 9.85  ? 79  SER B C   1 
ATOM   617  O  O   . SER A 1 79  ? 7.643   7.855   -24.670 1.00 10.51 ? 79  SER B O   1 
ATOM   618  C  CB  . SER A 1 79  ? 5.634   7.567   -22.470 1.00 9.88  ? 79  SER B CB  1 
ATOM   619  O  OG  . SER A 1 79  ? 4.345   7.271   -21.895 1.00 10.31 ? 79  SER B OG  1 
ATOM   620  N  N   . VAL A 1 80  ? 7.240   10.069  -24.219 1.00 9.69  ? 80  VAL B N   1 
ATOM   621  C  CA  . VAL A 1 80  ? 8.475   10.565  -24.877 1.00 9.40  ? 80  VAL B CA  1 
ATOM   622  C  C   . VAL A 1 80  ? 9.095   11.693  -24.078 1.00 9.50  ? 80  VAL B C   1 
ATOM   623  O  O   . VAL A 1 80  ? 8.403   12.404  -23.291 1.00 9.69  ? 80  VAL B O   1 
ATOM   624  C  CB  . VAL A 1 80  ? 8.222   11.104  -26.300 1.00 10.44 ? 80  VAL B CB  1 
ATOM   625  C  CG1 . VAL A 1 80  ? 7.783   10.002  -27.260 1.00 9.88  ? 80  VAL B CG1 1 
ATOM   626  C  CG2 . VAL A 1 80  ? 7.178   12.215  -26.234 1.00 10.85 ? 80  VAL B CG2 1 
ATOM   627  N  N   . LEU A 1 81  ? 10.374  11.886  -24.328 1.00 10.20 ? 81  LEU B N   1 
ATOM   628  C  CA  . LEU A 1 81  ? 11.137  13.063  -23.850 1.00 9.82  ? 81  LEU B CA  1 
ATOM   629  C  C   . LEU A 1 81  ? 11.681  13.747  -25.086 1.00 10.18 ? 81  LEU B C   1 
ATOM   630  O  O   . LEU A 1 81  ? 12.271  13.092  -25.951 1.00 10.85 ? 81  LEU B O   1 
ATOM   631  C  CB  . LEU A 1 81  ? 12.358  12.606  -22.992 1.00 9.98  ? 81  LEU B CB  1 
ATOM   632  C  CG  . LEU A 1 81  ? 13.407  13.650  -22.616 1.00 10.30 ? 81  LEU B CG  1 
ATOM   633  C  CD1 . LEU A 1 81  ? 12.740  14.660  -21.694 1.00 12.04 ? 81  LEU B CD1 1 
ATOM   634  C  CD2 . LEU A 1 81  ? 14.423  12.890  -21.765 1.00 11.32 ? 81  LEU B CD2 1 
ATOM   635  N  N   . ARG A 1 82  ? 11.498  15.060  -25.122 1.00 9.47  ? 82  ARG B N   1 
ATOM   636  C  CA  . ARG A 1 82  ? 11.928  15.897  -26.257 1.00 11.68 ? 82  ARG B CA  1 
ATOM   637  C  C   . ARG A 1 82  ? 12.647  17.154  -25.716 1.00 11.53 ? 82  ARG B C   1 
ATOM   638  O  O   . ARG A 1 82  ? 12.493  17.522  -24.557 1.00 10.81 ? 82  ARG B O   1 
ATOM   639  C  CB  . ARG A 1 82  ? 10.698  16.360  -27.089 1.00 13.42 ? 82  ARG B CB  1 
ATOM   640  C  CG  . ARG A 1 82  ? 9.626   15.292  -27.380 1.00 18.72 ? 82  ARG B CG  1 
ATOM   641  C  CD  . ARG A 1 82  ? 8.172   15.747  -27.615 1.00 18.96 ? 82  ARG B CD  1 
ATOM   642  N  NE  . ARG A 1 82  ? 7.447   16.390  -26.489 1.00 18.81 ? 82  ARG B NE  1 
ATOM   643  C  CZ  . ARG A 1 82  ? 6.148   16.279  -26.263 1.00 18.58 ? 82  ARG B CZ  1 
ATOM   644  N  NH1 . ARG A 1 82  ? 5.386   15.488  -27.012 1.00 16.95 ? 82  ARG B NH1 1 
ATOM   645  N  NH2 . ARG A 1 82  ? 5.600   17.001  -25.255 1.00 18.34 ? 82  ARG B NH2 1 
ATOM   646  N  N   . GLY A 1 83  ? 13.446  17.831  -26.545 1.00 10.64 ? 83  GLY B N   1 
ATOM   647  C  CA  . GLY A 1 83  ? 13.956  19.099  -26.113 1.00 11.27 ? 83  GLY B CA  1 
ATOM   648  C  C   . GLY A 1 83  ? 15.211  18.831  -25.302 1.00 11.04 ? 83  GLY B C   1 
ATOM   649  O  O   . GLY A 1 83  ? 15.895  17.825  -25.552 1.00 11.59 ? 83  GLY B O   1 
ATOM   650  N  N   . GLY A 1 84  ? 15.530  19.696  -24.336 1.00 10.67 ? 84  GLY B N   1 
ATOM   651  C  CA  . GLY A 1 84  ? 16.797  19.559  -23.583 1.00 11.30 ? 84  GLY B CA  1 
ATOM   652  C  C   . GLY A 1 84  ? 17.972  19.665  -24.550 1.00 12.23 ? 84  GLY B C   1 
ATOM   653  O  O   . GLY A 1 84  ? 17.942  20.435  -25.506 1.00 12.78 ? 84  GLY B O   1 
ATOM   654  N  N   . PRO A 1 85  ? 18.983  18.837  -24.379 1.00 12.60 ? 85  PRO B N   1 
ATOM   655  C  CA  . PRO A 1 85  ? 20.118  18.804  -25.344 1.00 11.39 ? 85  PRO B CA  1 
ATOM   656  C  C   . PRO A 1 85  ? 19.880  17.860  -26.526 1.00 11.43 ? 85  PRO B C   1 
ATOM   657  O  O   . PRO A 1 85  ? 20.748  17.711  -27.377 1.00 12.72 ? 85  PRO B O   1 
ATOM   658  C  CB  . PRO A 1 85  ? 21.267  18.160  -24.485 1.00 11.99 ? 85  PRO B CB  1 
ATOM   659  C  CG  . PRO A 1 85  ? 20.494  17.253  -23.566 1.00 10.85 ? 85  PRO B CG  1 
ATOM   660  C  CD  . PRO A 1 85  ? 19.238  17.985  -23.177 1.00 11.86 ? 85  PRO B CD  1 
ATOM   661  N  N   . LEU A 1 86  ? 18.696  17.253  -26.591 1.00 10.69 ? 86  LEU B N   1 
ATOM   662  C  CA  . LEU A 1 86  ? 18.412  16.173  -27.519 1.00 11.39 ? 86  LEU B CA  1 
ATOM   663  C  C   . LEU A 1 86  ? 17.989  16.669  -28.910 1.00 11.45 ? 86  LEU B C   1 
ATOM   664  O  O   . LEU A 1 86  ? 17.242  17.645  -29.037 1.00 12.64 ? 86  LEU B O   1 
ATOM   665  C  CB  . LEU A 1 86  ? 17.255  15.305  -26.952 1.00 10.52 ? 86  LEU B CB  1 
ATOM   666  C  CG  . LEU A 1 86  ? 17.565  14.743  -25.551 1.00 10.57 ? 86  LEU B CG  1 
ATOM   667  C  CD1 . LEU A 1 86  ? 16.310  14.106  -24.980 1.00 10.04 ? 86  LEU B CD1 1 
ATOM   668  C  CD2 . LEU A 1 86  ? 18.774  13.755  -25.539 1.00 10.62 ? 86  LEU B CD2 1 
ATOM   669  N  N   . THR A 1 87  ? 18.459  15.988  -29.950 1.00 12.16 ? 87  THR B N   1 
ATOM   670  C  CA  . THR A 1 87  ? 17.839  16.144  -31.282 1.00 12.40 ? 87  THR B CA  1 
ATOM   671  C  C   . THR A 1 87  ? 16.741  15.117  -31.420 1.00 12.44 ? 87  THR B C   1 
ATOM   672  O  O   . THR A 1 87  ? 17.002  13.890  -31.289 1.00 14.14 ? 87  THR B O   1 
ATOM   673  C  CB  . THR A 1 87  ? 18.953  15.920  -32.343 1.00 12.99 ? 87  THR B CB  1 
ATOM   674  O  OG1 . THR A 1 87  ? 20.000  16.874  -32.121 1.00 16.97 ? 87  THR B OG1 1 
ATOM   675  C  CG2 . THR A 1 87  ? 18.384  16.018  -33.780 1.00 12.82 ? 87  THR B CG2 1 
ATOM   676  N  N   . GLY A 1 88  ? 15.502  15.536  -31.697 1.00 11.82 ? 88  GLY B N   1 
ATOM   677  C  CA  . GLY A 1 88  ? 14.471  14.536  -31.968 1.00 12.88 ? 88  GLY B CA  1 
ATOM   678  C  C   . GLY A 1 88  ? 13.819  13.987  -30.692 1.00 13.10 ? 88  GLY B C   1 
ATOM   679  O  O   . GLY A 1 88  ? 13.982  14.556  -29.579 1.00 15.56 ? 88  GLY B O   1 
ATOM   680  N  N   . SER A 1 89  ? 13.079  12.899  -30.836 1.00 12.78 ? 89  SER B N   1 
ATOM   681  C  CA  . SER A 1 89  ? 12.203  12.432  -29.760 1.00 11.96 ? 89  SER B CA  1 
ATOM   682  C  C   . SER A 1 89  ? 12.750  11.115  -29.233 1.00 12.03 ? 89  SER B C   1 
ATOM   683  O  O   . SER A 1 89  ? 13.064  10.210  -30.012 1.00 12.73 ? 89  SER B O   1 
ATOM   684  C  CB  . SER A 1 89  ? 10.763  12.197  -30.307 1.00 12.61 ? 89  SER B CB  1 
ATOM   685  O  OG  . SER A 1 89  ? 9.866   11.699  -29.322 1.00 13.92 ? 89  SER B OG  1 
ATOM   686  N  N   . TYR A 1 90  ? 12.795  10.990  -27.884 1.00 10.29 ? 90  TYR B N   1 
ATOM   687  C  CA  . TYR A 1 90  ? 13.362  9.844   -27.214 1.00 9.99  ? 90  TYR B CA  1 
ATOM   688  C  C   . TYR A 1 90  ? 12.262  9.155   -26.436 1.00 9.09  ? 90  TYR B C   1 
ATOM   689  O  O   . TYR A 1 90  ? 11.493  9.795   -25.712 1.00 9.83  ? 90  TYR B O   1 
ATOM   690  C  CB  . TYR A 1 90  ? 14.503  10.252  -26.235 1.00 9.83  ? 90  TYR B CB  1 
ATOM   691  C  CG  . TYR A 1 90  ? 15.842  10.479  -26.899 1.00 9.81  ? 90  TYR B CG  1 
ATOM   692  C  CD1 . TYR A 1 90  ? 16.011  11.572  -27.791 1.00 10.49 ? 90  TYR B CD1 1 
ATOM   693  C  CD2 . TYR A 1 90  ? 16.938  9.668   -26.628 1.00 9.89  ? 90  TYR B CD2 1 
ATOM   694  C  CE1 . TYR A 1 90  ? 17.242  11.806  -28.403 1.00 10.57 ? 90  TYR B CE1 1 
ATOM   695  C  CE2 . TYR A 1 90  ? 18.175  9.942   -27.217 1.00 9.28  ? 90  TYR B CE2 1 
ATOM   696  C  CZ  . TYR A 1 90  ? 18.307  11.009  -28.074 1.00 10.37 ? 90  TYR B CZ  1 
ATOM   697  O  OH  . TYR A 1 90  ? 19.488  11.232  -28.689 1.00 11.11 ? 90  TYR B OH  1 
ATOM   698  N  N   . ARG A 1 91  ? 12.137  7.838   -26.640 1.00 8.96  ? 91  ARG B N   1 
ATOM   699  C  CA  . ARG A 1 91  ? 10.936  7.117   -26.207 1.00 8.60  ? 91  ARG B CA  1 
ATOM   700  C  C   . ARG A 1 91  ? 11.190  6.468   -24.843 1.00 8.89  ? 91  ARG B C   1 
ATOM   701  O  O   . ARG A 1 91  ? 12.222  5.851   -24.652 1.00 9.10  ? 91  ARG B O   1 
ATOM   702  C  CB  . ARG A 1 91  ? 10.595  6.044   -27.245 1.00 8.83  ? 91  ARG B CB  1 
ATOM   703  C  CG  . ARG A 1 91  ? 9.324   5.224   -26.905 1.00 9.17  ? 91  ARG B CG  1 
ATOM   704  C  CD  . ARG A 1 91  ? 9.016   4.188   -28.063 1.00 9.58  ? 91  ARG B CD  1 
ATOM   705  N  NE  . ARG A 1 91  ? 8.919   4.895   -29.357 1.00 8.87  ? 91  ARG B NE  1 
ATOM   706  C  CZ  . ARG A 1 91  ? 8.827   4.233   -30.540 1.00 10.08 ? 91  ARG B CZ  1 
ATOM   707  N  NH1 . ARG A 1 91  ? 8.781   2.889   -30.583 1.00 9.87  ? 91  ARG B NH1 1 
ATOM   708  N  NH2 . ARG A 1 91  ? 8.778   4.916   -31.707 1.00 9.89  ? 91  ARG B NH2 1 
ATOM   709  N  N   . LEU A 1 92  ? 10.192  6.530   -23.947 1.00 8.26  ? 92  LEU B N   1 
ATOM   710  C  CA  . LEU A 1 92  ? 10.346  5.969   -22.563 1.00 7.73  ? 92  LEU B CA  1 
ATOM   711  C  C   . LEU A 1 92  ? 10.406  4.430   -22.560 1.00 9.01  ? 92  LEU B C   1 
ATOM   712  O  O   . LEU A 1 92  ? 9.544   3.742   -23.174 1.00 9.72  ? 92  LEU B O   1 
ATOM   713  C  CB  . LEU A 1 92  ? 9.192   6.447   -21.701 1.00 8.06  ? 92  LEU B CB  1 
ATOM   714  C  CG  . LEU A 1 92  ? 9.105   5.969   -20.222 1.00 8.55  ? 92  LEU B CG  1 
ATOM   715  C  CD1 . LEU A 1 92  ? 10.292  6.396   -19.332 1.00 9.01  ? 92  LEU B CD1 1 
ATOM   716  C  CD2 . LEU A 1 92  ? 7.756   6.464   -19.674 1.00 8.07  ? 92  LEU B CD2 1 
ATOM   717  N  N   . ARG A 1 93  ? 11.400  3.896   -21.877 1.00 8.89  ? 93  ARG B N   1 
ATOM   718  C  CA  . ARG A 1 93  ? 11.625  2.442   -21.797 1.00 9.52  ? 93  ARG B CA  1 
ATOM   719  C  C   . ARG A 1 93  ? 11.406  1.889   -20.416 1.00 9.63  ? 93  ARG B C   1 
ATOM   720  O  O   . ARG A 1 93  ? 10.691  0.908   -20.215 1.00 9.43  ? 93  ARG B O   1 
ATOM   721  C  CB  . ARG A 1 93  ? 13.086  2.121   -22.256 1.00 11.38 ? 93  ARG B CB  1 
ATOM   722  C  CG  . ARG A 1 93  ? 13.491  0.640   -22.111 1.00 11.97 ? 93  ARG B CG  1 
ATOM   723  C  CD  . ARG A 1 93  ? 12.870  -0.182  -23.191 1.00 14.12 ? 93  ARG B CD  1 
ATOM   724  N  NE  . ARG A 1 93  ? 13.316  -1.587  -23.143 1.00 13.55 ? 93  ARG B NE  1 
ATOM   725  C  CZ  . ARG A 1 93  ? 13.054  -2.521  -24.073 1.00 15.97 ? 93  ARG B CZ  1 
ATOM   726  N  NH1 . ARG A 1 93  ? 12.304  -2.265  -25.167 1.00 13.94 ? 93  ARG B NH1 1 
ATOM   727  N  NH2 . ARG A 1 93  ? 13.521  -3.750  -23.888 1.00 16.52 ? 93  ARG B NH2 1 
ATOM   728  N  N   . GLN A 1 94  ? 12.105  2.484   -19.436 1.00 9.63  ? 94  GLN B N   1 
ATOM   729  C  CA  . GLN A 1 94  ? 12.138  1.884   -18.088 1.00 9.48  ? 94  GLN B CA  1 
ATOM   730  C  C   . GLN A 1 94  ? 12.558  2.894   -17.029 1.00 9.58  ? 94  GLN B C   1 
ATOM   731  O  O   . GLN A 1 94  ? 13.207  3.909   -17.348 1.00 9.43  ? 94  GLN B O   1 
ATOM   732  C  CB  . GLN A 1 94  ? 12.982  0.590   -18.043 1.00 13.04 ? 94  GLN B CB  1 
ATOM   733  C  CG  . GLN A 1 94  ? 14.417  0.736   -18.422 1.00 15.83 ? 94  GLN B CG  1 
ATOM   734  C  CD  . GLN A 1 94  ? 15.374  0.751   -17.188 1.00 16.83 ? 94  GLN B CD  1 
ATOM   735  O  OE1 . GLN A 1 94  ? 15.141  1.433   -16.206 1.00 16.26 ? 94  GLN B OE1 1 
ATOM   736  N  NE2 . GLN A 1 94  ? 16.505  0.075   -17.323 1.00 21.56 ? 94  GLN B NE2 1 
ATOM   737  N  N   . VAL A 1 95  ? 12.107  2.657   -15.793 1.00 9.53  ? 95  VAL B N   1 
ATOM   738  C  CA  . VAL A 1 95  ? 12.548  3.498   -14.632 1.00 8.41  ? 95  VAL B CA  1 
ATOM   739  C  C   . VAL A 1 95  ? 13.138  2.572   -13.566 1.00 8.45  ? 95  VAL B C   1 
ATOM   740  O  O   . VAL A 1 95  ? 12.630  1.468   -13.327 1.00 8.86  ? 95  VAL B O   1 
ATOM   741  C  CB  . VAL A 1 95  ? 11.301  4.254   -14.080 1.00 7.80  ? 95  VAL B CB  1 
ATOM   742  C  CG1 . VAL A 1 95  ? 11.606  4.801   -12.678 1.00 8.43  ? 95  VAL B CG1 1 
ATOM   743  C  CG2 . VAL A 1 95  ? 10.990  5.380   -15.070 1.00 7.73  ? 95  VAL B CG2 1 
ATOM   744  N  N   . HIS A 1 96  ? 14.203  3.030   -12.888 1.00 8.10  ? 96  HIS B N   1 
ATOM   745  C  CA  . HIS A 1 96  ? 14.713  2.299   -11.738 1.00 8.06  ? 96  HIS B CA  1 
ATOM   746  C  C   . HIS A 1 96  ? 15.354  3.336   -10.782 1.00 7.82  ? 96  HIS B C   1 
ATOM   747  O  O   . HIS A 1 96  ? 15.336  4.547   -11.068 1.00 8.53  ? 96  HIS B O   1 
ATOM   748  C  CB  . HIS A 1 96  ? 15.707  1.250   -12.236 1.00 8.41  ? 96  HIS B CB  1 
ATOM   749  C  CG  . HIS A 1 96  ? 16.871  1.860   -12.916 1.00 8.40  ? 96  HIS B CG  1 
ATOM   750  N  ND1 . HIS A 1 96  ? 16.904  2.090   -14.269 1.00 9.92  ? 96  HIS B ND1 1 
ATOM   751  C  CD2 . HIS A 1 96  ? 18.014  2.402   -12.404 1.00 8.52  ? 96  HIS B CD2 1 
ATOM   752  C  CE1 . HIS A 1 96  ? 18.051  2.691   -14.582 1.00 9.65  ? 96  HIS B CE1 1 
ATOM   753  N  NE2 . HIS A 1 96  ? 18.748  2.876   -13.468 1.00 8.54  ? 96  HIS B NE2 1 
ATOM   754  N  N   . LEU A 1 97  ? 15.936  2.877   -9.674  1.00 8.08  ? 97  LEU B N   1 
ATOM   755  C  CA  . LEU A 1 97  ? 16.347  3.736   -8.581  1.00 8.21  ? 97  LEU B CA  1 
ATOM   756  C  C   . LEU A 1 97  ? 17.655  3.216   -8.030  1.00 8.05  ? 97  LEU B C   1 
ATOM   757  O  O   . LEU A 1 97  ? 17.862  1.969   -7.951  1.00 8.76  ? 97  LEU B O   1 
ATOM   758  C  CB  . LEU A 1 97  ? 15.307  3.651   -7.426  1.00 8.13  ? 97  LEU B CB  1 
ATOM   759  C  CG  . LEU A 1 97  ? 15.526  4.616   -6.290  1.00 8.88  ? 97  LEU B CG  1 
ATOM   760  C  CD1 . LEU A 1 97  ? 15.280  6.082   -6.659  1.00 9.66  ? 97  LEU B CD1 1 
ATOM   761  C  CD2 . LEU A 1 97  ? 14.590  4.203   -5.092  1.00 8.94  ? 97  LEU B CD2 1 
ATOM   762  N  N   . HIS A 1 98  ? 18.534  4.152   -7.650  1.00 8.33  ? 98  HIS B N   1 
ATOM   763  C  CA  . HIS A 1 98  ? 19.792  3.736   -6.963  1.00 8.57  ? 98  HIS B CA  1 
ATOM   764  C  C   . HIS A 1 98  ? 19.796  4.357   -5.581  1.00 8.98  ? 98  HIS B C   1 
ATOM   765  O  O   . HIS A 1 98  ? 19.322  5.508   -5.416  1.00 8.60  ? 98  HIS B O   1 
ATOM   766  C  CB  . HIS A 1 98  ? 21.033  4.272   -7.687  1.00 8.10  ? 98  HIS B CB  1 
ATOM   767  C  CG  . HIS A 1 98  ? 21.167  3.819   -9.115  1.00 8.72  ? 98  HIS B CG  1 
ATOM   768  N  ND1 . HIS A 1 98  ? 21.864  2.684   -9.479  1.00 8.61  ? 98  HIS B ND1 1 
ATOM   769  C  CD2 . HIS A 1 98  ? 20.603  4.304   -10.253 1.00 8.71  ? 98  HIS B CD2 1 
ATOM   770  C  CE1 . HIS A 1 98  ? 21.758  2.503   -10.801 1.00 9.42  ? 98  HIS B CE1 1 
ATOM   771  N  NE2 . HIS A 1 98  ? 21.017  3.498   -11.290 1.00 8.69  ? 98  HIS B NE2 1 
ATOM   772  N  N   . TRP A 1 99  ? 20.411  3.669   -4.613  1.00 8.38  ? 99  TRP B N   1 
ATOM   773  C  CA  . TRP A 1 99  ? 20.516  4.117   -3.239  1.00 8.59  ? 99  TRP B CA  1 
ATOM   774  C  C   . TRP A 1 99  ? 21.827  3.640   -2.664  1.00 8.85  ? 99  TRP B C   1 
ATOM   775  O  O   . TRP A 1 99  ? 22.623  3.026   -3.374  1.00 8.72  ? 99  TRP B O   1 
ATOM   776  C  CB  . TRP A 1 99  ? 19.298  3.643   -2.398  1.00 8.05  ? 99  TRP B CB  1 
ATOM   777  C  CG  . TRP A 1 99  ? 19.127  2.151   -2.432  1.00 8.03  ? 99  TRP B CG  1 
ATOM   778  C  CD1 . TRP A 1 99  ? 19.694  1.249   -1.611  1.00 7.83  ? 99  TRP B CD1 1 
ATOM   779  C  CD2 . TRP A 1 99  ? 18.252  1.439   -3.273  1.00 8.14  ? 99  TRP B CD2 1 
ATOM   780  N  NE1 . TRP A 1 99  ? 19.288  -0.040  -1.937  1.00 8.58  ? 99  TRP B NE1 1 
ATOM   781  C  CE2 . TRP A 1 99  ? 18.385  0.058   -2.971  1.00 8.64  ? 99  TRP B CE2 1 
ATOM   782  C  CE3 . TRP A 1 99  ? 17.435  1.816   -4.376  1.00 8.16  ? 99  TRP B CE3 1 
ATOM   783  C  CZ2 . TRP A 1 99  ? 17.684  -0.931  -3.656  1.00 8.54  ? 99  TRP B CZ2 1 
ATOM   784  C  CZ3 . TRP A 1 99  ? 16.743  0.836   -5.036  1.00 8.14  ? 99  TRP B CZ3 1 
ATOM   785  C  CH2 . TRP A 1 99  ? 16.855  -0.541  -4.703  1.00 9.56  ? 99  TRP B CH2 1 
ATOM   786  N  N   . GLY A 1 100 ? 22.062  3.923   -1.406  1.00 9.26  ? 100 GLY B N   1 
ATOM   787  C  CA  . GLY A 1 100 ? 23.255  3.456   -0.691  1.00 9.08  ? 100 GLY B CA  1 
ATOM   788  C  C   . GLY A 1 100 ? 22.800  2.870   0.659   1.00 9.76  ? 100 GLY B C   1 
ATOM   789  O  O   . GLY A 1 100 ? 21.564  2.846   0.959   1.00 9.72  ? 100 GLY B O   1 
ATOM   790  N  N   . SER A 1 101 ? 23.781  2.351   1.453   1.00 11.16 ? 101 SER B N   1 
ATOM   791  C  CA  . SER A 1 101 ? 23.410  1.836   2.766   1.00 11.35 ? 101 SER B CA  1 
ATOM   792  C  C   . SER A 1 101 ? 23.089  2.932   3.789   1.00 12.38 ? 101 SER B C   1 
ATOM   793  O  O   . SER A 1 101 ? 22.442  2.663   4.814   1.00 12.59 ? 101 SER B O   1 
ATOM   794  C  CB  . SER A 1 101 ? 24.478  0.886   3.286   1.00 12.19 ? 101 SER B CB  1 
ATOM   795  O  OG  . SER A 1 101 ? 25.535  1.637   3.740   1.00 13.55 ? 101 SER B OG  1 
ATOM   796  N  N   . ALA A 1 102 ? 23.459  4.171   3.471   1.00 12.38 ? 102 ALA B N   1 
ATOM   797  C  CA  . ALA A 1 102 ? 23.215  5.320   4.376   1.00 11.67 ? 102 ALA B CA  1 
ATOM   798  C  C   . ALA A 1 102 ? 22.425  6.399   3.627   1.00 12.65 ? 102 ALA B C   1 
ATOM   799  O  O   . ALA A 1 102 ? 22.663  6.643   2.455   1.00 12.58 ? 102 ALA B O   1 
ATOM   800  C  CB  . ALA A 1 102 ? 24.525  5.884   4.902   1.00 11.87 ? 102 ALA B CB  1 
ATOM   801  N  N   . ASP A 1 103 ? 21.509  7.023   4.334   1.00 12.04 ? 103 ASP B N   1 
ATOM   802  C  CA  . ASP A 1 103 ? 20.663  8.072   3.723   1.00 12.00 ? 103 ASP B CA  1 
ATOM   803  C  C   . ASP A 1 103 ? 21.385  9.281   3.232   1.00 13.37 ? 103 ASP B C   1 
ATOM   804  O  O   . ASP A 1 103 ? 20.779  10.044  2.473   1.00 14.31 ? 103 ASP B O   1 
ATOM   805  C  CB  . ASP A 1 103 ? 19.567  8.474   4.740   1.00 12.33 ? 103 ASP B CB  1 
ATOM   806  C  CG  . ASP A 1 103 ? 18.448  7.413   4.881   1.00 13.35 ? 103 ASP B CG  1 
ATOM   807  O  OD1 . ASP A 1 103 ? 18.516  6.323   4.291   1.00 15.57 ? 103 ASP B OD1 1 
ATOM   808  O  OD2 . ASP A 1 103 ? 17.465  7.660   5.615   1.00 16.05 ? 103 ASP B OD2 1 
ATOM   809  N  N   . ASP A 1 104 ? 22.667  9.488   3.578   1.00 14.98 ? 104 ASP B N   1 
ATOM   810  C  CA  . ASP A 1 104 ? 23.340  10.669  3.053   1.00 17.72 ? 104 ASP B CA  1 
ATOM   811  C  C   . ASP A 1 104 ? 24.385  10.319  2.031   1.00 16.32 ? 104 ASP B C   1 
ATOM   812  O  O   . ASP A 1 104 ? 25.243  11.153  1.709   1.00 17.75 ? 104 ASP B O   1 
ATOM   813  C  CB  . ASP A 1 104 ? 23.977  11.452  4.222   1.00 19.58 ? 104 ASP B CB  1 
ATOM   814  C  CG  . ASP A 1 104 ? 25.026  10.615  4.990   1.00 22.65 ? 104 ASP B CG  1 
ATOM   815  O  OD1 . ASP A 1 104 ? 24.988  9.385   4.999   1.00 19.77 ? 104 ASP B OD1 1 
ATOM   816  O  OD2 . ASP A 1 104 ? 25.953  11.189  5.601   1.00 26.47 ? 104 ASP B OD2 1 
ATOM   817  N  N   . HIS A 1 105 ? 24.352  9.095   1.504   1.00 13.99 ? 105 HIS B N   1 
ATOM   818  C  CA  . HIS A 1 105 ? 25.305  8.751   0.493   1.00 14.26 ? 105 HIS B CA  1 
ATOM   819  C  C   . HIS A 1 105 ? 24.707  7.673   -0.429  1.00 12.35 ? 105 HIS B C   1 
ATOM   820  O  O   . HIS A 1 105 ? 25.162  6.563   -0.464  1.00 12.43 ? 105 HIS B O   1 
ATOM   821  C  CB  . HIS A 1 105 ? 26.586  8.234   1.181   1.00 18.38 ? 105 HIS B CB  1 
ATOM   822  C  CG  . HIS A 1 105 ? 27.789  8.335   0.311   1.00 23.28 ? 105 HIS B CG  1 
ATOM   823  N  ND1 . HIS A 1 105 ? 28.319  7.247   -0.350  1.00 25.91 ? 105 HIS B ND1 1 
ATOM   824  C  CD2 . HIS A 1 105 ? 28.522  9.417   -0.070  1.00 26.39 ? 105 HIS B CD2 1 
ATOM   825  C  CE1 . HIS A 1 105 ? 29.365  7.643   -1.065  1.00 30.03 ? 105 HIS B CE1 1 
ATOM   826  N  NE2 . HIS A 1 105 ? 29.496  8.958   -0.927  1.00 28.15 ? 105 HIS B NE2 1 
ATOM   827  N  N   . GLY A 1 106 ? 23.667  8.029   -1.181  1.00 10.91 ? 106 GLY B N   1 
ATOM   828  C  CA  . GLY A 1 106 ? 22.927  7.074   -1.963  1.00 10.15 ? 106 GLY B CA  1 
ATOM   829  C  C   . GLY A 1 106 ? 22.905  7.391   -3.467  1.00 10.85 ? 106 GLY B C   1 
ATOM   830  O  O   . GLY A 1 106 ? 22.695  6.470   -4.267  1.00 11.32 ? 106 GLY B O   1 
ATOM   831  N  N   . SER A 1 107 ? 23.122  8.650   -3.844  1.00 9.78  ? 107 SER B N   1 
ATOM   832  C  CA  . SER A 1 107 ? 22.948  8.995   -5.300  1.00 9.16  ? 107 SER B CA  1 
ATOM   833  C  C   . SER A 1 107 ? 24.199  8.591   -6.084  1.00 8.91  ? 107 SER B C   1 
ATOM   834  O  O   . SER A 1 107 ? 25.251  8.235   -5.519  1.00 9.44  ? 107 SER B O   1 
ATOM   835  C  CB  . SER A 1 107 ? 22.649  10.499  -5.486  1.00 9.09  ? 107 SER B CB  1 
ATOM   836  O  OG  . SER A 1 107 ? 23.717  11.238  -4.955  1.00 9.48  ? 107 SER B OG  1 
ATOM   837  N  N   . GLU A 1 108 ? 24.059  8.590   -7.409  1.00 10.29 ? 108 GLU B N   1 
ATOM   838  C  CA  . GLU A 1 108 ? 25.175  8.258   -8.303  1.00 8.87  ? 108 GLU B CA  1 
ATOM   839  C  C   . GLU A 1 108 ? 25.858  9.552   -8.711  1.00 9.13  ? 108 GLU B C   1 
ATOM   840  O  O   . GLU A 1 108 ? 27.051  9.694   -8.524  1.00 8.83  ? 108 GLU B O   1 
ATOM   841  C  CB  . GLU A 1 108 ? 24.614  7.492   -9.513  1.00 10.76 ? 108 GLU B CB  1 
ATOM   842  C  CG  . GLU A 1 108 ? 24.177  6.074   -9.123  1.00 11.23 ? 108 GLU B CG  1 
ATOM   843  C  CD  . GLU A 1 108 ? 24.336  5.007   -10.172 1.00 11.43 ? 108 GLU B CD  1 
ATOM   844  O  OE1 . GLU A 1 108 ? 23.774  5.240   -11.290 1.00 10.46 ? 108 GLU B OE1 1 
ATOM   845  O  OE2 . GLU A 1 108 ? 24.837  3.902   -9.891  1.00 11.59 ? 108 GLU B OE2 1 
ATOM   846  N  N   . HIS A 1 109 ? 25.133  10.530  -9.233  1.00 8.92  ? 109 HIS B N   1 
ATOM   847  C  CA  . HIS A 1 109 ? 25.703  11.853  -9.427  1.00 9.35  ? 109 HIS B CA  1 
ATOM   848  C  C   . HIS A 1 109 ? 25.817  12.548  -8.073  1.00 9.29  ? 109 HIS B C   1 
ATOM   849  O  O   . HIS A 1 109 ? 25.011  12.323  -7.172  1.00 9.26  ? 109 HIS B O   1 
ATOM   850  C  CB  . HIS A 1 109 ? 24.852  12.636  -10.408 1.00 9.17  ? 109 HIS B CB  1 
ATOM   851  C  CG  . HIS A 1 109 ? 24.922  12.039  -11.786 1.00 9.37  ? 109 HIS B CG  1 
ATOM   852  N  ND1 . HIS A 1 109 ? 24.047  11.060  -12.218 1.00 9.39  ? 109 HIS B ND1 1 
ATOM   853  C  CD2 . HIS A 1 109 ? 25.786  12.261  -12.804 1.00 8.65  ? 109 HIS B CD2 1 
ATOM   854  C  CE1 . HIS A 1 109 ? 24.407  10.657  -13.422 1.00 9.33  ? 109 HIS B CE1 1 
ATOM   855  N  NE2 . HIS A 1 109 ? 25.476  11.344  -13.795 1.00 10.62 ? 109 HIS B NE2 1 
ATOM   856  N  N   . ILE A 1 110 ? 26.848  13.384  -7.990  1.00 10.08 ? 110 ILE B N   1 
ATOM   857  C  CA  . ILE A 1 110 ? 27.154  14.023  -6.714  1.00 9.89  ? 110 ILE B CA  1 
ATOM   858  C  C   . ILE A 1 110 ? 27.298  15.528  -7.068  1.00 11.59 ? 110 ILE B C   1 
ATOM   859  O  O   . ILE A 1 110 ? 27.942  15.850  -8.081  1.00 12.53 ? 110 ILE B O   1 
ATOM   860  C  CB  . ILE A 1 110 ? 28.492  13.461  -6.173  1.00 11.55 ? 110 ILE B CB  1 
ATOM   861  C  CG1 . ILE A 1 110 ? 28.443  11.943  -5.923  1.00 11.16 ? 110 ILE B CG1 1 
ATOM   862  C  CG2 . ILE A 1 110 ? 28.882  14.181  -4.849  1.00 10.49 ? 110 ILE B CG2 1 
ATOM   863  C  CD1 . ILE A 1 110 ? 29.804  11.402  -5.493  1.00 13.95 ? 110 ILE B CD1 1 
ATOM   864  N  N   . VAL A 1 111 ? 26.737  16.443  -6.283  1.00 10.19 ? 111 VAL B N   1 
ATOM   865  C  CA  . VAL A 1 111 ? 26.748  17.855  -6.656  1.00 11.58 ? 111 VAL B CA  1 
ATOM   866  C  C   . VAL A 1 111 ? 27.541  18.630  -5.585  1.00 11.32 ? 111 VAL B C   1 
ATOM   867  O  O   . VAL A 1 111 ? 27.127  18.792  -4.419  1.00 11.27 ? 111 VAL B O   1 
ATOM   868  C  CB  . VAL A 1 111 ? 25.299  18.440  -6.837  1.00 12.93 ? 111 VAL B CB  1 
ATOM   869  C  CG1 . VAL A 1 111 ? 25.297  19.908  -7.230  1.00 12.38 ? 111 VAL B CG1 1 
ATOM   870  C  CG2 . VAL A 1 111 ? 24.512  17.630  -7.886  1.00 13.10 ? 111 VAL B CG2 1 
ATOM   871  N  N   . ASP A 1 112 ? 28.666  19.135  -6.016  1.00 12.08 ? 112 ASP B N   1 
ATOM   872  C  CA  . ASP A 1 112 ? 29.609  19.834  -5.082  1.00 13.10 ? 112 ASP B CA  1 
ATOM   873  C  C   . ASP A 1 112 ? 29.854  19.053  -3.822  1.00 13.24 ? 112 ASP B C   1 
ATOM   874  O  O   . ASP A 1 112 ? 29.917  19.609  -2.702  1.00 13.40 ? 112 ASP B O   1 
ATOM   875  C  CB  . ASP A 1 112 ? 29.145  21.281  -4.797  1.00 14.36 ? 112 ASP B CB  1 
ATOM   876  C  CG  . ASP A 1 112 ? 29.206  22.169  -6.056  1.00 14.94 ? 112 ASP B CG  1 
ATOM   877  O  OD1 . ASP A 1 112 ? 30.180  22.082  -6.833  1.00 16.57 ? 112 ASP B OD1 1 
ATOM   878  O  OD2 . ASP A 1 112 ? 28.270  22.972  -6.232  1.00 18.53 ? 112 ASP B OD2 1 
ATOM   879  N  N   . GLY A 1 113 ? 30.035  17.744  -4.008  1.00 12.28 ? 113 GLY B N   1 
ATOM   880  C  CA  . GLY A 1 113 ? 30.314  16.845  -2.933  1.00 14.09 ? 113 GLY B CA  1 
ATOM   881  C  C   . GLY A 1 113 ? 29.115  16.367  -2.172  1.00 13.63 ? 113 GLY B C   1 
ATOM   882  O  O   . GLY A 1 113 ? 29.252  15.499  -1.293  1.00 14.72 ? 113 GLY B O   1 
ATOM   883  N  N   . VAL A 1 114 ? 27.938  16.901  -2.497  1.00 12.61 ? 114 VAL B N   1 
ATOM   884  C  CA  . VAL A 1 114 ? 26.728  16.420  -1.812  1.00 13.11 ? 114 VAL B CA  1 
ATOM   885  C  C   . VAL A 1 114 ? 26.174  15.203  -2.538  1.00 13.84 ? 114 VAL B C   1 
ATOM   886  O  O   . VAL A 1 114 ? 25.822  15.329  -3.719  1.00 13.76 ? 114 VAL B O   1 
ATOM   887  C  CB  . VAL A 1 114 ? 25.655  17.544  -1.652  1.00 13.83 ? 114 VAL B CB  1 
ATOM   888  C  CG1 . VAL A 1 114 ? 24.327  16.978  -1.006  1.00 13.54 ? 114 VAL B CG1 1 
ATOM   889  C  CG2 . VAL A 1 114 ? 26.249  18.667  -0.827  1.00 12.67 ? 114 VAL B CG2 1 
ATOM   890  N  N   . SER A 1 115 ? 26.100  14.055  -1.839  1.00 13.38 ? 115 SER B N   1 
ATOM   891  C  CA  . SER A 1 115 ? 25.372  12.874  -2.334  1.00 12.94 ? 115 SER B CA  1 
ATOM   892  C  C   . SER A 1 115 ? 23.973  12.959  -1.788  1.00 14.12 ? 115 SER B C   1 
ATOM   893  O  O   . SER A 1 115 ? 23.779  13.248  -0.568  1.00 16.28 ? 115 SER B O   1 
ATOM   894  C  CB  . SER A 1 115 ? 26.006  11.545  -1.887  1.00 13.81 ? 115 SER B CB  1 
ATOM   895  O  OG  . SER A 1 115 ? 27.260  11.468  -2.497  1.00 16.75 ? 115 SER B OG  1 
ATOM   896  N  N   . TYR A 1 116 ? 22.969  12.682  -2.634  1.00 12.29 ? 116 TYR B N   1 
ATOM   897  C  CA  . TYR A 1 116 ? 21.594  12.680  -2.140  1.00 10.55 ? 116 TYR B CA  1 
ATOM   898  C  C   . TYR A 1 116 ? 21.260  11.301  -1.582  1.00 10.33 ? 116 TYR B C   1 
ATOM   899  O  O   . TYR A 1 116 ? 22.084  10.402  -1.630  1.00 10.16 ? 116 TYR B O   1 
ATOM   900  C  CB  . TYR A 1 116 ? 20.701  13.108  -3.274  1.00 10.94 ? 116 TYR B CB  1 
ATOM   901  C  CG  . TYR A 1 116 ? 20.923  14.560  -3.608  1.00 11.52 ? 116 TYR B CG  1 
ATOM   902  C  CD1 . TYR A 1 116 ? 20.193  15.528  -2.907  1.00 13.41 ? 116 TYR B CD1 1 
ATOM   903  C  CD2 . TYR A 1 116 ? 21.880  14.978  -4.573  1.00 12.21 ? 116 TYR B CD2 1 
ATOM   904  C  CE1 . TYR A 1 116 ? 20.347  16.868  -3.197  1.00 15.09 ? 116 TYR B CE1 1 
ATOM   905  C  CE2 . TYR A 1 116 ? 22.021  16.353  -4.887  1.00 13.65 ? 116 TYR B CE2 1 
ATOM   906  C  CZ  . TYR A 1 116 ? 21.281  17.267  -4.149  1.00 15.55 ? 116 TYR B CZ  1 
ATOM   907  O  OH  . TYR A 1 116 ? 21.312  18.662  -4.365  1.00 20.99 ? 116 TYR B OH  1 
ATOM   908  N  N   . ALA A 1 117 ? 20.056  11.097  -1.054  1.00 9.03  ? 117 ALA B N   1 
ATOM   909  C  CA  . ALA A 1 117 ? 19.696  9.835   -0.451  1.00 8.20  ? 117 ALA B CA  1 
ATOM   910  C  C   . ALA A 1 117 ? 19.512  8.771   -1.543  1.00 8.65  ? 117 ALA B C   1 
ATOM   911  O  O   . ALA A 1 117 ? 19.705  7.603   -1.303  1.00 9.35  ? 117 ALA B O   1 
ATOM   912  C  CB  . ALA A 1 117 ? 18.378  10.031  0.336   1.00 8.29  ? 117 ALA B CB  1 
ATOM   913  N  N   . ALA A 1 118 ? 19.070  9.168   -2.739  1.00 8.26  ? 118 ALA B N   1 
ATOM   914  C  CA  . ALA A 1 118 ? 18.785  8.153   -3.817  1.00 7.10  ? 118 ALA B CA  1 
ATOM   915  C  C   . ALA A 1 118 ? 18.742  8.939   -5.147  1.00 7.34  ? 118 ALA B C   1 
ATOM   916  O  O   . ALA A 1 118 ? 18.772  10.161  -5.156  1.00 7.05  ? 118 ALA B O   1 
ATOM   917  C  CB  . ALA A 1 118 ? 17.466  7.345   -3.548  1.00 6.76  ? 118 ALA B CB  1 
ATOM   918  N  N   . GLU A 1 119 ? 18.716  8.190   -6.251  1.00 7.63  ? 119 GLU B N   1 
ATOM   919  C  CA  . GLU A 1 119 ? 18.624  8.797   -7.557  1.00 7.23  ? 119 GLU B CA  1 
ATOM   920  C  C   . GLU A 1 119 ? 17.797  7.930   -8.437  1.00 7.61  ? 119 GLU B C   1 
ATOM   921  O  O   . GLU A 1 119 ? 18.120  6.745   -8.675  1.00 8.15  ? 119 GLU B O   1 
ATOM   922  C  CB  . GLU A 1 119 ? 20.048  8.947   -8.124  1.00 7.50  ? 119 GLU B CB  1 
ATOM   923  C  CG  . GLU A 1 119 ? 20.051  9.809   -9.404  1.00 7.04  ? 119 GLU B CG  1 
ATOM   924  C  CD  . GLU A 1 119 ? 21.469  10.036  -9.863  1.00 7.79  ? 119 GLU B CD  1 
ATOM   925  O  OE1 . GLU A 1 119 ? 22.323  10.265  -8.983  1.00 7.71  ? 119 GLU B OE1 1 
ATOM   926  O  OE2 . GLU A 1 119 ? 21.724  10.076  -11.108 1.00 8.43  ? 119 GLU B OE2 1 
ATOM   927  N  N   . LEU A 1 120 ? 16.765  8.562   -9.037  1.00 8.21  ? 120 LEU B N   1 
ATOM   928  C  CA  . LEU A 1 120 ? 15.837  7.865   -9.910  1.00 8.11  ? 120 LEU B CA  1 
ATOM   929  C  C   . LEU A 1 120 ? 16.348  8.078   -11.336 1.00 7.07  ? 120 LEU B C   1 
ATOM   930  O  O   . LEU A 1 120 ? 16.718  9.185   -11.689 1.00 7.69  ? 120 LEU B O   1 
ATOM   931  C  CB  . LEU A 1 120 ? 14.435  8.504   -9.753  1.00 9.13  ? 120 LEU B CB  1 
ATOM   932  C  CG  . LEU A 1 120 ? 13.286  7.847   -10.501 1.00 10.44 ? 120 LEU B CG  1 
ATOM   933  C  CD1 . LEU A 1 120 ? 12.794  6.600   -9.755  1.00 9.92  ? 120 LEU B CD1 1 
ATOM   934  C  CD2 . LEU A 1 120 ? 12.107  8.786   -10.780 1.00 10.22 ? 120 LEU B CD2 1 
ATOM   935  N  N   . HIS A 1 121 ? 16.367  7.005   -12.122 1.00 7.15  ? 121 HIS B N   1 
ATOM   936  C  CA  . HIS A 1 121 ? 16.778  7.071   -13.546 1.00 7.50  ? 121 HIS B CA  1 
ATOM   937  C  C   . HIS A 1 121 ? 15.577  6.771   -14.431 1.00 7.21  ? 121 HIS B C   1 
ATOM   938  O  O   . HIS A 1 121 ? 14.943  5.693   -14.255 1.00 7.50  ? 121 HIS B O   1 
ATOM   939  C  CB  . HIS A 1 121 ? 17.943  6.116   -13.799 1.00 8.60  ? 121 HIS B CB  1 
ATOM   940  C  CG  . HIS A 1 121 ? 19.204  6.654   -13.204 1.00 7.91  ? 121 HIS B CG  1 
ATOM   941  N  ND1 . HIS A 1 121 ? 20.314  5.882   -12.944 1.00 8.65  ? 121 HIS B ND1 1 
ATOM   942  C  CD2 . HIS A 1 121 ? 19.504  7.920   -12.815 1.00 7.76  ? 121 HIS B CD2 1 
ATOM   943  C  CE1 . HIS A 1 121 ? 21.270  6.659   -12.440 1.00 7.74  ? 121 HIS B CE1 1 
ATOM   944  N  NE2 . HIS A 1 121 ? 20.798  7.898   -12.343 1.00 7.52  ? 121 HIS B NE2 1 
ATOM   945  N  N   . VAL A 1 122 ? 15.331  7.675   -15.426 1.00 6.57  ? 122 VAL B N   1 
ATOM   946  C  CA  . VAL A 1 122 ? 14.220  7.446   -16.390 1.00 6.85  ? 122 VAL B CA  1 
ATOM   947  C  C   . VAL A 1 122 ? 14.916  7.234   -17.730 1.00 7.13  ? 122 VAL B C   1 
ATOM   948  O  O   . VAL A 1 122 ? 15.522  8.180   -18.235 1.00 7.58  ? 122 VAL B O   1 
ATOM   949  C  CB  . VAL A 1 122 ? 13.207  8.647   -16.425 1.00 6.77  ? 122 VAL B CB  1 
ATOM   950  C  CG1 . VAL A 1 122 ? 11.975  8.317   -17.278 1.00 6.75  ? 122 VAL B CG1 1 
ATOM   951  C  CG2 . VAL A 1 122 ? 12.728  9.010   -14.995 1.00 8.10  ? 122 VAL B CG2 1 
ATOM   952  N  N   . VAL A 1 123 ? 14.870  6.004   -18.275 1.00 7.24  ? 123 VAL B N   1 
ATOM   953  C  CA  . VAL A 1 123 ? 15.706  5.661   -19.431 1.00 7.23  ? 123 VAL B CA  1 
ATOM   954  C  C   . VAL A 1 123 ? 14.835  5.752   -20.730 1.00 7.65  ? 123 VAL B C   1 
ATOM   955  O  O   . VAL A 1 123 ? 13.721  5.224   -20.787 1.00 7.57  ? 123 VAL B O   1 
ATOM   956  C  CB  . VAL A 1 123 ? 16.233  4.213   -19.277 1.00 7.84  ? 123 VAL B CB  1 
ATOM   957  C  CG1 . VAL A 1 123 ? 17.026  3.790   -20.513 1.00 7.96  ? 123 VAL B CG1 1 
ATOM   958  C  CG2 . VAL A 1 123 ? 17.074  4.032   -18.000 1.00 6.81  ? 123 VAL B CG2 1 
ATOM   959  N  N   . HIS A 1 124 ? 15.359  6.452   -21.732 1.00 7.81  ? 124 HIS B N   1 
ATOM   960  C  CA  . HIS A 1 124 ? 14.628  6.638   -23.014 1.00 8.10  ? 124 HIS B CA  1 
ATOM   961  C  C   . HIS A 1 124 ? 15.565  6.295   -24.153 1.00 8.76  ? 124 HIS B C   1 
ATOM   962  O  O   . HIS A 1 124 ? 16.774  6.431   -24.010 1.00 9.60  ? 124 HIS B O   1 
ATOM   963  C  CB  . HIS A 1 124 ? 14.298  8.114   -23.216 1.00 9.01  ? 124 HIS B CB  1 
ATOM   964  C  CG  . HIS A 1 124 ? 13.614  8.789   -22.052 1.00 9.23  ? 124 HIS B CG  1 
ATOM   965  N  ND1 . HIS A 1 124 ? 14.319  9.200   -20.920 1.00 8.61  ? 124 HIS B ND1 1 
ATOM   966  C  CD2 . HIS A 1 124 ? 12.326  9.209   -21.877 1.00 8.78  ? 124 HIS B CD2 1 
ATOM   967  C  CE1 . HIS A 1 124 ? 13.472  9.752   -20.074 1.00 9.19  ? 124 HIS B CE1 1 
ATOM   968  N  NE2 . HIS A 1 124 ? 12.271  9.791   -20.628 1.00 8.69  ? 124 HIS B NE2 1 
ATOM   969  N  N   . TRP A 1 125 ? 14.997  6.051   -25.336 1.00 8.79  ? 125 TRP B N   1 
ATOM   970  C  CA  . TRP A 1 125 ? 15.824  5.741   -26.510 1.00 9.24  ? 125 TRP B CA  1 
ATOM   971  C  C   . TRP A 1 125 ? 15.408  6.483   -27.767 1.00 9.97  ? 125 TRP B C   1 
ATOM   972  O  O   . TRP A 1 125 ? 14.242  6.858   -27.926 1.00 9.70  ? 125 TRP B O   1 
ATOM   973  C  CB  . TRP A 1 125 ? 15.942  4.209   -26.801 1.00 11.17 ? 125 TRP B CB  1 
ATOM   974  C  CG  . TRP A 1 125 ? 14.602  3.497   -27.065 1.00 10.57 ? 125 TRP B CG  1 
ATOM   975  C  CD1 . TRP A 1 125 ? 13.712  3.042   -26.146 1.00 11.98 ? 125 TRP B CD1 1 
ATOM   976  C  CD2 . TRP A 1 125 ? 14.063  3.121   -28.351 1.00 11.27 ? 125 TRP B CD2 1 
ATOM   977  N  NE1 . TRP A 1 125 ? 12.618  2.454   -26.771 1.00 11.27 ? 125 TRP B NE1 1 
ATOM   978  C  CE2 . TRP A 1 125 ? 12.829  2.474   -28.119 1.00 12.10 ? 125 TRP B CE2 1 
ATOM   979  C  CE3 . TRP A 1 125 ? 14.513  3.272   -29.674 1.00 11.67 ? 125 TRP B CE3 1 
ATOM   980  C  CZ2 . TRP A 1 125 ? 11.994  1.998   -29.160 1.00 11.42 ? 125 TRP B CZ2 1 
ATOM   981  C  CZ3 . TRP A 1 125 ? 13.661  2.767   -30.744 1.00 11.54 ? 125 TRP B CZ3 1 
ATOM   982  C  CH2 . TRP A 1 125 ? 12.451  2.161   -30.478 1.00 12.54 ? 125 TRP B CH2 1 
ATOM   983  N  N   . ASN A 1 126 ? 16.395  6.675   -28.652 1.00 9.11  ? 126 ASN B N   1 
ATOM   984  C  CA  . ASN A 1 126 ? 16.228  7.559   -29.789 1.00 10.58 ? 126 ASN B CA  1 
ATOM   985  C  C   . ASN A 1 126 ? 15.473  6.798   -30.905 1.00 10.93 ? 126 ASN B C   1 
ATOM   986  O  O   . ASN A 1 126 ? 16.094  6.174   -31.756 1.00 10.59 ? 126 ASN B O   1 
ATOM   987  C  CB  . ASN A 1 126 ? 17.604  7.985   -30.290 1.00 11.49 ? 126 ASN B CB  1 
ATOM   988  C  CG  . ASN A 1 126 ? 17.519  9.117   -31.340 1.00 12.11 ? 126 ASN B CG  1 
ATOM   989  O  OD1 . ASN A 1 126 ? 16.448  9.348   -31.924 1.00 14.13 ? 126 ASN B OD1 1 
ATOM   990  N  ND2 . ASN A 1 126 ? 18.651  9.780   -31.609 1.00 13.09 ? 126 ASN B ND2 1 
ATOM   991  N  N   . SER A 1 127 ? 14.159  6.890   -30.888 1.00 10.29 ? 127 SER B N   1 
ATOM   992  C  CA  . SER A 1 127 ? 13.369  6.136   -31.887 1.00 10.50 ? 127 SER B CA  1 
ATOM   993  C  C   . SER A 1 127 ? 13.286  6.924   -33.184 1.00 12.09 ? 127 SER B C   1 
ATOM   994  O  O   . SER A 1 127 ? 12.875  6.347   -34.224 1.00 11.47 ? 127 SER B O   1 
ATOM   995  C  CB  . SER A 1 127 ? 12.003  5.747   -31.332 1.00 10.14 ? 127 SER B CB  1 
ATOM   996  O  OG  . SER A 1 127 ? 11.258  6.848   -30.908 1.00 11.92 ? 127 SER B OG  1 
ATOM   997  N  N   . ASP A 1 128 ? 13.660  8.187   -33.144 1.00 11.53 ? 128 ASP B N   1 
ATOM   998  C  CA  . ASP A 1 128 ? 13.699  8.960   -34.395 1.00 12.59 ? 128 ASP B CA  1 
ATOM   999  C  C   . ASP A 1 128 ? 14.794  8.507   -35.312 1.00 13.41 ? 128 ASP B C   1 
ATOM   1000 O  O   . ASP A 1 128 ? 14.706  8.723   -36.532 1.00 15.42 ? 128 ASP B O   1 
ATOM   1001 C  CB  . ASP A 1 128 ? 13.900  10.462  -34.157 1.00 12.36 ? 128 ASP B CB  1 
ATOM   1002 C  CG  . ASP A 1 128 ? 12.604  11.182  -33.749 1.00 12.26 ? 128 ASP B CG  1 
ATOM   1003 O  OD1 . ASP A 1 128 ? 11.533  10.583  -33.642 1.00 14.55 ? 128 ASP B OD1 1 
ATOM   1004 O  OD2 . ASP A 1 128 ? 12.654  12.389  -33.594 1.00 12.24 ? 128 ASP B OD2 1 
ATOM   1005 N  N   . LYS A 1 129 ? 15.827  7.855   -34.736 1.00 13.25 ? 129 LYS B N   1 
ATOM   1006 C  CA  . LYS A 1 129 ? 16.951  7.381   -35.555 1.00 14.28 ? 129 LYS B CA  1 
ATOM   1007 C  C   . LYS A 1 129 ? 17.242  5.918   -35.546 1.00 14.42 ? 129 LYS B C   1 
ATOM   1008 O  O   . LYS A 1 129 ? 17.975  5.459   -36.422 1.00 14.54 ? 129 LYS B O   1 
ATOM   1009 C  CB  . LYS A 1 129 ? 18.246  8.039   -35.070 1.00 15.86 ? 129 LYS B CB  1 
ATOM   1010 C  CG  . LYS A 1 129 ? 18.394  9.458   -35.541 1.00 21.55 ? 129 LYS B CG  1 
ATOM   1011 C  CD  . LYS A 1 129 ? 19.740  10.065  -35.098 1.00 22.06 ? 129 LYS B CD  1 
ATOM   1012 C  CE  . LYS A 1 129 ? 20.963  9.528   -35.864 1.00 25.05 ? 129 LYS B CE  1 
ATOM   1013 N  NZ  . LYS A 1 129 ? 22.226  10.272  -35.514 1.00 25.17 ? 129 LYS B NZ  1 
ATOM   1014 N  N   . TYR A 1 130 ? 16.780  5.188   -34.517 1.00 12.87 ? 130 TYR B N   1 
ATOM   1015 C  CA  . TYR A 1 130 ? 17.117  3.751   -34.400 1.00 12.50 ? 130 TYR B CA  1 
ATOM   1016 C  C   . TYR A 1 130 ? 15.842  2.945   -34.270 1.00 12.33 ? 130 TYR B C   1 
ATOM   1017 O  O   . TYR A 1 130 ? 14.838  3.456   -33.788 1.00 14.63 ? 130 TYR B O   1 
ATOM   1018 C  CB  . TYR A 1 130 ? 18.046  3.481   -33.159 1.00 12.36 ? 130 TYR B CB  1 
ATOM   1019 C  CG  . TYR A 1 130 ? 19.229  4.334   -33.263 1.00 12.86 ? 130 TYR B CG  1 
ATOM   1020 C  CD1 . TYR A 1 130 ? 20.140  4.122   -34.308 1.00 15.80 ? 130 TYR B CD1 1 
ATOM   1021 C  CD2 . TYR A 1 130 ? 19.407  5.452   -32.448 1.00 14.67 ? 130 TYR B CD2 1 
ATOM   1022 C  CE1 . TYR A 1 130 ? 21.222  4.920   -34.503 1.00 16.99 ? 130 TYR B CE1 1 
ATOM   1023 C  CE2 . TYR A 1 130 ? 20.522  6.244   -32.556 1.00 14.09 ? 130 TYR B CE2 1 
ATOM   1024 C  CZ  . TYR A 1 130 ? 21.435  6.002   -33.612 1.00 18.01 ? 130 TYR B CZ  1 
ATOM   1025 O  OH  . TYR A 1 130 ? 22.526  6.806   -33.832 1.00 17.11 ? 130 TYR B OH  1 
ATOM   1026 N  N   . PRO A 1 131 ? 15.860  1.654   -34.673 1.00 12.97 ? 131 PRO B N   1 
ATOM   1027 C  CA  . PRO A 1 131 ? 14.563  0.932   -34.715 1.00 13.45 ? 131 PRO B CA  1 
ATOM   1028 C  C   . PRO A 1 131 ? 14.139  0.279   -33.403 1.00 13.45 ? 131 PRO B C   1 
ATOM   1029 O  O   . PRO A 1 131 ? 13.006  -0.211  -33.272 1.00 14.43 ? 131 PRO B O   1 
ATOM   1030 C  CB  . PRO A 1 131 ? 14.817  -0.198  -35.764 1.00 14.45 ? 131 PRO B CB  1 
ATOM   1031 C  CG  . PRO A 1 131 ? 16.310  -0.364  -35.805 1.00 14.15 ? 131 PRO B CG  1 
ATOM   1032 C  CD  . PRO A 1 131 ? 16.925  0.979   -35.443 1.00 12.16 ? 131 PRO B CD  1 
ATOM   1033 N  N   . SER A 1 132 ? 15.062  0.190   -32.453 1.00 13.12 ? 132 SER B N   1 
ATOM   1034 C  CA  . SER A 1 132 ? 14.732  -0.464  -31.199 1.00 12.45 ? 132 SER B CA  1 
ATOM   1035 C  C   . SER A 1 132 ? 15.663  0.083   -30.123 1.00 11.40 ? 132 SER B C   1 
ATOM   1036 O  O   . SER A 1 132 ? 16.761  0.569   -30.409 1.00 12.42 ? 132 SER B O   1 
ATOM   1037 C  CB  . SER A 1 132 ? 14.904  -2.019  -31.307 1.00 12.64 ? 132 SER B CB  1 
ATOM   1038 O  OG  . SER A 1 132 ? 16.245  -2.365  -31.511 1.00 13.81 ? 132 SER B OG  1 
ATOM   1039 N  N   . PHE A 1 133 ? 15.230  -0.142  -28.873 1.00 13.28 ? 133 PHE B N   1 
ATOM   1040 C  CA  . PHE A 1 133 ? 16.022  0.148   -27.685 1.00 14.78 ? 133 PHE B CA  1 
ATOM   1041 C  C   . PHE A 1 133 ? 17.361  -0.520  -27.801 1.00 15.78 ? 133 PHE B C   1 
ATOM   1042 O  O   . PHE A 1 133 ? 18.418  0.144   -27.568 1.00 15.81 ? 133 PHE B O   1 
ATOM   1043 C  CB  . PHE A 1 133 ? 15.246  -0.262  -26.381 1.00 14.39 ? 133 PHE B CB  1 
ATOM   1044 C  CG  . PHE A 1 133 ? 16.082  -0.178  -25.138 1.00 14.37 ? 133 PHE B CG  1 
ATOM   1045 C  CD1 . PHE A 1 133 ? 16.435  1.060   -24.602 1.00 15.76 ? 133 PHE B CD1 1 
ATOM   1046 C  CD2 . PHE A 1 133 ? 16.508  -1.355  -24.509 1.00 15.60 ? 133 PHE B CD2 1 
ATOM   1047 C  CE1 . PHE A 1 133 ? 17.257  1.139   -23.457 1.00 15.86 ? 133 PHE B CE1 1 
ATOM   1048 C  CE2 . PHE A 1 133 ? 17.332  -1.297  -23.336 1.00 18.45 ? 133 PHE B CE2 1 
ATOM   1049 C  CZ  . PHE A 1 133 ? 17.686  -0.043  -22.818 1.00 17.97 ? 133 PHE B CZ  1 
ATOM   1050 N  N   . VAL A 1 134 ? 17.358  -1.808  -28.146 1.00 15.83 ? 134 VAL B N   1 
ATOM   1051 C  CA  . VAL A 1 134 ? 18.616  -2.565  -28.128 1.00 19.21 ? 134 VAL B CA  1 
ATOM   1052 C  C   . VAL A 1 134 ? 19.625  -1.997  -29.115 1.00 17.85 ? 134 VAL B C   1 
ATOM   1053 O  O   . VAL A 1 134 ? 20.803  -1.891  -28.798 1.00 20.63 ? 134 VAL B O   1 
ATOM   1054 C  CB  . VAL A 1 134 ? 18.379  -4.103  -28.310 1.00 22.46 ? 134 VAL B CB  1 
ATOM   1055 C  CG1 . VAL A 1 134 ? 19.699  -4.872  -28.260 1.00 28.88 ? 134 VAL B CG1 1 
ATOM   1056 C  CG2 . VAL A 1 134 ? 17.567  -4.623  -27.157 1.00 22.32 ? 134 VAL B CG2 1 
ATOM   1057 N  N   . GLU A 1 135 ? 19.197  -1.629  -30.308 1.00 16.01 ? 135 GLU B N   1 
ATOM   1058 C  CA  . GLU A 1 135 ? 20.106  -0.993  -31.275 1.00 17.60 ? 135 GLU B CA  1 
ATOM   1059 C  C   . GLU A 1 135 ? 20.585  0.410   -30.819 1.00 16.41 ? 135 GLU B C   1 
ATOM   1060 O  O   . GLU A 1 135 ? 21.782  0.787   -31.023 1.00 16.62 ? 135 GLU B O   1 
ATOM   1061 C  CB  . GLU A 1 135 ? 19.398  -0.850  -32.672 1.00 20.63 ? 135 GLU B CB  1 
ATOM   1062 C  CG  . GLU A 1 135 ? 19.089  -2.161  -33.418 1.00 26.06 ? 135 GLU B CG  1 
ATOM   1063 C  CD  . GLU A 1 135 ? 20.294  -2.730  -34.159 1.00 32.83 ? 135 GLU B CD  1 
ATOM   1064 O  OE1 . GLU A 1 135 ? 20.109  -3.736  -34.891 1.00 35.73 ? 135 GLU B OE1 1 
ATOM   1065 O  OE2 . GLU A 1 135 ? 21.434  -2.190  -34.025 1.00 32.56 ? 135 GLU B OE2 1 
ATOM   1066 N  N   . ALA A 1 136 ? 19.668  1.187   -30.224 1.00 12.78 ? 136 ALA B N   1 
ATOM   1067 C  CA  . ALA A 1 136 ? 19.975  2.568   -29.788 1.00 11.98 ? 136 ALA B CA  1 
ATOM   1068 C  C   . ALA A 1 136 ? 21.028  2.513   -28.671 1.00 11.01 ? 136 ALA B C   1 
ATOM   1069 O  O   . ALA A 1 136 ? 21.895  3.370   -28.574 1.00 11.47 ? 136 ALA B O   1 
ATOM   1070 C  CB  . ALA A 1 136 ? 18.720  3.329   -29.261 1.00 11.82 ? 136 ALA B CB  1 
ATOM   1071 N  N   . ALA A 1 137 ? 20.982  1.442   -27.861 1.00 12.08 ? 137 ALA B N   1 
ATOM   1072 C  CA  . ALA A 1 137 ? 21.840  1.395   -26.681 1.00 12.72 ? 137 ALA B CA  1 
ATOM   1073 C  C   . ALA A 1 137 ? 23.285  1.343   -27.068 1.00 15.17 ? 137 ALA B C   1 
ATOM   1074 O  O   . ALA A 1 137 ? 24.138  1.580   -26.205 1.00 14.31 ? 137 ALA B O   1 
ATOM   1075 C  CB  . ALA A 1 137 ? 21.509  0.176   -25.832 1.00 13.87 ? 137 ALA B CB  1 
ATOM   1076 N  N   . HIS A 1 138 ? 23.548  1.061   -28.356 1.00 16.54 ? 138 HIS B N   1 
ATOM   1077 C  CA  . HIS A 1 138 ? 24.906  0.931   -28.924 1.00 19.16 ? 138 HIS B CA  1 
ATOM   1078 C  C   . HIS A 1 138 ? 25.408  2.113   -29.733 1.00 19.72 ? 138 HIS B C   1 
ATOM   1079 O  O   . HIS A 1 138 ? 26.407  2.009   -30.463 1.00 21.19 ? 138 HIS B O   1 
ATOM   1080 C  CB  . HIS A 1 138 ? 25.021  -0.368  -29.773 1.00 20.34 ? 138 HIS B CB  1 
ATOM   1081 C  CG  . HIS A 1 138 ? 25.023  -1.592  -28.923 1.00 23.31 ? 138 HIS B CG  1 
ATOM   1082 N  ND1 . HIS A 1 138 ? 26.174  -2.086  -28.339 1.00 27.62 ? 138 HIS B ND1 1 
ATOM   1083 C  CD2 . HIS A 1 138 ? 24.006  -2.345  -28.438 1.00 25.06 ? 138 HIS B CD2 1 
ATOM   1084 C  CE1 . HIS A 1 138 ? 25.874  -3.135  -27.580 1.00 26.37 ? 138 HIS B CE1 1 
ATOM   1085 N  NE2 . HIS A 1 138 ? 24.566  -3.321  -27.628 1.00 25.77 ? 138 HIS B NE2 1 
ATOM   1086 N  N   . GLU A 1 139 ? 24.716  3.237   -29.649 1.00 18.13 ? 139 GLU B N   1 
ATOM   1087 C  CA  . GLU A 1 139 ? 25.084  4.416   -30.437 1.00 17.81 ? 139 GLU B CA  1 
ATOM   1088 C  C   . GLU A 1 139 ? 25.318  5.596   -29.510 1.00 17.12 ? 139 GLU B C   1 
ATOM   1089 O  O   . GLU A 1 139 ? 24.596  5.700   -28.486 1.00 13.92 ? 139 GLU B O   1 
ATOM   1090 C  CB  . GLU A 1 139 ? 23.914  4.772   -31.362 1.00 19.55 ? 139 GLU B CB  1 
ATOM   1091 C  CG  . GLU A 1 139 ? 23.432  3.587   -32.191 1.00 22.95 ? 139 GLU B CG  1 
ATOM   1092 C  CD  . GLU A 1 139 ? 24.211  3.423   -33.456 1.00 29.12 ? 139 GLU B CD  1 
ATOM   1093 O  OE1 . GLU A 1 139 ? 23.801  2.537   -34.267 1.00 29.87 ? 139 GLU B OE1 1 
ATOM   1094 O  OE2 . GLU A 1 139 ? 25.216  4.167   -33.625 1.00 32.10 ? 139 GLU B OE2 1 
ATOM   1095 N  N   . PRO A 1 140 ? 26.238  6.528   -29.866 1.00 17.16 ? 140 PRO B N   1 
ATOM   1096 C  CA  . PRO A 1 140 ? 26.569  7.590   -28.917 1.00 17.32 ? 140 PRO B CA  1 
ATOM   1097 C  C   . PRO A 1 140 ? 25.370  8.514   -28.647 1.00 16.83 ? 140 PRO B C   1 
ATOM   1098 O  O   . PRO A 1 140 ? 25.249  9.076   -27.538 1.00 15.47 ? 140 PRO B O   1 
ATOM   1099 C  CB  . PRO A 1 140 ? 27.722  8.341   -29.602 1.00 18.95 ? 140 PRO B CB  1 
ATOM   1100 C  CG  . PRO A 1 140 ? 28.290  7.353   -30.537 1.00 19.86 ? 140 PRO B CG  1 
ATOM   1101 C  CD  . PRO A 1 140 ? 27.105  6.615   -31.086 1.00 19.95 ? 140 PRO B CD  1 
ATOM   1102 N  N   . ASP A 1 141 ? 24.465  8.605   -29.599 1.00 13.87 ? 141 ASP B N   1 
ATOM   1103 C  CA  . ASP A 1 141 ? 23.236  9.424   -29.370 1.00 14.99 ? 141 ASP B CA  1 
ATOM   1104 C  C   . ASP A 1 141 ? 21.990  8.536   -29.185 1.00 13.85 ? 141 ASP B C   1 
ATOM   1105 O  O   . ASP A 1 141 ? 20.898  8.965   -29.472 1.00 13.20 ? 141 ASP B O   1 
ATOM   1106 C  CB  . ASP A 1 141 ? 23.038  10.419  -30.533 1.00 16.30 ? 141 ASP B CB  1 
ATOM   1107 C  CG  . ASP A 1 141 ? 22.792  9.725   -31.861 1.00 19.04 ? 141 ASP B CG  1 
ATOM   1108 O  OD1 . ASP A 1 141 ? 23.097  8.504   -32.013 1.00 15.63 ? 141 ASP B OD1 1 
ATOM   1109 O  OD2 . ASP A 1 141 ? 22.278  10.430  -32.762 1.00 21.17 ? 141 ASP B OD2 1 
ATOM   1110 N  N   . GLY A 1 142 ? 22.167  7.309   -28.696 1.00 11.64 ? 142 GLY B N   1 
ATOM   1111 C  CA  . GLY A 1 142 ? 21.067  6.305   -28.678 1.00 10.75 ? 142 GLY B CA  1 
ATOM   1112 C  C   . GLY A 1 142 ? 20.088  6.521   -27.513 1.00 9.74  ? 142 GLY B C   1 
ATOM   1113 O  O   . GLY A 1 142 ? 18.877  6.272   -27.619 1.00 10.42 ? 142 GLY B O   1 
ATOM   1114 N  N   . LEU A 1 143 ? 20.659  6.877   -26.383 1.00 9.54  ? 143 LEU B N   1 
ATOM   1115 C  CA  . LEU A 1 143 ? 19.867  6.869   -25.122 1.00 9.12  ? 143 LEU B CA  1 
ATOM   1116 C  C   . LEU A 1 143 ? 19.904  8.255   -24.446 1.00 9.32  ? 143 LEU B C   1 
ATOM   1117 O  O   . LEU A 1 143 ? 20.856  8.990   -24.567 1.00 10.33 ? 143 LEU B O   1 
ATOM   1118 C  CB  . LEU A 1 143 ? 20.414  5.797   -24.131 1.00 8.20  ? 143 LEU B CB  1 
ATOM   1119 C  CG  . LEU A 1 143 ? 20.493  4.356   -24.605 1.00 8.97  ? 143 LEU B CG  1 
ATOM   1120 C  CD1 . LEU A 1 143 ? 20.986  3.455   -23.406 1.00 8.04  ? 143 LEU B CD1 1 
ATOM   1121 C  CD2 . LEU A 1 143 ? 19.171  3.785   -25.165 1.00 9.29  ? 143 LEU B CD2 1 
ATOM   1122 N  N   . ALA A 1 144 ? 18.857  8.548   -23.666 1.00 9.25  ? 144 ALA B N   1 
ATOM   1123 C  CA  . ALA A 1 144 ? 18.825  9.766   -22.831 1.00 8.34  ? 144 ALA B CA  1 
ATOM   1124 C  C   . ALA A 1 144 ? 18.309  9.297   -21.485 1.00 8.23  ? 144 ALA B C   1 
ATOM   1125 O  O   . ALA A 1 144 ? 17.305  8.650   -21.442 1.00 8.20  ? 144 ALA B O   1 
ATOM   1126 C  CB  . ALA A 1 144 ? 17.889  10.834  -23.359 1.00 9.23  ? 144 ALA B CB  1 
ATOM   1127 N  N   . VAL A 1 145 ? 19.004  9.605   -20.412 1.00 8.20  ? 145 VAL B N   1 
ATOM   1128 C  CA  . VAL A 1 145 ? 18.482  9.247   -19.109 1.00 8.53  ? 145 VAL B CA  1 
ATOM   1129 C  C   . VAL A 1 145 ? 18.197  10.560  -18.362 1.00 8.25  ? 145 VAL B C   1 
ATOM   1130 O  O   . VAL A 1 145 ? 19.068  11.437  -18.259 1.00 9.03  ? 145 VAL B O   1 
ATOM   1131 C  CB  . VAL A 1 145 ? 19.481  8.366   -18.308 1.00 9.10  ? 145 VAL B CB  1 
ATOM   1132 C  CG1 . VAL A 1 145 ? 18.842  7.949   -16.979 1.00 8.81  ? 145 VAL B CG1 1 
ATOM   1133 C  CG2 . VAL A 1 145 ? 19.822  7.111   -19.085 1.00 10.37 ? 145 VAL B CG2 1 
ATOM   1134 N  N   . LEU A 1 146 ? 16.994  10.692  -17.830 1.00 8.88  ? 146 LEU B N   1 
ATOM   1135 C  CA  . LEU A 1 146 ? 16.681  11.785  -16.904 1.00 9.46  ? 146 LEU B CA  1 
ATOM   1136 C  C   . LEU A 1 146 ? 16.950  11.267  -15.475 1.00 9.81  ? 146 LEU B C   1 
ATOM   1137 O  O   . LEU A 1 146 ? 16.450  10.170  -15.088 1.00 9.01  ? 146 LEU B O   1 
ATOM   1138 C  CB  . LEU A 1 146 ? 15.224  12.170  -17.149 1.00 11.51 ? 146 LEU B CB  1 
ATOM   1139 C  CG  . LEU A 1 146 ? 14.702  13.326  -16.328 1.00 13.27 ? 146 LEU B CG  1 
ATOM   1140 C  CD1 . LEU A 1 146 ? 15.238  14.637  -16.881 1.00 15.64 ? 146 LEU B CD1 1 
ATOM   1141 C  CD2 . LEU A 1 146 ? 13.150  13.283  -16.450 1.00 13.40 ? 146 LEU B CD2 1 
ATOM   1142 N  N   . GLY A 1 147 ? 17.808  12.023  -14.746 1.00 9.13  ? 147 GLY B N   1 
ATOM   1143 C  CA  . GLY A 1 147 ? 18.237  11.698  -13.389 1.00 8.54  ? 147 GLY B CA  1 
ATOM   1144 C  C   . GLY A 1 147 ? 17.485  12.612  -12.439 1.00 8.94  ? 147 GLY B C   1 
ATOM   1145 O  O   . GLY A 1 147 ? 17.502  13.882  -12.625 1.00 9.78  ? 147 GLY B O   1 
ATOM   1146 N  N   . VAL A 1 148 ? 16.823  12.036  -11.397 1.00 8.44  ? 148 VAL B N   1 
ATOM   1147 C  CA  . VAL A 1 148 ? 16.133  12.844  -10.421 1.00 8.89  ? 148 VAL B CA  1 
ATOM   1148 C  C   . VAL A 1 148 ? 16.668  12.473  -9.009  1.00 8.90  ? 148 VAL B C   1 
ATOM   1149 O  O   . VAL A 1 148 ? 16.608  11.291  -8.602  1.00 9.06  ? 148 VAL B O   1 
ATOM   1150 C  CB  . VAL A 1 148 ? 14.601  12.572  -10.486 1.00 8.78  ? 148 VAL B CB  1 
ATOM   1151 C  CG1 . VAL A 1 148 ? 13.844  13.347  -9.443  1.00 10.16 ? 148 VAL B CG1 1 
ATOM   1152 C  CG2 . VAL A 1 148 ? 13.979  12.878  -11.881 1.00 8.72  ? 148 VAL B CG2 1 
ATOM   1153 N  N   . PHE A 1 149 ? 17.169  13.450  -8.251  1.00 9.53  ? 149 PHE B N   1 
ATOM   1154 C  CA  . PHE A 1 149 ? 17.656  13.194  -6.912  1.00 8.32  ? 149 PHE B CA  1 
ATOM   1155 C  C   . PHE A 1 149 ? 16.500  13.090  -5.934  1.00 9.04  ? 149 PHE B C   1 
ATOM   1156 O  O   . PHE A 1 149 ? 15.454  13.774  -6.119  1.00 8.76  ? 149 PHE B O   1 
ATOM   1157 C  CB  . PHE A 1 149 ? 18.554  14.369  -6.468  1.00 8.43  ? 149 PHE B CB  1 
ATOM   1158 C  CG  . PHE A 1 149 ? 19.796  14.511  -7.270  1.00 8.32  ? 149 PHE B CG  1 
ATOM   1159 C  CD1 . PHE A 1 149 ? 20.714  13.421  -7.346  1.00 8.70  ? 149 PHE B CD1 1 
ATOM   1160 C  CD2 . PHE A 1 149 ? 20.080  15.718  -7.892  1.00 8.52  ? 149 PHE B CD2 1 
ATOM   1161 C  CE1 . PHE A 1 149 ? 21.938  13.555  -8.085  1.00 8.85  ? 149 PHE B CE1 1 
ATOM   1162 C  CE2 . PHE A 1 149 ? 21.259  15.869  -8.639  1.00 8.36  ? 149 PHE B CE2 1 
ATOM   1163 C  CZ  . PHE A 1 149 ? 22.177  14.790  -8.737  1.00 9.14  ? 149 PHE B CZ  1 
ATOM   1164 N  N   . LEU A 1 150 ? 16.692  12.224  -4.933  1.00 8.29  ? 150 LEU B N   1 
ATOM   1165 C  CA  . LEU A 1 150 ? 15.741  12.117  -3.827  1.00 8.64  ? 150 LEU B CA  1 
ATOM   1166 C  C   . LEU A 1 150 ? 16.441  12.533  -2.555  1.00 9.72  ? 150 LEU B C   1 
ATOM   1167 O  O   . LEU A 1 150 ? 17.566  12.092  -2.313  1.00 9.27  ? 150 LEU B O   1 
ATOM   1168 C  CB  . LEU A 1 150 ? 15.206  10.694  -3.695  1.00 10.01 ? 150 LEU B CB  1 
ATOM   1169 C  CG  . LEU A 1 150 ? 14.158  10.174  -4.717  1.00 8.91  ? 150 LEU B CG  1 
ATOM   1170 C  CD1 . LEU A 1 150 ? 14.889  9.884   -6.035  1.00 9.92  ? 150 LEU B CD1 1 
ATOM   1171 C  CD2 . LEU A 1 150 ? 13.594  8.879   -4.168  1.00 9.75  ? 150 LEU B CD2 1 
ATOM   1172 N  N   . GLN A 1 151 ? 15.797  13.404  -1.750  1.00 10.03 ? 151 GLN B N   1 
ATOM   1173 C  CA  . GLN A 1 151 ? 16.386  13.900  -0.518  1.00 11.70 ? 151 GLN B CA  1 
ATOM   1174 C  C   . GLN A 1 151 ? 15.466  13.452  0.581   1.00 11.51 ? 151 GLN B C   1 
ATOM   1175 O  O   . GLN A 1 151 ? 14.268  13.420  0.361   1.00 11.03 ? 151 GLN B O   1 
ATOM   1176 C  CB  . GLN A 1 151 ? 16.550  15.441  -0.528  1.00 15.67 ? 151 GLN B CB  1 
ATOM   1177 C  CG  . GLN A 1 151 ? 15.220  16.129  -0.711  1.00 20.54 ? 151 GLN B CG  1 
ATOM   1178 C  CD  . GLN A 1 151 ? 15.253  17.664  -0.760  1.00 28.80 ? 151 GLN B CD  1 
ATOM   1179 O  OE1 . GLN A 1 151 ? 16.321  18.304  -0.790  1.00 31.39 ? 151 GLN B OE1 1 
ATOM   1180 N  NE2 . GLN A 1 151 ? 14.031  18.256  -0.777  1.00 29.83 ? 151 GLN B NE2 1 
ATOM   1181 N  N   . ILE A 1 152 ? 16.019  13.190  1.772   1.00 11.14 ? 152 ILE B N   1 
ATOM   1182 C  CA  . ILE A 1 152 ? 15.187  12.814  2.929   1.00 12.72 ? 152 ILE B CA  1 
ATOM   1183 C  C   . ILE A 1 152 ? 14.331  14.018  3.355   1.00 13.98 ? 152 ILE B C   1 
ATOM   1184 O  O   . ILE A 1 152 ? 14.822  15.159  3.408   1.00 13.91 ? 152 ILE B O   1 
ATOM   1185 C  CB  . ILE A 1 152 ? 16.057  12.334  4.119   1.00 14.19 ? 152 ILE B CB  1 
ATOM   1186 C  CG1 . ILE A 1 152 ? 16.850  11.061  3.715   1.00 15.10 ? 152 ILE B CG1 1 
ATOM   1187 C  CG2 . ILE A 1 152 ? 15.174  12.066  5.369   1.00 13.89 ? 152 ILE B CG2 1 
ATOM   1188 C  CD1 . ILE A 1 152 ? 15.965  9.863   3.365   1.00 15.10 ? 152 ILE B CD1 1 
ATOM   1189 N  N   . GLY A 1 153 ? 13.036  13.769  3.540   1.00 14.51 ? 153 GLY B N   1 
ATOM   1190 C  CA  . GLY A 1 153 ? 12.112  14.825  3.959   1.00 15.49 ? 153 GLY B CA  1 
ATOM   1191 C  C   . GLY A 1 153 ? 10.830  14.166  4.346   1.00 16.09 ? 153 GLY B C   1 
ATOM   1192 O  O   . GLY A 1 153 ? 10.792  13.036  4.918   1.00 17.55 ? 153 GLY B O   1 
ATOM   1193 N  N   A GLU A 1 154 ? 9.743   14.858  4.040   0.50 15.31 ? 154 GLU B N   1 
ATOM   1194 N  N   B GLU A 1 154 ? 9.748   14.831  4.027   0.50 16.80 ? 154 GLU B N   1 
ATOM   1195 C  CA  A GLU A 1 154 ? 8.417   14.317  4.277   0.50 15.05 ? 154 GLU B CA  1 
ATOM   1196 C  CA  B GLU A 1 154 ? 8.457   14.295  4.345   0.50 17.38 ? 154 GLU B CA  1 
ATOM   1197 C  C   A GLU A 1 154 ? 8.244   13.059  3.418   0.50 15.15 ? 154 GLU B C   1 
ATOM   1198 C  C   B GLU A 1 154 ? 8.153   13.146  3.380   0.50 16.41 ? 154 GLU B C   1 
ATOM   1199 O  O   A GLU A 1 154 ? 8.948   12.891  2.392   0.50 14.58 ? 154 GLU B O   1 
ATOM   1200 O  O   B GLU A 1 154 ? 8.693   13.135  2.241   0.50 15.13 ? 154 GLU B O   1 
ATOM   1201 C  CB  A GLU A 1 154 ? 7.313   15.367  3.982   0.50 15.67 ? 154 GLU B CB  1 
ATOM   1202 C  CB  B GLU A 1 154 ? 7.459   15.447  4.297   0.50 21.12 ? 154 GLU B CB  1 
ATOM   1203 C  CG  A GLU A 1 154 ? 7.404   16.652  4.836   0.50 15.37 ? 154 GLU B CG  1 
ATOM   1204 C  CG  B GLU A 1 154 ? 7.998   16.571  5.183   0.50 23.99 ? 154 GLU B CG  1 
ATOM   1205 C  CD  A GLU A 1 154 ? 7.315   16.372  6.352   0.50 16.01 ? 154 GLU B CD  1 
ATOM   1206 C  CD  B GLU A 1 154 ? 7.507   17.952  4.828   0.50 26.63 ? 154 GLU B CD  1 
ATOM   1207 O  OE1 A GLU A 1 154 ? 6.546   15.472  6.731   0.50 16.15 ? 154 GLU B OE1 1 
ATOM   1208 O  OE1 B GLU A 1 154 ? 6.840   18.075  3.794   0.50 30.05 ? 154 GLU B OE1 1 
ATOM   1209 O  OE2 A GLU A 1 154 ? 8.041   17.021  7.145   0.50 17.15 ? 154 GLU B OE2 1 
ATOM   1210 O  OE2 B GLU A 1 154 ? 7.803   18.924  5.586   0.50 29.91 ? 154 GLU B OE2 1 
ATOM   1211 N  N   . PRO A 1 155 ? 7.319   12.173  3.813   1.00 15.10 ? 155 PRO B N   1 
ATOM   1212 C  CA  . PRO A 1 155 ? 7.008   11.025  2.972   1.00 13.67 ? 155 PRO B CA  1 
ATOM   1213 C  C   . PRO A 1 155 ? 6.379   11.545  1.682   1.00 12.44 ? 155 PRO B C   1 
ATOM   1214 O  O   . PRO A 1 155 ? 5.685   12.582  1.713   1.00 12.41 ? 155 PRO B O   1 
ATOM   1215 C  CB  . PRO A 1 155 ? 5.904   10.272  3.739   1.00 15.83 ? 155 PRO B CB  1 
ATOM   1216 C  CG  . PRO A 1 155 ? 5.917   10.802  5.113   1.00 16.49 ? 155 PRO B CG  1 
ATOM   1217 C  CD  . PRO A 1 155 ? 6.559   12.146  5.099   1.00 16.95 ? 155 PRO B CD  1 
ATOM   1218 N  N   . ASN A 1 156 ? 6.656   10.860  0.587   1.00 11.03 ? 156 ASN B N   1 
ATOM   1219 C  CA  . ASN A 1 156 ? 6.208   11.353  -0.717  1.00 10.76 ? 156 ASN B CA  1 
ATOM   1220 C  C   . ASN A 1 156 ? 5.091   10.408  -1.166  1.00 11.74 ? 156 ASN B C   1 
ATOM   1221 O  O   . ASN A 1 156 ? 5.310   9.183   -1.514  1.00 10.64 ? 156 ASN B O   1 
ATOM   1222 C  CB  . ASN A 1 156 ? 7.389   11.280  -1.731  1.00 10.94 ? 156 ASN B CB  1 
ATOM   1223 C  CG  . ASN A 1 156 ? 7.077   11.979  -3.040  1.00 10.69 ? 156 ASN B CG  1 
ATOM   1224 O  OD1 . ASN A 1 156 ? 5.931   12.079  -3.431  1.00 11.93 ? 156 ASN B OD1 1 
ATOM   1225 N  ND2 . ASN A 1 156 ? 8.118   12.452  -3.728  1.00 11.17 ? 156 ASN B ND2 1 
ATOM   1226 N  N   . SER A 1 157 ? 3.870   10.944  -1.246  1.00 12.40 ? 157 SER B N   1 
ATOM   1227 C  CA  . SER A 1 157 ? 2.780   10.050  -1.617  1.00 12.60 ? 157 SER B CA  1 
ATOM   1228 C  C   . SER A 1 157 ? 2.912   9.513   -3.050  1.00 12.90 ? 157 SER B C   1 
ATOM   1229 O  O   . SER A 1 157 ? 2.327   8.459   -3.407  1.00 14.77 ? 157 SER B O   1 
ATOM   1230 C  CB  . SER A 1 157 ? 1.436   10.743  -1.328  1.00 14.58 ? 157 SER B CB  1 
ATOM   1231 O  OG  . SER A 1 157 ? 1.276   11.799  -2.240  1.00 16.76 ? 157 SER B OG  1 
ATOM   1232 N  N   . GLN A 1 158 ? 3.684   10.202  -3.883  1.00 11.73 ? 158 GLN B N   1 
ATOM   1233 C  CA  . GLN A 1 158 ? 3.846   9.736   -5.270  1.00 13.31 ? 158 GLN B CA  1 
ATOM   1234 C  C   . GLN A 1 158 ? 4.717   8.504   -5.328  1.00 12.76 ? 158 GLN B C   1 
ATOM   1235 O  O   . GLN A 1 158 ? 4.883   7.931   -6.423  1.00 12.47 ? 158 GLN B O   1 
ATOM   1236 C  CB  . GLN A 1 158 ? 4.458   10.796  -6.180  1.00 14.31 ? 158 GLN B CB  1 
ATOM   1237 C  CG  . GLN A 1 158 ? 3.603   12.092  -6.214  1.00 15.86 ? 158 GLN B CG  1 
ATOM   1238 C  CD  . GLN A 1 158 ? 2.268   11.923  -6.924  1.00 18.94 ? 158 GLN B CD  1 
ATOM   1239 O  OE1 . GLN A 1 158 ? 1.307   12.676  -6.665  1.00 25.79 ? 158 GLN B OE1 1 
ATOM   1240 N  NE2 . GLN A 1 158 ? 2.178   10.932  -7.791  1.00 16.29 ? 158 GLN B NE2 1 
ATOM   1241 N  N   . LEU A 1 159 ? 5.382   8.167   -4.199  1.00 11.20 ? 159 LEU B N   1 
ATOM   1242 C  CA  . LEU A 1 159 ? 6.199   6.939   -4.218  1.00 10.90 ? 159 LEU B CA  1 
ATOM   1243 C  C   . LEU A 1 159 ? 5.428   5.744   -3.647  1.00 12.26 ? 159 LEU B C   1 
ATOM   1244 O  O   . LEU A 1 159 ? 5.947   4.634   -3.664  1.00 11.93 ? 159 LEU B O   1 
ATOM   1245 C  CB  . LEU A 1 159 ? 7.480   7.144   -3.405  1.00 12.33 ? 159 LEU B CB  1 
ATOM   1246 C  CG  . LEU A 1 159 ? 8.468   8.069   -4.045  1.00 12.72 ? 159 LEU B CG  1 
ATOM   1247 C  CD1 . LEU A 1 159 ? 9.629   8.320   -3.100  1.00 13.91 ? 159 LEU B CD1 1 
ATOM   1248 C  CD2 . LEU A 1 159 ? 9.032   7.471   -5.341  1.00 13.33 ? 159 LEU B CD2 1 
ATOM   1249 N  N   . GLN A 1 160 ? 4.217   5.985   -3.110  1.00 11.06 ? 160 GLN B N   1 
ATOM   1250 C  CA  . GLN A 1 160 ? 3.435   4.925   -2.424  1.00 12.53 ? 160 GLN B CA  1 
ATOM   1251 C  C   . GLN A 1 160 ? 3.120   3.774   -3.395  1.00 12.48 ? 160 GLN B C   1 
ATOM   1252 O  O   . GLN A 1 160 ? 3.193   2.571   -3.008  1.00 14.61 ? 160 GLN B O   1 
ATOM   1253 C  CB  . GLN A 1 160 ? 2.105   5.526   -1.892  1.00 13.41 ? 160 GLN B CB  1 
ATOM   1254 C  CG  . GLN A 1 160 ? 1.306   4.566   -0.966  1.00 16.59 ? 160 GLN B CG  1 
ATOM   1255 C  CD  . GLN A 1 160 ? 1.984   4.370   0.400   1.00 22.97 ? 160 GLN B CD  1 
ATOM   1256 O  OE1 . GLN A 1 160 ? 2.531   5.335   0.979   1.00 24.39 ? 160 GLN B OE1 1 
ATOM   1257 N  NE2 . GLN A 1 160 ? 1.975   3.115   0.913   1.00 19.96 ? 160 GLN B NE2 1 
ATOM   1258 N  N   . LYS A 1 161 ? 2.778   4.108   -4.644  1.00 10.93 ? 161 LYS B N   1 
ATOM   1259 C  CA  . LYS A 1 161 ? 2.439   3.047   -5.589  1.00 12.47 ? 161 LYS B CA  1 
ATOM   1260 C  C   . LYS A 1 161 ? 3.592   2.033   -5.748  1.00 13.03 ? 161 LYS B C   1 
ATOM   1261 O  O   . LYS A 1 161 ? 3.363   0.786   -5.829  1.00 13.09 ? 161 LYS B O   1 
ATOM   1262 C  CB  . LYS A 1 161 ? 1.970   3.643   -6.956  1.00 12.45 ? 161 LYS B CB  1 
ATOM   1263 C  CG  . LYS A 1 161 ? 1.359   2.563   -7.927  1.00 14.58 ? 161 LYS B CG  1 
ATOM   1264 C  CD  . LYS A 1 161 ? 0.925   3.153   -9.252  1.00 15.78 ? 161 LYS B CD  1 
ATOM   1265 C  CE  . LYS A 1 161 ? 0.757   2.143   -10.359 1.00 13.75 ? 161 LYS B CE  1 
ATOM   1266 N  NZ  . LYS A 1 161 ? -0.411  1.275   -9.969  1.00 13.58 ? 161 LYS B NZ  1 
ATOM   1267 N  N   . ILE A 1 162 ? 4.829   2.586   -5.799  1.00 13.20 ? 162 ILE B N   1 
ATOM   1268 C  CA  . ILE A 1 162 ? 5.996   1.773   -5.947  1.00 11.02 ? 162 ILE B CA  1 
ATOM   1269 C  C   . ILE A 1 162 ? 6.244   0.988   -4.646  1.00 10.93 ? 162 ILE B C   1 
ATOM   1270 O  O   . ILE A 1 162 ? 6.409   -0.234  -4.650  1.00 9.59  ? 162 ILE B O   1 
ATOM   1271 C  CB  . ILE A 1 162 ? 7.238   2.586   -6.355  1.00 11.00 ? 162 ILE B CB  1 
ATOM   1272 C  CG1 . ILE A 1 162 ? 7.132   2.987   -7.824  1.00 10.55 ? 162 ILE B CG1 1 
ATOM   1273 C  CG2 . ILE A 1 162 ? 8.481   1.763   -6.100  1.00 9.14  ? 162 ILE B CG2 1 
ATOM   1274 C  CD1 . ILE A 1 162 ? 8.163   4.041   -8.211  1.00 12.03 ? 162 ILE B CD1 1 
ATOM   1275 N  N   . THR A 1 163 ? 6.244   1.687   -3.520  1.00 11.64 ? 163 THR B N   1 
ATOM   1276 C  CA  . THR A 1 163 ? 6.652   0.971   -2.312  1.00 13.22 ? 163 THR B CA  1 
ATOM   1277 C  C   . THR A 1 163 ? 5.651   -0.144  -1.920  1.00 13.40 ? 163 THR B C   1 
ATOM   1278 O  O   . THR A 1 163 ? 6.060   -1.133  -1.353  1.00 13.40 ? 163 THR B O   1 
ATOM   1279 C  CB  . THR A 1 163 ? 6.929   1.904   -1.102  1.00 13.22 ? 163 THR B CB  1 
ATOM   1280 O  OG1 . THR A 1 163 ? 5.708   2.596   -0.739  1.00 14.24 ? 163 THR B OG1 1 
ATOM   1281 C  CG2 . THR A 1 163 ? 7.975   2.898   -1.381  1.00 12.58 ? 163 THR B CG2 1 
ATOM   1282 N  N   . ASP A 1 164 ? 4.349   0.038   -2.183  1.00 14.62 ? 164 ASP B N   1 
ATOM   1283 C  CA  . ASP A 1 164 ? 3.364   -0.986  -1.898  1.00 14.29 ? 164 ASP B CA  1 
ATOM   1284 C  C   . ASP A 1 164 ? 3.626   -2.291  -2.633  1.00 14.49 ? 164 ASP B C   1 
ATOM   1285 O  O   . ASP A 1 164 ? 3.049   -3.315  -2.213  1.00 14.52 ? 164 ASP B O   1 
ATOM   1286 C  CB  . ASP A 1 164 ? 1.910   -0.529  -2.239  1.00 14.34 ? 164 ASP B CB  1 
ATOM   1287 C  CG  . ASP A 1 164 ? 1.347   0.497   -1.246  1.00 16.99 ? 164 ASP B CG  1 
ATOM   1288 O  OD1 . ASP A 1 164 ? 1.933   0.597   -0.116  1.00 18.61 ? 164 ASP B OD1 1 
ATOM   1289 O  OD2 . ASP A 1 164 ? 0.303   1.136   -1.604  1.00 17.51 ? 164 ASP B OD2 1 
ATOM   1290 N  N   . THR A 1 165 ? 4.450   -2.279  -3.712  1.00 12.45 ? 165 THR B N   1 
ATOM   1291 C  CA  . THR A 1 165 ? 4.705   -3.530  -4.450  1.00 12.87 ? 165 THR B CA  1 
ATOM   1292 C  C   . THR A 1 165 ? 5.963   -4.214  -3.977  1.00 11.23 ? 165 THR B C   1 
ATOM   1293 O  O   . THR A 1 165 ? 6.218   -5.392  -4.371  1.00 10.93 ? 165 THR B O   1 
ATOM   1294 C  CB  . THR A 1 165 ? 4.931   -3.283  -5.963  1.00 12.68 ? 165 THR B CB  1 
ATOM   1295 O  OG1 . THR A 1 165 ? 6.217   -2.667  -6.168  1.00 12.37 ? 165 THR B OG1 1 
ATOM   1296 C  CG2 . THR A 1 165 ? 3.761   -2.431  -6.580  1.00 12.84 ? 165 THR B CG2 1 
ATOM   1297 N  N   . LEU A 1 166 ? 6.796   -3.549  -3.144  1.00 11.04 ? 166 LEU B N   1 
ATOM   1298 C  CA  . LEU A 1 166 ? 8.122   -4.102  -2.874  1.00 12.80 ? 166 LEU B CA  1 
ATOM   1299 C  C   . LEU A 1 166 ? 8.165   -5.517  -2.217  1.00 13.92 ? 166 LEU B C   1 
ATOM   1300 O  O   . LEU A 1 166 ? 9.051   -6.346  -2.544  1.00 13.94 ? 166 LEU B O   1 
ATOM   1301 C  CB  . LEU A 1 166 ? 8.992   -3.158  -2.036  1.00 11.53 ? 166 LEU B CB  1 
ATOM   1302 C  CG  . LEU A 1 166 ? 9.249   -1.855  -2.794  1.00 11.39 ? 166 LEU B CG  1 
ATOM   1303 C  CD1 . LEU A 1 166 ? 9.896   -0.875  -1.807  1.00 11.73 ? 166 LEU B CD1 1 
ATOM   1304 C  CD2 . LEU A 1 166 ? 10.159  -2.052  -4.019  1.00 11.51 ? 166 LEU B CD2 1 
ATOM   1305 N  N   . ASP A 1 167 ? 7.186   -5.791  -1.355  1.00 15.70 ? 167 ASP B N   1 
ATOM   1306 C  CA  . ASP A 1 167 ? 7.083   -7.079  -0.673  1.00 17.36 ? 167 ASP B CA  1 
ATOM   1307 C  C   . ASP A 1 167 ? 6.793   -8.164  -1.712  1.00 19.66 ? 167 ASP B C   1 
ATOM   1308 O  O   . ASP A 1 167 ? 7.337   -9.271  -1.608  1.00 20.47 ? 167 ASP B O   1 
ATOM   1309 C  CB  . ASP A 1 167 ? 5.875   -7.052  0.275   1.00 19.11 ? 167 ASP B CB  1 
ATOM   1310 C  CG  . ASP A 1 167 ? 6.175   -6.397  1.610   1.00 24.73 ? 167 ASP B CG  1 
ATOM   1311 O  OD1 . ASP A 1 167 ? 7.338   -6.028  1.887   1.00 25.88 ? 167 ASP B OD1 1 
ATOM   1312 O  OD2 . ASP A 1 167 ? 5.214   -6.259  2.391   1.00 29.77 ? 167 ASP B OD2 1 
ATOM   1313 N  N   . SER A 1 168 ? 5.995   -7.844  -2.728  1.00 17.57 ? 168 SER B N   1 
ATOM   1314 C  CA  . SER A 1 168 ? 5.682   -8.827  -3.733  1.00 17.75 ? 168 SER B CA  1 
ATOM   1315 C  C   . SER A 1 168 ? 6.849   -9.138  -4.685  1.00 17.28 ? 168 SER B C   1 
ATOM   1316 O  O   . SER A 1 168 ? 6.834   -10.152 -5.407  1.00 16.44 ? 168 SER B O   1 
ATOM   1317 C  CB  . SER A 1 168 ? 4.431   -8.369  -4.497  1.00 18.79 ? 168 SER B CB  1 
ATOM   1318 O  OG  . SER A 1 168 ? 4.800   -7.413  -5.456  1.00 19.27 ? 168 SER B OG  1 
ATOM   1319 N  N   . ILE A 1 169 ? 7.856   -8.277  -4.695  1.00 16.07 ? 169 ILE B N   1 
ATOM   1320 C  CA  . ILE A 1 169 ? 8.990   -8.525  -5.567  1.00 14.31 ? 169 ILE B CA  1 
ATOM   1321 C  C   . ILE A 1 169 ? 10.297  -8.695  -4.800  1.00 13.50 ? 169 ILE B C   1 
ATOM   1322 O  O   . ILE A 1 169 ? 11.371  -8.290  -5.261  1.00 12.46 ? 169 ILE B O   1 
ATOM   1323 C  CB  . ILE A 1 169 ? 9.145   -7.460  -6.706  1.00 13.72 ? 169 ILE B CB  1 
ATOM   1324 C  CG1 . ILE A 1 169 ? 9.316   -6.060  -6.133  1.00 12.37 ? 169 ILE B CG1 1 
ATOM   1325 C  CG2 . ILE A 1 169 ? 7.972   -7.597  -7.697  1.00 15.03 ? 169 ILE B CG2 1 
ATOM   1326 C  CD1 . ILE A 1 169 ? 9.800   -5.015  -7.211  1.00 14.63 ? 169 ILE B CD1 1 
ATOM   1327 N  N   . LYS A 1 170 ? 10.205  -9.306  -3.618  1.00 15.20 ? 170 LYS B N   1 
ATOM   1328 C  CA  . LYS A 1 170 ? 11.391  -9.419  -2.806  1.00 15.87 ? 170 LYS B CA  1 
ATOM   1329 C  C   . LYS A 1 170 ? 12.552  -10.140 -3.497  1.00 13.86 ? 170 LYS B C   1 
ATOM   1330 O  O   . LYS A 1 170 ? 13.688  -9.649  -3.492  1.00 14.32 ? 170 LYS B O   1 
ATOM   1331 C  CB  . LYS A 1 170 ? 11.035  -10.014 -1.456  1.00 18.09 ? 170 LYS B CB  1 
ATOM   1332 C  CG  . LYS A 1 170 ? 12.225  -10.204 -0.505  1.00 22.62 ? 170 LYS B CG  1 
ATOM   1333 C  CD  . LYS A 1 170 ? 11.763  -10.853 0.829   1.00 26.54 ? 170 LYS B CD  1 
ATOM   1334 C  CE  . LYS A 1 170 ? 12.926  -11.538 1.579   1.00 33.33 ? 170 LYS B CE  1 
ATOM   1335 N  NZ  . LYS A 1 170 ? 13.125  -11.176 3.037   1.00 37.90 ? 170 LYS B NZ  1 
ATOM   1336 N  N   . GLU A 1 171 ? 12.267  -11.296 -4.097  1.00 15.36 ? 171 GLU B N   1 
ATOM   1337 C  CA  . GLU A 1 171 ? 13.323  -12.114 -4.673  1.00 16.39 ? 171 GLU B CA  1 
ATOM   1338 C  C   . GLU A 1 171 ? 13.623  -11.669 -6.062  1.00 14.64 ? 171 GLU B C   1 
ATOM   1339 O  O   . GLU A 1 171 ? 12.697  -11.266 -6.787  1.00 15.68 ? 171 GLU B O   1 
ATOM   1340 C  CB  . GLU A 1 171 ? 12.878  -13.615 -4.710  1.00 19.70 ? 171 GLU B CB  1 
ATOM   1341 C  CG  . GLU A 1 171 ? 12.528  -14.225 -3.323  1.00 24.94 ? 171 GLU B CG  1 
ATOM   1342 C  CD  . GLU A 1 171 ? 11.195  -13.719 -2.705  1.00 27.43 ? 171 GLU B CD  1 
ATOM   1343 O  OE1 . GLU A 1 171 ? 11.092  -13.697 -1.458  1.00 34.69 ? 171 GLU B OE1 1 
ATOM   1344 O  OE2 . GLU A 1 171 ? 10.239  -13.293 -3.425  1.00 31.80 ? 171 GLU B OE2 1 
ATOM   1345 N  N   . LYS A 1 172 ? 14.884  -11.737 -6.463  1.00 15.44 ? 172 LYS B N   1 
ATOM   1346 C  CA  . LYS A 1 172 ? 15.314  -11.439 -7.844  1.00 15.52 ? 172 LYS B CA  1 
ATOM   1347 C  C   . LYS A 1 172 ? 14.454  -12.260 -8.831  1.00 17.76 ? 172 LYS B C   1 
ATOM   1348 O  O   . LYS A 1 172 ? 14.309  -13.488 -8.648  1.00 14.74 ? 172 LYS B O   1 
ATOM   1349 C  CB  . LYS A 1 172 ? 16.815  -11.812 -8.029  1.00 15.21 ? 172 LYS B CB  1 
ATOM   1350 C  CG  . LYS A 1 172 ? 17.324  -11.721 -9.489  1.00 14.82 ? 172 LYS B CG  1 
ATOM   1351 C  CD  . LYS A 1 172 ? 18.802  -12.064 -9.530  1.00 16.23 ? 172 LYS B CD  1 
ATOM   1352 C  CE  . LYS A 1 172 ? 19.378  -11.946 -10.929 1.00 17.27 ? 172 LYS B CE  1 
ATOM   1353 N  NZ  . LYS A 1 172 ? 20.846  -12.225 -10.840 1.00 20.87 ? 172 LYS B NZ  1 
ATOM   1354 N  N   . GLY A 1 173 ? 13.968  -11.574 -9.878  1.00 16.77 ? 173 GLY B N   1 
ATOM   1355 C  CA  . GLY A 1 173 ? 13.173  -12.196 -10.938 1.00 17.06 ? 173 GLY B CA  1 
ATOM   1356 C  C   . GLY A 1 173 ? 11.680  -12.090 -10.726 1.00 17.16 ? 173 GLY B C   1 
ATOM   1357 O  O   . GLY A 1 173 ? 10.914  -12.241 -11.674 1.00 18.56 ? 173 GLY B O   1 
ATOM   1358 N  N   . LYS A 1 174 ? 11.236  -11.796 -9.516  1.00 16.08 ? 174 LYS B N   1 
ATOM   1359 C  CA  . LYS A 1 174 ? 9.818   -11.598 -9.270  1.00 16.02 ? 174 LYS B CA  1 
ATOM   1360 C  C   . LYS A 1 174 ? 9.315   -10.362 -9.984  1.00 16.79 ? 174 LYS B C   1 
ATOM   1361 O  O   . LYS A 1 174 ? 10.039  -9.377  -10.148 1.00 14.20 ? 174 LYS B O   1 
ATOM   1362 C  CB  . LYS A 1 174 ? 9.498   -11.470 -7.786  1.00 19.49 ? 174 LYS B CB  1 
ATOM   1363 C  CG  . LYS A 1 174 ? 9.724   -12.729 -6.946  1.00 23.55 ? 174 LYS B CG  1 
ATOM   1364 C  CD  . LYS A 1 174 ? 9.093   -13.944 -7.584  1.00 28.38 ? 174 LYS B CD  1 
ATOM   1365 C  CE  . LYS A 1 174 ? 9.372   -15.161 -6.734  1.00 35.33 ? 174 LYS B CE  1 
ATOM   1366 N  NZ  . LYS A 1 174 ? 8.728   -15.012 -5.394  1.00 36.59 ? 174 LYS B NZ  1 
ATOM   1367 N  N   . GLN A 1 175 ? 8.055   -10.428 -10.393 1.00 18.58 ? 175 GLN B N   1 
ATOM   1368 C  CA  . GLN A 1 175 ? 7.404   -9.315  -11.087 1.00 21.56 ? 175 GLN B CA  1 
ATOM   1369 C  C   . GLN A 1 175 ? 5.928   -9.245  -10.810 1.00 20.93 ? 175 GLN B C   1 
ATOM   1370 O  O   . GLN A 1 175 ? 5.321   -10.245 -10.404 1.00 21.21 ? 175 GLN B O   1 
ATOM   1371 C  CB  . GLN A 1 175 ? 7.657   -9.307  -12.561 1.00 26.15 ? 175 GLN B CB  1 
ATOM   1372 C  CG  . GLN A 1 175 ? 7.167   -10.446 -13.382 1.00 32.15 ? 175 GLN B CG  1 
ATOM   1373 C  CD  . GLN A 1 175 ? 7.659   -10.315 -14.837 1.00 39.97 ? 175 GLN B CD  1 
ATOM   1374 O  OE1 . GLN A 1 175 ? 6.885   -10.551 -15.780 1.00 45.40 ? 175 GLN B OE1 1 
ATOM   1375 N  NE2 . GLN A 1 175 ? 8.942   -9.921  -15.024 1.00 31.89 ? 175 GLN B NE2 1 
ATOM   1376 N  N   . THR A 1 176 ? 5.359   -8.051  -10.983 1.00 17.38 ? 176 THR B N   1 
ATOM   1377 C  CA  . THR A 1 176 ? 3.988   -7.834  -10.596 1.00 15.57 ? 176 THR B CA  1 
ATOM   1378 C  C   . THR A 1 176 ? 3.428   -6.840  -11.602 1.00 12.63 ? 176 THR B C   1 
ATOM   1379 O  O   . THR A 1 176 ? 4.092   -5.871  -11.969 1.00 12.78 ? 176 THR B O   1 
ATOM   1380 C  CB  . THR A 1 176 ? 3.962   -7.199  -9.170  1.00 18.75 ? 176 THR B CB  1 
ATOM   1381 O  OG1 . THR A 1 176 ? 4.418   -8.174  -8.217  1.00 23.01 ? 176 THR B OG1 1 
ATOM   1382 C  CG2 . THR A 1 176 ? 2.544   -6.760  -8.866  1.00 22.09 ? 176 THR B CG2 1 
ATOM   1383 N  N   . ARG A 1 177 ? 2.237   -7.120  -12.116 1.00 12.03 ? 177 ARG B N   1 
ATOM   1384 C  CA  . ARG A 1 177 ? 1.628   -6.174  -13.071 1.00 12.12 ? 177 ARG B CA  1 
ATOM   1385 C  C   . ARG A 1 177 ? 1.520   -4.795  -12.338 1.00 11.89 ? 177 ARG B C   1 
ATOM   1386 O  O   . ARG A 1 177 ? 1.097   -4.706  -11.176 1.00 12.95 ? 177 ARG B O   1 
ATOM   1387 C  CB  . ARG A 1 177 ? 0.309   -6.704  -13.599 1.00 12.70 ? 177 ARG B CB  1 
ATOM   1388 C  CG  . ARG A 1 177 ? 0.547   -7.850  -14.579 1.00 13.07 ? 177 ARG B CG  1 
ATOM   1389 C  CD  . ARG A 1 177 ? -0.750  -8.298  -15.173 1.00 13.71 ? 177 ARG B CD  1 
ATOM   1390 N  NE  . ARG A 1 177 ? -1.274  -7.325  -16.110 1.00 14.05 ? 177 ARG B NE  1 
ATOM   1391 C  CZ  . ARG A 1 177 ? -2.343  -7.521  -16.859 1.00 13.58 ? 177 ARG B CZ  1 
ATOM   1392 N  NH1 . ARG A 1 177 ? -2.988  -8.700  -16.822 1.00 13.11 ? 177 ARG B NH1 1 
ATOM   1393 N  NH2 . ARG A 1 177 ? -2.724  -6.544  -17.685 1.00 14.36 ? 177 ARG B NH2 1 
ATOM   1394 N  N   . PHE A 1 178 ? 1.701   -3.745  -13.122 1.00 10.88 ? 178 PHE B N   1 
ATOM   1395 C  CA  . PHE A 1 178 ? 1.878   -2.395  -12.567 1.00 10.79 ? 178 PHE B CA  1 
ATOM   1396 C  C   . PHE A 1 178 ? 1.592   -1.392  -13.676 1.00 11.16 ? 178 PHE B C   1 
ATOM   1397 O  O   . PHE A 1 178 ? 2.434   -1.192  -14.571 1.00 12.49 ? 178 PHE B O   1 
ATOM   1398 C  CB  . PHE A 1 178 ? 3.339   -2.270  -12.127 1.00 10.13 ? 178 PHE B CB  1 
ATOM   1399 C  CG  . PHE A 1 178 ? 3.686   -0.950  -11.396 1.00 10.73 ? 178 PHE B CG  1 
ATOM   1400 C  CD1 . PHE A 1 178 ? 3.582   -0.866  -10.024 1.00 11.38 ? 178 PHE B CD1 1 
ATOM   1401 C  CD2 . PHE A 1 178 ? 4.263   0.148   -12.099 1.00 12.15 ? 178 PHE B CD2 1 
ATOM   1402 C  CE1 . PHE A 1 178 ? 3.974   0.311   -9.326  1.00 12.98 ? 178 PHE B CE1 1 
ATOM   1403 C  CE2 . PHE A 1 178 ? 4.627   1.339   -11.406 1.00 12.18 ? 178 PHE B CE2 1 
ATOM   1404 C  CZ  . PHE A 1 178 ? 4.486   1.422   -10.022 1.00 12.61 ? 178 PHE B CZ  1 
ATOM   1405 N  N   . THR A 1 179 ? 0.439   -0.750  -13.581 1.00 12.00 ? 179 THR B N   1 
ATOM   1406 C  CA  . THR A 1 179 ? 0.031   0.222   -14.617 1.00 12.85 ? 179 THR B CA  1 
ATOM   1407 C  C   . THR A 1 179 ? -0.695  1.366   -13.959 1.00 13.50 ? 179 THR B C   1 
ATOM   1408 O  O   . THR A 1 179 ? -0.791  1.451   -12.717 1.00 12.58 ? 179 THR B O   1 
ATOM   1409 C  CB  . THR A 1 179 ? -0.754  -0.413  -15.829 1.00 13.98 ? 179 THR B CB  1 
ATOM   1410 O  OG1 . THR A 1 179 ? -0.800  0.504   -16.962 1.00 14.81 ? 179 THR B OG1 1 
ATOM   1411 C  CG2 . THR A 1 179 ? -2.161  -0.788  -15.409 1.00 15.00 ? 179 THR B CG2 1 
ATOM   1412 N  N   . ASN A 1 180 ? -1.146  2.300   -14.795 1.00 12.84 ? 180 ASN B N   1 
ATOM   1413 C  CA  . ASN A 1 180 ? -1.592  3.609   -14.315 1.00 13.20 ? 180 ASN B CA  1 
ATOM   1414 C  C   . ASN A 1 180 ? -0.537  4.237   -13.372 1.00 12.69 ? 180 ASN B C   1 
ATOM   1415 O  O   . ASN A 1 180 ? -0.850  4.641   -12.220 1.00 12.27 ? 180 ASN B O   1 
ATOM   1416 C  CB  . ASN A 1 180 ? -2.980  3.516   -13.616 1.00 15.03 ? 180 ASN B CB  1 
ATOM   1417 C  CG  . ASN A 1 180 ? -3.612  4.918   -13.392 1.00 17.40 ? 180 ASN B CG  1 
ATOM   1418 O  OD1 . ASN A 1 180 ? -3.445  5.816   -14.207 1.00 18.78 ? 180 ASN B OD1 1 
ATOM   1419 N  ND2 . ASN A 1 180 ? -4.334  5.095   -12.253 1.00 19.65 ? 180 ASN B ND2 1 
ATOM   1420 N  N   . PHE A 1 181 ? 0.691   4.342   -13.834 1.00 11.14 ? 181 PHE B N   1 
ATOM   1421 C  CA  . PHE A 1 181 ? 1.700   4.986   -13.015 1.00 11.25 ? 181 PHE B CA  1 
ATOM   1422 C  C   . PHE A 1 181 ? 1.951   6.382   -13.586 1.00 10.52 ? 181 PHE B C   1 
ATOM   1423 O  O   . PHE A 1 181 ? 2.527   6.519   -14.665 1.00 10.59 ? 181 PHE B O   1 
ATOM   1424 C  CB  . PHE A 1 181 ? 2.984   4.143   -13.090 1.00 10.69 ? 181 PHE B CB  1 
ATOM   1425 C  CG  . PHE A 1 181 ? 4.208   4.809   -12.511 1.00 10.51 ? 181 PHE B CG  1 
ATOM   1426 C  CD1 . PHE A 1 181 ? 4.179   5.451   -11.261 1.00 10.48 ? 181 PHE B CD1 1 
ATOM   1427 C  CD2 . PHE A 1 181 ? 5.421   4.711   -13.175 1.00 10.59 ? 181 PHE B CD2 1 
ATOM   1428 C  CE1 . PHE A 1 181 ? 5.340   6.013   -10.743 1.00 10.61 ? 181 PHE B CE1 1 
ATOM   1429 C  CE2 . PHE A 1 181 ? 6.608   5.254   -12.647 1.00 11.16 ? 181 PHE B CE2 1 
ATOM   1430 C  CZ  . PHE A 1 181 ? 6.555   5.881   -11.412 1.00 11.11 ? 181 PHE B CZ  1 
ATOM   1431 N  N   . ASP A 1 182 ? 1.560   7.385   -12.811 1.00 10.49 ? 182 ASP B N   1 
ATOM   1432 C  CA  . ASP A 1 182 ? 1.581   8.755   -13.284 1.00 10.58 ? 182 ASP B CA  1 
ATOM   1433 C  C   . ASP A 1 182 ? 3.015   9.321   -13.025 1.00 10.27 ? 182 ASP B C   1 
ATOM   1434 O  O   . ASP A 1 182 ? 3.281   10.095  -12.105 1.00 11.49 ? 182 ASP B O   1 
ATOM   1435 C  CB  . ASP A 1 182 ? 0.503   9.528   -12.576 1.00 11.16 ? 182 ASP B CB  1 
ATOM   1436 C  CG  . ASP A 1 182 ? 0.328   10.961  -13.138 1.00 12.68 ? 182 ASP B CG  1 
ATOM   1437 O  OD1 . ASP A 1 182 ? 0.795   11.255  -14.294 1.00 12.06 ? 182 ASP B OD1 1 
ATOM   1438 O  OD2 . ASP A 1 182 ? -0.268  11.770  -12.398 1.00 12.87 ? 182 ASP B OD2 1 
ATOM   1439 N  N   . LEU A 1 183 ? 3.943   8.886   -13.861 1.00 10.61 ? 183 LEU B N   1 
ATOM   1440 C  CA  . LEU A 1 183 ? 5.374   9.255   -13.666 1.00 10.52 ? 183 LEU B CA  1 
ATOM   1441 C  C   . LEU A 1 183 ? 5.581   10.776  -13.719 1.00 10.56 ? 183 LEU B C   1 
ATOM   1442 O  O   . LEU A 1 183 ? 6.423   11.306  -13.035 1.00 10.15 ? 183 LEU B O   1 
ATOM   1443 C  CB  . LEU A 1 183 ? 6.227   8.560   -14.764 1.00 10.80 ? 183 LEU B CB  1 
ATOM   1444 C  CG  . LEU A 1 183 ? 7.718   8.916   -14.810 1.00 10.32 ? 183 LEU B CG  1 
ATOM   1445 C  CD1 . LEU A 1 183 ? 8.402   8.614   -13.453 1.00 11.80 ? 183 LEU B CD1 1 
ATOM   1446 C  CD2 . LEU A 1 183 ? 8.426   8.162   -15.950 1.00 11.64 ? 183 LEU B CD2 1 
ATOM   1447 N  N   . LEU A 1 184 ? 4.815   11.472  -14.566 1.00 9.91  ? 184 LEU B N   1 
ATOM   1448 C  CA  . LEU A 1 184 ? 4.863   12.959  -14.595 1.00 10.82 ? 184 LEU B CA  1 
ATOM   1449 C  C   . LEU A 1 184 ? 4.777   13.605  -13.221 1.00 11.26 ? 184 LEU B C   1 
ATOM   1450 O  O   . LEU A 1 184 ? 5.497   14.603  -12.908 1.00 10.76 ? 184 LEU B O   1 
ATOM   1451 C  CB  . LEU A 1 184 ? 3.689   13.454  -15.465 1.00 11.94 ? 184 LEU B CB  1 
ATOM   1452 C  CG  . LEU A 1 184 ? 3.701   14.991  -15.520 1.00 14.27 ? 184 LEU B CG  1 
ATOM   1453 C  CD1 . LEU A 1 184 ? 4.839   15.606  -16.334 1.00 16.01 ? 184 LEU B CD1 1 
ATOM   1454 C  CD2 . LEU A 1 184 ? 2.314   15.438  -16.036 1.00 14.98 ? 184 LEU B CD2 1 
ATOM   1455 N  N   . SER A 1 185 ? 3.894   13.038  -12.403 1.00 10.40 ? 185 SER B N   1 
ATOM   1456 C  CA  . SER A 1 185 ? 3.555   13.638  -11.132 1.00 11.57 ? 185 SER B CA  1 
ATOM   1457 C  C   . SER A 1 185 ? 4.645   13.350  -10.075 1.00 12.87 ? 185 SER B C   1 
ATOM   1458 O  O   . SER A 1 185 ? 4.603   13.936  -8.948  1.00 13.58 ? 185 SER B O   1 
ATOM   1459 C  CB  . SER A 1 185 ? 2.149   13.230  -10.641 1.00 11.83 ? 185 SER B CB  1 
ATOM   1460 O  OG  . SER A 1 185 ? 1.156   13.861  -11.449 1.00 12.82 ? 185 SER B OG  1 
ATOM   1461 N  N   . LEU A 1 186 ? 5.599   12.483  -10.414 1.00 12.17 ? 186 LEU B N   1 
ATOM   1462 C  CA  . LEU A 1 186 ? 6.715   12.178  -9.491  1.00 13.19 ? 186 LEU B CA  1 
ATOM   1463 C  C   . LEU A 1 186 ? 7.831   13.169  -9.681  1.00 11.89 ? 186 LEU B C   1 
ATOM   1464 O  O   . LEU A 1 186 ? 8.643   13.360  -8.806  1.00 11.94 ? 186 LEU B O   1 
ATOM   1465 C  CB  . LEU A 1 186 ? 7.255   10.752  -9.733  1.00 13.54 ? 186 LEU B CB  1 
ATOM   1466 C  CG  . LEU A 1 186 ? 8.350   10.150  -8.821  1.00 16.93 ? 186 LEU B CG  1 
ATOM   1467 C  CD1 . LEU A 1 186 ? 7.958   10.195  -7.353  1.00 14.60 ? 186 LEU B CD1 1 
ATOM   1468 C  CD2 . LEU A 1 186 ? 8.621   8.680   -9.193  1.00 14.71 ? 186 LEU B CD2 1 
ATOM   1469 N  N   . LEU A 1 187 ? 7.873   13.845  -10.808 1.00 12.35 ? 187 LEU B N   1 
ATOM   1470 C  CA  . LEU A 1 187 ? 8.995   14.718  -11.075 1.00 11.75 ? 187 LEU B CA  1 
ATOM   1471 C  C   . LEU A 1 187 ? 8.899   16.009  -10.253 1.00 11.14 ? 187 LEU B C   1 
ATOM   1472 O  O   . LEU A 1 187 ? 7.765   16.444  -9.851  1.00 11.79 ? 187 LEU B O   1 
ATOM   1473 C  CB  . LEU A 1 187 ? 8.946   15.138  -12.573 1.00 13.12 ? 187 LEU B CB  1 
ATOM   1474 C  CG  . LEU A 1 187 ? 9.042   13.942  -13.552 1.00 13.55 ? 187 LEU B CG  1 
ATOM   1475 C  CD1 . LEU A 1 187 ? 8.793   14.364  -14.991 1.00 15.76 ? 187 LEU B CD1 1 
ATOM   1476 C  CD2 . LEU A 1 187 ? 10.380  13.240  -13.362 1.00 12.55 ? 187 LEU B CD2 1 
ATOM   1477 N  N   . PRO A 1 188 ? 10.032  16.684  -10.045 1.00 10.74 ? 188 PRO B N   1 
ATOM   1478 C  CA  . PRO A 1 188 ? 10.028  17.961  -9.330  1.00 11.57 ? 188 PRO B CA  1 
ATOM   1479 C  C   . PRO A 1 188 ? 9.353   19.017  -10.242 1.00 13.05 ? 188 PRO B C   1 
ATOM   1480 O  O   . PRO A 1 188 ? 9.180   18.780  -11.436 1.00 12.34 ? 188 PRO B O   1 
ATOM   1481 C  CB  . PRO A 1 188 ? 11.523  18.267  -9.134  1.00 11.03 ? 188 PRO B CB  1 
ATOM   1482 C  CG  . PRO A 1 188 ? 12.201  17.608  -10.296 1.00 12.44 ? 188 PRO B CG  1 
ATOM   1483 C  CD  . PRO A 1 188 ? 11.402  16.318  -10.489 1.00 9.95  ? 188 PRO B CD  1 
ATOM   1484 N  N   . PRO A 1 189 ? 8.890   20.092  -9.631  1.00 16.17 ? 189 PRO B N   1 
ATOM   1485 C  CA  . PRO A 1 189 ? 8.161   21.148  -10.382 1.00 15.86 ? 189 PRO B CA  1 
ATOM   1486 C  C   . PRO A 1 189 ? 9.062   22.002  -11.285 1.00 15.83 ? 189 PRO B C   1 
ATOM   1487 O  O   . PRO A 1 189 ? 8.583   22.505  -12.310 1.00 18.06 ? 189 PRO B O   1 
ATOM   1488 C  CB  . PRO A 1 189 ? 7.505   21.969  -9.245  1.00 18.15 ? 189 PRO B CB  1 
ATOM   1489 C  CG  . PRO A 1 189 ? 8.489   21.845  -8.104  1.00 16.54 ? 189 PRO B CG  1 
ATOM   1490 C  CD  . PRO A 1 189 ? 8.949   20.387  -8.168  1.00 13.77 ? 189 PRO B CD  1 
ATOM   1491 N  N   . SER A 1 190 ? 10.356  22.098  -10.975 1.00 14.86 ? 190 SER B N   1 
ATOM   1492 C  CA  . SER A 1 190 ? 11.394  22.743  -11.877 1.00 13.27 ? 190 SER B CA  1 
ATOM   1493 C  C   . SER A 1 190 ? 12.128  21.712  -12.708 1.00 11.95 ? 190 SER B C   1 
ATOM   1494 O  O   . SER A 1 190 ? 12.626  20.723  -12.162 1.00 10.84 ? 190 SER B O   1 
ATOM   1495 C  CB  . SER A 1 190 ? 12.408  23.565  -11.099 1.00 14.60 ? 190 SER B CB  1 
ATOM   1496 O  OG  . SER A 1 190 ? 13.474  24.084  -11.973 1.00 17.40 ? 190 SER B OG  1 
ATOM   1497 N  N   . TRP A 1 191 ? 12.249  21.990  -14.002 1.00 11.34 ? 191 TRP B N   1 
ATOM   1498 C  CA  . TRP A 1 191 ? 12.956  21.102  -14.853 1.00 11.83 ? 191 TRP B CA  1 
ATOM   1499 C  C   . TRP A 1 191 ? 14.257  21.695  -15.346 1.00 11.74 ? 191 TRP B C   1 
ATOM   1500 O  O   . TRP A 1 191 ? 14.727  21.254  -16.408 1.00 11.69 ? 191 TRP B O   1 
ATOM   1501 C  CB  . TRP A 1 191 ? 12.057  20.731  -16.078 1.00 12.61 ? 191 TRP B CB  1 
ATOM   1502 C  CG  . TRP A 1 191 ? 10.780  19.896  -15.700 1.00 14.06 ? 191 TRP B CG  1 
ATOM   1503 C  CD1 . TRP A 1 191 ? 10.476  19.339  -14.476 1.00 14.22 ? 191 TRP B CD1 1 
ATOM   1504 C  CD2 . TRP A 1 191 ? 9.707   19.530  -16.587 1.00 15.31 ? 191 TRP B CD2 1 
ATOM   1505 N  NE1 . TRP A 1 191 ? 9.273   18.644  -14.548 1.00 16.37 ? 191 TRP B NE1 1 
ATOM   1506 C  CE2 . TRP A 1 191 ? 8.778   18.743  -15.829 1.00 15.72 ? 191 TRP B CE2 1 
ATOM   1507 C  CE3 . TRP A 1 191 ? 9.451   19.768  -17.953 1.00 15.03 ? 191 TRP B CE3 1 
ATOM   1508 C  CZ2 . TRP A 1 191 ? 7.565   18.219  -16.403 1.00 17.32 ? 191 TRP B CZ2 1 
ATOM   1509 C  CZ3 . TRP A 1 191 ? 8.270   19.285  -18.515 1.00 16.49 ? 191 TRP B CZ3 1 
ATOM   1510 C  CH2 . TRP A 1 191 ? 7.322   18.518  -17.729 1.00 16.21 ? 191 TRP B CH2 1 
ATOM   1511 N  N   . ASP A 1 192 ? 14.876  22.622  -14.590 1.00 11.61 ? 192 ASP B N   1 
ATOM   1512 C  CA  . ASP A 1 192 ? 16.239  23.048  -14.863 1.00 11.65 ? 192 ASP B CA  1 
ATOM   1513 C  C   . ASP A 1 192 ? 17.164  21.853  -14.719 1.00 11.97 ? 192 ASP B C   1 
ATOM   1514 O  O   . ASP A 1 192 ? 16.963  20.989  -13.818 1.00 11.25 ? 192 ASP B O   1 
ATOM   1515 C  CB  . ASP A 1 192 ? 16.711  24.103  -13.882 1.00 12.35 ? 192 ASP B CB  1 
ATOM   1516 C  CG  . ASP A 1 192 ? 15.911  25.420  -13.954 1.00 15.44 ? 192 ASP B CG  1 
ATOM   1517 O  OD1 . ASP A 1 192 ? 15.187  25.725  -14.943 1.00 17.20 ? 192 ASP B OD1 1 
ATOM   1518 O  OD2 . ASP A 1 192 ? 16.042  26.150  -12.946 1.00 18.54 ? 192 ASP B OD2 1 
ATOM   1519 N  N   . TYR A 1 193 ? 18.190  21.787  -15.559 1.00 11.27 ? 193 TYR B N   1 
ATOM   1520 C  CA  . TYR A 1 193 ? 19.020  20.565  -15.630 1.00 10.39 ? 193 TYR B CA  1 
ATOM   1521 C  C   . TYR A 1 193 ? 20.507  20.867  -15.935 1.00 10.47 ? 193 TYR B C   1 
ATOM   1522 O  O   . TYR A 1 193 ? 20.787  21.922  -16.529 1.00 10.24 ? 193 TYR B O   1 
ATOM   1523 C  CB  . TYR A 1 193 ? 18.435  19.587  -16.689 1.00 9.68  ? 193 TYR B CB  1 
ATOM   1524 C  CG  . TYR A 1 193 ? 18.469  20.112  -18.115 1.00 9.66  ? 193 TYR B CG  1 
ATOM   1525 C  CD1 . TYR A 1 193 ? 19.579  19.907  -18.928 1.00 9.51  ? 193 TYR B CD1 1 
ATOM   1526 C  CD2 . TYR A 1 193 ? 17.348  20.815  -18.657 1.00 11.10 ? 193 TYR B CD2 1 
ATOM   1527 C  CE1 . TYR A 1 193 ? 19.633  20.434  -20.209 1.00 10.33 ? 193 TYR B CE1 1 
ATOM   1528 C  CE2 . TYR A 1 193 ? 17.387  21.296  -19.941 1.00 10.58 ? 193 TYR B CE2 1 
ATOM   1529 C  CZ  . TYR A 1 193 ? 18.522  21.104  -20.721 1.00 11.11 ? 193 TYR B CZ  1 
ATOM   1530 O  OH  . TYR A 1 193 ? 18.538  21.630  -22.005 1.00 10.76 ? 193 TYR B OH  1 
ATOM   1531 N  N   . TRP A 1 194 ? 21.370  19.904  -15.591 1.00 10.24 ? 194 TRP B N   1 
ATOM   1532 C  CA  . TRP A 1 194 ? 22.731  19.789  -16.103 1.00 10.19 ? 194 TRP B CA  1 
ATOM   1533 C  C   . TRP A 1 194 ? 22.728  18.661  -17.120 1.00 10.11 ? 194 TRP B C   1 
ATOM   1534 O  O   . TRP A 1 194 ? 21.946  17.708  -16.996 1.00 10.15 ? 194 TRP B O   1 
ATOM   1535 C  CB  . TRP A 1 194 ? 23.717  19.407  -14.960 1.00 11.33 ? 194 TRP B CB  1 
ATOM   1536 C  CG  . TRP A 1 194 ? 23.833  20.429  -13.907 1.00 10.87 ? 194 TRP B CG  1 
ATOM   1537 C  CD1 . TRP A 1 194 ? 24.436  21.680  -13.998 1.00 12.71 ? 194 TRP B CD1 1 
ATOM   1538 C  CD2 . TRP A 1 194 ? 23.366  20.329  -12.537 1.00 12.54 ? 194 TRP B CD2 1 
ATOM   1539 N  NE1 . TRP A 1 194 ? 24.308  22.372  -12.841 1.00 12.75 ? 194 TRP B NE1 1 
ATOM   1540 C  CE2 . TRP A 1 194 ? 23.696  21.564  -11.900 1.00 12.52 ? 194 TRP B CE2 1 
ATOM   1541 C  CE3 . TRP A 1 194 ? 22.650  19.355  -11.827 1.00 11.58 ? 194 TRP B CE3 1 
ATOM   1542 C  CZ2 . TRP A 1 194 ? 23.344  21.853  -10.550 1.00 12.62 ? 194 TRP B CZ2 1 
ATOM   1543 C  CZ3 . TRP A 1 194 ? 22.311  19.614  -10.484 1.00 12.41 ? 194 TRP B CZ3 1 
ATOM   1544 C  CH2 . TRP A 1 194 ? 22.668  20.873  -9.857  1.00 11.80 ? 194 TRP B CH2 1 
ATOM   1545 N  N   . THR A 1 195 ? 23.665  18.716  -18.050 1.00 9.74  ? 195 THR B N   1 
ATOM   1546 C  CA  . THR A 1 195 ? 23.752  17.678  -19.067 1.00 8.96  ? 195 THR B CA  1 
ATOM   1547 C  C   . THR A 1 195 ? 25.211  17.399  -19.457 1.00 9.23  ? 195 THR B C   1 
ATOM   1548 O  O   . THR A 1 195 ? 26.047  18.318  -19.473 1.00 8.94  ? 195 THR B O   1 
ATOM   1549 C  CB  . THR A 1 195 ? 22.910  18.032  -20.354 1.00 8.62  ? 195 THR B CB  1 
ATOM   1550 O  OG1 . THR A 1 195 ? 23.005  16.916  -21.290 1.00 8.62  ? 195 THR B OG1 1 
ATOM   1551 C  CG2 . THR A 1 195 ? 23.344  19.381  -21.008 1.00 8.62  ? 195 THR B CG2 1 
ATOM   1552 N  N   . TYR A 1 196 ? 25.503  16.128  -19.757 1.00 8.30  ? 196 TYR B N   1 
ATOM   1553 C  CA  . TYR A 1 196 ? 26.852  15.799  -20.306 1.00 8.60  ? 196 TYR B CA  1 
ATOM   1554 C  C   . TYR A 1 196 ? 26.716  14.434  -20.993 1.00 8.70  ? 196 TYR B C   1 
ATOM   1555 O  O   . TYR A 1 196 ? 25.751  13.654  -20.754 1.00 9.42  ? 196 TYR B O   1 
ATOM   1556 C  CB  . TYR A 1 196 ? 27.913  15.776  -19.138 1.00 9.11  ? 196 TYR B CB  1 
ATOM   1557 C  CG  . TYR A 1 196 ? 27.699  14.548  -18.223 1.00 9.04  ? 196 TYR B CG  1 
ATOM   1558 C  CD1 . TYR A 1 196 ? 26.691  14.539  -17.243 1.00 8.61  ? 196 TYR B CD1 1 
ATOM   1559 C  CD2 . TYR A 1 196 ? 28.495  13.390  -18.378 1.00 9.02  ? 196 TYR B CD2 1 
ATOM   1560 C  CE1 . TYR A 1 196 ? 26.546  13.418  -16.393 1.00 8.63  ? 196 TYR B CE1 1 
ATOM   1561 C  CE2 . TYR A 1 196 ? 28.284  12.238  -17.623 1.00 8.51  ? 196 TYR B CE2 1 
ATOM   1562 C  CZ  . TYR A 1 196 ? 27.349  12.261  -16.606 1.00 8.83  ? 196 TYR B CZ  1 
ATOM   1563 O  OH  . TYR A 1 196 ? 27.153  11.108  -15.861 1.00 8.43  ? 196 TYR B OH  1 
ATOM   1564 N  N   . PRO A 1 197 ? 27.655  14.112  -21.887 1.00 8.41  ? 197 PRO B N   1 
ATOM   1565 C  CA  . PRO A 1 197 ? 27.667  12.813  -22.572 1.00 8.99  ? 197 PRO B CA  1 
ATOM   1566 C  C   . PRO A 1 197 ? 28.295  11.782  -21.651 1.00 10.12 ? 197 PRO B C   1 
ATOM   1567 O  O   . PRO A 1 197 ? 29.423  12.029  -21.124 1.00 10.89 ? 197 PRO B O   1 
ATOM   1568 C  CB  . PRO A 1 197 ? 28.549  13.104  -23.818 1.00 8.62  ? 197 PRO B CB  1 
ATOM   1569 C  CG  . PRO A 1 197 ? 29.523  14.146  -23.297 1.00 8.22  ? 197 PRO B CG  1 
ATOM   1570 C  CD  . PRO A 1 197 ? 28.723  15.013  -22.346 1.00 9.34  ? 197 PRO B CD  1 
ATOM   1571 N  N   . GLY A 1 198 ? 27.585  10.667  -21.430 1.00 9.81  ? 198 GLY B N   1 
ATOM   1572 C  CA  . GLY A 1 198 ? 28.161  9.633   -20.572 1.00 10.19 ? 198 GLY B CA  1 
ATOM   1573 C  C   . GLY A 1 198 ? 27.746  8.237   -20.975 1.00 10.68 ? 198 GLY B C   1 
ATOM   1574 O  O   . GLY A 1 198 ? 27.650  7.928   -22.199 1.00 10.16 ? 198 GLY B O   1 
ATOM   1575 N  N   . SER A 1 199 ? 27.493  7.398   -19.971 1.00 10.49 ? 199 SER B N   1 
ATOM   1576 C  CA  . SER A 1 199 ? 27.348  5.951   -20.213 1.00 10.17 ? 199 SER B CA  1 
ATOM   1577 C  C   . SER A 1 199 ? 26.232  5.442   -19.340 1.00 10.29 ? 199 SER B C   1 
ATOM   1578 O  O   . SER A 1 199 ? 25.754  6.147   -18.488 1.00 10.95 ? 199 SER B O   1 
ATOM   1579 C  CB  . SER A 1 199 ? 28.676  5.201   -19.835 1.00 10.41 ? 199 SER B CB  1 
ATOM   1580 O  OG  . SER A 1 199 ? 28.849  5.212   -18.426 1.00 10.27 ? 199 SER B OG  1 
ATOM   1581 N  N   . LEU A 1 200 ? 25.849  4.199   -19.579 1.00 9.47  ? 200 LEU B N   1 
ATOM   1582 C  CA  . LEU A 1 200 ? 25.164  3.391   -18.584 1.00 9.74  ? 200 LEU B CA  1 
ATOM   1583 C  C   . LEU A 1 200 ? 26.044  3.347   -17.317 1.00 9.97  ? 200 LEU B C   1 
ATOM   1584 O  O   . LEU A 1 200 ? 27.256  3.274   -17.382 1.00 9.46  ? 200 LEU B O   1 
ATOM   1585 C  CB  . LEU A 1 200 ? 25.025  1.937   -19.098 1.00 9.57  ? 200 LEU B CB  1 
ATOM   1586 C  CG  . LEU A 1 200 ? 23.722  1.617   -19.883 1.00 10.96 ? 200 LEU B CG  1 
ATOM   1587 C  CD1 . LEU A 1 200 ? 23.752  2.390   -21.174 1.00 9.86  ? 200 LEU B CD1 1 
ATOM   1588 C  CD2 . LEU A 1 200 ? 23.568  0.136   -20.146 1.00 10.84 ? 200 LEU B CD2 1 
ATOM   1589 N  N   . THR A 1 201 ? 25.378  3.404   -16.148 1.00 9.24  ? 201 THR B N   1 
ATOM   1590 C  CA  . THR A 1 201 ? 26.141  3.317   -14.880 1.00 9.92  ? 201 THR B CA  1 
ATOM   1591 C  C   . THR A 1 201 ? 26.140  1.893   -14.376 1.00 10.98 ? 201 THR B C   1 
ATOM   1592 O  O   . THR A 1 201 ? 26.671  1.641   -13.269 1.00 11.98 ? 201 THR B O   1 
ATOM   1593 C  CB  . THR A 1 201 ? 25.518  4.213   -13.794 1.00 9.86  ? 201 THR B CB  1 
ATOM   1594 O  OG1 . THR A 1 201 ? 24.249  3.645   -13.415 1.00 10.50 ? 201 THR B OG1 1 
ATOM   1595 C  CG2 . THR A 1 201 ? 25.377  5.682   -14.332 1.00 10.26 ? 201 THR B CG2 1 
ATOM   1596 N  N   . VAL A 1 202 ? 25.569  0.969   -15.158 1.00 10.61 ? 202 VAL B N   1 
ATOM   1597 C  CA  . VAL A 1 202 ? 25.625  -0.473  -14.837 1.00 10.70 ? 202 VAL B CA  1 
ATOM   1598 C  C   . VAL A 1 202 ? 26.184  -1.172  -16.111 1.00 11.70 ? 202 VAL B C   1 
ATOM   1599 O  O   . VAL A 1 202 ? 26.026  -0.663  -17.259 1.00 12.30 ? 202 VAL B O   1 
ATOM   1600 C  CB  . VAL A 1 202 ? 24.245  -1.032  -14.484 1.00 10.81 ? 202 VAL B CB  1 
ATOM   1601 C  CG1 . VAL A 1 202 ? 23.674  -0.404  -13.162 1.00 11.76 ? 202 VAL B CG1 1 
ATOM   1602 C  CG2 . VAL A 1 202 ? 23.207  -0.953  -15.627 1.00 10.86 ? 202 VAL B CG2 1 
ATOM   1603 N  N   . PRO A 1 203 ? 26.811  -2.320  -15.933 1.00 12.60 ? 203 PRO B N   1 
ATOM   1604 C  CA  . PRO A 1 203 ? 27.118  -3.190  -17.071 1.00 12.21 ? 203 PRO B CA  1 
ATOM   1605 C  C   . PRO A 1 203 ? 25.901  -3.307  -18.030 1.00 11.30 ? 203 PRO B C   1 
ATOM   1606 O  O   . PRO A 1 203 ? 24.730  -3.525  -17.603 1.00 11.17 ? 203 PRO B O   1 
ATOM   1607 C  CB  . PRO A 1 203 ? 27.435  -4.529  -16.363 1.00 11.79 ? 203 PRO B CB  1 
ATOM   1608 C  CG  . PRO A 1 203 ? 28.176  -4.089  -15.112 1.00 13.17 ? 203 PRO B CG  1 
ATOM   1609 C  CD  . PRO A 1 203 ? 27.202  -2.977  -14.665 1.00 12.44 ? 203 PRO B CD  1 
ATOM   1610 N  N   . PRO A 1 204 ? 26.169  -3.263  -19.358 1.00 11.94 ? 204 PRO B N   1 
ATOM   1611 C  CA  . PRO A 1 204 ? 27.443  -3.273  -20.035 1.00 12.40 ? 204 PRO B CA  1 
ATOM   1612 C  C   . PRO A 1 204 ? 28.141  -1.936  -20.172 1.00 11.26 ? 204 PRO B C   1 
ATOM   1613 O  O   . PRO A 1 204 ? 29.141  -1.848  -20.894 1.00 12.74 ? 204 PRO B O   1 
ATOM   1614 C  CB  . PRO A 1 204 ? 27.094  -3.815  -21.434 1.00 12.67 ? 204 PRO B CB  1 
ATOM   1615 C  CG  . PRO A 1 204 ? 25.700  -3.282  -21.677 1.00 12.86 ? 204 PRO B CG  1 
ATOM   1616 C  CD  . PRO A 1 204 ? 25.023  -3.358  -20.300 1.00 12.64 ? 204 PRO B CD  1 
ATOM   1617 N  N   . LEU A 1 205 ? 27.664  -0.917  -19.467 1.00 12.11 ? 205 LEU B N   1 
ATOM   1618 C  CA  . LEU A 1 205 ? 28.417  0.357   -19.312 1.00 11.43 ? 205 LEU B CA  1 
ATOM   1619 C  C   . LEU A 1 205 ? 28.620  1.123   -20.627 1.00 11.00 ? 205 LEU B C   1 
ATOM   1620 O  O   . LEU A 1 205 ? 29.547  1.876   -20.792 1.00 10.37 ? 205 LEU B O   1 
ATOM   1621 C  CB  . LEU A 1 205 ? 29.797  0.203   -18.537 1.00 11.65 ? 205 LEU B CB  1 
ATOM   1622 C  CG  . LEU A 1 205 ? 29.657  -0.396  -17.143 1.00 12.80 ? 205 LEU B CG  1 
ATOM   1623 C  CD1 . LEU A 1 205 ? 31.034  -0.848  -16.610 1.00 13.76 ? 205 LEU B CD1 1 
ATOM   1624 C  CD2 . LEU A 1 205 ? 29.067  0.688   -16.191 1.00 11.22 ? 205 LEU B CD2 1 
ATOM   1625 N  N   . LEU A 1 206 ? 27.748  0.865   -21.600 1.00 11.44 ? 206 LEU B N   1 
ATOM   1626 C  CA  . LEU A 1 206 ? 27.926  1.451   -22.937 1.00 12.52 ? 206 LEU B CA  1 
ATOM   1627 C  C   . LEU A 1 206 ? 27.845  2.954   -22.952 1.00 13.00 ? 206 LEU B C   1 
ATOM   1628 O  O   . LEU A 1 206 ? 27.034  3.556   -22.221 1.00 13.19 ? 206 LEU B O   1 
ATOM   1629 C  CB  . LEU A 1 206 ? 26.825  0.905   -23.823 1.00 13.35 ? 206 LEU B CB  1 
ATOM   1630 C  CG  . LEU A 1 206 ? 26.840  -0.629  -24.076 1.00 14.01 ? 206 LEU B CG  1 
ATOM   1631 C  CD1 . LEU A 1 206 ? 25.477  -1.001  -24.635 1.00 15.04 ? 206 LEU B CD1 1 
ATOM   1632 C  CD2 . LEU A 1 206 ? 28.000  -0.991  -25.004 1.00 16.38 ? 206 LEU B CD2 1 
ATOM   1633 N  N   . GLU A 1 207 ? 28.715  3.546   -23.755 1.00 11.13 ? 207 GLU B N   1 
ATOM   1634 C  CA  . GLU A 1 207 ? 28.850  4.985   -23.808 1.00 12.41 ? 207 GLU B CA  1 
ATOM   1635 C  C   . GLU A 1 207 ? 27.894  5.578   -24.827 1.00 12.73 ? 207 GLU B C   1 
ATOM   1636 O  O   . GLU A 1 207 ? 28.299  6.062   -25.894 1.00 12.62 ? 207 GLU B O   1 
ATOM   1637 C  CB  . GLU A 1 207 ? 30.313  5.365   -24.111 1.00 13.40 ? 207 GLU B CB  1 
ATOM   1638 C  CG  . GLU A 1 207 ? 31.198  5.022   -22.901 1.00 13.59 ? 207 GLU B CG  1 
ATOM   1639 C  CD  . GLU A 1 207 ? 32.680  5.432   -23.032 1.00 14.47 ? 207 GLU B CD  1 
ATOM   1640 O  OE1 . GLU A 1 207 ? 33.173  5.663   -24.192 1.00 16.26 ? 207 GLU B OE1 1 
ATOM   1641 O  OE2 . GLU A 1 207 ? 33.374  5.498   -21.982 1.00 13.84 ? 207 GLU B OE2 1 
ATOM   1642 N  N   . SER A 1 208 ? 26.610  5.532   -24.472 1.00 12.34 ? 208 SER B N   1 
ATOM   1643 C  CA  . SER A 1 208 ? 25.525  5.811   -25.420 1.00 12.48 ? 208 SER B CA  1 
ATOM   1644 C  C   . SER A 1 208 ? 24.493  6.759   -24.803 1.00 11.49 ? 208 SER B C   1 
ATOM   1645 O  O   . SER A 1 208 ? 23.409  6.938   -25.364 1.00 11.29 ? 208 SER B O   1 
ATOM   1646 C  CB  . SER A 1 208 ? 24.874  4.481   -25.795 1.00 13.46 ? 208 SER B CB  1 
ATOM   1647 O  OG  . SER A 1 208 ? 24.467  3.794   -24.604 1.00 15.91 ? 208 SER B OG  1 
ATOM   1648 N  N   . VAL A 1 209 ? 24.846  7.398   -23.684 1.00 10.33 ? 209 VAL B N   1 
ATOM   1649 C  CA  . VAL A 1 209 ? 23.860  8.115   -22.873 1.00 10.06 ? 209 VAL B CA  1 
ATOM   1650 C  C   . VAL A 1 209 ? 24.102  9.651   -22.861 1.00 10.11 ? 209 VAL B C   1 
ATOM   1651 O  O   . VAL A 1 209 ? 25.197  10.107  -22.520 1.00 10.63 ? 209 VAL B O   1 
ATOM   1652 C  CB  . VAL A 1 209 ? 23.761  7.579   -21.416 1.00 10.13 ? 209 VAL B CB  1 
ATOM   1653 C  CG1 . VAL A 1 209 ? 22.662  8.431   -20.633 1.00 9.62  ? 209 VAL B CG1 1 
ATOM   1654 C  CG2 . VAL A 1 209 ? 23.394  6.069   -21.352 1.00 8.93  ? 209 VAL B CG2 1 
ATOM   1655 N  N   . THR A 1 210 ? 23.088  10.416  -23.281 1.00 9.28  ? 210 THR B N   1 
ATOM   1656 C  CA  . THR A 1 210 ? 22.999  11.842  -22.949 1.00 8.27  ? 210 THR B CA  1 
ATOM   1657 C  C   . THR A 1 210 ? 22.330  11.984  -21.572 1.00 9.02  ? 210 THR B C   1 
ATOM   1658 O  O   . THR A 1 210 ? 21.150  11.634  -21.406 1.00 9.11  ? 210 THR B O   1 
ATOM   1659 C  CB  . THR A 1 210 ? 22.206  12.597  -24.019 1.00 10.20 ? 210 THR B CB  1 
ATOM   1660 O  OG1 . THR A 1 210 ? 22.820  12.373  -25.318 1.00 9.40  ? 210 THR B OG1 1 
ATOM   1661 C  CG2 . THR A 1 210 ? 22.294  14.098  -23.738 1.00 9.05  ? 210 THR B CG2 1 
ATOM   1662 N  N   . TRP A 1 211 ? 23.150  12.294  -20.566 1.00 7.59  ? 211 TRP B N   1 
ATOM   1663 C  CA  . TRP A 1 211 ? 22.604  12.511  -19.227 1.00 7.67  ? 211 TRP B CA  1 
ATOM   1664 C  C   . TRP A 1 211 ? 21.977  13.878  -19.101 1.00 7.88  ? 211 TRP B C   1 
ATOM   1665 O  O   . TRP A 1 211 ? 22.540  14.886  -19.527 1.00 7.42  ? 211 TRP B O   1 
ATOM   1666 C  CB  . TRP A 1 211 ? 23.735  12.403  -18.194 1.00 7.59  ? 211 TRP B CB  1 
ATOM   1667 C  CG  . TRP A 1 211 ? 23.953  10.934  -17.950 1.00 8.02  ? 211 TRP B CG  1 
ATOM   1668 C  CD1 . TRP A 1 211 ? 24.885  10.101  -18.507 1.00 7.77  ? 211 TRP B CD1 1 
ATOM   1669 C  CD2 . TRP A 1 211 ? 23.175  10.147  -17.054 1.00 8.12  ? 211 TRP B CD2 1 
ATOM   1670 N  NE1 . TRP A 1 211 ? 24.705  8.811   -18.028 1.00 7.46  ? 211 TRP B NE1 1 
ATOM   1671 C  CE2 . TRP A 1 211 ? 23.673  8.832   -17.104 1.00 7.94  ? 211 TRP B CE2 1 
ATOM   1672 C  CE3 . TRP A 1 211 ? 22.091  10.458  -16.185 1.00 8.18  ? 211 TRP B CE3 1 
ATOM   1673 C  CZ2 . TRP A 1 211 ? 23.118  7.793   -16.364 1.00 8.67  ? 211 TRP B CZ2 1 
ATOM   1674 C  CZ3 . TRP A 1 211 ? 21.555  9.409   -15.393 1.00 9.21  ? 211 TRP B CZ3 1 
ATOM   1675 C  CH2 . TRP A 1 211 ? 22.055  8.092   -15.517 1.00 8.63  ? 211 TRP B CH2 1 
ATOM   1676 N  N   . ILE A 1 212 ? 20.805  13.878  -18.455 1.00 7.76  ? 212 ILE B N   1 
ATOM   1677 C  CA  . ILE A 1 212 ? 20.045  15.118  -18.188 1.00 7.98  ? 212 ILE B CA  1 
ATOM   1678 C  C   . ILE A 1 212 ? 19.711  14.951  -16.711 1.00 9.00  ? 212 ILE B C   1 
ATOM   1679 O  O   . ILE A 1 212 ? 18.829  14.173  -16.382 1.00 9.39  ? 212 ILE B O   1 
ATOM   1680 C  CB  . ILE A 1 212 ? 18.765  15.168  -19.042 1.00 7.90  ? 212 ILE B CB  1 
ATOM   1681 C  CG1 . ILE A 1 212 ? 19.172  15.157  -20.510 1.00 8.67  ? 212 ILE B CG1 1 
ATOM   1682 C  CG2 . ILE A 1 212 ? 17.910  16.418  -18.628 1.00 8.10  ? 212 ILE B CG2 1 
ATOM   1683 C  CD1 . ILE A 1 212 ? 17.991  14.979  -21.478 1.00 8.63  ? 212 ILE B CD1 1 
ATOM   1684 N  N   . VAL A 1 213 ? 20.460  15.635  -15.827 1.00 8.66  ? 213 VAL B N   1 
ATOM   1685 C  CA  . VAL A 1 213 ? 20.252  15.528  -14.377 1.00 9.33  ? 213 VAL B CA  1 
ATOM   1686 C  C   . VAL A 1 213 ? 19.527  16.756  -13.889 1.00 9.00  ? 213 VAL B C   1 
ATOM   1687 O  O   . VAL A 1 213 ? 20.045  17.869  -14.007 1.00 9.64  ? 213 VAL B O   1 
ATOM   1688 C  CB  . VAL A 1 213 ? 21.632  15.411  -13.676 1.00 9.47  ? 213 VAL B CB  1 
ATOM   1689 C  CG1 . VAL A 1 213 ? 21.440  15.315  -12.141 1.00 9.22  ? 213 VAL B CG1 1 
ATOM   1690 C  CG2 . VAL A 1 213 ? 22.323  14.136  -14.199 1.00 10.61 ? 213 VAL B CG2 1 
ATOM   1691 N  N   . LEU A 1 214 ? 18.343  16.557  -13.313 1.00 9.33  ? 214 LEU B N   1 
ATOM   1692 C  CA  . LEU A 1 214 ? 17.579  17.694  -12.796 1.00 9.68  ? 214 LEU B CA  1 
ATOM   1693 C  C   . LEU A 1 214 ? 18.194  18.279  -11.534 1.00 10.61 ? 214 LEU B C   1 
ATOM   1694 O  O   . LEU A 1 214 ? 18.631  17.555  -10.609 1.00 10.67 ? 214 LEU B O   1 
ATOM   1695 C  CB  . LEU A 1 214 ? 16.100  17.302  -12.471 1.00 9.90  ? 214 LEU B CB  1 
ATOM   1696 C  CG  . LEU A 1 214 ? 15.347  16.764  -13.672 1.00 10.89 ? 214 LEU B CG  1 
ATOM   1697 C  CD1 . LEU A 1 214 ? 13.857  16.641  -13.311 1.00 11.06 ? 214 LEU B CD1 1 
ATOM   1698 C  CD2 . LEU A 1 214 ? 15.493  17.763  -14.849 1.00 9.74  ? 214 LEU B CD2 1 
ATOM   1699 N  N   . LYS A 1 215 ? 18.277  19.608  -11.524 1.00 10.93 ? 215 LYS B N   1 
ATOM   1700 C  CA  . LYS A 1 215 ? 18.766  20.253  -10.303 1.00 11.76 ? 215 LYS B CA  1 
ATOM   1701 C  C   . LYS A 1 215 ? 17.911  19.999  -9.035  1.00 12.20 ? 215 LYS B C   1 
ATOM   1702 O  O   . LYS A 1 215 ? 18.461  19.788  -7.923  1.00 11.82 ? 215 LYS B O   1 
ATOM   1703 C  CB  . LYS A 1 215 ? 18.964  21.736  -10.524 1.00 14.23 ? 215 LYS B CB  1 
ATOM   1704 C  CG  . LYS A 1 215 ? 19.403  22.446  -9.212  1.00 16.11 ? 215 LYS B CG  1 
ATOM   1705 C  CD  . LYS A 1 215 ? 19.843  23.880  -9.519  1.00 19.89 ? 215 LYS B CD  1 
ATOM   1706 C  CE  . LYS A 1 215 ? 19.883  24.713  -8.226  1.00 23.96 ? 215 LYS B CE  1 
ATOM   1707 N  NZ  . LYS A 1 215 ? 20.561  26.036  -8.435  1.00 27.33 ? 215 LYS B NZ  1 
ATOM   1708 N  N   . GLN A 1 216 ? 16.614  20.083  -9.191  1.00 10.70 ? 216 GLN B N   1 
ATOM   1709 C  CA  . GLN A 1 216 ? 15.724  20.049  -7.976  1.00 11.43 ? 216 GLN B CA  1 
ATOM   1710 C  C   . GLN A 1 216 ? 15.440  18.601  -7.512  1.00 10.35 ? 216 GLN B C   1 
ATOM   1711 O  O   . GLN A 1 216 ? 14.871  17.810  -8.268  1.00 10.29 ? 216 GLN B O   1 
ATOM   1712 C  CB  . GLN A 1 216 ? 14.385  20.685  -8.315  1.00 11.85 ? 216 GLN B CB  1 
ATOM   1713 C  CG  . GLN A 1 216 ? 13.514  20.729  -7.026  1.00 13.57 ? 216 GLN B CG  1 
ATOM   1714 C  CD  . GLN A 1 216 ? 12.337  21.686  -7.137  1.00 16.16 ? 216 GLN B CD  1 
ATOM   1715 O  OE1 . GLN A 1 216 ? 11.810  22.108  -6.097  1.00 19.41 ? 216 GLN B OE1 1 
ATOM   1716 N  NE2 . GLN A 1 216 ? 11.834  21.902  -8.325  1.00 14.46 ? 216 GLN B NE2 1 
ATOM   1717 N  N   . PRO A 1 217 ? 15.802  18.260  -6.265  1.00 10.46 ? 217 PRO B N   1 
ATOM   1718 C  CA  . PRO A 1 217 ? 15.401  16.956  -5.719  1.00 10.17 ? 217 PRO B CA  1 
ATOM   1719 C  C   . PRO A 1 217 ? 13.911  16.873  -5.377  1.00 10.05 ? 217 PRO B C   1 
ATOM   1720 O  O   . PRO A 1 217 ? 13.236  17.906  -5.295  1.00 10.37 ? 217 PRO B O   1 
ATOM   1721 C  CB  . PRO A 1 217 ? 16.251  16.811  -4.449  1.00 11.39 ? 217 PRO B CB  1 
ATOM   1722 C  CG  . PRO A 1 217 ? 17.244  17.942  -4.533  1.00 13.21 ? 217 PRO B CG  1 
ATOM   1723 C  CD  . PRO A 1 217 ? 16.575  19.027  -5.295  1.00 10.51 ? 217 PRO B CD  1 
ATOM   1724 N  N   . ILE A 1 218 ? 13.414  15.646  -5.327  1.00 8.90  ? 218 ILE B N   1 
ATOM   1725 C  CA  . ILE A 1 218 ? 12.099  15.305  -4.731  1.00 8.88  ? 218 ILE B CA  1 
ATOM   1726 C  C   . ILE A 1 218 ? 12.369  14.660  -3.358  1.00 9.38  ? 218 ILE B C   1 
ATOM   1727 O  O   . ILE A 1 218 ? 13.501  14.174  -3.031  1.00 9.61  ? 218 ILE B O   1 
ATOM   1728 C  CB  . ILE A 1 218 ? 11.278  14.344  -5.613  1.00 8.60  ? 218 ILE B CB  1 
ATOM   1729 C  CG1 . ILE A 1 218 ? 11.968  12.975  -5.827  1.00 9.82  ? 218 ILE B CG1 1 
ATOM   1730 C  CG2 . ILE A 1 218 ? 11.110  14.947  -7.038  1.00 10.57 ? 218 ILE B CG2 1 
ATOM   1731 C  CD1 . ILE A 1 218 ? 11.150  11.939  -6.575  1.00 9.71  ? 218 ILE B CD1 1 
ATOM   1732 N  N   . ASN A 1 219 ? 11.316  14.664  -2.555  1.00 9.64  ? 219 ASN B N   1 
ATOM   1733 C  CA  . ASN A 1 219 ? 11.469  14.145  -1.215  1.00 10.52 ? 219 ASN B CA  1 
ATOM   1734 C  C   . ASN A 1 219 ? 11.098  12.654  -1.117  1.00 9.68  ? 219 ASN B C   1 
ATOM   1735 O  O   . ASN A 1 219 ? 10.389  12.093  -1.973  1.00 10.05 ? 219 ASN B O   1 
ATOM   1736 C  CB  . ASN A 1 219 ? 10.600  14.926  -0.225  1.00 12.78 ? 219 ASN B CB  1 
ATOM   1737 C  CG  . ASN A 1 219 ? 9.158   15.053  -0.689  1.00 16.57 ? 219 ASN B CG  1 
ATOM   1738 O  OD1 . ASN A 1 219 ? 8.836   15.693  -1.762  1.00 19.73 ? 219 ASN B OD1 1 
ATOM   1739 N  ND2 . ASN A 1 219 ? 8.229   14.466  0.095   1.00 15.82 ? 219 ASN B ND2 1 
ATOM   1740 N  N   . ILE A 1 220 ? 11.659  12.038  -0.087  1.00 9.12  ? 220 ILE B N   1 
ATOM   1741 C  CA  . ILE A 1 220 ? 11.317  10.663  0.297   1.00 10.54 ? 220 ILE B CA  1 
ATOM   1742 C  C   . ILE A 1 220 ? 11.545  10.579  1.818   1.00 10.71 ? 220 ILE B C   1 
ATOM   1743 O  O   . ILE A 1 220 ? 12.471  11.207  2.364   1.00 11.67 ? 220 ILE B O   1 
ATOM   1744 C  CB  . ILE A 1 220 ? 12.224  9.638   -0.431  1.00 10.83 ? 220 ILE B CB  1 
ATOM   1745 C  CG1 . ILE A 1 220 ? 11.731  8.226   -0.128  1.00 10.77 ? 220 ILE B CG1 1 
ATOM   1746 C  CG2 . ILE A 1 220 ? 13.735  9.827   -0.083  1.00 10.17 ? 220 ILE B CG2 1 
ATOM   1747 C  CD1 . ILE A 1 220 ? 12.321  7.144   -1.064  1.00 10.41 ? 220 ILE B CD1 1 
ATOM   1748 N  N   . SER A 1 221 ? 10.692  9.840   2.532   1.00 9.76  ? 221 SER B N   1 
ATOM   1749 C  CA  . SER A 1 221 ? 11.052  9.649   3.950   1.00 11.08 ? 221 SER B CA  1 
ATOM   1750 C  C   . SER A 1 221 ? 12.106  8.549   4.151   1.00 10.62 ? 221 SER B C   1 
ATOM   1751 O  O   . SER A 1 221 ? 12.309  7.670   3.260   1.00 10.20 ? 221 SER B O   1 
ATOM   1752 C  CB  . SER A 1 221 ? 9.808   9.326   4.803   1.00 10.80 ? 221 SER B CB  1 
ATOM   1753 O  OG  . SER A 1 221 ? 9.409   7.982   4.534   1.00 11.40 ? 221 SER B OG  1 
ATOM   1754 N  N   . SER A 1 222 ? 12.798  8.609   5.310   1.00 11.83 ? 222 SER B N   1 
ATOM   1755 C  CA  . SER A 1 222 ? 13.780  7.561   5.611   1.00 12.75 ? 222 SER B CA  1 
ATOM   1756 C  C   . SER A 1 222 ? 13.109  6.178   5.592   1.00 11.91 ? 222 SER B C   1 
ATOM   1757 O  O   . SER A 1 222 ? 13.696  5.185   5.093   1.00 10.67 ? 222 SER B O   1 
ATOM   1758 C  CB  . SER A 1 222 ? 14.414  7.827   6.990   1.00 15.05 ? 222 SER B CB  1 
ATOM   1759 O  OG  . SER A 1 222 ? 15.411  6.858   7.145   1.00 22.56 ? 222 SER B OG  1 
ATOM   1760 N  N   . GLN A 1 223 ? 11.859  6.088   6.086   1.00 12.36 ? 223 GLN B N   1 
ATOM   1761 C  CA  . GLN A 1 223 ? 11.170  4.782   6.164   1.00 11.96 ? 223 GLN B CA  1 
ATOM   1762 C  C   . GLN A 1 223 ? 10.754  4.268   4.765   1.00 11.84 ? 223 GLN B C   1 
ATOM   1763 O  O   . GLN A 1 223 ? 10.863  3.066   4.485   1.00 11.43 ? 223 GLN B O   1 
ATOM   1764 C  CB  . GLN A 1 223 ? 9.956   4.837   7.126   1.00 13.38 ? 223 GLN B CB  1 
ATOM   1765 C  CG  . GLN A 1 223 ? 10.453  5.107   8.545   1.00 15.01 ? 223 GLN B CG  1 
ATOM   1766 C  CD  . GLN A 1 223 ? 10.473  6.577   8.977   1.00 18.30 ? 223 GLN B CD  1 
ATOM   1767 O  OE1 . GLN A 1 223 ? 10.534  6.864   10.193  1.00 21.51 ? 223 GLN B OE1 1 
ATOM   1768 N  NE2 . GLN A 1 223 ? 10.353  7.501   8.033   1.00 14.15 ? 223 GLN B NE2 1 
ATOM   1769 N  N   . GLN A 1 224 ? 10.431  5.201   3.856   1.00 10.47 ? 224 GLN B N   1 
ATOM   1770 C  CA  . GLN A 1 224 ? 10.153  4.813   2.503   1.00 11.47 ? 224 GLN B CA  1 
ATOM   1771 C  C   . GLN A 1 224 ? 11.422  4.270   1.859   1.00 11.22 ? 224 GLN B C   1 
ATOM   1772 O  O   . GLN A 1 224 ? 11.381  3.212   1.176   1.00 9.88  ? 224 GLN B O   1 
ATOM   1773 C  CB  . GLN A 1 224 ? 9.617   6.003   1.661   1.00 11.32 ? 224 GLN B CB  1 
ATOM   1774 C  CG  . GLN A 1 224 ? 8.142   6.305   1.939   1.00 11.21 ? 224 GLN B CG  1 
ATOM   1775 C  CD  . GLN A 1 224 ? 7.683   7.482   1.109   1.00 11.48 ? 224 GLN B CD  1 
ATOM   1776 O  OE1 . GLN A 1 224 ? 8.314   8.589   1.127   1.00 11.36 ? 224 GLN B OE1 1 
ATOM   1777 N  NE2 . GLN A 1 224 ? 6.536   7.287   0.403   1.00 10.99 ? 224 GLN B NE2 1 
ATOM   1778 N  N   . LEU A 1 225 ? 12.511  5.027   2.011   1.00 11.16 ? 225 LEU B N   1 
ATOM   1779 C  CA  . LEU A 1 225 ? 13.773  4.626   1.355   1.00 10.40 ? 225 LEU B CA  1 
ATOM   1780 C  C   . LEU A 1 225 ? 14.238  3.231   1.889   1.00 11.88 ? 225 LEU B C   1 
ATOM   1781 O  O   . LEU A 1 225 ? 14.744  2.411   1.122   1.00 11.28 ? 225 LEU B O   1 
ATOM   1782 C  CB  . LEU A 1 225 ? 14.857  5.704   1.538   1.00 9.29  ? 225 LEU B CB  1 
ATOM   1783 C  CG  . LEU A 1 225 ? 16.183  5.310   0.894   1.00 9.96  ? 225 LEU B CG  1 
ATOM   1784 C  CD1 . LEU A 1 225 ? 15.987  5.138   -0.596  1.00 10.44 ? 225 LEU B CD1 1 
ATOM   1785 C  CD2 . LEU A 1 225 ? 17.141  6.448   1.111   1.00 9.97  ? 225 LEU B CD2 1 
ATOM   1786 N  N   . ALA A 1 226 ? 14.091  2.967   3.202   1.00 10.42 ? 226 ALA B N   1 
ATOM   1787 C  CA  . ALA A 1 226 ? 14.557  1.721   3.772   1.00 12.41 ? 226 ALA B CA  1 
ATOM   1788 C  C   . ALA A 1 226 ? 13.892  0.493   3.173   1.00 12.39 ? 226 ALA B C   1 
ATOM   1789 O  O   . ALA A 1 226 ? 14.493  -0.575  3.155   1.00 12.55 ? 226 ALA B O   1 
ATOM   1790 C  CB  . ALA A 1 226 ? 14.419  1.758   5.327   1.00 12.77 ? 226 ALA B CB  1 
ATOM   1791 N  N   . LYS A 1 227 ? 12.629  0.632   2.707   1.00 11.81 ? 227 LYS B N   1 
ATOM   1792 C  CA  . LYS A 1 227 ? 11.968  -0.462  2.044   1.00 12.01 ? 227 LYS B CA  1 
ATOM   1793 C  C   . LYS A 1 227 ? 12.751  -1.024  0.848   1.00 12.20 ? 227 LYS B C   1 
ATOM   1794 O  O   . LYS A 1 227 ? 12.689  -2.255  0.644   1.00 11.93 ? 227 LYS B O   1 
ATOM   1795 C  CB  . LYS A 1 227 ? 10.536  -0.075  1.624   1.00 14.32 ? 227 LYS B CB  1 
ATOM   1796 C  CG  . LYS A 1 227 ? 9.593   -0.042  2.838   1.00 18.19 ? 227 LYS B CG  1 
ATOM   1797 C  CD  . LYS A 1 227 ? 8.092   -0.067  2.509   1.00 24.57 ? 227 LYS B CD  1 
ATOM   1798 C  CE  . LYS A 1 227 ? 7.591   -1.296  1.707   1.00 26.18 ? 227 LYS B CE  1 
ATOM   1799 N  NZ  . LYS A 1 227 ? 7.949   -2.688  2.174   1.00 30.57 ? 227 LYS B NZ  1 
ATOM   1800 N  N   . PHE A 1 228 ? 13.437  -0.145  0.096   1.00 10.80 ? 228 PHE B N   1 
ATOM   1801 C  CA  . PHE A 1 228 ? 14.167  -0.607  -1.083  1.00 10.49 ? 228 PHE B CA  1 
ATOM   1802 C  C   . PHE A 1 228 ? 15.301  -1.549  -0.729  1.00 10.98 ? 228 PHE B C   1 
ATOM   1803 O  O   . PHE A 1 228 ? 15.590  -2.474  -1.482  1.00 10.97 ? 228 PHE B O   1 
ATOM   1804 C  CB  . PHE A 1 228 ? 14.660  0.555   -1.941  1.00 9.96  ? 228 PHE B CB  1 
ATOM   1805 C  CG  . PHE A 1 228 ? 13.517  1.302   -2.524  1.00 11.47 ? 228 PHE B CG  1 
ATOM   1806 C  CD1 . PHE A 1 228 ? 12.836  0.786   -3.651  1.00 10.57 ? 228 PHE B CD1 1 
ATOM   1807 C  CD2 . PHE A 1 228 ? 13.086  2.498   -1.938  1.00 10.75 ? 228 PHE B CD2 1 
ATOM   1808 C  CE1 . PHE A 1 228 ? 11.768  1.472   -4.155  1.00 11.53 ? 228 PHE B CE1 1 
ATOM   1809 C  CE2 . PHE A 1 228 ? 11.975  3.169   -2.428  1.00 11.28 ? 228 PHE B CE2 1 
ATOM   1810 C  CZ  . PHE A 1 228 ? 11.301  2.634   -3.521  1.00 11.64 ? 228 PHE B CZ  1 
ATOM   1811 N  N   . ARG A 1 229 ? 15.916  -1.332  0.437   1.00 10.42 ? 229 ARG B N   1 
ATOM   1812 C  CA  . ARG A 1 229 ? 17.030  -2.182  0.891   1.00 11.22 ? 229 ARG B CA  1 
ATOM   1813 C  C   . ARG A 1 229 ? 16.589  -3.597  1.223   1.00 12.94 ? 229 ARG B C   1 
ATOM   1814 O  O   . ARG A 1 229 ? 17.469  -4.431  1.392   1.00 13.68 ? 229 ARG B O   1 
ATOM   1815 C  CB  . ARG A 1 229 ? 17.775  -1.583  2.052   1.00 10.95 ? 229 ARG B CB  1 
ATOM   1816 C  CG  . ARG A 1 229 ? 18.274  -0.196  1.745   1.00 10.71 ? 229 ARG B CG  1 
ATOM   1817 C  CD  . ARG A 1 229 ? 19.305  0.284   2.786   1.00 10.40 ? 229 ARG B CD  1 
ATOM   1818 N  NE  . ARG A 1 229 ? 19.592  1.713   2.556   1.00 8.73  ? 229 ARG B NE  1 
ATOM   1819 C  CZ  . ARG A 1 229 ? 18.954  2.778   3.059   1.00 8.58  ? 229 ARG B CZ  1 
ATOM   1820 N  NH1 . ARG A 1 229 ? 17.948  2.673   3.927   1.00 9.30  ? 229 ARG B NH1 1 
ATOM   1821 N  NH2 . ARG A 1 229 ? 19.358  3.990   2.679   1.00 8.11  ? 229 ARG B NH2 1 
ATOM   1822 N  N   . SER A 1 230 ? 15.275  -3.824  1.468   1.00 13.67 ? 230 SER B N   1 
ATOM   1823 C  CA  . SER A 1 230 ? 14.781  -5.203  1.662   1.00 15.05 ? 230 SER B CA  1 
ATOM   1824 C  C   . SER A 1 230 ? 14.670  -6.014  0.413   1.00 14.39 ? 230 SER B C   1 
ATOM   1825 O  O   . SER A 1 230 ? 14.503  -7.199  0.521   1.00 15.13 ? 230 SER B O   1 
ATOM   1826 C  CB  . SER A 1 230 ? 13.429  -5.233  2.395   1.00 18.40 ? 230 SER B CB  1 
ATOM   1827 O  OG  . SER A 1 230 ? 13.711  -4.932  3.748   1.00 27.18 ? 230 SER B OG  1 
ATOM   1828 N  N   . LEU A 1 231 ? 14.876  -5.429  -0.775  1.00 12.95 ? 231 LEU B N   1 
ATOM   1829 C  CA  . LEU A 1 231 ? 14.934  -6.226  -1.973  1.00 11.91 ? 231 LEU B CA  1 
ATOM   1830 C  C   . LEU A 1 231 ? 16.161  -7.132  -1.956  1.00 12.78 ? 231 LEU B C   1 
ATOM   1831 O  O   . LEU A 1 231 ? 17.209  -6.713  -1.460  1.00 12.77 ? 231 LEU B O   1 
ATOM   1832 C  CB  . LEU A 1 231 ? 14.954  -5.282  -3.216  1.00 11.80 ? 231 LEU B CB  1 
ATOM   1833 C  CG  . LEU A 1 231 ? 13.632  -4.523  -3.503  1.00 11.29 ? 231 LEU B CG  1 
ATOM   1834 C  CD1 . LEU A 1 231 ? 14.006  -3.588  -4.653  1.00 11.59 ? 231 LEU B CD1 1 
ATOM   1835 C  CD2 . LEU A 1 231 ? 12.423  -5.436  -3.793  1.00 11.99 ? 231 LEU B CD2 1 
ATOM   1836 N  N   . LEU A 1 232 ? 16.067  -8.362  -2.477  1.00 12.24 ? 232 LEU B N   1 
ATOM   1837 C  CA  . LEU A 1 232 ? 17.251  -9.205  -2.609  1.00 12.81 ? 232 LEU B CA  1 
ATOM   1838 C  C   . LEU A 1 232 ? 17.975  -9.059  -3.921  1.00 12.83 ? 232 LEU B C   1 
ATOM   1839 O  O   . LEU A 1 232 ? 17.326  -8.827  -4.973  1.00 13.95 ? 232 LEU B O   1 
ATOM   1840 C  CB  . LEU A 1 232 ? 16.881  -10.709 -2.442  1.00 12.35 ? 232 LEU B CB  1 
ATOM   1841 C  CG  . LEU A 1 232 ? 16.122  -10.999 -1.144  1.00 14.91 ? 232 LEU B CG  1 
ATOM   1842 C  CD1 . LEU A 1 232 ? 15.648  -12.447 -1.001  1.00 14.12 ? 232 LEU B CD1 1 
ATOM   1843 C  CD2 . LEU A 1 232 ? 16.919  -10.578 0.088   1.00 16.89 ? 232 LEU B CD2 1 
ATOM   1844 N  N   . CYS A 1 233 ? 19.297  -9.279  -3.930  1.00 13.46 ? 233 CYS B N   1 
ATOM   1845 C  CA  . CYS A 1 233 ? 20.012  -9.420  -5.232  1.00 13.19 ? 233 CYS B CA  1 
ATOM   1846 C  C   . CYS A 1 233 ? 20.109  -10.922 -5.619  1.00 16.28 ? 233 CYS B C   1 
ATOM   1847 O  O   . CYS A 1 233 ? 20.847  -11.280 -6.560  1.00 15.04 ? 233 CYS B O   1 
ATOM   1848 C  CB  . CYS A 1 233 ? 21.413  -8.854  -5.164  1.00 13.97 ? 233 CYS B CB  1 
ATOM   1849 S  SG  . CYS A 1 233 ? 22.473  -9.615  -3.878  1.00 17.40 ? 233 CYS B SG  1 
ATOM   1850 N  N   . THR A 1 234 ? 19.302  -11.728 -4.936  1.00 16.34 ? 234 THR B N   1 
ATOM   1851 C  CA  . THR A 1 234 ? 19.322  -13.196 -5.091  1.00 16.30 ? 234 THR B CA  1 
ATOM   1852 C  C   . THR A 1 234 ? 17.898  -13.703 -5.386  1.00 17.47 ? 234 THR B C   1 
ATOM   1853 O  O   . THR A 1 234 ? 16.883  -13.124 -4.956  1.00 17.05 ? 234 THR B O   1 
ATOM   1854 C  CB  . THR A 1 234 ? 19.890  -13.893 -3.833  1.00 18.02 ? 234 THR B CB  1 
ATOM   1855 O  OG1 . THR A 1 234 ? 19.163  -13.465 -2.680  1.00 18.07 ? 234 THR B OG1 1 
ATOM   1856 C  CG2 . THR A 1 234 ? 21.338  -13.642 -3.667  1.00 17.53 ? 234 THR B CG2 1 
ATOM   1857 N  N   . ALA A 1 235 ? 17.850  -14.791 -6.142  1.00 19.48 ? 235 ALA B N   1 
ATOM   1858 C  CA  . ALA A 1 235 ? 16.620  -15.374 -6.662  1.00 20.66 ? 235 ALA B CA  1 
ATOM   1859 C  C   . ALA A 1 235 ? 16.101  -16.398 -5.655  1.00 24.29 ? 235 ALA B C   1 
ATOM   1860 O  O   . ALA A 1 235 ? 16.785  -16.719 -4.647  1.00 21.97 ? 235 ALA B O   1 
ATOM   1861 C  CB  . ALA A 1 235 ? 16.900  -16.037 -8.018  1.00 21.85 ? 235 ALA B CB  1 
ATOM   1862 N  N   . GLU A 1 236 ? 14.872  -16.858 -5.911  1.00 26.36 ? 236 GLU B N   1 
ATOM   1863 C  CA  . GLU A 1 236 ? 14.221  -17.891 -5.099  1.00 33.22 ? 236 GLU B CA  1 
ATOM   1864 C  C   . GLU A 1 236 ? 15.145  -19.129 -5.102  1.00 29.98 ? 236 GLU B C   1 
ATOM   1865 O  O   . GLU A 1 236 ? 15.734  -19.469 -6.139  1.00 27.01 ? 236 GLU B O   1 
ATOM   1866 C  CB  . GLU A 1 236 ? 12.816  -18.183 -5.674  1.00 39.35 ? 236 GLU B CB  1 
ATOM   1867 C  CG  . GLU A 1 236 ? 12.035  -19.332 -5.030  1.00 47.69 ? 236 GLU B CG  1 
ATOM   1868 C  CD  . GLU A 1 236 ? 11.454  -19.010 -3.654  1.00 48.50 ? 236 GLU B CD  1 
ATOM   1869 O  OE1 . GLU A 1 236 ? 11.471  -19.903 -2.779  1.00 54.75 ? 236 GLU B OE1 1 
ATOM   1870 O  OE2 . GLU A 1 236 ? 10.968  -17.881 -3.442  1.00 57.54 ? 236 GLU B OE2 1 
ATOM   1871 N  N   . GLY A 1 237 ? 15.342  -19.689 -3.912  1.00 32.23 ? 237 GLY B N   1 
ATOM   1872 C  CA  . GLY A 1 237 ? 16.266  -20.821 -3.645  1.00 36.81 ? 237 GLY B CA  1 
ATOM   1873 C  C   . GLY A 1 237 ? 17.779  -20.589 -3.778  1.00 39.97 ? 237 GLY B C   1 
ATOM   1874 O  O   . GLY A 1 237 ? 18.539  -21.555 -3.875  1.00 43.96 ? 237 GLY B O   1 
ATOM   1875 N  N   . GLU A 1 238 ? 18.214  -19.323 -3.823  1.00 37.84 ? 238 GLU B N   1 
ATOM   1876 C  CA  . GLU A 1 238 ? 19.627  -18.924 -3.776  1.00 34.41 ? 238 GLU B CA  1 
ATOM   1877 C  C   . GLU A 1 238 ? 19.801  -18.353 -2.352  1.00 33.85 ? 238 GLU B C   1 
ATOM   1878 O  O   . GLU A 1 238 ? 18.861  -17.785 -1.830  1.00 32.83 ? 238 GLU B O   1 
ATOM   1879 C  CB  . GLU A 1 238 ? 19.878  -17.864 -4.863  1.00 37.89 ? 238 GLU B CB  1 
ATOM   1880 C  CG  . GLU A 1 238 ? 21.325  -17.519 -5.194  1.00 38.24 ? 238 GLU B CG  1 
ATOM   1881 C  CD  . GLU A 1 238 ? 21.488  -16.365 -6.204  1.00 42.74 ? 238 GLU B CD  1 
ATOM   1882 O  OE1 . GLU A 1 238 ? 22.603  -15.810 -6.273  1.00 38.50 ? 238 GLU B OE1 1 
ATOM   1883 O  OE2 . GLU A 1 238 ? 20.537  -15.988 -6.946  1.00 39.99 ? 238 GLU B OE2 1 
ATOM   1884 N  N   . ALA A 1 239 ? 20.951  -18.527 -1.698  1.00 29.89 ? 239 ALA B N   1 
ATOM   1885 C  CA  . ALA A 1 239 ? 21.176  -18.013 -0.321  1.00 29.28 ? 239 ALA B CA  1 
ATOM   1886 C  C   . ALA A 1 239 ? 20.997  -16.471 -0.290  1.00 24.70 ? 239 ALA B C   1 
ATOM   1887 O  O   . ALA A 1 239 ? 21.650  -15.804 -1.089  1.00 26.67 ? 239 ALA B O   1 
ATOM   1888 C  CB  . ALA A 1 239 ? 22.576  -18.371 0.143   1.00 32.63 ? 239 ALA B CB  1 
ATOM   1889 N  N   . ALA A 1 240 ? 20.133  -15.956 0.595   1.00 23.35 ? 240 ALA B N   1 
ATOM   1890 C  CA  . ALA A 1 240 ? 19.655  -14.545 0.526   1.00 19.78 ? 240 ALA B CA  1 
ATOM   1891 C  C   . ALA A 1 240 ? 20.790  -13.535 0.738   1.00 19.61 ? 240 ALA B C   1 
ATOM   1892 O  O   . ALA A 1 240 ? 21.649  -13.672 1.636   1.00 21.25 ? 240 ALA B O   1 
ATOM   1893 C  CB  . ALA A 1 240 ? 18.544  -14.281 1.526   1.00 19.54 ? 240 ALA B CB  1 
ATOM   1894 N  N   . ALA A 1 241 ? 20.788  -12.498 -0.078  1.00 17.19 ? 241 ALA B N   1 
ATOM   1895 C  CA  . ALA A 1 241 ? 21.689  -11.378 0.159   1.00 14.64 ? 241 ALA B CA  1 
ATOM   1896 C  C   . ALA A 1 241 ? 20.825  -10.181 -0.239  1.00 14.32 ? 241 ALA B C   1 
ATOM   1897 O  O   . ALA A 1 241 ? 20.157  -10.236 -1.263  1.00 12.77 ? 241 ALA B O   1 
ATOM   1898 C  CB  . ALA A 1 241 ? 22.959  -11.468 -0.688  1.00 13.86 ? 241 ALA B CB  1 
ATOM   1899 N  N   . PHE A 1 242 ? 20.918  -9.117  0.565   1.00 14.56 ? 242 PHE B N   1 
ATOM   1900 C  CA  . PHE A 1 242 ? 20.132  -7.900  0.372   1.00 13.74 ? 242 PHE B CA  1 
ATOM   1901 C  C   . PHE A 1 242 ? 20.818  -6.832  -0.482  1.00 12.91 ? 242 PHE B C   1 
ATOM   1902 O  O   . PHE A 1 242 ? 22.030  -6.591  -0.380  1.00 13.89 ? 242 PHE B O   1 
ATOM   1903 C  CB  . PHE A 1 242 ? 19.819  -7.291  1.746   1.00 13.51 ? 242 PHE B CB  1 
ATOM   1904 C  CG  . PHE A 1 242 ? 18.928  -8.136  2.593   1.00 15.56 ? 242 PHE B CG  1 
ATOM   1905 C  CD1 . PHE A 1 242 ? 19.486  -9.067  3.489   1.00 16.67 ? 242 PHE B CD1 1 
ATOM   1906 C  CD2 . PHE A 1 242 ? 17.519  -7.999  2.551   1.00 16.77 ? 242 PHE B CD2 1 
ATOM   1907 C  CE1 . PHE A 1 242 ? 18.648  -9.872  4.295   1.00 18.14 ? 242 PHE B CE1 1 
ATOM   1908 C  CE2 . PHE A 1 242 ? 16.698  -8.775  3.388   1.00 18.30 ? 242 PHE B CE2 1 
ATOM   1909 C  CZ  . PHE A 1 242 ? 17.258  -9.733  4.230   1.00 19.41 ? 242 PHE B CZ  1 
ATOM   1910 N  N   . LEU A 1 243 ? 20.006  -6.117  -1.262  1.00 11.92 ? 243 LEU B N   1 
ATOM   1911 C  CA  . LEU A 1 243 ? 20.507  -5.029  -2.094  1.00 12.85 ? 243 LEU B CA  1 
ATOM   1912 C  C   . LEU A 1 243 ? 20.516  -3.731  -1.238  1.00 11.19 ? 243 LEU B C   1 
ATOM   1913 O  O   . LEU A 1 243 ? 19.672  -2.818  -1.338  1.00 11.65 ? 243 LEU B O   1 
ATOM   1914 C  CB  . LEU A 1 243 ? 19.565  -4.948  -3.315  1.00 13.60 ? 243 LEU B CB  1 
ATOM   1915 C  CG  . LEU A 1 243 ? 19.996  -4.122  -4.481  1.00 14.72 ? 243 LEU B CG  1 
ATOM   1916 C  CD1 . LEU A 1 243 ? 21.212  -4.718  -5.136  1.00 16.07 ? 243 LEU B CD1 1 
ATOM   1917 C  CD2 . LEU A 1 243 ? 18.775  -4.015  -5.411  1.00 14.43 ? 243 LEU B CD2 1 
ATOM   1918 N  N   . VAL A 1 244 ? 21.442  -3.691  -0.287  1.00 11.15 ? 244 VAL B N   1 
ATOM   1919 C  CA  . VAL A 1 244 ? 21.479  -2.538  0.612   1.00 11.69 ? 244 VAL B CA  1 
ATOM   1920 C  C   . VAL A 1 244 ? 22.080  -1.313  -0.081  1.00 10.75 ? 244 VAL B C   1 
ATOM   1921 O  O   . VAL A 1 244 ? 21.867  -0.199  0.361   1.00 9.68  ? 244 VAL B O   1 
ATOM   1922 C  CB  . VAL A 1 244 ? 22.243  -2.875  1.919   1.00 12.50 ? 244 VAL B CB  1 
ATOM   1923 C  CG1 . VAL A 1 244 ? 21.503  -3.971  2.717   1.00 13.77 ? 244 VAL B CG1 1 
ATOM   1924 C  CG2 . VAL A 1 244 ? 23.714  -3.116  1.669   1.00 13.36 ? 244 VAL B CG2 1 
ATOM   1925 N  N   . SER A 1 245 ? 22.853  -1.526  -1.149  1.00 10.26 ? 245 SER B N   1 
ATOM   1926 C  CA  . SER A 1 245 ? 23.471  -0.385  -1.872  1.00 10.58 ? 245 SER B CA  1 
ATOM   1927 C  C   . SER A 1 245 ? 23.656  -0.765  -3.322  1.00 11.33 ? 245 SER B C   1 
ATOM   1928 O  O   . SER A 1 245 ? 24.141  -1.848  -3.607  1.00 11.09 ? 245 SER B O   1 
ATOM   1929 C  CB  . SER A 1 245 ? 24.856  -0.081  -1.282  1.00 11.75 ? 245 SER B CB  1 
ATOM   1930 O  OG  . SER A 1 245 ? 25.428  1.058   -1.871  1.00 12.20 ? 245 SER B OG  1 
ATOM   1931 N  N   . ASN A 1 246 ? 23.287  0.131   -4.241  1.00 10.40 ? 246 ASN B N   1 
ATOM   1932 C  CA  . ASN A 1 246 ? 23.388  -0.206  -5.673  1.00 10.15 ? 246 ASN B CA  1 
ATOM   1933 C  C   . ASN A 1 246 ? 23.768  1.058   -6.498  1.00 10.73 ? 246 ASN B C   1 
ATOM   1934 O  O   . ASN A 1 246 ? 23.177  1.310   -7.553  1.00 11.64 ? 246 ASN B O   1 
ATOM   1935 C  CB  . ASN A 1 246 ? 22.083  -0.832  -6.133  1.00 9.86  ? 246 ASN B CB  1 
ATOM   1936 C  CG  . ASN A 1 246 ? 20.882  0.142   -6.040  1.00 10.50 ? 246 ASN B CG  1 
ATOM   1937 O  OD1 . ASN A 1 246 ? 20.966  1.183   -5.390  1.00 11.40 ? 246 ASN B OD1 1 
ATOM   1938 N  ND2 . ASN A 1 246 ? 19.785  -0.184  -6.691  1.00 9.10  ? 246 ASN B ND2 1 
ATOM   1939 N  N   . HIS A 1 247 ? 24.755  1.809   -6.013  1.00 10.22 ? 247 HIS B N   1 
ATOM   1940 C  CA  . HIS A 1 247 ? 25.218  2.988   -6.753  1.00 9.93  ? 247 HIS B CA  1 
ATOM   1941 C  C   . HIS A 1 247 ? 26.694  2.836   -7.118  1.00 11.23 ? 247 HIS B C   1 
ATOM   1942 O  O   . HIS A 1 247 ? 27.517  2.360   -6.293  1.00 13.34 ? 247 HIS B O   1 
ATOM   1943 C  CB  . HIS A 1 247 ? 24.967  4.343   -5.978  1.00 10.16 ? 247 HIS B CB  1 
ATOM   1944 C  CG  . HIS A 1 247 ? 25.765  4.478   -4.708  1.00 11.74 ? 247 HIS B CG  1 
ATOM   1945 N  ND1 . HIS A 1 247 ? 25.338  3.914   -3.519  1.00 12.93 ? 247 HIS B ND1 1 
ATOM   1946 C  CD2 . HIS A 1 247 ? 26.953  5.081   -4.436  1.00 12.63 ? 247 HIS B CD2 1 
ATOM   1947 C  CE1 . HIS A 1 247 ? 26.255  4.117   -2.579  1.00 12.25 ? 247 HIS B CE1 1 
ATOM   1948 N  NE2 . HIS A 1 247 ? 27.216  4.861   -3.088  1.00 12.46 ? 247 HIS B NE2 1 
ATOM   1949 N  N   . ARG A 1 248 ? 27.020  3.239   -8.340  1.00 10.58 ? 248 ARG B N   1 
ATOM   1950 C  CA  . ARG A 1 248 ? 28.402  3.195   -8.839  1.00 10.52 ? 248 ARG B CA  1 
ATOM   1951 C  C   . ARG A 1 248 ? 29.125  4.456   -8.340  1.00 11.44 ? 248 ARG B C   1 
ATOM   1952 O  O   . ARG A 1 248 ? 28.524  5.555   -8.279  1.00 12.10 ? 248 ARG B O   1 
ATOM   1953 C  CB  . ARG A 1 248 ? 28.371  3.265   -10.369 1.00 11.22 ? 248 ARG B CB  1 
ATOM   1954 C  CG  . ARG A 1 248 ? 29.788  3.010   -10.961 1.00 11.04 ? 248 ARG B CG  1 
ATOM   1955 C  CD  . ARG A 1 248 ? 29.857  3.195   -12.460 1.00 11.77 ? 248 ARG B CD  1 
ATOM   1956 N  NE  . ARG A 1 248 ? 31.079  2.584   -12.963 1.00 11.70 ? 248 ARG B NE  1 
ATOM   1957 C  CZ  . ARG A 1 248 ? 31.563  2.738   -14.196 1.00 12.69 ? 248 ARG B CZ  1 
ATOM   1958 N  NH1 . ARG A 1 248 ? 30.957  3.539   -15.091 1.00 12.40 ? 248 ARG B NH1 1 
ATOM   1959 N  NH2 . ARG A 1 248 ? 32.668  2.098   -14.523 1.00 13.17 ? 248 ARG B NH2 1 
ATOM   1960 N  N   . PRO A 1 249 ? 30.455  4.365   -8.026  1.00 11.53 ? 249 PRO B N   1 
ATOM   1961 C  CA  . PRO A 1 249 ? 31.155  5.556   -7.619  1.00 11.17 ? 249 PRO B CA  1 
ATOM   1962 C  C   . PRO A 1 249 ? 31.312  6.566   -8.786  1.00 11.46 ? 249 PRO B C   1 
ATOM   1963 O  O   . PRO A 1 249 ? 31.198  6.165   -9.971  1.00 11.50 ? 249 PRO B O   1 
ATOM   1964 C  CB  . PRO A 1 249 ? 32.594  5.009   -7.331  1.00 11.35 ? 249 PRO B CB  1 
ATOM   1965 C  CG  . PRO A 1 249 ? 32.441  3.580   -6.937  1.00 10.98 ? 249 PRO B CG  1 
ATOM   1966 C  CD  . PRO A 1 249 ? 31.272  3.132   -7.853  1.00 12.54 ? 249 PRO B CD  1 
ATOM   1967 N  N   . PRO A 1 250 ? 31.660  7.829   -8.499  1.00 13.22 ? 250 PRO B N   1 
ATOM   1968 C  CA  . PRO A 1 250 ? 31.893  8.752   -9.627  1.00 12.72 ? 250 PRO B CA  1 
ATOM   1969 C  C   . PRO A 1 250 ? 33.123  8.409   -10.466 1.00 13.07 ? 250 PRO B C   1 
ATOM   1970 O  O   . PRO A 1 250 ? 34.144  7.847   -9.939  1.00 13.14 ? 250 PRO B O   1 
ATOM   1971 C  CB  . PRO A 1 250 ? 32.049  10.112  -8.918  1.00 15.36 ? 250 PRO B CB  1 
ATOM   1972 C  CG  . PRO A 1 250 ? 32.696  9.752   -7.616  1.00 15.27 ? 250 PRO B CG  1 
ATOM   1973 C  CD  . PRO A 1 250 ? 32.058  8.437   -7.216  1.00 13.95 ? 250 PRO B CD  1 
ATOM   1974 N  N   . GLN A 1 251 ? 33.053  8.752   -11.743 1.00 12.88 ? 251 GLN B N   1 
ATOM   1975 C  CA  . GLN A 1 251 ? 34.065  8.344   -12.750 1.00 13.68 ? 251 GLN B CA  1 
ATOM   1976 C  C   . GLN A 1 251 ? 34.745  9.602   -13.261 1.00 14.97 ? 251 GLN B C   1 
ATOM   1977 O  O   . GLN A 1 251 ? 34.220  10.673  -13.187 1.00 14.04 ? 251 GLN B O   1 
ATOM   1978 C  CB  . GLN A 1 251 ? 33.378  7.563   -13.901 1.00 14.72 ? 251 GLN B CB  1 
ATOM   1979 C  CG  . GLN A 1 251 ? 32.586  6.331   -13.387 1.00 15.85 ? 251 GLN B CG  1 
ATOM   1980 C  CD  . GLN A 1 251 ? 33.495  5.308   -12.694 1.00 17.79 ? 251 GLN B CD  1 
ATOM   1981 O  OE1 . GLN A 1 251 ? 33.173  4.798   -11.582 1.00 19.83 ? 251 GLN B OE1 1 
ATOM   1982 N  NE2 . GLN A 1 251 ? 34.647  5.046   -13.281 1.00 15.56 ? 251 GLN B NE2 1 
ATOM   1983 N  N   . PRO A 1 252 ? 35.964  9.470   -13.785 1.00 15.02 ? 252 PRO B N   1 
ATOM   1984 C  CA  . PRO A 1 252 ? 36.710  10.665  -14.185 1.00 16.19 ? 252 PRO B CA  1 
ATOM   1985 C  C   . PRO A 1 252 ? 36.033  11.419  -15.349 1.00 15.02 ? 252 PRO B C   1 
ATOM   1986 O  O   . PRO A 1 252 ? 35.574  10.793  -16.336 1.00 14.74 ? 252 PRO B O   1 
ATOM   1987 C  CB  . PRO A 1 252 ? 38.034  10.069  -14.719 1.00 15.81 ? 252 PRO B CB  1 
ATOM   1988 C  CG  . PRO A 1 252 ? 38.164  8.706   -14.068 1.00 17.29 ? 252 PRO B CG  1 
ATOM   1989 C  CD  . PRO A 1 252 ? 36.725  8.205   -13.940 1.00 16.12 ? 252 PRO B CD  1 
ATOM   1990 N  N   . LEU A 1 253 ? 36.017  12.735  -15.242 1.00 14.76 ? 253 LEU B N   1 
ATOM   1991 C  CA  . LEU A 1 253 ? 35.346  13.523  -16.248 1.00 14.15 ? 253 LEU B CA  1 
ATOM   1992 C  C   . LEU A 1 253 ? 36.079  13.528  -17.610 1.00 15.79 ? 253 LEU B C   1 
ATOM   1993 O  O   . LEU A 1 253 ? 35.429  13.713  -18.699 1.00 14.56 ? 253 LEU B O   1 
ATOM   1994 C  CB  . LEU A 1 253 ? 35.096  14.931  -15.716 1.00 14.50 ? 253 LEU B CB  1 
ATOM   1995 C  CG  . LEU A 1 253 ? 34.174  15.873  -16.483 1.00 14.89 ? 253 LEU B CG  1 
ATOM   1996 C  CD1 . LEU A 1 253 ? 32.798  15.225  -16.677 1.00 14.64 ? 253 LEU B CD1 1 
ATOM   1997 C  CD2 . LEU A 1 253 ? 34.124  17.219  -15.760 1.00 14.14 ? 253 LEU B CD2 1 
ATOM   1998 N  N   . LYS A 1 254 ? 37.414  13.391  -17.567 1.00 17.00 ? 254 LYS B N   1 
ATOM   1999 C  CA  . LYS A 1 254 ? 38.186  13.199  -18.790 1.00 16.65 ? 254 LYS B CA  1 
ATOM   2000 C  C   . LYS A 1 254 ? 37.907  14.327  -19.842 1.00 15.71 ? 254 LYS B C   1 
ATOM   2001 O  O   . LYS A 1 254 ? 37.899  14.062  -21.072 1.00 15.47 ? 254 LYS B O   1 
ATOM   2002 C  CB  . LYS A 1 254 ? 37.900  11.798  -19.378 1.00 19.52 ? 254 LYS B CB  1 
ATOM   2003 C  CG  . LYS A 1 254 ? 38.366  10.575  -18.555 1.00 21.87 ? 254 LYS B CG  1 
ATOM   2004 C  CD  . LYS A 1 254 ? 39.873  10.458  -18.527 1.00 23.54 ? 254 LYS B CD  1 
ATOM   2005 C  CE  . LYS A 1 254 ? 40.408  9.099   -18.009 1.00 26.59 ? 254 LYS B CE  1 
ATOM   2006 N  NZ  . LYS A 1 254 ? 39.742  7.994   -18.733 1.00 39.12 ? 254 LYS B NZ  1 
ATOM   2007 N  N   . GLY A 1 255 ? 37.724  15.563  -19.350 1.00 15.80 ? 255 GLY B N   1 
ATOM   2008 C  CA  . GLY A 1 255 ? 37.648  16.745  -20.228 1.00 15.36 ? 255 GLY B CA  1 
ATOM   2009 C  C   . GLY A 1 255 ? 36.314  16.914  -20.934 1.00 15.88 ? 255 GLY B C   1 
ATOM   2010 O  O   . GLY A 1 255 ? 36.150  17.819  -21.756 1.00 16.37 ? 255 GLY B O   1 
ATOM   2011 N  N   . ARG A 1 256 ? 35.333  16.099  -20.556 1.00 12.92 ? 256 ARG B N   1 
ATOM   2012 C  CA  . ARG A 1 256 ? 33.962  16.409  -20.958 1.00 13.61 ? 256 ARG B CA  1 
ATOM   2013 C  C   . ARG A 1 256 ? 33.425  17.717  -20.374 1.00 15.33 ? 256 ARG B C   1 
ATOM   2014 O  O   . ARG A 1 256 ? 33.880  18.198  -19.293 1.00 17.11 ? 256 ARG B O   1 
ATOM   2015 C  CB  . ARG A 1 256 ? 33.034  15.241  -20.583 1.00 13.20 ? 256 ARG B CB  1 
ATOM   2016 C  CG  . ARG A 1 256 ? 33.262  13.999  -21.415 1.00 12.55 ? 256 ARG B CG  1 
ATOM   2017 C  CD  . ARG A 1 256 ? 32.419  12.842  -20.875 1.00 11.64 ? 256 ARG B CD  1 
ATOM   2018 N  NE  . ARG A 1 256 ? 32.980  12.349  -19.569 1.00 13.33 ? 256 ARG B NE  1 
ATOM   2019 C  CZ  . ARG A 1 256 ? 32.385  11.428  -18.811 1.00 12.72 ? 256 ARG B CZ  1 
ATOM   2020 N  NH1 . ARG A 1 256 ? 31.168  11.008  -19.138 1.00 11.45 ? 256 ARG B NH1 1 
ATOM   2021 N  NH2 . ARG A 1 256 ? 32.977  10.990  -17.711 1.00 11.75 ? 256 ARG B NH2 1 
ATOM   2022 N  N   . LYS A 1 257 ? 32.465  18.329  -21.074 1.00 16.37 ? 257 LYS B N   1 
ATOM   2023 C  CA  . LYS A 1 257 ? 31.923  19.581  -20.638 1.00 19.01 ? 257 LYS B CA  1 
ATOM   2024 C  C   . LYS A 1 257 ? 30.604  19.278  -19.970 1.00 16.45 ? 257 LYS B C   1 
ATOM   2025 O  O   . LYS A 1 257 ? 29.736  18.671  -20.625 1.00 17.62 ? 257 LYS B O   1 
ATOM   2026 C  CB  . LYS A 1 257 ? 31.647  20.465  -21.876 1.00 23.92 ? 257 LYS B CB  1 
ATOM   2027 C  CG  . LYS A 1 257 ? 31.358  21.912  -21.514 1.00 28.16 ? 257 LYS B CG  1 
ATOM   2028 C  CD  . LYS A 1 257 ? 30.926  22.724  -22.744 1.00 33.12 ? 257 LYS B CD  1 
ATOM   2029 C  CE  . LYS A 1 257 ? 31.931  22.707  -23.915 1.00 37.61 ? 257 LYS B CE  1 
ATOM   2030 N  NZ  . LYS A 1 257 ? 31.575  23.791  -24.900 1.00 37.52 ? 257 LYS B NZ  1 
ATOM   2031 N  N   . VAL A 1 258 ? 30.424  19.699  -18.715 1.00 15.53 ? 258 VAL B N   1 
ATOM   2032 C  CA  . VAL A 1 258 ? 29.033  19.608  -18.111 1.00 14.39 ? 258 VAL B CA  1 
ATOM   2033 C  C   . VAL A 1 258 ? 28.352  20.942  -18.370 1.00 14.17 ? 258 VAL B C   1 
ATOM   2034 O  O   . VAL A 1 258 ? 28.926  21.989  -18.032 1.00 14.44 ? 258 VAL B O   1 
ATOM   2035 C  CB  . VAL A 1 258 ? 29.083  19.322  -16.612 1.00 13.94 ? 258 VAL B CB  1 
ATOM   2036 C  CG1 . VAL A 1 258 ? 27.654  19.178  -16.069 1.00 16.40 ? 258 VAL B CG1 1 
ATOM   2037 C  CG2 . VAL A 1 258 ? 29.866  18.022  -16.410 1.00 15.05 ? 258 VAL B CG2 1 
ATOM   2038 N  N   . ARG A 1 259 ? 27.158  20.931  -18.993 1.00 11.96 ? 259 ARG B N   1 
ATOM   2039 C  CA  . ARG A 1 259 ? 26.503  22.238  -19.284 1.00 12.23 ? 259 ARG B CA  1 
ATOM   2040 C  C   . ARG A 1 259 ? 25.212  22.377  -18.448 1.00 12.68 ? 259 ARG B C   1 
ATOM   2041 O  O   . ARG A 1 259 ? 24.592  21.362  -17.997 1.00 12.26 ? 259 ARG B O   1 
ATOM   2042 C  CB  . ARG A 1 259 ? 26.111  22.333  -20.746 1.00 11.36 ? 259 ARG B CB  1 
ATOM   2043 C  CG  . ARG A 1 259 ? 27.322  22.288  -21.681 1.00 12.72 ? 259 ARG B CG  1 
ATOM   2044 C  CD  . ARG A 1 259 ? 26.872  22.155  -23.153 1.00 12.13 ? 259 ARG B CD  1 
ATOM   2045 N  NE  . ARG A 1 259 ? 26.210  20.898  -23.476 1.00 13.04 ? 259 ARG B NE  1 
ATOM   2046 C  CZ  . ARG A 1 259 ? 25.380  20.731  -24.514 1.00 12.47 ? 259 ARG B CZ  1 
ATOM   2047 N  NH1 . ARG A 1 259 ? 25.067  21.802  -25.310 1.00 13.15 ? 259 ARG B NH1 1 
ATOM   2048 N  NH2 . ARG A 1 259 ? 24.848  19.503  -24.712 1.00 12.46 ? 259 ARG B NH2 1 
ATOM   2049 N  N   . ALA A 1 260 ? 24.857  23.615  -18.200 1.00 12.93 ? 260 ALA B N   1 
ATOM   2050 C  CA  . ALA A 1 260 ? 23.619  23.919  -17.427 1.00 13.36 ? 260 ALA B CA  1 
ATOM   2051 C  C   . ALA A 1 260 ? 22.598  24.596  -18.311 1.00 13.92 ? 260 ALA B C   1 
ATOM   2052 O  O   . ALA A 1 260 ? 22.974  25.471  -19.106 1.00 14.34 ? 260 ALA B O   1 
ATOM   2053 C  CB  . ALA A 1 260 ? 23.966  24.827  -16.235 1.00 12.93 ? 260 ALA B CB  1 
ATOM   2054 N  N   . SER A 1 261 ? 21.301  24.256  -18.133 1.00 13.52 ? 261 SER B N   1 
ATOM   2055 C  CA  . SER A 1 261 ? 20.217  24.896  -18.874 1.00 13.84 ? 261 SER B CA  1 
ATOM   2056 C  C   . SER A 1 261 ? 19.843  26.278  -18.317 1.00 14.45 ? 261 SER B C   1 
ATOM   2057 O  O   . SER A 1 261 ? 18.996  26.937  -18.905 1.00 15.17 ? 261 SER B O   1 
ATOM   2058 C  CB  . SER A 1 261 ? 18.945  24.035  -18.867 1.00 13.04 ? 261 SER B CB  1 
ATOM   2059 O  OG  . SER A 1 261 ? 18.400  24.061  -17.527 1.00 15.09 ? 261 SER B OG  1 
ATOM   2060 N  N   . PHE A 1 262 ? 20.404  26.655  -17.188 1.00 15.37 ? 262 PHE B N   1 
ATOM   2061 C  CA  . PHE A 1 262 ? 19.975  27.789  -16.400 1.00 20.51 ? 262 PHE B CA  1 
ATOM   2062 C  C   . PHE A 1 262 ? 21.190  28.583  -15.907 1.00 23.17 ? 262 PHE B C   1 
ATOM   2063 O  O   . PHE A 1 262 ? 22.316  28.071  -15.842 1.00 21.73 ? 262 PHE B O   1 
ATOM   2064 C  CB  . PHE A 1 262 ? 19.198  27.277  -15.144 1.00 19.05 ? 262 PHE B CB  1 
ATOM   2065 C  CG  . PHE A 1 262 ? 20.026  26.432  -14.241 1.00 19.62 ? 262 PHE B CG  1 
ATOM   2066 C  CD1 . PHE A 1 262 ? 20.213  25.062  -14.500 1.00 18.68 ? 262 PHE B CD1 1 
ATOM   2067 C  CD2 . PHE A 1 262 ? 20.688  26.993  -13.130 1.00 22.04 ? 262 PHE B CD2 1 
ATOM   2068 C  CE1 . PHE A 1 262 ? 21.044  24.269  -13.700 1.00 18.50 ? 262 PHE B CE1 1 
ATOM   2069 C  CE2 . PHE A 1 262 ? 21.547  26.220  -12.341 1.00 19.57 ? 262 PHE B CE2 1 
ATOM   2070 C  CZ  . PHE A 1 262 ? 21.716  24.854  -12.622 1.00 19.47 ? 262 PHE B CZ  1 
ATOM   2071 N  N   . HIS A 1 263 ? 20.972  29.816  -15.464 1.00 28.95 ? 263 HIS B N   1 
ATOM   2072 C  CA  . HIS A 1 263 ? 22.005  30.489  -14.640 1.00 32.68 ? 263 HIS B CA  1 
ATOM   2073 C  C   . HIS A 1 263 ? 21.372  31.539  -13.734 1.00 38.80 ? 263 HIS B C   1 
ATOM   2074 O  O   . HIS A 1 263 ? 22.077  32.184  -12.959 1.00 44.35 ? 263 HIS B O   1 
ATOM   2075 C  CB  . HIS A 1 263 ? 23.115  31.125  -15.522 1.00 31.43 ? 263 HIS B CB  1 
ATOM   2076 C  CG  . HIS A 1 263 ? 22.617  32.178  -16.478 1.00 32.46 ? 263 HIS B CG  1 
ATOM   2077 N  ND1 . HIS A 1 263 ? 21.277  32.360  -16.784 1.00 35.65 ? 263 HIS B ND1 1 
ATOM   2078 C  CD2 . HIS A 1 263 ? 23.291  33.100  -17.207 1.00 33.80 ? 263 HIS B CD2 1 
ATOM   2079 C  CE1 . HIS A 1 263 ? 21.147  33.342  -17.656 1.00 33.50 ? 263 HIS B CE1 1 
ATOM   2080 N  NE2 . HIS A 1 263 ? 22.356  33.810  -17.927 1.00 38.52 ? 263 HIS B NE2 1 
ATOM   2081 O  OXT . HIS A 1 263 ? 20.157  31.770  -13.772 1.00 38.08 ? 263 HIS B OXT 1 
ATOM   2082 N  N   . SER B 1 6   ? -24.114 42.097  -28.554 1.00 42.14 ? 6   SER A N   1 
ATOM   2083 C  CA  . SER B 1 6   ? -22.869 41.486  -27.952 1.00 35.47 ? 6   SER A CA  1 
ATOM   2084 C  C   . SER B 1 6   ? -21.716 41.374  -28.956 1.00 33.07 ? 6   SER A C   1 
ATOM   2085 O  O   . SER B 1 6   ? -21.925 41.268  -30.176 1.00 32.39 ? 6   SER A O   1 
ATOM   2086 C  CB  . SER B 1 6   ? -23.163 40.145  -27.331 1.00 38.47 ? 6   SER A CB  1 
ATOM   2087 O  OG  . SER B 1 6   ? -23.130 40.294  -25.921 1.00 46.87 ? 6   SER A OG  1 
ATOM   2088 N  N   . TRP B 1 7   ? -20.498 41.353  -28.438 1.00 25.16 ? 7   TRP A N   1 
ATOM   2089 C  CA  . TRP B 1 7   ? -19.335 41.672  -29.252 1.00 19.68 ? 7   TRP A CA  1 
ATOM   2090 C  C   . TRP B 1 7   ? -18.965 40.504  -30.157 1.00 16.09 ? 7   TRP A C   1 
ATOM   2091 O  O   . TRP B 1 7   ? -19.305 39.330  -29.887 1.00 16.96 ? 7   TRP A O   1 
ATOM   2092 C  CB  . TRP B 1 7   ? -18.185 42.053  -28.307 1.00 17.96 ? 7   TRP A CB  1 
ATOM   2093 C  CG  . TRP B 1 7   ? -17.683 40.883  -27.519 1.00 18.00 ? 7   TRP A CG  1 
ATOM   2094 C  CD1 . TRP B 1 7   ? -18.109 40.469  -26.277 1.00 16.88 ? 7   TRP A CD1 1 
ATOM   2095 C  CD2 . TRP B 1 7   ? -16.628 40.001  -27.904 1.00 16.06 ? 7   TRP A CD2 1 
ATOM   2096 N  NE1 . TRP B 1 7   ? -17.383 39.380  -25.855 1.00 16.65 ? 7   TRP A NE1 1 
ATOM   2097 C  CE2 . TRP B 1 7   ? -16.455 39.060  -26.829 1.00 15.97 ? 7   TRP A CE2 1 
ATOM   2098 C  CE3 . TRP B 1 7   ? -15.795 39.919  -29.025 1.00 15.85 ? 7   TRP A CE3 1 
ATOM   2099 C  CZ2 . TRP B 1 7   ? -15.486 38.031  -26.871 1.00 14.78 ? 7   TRP A CZ2 1 
ATOM   2100 C  CZ3 . TRP B 1 7   ? -14.825 38.880  -29.058 1.00 16.42 ? 7   TRP A CZ3 1 
ATOM   2101 C  CH2 . TRP B 1 7   ? -14.697 37.943  -27.999 1.00 13.26 ? 7   TRP A CH2 1 
ATOM   2102 N  N   . GLY B 1 8   ? -18.269 40.797  -31.243 1.00 15.22 ? 8   GLY A N   1 
ATOM   2103 C  CA  . GLY B 1 8   ? -17.718 39.716  -32.096 1.00 13.47 ? 8   GLY A CA  1 
ATOM   2104 C  C   . GLY B 1 8   ? -16.688 40.264  -33.020 1.00 13.20 ? 8   GLY A C   1 
ATOM   2105 O  O   . GLY B 1 8   ? -15.979 41.195  -32.629 1.00 13.75 ? 8   GLY A O   1 
ATOM   2106 N  N   . TYR B 1 9   ? -16.642 39.745  -34.250 1.00 12.25 ? 9   TYR A N   1 
ATOM   2107 C  CA  . TYR B 1 9   ? -15.693 40.186  -35.265 1.00 13.57 ? 9   TYR A CA  1 
ATOM   2108 C  C   . TYR B 1 9   ? -16.327 40.604  -36.568 1.00 15.88 ? 9   TYR A C   1 
ATOM   2109 O  O   . TYR B 1 9   ? -15.615 40.858  -37.572 1.00 17.13 ? 9   TYR A O   1 
ATOM   2110 C  CB  . TYR B 1 9   ? -14.633 39.079  -35.518 1.00 12.26 ? 9   TYR A CB  1 
ATOM   2111 C  CG  . TYR B 1 9   ? -13.804 38.825  -34.252 1.00 11.68 ? 9   TYR A CG  1 
ATOM   2112 C  CD1 . TYR B 1 9   ? -12.642 39.594  -33.981 1.00 13.16 ? 9   TYR A CD1 1 
ATOM   2113 C  CD2 . TYR B 1 9   ? -14.138 37.762  -33.369 1.00 11.22 ? 9   TYR A CD2 1 
ATOM   2114 C  CE1 . TYR B 1 9   ? -11.844 39.351  -32.838 1.00 11.58 ? 9   TYR A CE1 1 
ATOM   2115 C  CE2 . TYR B 1 9   ? -13.344 37.487  -32.254 1.00 11.85 ? 9   TYR A CE2 1 
ATOM   2116 C  CZ  . TYR B 1 9   ? -12.237 38.285  -31.993 1.00 11.99 ? 9   TYR A CZ  1 
ATOM   2117 O  OH  . TYR B 1 9   ? -11.500 38.018  -30.899 1.00 10.80 ? 9   TYR A OH  1 
ATOM   2118 N  N   . ARG B 1 10  ? -17.652 40.732  -36.513 1.00 18.41 ? 10  ARG A N   1 
ATOM   2119 C  CA  . ARG B 1 10  ? -18.498 41.028  -37.711 1.00 20.58 ? 10  ARG A CA  1 
ATOM   2120 C  C   . ARG B 1 10  ? -18.534 42.552  -37.891 1.00 20.31 ? 10  ARG A C   1 
ATOM   2121 O  O   . ARG B 1 10  ? -18.018 43.297  -37.089 1.00 19.72 ? 10  ARG A O   1 
ATOM   2122 C  CB  . ARG B 1 10  ? -19.904 40.429  -37.512 1.00 20.38 ? 10  ARG A CB  1 
ATOM   2123 C  CG  . ARG B 1 10  ? -19.856 38.896  -37.521 1.00 23.85 ? 10  ARG A CG  1 
ATOM   2124 C  CD  . ARG B 1 10  ? -21.185 38.244  -37.211 1.00 25.31 ? 10  ARG A CD  1 
ATOM   2125 N  NE  . ARG B 1 10  ? -22.031 38.283  -38.417 1.00 30.00 ? 10  ARG A NE  1 
ATOM   2126 C  CZ  . ARG B 1 10  ? -23.296 37.835  -38.445 1.00 29.31 ? 10  ARG A CZ  1 
ATOM   2127 N  NH1 . ARG B 1 10  ? -23.870 37.262  -37.363 1.00 24.96 ? 10  ARG A NH1 1 
ATOM   2128 N  NH2 . ARG B 1 10  ? -23.980 37.930  -39.589 1.00 33.88 ? 10  ARG A NH2 1 
ATOM   2129 N  N   . GLU B 1 11  ? -19.114 43.044  -38.978 1.00 21.50 ? 11  GLU A N   1 
ATOM   2130 C  CA  . GLU B 1 11  ? -19.156 44.477  -39.161 1.00 22.54 ? 11  GLU A CA  1 
ATOM   2131 C  C   . GLU B 1 11  ? -19.724 45.305  -37.990 1.00 20.70 ? 11  GLU A C   1 
ATOM   2132 O  O   . GLU B 1 11  ? -19.114 46.325  -37.599 1.00 21.46 ? 11  GLU A O   1 
ATOM   2133 C  CB  . GLU B 1 11  ? -19.999 44.758  -40.415 1.00 30.75 ? 11  GLU A CB  1 
ATOM   2134 C  CG  . GLU B 1 11  ? -19.642 46.058  -41.104 1.00 39.79 ? 11  GLU A CG  1 
ATOM   2135 C  CD  . GLU B 1 11  ? -20.459 46.282  -42.379 1.00 50.90 ? 11  GLU A CD  1 
ATOM   2136 O  OE1 . GLU B 1 11  ? -20.803 47.464  -42.658 1.00 57.99 ? 11  GLU A OE1 1 
ATOM   2137 O  OE2 . GLU B 1 11  ? -20.745 45.290  -43.099 1.00 47.70 ? 11  GLU A OE2 1 
ATOM   2138 N  N   . HIS B 1 12  ? -20.887 44.941  -37.463 0.50 17.82 ? 12  HIS A N   1 
ATOM   2139 C  CA  . HIS B 1 12  ? -21.536 45.804  -36.465 0.50 18.96 ? 12  HIS A CA  1 
ATOM   2140 C  C   . HIS B 1 12  ? -21.050 45.634  -35.016 0.50 17.02 ? 12  HIS A C   1 
ATOM   2141 O  O   . HIS B 1 12  ? -21.369 46.400  -34.164 0.50 16.21 ? 12  HIS A O   1 
ATOM   2142 C  CB  . HIS B 1 12  ? -23.055 45.666  -36.543 0.50 20.70 ? 12  HIS A CB  1 
ATOM   2143 C  CG  . HIS B 1 12  ? -23.627 46.071  -37.873 0.50 24.04 ? 12  HIS A CG  1 
ATOM   2144 N  ND1 . HIS B 1 12  ? -23.830 47.387  -38.231 0.50 26.33 ? 12  HIS A ND1 1 
ATOM   2145 C  CD2 . HIS B 1 12  ? -24.033 45.328  -38.930 0.50 26.33 ? 12  HIS A CD2 1 
ATOM   2146 C  CE1 . HIS B 1 12  ? -24.365 47.432  -39.437 0.50 27.80 ? 12  HIS A CE1 1 
ATOM   2147 N  NE2 . HIS B 1 12  ? -24.501 46.196  -39.881 0.50 26.77 ? 12  HIS A NE2 1 
ATOM   2148 N  N   . ASN B 1 13  ? -20.268 44.606  -34.758 1.00 18.53 ? 13  ASN A N   1 
ATOM   2149 C  CA  . ASN B 1 13  ? -19.947 44.232  -33.378 1.00 17.09 ? 13  ASN A CA  1 
ATOM   2150 C  C   . ASN B 1 13  ? -18.439 43.997  -33.248 1.00 17.30 ? 13  ASN A C   1 
ATOM   2151 O  O   . ASN B 1 13  ? -17.982 43.501  -32.204 1.00 19.62 ? 13  ASN A O   1 
ATOM   2152 C  CB  . ASN B 1 13  ? -20.756 42.978  -32.921 1.00 18.21 ? 13  ASN A CB  1 
ATOM   2153 C  CG  . ASN B 1 13  ? -20.344 41.668  -33.615 1.00 16.87 ? 13  ASN A CG  1 
ATOM   2154 O  OD1 . ASN B 1 13  ? -19.476 41.641  -34.490 1.00 15.55 ? 13  ASN A OD1 1 
ATOM   2155 N  ND2 . ASN B 1 13  ? -21.056 40.572  -33.261 1.00 17.54 ? 13  ASN A ND2 1 
ATOM   2156 N  N   . GLY B 1 14  ? -17.715 44.236  -34.321 1.00 16.82 ? 14  GLY A N   1 
ATOM   2157 C  CA  . GLY B 1 14  ? -16.263 43.910  -34.400 1.00 19.62 ? 14  GLY A CA  1 
ATOM   2158 C  C   . GLY B 1 14  ? -15.360 44.897  -33.647 1.00 16.91 ? 14  GLY A C   1 
ATOM   2159 O  O   . GLY B 1 14  ? -15.813 45.813  -33.014 1.00 18.85 ? 14  GLY A O   1 
ATOM   2160 N  N   . PRO B 1 15  ? -14.034 44.690  -33.706 1.00 17.41 ? 15  PRO A N   1 
ATOM   2161 C  CA  . PRO B 1 15  ? -13.061 45.401  -32.867 1.00 16.87 ? 15  PRO A CA  1 
ATOM   2162 C  C   . PRO B 1 15  ? -13.174 46.909  -32.825 1.00 18.81 ? 15  PRO A C   1 
ATOM   2163 O  O   . PRO B 1 15  ? -13.090 47.490  -31.742 1.00 18.20 ? 15  PRO A O   1 
ATOM   2164 C  CB  . PRO B 1 15  ? -11.723 44.999  -33.477 1.00 16.53 ? 15  PRO A CB  1 
ATOM   2165 C  CG  . PRO B 1 15  ? -11.965 43.648  -34.012 1.00 15.59 ? 15  PRO A CG  1 
ATOM   2166 C  CD  . PRO B 1 15  ? -13.408 43.584  -34.453 1.00 17.34 ? 15  PRO A CD  1 
ATOM   2167 N  N   . ILE B 1 16  ? -13.425 47.548  -33.990 1.00 21.88 ? 16  ILE A N   1 
ATOM   2168 C  CA  . ILE B 1 16  ? -13.656 49.033  -34.031 1.00 26.22 ? 16  ILE A CA  1 
ATOM   2169 C  C   . ILE B 1 16  ? -14.771 49.497  -33.105 1.00 24.09 ? 16  ILE A C   1 
ATOM   2170 O  O   . ILE B 1 16  ? -14.712 50.616  -32.561 1.00 26.39 ? 16  ILE A O   1 
ATOM   2171 C  CB  . ILE B 1 16  ? -13.816 49.590  -35.494 1.00 28.33 ? 16  ILE A CB  1 
ATOM   2172 C  CG1 . ILE B 1 16  ? -13.520 51.107  -35.552 1.00 34.13 ? 16  ILE A CG1 1 
ATOM   2173 C  CG2 . ILE B 1 16  ? -15.192 49.262  -36.094 1.00 29.08 ? 16  ILE A CG2 1 
ATOM   2174 C  CD1 . ILE B 1 16  ? -12.040 51.435  -35.688 1.00 37.34 ? 16  ILE A CD1 1 
ATOM   2175 N  N   . HIS B 1 17  ? -15.769 48.633  -32.878 1.00 23.36 ? 17  HIS A N   1 
ATOM   2176 C  CA  . HIS B 1 17  ? -16.897 48.949  -32.012 1.00 21.64 ? 17  HIS A CA  1 
ATOM   2177 C  C   . HIS B 1 17  ? -16.749 48.672  -30.553 1.00 21.76 ? 17  HIS A C   1 
ATOM   2178 O  O   . HIS B 1 17  ? -17.556 49.151  -29.790 1.00 20.21 ? 17  HIS A O   1 
ATOM   2179 C  CB  . HIS B 1 17  ? -18.168 48.247  -32.506 1.00 26.06 ? 17  HIS A CB  1 
ATOM   2180 C  CG  . HIS B 1 17  ? -18.571 48.678  -33.885 1.00 30.99 ? 17  HIS A CG  1 
ATOM   2181 N  ND1 . HIS B 1 17  ? -19.225 49.869  -34.125 1.00 32.42 ? 17  HIS A ND1 1 
ATOM   2182 C  CD2 . HIS B 1 17  ? -18.372 48.103  -35.096 1.00 31.62 ? 17  HIS A CD2 1 
ATOM   2183 C  CE1 . HIS B 1 17  ? -19.423 49.997  -35.431 1.00 35.38 ? 17  HIS A CE1 1 
ATOM   2184 N  NE2 . HIS B 1 17  ? -18.903 48.946  -36.045 1.00 32.00 ? 17  HIS A NE2 1 
ATOM   2185 N  N   . TRP B 1 18  ? -15.717 47.919  -30.107 1.00 18.28 ? 18  TRP A N   1 
ATOM   2186 C  CA  . TRP B 1 18  ? -15.667 47.500  -28.677 1.00 16.54 ? 18  TRP A CA  1 
ATOM   2187 C  C   . TRP B 1 18  ? -15.530 48.657  -27.726 1.00 17.18 ? 18  TRP A C   1 
ATOM   2188 O  O   . TRP B 1 18  ? -16.007 48.579  -26.589 1.00 19.99 ? 18  TRP A O   1 
ATOM   2189 C  CB  . TRP B 1 18  ? -14.493 46.474  -28.475 1.00 14.94 ? 18  TRP A CB  1 
ATOM   2190 C  CG  . TRP B 1 18  ? -14.627 45.176  -29.337 1.00 12.67 ? 18  TRP A CG  1 
ATOM   2191 C  CD1 . TRP B 1 18  ? -15.735 44.716  -30.029 1.00 13.72 ? 18  TRP A CD1 1 
ATOM   2192 C  CD2 . TRP B 1 18  ? -13.595 44.228  -29.574 1.00 12.90 ? 18  TRP A CD2 1 
ATOM   2193 N  NE1 . TRP B 1 18  ? -15.439 43.505  -30.665 1.00 12.20 ? 18  TRP A NE1 1 
ATOM   2194 C  CE2 . TRP B 1 18  ? -14.127 43.191  -30.374 1.00 13.20 ? 18  TRP A CE2 1 
ATOM   2195 C  CE3 . TRP B 1 18  ? -12.248 44.138  -29.139 1.00 13.15 ? 18  TRP A CE3 1 
ATOM   2196 C  CZ2 . TRP B 1 18  ? -13.359 42.063  -30.780 1.00 11.70 ? 18  TRP A CZ2 1 
ATOM   2197 C  CZ3 . TRP B 1 18  ? -11.515 43.004  -29.513 1.00 12.28 ? 18  TRP A CZ3 1 
ATOM   2198 C  CH2 . TRP B 1 18  ? -12.051 42.019  -30.354 1.00 13.39 ? 18  TRP A CH2 1 
ATOM   2199 N  N   . LYS B 1 19  ? -14.871 49.728  -28.178 1.00 19.73 ? 19  LYS A N   1 
ATOM   2200 C  CA  . LYS B 1 19  ? -14.668 50.940  -27.370 1.00 20.55 ? 19  LYS A CA  1 
ATOM   2201 C  C   . LYS B 1 19  ? -15.990 51.557  -26.925 1.00 27.38 ? 19  LYS A C   1 
ATOM   2202 O  O   . LYS B 1 19  ? -16.060 52.205  -25.868 1.00 25.93 ? 19  LYS A O   1 
ATOM   2203 C  CB  . LYS B 1 19  ? -13.822 51.983  -28.105 1.00 22.96 ? 19  LYS A CB  1 
ATOM   2204 C  CG  . LYS B 1 19  ? -14.391 52.573  -29.424 1.00 24.97 ? 19  LYS A CG  1 
ATOM   2205 C  CD  . LYS B 1 19  ? -13.456 53.601  -30.084 1.00 27.19 ? 19  LYS A CD  1 
ATOM   2206 C  CE  . LYS B 1 19  ? -12.165 53.010  -30.676 1.00 26.93 ? 19  LYS A CE  1 
ATOM   2207 N  NZ  . LYS B 1 19  ? -12.294 52.444  -32.045 1.00 23.42 ? 19  LYS A NZ  1 
ATOM   2208 N  N   . GLU B 1 20  ? -17.058 51.305  -27.697 1.00 25.94 ? 20  GLU A N   1 
ATOM   2209 C  CA  . GLU B 1 20  ? -18.397 51.764  -27.240 1.00 27.38 ? 20  GLU A CA  1 
ATOM   2210 C  C   . GLU B 1 20  ? -18.857 51.244  -25.898 1.00 28.81 ? 20  GLU A C   1 
ATOM   2211 O  O   . GLU B 1 20  ? -19.497 51.978  -25.105 1.00 35.34 ? 20  GLU A O   1 
ATOM   2212 C  CB  . GLU B 1 20  ? -19.466 51.448  -28.280 1.00 24.45 ? 20  GLU A CB  1 
ATOM   2213 C  CG  . GLU B 1 20  ? -19.199 52.186  -29.595 1.00 30.99 ? 20  GLU A CG  1 
ATOM   2214 C  CD  . GLU B 1 20  ? -19.924 51.589  -30.748 1.00 27.66 ? 20  GLU A CD  1 
ATOM   2215 O  OE1 . GLU B 1 20  ? -21.007 50.987  -30.495 1.00 35.12 ? 20  GLU A OE1 1 
ATOM   2216 O  OE2 . GLU B 1 20  ? -19.418 51.739  -31.880 1.00 31.10 ? 20  GLU A OE2 1 
ATOM   2217 N  N   . PHE B 1 21  ? -18.623 49.981  -25.613 1.00 27.20 ? 21  PHE A N   1 
ATOM   2218 C  CA  . PHE B 1 21  ? -19.100 49.477  -24.342 1.00 28.60 ? 21  PHE A CA  1 
ATOM   2219 C  C   . PHE B 1 21  ? -17.927 49.163  -23.444 1.00 27.21 ? 21  PHE A C   1 
ATOM   2220 O  O   . PHE B 1 21  ? -18.152 48.875  -22.296 1.00 26.93 ? 21  PHE A O   1 
ATOM   2221 C  CB  . PHE B 1 21  ? -19.984 48.222  -24.469 1.00 35.15 ? 21  PHE A CB  1 
ATOM   2222 C  CG  . PHE B 1 21  ? -21.145 48.377  -25.419 1.00 46.12 ? 21  PHE A CG  1 
ATOM   2223 C  CD1 . PHE B 1 21  ? -20.991 48.089  -26.799 1.00 51.36 ? 21  PHE A CD1 1 
ATOM   2224 C  CD2 . PHE B 1 21  ? -22.390 48.800  -24.950 1.00 50.72 ? 21  PHE A CD2 1 
ATOM   2225 C  CE1 . PHE B 1 21  ? -22.064 48.240  -27.689 1.00 57.48 ? 21  PHE A CE1 1 
ATOM   2226 C  CE2 . PHE B 1 21  ? -23.467 48.947  -25.829 1.00 60.71 ? 21  PHE A CE2 1 
ATOM   2227 C  CZ  . PHE B 1 21  ? -23.304 48.669  -27.200 1.00 61.82 ? 21  PHE A CZ  1 
ATOM   2228 N  N   . PHE B 1 22  ? -16.705 49.158  -23.997 1.00 23.27 ? 22  PHE A N   1 
ATOM   2229 C  CA  . PHE B 1 22  ? -15.505 48.864  -23.180 1.00 22.82 ? 22  PHE A CA  1 
ATOM   2230 C  C   . PHE B 1 22  ? -14.462 49.944  -23.460 1.00 21.71 ? 22  PHE A C   1 
ATOM   2231 O  O   . PHE B 1 22  ? -13.561 49.778  -24.293 1.00 21.71 ? 22  PHE A O   1 
ATOM   2232 C  CB  . PHE B 1 22  ? -14.979 47.433  -23.471 1.00 20.77 ? 22  PHE A CB  1 
ATOM   2233 C  CG  . PHE B 1 22  ? -15.991 46.332  -23.201 1.00 21.59 ? 22  PHE A CG  1 
ATOM   2234 C  CD1 . PHE B 1 22  ? -16.164 45.836  -21.953 1.00 21.91 ? 22  PHE A CD1 1 
ATOM   2235 C  CD2 . PHE B 1 22  ? -16.762 45.811  -24.232 1.00 21.17 ? 22  PHE A CD2 1 
ATOM   2236 C  CE1 . PHE B 1 22  ? -17.109 44.841  -21.710 1.00 25.68 ? 22  PHE A CE1 1 
ATOM   2237 C  CE2 . PHE B 1 22  ? -17.712 44.801  -24.035 1.00 22.92 ? 22  PHE A CE2 1 
ATOM   2238 C  CZ  . PHE B 1 22  ? -17.905 44.311  -22.763 1.00 24.50 ? 22  PHE A CZ  1 
ATOM   2239 N  N   . PRO B 1 23  ? -14.582 51.113  -22.789 1.00 22.68 ? 23  PRO A N   1 
ATOM   2240 C  CA  . PRO B 1 23  ? -13.693 52.161  -23.248 1.00 21.03 ? 23  PRO A CA  1 
ATOM   2241 C  C   . PRO B 1 23  ? -12.228 51.942  -22.873 1.00 17.55 ? 23  PRO A C   1 
ATOM   2242 O  O   . PRO B 1 23  ? -11.380 52.654  -23.430 1.00 20.12 ? 23  PRO A O   1 
ATOM   2243 C  CB  . PRO B 1 23  ? -14.233 53.444  -22.583 1.00 22.57 ? 23  PRO A CB  1 
ATOM   2244 C  CG  . PRO B 1 23  ? -14.944 52.936  -21.371 1.00 22.05 ? 23  PRO A CG  1 
ATOM   2245 C  CD  . PRO B 1 23  ? -15.393 51.515  -21.621 1.00 24.87 ? 23  PRO A CD  1 
ATOM   2246 N  N   . ILE B 1 24  ? -11.943 50.954  -22.024 1.00 17.05 ? 24  ILE A N   1 
ATOM   2247 C  CA  . ILE B 1 24  ? -10.543 50.515  -21.800 1.00 15.64 ? 24  ILE A CA  1 
ATOM   2248 C  C   . ILE B 1 24  ? -9.892  50.055  -23.148 1.00 16.50 ? 24  ILE A C   1 
ATOM   2249 O  O   . ILE B 1 24  ? -8.654  49.979  -23.285 1.00 15.11 ? 24  ILE A O   1 
ATOM   2250 C  CB  . ILE B 1 24  ? -10.410 49.516  -20.628 1.00 16.10 ? 24  ILE A CB  1 
ATOM   2251 C  CG1 . ILE B 1 24  ? -8.953  49.460  -20.072 1.00 16.27 ? 24  ILE A CG1 1 
ATOM   2252 C  CG2 . ILE B 1 24  ? -10.847 48.104  -21.053 1.00 17.36 ? 24  ILE A CG2 1 
ATOM   2253 C  CD1 . ILE B 1 24  ? -8.443  50.724  -19.384 1.00 18.40 ? 24  ILE A CD1 1 
ATOM   2254 N  N   . ALA B 1 25  ? -10.694 49.856  -24.196 1.00 14.76 ? 25  ALA A N   1 
ATOM   2255 C  CA  . ALA B 1 25  ? -10.139 49.548  -25.487 1.00 15.53 ? 25  ALA A CA  1 
ATOM   2256 C  C   . ALA B 1 25  ? -9.089  50.526  -25.987 1.00 15.17 ? 25  ALA A C   1 
ATOM   2257 O  O   . ALA B 1 25  ? -8.216  50.152  -26.770 1.00 13.91 ? 25  ALA A O   1 
ATOM   2258 C  CB  . ALA B 1 25  ? -11.261 49.494  -26.497 1.00 14.58 ? 25  ALA A CB  1 
ATOM   2259 N  N   . ASP B 1 26  ? -9.208  51.808  -25.588 1.00 16.69 ? 26  ASP A N   1 
ATOM   2260 C  CA  . ASP B 1 26  ? -8.251  52.836  -25.961 1.00 17.42 ? 26  ASP A CA  1 
ATOM   2261 C  C   . ASP B 1 26  ? -7.348  53.186  -24.791 1.00 17.71 ? 26  ASP A C   1 
ATOM   2262 O  O   . ASP B 1 26  ? -6.837  54.285  -24.734 1.00 16.43 ? 26  ASP A O   1 
ATOM   2263 C  CB  . ASP B 1 26  ? -8.986  54.071  -26.481 1.00 22.22 ? 26  ASP A CB  1 
ATOM   2264 C  CG  . ASP B 1 26  ? -9.878  53.762  -27.692 1.00 24.07 ? 26  ASP A CG  1 
ATOM   2265 O  OD1 . ASP B 1 26  ? -9.370  53.122  -28.646 1.00 23.33 ? 26  ASP A OD1 1 
ATOM   2266 O  OD2 . ASP B 1 26  ? -11.092 54.162  -27.664 1.00 27.36 ? 26  ASP A OD2 1 
ATOM   2267 N  N   . GLY B 1 27  ? -7.161  52.234  -23.863 1.00 15.33 ? 27  GLY A N   1 
ATOM   2268 C  CA  . GLY B 1 27  ? -6.325  52.421  -22.709 1.00 15.31 ? 27  GLY A CA  1 
ATOM   2269 C  C   . GLY B 1 27  ? -4.846  52.330  -23.020 1.00 14.08 ? 27  GLY A C   1 
ATOM   2270 O  O   . GLY B 1 27  ? -4.439  52.320  -24.171 1.00 15.81 ? 27  GLY A O   1 
ATOM   2271 N  N   . ASP B 1 28  ? -4.048  52.377  -21.947 1.00 13.64 ? 28  ASP A N   1 
ATOM   2272 C  CA  . ASP B 1 28  ? -2.595  52.562  -22.025 1.00 12.60 ? 28  ASP A CA  1 
ATOM   2273 C  C   . ASP B 1 28  ? -1.881  51.238  -22.048 1.00 12.24 ? 28  ASP A C   1 
ATOM   2274 O  O   . ASP B 1 28  ? -0.691  51.160  -22.431 1.00 12.81 ? 28  ASP A O   1 
ATOM   2275 C  CB  . ASP B 1 28  ? -2.068  53.363  -20.841 1.00 13.43 ? 28  ASP A CB  1 
ATOM   2276 C  CG  . ASP B 1 28  ? -2.308  54.900  -21.002 1.00 14.95 ? 28  ASP A CG  1 
ATOM   2277 O  OD1 . ASP B 1 28  ? -2.670  55.392  -22.102 1.00 18.73 ? 28  ASP A OD1 1 
ATOM   2278 O  OD2 . ASP B 1 28  ? -2.158  55.599  -20.013 1.00 16.93 ? 28  ASP A OD2 1 
ATOM   2279 N  N   . GLN B 1 29  ? -2.589  50.183  -21.644 1.00 9.99  ? 29  GLN A N   1 
ATOM   2280 C  CA  . GLN B 1 29  ? -1.886  48.865  -21.690 1.00 9.69  ? 29  GLN A CA  1 
ATOM   2281 C  C   . GLN B 1 29  ? -2.686  47.805  -22.507 1.00 8.64  ? 29  GLN A C   1 
ATOM   2282 O  O   . GLN B 1 29  ? -2.998  46.696  -22.005 1.00 8.87  ? 29  GLN A O   1 
ATOM   2283 C  CB  . GLN B 1 29  ? -1.620  48.408  -20.272 1.00 10.64 ? 29  GLN A CB  1 
ATOM   2284 C  CG  . GLN B 1 29  ? -0.550  49.276  -19.608 1.00 11.38 ? 29  GLN A CG  1 
ATOM   2285 C  CD  . GLN B 1 29  ? 0.201   48.616  -18.449 1.00 12.65 ? 29  GLN A CD  1 
ATOM   2286 O  OE1 . GLN B 1 29  ? -0.249  47.629  -17.850 1.00 11.27 ? 29  GLN A OE1 1 
ATOM   2287 N  NE2 . GLN B 1 29  ? 1.371   49.209  -18.118 1.00 11.98 ? 29  GLN A NE2 1 
ATOM   2288 N  N   . GLN B 1 30  ? -3.019  48.140  -23.754 1.00 8.37  ? 30  GLN A N   1 
ATOM   2289 C  CA  . GLN B 1 30  ? -3.846  47.266  -24.518 1.00 9.02  ? 30  GLN A CA  1 
ATOM   2290 C  C   . GLN B 1 30  ? -3.045  46.318  -25.365 1.00 8.32  ? 30  GLN A C   1 
ATOM   2291 O  O   . GLN B 1 30  ? -1.902  46.616  -25.763 1.00 9.98  ? 30  GLN A O   1 
ATOM   2292 C  CB  . GLN B 1 30  ? -4.803  48.115  -25.435 1.00 9.23  ? 30  GLN A CB  1 
ATOM   2293 C  CG  . GLN B 1 30  ? -5.896  48.776  -24.624 1.00 10.39 ? 30  GLN A CG  1 
ATOM   2294 C  CD  . GLN B 1 30  ? -6.867  47.729  -24.080 1.00 9.68  ? 30  GLN A CD  1 
ATOM   2295 O  OE1 . GLN B 1 30  ? -7.635  47.116  -24.839 1.00 11.05 ? 30  GLN A OE1 1 
ATOM   2296 N  NE2 . GLN B 1 30  ? -6.851  47.527  -22.765 1.00 9.86  ? 30  GLN A NE2 1 
ATOM   2297 N  N   . SER B 1 31  ? -3.651  45.156  -25.643 1.00 9.04  ? 31  SER A N   1 
ATOM   2298 C  CA  . SER B 1 31  ? -3.044  44.130  -26.460 1.00 8.81  ? 31  SER A CA  1 
ATOM   2299 C  C   . SER B 1 31  ? -3.935  43.768  -27.629 1.00 8.61  ? 31  SER A C   1 
ATOM   2300 O  O   . SER B 1 31  ? -5.144  43.963  -27.614 1.00 9.69  ? 31  SER A O   1 
ATOM   2301 C  CB  . SER B 1 31  ? -2.787  42.846  -25.616 1.00 8.43  ? 31  SER A CB  1 
ATOM   2302 O  OG  . SER B 1 31  ? -1.831  43.120  -24.610 1.00 8.55  ? 31  SER A OG  1 
ATOM   2303 N  N   . PRO B 1 32  ? -3.363  43.192  -28.641 1.00 9.11  ? 32  PRO A N   1 
ATOM   2304 C  CA  . PRO B 1 32  ? -1.970  42.908  -28.846 1.00 9.08  ? 32  PRO A CA  1 
ATOM   2305 C  C   . PRO B 1 32  ? -1.185  44.150  -29.272 1.00 9.96  ? 32  PRO A C   1 
ATOM   2306 O  O   . PRO B 1 32  ? -1.759  45.244  -29.330 1.00 10.22 ? 32  PRO A O   1 
ATOM   2307 C  CB  . PRO B 1 32  ? -2.025  41.904  -30.034 1.00 9.63  ? 32  PRO A CB  1 
ATOM   2308 C  CG  . PRO B 1 32  ? -3.151  42.420  -30.899 1.00 9.96  ? 32  PRO A CG  1 
ATOM   2309 C  CD  . PRO B 1 32  ? -4.185  42.873  -29.844 1.00 8.76  ? 32  PRO A CD  1 
ATOM   2310 N  N   . ILE B 1 33  ? 0.095   43.969  -29.655 1.00 8.46  ? 33  ILE A N   1 
ATOM   2311 C  CA  . ILE B 1 33  ? 0.959   45.121  -29.972 1.00 9.32  ? 33  ILE A CA  1 
ATOM   2312 C  C   . ILE B 1 33  ? 1.790   44.710  -31.159 1.00 9.33  ? 33  ILE A C   1 
ATOM   2313 O  O   . ILE B 1 33  ? 1.866   43.525  -31.504 1.00 9.57  ? 33  ILE A O   1 
ATOM   2314 C  CB  . ILE B 1 33  ? 1.953   45.478  -28.808 1.00 8.59  ? 33  ILE A CB  1 
ATOM   2315 C  CG1 . ILE B 1 33  ? 2.869   44.297  -28.446 1.00 9.53  ? 33  ILE A CG1 1 
ATOM   2316 C  CG2 . ILE B 1 33  ? 1.157   45.949  -27.575 1.00 8.37  ? 33  ILE A CG2 1 
ATOM   2317 C  CD1 . ILE B 1 33  ? 4.031   44.705  -27.534 1.00 8.89  ? 33  ILE A CD1 1 
ATOM   2318 N  N   . GLU B 1 34  ? 2.467   45.689  -31.742 1.00 10.00 ? 34  GLU A N   1 
ATOM   2319 C  CA  . GLU B 1 34  ? 3.567   45.431  -32.674 1.00 10.93 ? 34  GLU A CA  1 
ATOM   2320 C  C   . GLU B 1 34  ? 4.881   45.343  -31.871 1.00 11.87 ? 34  GLU A C   1 
ATOM   2321 O  O   . GLU B 1 34  ? 5.134   46.180  -30.942 1.00 12.96 ? 34  GLU A O   1 
ATOM   2322 C  CB  . GLU B 1 34  ? 3.685   46.604  -33.650 1.00 11.47 ? 34  GLU A CB  1 
ATOM   2323 C  CG  . GLU B 1 34  ? 2.518   46.655  -34.666 1.00 11.69 ? 34  GLU A CG  1 
ATOM   2324 C  CD  . GLU B 1 34  ? 2.796   47.668  -35.725 1.00 14.44 ? 34  GLU A CD  1 
ATOM   2325 O  OE1 . GLU B 1 34  ? 3.537   47.310  -36.704 1.00 15.68 ? 34  GLU A OE1 1 
ATOM   2326 O  OE2 . GLU B 1 34  ? 2.368   48.833  -35.544 1.00 14.37 ? 34  GLU A OE2 1 
ATOM   2327 N  N   . ILE B 1 35  ? 5.698   44.370  -32.212 1.00 11.24 ? 35  ILE A N   1 
ATOM   2328 C  CA  . ILE B 1 35  ? 6.946   44.184  -31.470 1.00 12.04 ? 35  ILE A CA  1 
ATOM   2329 C  C   . ILE B 1 35  ? 8.080   44.623  -32.383 1.00 13.40 ? 35  ILE A C   1 
ATOM   2330 O  O   . ILE B 1 35  ? 8.296   43.984  -33.419 1.00 13.44 ? 35  ILE A O   1 
ATOM   2331 C  CB  . ILE B 1 35  ? 7.143   42.699  -31.044 1.00 12.88 ? 35  ILE A CB  1 
ATOM   2332 C  CG1 . ILE B 1 35  ? 6.004   42.328  -30.068 1.00 13.04 ? 35  ILE A CG1 1 
ATOM   2333 C  CG2 . ILE B 1 35  ? 8.565   42.580  -30.452 1.00 13.73 ? 35  ILE A CG2 1 
ATOM   2334 C  CD1 . ILE B 1 35  ? 5.912   40.861  -29.714 1.00 13.62 ? 35  ILE A CD1 1 
ATOM   2335 N  N   . LYS B 1 36  ? 8.740   45.727  -31.993 1.00 14.13 ? 36  LYS A N   1 
ATOM   2336 C  CA  . LYS B 1 36  ? 9.867   46.317  -32.795 1.00 15.83 ? 36  LYS A CA  1 
ATOM   2337 C  C   . LYS B 1 36  ? 11.132  45.809  -32.165 1.00 16.97 ? 36  LYS A C   1 
ATOM   2338 O  O   . LYS B 1 36  ? 11.526  46.339  -31.135 1.00 17.65 ? 36  LYS A O   1 
ATOM   2339 C  CB  . LYS B 1 36  ? 9.848   47.849  -32.712 1.00 16.61 ? 36  LYS A CB  1 
ATOM   2340 C  CG  . LYS B 1 36  ? 10.963  48.591  -33.479 1.00 20.29 ? 36  LYS A CG  1 
ATOM   2341 C  CD  . LYS B 1 36  ? 10.631  50.077  -33.507 1.00 19.38 ? 36  LYS A CD  1 
ATOM   2342 C  CE  . LYS B 1 36  ? 9.659   50.342  -34.686 1.00 24.10 ? 36  LYS A CE  1 
ATOM   2343 N  NZ  . LYS B 1 36  ? 9.516   51.801  -35.048 1.00 19.02 ? 36  LYS A NZ  1 
ATOM   2344 N  N   . THR B 1 37  ? 11.721  44.768  -32.748 1.00 17.42 ? 37  THR A N   1 
ATOM   2345 C  CA  . THR B 1 37  ? 12.856  44.091  -32.087 1.00 20.57 ? 37  THR A CA  1 
ATOM   2346 C  C   . THR B 1 37  ? 14.098  44.996  -31.834 1.00 23.19 ? 37  THR A C   1 
ATOM   2347 O  O   . THR B 1 37  ? 14.848  44.781  -30.843 1.00 22.93 ? 37  THR A O   1 
ATOM   2348 C  CB  . THR B 1 37  ? 13.299  42.799  -32.761 1.00 18.56 ? 37  THR A CB  1 
ATOM   2349 O  OG1 . THR B 1 37  ? 13.702  43.060  -34.110 1.00 20.86 ? 37  THR A OG1 1 
ATOM   2350 C  CG2 . THR B 1 37  ? 12.150  41.781  -32.821 1.00 17.91 ? 37  THR A CG2 1 
ATOM   2351 N  N   . LYS B 1 38  ? 14.339  46.009  -32.663 1.00 25.83 ? 38  LYS A N   1 
ATOM   2352 C  CA  . LYS B 1 38  ? 15.516  46.834  -32.388 1.00 30.69 ? 38  LYS A CA  1 
ATOM   2353 C  C   . LYS B 1 38  ? 15.366  47.601  -31.060 1.00 29.67 ? 38  LYS A C   1 
ATOM   2354 O  O   . LYS B 1 38  ? 16.364  47.924  -30.408 1.00 31.46 ? 38  LYS A O   1 
ATOM   2355 C  CB  . LYS B 1 38  ? 15.908  47.712  -33.610 1.00 37.70 ? 38  LYS A CB  1 
ATOM   2356 C  CG  . LYS B 1 38  ? 15.163  49.032  -33.784 1.00 45.54 ? 38  LYS A CG  1 
ATOM   2357 C  CD  . LYS B 1 38  ? 15.542  49.717  -35.098 1.00 53.86 ? 38  LYS A CD  1 
ATOM   2358 C  CE  . LYS B 1 38  ? 14.535  50.800  -35.469 1.00 60.05 ? 38  LYS A CE  1 
ATOM   2359 N  NZ  . LYS B 1 38  ? 14.724  51.987  -34.582 1.00 70.98 ? 38  LYS A NZ  1 
ATOM   2360 N  N   . GLU B 1 39  ? 14.131  47.876  -30.645 1.00 32.25 ? 39  GLU A N   1 
ATOM   2361 C  CA  . GLU B 1 39  ? 13.895  48.619  -29.392 1.00 33.74 ? 39  GLU A CA  1 
ATOM   2362 C  C   . GLU B 1 39  ? 13.912  47.690  -28.157 1.00 29.28 ? 39  GLU A C   1 
ATOM   2363 O  O   . GLU B 1 39  ? 14.086  48.142  -27.033 1.00 30.90 ? 39  GLU A O   1 
ATOM   2364 C  CB  . GLU B 1 39  ? 12.574  49.411  -29.425 1.00 38.90 ? 39  GLU A CB  1 
ATOM   2365 C  CG  . GLU B 1 39  ? 12.429  50.443  -30.537 1.00 52.59 ? 39  GLU A CG  1 
ATOM   2366 C  CD  . GLU B 1 39  ? 13.242  51.725  -30.361 1.00 64.37 ? 39  GLU A CD  1 
ATOM   2367 O  OE1 . GLU B 1 39  ? 13.415  52.437  -31.383 1.00 73.56 ? 39  GLU A OE1 1 
ATOM   2368 O  OE2 . GLU B 1 39  ? 13.705  52.042  -29.231 1.00 70.64 ? 39  GLU A OE2 1 
ATOM   2369 N  N   . VAL B 1 40  ? 13.755  46.399  -28.372 1.00 23.50 ? 40  VAL A N   1 
ATOM   2370 C  CA  . VAL B 1 40  ? 13.558  45.457  -27.246 1.00 20.86 ? 40  VAL A CA  1 
ATOM   2371 C  C   . VAL B 1 40  ? 14.879  45.258  -26.537 1.00 20.01 ? 40  VAL A C   1 
ATOM   2372 O  O   . VAL B 1 40  ? 15.870  44.940  -27.168 1.00 21.06 ? 40  VAL A O   1 
ATOM   2373 C  CB  . VAL B 1 40  ? 13.098  44.073  -27.772 1.00 17.88 ? 40  VAL A CB  1 
ATOM   2374 C  CG1 . VAL B 1 40  ? 13.106  43.059  -26.661 1.00 19.03 ? 40  VAL A CG1 1 
ATOM   2375 C  CG2 . VAL B 1 40  ? 11.703  44.160  -28.386 1.00 18.84 ? 40  VAL A CG2 1 
ATOM   2376 N  N   . LYS B 1 41  ? 14.862  45.287  -25.224 1.00 19.07 ? 41  LYS A N   1 
ATOM   2377 C  CA  . LYS B 1 41  ? 16.129  45.047  -24.491 1.00 21.65 ? 41  LYS A CA  1 
ATOM   2378 C  C   . LYS B 1 41  ? 16.110  43.671  -23.816 1.00 17.74 ? 41  LYS A C   1 
ATOM   2379 O  O   . LYS B 1 41  ? 15.079  43.287  -23.228 1.00 16.39 ? 41  LYS A O   1 
ATOM   2380 C  CB  . LYS B 1 41  ? 16.334  46.132  -23.401 1.00 25.73 ? 41  LYS A CB  1 
ATOM   2381 C  CG  . LYS B 1 41  ? 16.687  47.526  -23.959 1.00 30.59 ? 41  LYS A CG  1 
ATOM   2382 C  CD  . LYS B 1 41  ? 16.969  48.524  -22.817 1.00 39.24 ? 41  LYS A CD  1 
ATOM   2383 C  CE  . LYS B 1 41  ? 18.397  48.390  -22.240 1.00 46.19 ? 41  LYS A CE  1 
ATOM   2384 N  NZ  . LYS B 1 41  ? 18.618  47.448  -21.082 1.00 46.37 ? 41  LYS A NZ  1 
ATOM   2385 N  N   . TYR B 1 42  ? 17.236  42.949  -23.862 1.00 17.56 ? 42  TYR A N   1 
ATOM   2386 C  CA  . TYR B 1 42  ? 17.364  41.700  -23.079 1.00 16.28 ? 42  TYR A CA  1 
ATOM   2387 C  C   . TYR B 1 42  ? 17.368  42.094  -21.621 1.00 15.93 ? 42  TYR A C   1 
ATOM   2388 O  O   . TYR B 1 42  ? 18.053  43.055  -21.243 1.00 16.56 ? 42  TYR A O   1 
ATOM   2389 C  CB  . TYR B 1 42  ? 18.709  41.032  -23.438 1.00 15.50 ? 42  TYR A CB  1 
ATOM   2390 C  CG  . TYR B 1 42  ? 19.130  39.958  -22.490 1.00 16.18 ? 42  TYR A CG  1 
ATOM   2391 C  CD1 . TYR B 1 42  ? 18.441  38.751  -22.403 1.00 15.78 ? 42  TYR A CD1 1 
ATOM   2392 C  CD2 . TYR B 1 42  ? 20.258  40.123  -21.649 1.00 17.47 ? 42  TYR A CD2 1 
ATOM   2393 C  CE1 . TYR B 1 42  ? 18.846  37.729  -21.514 1.00 17.46 ? 42  TYR A CE1 1 
ATOM   2394 C  CE2 . TYR B 1 42  ? 20.675  39.108  -20.766 1.00 17.36 ? 42  TYR A CE2 1 
ATOM   2395 C  CZ  . TYR B 1 42  ? 19.999  37.929  -20.710 1.00 19.69 ? 42  TYR A CZ  1 
ATOM   2396 O  OH  . TYR B 1 42  ? 20.361  36.930  -19.847 1.00 23.40 ? 42  TYR A OH  1 
ATOM   2397 N  N   . ASP B 1 43  ? 16.659  41.352  -20.789 1.00 15.31 ? 43  ASP A N   1 
ATOM   2398 C  CA  . ASP B 1 43  ? 16.662  41.618  -19.361 1.00 14.62 ? 43  ASP A CA  1 
ATOM   2399 C  C   . ASP B 1 43  ? 17.244  40.408  -18.648 1.00 14.76 ? 43  ASP A C   1 
ATOM   2400 O  O   . ASP B 1 43  ? 16.590  39.350  -18.517 1.00 14.32 ? 43  ASP A O   1 
ATOM   2401 C  CB  . ASP B 1 43  ? 15.220  41.875  -18.881 1.00 16.11 ? 43  ASP A CB  1 
ATOM   2402 C  CG  . ASP B 1 43  ? 15.156  42.298  -17.439 1.00 17.84 ? 43  ASP A CG  1 
ATOM   2403 O  OD1 . ASP B 1 43  ? 16.148  42.216  -16.681 1.00 17.56 ? 43  ASP A OD1 1 
ATOM   2404 O  OD2 . ASP B 1 43  ? 14.075  42.759  -17.027 1.00 19.89 ? 43  ASP A OD2 1 
ATOM   2405 N  N   . SER B 1 44  ? 18.447  40.575  -18.095 1.00 15.71 ? 44  SER A N   1 
ATOM   2406 C  CA  . SER B 1 44  ? 19.033  39.419  -17.368 1.00 16.36 ? 44  SER A CA  1 
ATOM   2407 C  C   . SER B 1 44  ? 18.358  39.105  -16.015 1.00 15.87 ? 44  SER A C   1 
ATOM   2408 O  O   . SER B 1 44  ? 18.634  38.061  -15.426 1.00 18.36 ? 44  SER A O   1 
ATOM   2409 C  CB  . SER B 1 44  ? 20.561  39.652  -17.137 1.00 18.12 ? 44  SER A CB  1 
ATOM   2410 O  OG  . SER B 1 44  ? 20.692  40.863  -16.419 1.00 20.51 ? 44  SER A OG  1 
ATOM   2411 N  N   . SER B 1 45  ? 17.447  39.948  -15.522 1.00 15.49 ? 45  SER A N   1 
ATOM   2412 C  CA  . SER B 1 45  ? 16.758  39.604  -14.284 1.00 17.91 ? 45  SER A CA  1 
ATOM   2413 C  C   . SER B 1 45  ? 15.604  38.605  -14.515 1.00 17.53 ? 45  SER A C   1 
ATOM   2414 O  O   . SER B 1 45  ? 15.111  38.000  -13.544 1.00 21.02 ? 45  SER A O   1 
ATOM   2415 C  CB  . SER B 1 45  ? 16.257  40.839  -13.544 1.00 16.56 ? 45  SER A CB  1 
ATOM   2416 O  OG  . SER B 1 45  ? 15.113  41.385  -14.226 1.00 19.79 ? 45  SER A OG  1 
ATOM   2417 N  N   . LEU B 1 46  ? 15.245  38.336  -15.787 1.00 16.73 ? 46  LEU A N   1 
ATOM   2418 C  CA  . LEU B 1 46  ? 14.238  37.311  -16.060 1.00 15.24 ? 46  LEU A CA  1 
ATOM   2419 C  C   . LEU B 1 46  ? 14.708  35.916  -15.643 1.00 15.97 ? 46  LEU A C   1 
ATOM   2420 O  O   . LEU B 1 46  ? 15.827  35.457  -15.979 1.00 19.26 ? 46  LEU A O   1 
ATOM   2421 C  CB  . LEU B 1 46  ? 13.834  37.343  -17.541 1.00 12.64 ? 46  LEU A CB  1 
ATOM   2422 C  CG  . LEU B 1 46  ? 13.153  38.653  -18.044 1.00 11.10 ? 46  LEU A CG  1 
ATOM   2423 C  CD1 . LEU B 1 46  ? 13.093  38.630  -19.545 1.00 10.37 ? 46  LEU A CD1 1 
ATOM   2424 C  CD2 . LEU B 1 46  ? 11.697  38.778  -17.492 1.00 12.22 ? 46  LEU A CD2 1 
ATOM   2425 N  N   . ARG B 1 47  ? 13.876  35.243  -14.889 1.00 16.50 ? 47  ARG A N   1 
ATOM   2426 C  CA  . ARG B 1 47  ? 14.208  33.924  -14.356 1.00 17.83 ? 47  ARG A CA  1 
ATOM   2427 C  C   . ARG B 1 47  ? 13.906  32.880  -15.425 1.00 15.64 ? 47  ARG A C   1 
ATOM   2428 O  O   . ARG B 1 47  ? 13.168  33.156  -16.384 1.00 15.95 ? 47  ARG A O   1 
ATOM   2429 C  CB  . ARG B 1 47  ? 13.444  33.712  -13.040 1.00 19.40 ? 47  ARG A CB  1 
ATOM   2430 C  CG  . ARG B 1 47  ? 13.906  34.600  -11.848 1.00 26.27 ? 47  ARG A CG  1 
ATOM   2431 C  CD  . ARG B 1 47  ? 15.361  34.266  -11.395 1.00 34.59 ? 47  ARG A CD  1 
ATOM   2432 N  NE  . ARG B 1 47  ? 15.530  32.804  -11.113 1.00 43.94 ? 47  ARG A NE  1 
ATOM   2433 C  CZ  . ARG B 1 47  ? 16.667  32.080  -11.191 1.00 49.58 ? 47  ARG A CZ  1 
ATOM   2434 N  NH1 . ARG B 1 47  ? 16.639  30.767  -10.949 1.00 50.79 ? 47  ARG A NH1 1 
ATOM   2435 N  NH2 . ARG B 1 47  ? 17.833  32.630  -11.540 1.00 54.34 ? 47  ARG A NH2 1 
ATOM   2436 N  N   . PRO B 1 48  ? 14.463  31.660  -15.307 1.00 17.08 ? 48  PRO A N   1 
ATOM   2437 C  CA  . PRO B 1 48  ? 14.128  30.629  -16.320 1.00 15.83 ? 48  PRO A CA  1 
ATOM   2438 C  C   . PRO B 1 48  ? 12.590  30.412  -16.372 1.00 14.37 ? 48  PRO A C   1 
ATOM   2439 O  O   . PRO B 1 48  ? 11.938  30.451  -15.324 1.00 14.77 ? 48  PRO A O   1 
ATOM   2440 C  CB  . PRO B 1 48  ? 14.828  29.375  -15.808 1.00 17.42 ? 48  PRO A CB  1 
ATOM   2441 C  CG  . PRO B 1 48  ? 15.901  29.890  -14.916 1.00 17.81 ? 48  PRO A CG  1 
ATOM   2442 C  CD  . PRO B 1 48  ? 15.391  31.137  -14.273 1.00 16.60 ? 48  PRO A CD  1 
ATOM   2443 N  N   . LEU B 1 49  ? 12.076  30.316  -17.580 1.00 14.00 ? 49  LEU A N   1 
ATOM   2444 C  CA  . LEU B 1 49  ? 10.618  30.073  -17.738 1.00 14.27 ? 49  LEU A CA  1 
ATOM   2445 C  C   . LEU B 1 49  ? 10.352  28.618  -17.443 1.00 14.96 ? 49  LEU A C   1 
ATOM   2446 O  O   . LEU B 1 49  ? 11.065  27.771  -17.973 1.00 16.53 ? 49  LEU A O   1 
ATOM   2447 C  CB  . LEU B 1 49  ? 10.167  30.327  -19.156 1.00 14.35 ? 49  LEU A CB  1 
ATOM   2448 C  CG  . LEU B 1 49  ? 8.693   30.560  -19.357 1.00 13.42 ? 49  LEU A CG  1 
ATOM   2449 C  CD1 . LEU B 1 49  ? 8.180   31.823  -18.679 1.00 12.74 ? 49  LEU A CD1 1 
ATOM   2450 C  CD2 . LEU B 1 49  ? 8.487   30.677  -20.872 1.00 13.41 ? 49  LEU A CD2 1 
ATOM   2451 N  N   . SER B 1 50  ? 9.362   28.343  -16.596 1.00 13.47 ? 50  SER A N   1 
ATOM   2452 C  CA  . SER B 1 50  ? 8.999   26.986  -16.252 1.00 11.81 ? 50  SER A CA  1 
ATOM   2453 C  C   . SER B 1 50  ? 7.603   26.709  -16.703 1.00 13.20 ? 50  SER A C   1 
ATOM   2454 O  O   . SER B 1 50  ? 6.665   27.444  -16.291 1.00 11.41 ? 50  SER A O   1 
ATOM   2455 C  CB  . SER B 1 50  ? 9.101   26.800  -14.720 1.00 13.03 ? 50  SER A CB  1 
ATOM   2456 O  OG  . SER B 1 50  ? 8.645   25.508  -14.298 1.00 11.74 ? 50  SER A OG  1 
ATOM   2457 N  N   . ILE B 1 51  ? 7.449   25.656  -17.518 1.00 11.77 ? 51  ILE A N   1 
ATOM   2458 C  CA  . ILE B 1 51  ? 6.110   25.285  -18.005 1.00 11.90 ? 51  ILE A CA  1 
ATOM   2459 C  C   . ILE B 1 51  ? 5.944   23.808  -17.758 1.00 13.10 ? 51  ILE A C   1 
ATOM   2460 O  O   . ILE B 1 51  ? 6.745   23.052  -18.230 1.00 13.03 ? 51  ILE A O   1 
ATOM   2461 C  CB  . ILE B 1 51  ? 5.954   25.512  -19.508 1.00 11.60 ? 51  ILE A CB  1 
ATOM   2462 C  CG1 . ILE B 1 51  ? 6.292   26.958  -19.883 1.00 11.69 ? 51  ILE A CG1 1 
ATOM   2463 C  CG2 . ILE B 1 51  ? 4.469   25.200  -19.926 1.00 10.91 ? 51  ILE A CG2 1 
ATOM   2464 C  CD1 . ILE B 1 51  ? 6.140   27.334  -21.366 1.00 13.64 ? 51  ILE A CD1 1 
ATOM   2465 N  N   . LYS B 1 52  ? 4.905   23.412  -17.018 1.00 12.20 ? 52  LYS A N   1 
ATOM   2466 C  CA  . LYS B 1 52  ? 4.637   22.014  -16.788 1.00 13.45 ? 52  LYS A CA  1 
ATOM   2467 C  C   . LYS B 1 52  ? 3.131   21.808  -17.007 1.00 13.09 ? 52  LYS A C   1 
ATOM   2468 O  O   . LYS B 1 52  ? 2.333   22.460  -16.289 1.00 13.87 ? 52  LYS A O   1 
ATOM   2469 C  CB  . LYS B 1 52  ? 5.027   21.663  -15.338 1.00 17.79 ? 52  LYS A CB  1 
ATOM   2470 C  CG  . LYS B 1 52  ? 4.629   20.246  -14.931 1.00 23.49 ? 52  LYS A CG  1 
ATOM   2471 C  CD  . LYS B 1 52  ? 4.381   20.122  -13.412 1.00 30.71 ? 52  LYS A CD  1 
ATOM   2472 C  CE  . LYS B 1 52  ? 3.982   18.697  -12.953 1.00 27.57 ? 52  LYS A CE  1 
ATOM   2473 N  NZ  . LYS B 1 52  ? 2.563   18.247  -13.259 1.00 22.44 ? 52  LYS A NZ  1 
ATOM   2474 N  N   . TYR B 1 53  ? 2.770   20.965  -17.963 0.50 8.96  ? 53  TYR A N   1 
ATOM   2475 C  CA  . TYR B 1 53  ? 1.385   20.735  -18.258 0.50 8.19  ? 53  TYR A CA  1 
ATOM   2476 C  C   . TYR B 1 53  ? 1.143   19.254  -18.201 0.50 8.68  ? 53  TYR A C   1 
ATOM   2477 O  O   . TYR B 1 53  ? 1.875   18.480  -18.728 0.50 8.16  ? 53  TYR A O   1 
ATOM   2478 C  CB  . TYR B 1 53  ? 0.953   21.279  -19.621 0.50 6.85  ? 53  TYR A CB  1 
ATOM   2479 C  CG  . TYR B 1 53  ? 1.049   22.803  -19.812 0.50 5.59  ? 53  TYR A CG  1 
ATOM   2480 C  CD1 . TYR B 1 53  ? 0.723   23.699  -18.789 0.50 5.23  ? 53  TYR A CD1 1 
ATOM   2481 C  CD2 . TYR B 1 53  ? 1.477   23.320  -21.021 0.50 5.20  ? 53  TYR A CD2 1 
ATOM   2482 C  CE1 . TYR B 1 53  ? 0.801   25.058  -19.005 0.50 4.77  ? 53  TYR A CE1 1 
ATOM   2483 C  CE2 . TYR B 1 53  ? 1.529   24.680  -21.264 0.50 4.63  ? 53  TYR A CE2 1 
ATOM   2484 C  CZ  . TYR B 1 53  ? 1.182   25.557  -20.236 0.50 4.69  ? 53  TYR A CZ  1 
ATOM   2485 O  OH  . TYR B 1 53  ? 1.331   26.872  -20.538 0.50 3.92  ? 53  TYR A OH  1 
ATOM   2486 N  N   . ASP B 1 54  ? 0.033   18.900  -17.600 1.00 10.83 ? 54  ASP A N   1 
ATOM   2487 C  CA  . ASP B 1 54  ? -0.402  17.501  -17.427 1.00 11.82 ? 54  ASP A CA  1 
ATOM   2488 C  C   . ASP B 1 54  ? -1.527  17.230  -18.416 1.00 12.18 ? 54  ASP A C   1 
ATOM   2489 O  O   . ASP B 1 54  ? -2.529  17.943  -18.440 1.00 13.08 ? 54  ASP A O   1 
ATOM   2490 C  CB  . ASP B 1 54  ? -0.953  17.378  -15.986 1.00 13.07 ? 54  ASP A CB  1 
ATOM   2491 C  CG  . ASP B 1 54  ? -1.256  15.950  -15.577 1.00 14.89 ? 54  ASP A CG  1 
ATOM   2492 O  OD1 . ASP B 1 54  ? -1.719  15.149  -16.449 1.00 14.34 ? 54  ASP A OD1 1 
ATOM   2493 O  OD2 . ASP B 1 54  ? -1.094  15.687  -14.317 1.00 15.59 ? 54  ASP A OD2 1 
ATOM   2494 N  N   . PRO B 1 55  ? -1.354  16.255  -19.298 1.00 13.11 ? 55  PRO A N   1 
ATOM   2495 C  CA  . PRO B 1 55  ? -2.385  15.987  -20.295 1.00 12.72 ? 55  PRO A CA  1 
ATOM   2496 C  C   . PRO B 1 55  ? -3.765  15.659  -19.666 1.00 15.10 ? 55  PRO A C   1 
ATOM   2497 O  O   . PRO B 1 55  ? -4.798  15.831  -20.325 1.00 14.01 ? 55  PRO A O   1 
ATOM   2498 C  CB  . PRO B 1 55  ? -1.804  14.812  -21.093 1.00 13.70 ? 55  PRO A CB  1 
ATOM   2499 C  CG  . PRO B 1 55  ? -0.312  14.957  -20.927 1.00 13.74 ? 55  PRO A CG  1 
ATOM   2500 C  CD  . PRO B 1 55  ? -0.150  15.418  -19.492 1.00 13.73 ? 55  PRO A CD  1 
ATOM   2501 N  N   . SER B 1 56  ? -3.790  15.222  -18.403 1.00 14.04 ? 56  SER A N   1 
ATOM   2502 C  CA  . SER B 1 56  ? -5.091  14.826  -17.849 1.00 15.77 ? 56  SER A CA  1 
ATOM   2503 C  C   . SER B 1 56  ? -5.845  16.048  -17.338 1.00 16.13 ? 56  SER A C   1 
ATOM   2504 O  O   . SER B 1 56  ? -7.056  15.914  -17.014 1.00 14.57 ? 56  SER A O   1 
ATOM   2505 C  CB  . SER B 1 56  ? -4.923  13.805  -16.680 1.00 17.49 ? 56  SER A CB  1 
ATOM   2506 O  OG  . SER B 1 56  ? -4.305  14.443  -15.577 1.00 16.68 ? 56  SER A OG  1 
ATOM   2507 N  N   . SER B 1 57  ? -5.171  17.216  -17.301 1.00 12.10 ? 57  SER A N   1 
ATOM   2508 C  CA  . SER B 1 57  ? -5.853  18.457  -16.922 1.00 12.02 ? 57  SER A CA  1 
ATOM   2509 C  C   . SER B 1 57  ? -6.970  18.898  -17.902 1.00 11.58 ? 57  SER A C   1 
ATOM   2510 O  O   . SER B 1 57  ? -7.928  19.546  -17.486 1.00 12.36 ? 57  SER A O   1 
ATOM   2511 C  CB  . SER B 1 57  ? -4.826  19.609  -16.816 1.00 12.71 ? 57  SER A CB  1 
ATOM   2512 O  OG  . SER B 1 57  ? -3.923  19.412  -15.736 1.00 14.03 ? 57  SER A OG  1 
ATOM   2513 N  N   . ALA B 1 58  ? -6.845  18.626  -19.185 1.00 10.36 ? 58  ALA A N   1 
ATOM   2514 C  CA  . ALA B 1 58  ? -7.794  19.098  -20.199 1.00 11.75 ? 58  ALA A CA  1 
ATOM   2515 C  C   . ALA B 1 58  ? -9.123  18.352  -19.983 1.00 12.90 ? 58  ALA A C   1 
ATOM   2516 O  O   . ALA B 1 58  ? -9.120  17.125  -19.719 1.00 15.06 ? 58  ALA A O   1 
ATOM   2517 C  CB  . ALA B 1 58  ? -7.267  18.777  -21.590 1.00 10.40 ? 58  ALA A CB  1 
ATOM   2518 N  N   . LYS B 1 59  ? -10.238 19.065  -20.059 1.00 12.18 ? 59  LYS A N   1 
ATOM   2519 C  CA  . LYS B 1 59  ? -11.529 18.415  -19.827 1.00 12.72 ? 59  LYS A CA  1 
ATOM   2520 C  C   . LYS B 1 59  ? -12.483 18.513  -21.017 1.00 11.83 ? 59  LYS A C   1 
ATOM   2521 O  O   . LYS B 1 59  ? -13.095 17.501  -21.366 1.00 11.68 ? 59  LYS A O   1 
ATOM   2522 C  CB  . LYS B 1 59  ? -12.153 18.991  -18.570 1.00 14.12 ? 59  LYS A CB  1 
ATOM   2523 C  CG  . LYS B 1 59  ? -11.348 18.577  -17.310 1.00 17.20 ? 59  LYS A CG  1 
ATOM   2524 C  CD  . LYS B 1 59  ? -11.112 17.032  -17.147 1.00 19.30 ? 59  LYS A CD  1 
ATOM   2525 C  CE  . LYS B 1 59  ? -10.052 16.761  -16.044 1.00 19.42 ? 59  LYS A CE  1 
ATOM   2526 N  NZ  . LYS B 1 59  ? -9.650  15.321  -15.860 1.00 20.48 ? 59  LYS A NZ  1 
ATOM   2527 N  N   . ILE B 1 60  ? -12.669 19.715  -21.564 1.00 11.20 ? 60  ILE A N   1 
ATOM   2528 C  CA  . ILE B 1 60  ? -13.709 19.902  -22.575 1.00 12.54 ? 60  ILE A CA  1 
ATOM   2529 C  C   . ILE B 1 60  ? -13.205 20.890  -23.623 1.00 13.25 ? 60  ILE A C   1 
ATOM   2530 O  O   . ILE B 1 60  ? -12.469 21.828  -23.308 1.00 12.65 ? 60  ILE A O   1 
ATOM   2531 C  CB  . ILE B 1 60  ? -15.050 20.477  -21.993 1.00 14.30 ? 60  ILE A CB  1 
ATOM   2532 C  CG1 . ILE B 1 60  ? -14.842 21.896  -21.368 1.00 19.36 ? 60  ILE A CG1 1 
ATOM   2533 C  CG2 . ILE B 1 60  ? -15.670 19.448  -21.010 1.00 14.33 ? 60  ILE A CG2 1 
ATOM   2534 C  CD1 . ILE B 1 60  ? -15.994 22.960  -21.313 1.00 24.13 ? 60  ILE A CD1 1 
ATOM   2535 N  N   . ILE B 1 61  ? -13.695 20.698  -24.850 1.00 11.62 ? 61  ILE A N   1 
ATOM   2536 C  CA  . ILE B 1 61  ? -13.438 21.667  -25.883 1.00 10.90 ? 61  ILE A CA  1 
ATOM   2537 C  C   . ILE B 1 61  ? -14.813 22.122  -26.364 1.00 11.99 ? 61  ILE A C   1 
ATOM   2538 O  O   . ILE B 1 61  ? -15.747 21.338  -26.444 1.00 11.84 ? 61  ILE A O   1 
ATOM   2539 C  CB  . ILE B 1 61  ? -12.580 21.136  -27.065 1.00 10.73 ? 61  ILE A CB  1 
ATOM   2540 C  CG1 . ILE B 1 61  ? -12.084 22.338  -27.913 1.00 9.68  ? 61  ILE A CG1 1 
ATOM   2541 C  CG2 . ILE B 1 61  ? -13.342 20.020  -27.880 1.00 10.27 ? 61  ILE A CG2 1 
ATOM   2542 C  CD1 . ILE B 1 61  ? -11.222 21.926  -29.088 1.00 9.94  ? 61  ILE A CD1 1 
ATOM   2543 N  N   . SER B 1 62  ? -14.914 23.414  -26.571 1.00 11.95 ? 62  SER A N   1 
ATOM   2544 C  CA  . SER B 1 62  ? -16.178 24.023  -26.929 1.00 12.88 ? 62  SER A CA  1 
ATOM   2545 C  C   . SER B 1 62  ? -16.018 25.118  -27.940 1.00 14.33 ? 62  SER A C   1 
ATOM   2546 O  O   . SER B 1 62  ? -14.890 25.613  -28.152 1.00 14.47 ? 62  SER A O   1 
ATOM   2547 C  CB  . SER B 1 62  ? -16.851 24.615  -25.687 1.00 13.13 ? 62  SER A CB  1 
ATOM   2548 O  OG  . SER B 1 62  ? -16.118 25.710  -25.115 1.00 13.53 ? 62  SER A OG  1 
ATOM   2549 N  N   . ASN B 1 63  ? -17.138 25.474  -28.594 1.00 14.05 ? 63  ASN A N   1 
ATOM   2550 C  CA  . ASN B 1 63  ? -17.180 26.654  -29.461 1.00 13.34 ? 63  ASN A CA  1 
ATOM   2551 C  C   . ASN B 1 63  ? -17.783 27.787  -28.677 1.00 13.66 ? 63  ASN A C   1 
ATOM   2552 O  O   . ASN B 1 63  ? -19.020 27.806  -28.326 1.00 12.82 ? 63  ASN A O   1 
ATOM   2553 C  CB  . ASN B 1 63  ? -18.055 26.341  -30.699 1.00 12.62 ? 63  ASN A CB  1 
ATOM   2554 C  CG  . ASN B 1 63  ? -18.137 27.524  -31.695 1.00 14.34 ? 63  ASN A CG  1 
ATOM   2555 O  OD1 . ASN B 1 63  ? -17.890 28.668  -31.318 1.00 13.85 ? 63  ASN A OD1 1 
ATOM   2556 N  ND2 . ASN B 1 63  ? -18.460 27.232  -32.984 1.00 13.70 ? 63  ASN A ND2 1 
ATOM   2557 N  N   . SER B 1 64  ? -16.947 28.785  -28.384 1.00 14.17 ? 64  SER A N   1 
ATOM   2558 C  CA  . SER B 1 64  ? -17.389 29.908  -27.560 1.00 12.86 ? 64  SER A CA  1 
ATOM   2559 C  C   . SER B 1 64  ? -18.242 30.927  -28.375 1.00 12.82 ? 64  SER A C   1 
ATOM   2560 O  O   . SER B 1 64  ? -18.801 31.870  -27.816 1.00 14.31 ? 64  SER A O   1 
ATOM   2561 C  CB  . SER B 1 64  ? -16.159 30.620  -26.972 1.00 13.59 ? 64  SER A CB  1 
ATOM   2562 O  OG  . SER B 1 64  ? -15.399 31.260  -28.008 1.00 15.81 ? 64  SER A OG  1 
ATOM   2563 N  N   . GLY B 1 65  ? -18.234 30.751  -29.689 1.00 12.01 ? 65  GLY A N   1 
ATOM   2564 C  CA  . GLY B 1 65  ? -18.690 31.784  -30.645 1.00 12.26 ? 65  GLY A CA  1 
ATOM   2565 C  C   . GLY B 1 65  ? -17.608 32.701  -31.183 1.00 12.80 ? 65  GLY A C   1 
ATOM   2566 O  O   . GLY B 1 65  ? -17.822 33.393  -32.183 1.00 13.06 ? 65  GLY A O   1 
ATOM   2567 N  N   . HIS B 1 66  ? -16.441 32.678  -30.534 1.00 12.49 ? 66  HIS A N   1 
ATOM   2568 C  CA  . HIS B 1 66  ? -15.324 33.563  -30.812 1.00 12.26 ? 66  HIS A CA  1 
ATOM   2569 C  C   . HIS B 1 66  ? -14.025 32.803  -31.216 1.00 12.44 ? 66  HIS A C   1 
ATOM   2570 O  O   . HIS B 1 66  ? -13.111 33.454  -31.808 1.00 14.67 ? 66  HIS A O   1 
ATOM   2571 C  CB  . HIS B 1 66  ? -15.013 34.422  -29.594 1.00 12.08 ? 66  HIS A CB  1 
ATOM   2572 C  CG  . HIS B 1 66  ? -16.207 35.131  -29.074 1.00 13.09 ? 66  HIS A CG  1 
ATOM   2573 N  ND1 . HIS B 1 66  ? -16.753 34.863  -27.832 1.00 15.11 ? 66  HIS A ND1 1 
ATOM   2574 C  CD2 . HIS B 1 66  ? -17.034 36.017  -29.668 1.00 12.63 ? 66  HIS A CD2 1 
ATOM   2575 C  CE1 . HIS B 1 66  ? -17.812 35.639  -27.642 1.00 14.06 ? 66  HIS A CE1 1 
ATOM   2576 N  NE2 . HIS B 1 66  ? -17.987 36.364  -28.735 1.00 16.75 ? 66  HIS A NE2 1 
ATOM   2577 N  N   . SER B 1 67  ? -13.932 31.495  -30.900 1.00 10.78 ? 67  SER A N   1 
ATOM   2578 C  CA  . SER B 1 67  ? -12.823 30.585  -31.204 1.00 10.08 ? 67  SER A CA  1 
ATOM   2579 C  C   . SER B 1 67  ? -13.282 29.204  -30.653 1.00 10.44 ? 67  SER A C   1 
ATOM   2580 O  O   . SER B 1 67  ? -14.402 29.089  -30.090 1.00 11.49 ? 67  SER A O   1 
ATOM   2581 C  CB  . SER B 1 67  ? -11.515 31.034  -30.479 1.00 10.60 ? 67  SER A CB  1 
ATOM   2582 O  OG  . SER B 1 67  ? -10.422 30.224  -31.016 1.00 12.16 ? 67  SER A OG  1 
ATOM   2583 N  N   . PHE B 1 68  ? -12.441 28.172  -30.763 1.00 11.18 ? 68  PHE A N   1 
ATOM   2584 C  CA  . PHE B 1 68  ? -12.624 26.976  -29.899 1.00 10.59 ? 68  PHE A CA  1 
ATOM   2585 C  C   . PHE B 1 68  ? -11.968 27.357  -28.557 1.00 11.07 ? 68  PHE A C   1 
ATOM   2586 O  O   . PHE B 1 68  ? -11.154 28.276  -28.499 1.00 9.92  ? 68  PHE A O   1 
ATOM   2587 C  CB  . PHE B 1 68  ? -11.921 25.737  -30.523 1.00 11.06 ? 68  PHE A CB  1 
ATOM   2588 C  CG  . PHE B 1 68  ? -10.418 25.785  -30.465 1.00 10.77 ? 68  PHE A CG  1 
ATOM   2589 C  CD1 . PHE B 1 68  ? -9.716  25.451  -29.315 1.00 11.03 ? 68  PHE A CD1 1 
ATOM   2590 C  CD2 . PHE B 1 68  ? -9.694  26.152  -31.581 1.00 10.73 ? 68  PHE A CD2 1 
ATOM   2591 C  CE1 . PHE B 1 68  ? -8.316  25.496  -29.294 1.00 10.49 ? 68  PHE A CE1 1 
ATOM   2592 C  CE2 . PHE B 1 68  ? -8.286  26.186  -31.589 1.00 10.07 ? 68  PHE A CE2 1 
ATOM   2593 C  CZ  . PHE B 1 68  ? -7.581  25.849  -30.442 1.00 10.86 ? 68  PHE A CZ  1 
ATOM   2594 N  N   . ASN B 1 69  ? -12.388 26.696  -27.482 1.00 9.94  ? 69  ASN A N   1 
ATOM   2595 C  CA  . ASN B 1 69  ? -11.800 26.943  -26.210 1.00 11.43 ? 69  ASN A CA  1 
ATOM   2596 C  C   . ASN B 1 69  ? -11.592 25.562  -25.617 1.00 11.74 ? 69  ASN A C   1 
ATOM   2597 O  O   . ASN B 1 69  ? -12.572 24.739  -25.520 1.00 10.76 ? 69  ASN A O   1 
ATOM   2598 C  CB  . ASN B 1 69  ? -12.792 27.735  -25.369 1.00 12.98 ? 69  ASN A CB  1 
ATOM   2599 C  CG  . ASN B 1 69  ? -12.303 27.972  -24.030 1.00 17.81 ? 69  ASN A CG  1 
ATOM   2600 O  OD1 . ASN B 1 69  ? -11.586 28.947  -23.800 1.00 22.09 ? 69  ASN A OD1 1 
ATOM   2601 N  ND2 . ASN B 1 69  ? -12.623 27.075  -23.099 1.00 18.69 ? 69  ASN A ND2 1 
ATOM   2602 N  N   . VAL B 1 70  ? -10.352 25.269  -25.204 1.00 10.61 ? 70  VAL A N   1 
ATOM   2603 C  CA  . VAL B 1 70  ? -10.135 24.035  -24.383 1.00 11.08 ? 70  VAL A CA  1 
ATOM   2604 C  C   . VAL B 1 70  ? -10.106 24.450  -22.949 1.00 11.12 ? 70  VAL A C   1 
ATOM   2605 O  O   . VAL B 1 70  ? -9.332  25.328  -22.610 1.00 10.38 ? 70  VAL A O   1 
ATOM   2606 C  CB  . VAL B 1 70  ? -8.834  23.301  -24.729 1.00 10.88 ? 70  VAL A CB  1 
ATOM   2607 C  CG1 . VAL B 1 70  ? -8.652  22.105  -23.767 1.00 10.79 ? 70  VAL A CG1 1 
ATOM   2608 C  CG2 . VAL B 1 70  ? -8.852  22.861  -26.216 1.00 12.42 ? 70  VAL A CG2 1 
ATOM   2609 N  N   . ASP B 1 71  ? -10.999 23.904  -22.111 1.00 10.06 ? 71  ASP A N   1 
ATOM   2610 C  CA  . ASP B 1 71  ? -10.971 24.183  -20.661 1.00 11.15 ? 71  ASP A CA  1 
ATOM   2611 C  C   . ASP B 1 71  ? -10.290 23.103  -19.911 1.00 10.45 ? 71  ASP A C   1 
ATOM   2612 O  O   . ASP B 1 71  ? -10.461 21.914  -20.222 1.00 11.40 ? 71  ASP A O   1 
ATOM   2613 C  CB  . ASP B 1 71  ? -12.428 24.268  -20.081 1.00 13.01 ? 71  ASP A CB  1 
ATOM   2614 C  CG  . ASP B 1 71  ? -13.053 25.651  -20.259 1.00 19.79 ? 71  ASP A CG  1 
ATOM   2615 O  OD1 . ASP B 1 71  ? -12.340 26.660  -20.253 1.00 20.55 ? 71  ASP A OD1 1 
ATOM   2616 O  OD2 . ASP B 1 71  ? -14.303 25.718  -20.410 1.00 24.96 ? 71  ASP A OD2 1 
ATOM   2617 N  N   . PHE B 1 72  ? -9.506  23.521  -18.921 1.00 11.52 ? 72  PHE A N   1 
ATOM   2618 C  CA  . PHE B 1 72  ? -8.737  22.627  -18.051 1.00 10.95 ? 72  PHE A CA  1 
ATOM   2619 C  C   . PHE B 1 72  ? -9.245  22.694  -16.614 1.00 12.43 ? 72  PHE A C   1 
ATOM   2620 O  O   . PHE B 1 72  ? -9.746  23.740  -16.165 1.00 12.50 ? 72  PHE A O   1 
ATOM   2621 C  CB  . PHE B 1 72  ? -7.287  23.037  -18.079 1.00 10.76 ? 72  PHE A CB  1 
ATOM   2622 C  CG  . PHE B 1 72  ? -6.684  22.948  -19.455 1.00 11.34 ? 72  PHE A CG  1 
ATOM   2623 C  CD1 . PHE B 1 72  ? -6.874  24.025  -20.374 1.00 10.08 ? 72  PHE A CD1 1 
ATOM   2624 C  CD2 . PHE B 1 72  ? -5.895  21.837  -19.821 1.00 10.71 ? 72  PHE A CD2 1 
ATOM   2625 C  CE1 . PHE B 1 72  ? -6.295  23.957  -21.650 1.00 10.99 ? 72  PHE A CE1 1 
ATOM   2626 C  CE2 . PHE B 1 72  ? -5.320  21.762  -21.113 1.00 10.73 ? 72  PHE A CE2 1 
ATOM   2627 C  CZ  . PHE B 1 72  ? -5.535  22.837  -22.017 1.00 10.38 ? 72  PHE A CZ  1 
ATOM   2628 N  N   . ASP B 1 73  ? -9.093  21.589  -15.916 1.00 11.89 ? 73  ASP A N   1 
ATOM   2629 C  CA  . ASP B 1 73  ? -9.281  21.518  -14.447 1.00 13.78 ? 73  ASP A CA  1 
ATOM   2630 C  C   . ASP B 1 73  ? -8.278  22.424  -13.806 1.00 12.76 ? 73  ASP A C   1 
ATOM   2631 O  O   . ASP B 1 73  ? -7.060  22.148  -13.929 1.00 13.04 ? 73  ASP A O   1 
ATOM   2632 C  CB  . ASP B 1 73  ? -9.102  20.038  -14.011 1.00 15.31 ? 73  ASP A CB  1 
ATOM   2633 C  CG  . ASP B 1 73  ? -8.985  19.836  -12.491 1.00 21.99 ? 73  ASP A CG  1 
ATOM   2634 O  OD1 . ASP B 1 73  ? -8.762  20.787  -11.713 1.00 22.21 ? 73  ASP A OD1 1 
ATOM   2635 O  OD2 . ASP B 1 73  ? -8.949  18.637  -12.079 1.00 23.90 ? 73  ASP A OD2 1 
ATOM   2636 N  N   . ASP B 1 74  ? -8.746  23.533  -13.181 1.00 12.87 ? 74  ASP A N   1 
ATOM   2637 C  CA  . ASP B 1 74  ? -7.831  24.548  -12.643 1.00 12.64 ? 74  ASP A CA  1 
ATOM   2638 C  C   . ASP B 1 74  ? -7.995  24.616  -11.073 1.00 13.36 ? 74  ASP A C   1 
ATOM   2639 O  O   . ASP B 1 74  ? -8.117  25.724  -10.509 1.00 13.99 ? 74  ASP A O   1 
ATOM   2640 C  CB  . ASP B 1 74  ? -8.034  25.925  -13.328 1.00 13.48 ? 74  ASP A CB  1 
ATOM   2641 C  CG  . ASP B 1 74  ? -9.370  26.563  -13.045 1.00 13.29 ? 74  ASP A CG  1 
ATOM   2642 O  OD1 . ASP B 1 74  ? -10.306 25.839  -12.537 1.00 14.44 ? 74  ASP A OD1 1 
ATOM   2643 O  OD2 . ASP B 1 74  ? -9.513  27.834  -13.236 1.00 13.43 ? 74  ASP A OD2 1 
ATOM   2644 N  N   . THR B 1 75  ? -8.095  23.413  -10.466 1.00 13.24 ? 75  THR A N   1 
ATOM   2645 C  CA  . THR B 1 75  ? -8.238  23.245  -8.982  1.00 14.78 ? 75  THR A CA  1 
ATOM   2646 C  C   . THR B 1 75  ? -6.947  22.876  -8.274  1.00 15.58 ? 75  THR A C   1 
ATOM   2647 O  O   . THR B 1 75  ? -6.919  22.926  -7.058  1.00 14.62 ? 75  THR A O   1 
ATOM   2648 C  CB  . THR B 1 75  ? -9.329  22.149  -8.660  1.00 15.40 ? 75  THR A CB  1 
ATOM   2649 O  OG1 . THR B 1 75  ? -8.824  20.844  -9.048  1.00 15.25 ? 75  THR A OG1 1 
ATOM   2650 C  CG2 . THR B 1 75  ? -10.615 22.479  -9.406  1.00 16.26 ? 75  THR A CG2 1 
ATOM   2651 N  N   . GLU B 1 76  ? -5.901  22.513  -9.037  1.00 15.07 ? 76  GLU A N   1 
ATOM   2652 C  CA  . GLU B 1 76  ? -4.618  22.059  -8.531  1.00 16.84 ? 76  GLU A CA  1 
ATOM   2653 C  C   . GLU B 1 76  ? -3.529  22.648  -9.369  1.00 14.97 ? 76  GLU A C   1 
ATOM   2654 O  O   . GLU B 1 76  ? -3.837  23.275  -10.393 1.00 15.52 ? 76  GLU A O   1 
ATOM   2655 C  CB  . GLU B 1 76  ? -4.521  20.525  -8.577  1.00 21.94 ? 76  GLU A CB  1 
ATOM   2656 C  CG  . GLU B 1 76  ? -5.617  19.942  -7.726  1.00 27.12 ? 76  GLU A CG  1 
ATOM   2657 C  CD  . GLU B 1 76  ? -5.577  18.452  -7.586  1.00 36.59 ? 76  GLU A CD  1 
ATOM   2658 O  OE1 . GLU B 1 76  ? -4.559  17.812  -7.931  1.00 37.22 ? 76  GLU A OE1 1 
ATOM   2659 O  OE2 . GLU B 1 76  ? -6.603  17.942  -7.081  1.00 40.21 ? 76  GLU A OE2 1 
ATOM   2660 N  N   . ASN B 1 77  ? -2.308  22.456  -8.919  1.00 13.20 ? 77  ASN A N   1 
ATOM   2661 C  CA  . ASN B 1 77  ? -1.079  22.943  -9.584  1.00 13.29 ? 77  ASN A CA  1 
ATOM   2662 C  C   . ASN B 1 77  ? -0.341  21.934  -10.469 1.00 14.00 ? 77  ASN A C   1 
ATOM   2663 O  O   . ASN B 1 77  ? 0.860   22.013  -10.621 1.00 15.82 ? 77  ASN A O   1 
ATOM   2664 C  CB  . ASN B 1 77  ? -0.177  23.669  -8.590  1.00 14.60 ? 77  ASN A CB  1 
ATOM   2665 C  CG  . ASN B 1 77  ? -0.769  25.003  -8.103  1.00 14.68 ? 77  ASN A CG  1 
ATOM   2666 O  OD1 . ASN B 1 77  ? -1.566  25.631  -8.775  1.00 13.73 ? 77  ASN A OD1 1 
ATOM   2667 N  ND2 . ASN B 1 77  ? -0.276  25.489  -6.957  1.00 14.08 ? 77  ASN A ND2 1 
ATOM   2668 N  N   . LYS B 1 78  ? -1.132  21.094  -11.130 1.00 14.54 ? 78  LYS A N   1 
ATOM   2669 C  CA  . LYS B 1 78  ? -0.701  20.038  -12.098 1.00 15.18 ? 78  LYS A CA  1 
ATOM   2670 C  C   . LYS B 1 78  ? -0.236  20.695  -13.398 1.00 13.78 ? 78  LYS A C   1 
ATOM   2671 O  O   . LYS B 1 78  ? 0.723   20.241  -13.997 1.00 12.62 ? 78  LYS A O   1 
ATOM   2672 C  CB  . LYS B 1 78  ? -1.847  19.045  -12.371 1.00 18.23 ? 78  LYS A CB  1 
ATOM   2673 C  CG  . LYS B 1 78  ? -2.152  18.085  -11.189 1.00 21.96 ? 78  LYS A CG  1 
ATOM   2674 C  CD  . LYS B 1 78  ? -2.835  16.807  -11.665 1.00 24.49 ? 78  LYS A CD  1 
ATOM   2675 C  CE  . LYS B 1 78  ? -3.027  15.746  -10.587 1.00 30.09 ? 78  LYS A CE  1 
ATOM   2676 N  NZ  . LYS B 1 78  ? -1.718  15.233  -10.030 1.00 35.34 ? 78  LYS A NZ  1 
ATOM   2677 N  N   . SER B 1 79  ? -0.887  21.800  -13.792 1.00 13.19 ? 79  SER A N   1 
ATOM   2678 C  CA  . SER B 1 79  ? -0.513  22.508  -15.052 1.00 10.60 ? 79  SER A CA  1 
ATOM   2679 C  C   . SER B 1 79  ? -0.371  23.967  -14.715 1.00 10.72 ? 79  SER A C   1 
ATOM   2680 O  O   . SER B 1 79  ? -1.387  24.676  -14.470 1.00 10.78 ? 79  SER A O   1 
ATOM   2681 C  CB  . SER B 1 79  ? -1.649  22.308  -16.117 1.00 10.30 ? 79  SER A CB  1 
ATOM   2682 O  OG  . SER B 1 79  ? -1.746  20.905  -16.410 1.00 10.70 ? 79  SER A OG  1 
ATOM   2683 N  N   . VAL B 1 80  ? 0.912   24.421  -14.719 1.00 11.67 ? 80  VAL A N   1 
ATOM   2684 C  CA  . VAL B 1 80  ? 1.322   25.728  -14.194 1.00 11.66 ? 80  VAL A CA  1 
ATOM   2685 C  C   . VAL B 1 80  ? 2.438   26.302  -14.982 1.00 10.79 ? 80  VAL A C   1 
ATOM   2686 O  O   . VAL B 1 80  ? 3.287   25.583  -15.527 1.00 12.03 ? 80  VAL A O   1 
ATOM   2687 C  CB  . VAL B 1 80  ? 1.736   25.702  -12.692 1.00 13.12 ? 80  VAL A CB  1 
ATOM   2688 C  CG1 . VAL B 1 80  ? 0.547   25.354  -11.851 1.00 14.57 ? 80  VAL A CG1 1 
ATOM   2689 C  CG2 . VAL B 1 80  ? 2.769   24.600  -12.416 1.00 14.85 ? 80  VAL A CG2 1 
ATOM   2690 N  N   . LEU B 1 81  ? 2.360   27.624  -15.085 1.00 10.17 ? 81  LEU A N   1 
ATOM   2691 C  CA  . LEU B 1 81  ? 3.412   28.469  -15.627 1.00 10.46 ? 81  LEU A CA  1 
ATOM   2692 C  C   . LEU B 1 81  ? 4.070   29.247  -14.534 1.00 11.39 ? 81  LEU A C   1 
ATOM   2693 O  O   . LEU B 1 81  ? 3.376   29.887  -13.760 1.00 11.01 ? 81  LEU A O   1 
ATOM   2694 C  CB  . LEU B 1 81  ? 2.749   29.445  -16.631 1.00 10.08 ? 81  LEU A CB  1 
ATOM   2695 C  CG  . LEU B 1 81  ? 3.611   30.500  -17.305 1.00 9.68  ? 81  LEU A CG  1 
ATOM   2696 C  CD1 . LEU B 1 81  ? 4.741   29.948  -18.153 1.00 10.61 ? 81  LEU A CD1 1 
ATOM   2697 C  CD2 . LEU B 1 81  ? 2.703   31.356  -18.161 1.00 9.15  ? 81  LEU A CD2 1 
ATOM   2698 N  N   . ARG B 1 82  ? 5.423   29.214  -14.472 1.00 11.13 ? 82  ARG A N   1 
ATOM   2699 C  CA  . ARG B 1 82  ? 6.143   29.964  -13.440 1.00 11.92 ? 82  ARG A CA  1 
ATOM   2700 C  C   . ARG B 1 82  ? 7.440   30.545  -14.014 1.00 11.03 ? 82  ARG A C   1 
ATOM   2701 O  O   . ARG B 1 82  ? 7.833   30.205  -15.122 1.00 9.76  ? 82  ARG A O   1 
ATOM   2702 C  CB  . ARG B 1 82  ? 6.594   28.959  -12.323 1.00 13.60 ? 82  ARG A CB  1 
ATOM   2703 C  CG  . ARG B 1 82  ? 5.442   28.375  -11.476 1.00 17.18 ? 82  ARG A CG  1 
ATOM   2704 C  CD  . ARG B 1 82  ? 6.029   27.309  -10.535 1.00 19.24 ? 82  ARG A CD  1 
ATOM   2705 N  NE  . ARG B 1 82  ? 6.232   26.047  -11.293 1.00 28.64 ? 82  ARG A NE  1 
ATOM   2706 C  CZ  . ARG B 1 82  ? 5.821   24.817  -10.949 1.00 36.87 ? 82  ARG A CZ  1 
ATOM   2707 N  NH1 . ARG B 1 82  ? 5.172   24.600  -9.812  1.00 35.11 ? 82  ARG A NH1 1 
ATOM   2708 N  NH2 . ARG B 1 82  ? 6.072   23.786  -11.756 1.00 24.74 ? 82  ARG A NH2 1 
ATOM   2709 N  N   . GLY B 1 83  ? 8.123   31.384  -13.240 1.00 11.59 ? 83  GLY A N   1 
ATOM   2710 C  CA  . GLY B 1 83  ? 9.388   31.911  -13.768 1.00 10.76 ? 83  GLY A CA  1 
ATOM   2711 C  C   . GLY B 1 83  ? 9.224   33.026  -14.791 1.00 11.24 ? 83  GLY A C   1 
ATOM   2712 O  O   . GLY B 1 83  ? 8.171   33.682  -14.903 1.00 10.83 ? 83  GLY A O   1 
ATOM   2713 N  N   . GLY B 1 84  ? 10.280  33.209  -15.577 1.00 12.30 ? 84  GLY A N   1 
ATOM   2714 C  CA  . GLY B 1 84  ? 10.315  34.340  -16.483 1.00 10.50 ? 84  GLY A CA  1 
ATOM   2715 C  C   . GLY B 1 84  ? 10.062  35.642  -15.750 1.00 11.29 ? 84  GLY A C   1 
ATOM   2716 O  O   . GLY B 1 84  ? 10.775  35.980  -14.797 1.00 13.68 ? 84  GLY A O   1 
ATOM   2717 N  N   . PRO B 1 85  ? 9.066   36.406  -16.191 1.00 9.97  ? 85  PRO A N   1 
ATOM   2718 C  CA  . PRO B 1 85  ? 8.762   37.683  -15.581 1.00 9.96  ? 85  PRO A CA  1 
ATOM   2719 C  C   . PRO B 1 85  ? 7.865   37.528  -14.367 1.00 9.97  ? 85  PRO A C   1 
ATOM   2720 O  O   . PRO B 1 85  ? 7.631   38.534  -13.692 1.00 11.82 ? 85  PRO A O   1 
ATOM   2721 C  CB  . PRO B 1 85  ? 7.972   38.413  -16.653 1.00 9.95  ? 85  PRO A CB  1 
ATOM   2722 C  CG  . PRO B 1 85  ? 7.261   37.270  -17.415 1.00 10.87 ? 85  PRO A CG  1 
ATOM   2723 C  CD  . PRO B 1 85  ? 8.216   36.110  -17.385 1.00 9.52  ? 85  PRO A CD  1 
ATOM   2724 N  N   . LEU B 1 86  ? 7.390   36.297  -14.130 1.00 10.78 ? 86  LEU A N   1 
ATOM   2725 C  CA  . LEU B 1 86  ? 6.274   36.094  -13.170 1.00 11.29 ? 86  LEU A CA  1 
ATOM   2726 C  C   . LEU B 1 86  ? 6.742   35.996  -11.751 1.00 12.50 ? 86  LEU A C   1 
ATOM   2727 O  O   . LEU B 1 86  ? 7.781   35.374  -11.489 1.00 13.20 ? 86  LEU A O   1 
ATOM   2728 C  CB  . LEU B 1 86  ? 5.491   34.824  -13.558 1.00 10.48 ? 86  LEU A CB  1 
ATOM   2729 C  CG  . LEU B 1 86  ? 4.933   34.867  -14.990 1.00 9.54  ? 86  LEU A CG  1 
ATOM   2730 C  CD1 . LEU B 1 86  ? 4.428   33.486  -15.416 1.00 9.95  ? 86  LEU A CD1 1 
ATOM   2731 C  CD2 . LEU B 1 86  ? 3.825   35.951  -15.173 1.00 11.47 ? 86  LEU A CD2 1 
ATOM   2732 N  N   . THR B 1 87  ? 5.940   36.571  -10.847 1.00 12.44 ? 87  THR A N   1 
ATOM   2733 C  CA  . THR B 1 87  ? 6.088   36.290  -9.395  1.00 13.04 ? 87  THR A CA  1 
ATOM   2734 C  C   . THR B 1 87  ? 5.006   35.275  -9.006  1.00 13.18 ? 87  THR A C   1 
ATOM   2735 O  O   . THR B 1 87  ? 3.792   35.562  -9.185  1.00 14.98 ? 87  THR A O   1 
ATOM   2736 C  CB  . THR B 1 87  ? 5.908   37.591  -8.612  1.00 14.52 ? 87  THR A CB  1 
ATOM   2737 O  OG1 . THR B 1 87  ? 7.003   38.481  -8.925  1.00 19.36 ? 87  THR A OG1 1 
ATOM   2738 C  CG2 . THR B 1 87  ? 5.899   37.357  -7.033  1.00 16.22 ? 87  THR A CG2 1 
ATOM   2739 N  N   . GLY B 1 88  ? 5.428   34.115  -8.486  1.00 12.88 ? 88  GLY A N   1 
ATOM   2740 C  CA  . GLY B 1 88  ? 4.492   33.053  -8.038  1.00 12.79 ? 88  GLY A CA  1 
ATOM   2741 C  C   . GLY B 1 88  ? 3.912   32.197  -9.171  1.00 13.18 ? 88  GLY A C   1 
ATOM   2742 O  O   . GLY B 1 88  ? 4.461   32.184  -10.314 1.00 13.31 ? 88  GLY A O   1 
ATOM   2743 N  N   . SER B 1 89  ? 2.816   31.500  -8.904  1.00 12.37 ? 89  SER A N   1 
ATOM   2744 C  CA  . SER B 1 89  ? 2.460   30.380  -9.790  1.00 11.33 ? 89  SER A CA  1 
ATOM   2745 C  C   . SER B 1 89  ? 1.153   30.687  -10.531 1.00 10.66 ? 89  SER A C   1 
ATOM   2746 O  O   . SER B 1 89  ? 0.167   31.048  -9.895  1.00 10.37 ? 89  SER A O   1 
ATOM   2747 C  CB  . SER B 1 89  ? 2.307   29.066  -8.975  1.00 12.74 ? 89  SER A CB  1 
ATOM   2748 O  OG  . SER B 1 89  ? 2.125   27.947  -9.819  1.00 13.60 ? 89  SER A OG  1 
ATOM   2749 N  N   . TYR B 1 90  ? 1.198   30.528  -11.846 1.00 9.35  ? 90  TYR A N   1 
ATOM   2750 C  CA  . TYR B 1 90  ? 0.044   30.829  -12.673 1.00 9.40  ? 90  TYR A CA  1 
ATOM   2751 C  C   . TYR B 1 90  ? -0.577  29.557  -13.229 1.00 8.88  ? 90  TYR A C   1 
ATOM   2752 O  O   . TYR B 1 90  ? 0.046   28.801  -13.994 1.00 10.84 ? 90  TYR A O   1 
ATOM   2753 C  CB  . TYR B 1 90  ? 0.438   31.805  -13.799 1.00 9.00  ? 90  TYR A CB  1 
ATOM   2754 C  CG  . TYR B 1 90  ? 0.680   33.227  -13.272 1.00 8.60  ? 90  TYR A CG  1 
ATOM   2755 C  CD1 . TYR B 1 90  ? 1.790   33.555  -12.481 1.00 8.70  ? 90  TYR A CD1 1 
ATOM   2756 C  CD2 . TYR B 1 90  ? -0.227  34.247  -13.570 1.00 8.13  ? 90  TYR A CD2 1 
ATOM   2757 C  CE1 . TYR B 1 90  ? 1.954   34.850  -11.964 1.00 8.89  ? 90  TYR A CE1 1 
ATOM   2758 C  CE2 . TYR B 1 90  ? -0.095  35.558  -13.063 1.00 8.85  ? 90  TYR A CE2 1 
ATOM   2759 C  CZ  . TYR B 1 90  ? 1.033   35.852  -12.252 1.00 9.17  ? 90  TYR A CZ  1 
ATOM   2760 O  OH  . TYR B 1 90  ? 1.222   37.127  -11.820 1.00 9.95  ? 90  TYR A OH  1 
ATOM   2761 N  N   . ARG B 1 91  ? -1.858  29.342  -12.885 1.00 8.51  ? 91  ARG A N   1 
ATOM   2762 C  CA  . ARG B 1 91  ? -2.501  28.017  -13.153 1.00 8.21  ? 91  ARG A CA  1 
ATOM   2763 C  C   . ARG B 1 91  ? -3.114  28.054  -14.564 1.00 8.27  ? 91  ARG A C   1 
ATOM   2764 O  O   . ARG B 1 91  ? -3.818  29.010  -14.889 1.00 7.37  ? 91  ARG A O   1 
ATOM   2765 C  CB  . ARG B 1 91  ? -3.583  27.724  -12.076 1.00 7.95  ? 91  ARG A CB  1 
ATOM   2766 C  CG  . ARG B 1 91  ? -4.057  26.276  -12.108 1.00 7.77  ? 91  ARG A CG  1 
ATOM   2767 C  CD  . ARG B 1 91  ? -5.021  26.053  -10.922 1.00 9.03  ? 91  ARG A CD  1 
ATOM   2768 N  NE  . ARG B 1 91  ? -4.249  26.168  -9.686  1.00 9.25  ? 91  ARG A NE  1 
ATOM   2769 C  CZ  . ARG B 1 91  ? -4.855  26.342  -8.508  1.00 9.83  ? 91  ARG A CZ  1 
ATOM   2770 N  NH1 . ARG B 1 91  ? -6.189  26.529  -8.499  1.00 10.69 ? 91  ARG A NH1 1 
ATOM   2771 N  NH2 . ARG B 1 91  ? -4.089  26.441  -7.381  1.00 9.80  ? 91  ARG A NH2 1 
ATOM   2772 N  N   . LEU B 1 92  ? -2.925  26.977  -15.324 1.00 8.28  ? 92  LEU A N   1 
ATOM   2773 C  CA  . LEU B 1 92  ? -3.534  26.860  -16.631 1.00 8.01  ? 92  LEU A CA  1 
ATOM   2774 C  C   . LEU B 1 92  ? -5.082  26.846  -16.550 1.00 9.24  ? 92  LEU A C   1 
ATOM   2775 O  O   . LEU B 1 92  ? -5.666  26.042  -15.797 1.00 8.29  ? 92  LEU A O   1 
ATOM   2776 C  CB  . LEU B 1 92  ? -2.948  25.621  -17.311 1.00 7.83  ? 92  LEU A CB  1 
ATOM   2777 C  CG  . LEU B 1 92  ? -3.684  25.263  -18.616 1.00 7.99  ? 92  LEU A CG  1 
ATOM   2778 C  CD1 . LEU B 1 92  ? -3.401  26.373  -19.648 1.00 8.55  ? 92  LEU A CD1 1 
ATOM   2779 C  CD2 . LEU B 1 92  ? -3.188  23.877  -19.084 1.00 7.67  ? 92  LEU A CD2 1 
ATOM   2780 N  N   . ARG B 1 93  ? -5.701  27.686  -17.379 1.00 8.36  ? 93  ARG A N   1 
ATOM   2781 C  CA  . ARG B 1 93  ? -7.146  27.796  -17.424 1.00 10.20 ? 93  ARG A CA  1 
ATOM   2782 C  C   . ARG B 1 93  ? -7.717  27.346  -18.794 1.00 9.45  ? 93  ARG A C   1 
ATOM   2783 O  O   . ARG B 1 93  ? -8.675  26.524  -18.837 1.00 10.30 ? 93  ARG A O   1 
ATOM   2784 C  CB  . ARG B 1 93  ? -7.566  29.221  -17.063 1.00 10.26 ? 93  ARG A CB  1 
ATOM   2785 C  CG  . ARG B 1 93  ? -9.046  29.637  -17.320 1.00 10.93 ? 93  ARG A CG  1 
ATOM   2786 C  CD  . ARG B 1 93  ? -9.903  28.920  -16.306 1.00 13.09 ? 93  ARG A CD  1 
ATOM   2787 N  NE  . ARG B 1 93  ? -11.336 29.106  -16.579 1.00 15.16 ? 93  ARG A NE  1 
ATOM   2788 C  CZ  . ARG B 1 93  ? -12.288 29.011  -15.658 1.00 18.47 ? 93  ARG A CZ  1 
ATOM   2789 N  NH1 . ARG B 1 93  ? -12.022 28.659  -14.411 1.00 19.58 ? 93  ARG A NH1 1 
ATOM   2790 N  NH2 . ARG B 1 93  ? -13.563 29.240  -16.004 1.00 23.58 ? 93  ARG A NH2 1 
ATOM   2791 N  N   . GLN B 1 94  ? -7.212  27.925  -19.882 1.00 8.54  ? 94  GLN A N   1 
ATOM   2792 C  CA  . GLN B 1 94  ? -7.823  27.638  -21.170 1.00 8.43  ? 94  GLN A CA  1 
ATOM   2793 C  C   . GLN B 1 94  ? -6.873  27.908  -22.289 1.00 8.04  ? 94  GLN A C   1 
ATOM   2794 O  O   . GLN B 1 94  ? -5.886  28.645  -22.091 1.00 8.54  ? 94  GLN A O   1 
ATOM   2795 C  CB  . GLN B 1 94  ? -9.151  28.318  -21.396 1.00 9.69  ? 94  GLN A CB  1 
ATOM   2796 C  CG  . GLN B 1 94  ? -9.162  29.801  -21.150 1.00 11.36 ? 94  GLN A CG  1 
ATOM   2797 C  CD  . GLN B 1 94  ? -9.088  30.537  -22.449 1.00 12.91 ? 94  GLN A CD  1 
ATOM   2798 O  OE1 . GLN B 1 94  ? -8.380  30.110  -23.395 1.00 12.80 ? 94  GLN A OE1 1 
ATOM   2799 N  NE2 . GLN B 1 94  ? -9.860  31.642  -22.533 1.00 13.40 ? 94  GLN A NE2 1 
ATOM   2800 N  N   . VAL B 1 95  ? -7.181  27.291  -23.432 1.00 8.11  ? 95  VAL A N   1 
ATOM   2801 C  CA  . VAL B 1 95  ? -6.422  27.486  -24.665 1.00 8.29  ? 95  VAL A CA  1 
ATOM   2802 C  C   . VAL B 1 95  ? -7.405  27.843  -25.771 1.00 9.05  ? 95  VAL A C   1 
ATOM   2803 O  O   . VAL B 1 95  ? -8.440  27.196  -25.866 1.00 9.46  ? 95  VAL A O   1 
ATOM   2804 C  CB  . VAL B 1 95  ? -5.589  26.231  -25.027 1.00 8.95  ? 95  VAL A CB  1 
ATOM   2805 C  CG1 . VAL B 1 95  ? -5.011  26.228  -26.453 1.00 8.56  ? 95  VAL A CG1 1 
ATOM   2806 C  CG2 . VAL B 1 95  ? -4.425  26.114  -24.035 1.00 8.99  ? 95  VAL A CG2 1 
ATOM   2807 N  N   . HIS B 1 96  ? -7.056  28.846  -26.575 1.00 8.28  ? 96  HIS A N   1 
ATOM   2808 C  CA  . HIS B 1 96  ? -7.850  29.185  -27.790 1.00 7.83  ? 96  HIS A CA  1 
ATOM   2809 C  C   . HIS B 1 96  ? -6.945  29.647  -28.929 1.00 7.55  ? 96  HIS A C   1 
ATOM   2810 O  O   . HIS B 1 96  ? -5.733  29.803  -28.758 1.00 8.31  ? 96  HIS A O   1 
ATOM   2811 C  CB  . HIS B 1 96  ? -8.918  30.230  -27.457 1.00 7.22  ? 96  HIS A CB  1 
ATOM   2812 C  CG  . HIS B 1 96  ? -8.341  31.472  -26.960 1.00 7.99  ? 96  HIS A CG  1 
ATOM   2813 N  ND1 . HIS B 1 96  ? -8.056  31.686  -25.617 1.00 8.57  ? 96  HIS A ND1 1 
ATOM   2814 C  CD2 . HIS B 1 96  ? -7.935  32.590  -27.640 1.00 7.75  ? 96  HIS A CD2 1 
ATOM   2815 C  CE1 . HIS B 1 96  ? -7.538  32.902  -25.492 1.00 8.59  ? 96  HIS A CE1 1 
ATOM   2816 N  NE2 . HIS B 1 96  ? -7.454  33.468  -26.690 1.00 7.98  ? 96  HIS A NE2 1 
ATOM   2817 N  N   . LEU B 1 97  ? -7.530  29.939  -30.080 1.00 7.91  ? 97  LEU A N   1 
ATOM   2818 C  CA  . LEU B 1 97  ? -6.685  30.284  -31.231 1.00 8.04  ? 97  LEU A CA  1 
ATOM   2819 C  C   . LEU B 1 97  ? -7.289  31.509  -31.929 1.00 8.48  ? 97  LEU A C   1 
ATOM   2820 O  O   . LEU B 1 97  ? -8.532  31.592  -32.012 1.00 9.07  ? 97  LEU A O   1 
ATOM   2821 C  CB  . LEU B 1 97  ? -6.748  29.125  -32.241 1.00 7.89  ? 97  LEU A CB  1 
ATOM   2822 C  CG  . LEU B 1 97  ? -5.756  29.218  -33.457 1.00 7.91  ? 97  LEU A CG  1 
ATOM   2823 C  CD1 . LEU B 1 97  ? -4.253  29.106  -33.097 1.00 8.49  ? 97  LEU A CD1 1 
ATOM   2824 C  CD2 . LEU B 1 97  ? -6.124  28.032  -34.395 1.00 8.45  ? 97  LEU A CD2 1 
ATOM   2825 N  N   . HIS B 1 98  ? -6.448  32.359  -32.517 1.00 8.94  ? 98  HIS A N   1 
ATOM   2826 C  CA  . HIS B 1 98  ? -6.914  33.438  -33.388 1.00 8.95  ? 98  HIS A CA  1 
ATOM   2827 C  C   . HIS B 1 98  ? -6.357  33.259  -34.798 1.00 9.17  ? 98  HIS A C   1 
ATOM   2828 O  O   . HIS B 1 98  ? -5.172  32.864  -34.986 1.00 9.91  ? 98  HIS A O   1 
ATOM   2829 C  CB  . HIS B 1 98  ? -6.370  34.804  -32.847 1.00 7.57  ? 98  HIS A CB  1 
ATOM   2830 C  CG  . HIS B 1 98  ? -6.816  35.118  -31.455 1.00 8.11  ? 98  HIS A CG  1 
ATOM   2831 N  ND1 . HIS B 1 98  ? -7.980  35.806  -31.155 1.00 8.10  ? 98  HIS A ND1 1 
ATOM   2832 C  CD2 . HIS B 1 98  ? -6.237  34.798  -30.256 1.00 7.14  ? 98  HIS A CD2 1 
ATOM   2833 C  CE1 . HIS B 1 98  ? -8.052  35.971  -29.841 1.00 7.69  ? 98  HIS A CE1 1 
ATOM   2834 N  NE2 . HIS B 1 98  ? -7.073  35.289  -29.279 1.00 6.66  ? 98  HIS A NE2 1 
ATOM   2835 N  N   . TRP B 1 99  ? -7.141  33.612  -35.820 1.00 9.41  ? 99  TRP A N   1 
ATOM   2836 C  CA  . TRP B 1 99  ? -6.624  33.526  -37.201 1.00 9.57  ? 99  TRP A CA  1 
ATOM   2837 C  C   . TRP B 1 99  ? -7.292  34.651  -37.980 1.00 10.89 ? 99  TRP A C   1 
ATOM   2838 O  O   . TRP B 1 99  ? -8.108  35.410  -37.429 1.00 9.60  ? 99  TRP A O   1 
ATOM   2839 C  CB  . TRP B 1 99  ? -7.044  32.137  -37.772 1.00 9.89  ? 99  TRP A CB  1 
ATOM   2840 C  CG  . TRP B 1 99  ? -8.558  31.877  -37.662 1.00 10.25 ? 99  TRP A CG  1 
ATOM   2841 C  CD1 . TRP B 1 99  ? -9.556  32.266  -38.553 1.00 10.39 ? 99  TRP A CD1 1 
ATOM   2842 C  CD2 . TRP B 1 99  ? -9.226  31.159  -36.610 1.00 11.58 ? 99  TRP A CD2 1 
ATOM   2843 N  NE1 . TRP B 1 99  ? -10.807 31.873  -38.089 1.00 10.67 ? 99  TRP A NE1 1 
ATOM   2844 C  CE2 . TRP B 1 99  ? -10.626 31.131  -36.932 1.00 10.83 ? 99  TRP A CE2 1 
ATOM   2845 C  CE3 . TRP B 1 99  ? -8.762  30.476  -35.447 1.00 10.71 ? 99  TRP A CE3 1 
ATOM   2846 C  CZ2 . TRP B 1 99  ? -11.587 30.534  -36.095 1.00 10.60 ? 99  TRP A CZ2 1 
ATOM   2847 C  CZ3 . TRP B 1 99  ? -9.741  29.845  -34.604 1.00 10.94 ? 99  TRP A CZ3 1 
ATOM   2848 C  CH2 . TRP B 1 99  ? -11.107 29.836  -34.933 1.00 10.52 ? 99  TRP A CH2 1 
ATOM   2849 N  N   . GLY B 1 100 ? -6.908  34.792  -39.246 1.00 10.96 ? 100 GLY A N   1 
ATOM   2850 C  CA  . GLY B 1 100 ? -7.529  35.793  -40.151 1.00 11.93 ? 100 GLY A CA  1 
ATOM   2851 C  C   . GLY B 1 100 ? -8.270  35.086  -41.290 1.00 10.86 ? 100 GLY A C   1 
ATOM   2852 O  O   . GLY B 1 100 ? -8.271  33.843  -41.374 1.00 10.79 ? 100 GLY A O   1 
ATOM   2853 N  N   . SER B 1 101 ? -8.916  35.889  -42.152 1.00 10.37 ? 101 SER A N   1 
ATOM   2854 C  CA  . SER B 1 101 ? -9.600  35.295  -43.266 1.00 11.51 ? 101 SER A CA  1 
ATOM   2855 C  C   . SER B 1 101 ? -8.716  34.763  -44.372 1.00 12.37 ? 101 SER A C   1 
ATOM   2856 O  O   . SER B 1 101 ? -9.220  34.014  -45.225 1.00 13.99 ? 101 SER A O   1 
ATOM   2857 C  CB  . SER B 1 101 ? -10.634 36.255  -43.834 1.00 13.26 ? 101 SER A CB  1 
ATOM   2858 O  OG  . SER B 1 101 ? -10.020 37.340  -44.572 1.00 12.86 ? 101 SER A OG  1 
ATOM   2859 N  N   . ALA B 1 102 ? -7.450  35.155  -44.395 1.00 11.64 ? 102 ALA A N   1 
ATOM   2860 C  CA  . ALA B 1 102 ? -6.507  34.636  -45.377 1.00 12.69 ? 102 ALA A CA  1 
ATOM   2861 C  C   . ALA B 1 102 ? -5.218  34.254  -44.682 1.00 12.67 ? 102 ALA A C   1 
ATOM   2862 O  O   . ALA B 1 102 ? -4.886  34.855  -43.627 1.00 13.52 ? 102 ALA A O   1 
ATOM   2863 C  CB  . ALA B 1 102 ? -6.264  35.706  -46.481 1.00 14.61 ? 102 ALA A CB  1 
ATOM   2864 N  N   . ASP B 1 103 ? -4.449  33.346  -45.264 1.00 11.56 ? 103 ASP A N   1 
ATOM   2865 C  CA  . ASP B 1 103 ? -3.219  32.867  -44.628 1.00 13.84 ? 103 ASP A CA  1 
ATOM   2866 C  C   . ASP B 1 103 ? -2.108  33.903  -44.375 1.00 14.26 ? 103 ASP A C   1 
ATOM   2867 O  O   . ASP B 1 103 ? -1.220  33.650  -43.529 1.00 16.18 ? 103 ASP A O   1 
ATOM   2868 C  CB  . ASP B 1 103 ? -2.616  31.735  -45.488 1.00 13.65 ? 103 ASP A CB  1 
ATOM   2869 C  CG  . ASP B 1 103 ? -3.439  30.492  -45.483 1.00 14.25 ? 103 ASP A CG  1 
ATOM   2870 O  OD1 . ASP B 1 103 ? -4.342  30.361  -44.638 1.00 15.23 ? 103 ASP A OD1 1 
ATOM   2871 O  OD2 . ASP B 1 103 ? -3.238  29.629  -46.399 1.00 16.70 ? 103 ASP A OD2 1 
ATOM   2872 N  N   . ASP B 1 104 ? -2.126  35.066  -45.059 1.00 12.45 ? 104 ASP A N   1 
ATOM   2873 C  CA  . ASP B 1 104 ? -0.985  35.950  -45.013 1.00 13.90 ? 104 ASP A CA  1 
ATOM   2874 C  C   . ASP B 1 104 ? -0.951  36.779  -43.742 1.00 13.33 ? 104 ASP A C   1 
ATOM   2875 O  O   . ASP B 1 104 ? 0.094   37.310  -43.401 1.00 15.77 ? 104 ASP A O   1 
ATOM   2876 C  CB  . ASP B 1 104 ? -0.969  36.906  -46.197 1.00 15.34 ? 104 ASP A CB  1 
ATOM   2877 C  CG  . ASP B 1 104 ? -2.172  37.768  -46.223 1.00 16.30 ? 104 ASP A CG  1 
ATOM   2878 O  OD1 . ASP B 1 104 ? -3.202  37.295  -46.694 1.00 15.37 ? 104 ASP A OD1 1 
ATOM   2879 O  OD2 . ASP B 1 104 ? -2.092  38.936  -45.750 1.00 18.69 ? 104 ASP A OD2 1 
ATOM   2880 N  N   . HIS B 1 105 ? -2.082  36.845  -43.027 1.00 13.97 ? 105 HIS A N   1 
ATOM   2881 C  CA  . HIS B 1 105 ? -2.096  37.534  -41.757 1.00 13.96 ? 105 HIS A CA  1 
ATOM   2882 C  C   . HIS B 1 105 ? -3.268  37.057  -40.887 1.00 13.65 ? 105 HIS A C   1 
ATOM   2883 O  O   . HIS B 1 105 ? -4.230  36.519  -41.337 1.00 18.01 ? 105 HIS A O   1 
ATOM   2884 C  CB  . HIS B 1 105 ? -2.055  39.067  -41.944 1.00 15.17 ? 105 HIS A CB  1 
ATOM   2885 C  CG  . HIS B 1 105 ? -3.331  39.676  -42.396 1.00 17.91 ? 105 HIS A CG  1 
ATOM   2886 N  ND1 . HIS B 1 105 ? -3.661  39.846  -43.732 1.00 20.72 ? 105 HIS A ND1 1 
ATOM   2887 C  CD2 . HIS B 1 105 ? -4.342  40.233  -41.684 1.00 19.34 ? 105 HIS A CD2 1 
ATOM   2888 C  CE1 . HIS B 1 105 ? -4.829  40.468  -43.809 1.00 19.36 ? 105 HIS A CE1 1 
ATOM   2889 N  NE2 . HIS B 1 105 ? -5.276  40.689  -42.579 1.00 19.89 ? 105 HIS A NE2 1 
ATOM   2890 N  N   . GLY B 1 106 ? -3.102  37.147  -39.607 1.00 14.26 ? 106 GLY A N   1 
ATOM   2891 C  CA  . GLY B 1 106 ? -4.150  36.614  -38.763 1.00 13.63 ? 106 GLY A CA  1 
ATOM   2892 C  C   . GLY B 1 106 ? -3.630  36.495  -37.358 1.00 12.22 ? 106 GLY A C   1 
ATOM   2893 O  O   . GLY B 1 106 ? -4.445  36.365  -36.434 1.00 13.53 ? 106 GLY A O   1 
ATOM   2894 N  N   . SER B 1 107 ? -2.330  36.567  -37.187 1.00 10.97 ? 107 SER A N   1 
ATOM   2895 C  CA  . SER B 1 107 ? -1.840  36.644  -35.775 1.00 10.40 ? 107 SER A CA  1 
ATOM   2896 C  C   . SER B 1 107 ? -2.237  38.019  -35.113 1.00 10.34 ? 107 SER A C   1 
ATOM   2897 O  O   . SER B 1 107 ? -2.548  39.040  -35.829 1.00 10.59 ? 107 SER A O   1 
ATOM   2898 C  CB  . SER B 1 107 ? -0.355  36.421  -35.734 1.00 9.70  ? 107 SER A CB  1 
ATOM   2899 O  OG  . SER B 1 107 ? 0.338   37.522  -36.373 1.00 9.88  ? 107 SER A OG  1 
ATOM   2900 N  N   . GLU B 1 108 ? -2.325  38.010  -33.782 1.00 9.01  ? 108 GLU A N   1 
ATOM   2901 C  CA  . GLU B 1 108 ? -2.688  39.202  -33.062 1.00 10.21 ? 108 GLU A CA  1 
ATOM   2902 C  C   . GLU B 1 108 ? -1.437  40.055  -32.916 1.00 9.83  ? 108 GLU A C   1 
ATOM   2903 O  O   . GLU B 1 108 ? -1.432  41.211  -33.350 1.00 10.50 ? 108 GLU A O   1 
ATOM   2904 C  CB  . GLU B 1 108 ? -3.368  38.842  -31.703 1.00 10.82 ? 108 GLU A CB  1 
ATOM   2905 C  CG  . GLU B 1 108 ? -4.672  37.978  -31.944 1.00 10.02 ? 108 GLU A CG  1 
ATOM   2906 C  CD  . GLU B 1 108 ? -5.729  38.373  -30.948 1.00 10.63 ? 108 GLU A CD  1 
ATOM   2907 O  OE1 . GLU B 1 108 ? -5.477  38.152  -29.757 1.00 8.98  ? 108 GLU A OE1 1 
ATOM   2908 O  OE2 . GLU B 1 108 ? -6.781  38.883  -31.315 1.00 11.04 ? 108 GLU A OE2 1 
ATOM   2909 N  N   . HIS B 1 109 ? -0.394  39.523  -32.303 1.00 10.15 ? 109 HIS A N   1 
ATOM   2910 C  CA  . HIS B 1 109 ? 0.905   40.219  -32.330 1.00 10.29 ? 109 HIS A CA  1 
ATOM   2911 C  C   . HIS B 1 109 ? 1.529   40.164  -33.744 1.00 10.60 ? 109 HIS A C   1 
ATOM   2912 O  O   . HIS B 1 109 ? 1.302   39.206  -34.498 1.00 10.11 ? 109 HIS A O   1 
ATOM   2913 C  CB  . HIS B 1 109 ? 1.863   39.674  -31.276 1.00 9.95  ? 109 HIS A CB  1 
ATOM   2914 C  CG  . HIS B 1 109 ? 1.357   39.837  -29.883 1.00 10.04 ? 109 HIS A CG  1 
ATOM   2915 N  ND1 . HIS B 1 109 ? 0.448   38.974  -29.308 1.00 9.92  ? 109 HIS A ND1 1 
ATOM   2916 C  CD2 . HIS B 1 109 ? 1.605   40.782  -28.958 1.00 9.33  ? 109 HIS A CD2 1 
ATOM   2917 C  CE1 . HIS B 1 109 ? 0.139   39.383  -28.082 1.00 9.96  ? 109 HIS A CE1 1 
ATOM   2918 N  NE2 . HIS B 1 109 ? 0.812   40.487  -27.855 1.00 9.48  ? 109 HIS A NE2 1 
ATOM   2919 N  N   . ILE B 1 110 ? 2.288   41.222  -34.050 1.00 10.31 ? 110 ILE A N   1 
ATOM   2920 C  CA  . ILE B 1 110 ? 3.012   41.344  -35.313 1.00 11.21 ? 110 ILE A CA  1 
ATOM   2921 C  C   . ILE B 1 110 ? 4.458   41.774  -34.993 1.00 11.59 ? 110 ILE A C   1 
ATOM   2922 O  O   . ILE B 1 110 ? 4.676   42.725  -34.212 1.00 14.17 ? 110 ILE A O   1 
ATOM   2923 C  CB  . ILE B 1 110 ? 2.329   42.375  -36.211 1.00 12.72 ? 110 ILE A CB  1 
ATOM   2924 C  CG1 . ILE B 1 110 ? 0.895   41.935  -36.526 1.00 13.61 ? 110 ILE A CG1 1 
ATOM   2925 C  CG2 . ILE B 1 110 ? 3.092   42.572  -37.501 1.00 12.80 ? 110 ILE A CG2 1 
ATOM   2926 C  CD1 . ILE B 1 110 ? 0.123   42.954  -37.368 1.00 14.01 ? 110 ILE A CD1 1 
ATOM   2927 N  N   . VAL B 1 111 ? 5.427   41.106  -35.622 1.00 12.20 ? 111 VAL A N   1 
ATOM   2928 C  CA  . VAL B 1 111 ? 6.841   41.285  -35.157 1.00 12.79 ? 111 VAL A CA  1 
ATOM   2929 C  C   . VAL B 1 111 ? 7.591   41.946  -36.321 1.00 14.74 ? 111 VAL A C   1 
ATOM   2930 O  O   . VAL B 1 111 ? 7.721   41.285  -37.344 1.00 15.59 ? 111 VAL A O   1 
ATOM   2931 C  CB  . VAL B 1 111 ? 7.470   39.938  -34.879 1.00 14.79 ? 111 VAL A CB  1 
ATOM   2932 C  CG1 . VAL B 1 111 ? 8.986   40.073  -34.515 1.00 15.03 ? 111 VAL A CG1 1 
ATOM   2933 C  CG2 . VAL B 1 111 ? 6.685   39.264  -33.728 1.00 14.63 ? 111 VAL A CG2 1 
ATOM   2934 N  N   . ASP B 1 112 ? 8.061   43.197  -36.148 1.00 15.02 ? 112 ASP A N   1 
ATOM   2935 C  CA  . ASP B 1 112 ? 8.769   43.943  -37.263 1.00 15.94 ? 112 ASP A CA  1 
ATOM   2936 C  C   . ASP B 1 112 ? 7.951   43.888  -38.580 1.00 16.92 ? 112 ASP A C   1 
ATOM   2937 O  O   . ASP B 1 112 ? 8.498   43.727  -39.710 1.00 19.89 ? 112 ASP A O   1 
ATOM   2938 C  CB  . ASP B 1 112 ? 10.173  43.348  -37.418 1.00 16.91 ? 112 ASP A CB  1 
ATOM   2939 C  CG  . ASP B 1 112 ? 11.080  43.700  -36.212 1.00 18.94 ? 112 ASP A CG  1 
ATOM   2940 O  OD1 . ASP B 1 112 ? 10.970  44.825  -35.633 1.00 18.00 ? 112 ASP A OD1 1 
ATOM   2941 O  OD2 . ASP B 1 112 ? 11.922  42.836  -35.888 1.00 22.08 ? 112 ASP A OD2 1 
ATOM   2942 N  N   . GLY B 1 113 ? 6.631   43.981  -38.427 1.00 15.81 ? 113 GLY A N   1 
ATOM   2943 C  CA  . GLY B 1 113 ? 5.703   44.114  -39.585 1.00 15.96 ? 113 GLY A CA  1 
ATOM   2944 C  C   . GLY B 1 113 ? 5.302   42.767  -40.158 1.00 17.79 ? 113 GLY A C   1 
ATOM   2945 O  O   . GLY B 1 113 ? 4.485   42.691  -41.116 1.00 17.54 ? 113 GLY A O   1 
ATOM   2946 N  N   . VAL B 1 114 ? 5.855   41.711  -39.581 1.00 18.54 ? 114 VAL A N   1 
ATOM   2947 C  CA  . VAL B 1 114 ? 5.583   40.360  -40.061 1.00 19.03 ? 114 VAL A CA  1 
ATOM   2948 C  C   . VAL B 1 114 ? 4.430   39.729  -39.209 1.00 17.18 ? 114 VAL A C   1 
ATOM   2949 O  O   . VAL B 1 114 ? 4.540   39.590  -37.910 1.00 15.05 ? 114 VAL A O   1 
ATOM   2950 C  CB  . VAL B 1 114 ? 6.855   39.471  -40.027 1.00 21.07 ? 114 VAL A CB  1 
ATOM   2951 C  CG1 . VAL B 1 114 ? 6.537   38.005  -40.327 1.00 22.28 ? 114 VAL A CG1 1 
ATOM   2952 C  CG2 . VAL B 1 114 ? 7.925   40.015  -41.001 1.00 20.42 ? 114 VAL A CG2 1 
ATOM   2953 N  N   . SER B 1 115 ? 3.332   39.432  -39.921 1.00 13.25 ? 115 SER A N   1 
ATOM   2954 C  CA  . SER B 1 115 ? 2.232   38.645  -39.350 1.00 14.03 ? 115 SER A CA  1 
ATOM   2955 C  C   . SER B 1 115 ? 2.456   37.148  -39.623 1.00 12.91 ? 115 SER A C   1 
ATOM   2956 O  O   . SER B 1 115 ? 3.044   36.785  -40.609 1.00 15.72 ? 115 SER A O   1 
ATOM   2957 C  CB  . SER B 1 115 ? 0.893   39.055  -39.957 1.00 11.34 ? 115 SER A CB  1 
ATOM   2958 O  OG  . SER B 1 115 ? 0.524   40.373  -39.531 1.00 12.72 ? 115 SER A OG  1 
ATOM   2959 N  N   . TYR B 1 116 ? 1.933   36.295  -38.751 1.00 12.05 ? 116 TYR A N   1 
ATOM   2960 C  CA  . TYR B 1 116 ? 1.814   34.889  -38.987 1.00 11.92 ? 116 TYR A CA  1 
ATOM   2961 C  C   . TYR B 1 116 ? 0.383   34.569  -39.321 1.00 10.15 ? 116 TYR A C   1 
ATOM   2962 O  O   . TYR B 1 116 ? -0.496  35.447  -39.292 1.00 11.19 ? 116 TYR A O   1 
ATOM   2963 C  CB  . TYR B 1 116 ? 2.263   34.182  -37.696 1.00 13.66 ? 116 TYR A CB  1 
ATOM   2964 C  CG  . TYR B 1 116 ? 3.744   34.457  -37.465 1.00 14.36 ? 116 TYR A CG  1 
ATOM   2965 C  CD1 . TYR B 1 116 ? 4.709   33.739  -38.165 1.00 16.18 ? 116 TYR A CD1 1 
ATOM   2966 C  CD2 . TYR B 1 116 ? 4.182   35.503  -36.642 1.00 16.89 ? 116 TYR A CD2 1 
ATOM   2967 C  CE1 . TYR B 1 116 ? 6.053   33.947  -37.995 1.00 19.12 ? 116 TYR A CE1 1 
ATOM   2968 C  CE2 . TYR B 1 116 ? 5.558   35.728  -36.474 1.00 19.05 ? 116 TYR A CE2 1 
ATOM   2969 C  CZ  . TYR B 1 116 ? 6.465   34.944  -37.175 1.00 21.41 ? 116 TYR A CZ  1 
ATOM   2970 O  OH  . TYR B 1 116 ? 7.837   35.112  -37.053 1.00 23.98 ? 116 TYR A OH  1 
ATOM   2971 N  N   . ALA B 1 117 ? 0.116   33.310  -39.660 1.00 9.67  ? 117 ALA A N   1 
ATOM   2972 C  CA  . ALA B 1 117 ? -1.224  32.901  -40.138 1.00 8.72  ? 117 ALA A CA  1 
ATOM   2973 C  C   . ALA B 1 117 ? -2.198  32.798  -38.954 1.00 9.22  ? 117 ALA A C   1 
ATOM   2974 O  O   . ALA B 1 117 ? -3.393  33.059  -39.106 1.00 10.66 ? 117 ALA A O   1 
ATOM   2975 C  CB  . ALA B 1 117 ? -1.125  31.558  -40.840 1.00 9.25  ? 117 ALA A CB  1 
ATOM   2976 N  N   . ALA B 1 118 ? -1.676  32.469  -37.753 1.00 8.91  ? 118 ALA A N   1 
ATOM   2977 C  CA  . ALA B 1 118 ? -2.600  32.310  -36.595 1.00 7.87  ? 118 ALA A CA  1 
ATOM   2978 C  C   . ALA B 1 118 ? -1.786  32.459  -35.319 1.00 8.20  ? 118 ALA A C   1 
ATOM   2979 O  O   . ALA B 1 118 ? -0.576  32.515  -35.408 1.00 7.87  ? 118 ALA A O   1 
ATOM   2980 C  CB  . ALA B 1 118 ? -3.316  30.929  -36.638 1.00 9.06  ? 118 ALA A CB  1 
ATOM   2981 N  N   . GLU B 1 119 ? -2.439  32.514  -34.154 1.00 7.44  ? 119 GLU A N   1 
ATOM   2982 C  CA  . GLU B 1 119 ? -1.670  32.668  -32.899 1.00 7.63  ? 119 GLU A CA  1 
ATOM   2983 C  C   . GLU B 1 119 ? -2.468  31.974  -31.791 1.00 7.50  ? 119 GLU A C   1 
ATOM   2984 O  O   . GLU B 1 119 ? -3.649  32.200  -31.627 1.00 8.21  ? 119 GLU A O   1 
ATOM   2985 C  CB  . GLU B 1 119 ? -1.517  34.154  -32.569 1.00 7.73  ? 119 GLU A CB  1 
ATOM   2986 C  CG  . GLU B 1 119 ? -0.790  34.416  -31.245 1.00 7.78  ? 119 GLU A CG  1 
ATOM   2987 C  CD  . GLU B 1 119 ? -0.580  35.915  -31.082 1.00 8.72  ? 119 GLU A CD  1 
ATOM   2988 O  OE1 . GLU B 1 119 ? -0.448  36.609  -32.111 1.00 9.17  ? 119 GLU A OE1 1 
ATOM   2989 O  OE2 . GLU B 1 119 ? -0.531  36.397  -29.932 1.00 8.44  ? 119 GLU A OE2 1 
ATOM   2990 N  N   . LEU B 1 120 ? -1.801  31.073  -31.084 1.00 7.55  ? 120 LEU A N   1 
ATOM   2991 C  CA  . LEU B 1 120 ? -2.401  30.251  -30.092 1.00 7.52  ? 120 LEU A CA  1 
ATOM   2992 C  C   . LEU B 1 120 ? -2.223  30.996  -28.763 1.00 7.95  ? 120 LEU A C   1 
ATOM   2993 O  O   . LEU B 1 120 ? -1.140  31.476  -28.467 1.00 7.38  ? 120 LEU A O   1 
ATOM   2994 C  CB  . LEU B 1 120 ? -1.660  28.903  -29.993 1.00 7.64  ? 120 LEU A CB  1 
ATOM   2995 C  CG  . LEU B 1 120 ? -2.312  27.860  -29.067 1.00 8.08  ? 120 LEU A CG  1 
ATOM   2996 C  CD1 . LEU B 1 120 ? -3.538  27.260  -29.721 1.00 9.42  ? 120 LEU A CD1 1 
ATOM   2997 C  CD2 . LEU B 1 120 ? -1.268  26.781  -28.770 1.00 8.66  ? 120 LEU A CD2 1 
ATOM   2998 N  N   . HIS B 1 121 ? -3.262  31.011  -27.931 1.00 7.94  ? 121 HIS A N   1 
ATOM   2999 C  CA  . HIS B 1 121 ? -3.094  31.628  -26.635 1.00 7.57  ? 121 HIS A CA  1 
ATOM   3000 C  C   . HIS B 1 121 ? -3.349  30.577  -25.549 1.00 7.76  ? 121 HIS A C   1 
ATOM   3001 O  O   . HIS B 1 121 ? -4.373  29.914  -25.591 1.00 9.40  ? 121 HIS A O   1 
ATOM   3002 C  CB  . HIS B 1 121 ? -4.078  32.815  -26.462 1.00 7.57  ? 121 HIS A CB  1 
ATOM   3003 C  CG  . HIS B 1 121 ? -3.664  34.008  -27.241 1.00 6.83  ? 121 HIS A CG  1 
ATOM   3004 N  ND1 . HIS B 1 121 ? -4.533  35.022  -27.591 1.00 7.04  ? 121 HIS A ND1 1 
ATOM   3005 C  CD2 . HIS B 1 121 ? -2.445  34.338  -27.766 1.00 6.43  ? 121 HIS A CD2 1 
ATOM   3006 C  CE1 . HIS B 1 121 ? -3.854  35.951  -28.281 1.00 6.52  ? 121 HIS A CE1 1 
ATOM   3007 N  NE2 . HIS B 1 121 ? -2.590  35.561  -28.390 1.00 5.92  ? 121 HIS A NE2 1 
ATOM   3008 N  N   . VAL B 1 122 ? -2.485  30.563  -24.517 1.00 6.75  ? 122 VAL A N   1 
ATOM   3009 C  CA  . VAL B 1 122 ? -2.605  29.647  -23.421 1.00 6.74  ? 122 VAL A CA  1 
ATOM   3010 C  C   . VAL B 1 122 ? -2.760  30.570  -22.180 1.00 7.05  ? 122 VAL A C   1 
ATOM   3011 O  O   . VAL B 1 122 ? -1.823  31.290  -21.823 1.00 7.41  ? 122 VAL A O   1 
ATOM   3012 C  CB  . VAL B 1 122 ? -1.345  28.776  -23.248 1.00 6.57  ? 122 VAL A CB  1 
ATOM   3013 C  CG1 . VAL B 1 122 ? -1.592  27.701  -22.193 1.00 6.65  ? 122 VAL A CG1 1 
ATOM   3014 C  CG2 . VAL B 1 122 ? -0.897  28.110  -24.601 1.00 6.62  ? 122 VAL A CG2 1 
ATOM   3015 N  N   . VAL B 1 123 ? -3.909  30.511  -21.514 1.00 6.83  ? 123 VAL A N   1 
ATOM   3016 C  CA  . VAL B 1 123 ? -4.316  31.565  -20.539 1.00 6.90  ? 123 VAL A CA  1 
ATOM   3017 C  C   . VAL B 1 123 ? -4.164  30.958  -19.141 1.00 7.07  ? 123 VAL A C   1 
ATOM   3018 O  O   . VAL B 1 123 ? -4.637  29.825  -18.929 1.00 8.31  ? 123 VAL A O   1 
ATOM   3019 C  CB  . VAL B 1 123 ? -5.802  31.956  -20.768 1.00 7.01  ? 123 VAL A CB  1 
ATOM   3020 C  CG1 . VAL B 1 123 ? -6.261  32.965  -19.681 1.00 6.65  ? 123 VAL A CG1 1 
ATOM   3021 C  CG2 . VAL B 1 123 ? -5.953  32.523  -22.196 1.00 6.49  ? 123 VAL A CG2 1 
ATOM   3022 N  N   . HIS B 1 124 ? -3.462  31.666  -18.244 1.00 7.31  ? 124 HIS A N   1 
ATOM   3023 C  CA  . HIS B 1 124 ? -3.188  31.212  -16.884 1.00 8.23  ? 124 HIS A CA  1 
ATOM   3024 C  C   . HIS B 1 124 ? -3.563  32.299  -15.921 1.00 9.39  ? 124 HIS A C   1 
ATOM   3025 O  O   . HIS B 1 124 ? -3.524  33.472  -16.266 1.00 8.61  ? 124 HIS A O   1 
ATOM   3026 C  CB  . HIS B 1 124 ? -1.685  30.921  -16.661 1.00 7.98  ? 124 HIS A CB  1 
ATOM   3027 C  CG  . HIS B 1 124 ? -1.042  30.113  -17.733 1.00 7.38  ? 124 HIS A CG  1 
ATOM   3028 N  ND1 . HIS B 1 124 ? -0.780  30.606  -19.000 1.00 7.49  ? 124 HIS A ND1 1 
ATOM   3029 C  CD2 . HIS B 1 124 ? -0.580  28.825  -17.714 1.00 7.77  ? 124 HIS A CD2 1 
ATOM   3030 C  CE1 . HIS B 1 124 ? -0.196  29.636  -19.715 1.00 7.20  ? 124 HIS A CE1 1 
ATOM   3031 N  NE2 . HIS B 1 124 ? -0.035  28.569  -18.962 1.00 7.67  ? 124 HIS A NE2 1 
ATOM   3032 N  N   . TRP B 1 125 ? -3.815  31.906  -14.669 1.00 10.30 ? 125 TRP A N   1 
ATOM   3033 C  CA  . TRP B 1 125 ? -4.228  32.902  -13.613 1.00 10.09 ? 125 TRP A CA  1 
ATOM   3034 C  C   . TRP B 1 125 ? -3.469  32.648  -12.263 1.00 9.26  ? 125 TRP A C   1 
ATOM   3035 O  O   . TRP B 1 125 ? -3.128  31.504  -11.927 1.00 8.80  ? 125 TRP A O   1 
ATOM   3036 C  CB  . TRP B 1 125 ? -5.762  32.902  -13.405 1.00 9.89  ? 125 TRP A CB  1 
ATOM   3037 C  CG  . TRP B 1 125 ? -6.364  31.621  -12.925 1.00 9.97  ? 125 TRP A CG  1 
ATOM   3038 C  CD1 . TRP B 1 125 ? -6.724  30.552  -13.684 1.00 10.49 ? 125 TRP A CD1 1 
ATOM   3039 C  CD2 . TRP B 1 125 ? -6.707  31.271  -11.557 1.00 9.78  ? 125 TRP A CD2 1 
ATOM   3040 N  NE1 . TRP B 1 125 ? -7.304  29.542  -12.910 1.00 9.32  ? 125 TRP A NE1 1 
ATOM   3041 C  CE2 . TRP B 1 125 ? -7.237  29.941  -11.588 1.00 9.70  ? 125 TRP A CE2 1 
ATOM   3042 C  CE3 . TRP B 1 125 ? -6.565  31.937  -10.314 1.00 9.81  ? 125 TRP A CE3 1 
ATOM   3043 C  CZ2 . TRP B 1 125 ? -7.713  29.273  -10.446 1.00 9.01  ? 125 TRP A CZ2 1 
ATOM   3044 C  CZ3 . TRP B 1 125 ? -7.083  31.279  -9.173  1.00 9.54  ? 125 TRP A CZ3 1 
ATOM   3045 C  CH2 . TRP B 1 125 ? -7.576  29.934  -9.244  1.00 9.09  ? 125 TRP A CH2 1 
ATOM   3046 N  N   . ASN B 1 126 ? -3.221  33.726  -11.546 1.00 8.96  ? 126 ASN A N   1 
ATOM   3047 C  CA  . ASN B 1 126 ? -2.343  33.718  -10.363 1.00 8.98  ? 126 ASN A CA  1 
ATOM   3048 C  C   . ASN B 1 126 ? -3.135  33.132  -9.191  1.00 9.37  ? 126 ASN A C   1 
ATOM   3049 O  O   . ASN B 1 126 ? -3.917  33.855  -8.540  1.00 10.43 ? 126 ASN A O   1 
ATOM   3050 C  CB  . ASN B 1 126 ? -1.967  35.159  -10.043 1.00 9.22  ? 126 ASN A CB  1 
ATOM   3051 C  CG  . ASN B 1 126 ? -0.976  35.255  -8.865  1.00 11.57 ? 126 ASN A CG  1 
ATOM   3052 O  OD1 . ASN B 1 126 ? -0.887  34.338  -8.038  1.00 11.39 ? 126 ASN A OD1 1 
ATOM   3053 N  ND2 . ASN B 1 126 ? -0.263  36.363  -8.784  1.00 12.57 ? 126 ASN A ND2 1 
ATOM   3054 N  N   . SER B 1 127 ? -2.943  31.834  -8.943  1.00 8.91  ? 127 SER A N   1 
ATOM   3055 C  CA  . SER B 1 127 ? -3.747  31.136  -7.894  1.00 8.87  ? 127 SER A CA  1 
ATOM   3056 C  C   . SER B 1 127 ? -3.008  31.275  -6.551  1.00 10.88 ? 127 SER A C   1 
ATOM   3057 O  O   . SER B 1 127 ? -3.515  30.844  -5.507  1.00 9.12  ? 127 SER A O   1 
ATOM   3058 C  CB  . SER B 1 127 ? -3.895  29.654  -8.254  1.00 9.23  ? 127 SER A CB  1 
ATOM   3059 O  OG  . SER B 1 127 ? -2.611  29.056  -8.479  1.00 10.98 ? 127 SER A OG  1 
ATOM   3060 N  N   . ASP B 1 128 ? -1.816  31.863  -6.585  1.00 10.68 ? 128 ASP A N   1 
ATOM   3061 C  CA  . ASP B 1 128 ? -1.100  32.140  -5.301  1.00 11.75 ? 128 ASP A CA  1 
ATOM   3062 C  C   . ASP B 1 128 ? -1.713  33.356  -4.616  1.00 13.30 ? 128 ASP A C   1 
ATOM   3063 O  O   . ASP B 1 128 ? -1.511  33.529  -3.374  1.00 14.19 ? 128 ASP A O   1 
ATOM   3064 C  CB  . ASP B 1 128 ? 0.388   32.408  -5.543  1.00 12.68 ? 128 ASP A CB  1 
ATOM   3065 C  CG  . ASP B 1 128 ? 1.185   31.159  -5.782  1.00 13.01 ? 128 ASP A CG  1 
ATOM   3066 O  OD1 . ASP B 1 128 ? 0.684   30.036  -5.646  1.00 15.09 ? 128 ASP A OD1 1 
ATOM   3067 O  OD2 . ASP B 1 128 ? 2.368   31.317  -6.088  1.00 12.81 ? 128 ASP A OD2 1 
ATOM   3068 N  N   . LYS B 1 129 ? -2.382  34.247  -5.391  1.00 12.71 ? 129 LYS A N   1 
ATOM   3069 C  CA  . LYS B 1 129 ? -3.006  35.463  -4.816  1.00 13.24 ? 129 LYS A CA  1 
ATOM   3070 C  C   . LYS B 1 129 ? -4.495  35.583  -4.892  1.00 12.79 ? 129 LYS A C   1 
ATOM   3071 O  O   . LYS B 1 129 ? -5.108  36.336  -4.114  1.00 12.08 ? 129 LYS A O   1 
ATOM   3072 C  CB  . LYS B 1 129 ? -2.441  36.756  -5.408  1.00 14.64 ? 129 LYS A CB  1 
ATOM   3073 C  CG  . LYS B 1 129 ? -1.029  37.011  -4.914  1.00 15.83 ? 129 LYS A CG  1 
ATOM   3074 C  CD  . LYS B 1 129 ? -0.400  38.308  -5.458  1.00 17.68 ? 129 LYS A CD  1 
ATOM   3075 C  CE  . LYS B 1 129 ? -1.157  39.553  -5.003  1.00 17.99 ? 129 LYS A CE  1 
ATOM   3076 N  NZ  . LYS B 1 129 ? -0.438  40.747  -5.584  1.00 18.87 ? 129 LYS A NZ  1 
ATOM   3077 N  N   . TYR B 1 130 ? -5.086  34.974  -5.905  1.00 11.75 ? 130 TYR A N   1 
ATOM   3078 C  CA  . TYR B 1 130 ? -6.497  35.230  -6.207  1.00 11.88 ? 130 TYR A CA  1 
ATOM   3079 C  C   . TYR B 1 130 ? -7.316  33.941  -6.137  1.00 10.69 ? 130 TYR A C   1 
ATOM   3080 O  O   . TYR B 1 130 ? -6.776  32.870  -6.325  1.00 11.91 ? 130 TYR A O   1 
ATOM   3081 C  CB  . TYR B 1 130 ? -6.654  35.946  -7.604  1.00 11.21 ? 130 TYR A CB  1 
ATOM   3082 C  CG  . TYR B 1 130 ? -5.834  37.199  -7.617  1.00 12.95 ? 130 TYR A CG  1 
ATOM   3083 C  CD1 . TYR B 1 130 ? -6.068  38.209  -6.639  1.00 14.60 ? 130 TYR A CD1 1 
ATOM   3084 C  CD2 . TYR B 1 130 ? -4.772  37.388  -8.506  1.00 12.11 ? 130 TYR A CD2 1 
ATOM   3085 C  CE1 . TYR B 1 130 ? -5.279  39.327  -6.553  1.00 15.47 ? 130 TYR A CE1 1 
ATOM   3086 C  CE2 . TYR B 1 130 ? -3.982  38.540  -8.456  1.00 13.01 ? 130 TYR A CE2 1 
ATOM   3087 C  CZ  . TYR B 1 130 ? -4.218  39.517  -7.469  1.00 13.82 ? 130 TYR A CZ  1 
ATOM   3088 O  OH  . TYR B 1 130 ? -3.419  40.646  -7.352  1.00 12.66 ? 130 TYR A OH  1 
ATOM   3089 N  N   . PRO B 1 131 ? -8.647  34.027  -5.861  1.00 11.88 ? 131 PRO A N   1 
ATOM   3090 C  CA  . PRO B 1 131 ? -9.405  32.774  -5.660  1.00 12.31 ? 131 PRO A CA  1 
ATOM   3091 C  C   . PRO B 1 131 ? -9.921  32.118  -6.900  1.00 12.01 ? 131 PRO A C   1 
ATOM   3092 O  O   . PRO B 1 131 ? -10.374 30.978  -6.845  1.00 12.75 ? 131 PRO A O   1 
ATOM   3093 C  CB  . PRO B 1 131 ? -10.633 33.220  -4.845  1.00 12.96 ? 131 PRO A CB  1 
ATOM   3094 C  CG  . PRO B 1 131 ? -10.812 34.656  -5.220  1.00 13.38 ? 131 PRO A CG  1 
ATOM   3095 C  CD  . PRO B 1 131 ? -9.402  35.197  -5.403  1.00 12.81 ? 131 PRO A CD  1 
ATOM   3096 N  N   . SER B 1 132 ? -9.817  32.799  -8.062  1.00 12.41 ? 132 SER A N   1 
ATOM   3097 C  CA  . SER B 1 132 ? -10.394 32.249  -9.275  1.00 12.09 ? 132 SER A CA  1 
ATOM   3098 C  C   . SER B 1 132 ? -9.851  33.048  -10.443 1.00 11.41 ? 132 SER A C   1 
ATOM   3099 O  O   . SER B 1 132 ? -9.379  34.180  -10.271 1.00 11.40 ? 132 SER A O   1 
ATOM   3100 C  CB  . SER B 1 132 ? -11.946 32.410  -9.268  1.00 13.16 ? 132 SER A CB  1 
ATOM   3101 O  OG  . SER B 1 132 ? -12.315 33.782  -9.222  1.00 12.08 ? 132 SER A OG  1 
ATOM   3102 N  N   . PHE B 1 133 ? -10.034 32.455  -11.616 1.00 12.58 ? 133 PHE A N   1 
ATOM   3103 C  CA  . PHE B 1 133 ? -9.730  33.054  -12.871 1.00 12.60 ? 133 PHE A CA  1 
ATOM   3104 C  C   . PHE B 1 133 ? -10.519 34.329  -13.045 1.00 13.13 ? 133 PHE A C   1 
ATOM   3105 O  O   . PHE B 1 133 ? -9.983  35.332  -13.470 1.00 13.80 ? 133 PHE A O   1 
ATOM   3106 C  CB  . PHE B 1 133 ? -10.074 32.036  -13.959 1.00 14.34 ? 133 PHE A CB  1 
ATOM   3107 C  CG  . PHE B 1 133 ? -10.021 32.589  -15.346 1.00 13.51 ? 133 PHE A CG  1 
ATOM   3108 C  CD1 . PHE B 1 133 ? -8.828  33.098  -15.867 1.00 13.84 ? 133 PHE A CD1 1 
ATOM   3109 C  CD2 . PHE B 1 133 ? -11.157 32.490  -16.175 1.00 14.68 ? 133 PHE A CD2 1 
ATOM   3110 C  CE1 . PHE B 1 133 ? -8.781  33.618  -17.150 1.00 13.95 ? 133 PHE A CE1 1 
ATOM   3111 C  CE2 . PHE B 1 133 ? -11.093 32.965  -17.501 1.00 16.90 ? 133 PHE A CE2 1 
ATOM   3112 C  CZ  . PHE B 1 133 ? -9.878  33.529  -17.976 1.00 14.27 ? 133 PHE A CZ  1 
ATOM   3113 N  N   . VAL B 1 134 ? -11.808 34.296  -12.714 1.00 14.76 ? 134 VAL A N   1 
ATOM   3114 C  CA  . VAL B 1 134 ? -12.594 35.483  -12.870 1.00 17.09 ? 134 VAL A CA  1 
ATOM   3115 C  C   . VAL B 1 134 ? -12.169 36.657  -12.019 1.00 15.73 ? 134 VAL A C   1 
ATOM   3116 O  O   . VAL B 1 134 ? -12.249 37.792  -12.456 1.00 17.08 ? 134 VAL A O   1 
ATOM   3117 C  CB  . VAL B 1 134 ? -14.129 35.202  -12.837 1.00 21.77 ? 134 VAL A CB  1 
ATOM   3118 C  CG1 . VAL B 1 134 ? -14.503 34.210  -13.935 1.00 22.18 ? 134 VAL A CG1 1 
ATOM   3119 C  CG2 . VAL B 1 134 ? -14.529 34.646  -11.511 1.00 24.10 ? 134 VAL A CG2 1 
ATOM   3120 N  N   A GLU B 1 135 ? -11.719 36.417  -10.791 0.50 14.64 ? 135 GLU A N   1 
ATOM   3121 N  N   B GLU B 1 135 ? -11.744 36.392  -10.793 0.50 15.59 ? 135 GLU A N   1 
ATOM   3122 C  CA  A GLU B 1 135 ? -11.264 37.519  -9.961  0.50 14.27 ? 135 GLU A CA  1 
ATOM   3123 C  CA  B GLU B 1 135 ? -11.271 37.431  -9.914  0.50 15.73 ? 135 GLU A CA  1 
ATOM   3124 C  C   A GLU B 1 135 ? -9.829  37.998  -10.296 0.50 13.96 ? 135 GLU A C   1 
ATOM   3125 C  C   B GLU B 1 135 ? -9.926  37.978  -10.452 0.50 14.89 ? 135 GLU A C   1 
ATOM   3126 O  O   A GLU B 1 135 ? -9.485  39.181  -10.123 0.50 13.96 ? 135 GLU A O   1 
ATOM   3127 O  O   B GLU B 1 135 ? -9.770  39.188  -10.639 0.50 15.34 ? 135 GLU A O   1 
ATOM   3128 C  CB  A GLU B 1 135 ? -11.442 37.208  -8.453  0.50 13.79 ? 135 GLU A CB  1 
ATOM   3129 C  CB  B GLU B 1 135 ? -11.178 36.857  -8.480  0.50 16.66 ? 135 GLU A CB  1 
ATOM   3130 C  CG  A GLU B 1 135 ? -11.420 38.479  -7.644  0.50 15.37 ? 135 GLU A CG  1 
ATOM   3131 C  CG  B GLU B 1 135 ? -11.268 37.805  -7.321  0.50 19.64 ? 135 GLU A CG  1 
ATOM   3132 C  CD  A GLU B 1 135 ? -10.035 39.064  -7.633  0.50 13.76 ? 135 GLU A CD  1 
ATOM   3133 C  CD  B GLU B 1 135 ? -12.533 38.658  -7.266  0.50 18.66 ? 135 GLU A CD  1 
ATOM   3134 O  OE1 A GLU B 1 135 ? -9.085  38.254  -7.723  0.50 13.01 ? 135 GLU A OE1 1 
ATOM   3135 O  OE1 B GLU B 1 135 ? -13.633 38.240  -6.803  0.50 19.69 ? 135 GLU A OE1 1 
ATOM   3136 O  OE2 A GLU B 1 135 ? -9.907  40.304  -7.517  0.50 12.11 ? 135 GLU A OE2 1 
ATOM   3137 O  OE2 B GLU B 1 135 ? -12.376 39.821  -7.616  0.50 19.69 ? 135 GLU A OE2 1 
ATOM   3138 N  N   . ALA B 1 136 ? -8.993  37.064  -10.745 1.00 13.58 ? 136 ALA A N   1 
ATOM   3139 C  CA  . ALA B 1 136 ? -7.658  37.367  -11.160 1.00 12.06 ? 136 ALA A CA  1 
ATOM   3140 C  C   . ALA B 1 136 ? -7.649  38.252  -12.428 1.00 11.63 ? 136 ALA A C   1 
ATOM   3141 O  O   . ALA B 1 136 ? -6.781  39.102  -12.566 1.00 11.92 ? 136 ALA A O   1 
ATOM   3142 C  CB  . ALA B 1 136 ? -6.894  36.071  -11.446 1.00 10.58 ? 136 ALA A CB  1 
ATOM   3143 N  N   . ALA B 1 137 ? -8.628  38.026  -13.295 1.00 11.42 ? 137 ALA A N   1 
ATOM   3144 C  CA  . ALA B 1 137 ? -8.751  38.801  -14.518 1.00 10.93 ? 137 ALA A CA  1 
ATOM   3145 C  C   . ALA B 1 137 ? -8.886  40.339  -14.293 1.00 11.66 ? 137 ALA A C   1 
ATOM   3146 O  O   . ALA B 1 137 ? -8.727  41.089  -15.227 1.00 12.14 ? 137 ALA A O   1 
ATOM   3147 C  CB  . ALA B 1 137 ? -9.912  38.271  -15.356 1.00 12.41 ? 137 ALA A CB  1 
ATOM   3148 N  N   . HIS B 1 138 ? -9.245  40.755  -13.065 1.00 12.69 ? 138 HIS A N   1 
ATOM   3149 C  CA  . HIS B 1 138 ? -9.421  42.150  -12.658 1.00 15.16 ? 138 HIS A CA  1 
ATOM   3150 C  C   . HIS B 1 138 ? -8.227  42.726  -11.922 1.00 16.14 ? 138 HIS A C   1 
ATOM   3151 O  O   . HIS B 1 138 ? -8.348  43.810  -11.269 1.00 15.62 ? 138 HIS A O   1 
ATOM   3152 C  CB  . HIS B 1 138 ? -10.727 42.337  -11.777 1.00 15.24 ? 138 HIS A CB  1 
ATOM   3153 C  CG  . HIS B 1 138 ? -11.965 42.072  -12.548 1.00 18.11 ? 138 HIS A CG  1 
ATOM   3154 N  ND1 . HIS B 1 138 ? -12.622 43.055  -13.268 1.00 20.11 ? 138 HIS A ND1 1 
ATOM   3155 C  CD2 . HIS B 1 138 ? -12.589 40.904  -12.843 1.00 19.25 ? 138 HIS A CD2 1 
ATOM   3156 C  CE1 . HIS B 1 138 ? -13.612 42.510  -13.951 1.00 19.81 ? 138 HIS A CE1 1 
ATOM   3157 N  NE2 . HIS B 1 138 ? -13.639 41.212  -13.679 1.00 21.48 ? 138 HIS A NE2 1 
ATOM   3158 N  N   . GLU B 1 139 ? -7.092  41.996  -11.935 1.00 15.46 ? 139 GLU A N   1 
ATOM   3159 C  CA  . GLU B 1 139 ? -5.902  42.430  -11.205 1.00 16.27 ? 139 GLU A CA  1 
ATOM   3160 C  C   . GLU B 1 139 ? -4.697  42.587  -12.117 1.00 14.97 ? 139 GLU A C   1 
ATOM   3161 O  O   . GLU B 1 139 ? -4.514  41.746  -12.982 1.00 13.25 ? 139 GLU A O   1 
ATOM   3162 C  CB  . GLU B 1 139 ? -5.519  41.364  -10.191 1.00 18.26 ? 139 GLU A CB  1 
ATOM   3163 C  CG  . GLU B 1 139 ? -6.673  40.958  -9.285  1.00 20.81 ? 139 GLU A CG  1 
ATOM   3164 C  CD  . GLU B 1 139 ? -6.924  41.971  -8.193  1.00 21.77 ? 139 GLU A CD  1 
ATOM   3165 O  OE1 . GLU B 1 139 ? -6.259  43.044  -8.141  1.00 24.42 ? 139 GLU A OE1 1 
ATOM   3166 O  OE2 . GLU B 1 139 ? -7.784  41.638  -7.329  1.00 26.86 ? 139 GLU A OE2 1 
ATOM   3167 N  N   . PRO B 1 140 ? -3.857  43.601  -11.911 1.00 15.02 ? 140 PRO A N   1 
ATOM   3168 C  CA  . PRO B 1 140 ? -2.744  43.820  -12.887 1.00 13.89 ? 140 PRO A CA  1 
ATOM   3169 C  C   . PRO B 1 140 ? -1.818  42.604  -12.999 1.00 12.86 ? 140 PRO A C   1 
ATOM   3170 O  O   . PRO B 1 140 ? -1.274  42.318  -14.072 1.00 11.75 ? 140 PRO A O   1 
ATOM   3171 C  CB  . PRO B 1 140 ? -2.020  45.057  -12.327 1.00 16.46 ? 140 PRO A CB  1 
ATOM   3172 C  CG  . PRO B 1 140 ? -3.084  45.737  -11.540 1.00 19.49 ? 140 PRO A CG  1 
ATOM   3173 C  CD  . PRO B 1 140 ? -3.895  44.660  -10.869 1.00 17.70 ? 140 PRO A CD  1 
ATOM   3174 N  N   . ASP B 1 141 ? -1.633  41.881  -11.877 1.00 11.45 ? 141 ASP A N   1 
ATOM   3175 C  CA  . ASP B 1 141 ? -0.795  40.702  -11.841 1.00 12.29 ? 141 ASP A CA  1 
ATOM   3176 C  C   . ASP B 1 141 ? -1.620  39.417  -11.866 1.00 10.83 ? 141 ASP A C   1 
ATOM   3177 O  O   . ASP B 1 141 ? -1.140  38.348  -11.468 1.00 10.48 ? 141 ASP A O   1 
ATOM   3178 C  CB  . ASP B 1 141 ? 0.102   40.786  -10.606 1.00 11.80 ? 141 ASP A CB  1 
ATOM   3179 C  CG  . ASP B 1 141 ? -0.676  40.722  -9.284  1.00 13.79 ? 141 ASP A CG  1 
ATOM   3180 O  OD1 . ASP B 1 141 ? -1.903  40.893  -9.247  1.00 13.72 ? 141 ASP A OD1 1 
ATOM   3181 O  OD2 . ASP B 1 141 ? -0.034  40.506  -8.262  1.00 14.23 ? 141 ASP A OD2 1 
ATOM   3182 N  N   . GLY B 1 142 ? -2.861  39.499  -12.379 1.00 10.12 ? 142 GLY A N   1 
ATOM   3183 C  CA  . GLY B 1 142 ? -3.799  38.364  -12.261 1.00 9.58  ? 142 GLY A CA  1 
ATOM   3184 C  C   . GLY B 1 142 ? -3.545  37.253  -13.289 1.00 10.05 ? 142 GLY A C   1 
ATOM   3185 O  O   . GLY B 1 142 ? -3.620  36.107  -12.983 1.00 9.59  ? 142 GLY A O   1 
ATOM   3186 N  N   . LEU B 1 143 ? -3.204  37.649  -14.539 1.00 9.19  ? 143 LEU A N   1 
ATOM   3187 C  CA  . LEU B 1 143 ? -3.198  36.667  -15.628 1.00 7.79  ? 143 LEU A CA  1 
ATOM   3188 C  C   . LEU B 1 143 ? -1.818  36.640  -16.314 1.00 7.73  ? 143 LEU A C   1 
ATOM   3189 O  O   . LEU B 1 143 ? -1.088  37.640  -16.307 1.00 8.51  ? 143 LEU A O   1 
ATOM   3190 C  CB  . LEU B 1 143 ? -4.221  37.042  -16.687 1.00 7.72  ? 143 LEU A CB  1 
ATOM   3191 C  CG  . LEU B 1 143 ? -5.688  37.147  -16.145 1.00 7.64  ? 143 LEU A CG  1 
ATOM   3192 C  CD1 . LEU B 1 143 ? -6.567  37.477  -17.373 1.00 7.35  ? 143 LEU A CD1 1 
ATOM   3193 C  CD2 . LEU B 1 143 ? -6.235  35.870  -15.482 1.00 8.54  ? 143 LEU A CD2 1 
ATOM   3194 N  N   . ALA B 1 144 ? -1.524  35.493  -16.923 1.00 7.51  ? 144 ALA A N   1 
ATOM   3195 C  CA  . ALA B 1 144 ? -0.340  35.395  -17.785 1.00 7.81  ? 144 ALA A CA  1 
ATOM   3196 C  C   . ALA B 1 144 ? -0.768  34.630  -18.988 1.00 8.27  ? 144 ALA A C   1 
ATOM   3197 O  O   . ALA B 1 144 ? -1.421  33.565  -18.848 1.00 8.88  ? 144 ALA A O   1 
ATOM   3198 C  CB  . ALA B 1 144 ? 0.748   34.642  -17.012 1.00 8.53  ? 144 ALA A CB  1 
ATOM   3199 N  N   . VAL B 1 145 ? -0.405  35.132  -20.164 1.00 7.51  ? 145 VAL A N   1 
ATOM   3200 C  CA  . VAL B 1 145 ? -0.807  34.402  -21.387 1.00 7.78  ? 145 VAL A CA  1 
ATOM   3201 C  C   . VAL B 1 145 ? 0.442   34.115  -22.205 1.00 8.00  ? 145 VAL A C   1 
ATOM   3202 O  O   . VAL B 1 145 ? 1.282   35.042  -22.420 1.00 8.69  ? 145 VAL A O   1 
ATOM   3203 C  CB  . VAL B 1 145 ? -1.812  35.230  -22.212 1.00 6.99  ? 145 VAL A CB  1 
ATOM   3204 C  CG1 . VAL B 1 145 ? -2.222  34.417  -23.472 1.00 6.74  ? 145 VAL A CG1 1 
ATOM   3205 C  CG2 . VAL B 1 145 ? -3.059  35.544  -21.345 1.00 7.06  ? 145 VAL A CG2 1 
ATOM   3206 N  N   . LEU B 1 146 ? 0.573   32.862  -22.607 1.00 8.65  ? 146 LEU A N   1 
ATOM   3207 C  CA  . LEU B 1 146 ? 1.639   32.516  -23.555 1.00 9.13  ? 146 LEU A CA  1 
ATOM   3208 C  C   . LEU B 1 146 ? 1.072   32.609  -24.926 1.00 9.08  ? 146 LEU A C   1 
ATOM   3209 O  O   . LEU B 1 146 ? -0.018  32.069  -25.180 1.00 10.11 ? 146 LEU A O   1 
ATOM   3210 C  CB  . LEU B 1 146 ? 1.996   31.029  -23.377 1.00 11.87 ? 146 LEU A CB  1 
ATOM   3211 C  CG  . LEU B 1 146 ? 2.707   30.498  -22.192 1.00 15.58 ? 146 LEU A CG  1 
ATOM   3212 C  CD1 . LEU B 1 146 ? 2.910   28.978  -22.501 1.00 16.24 ? 146 LEU A CD1 1 
ATOM   3213 C  CD2 . LEU B 1 146 ? 4.046   31.183  -22.013 1.00 15.45 ? 146 LEU A CD2 1 
ATOM   3214 N  N   . GLY B 1 147 ? 1.801   33.283  -25.851 1.00 7.63  ? 147 GLY A N   1 
ATOM   3215 C  CA  . GLY B 1 147 ? 1.349   33.445  -27.296 1.00 7.61  ? 147 GLY A CA  1 
ATOM   3216 C  C   . GLY B 1 147 ? 2.341   32.606  -28.127 1.00 8.22  ? 147 GLY A C   1 
ATOM   3217 O  O   . GLY B 1 147 ? 3.545   32.630  -27.834 1.00 9.79  ? 147 GLY A O   1 
ATOM   3218 N  N   . VAL B 1 148 ? 1.783   31.741  -28.989 1.00 8.13  ? 148 VAL A N   1 
ATOM   3219 C  CA  . VAL B 1 148 ? 2.607   30.936  -29.905 1.00 8.42  ? 148 VAL A CA  1 
ATOM   3220 C  C   . VAL B 1 148 ? 2.117   31.227  -31.269 1.00 8.29  ? 148 VAL A C   1 
ATOM   3221 O  O   . VAL B 1 148 ? 0.910   31.080  -31.598 1.00 9.51  ? 148 VAL A O   1 
ATOM   3222 C  CB  . VAL B 1 148 ? 2.422   29.400  -29.650 1.00 8.12  ? 148 VAL A CB  1 
ATOM   3223 C  CG1 . VAL B 1 148 ? 3.317   28.583  -30.593 1.00 8.64  ? 148 VAL A CG1 1 
ATOM   3224 C  CG2 . VAL B 1 148 ? 2.801   29.072  -28.168 1.00 9.28  ? 148 VAL A CG2 1 
ATOM   3225 N  N   . PHE B 1 149 ? 3.060   31.604  -32.133 1.00 9.04  ? 149 PHE A N   1 
ATOM   3226 C  CA  . PHE B 1 149 ? 2.701   31.857  -33.494 1.00 8.94  ? 149 PHE A CA  1 
ATOM   3227 C  C   . PHE B 1 149 ? 2.577   30.584  -34.285 1.00 8.73  ? 149 PHE A C   1 
ATOM   3228 O  O   . PHE B 1 149 ? 3.375   29.659  -34.088 1.00 8.74  ? 149 PHE A O   1 
ATOM   3229 C  CB  . PHE B 1 149 ? 3.800   32.733  -34.103 1.00 8.95  ? 149 PHE A CB  1 
ATOM   3230 C  CG  . PHE B 1 149 ? 3.855   34.157  -33.534 1.00 9.50  ? 149 PHE A CG  1 
ATOM   3231 C  CD1 . PHE B 1 149 ? 2.745   35.012  -33.580 1.00 10.18 ? 149 PHE A CD1 1 
ATOM   3232 C  CD2 . PHE B 1 149 ? 5.080   34.645  -32.991 1.00 11.16 ? 149 PHE A CD2 1 
ATOM   3233 C  CE1 . PHE B 1 149 ? 2.842   36.342  -33.063 1.00 9.66  ? 149 PHE A CE1 1 
ATOM   3234 C  CE2 . PHE B 1 149 ? 5.190   35.984  -32.541 1.00 9.64  ? 149 PHE A CE2 1 
ATOM   3235 C  CZ  . PHE B 1 149 ? 4.050   36.808  -32.534 1.00 10.68 ? 149 PHE A CZ  1 
ATOM   3236 N  N   . LEU B 1 150 ? 1.628   30.573  -35.249 1.00 9.03  ? 150 LEU A N   1 
ATOM   3237 C  CA  . LEU B 1 150 ? 1.496   29.423  -36.216 1.00 10.14 ? 150 LEU A CA  1 
ATOM   3238 C  C   . LEU B 1 150 ? 1.784   30.021  -37.596 1.00 10.82 ? 150 LEU A C   1 
ATOM   3239 O  O   . LEU B 1 150 ? 1.091   30.946  -38.071 1.00 10.97 ? 150 LEU A O   1 
ATOM   3240 C  CB  . LEU B 1 150 ? 0.114   28.782  -36.172 1.00 10.32 ? 150 LEU A CB  1 
ATOM   3241 C  CG  . LEU B 1 150 ? -0.226  27.887  -34.966 1.00 10.22 ? 150 LEU A CG  1 
ATOM   3242 C  CD1 . LEU B 1 150 ? -0.408  28.676  -33.629 1.00 10.56 ? 150 LEU A CD1 1 
ATOM   3243 C  CD2 . LEU B 1 150 ? -1.553  27.136  -35.244 1.00 10.88 ? 150 LEU A CD2 1 
ATOM   3244 N  N   . GLN B 1 151 ? 2.865   29.532  -38.183 1.00 10.05 ? 151 GLN A N   1 
ATOM   3245 C  CA  . GLN B 1 151 ? 3.210   29.923  -39.551 1.00 10.04 ? 151 GLN A CA  1 
ATOM   3246 C  C   . GLN B 1 151 ? 2.715   28.834  -40.509 1.00 10.97 ? 151 GLN A C   1 
ATOM   3247 O  O   . GLN B 1 151 ? 2.697   27.638  -40.180 1.00 9.92  ? 151 GLN A O   1 
ATOM   3248 C  CB  . GLN B 1 151 ? 4.694   30.128  -39.706 1.00 12.52 ? 151 GLN A CB  1 
ATOM   3249 C  CG  . GLN B 1 151 ? 5.505   28.838  -39.539 1.00 12.77 ? 151 GLN A CG  1 
ATOM   3250 C  CD  . GLN B 1 151 ? 7.019   29.017  -39.652 1.00 16.52 ? 151 GLN A CD  1 
ATOM   3251 O  OE1 . GLN B 1 151 ? 7.528   30.102  -39.847 1.00 17.88 ? 151 GLN A OE1 1 
ATOM   3252 N  NE2 . GLN B 1 151 ? 7.752   27.890  -39.493 1.00 17.09 ? 151 GLN A NE2 1 
ATOM   3253 N  N   . ILE B 1 152 ? 2.382   29.229  -41.739 1.00 11.06 ? 152 ILE A N   1 
ATOM   3254 C  CA  . ILE B 1 152 ? 2.044   28.276  -42.781 1.00 11.89 ? 152 ILE A CA  1 
ATOM   3255 C  C   . ILE B 1 152 ? 3.261   27.333  -43.056 1.00 12.91 ? 152 ILE A C   1 
ATOM   3256 O  O   . ILE B 1 152 ? 4.417   27.800  -43.241 1.00 13.59 ? 152 ILE A O   1 
ATOM   3257 C  CB  . ILE B 1 152 ? 1.495   28.981  -44.059 1.00 12.34 ? 152 ILE A CB  1 
ATOM   3258 C  CG1 . ILE B 1 152 ? 0.132   29.685  -43.784 1.00 14.60 ? 152 ILE A CG1 1 
ATOM   3259 C  CG2 . ILE B 1 152 ? 1.370   27.907  -45.190 1.00 13.57 ? 152 ILE A CG2 1 
ATOM   3260 C  CD1 . ILE B 1 152 ? -0.952  28.715  -43.264 1.00 13.16 ? 152 ILE A CD1 1 
ATOM   3261 N  N   . GLY B 1 153 ? 3.039   26.026  -42.982 1.00 12.79 ? 153 GLY A N   1 
ATOM   3262 C  CA  . GLY B 1 153 ? 4.089   25.085  -43.280 1.00 14.05 ? 153 GLY A CA  1 
ATOM   3263 C  C   . GLY B 1 153 ? 3.463   23.741  -43.558 1.00 13.68 ? 153 GLY A C   1 
ATOM   3264 O  O   . GLY B 1 153 ? 2.240   23.584  -43.745 1.00 14.28 ? 153 GLY A O   1 
ATOM   3265 N  N   . GLU B 1 154 ? 4.304   22.736  -43.548 1.00 14.34 ? 154 GLU A N   1 
ATOM   3266 C  CA  . GLU B 1 154 ? 3.753   21.373  -43.726 1.00 15.24 ? 154 GLU A CA  1 
ATOM   3267 C  C   . GLU B 1 154 ? 2.851   21.060  -42.538 1.00 16.37 ? 154 GLU A C   1 
ATOM   3268 O  O   . GLU B 1 154 ? 3.127   21.610  -41.414 1.00 14.18 ? 154 GLU A O   1 
ATOM   3269 C  CB  . GLU B 1 154 ? 4.904   20.379  -43.918 1.00 16.79 ? 154 GLU A CB  1 
ATOM   3270 C  CG  . GLU B 1 154 ? 5.607   20.648  -45.265 1.00 17.03 ? 154 GLU A CG  1 
ATOM   3271 C  CD  . GLU B 1 154 ? 7.012   20.039  -45.338 1.00 20.17 ? 154 GLU A CD  1 
ATOM   3272 O  OE1 . GLU B 1 154 ? 7.621   19.873  -44.223 1.00 22.41 ? 154 GLU A OE1 1 
ATOM   3273 O  OE2 . GLU B 1 154 ? 7.486   19.735  -46.497 1.00 17.46 ? 154 GLU A OE2 1 
ATOM   3274 N  N   . PRO B 1 155 ? 1.786   20.207  -42.746 1.00 16.02 ? 155 PRO A N   1 
ATOM   3275 C  CA  . PRO B 1 155 ? 0.812   19.973  -41.658 1.00 15.20 ? 155 PRO A CA  1 
ATOM   3276 C  C   . PRO B 1 155 ? 1.458   19.475  -40.348 1.00 16.38 ? 155 PRO A C   1 
ATOM   3277 O  O   . PRO B 1 155 ? 2.456   18.706  -40.359 1.00 15.82 ? 155 PRO A O   1 
ATOM   3278 C  CB  . PRO B 1 155 ? -0.128  18.899  -42.216 1.00 13.96 ? 155 PRO A CB  1 
ATOM   3279 C  CG  . PRO B 1 155 ? 0.677   18.200  -43.307 1.00 16.46 ? 155 PRO A CG  1 
ATOM   3280 C  CD  . PRO B 1 155 ? 1.465   19.355  -43.921 1.00 14.57 ? 155 PRO A CD  1 
ATOM   3281 N  N   . ASN B 1 156 ? 0.854   19.928  -39.250 1.00 14.63 ? 156 ASN A N   1 
ATOM   3282 C  CA  . ASN B 1 156 ? 1.378   19.640  -37.910 1.00 15.29 ? 156 ASN A CA  1 
ATOM   3283 C  C   . ASN B 1 156 ? 0.514   18.541  -37.284 1.00 15.26 ? 156 ASN A C   1 
ATOM   3284 O  O   . ASN B 1 156 ? -0.666  18.786  -36.985 1.00 13.96 ? 156 ASN A O   1 
ATOM   3285 C  CB  . ASN B 1 156 ? 1.287   20.941  -37.109 1.00 13.63 ? 156 ASN A CB  1 
ATOM   3286 C  CG  . ASN B 1 156 ? 1.841   20.836  -35.734 1.00 15.49 ? 156 ASN A CG  1 
ATOM   3287 O  OD1 . ASN B 1 156 ? 1.866   19.736  -35.146 1.00 16.80 ? 156 ASN A OD1 1 
ATOM   3288 N  ND2 . ASN B 1 156 ? 2.255   21.973  -35.176 1.00 14.55 ? 156 ASN A ND2 1 
ATOM   3289 N  N   . SER B 1 157 ? 1.092   17.347  -37.090 1.00 16.89 ? 157 SER A N   1 
ATOM   3290 C  CA  . SER B 1 157 ? 0.292   16.234  -36.572 1.00 22.53 ? 157 SER A CA  1 
ATOM   3291 C  C   . SER B 1 157 ? -0.205  16.463  -35.172 1.00 20.58 ? 157 SER A C   1 
ATOM   3292 O  O   . SER B 1 157 ? -1.153  15.843  -34.731 1.00 21.67 ? 157 SER A O   1 
ATOM   3293 C  CB  . SER B 1 157 ? 1.031   14.912  -36.682 1.00 25.02 ? 157 SER A CB  1 
ATOM   3294 O  OG  . SER B 1 157 ? 2.238   15.013  -35.962 1.00 31.06 ? 157 SER A OG  1 
ATOM   3295 N  N   . GLN B 1 158 ? 0.404   17.398  -34.467 1.00 20.41 ? 158 GLN A N   1 
ATOM   3296 C  CA  . GLN B 1 158 ? -0.040  17.668  -33.075 1.00 21.16 ? 158 GLN A CA  1 
ATOM   3297 C  C   . GLN B 1 158 ? -1.349  18.439  -32.982 1.00 21.33 ? 158 GLN A C   1 
ATOM   3298 O  O   . GLN B 1 158 ? -1.957  18.546  -31.927 1.00 22.38 ? 158 GLN A O   1 
ATOM   3299 C  CB  . GLN B 1 158 ? 1.088   18.341  -32.247 1.00 23.61 ? 158 GLN A CB  1 
ATOM   3300 C  CG  . GLN B 1 158 ? 2.397   17.516  -32.122 1.00 27.00 ? 158 GLN A CG  1 
ATOM   3301 C  CD  . GLN B 1 158 ? 2.127   16.084  -31.674 1.00 32.33 ? 158 GLN A CD  1 
ATOM   3302 O  OE1 . GLN B 1 158 ? 2.278   15.131  -32.464 1.00 41.91 ? 158 GLN A OE1 1 
ATOM   3303 N  NE2 . GLN B 1 158 ? 1.633   15.920  -30.447 1.00 30.31 ? 158 GLN A NE2 1 
ATOM   3304 N  N   . LEU B 1 159 ? -1.778  19.013  -34.094 1.00 18.69 ? 159 LEU A N   1 
ATOM   3305 C  CA  . LEU B 1 159 ? -3.013  19.727  -34.127 1.00 17.89 ? 159 LEU A CA  1 
ATOM   3306 C  C   . LEU B 1 159 ? -4.187  18.777  -34.403 1.00 19.70 ? 159 LEU A C   1 
ATOM   3307 O  O   . LEU B 1 159 ? -5.336  19.162  -34.284 1.00 16.62 ? 159 LEU A O   1 
ATOM   3308 C  CB  . LEU B 1 159 ? -2.949  20.786  -35.235 1.00 17.69 ? 159 LEU A CB  1 
ATOM   3309 C  CG  . LEU B 1 159 ? -2.039  21.997  -34.997 1.00 16.95 ? 159 LEU A CG  1 
ATOM   3310 C  CD1 . LEU B 1 159 ? -2.058  22.884  -36.258 1.00 17.48 ? 159 LEU A CD1 1 
ATOM   3311 C  CD2 . LEU B 1 159 ? -2.422  22.851  -33.790 1.00 17.03 ? 159 LEU A CD2 1 
ATOM   3312 N  N   . GLN B 1 160 ? -3.892  17.519  -34.760 1.00 18.57 ? 160 GLN A N   1 
ATOM   3313 C  CA  . GLN B 1 160 ? -4.957  16.588  -35.101 1.00 19.66 ? 160 GLN A CA  1 
ATOM   3314 C  C   . GLN B 1 160 ? -5.984  16.474  -33.955 1.00 20.22 ? 160 GLN A C   1 
ATOM   3315 O  O   . GLN B 1 160 ? -7.182  16.478  -34.216 1.00 19.73 ? 160 GLN A O   1 
ATOM   3316 C  CB  . GLN B 1 160 ? -4.407  15.176  -35.441 1.00 19.93 ? 160 GLN A CB  1 
ATOM   3317 C  CG  . GLN B 1 160 ? -5.561  14.237  -35.937 1.00 18.69 ? 160 GLN A CG  1 
ATOM   3318 C  CD  . GLN B 1 160 ? -5.254  12.757  -36.074 1.00 21.95 ? 160 GLN A CD  1 
ATOM   3319 O  OE1 . GLN B 1 160 ? -6.175  11.947  -36.261 1.00 27.86 ? 160 GLN A OE1 1 
ATOM   3320 N  NE2 . GLN B 1 160 ? -3.987  12.403  -36.091 1.00 20.73 ? 160 GLN A NE2 1 
ATOM   3321 N  N   . LYS B 1 161 ? -5.519  16.280  -32.706 1.00 18.56 ? 161 LYS A N   1 
ATOM   3322 C  CA  . LYS B 1 161 ? -6.495  16.168  -31.639 1.00 18.37 ? 161 LYS A CA  1 
ATOM   3323 C  C   . LYS B 1 161 ? -7.538  17.300  -31.693 1.00 16.52 ? 161 LYS A C   1 
ATOM   3324 O  O   . LYS B 1 161 ? -8.728  17.054  -31.493 1.00 16.92 ? 161 LYS A O   1 
ATOM   3325 C  CB  . LYS B 1 161 ? -5.853  16.130  -30.237 1.00 20.80 ? 161 LYS A CB  1 
ATOM   3326 C  CG  . LYS B 1 161 ? -6.806  15.400  -29.262 1.00 21.35 ? 161 LYS A CG  1 
ATOM   3327 C  CD  . LYS B 1 161 ? -6.365  15.402  -27.832 1.00 24.66 ? 161 LYS A CD  1 
ATOM   3328 C  CE  . LYS B 1 161 ? -7.563  15.237  -26.933 1.00 22.83 ? 161 LYS A CE  1 
ATOM   3329 N  NZ  . LYS B 1 161 ? -8.022  13.815  -26.839 1.00 19.20 ? 161 LYS A NZ  1 
ATOM   3330 N  N   . ILE B 1 162 ? -7.120  18.540  -32.012 1.00 15.04 ? 162 ILE A N   1 
ATOM   3331 C  CA  . ILE B 1 162 ? -8.077  19.630  -32.043 1.00 14.47 ? 162 ILE A CA  1 
ATOM   3332 C  C   . ILE B 1 162 ? -8.912  19.586  -33.341 1.00 13.34 ? 162 ILE A C   1 
ATOM   3333 O  O   . ILE B 1 162 ? -10.129 19.670  -33.315 1.00 12.84 ? 162 ILE A O   1 
ATOM   3334 C  CB  . ILE B 1 162 ? -7.358  21.026  -31.909 1.00 13.17 ? 162 ILE A CB  1 
ATOM   3335 C  CG1 . ILE B 1 162 ? -6.662  21.142  -30.530 1.00 13.09 ? 162 ILE A CG1 1 
ATOM   3336 C  CG2 . ILE B 1 162 ? -8.341  22.153  -32.097 1.00 13.81 ? 162 ILE A CG2 1 
ATOM   3337 C  CD1 . ILE B 1 162 ? -5.701  22.362  -30.386 1.00 13.08 ? 162 ILE A CD1 1 
ATOM   3338 N  N   . THR B 1 163 ? -8.247  19.541  -34.502 1.00 14.72 ? 163 THR A N   1 
ATOM   3339 C  CA  . THR B 1 163 ? -8.989  19.580  -35.798 1.00 14.87 ? 163 THR A CA  1 
ATOM   3340 C  C   . THR B 1 163 ? -10.041 18.496  -35.896 1.00 15.12 ? 163 THR A C   1 
ATOM   3341 O  O   . THR B 1 163 ? -11.120 18.771  -36.422 1.00 15.77 ? 163 THR A O   1 
ATOM   3342 C  CB  . THR B 1 163 ? -8.088  19.543  -37.048 1.00 13.32 ? 163 THR A CB  1 
ATOM   3343 O  OG1 . THR B 1 163 ? -7.301  18.314  -37.137 1.00 15.83 ? 163 THR A OG1 1 
ATOM   3344 C  CG2 . THR B 1 163 ? -7.169  20.750  -36.983 1.00 14.51 ? 163 THR A CG2 1 
ATOM   3345 N  N   . ASP B 1 164 ? -9.730  17.316  -35.345 1.00 16.83 ? 164 ASP A N   1 
ATOM   3346 C  CA  . ASP B 1 164 ? -10.693 16.189  -35.302 1.00 17.46 ? 164 ASP A CA  1 
ATOM   3347 C  C   . ASP B 1 164 ? -12.011 16.537  -34.608 1.00 18.13 ? 164 ASP A C   1 
ATOM   3348 O  O   . ASP B 1 164 ? -12.987 15.916  -34.953 1.00 19.71 ? 164 ASP A O   1 
ATOM   3349 C  CB  . ASP B 1 164 ? -10.117 14.910  -34.680 1.00 19.83 ? 164 ASP A CB  1 
ATOM   3350 C  CG  . ASP B 1 164 ? -9.256  14.052  -35.647 1.00 23.61 ? 164 ASP A CG  1 
ATOM   3351 O  OD1 . ASP B 1 164 ? -9.183  14.296  -36.870 1.00 25.35 ? 164 ASP A OD1 1 
ATOM   3352 O  OD2 . ASP B 1 164 ? -8.632  13.098  -35.144 1.00 23.99 ? 164 ASP A OD2 1 
ATOM   3353 N  N   . THR B 1 165 ? -12.070 17.529  -33.692 1.00 15.00 ? 165 THR A N   1 
ATOM   3354 C  CA  . THR B 1 165 ? -13.277 17.823  -32.912 1.00 14.89 ? 165 THR A CA  1 
ATOM   3355 C  C   . THR B 1 165 ? -14.153 18.911  -33.554 1.00 15.25 ? 165 THR A C   1 
ATOM   3356 O  O   . THR B 1 165 ? -15.308 19.163  -33.142 1.00 15.56 ? 165 THR A O   1 
ATOM   3357 C  CB  . THR B 1 165 ? -12.932 18.314  -31.498 1.00 14.99 ? 165 THR A CB  1 
ATOM   3358 O  OG1 . THR B 1 165 ? -12.441 19.673  -31.562 1.00 15.75 ? 165 THR A OG1 1 
ATOM   3359 C  CG2 . THR B 1 165 ? -12.035 17.375  -30.813 1.00 15.31 ? 165 THR A CG2 1 
ATOM   3360 N  N   . LEU B 1 166 ? -13.606 19.587  -34.583 1.00 13.85 ? 166 LEU A N   1 
ATOM   3361 C  CA  . LEU B 1 166 ? -14.223 20.821  -35.063 1.00 15.32 ? 166 LEU A CA  1 
ATOM   3362 C  C   . LEU B 1 166 ? -15.646 20.649  -35.637 1.00 14.73 ? 166 LEU A C   1 
ATOM   3363 O  O   . LEU B 1 166 ? -16.482 21.503  -35.456 1.00 17.21 ? 166 LEU A O   1 
ATOM   3364 C  CB  . LEU B 1 166 ? -13.276 21.523  -36.067 1.00 14.90 ? 166 LEU A CB  1 
ATOM   3365 C  CG  . LEU B 1 166 ? -11.964 21.972  -35.402 1.00 16.21 ? 166 LEU A CG  1 
ATOM   3366 C  CD1 . LEU B 1 166 ? -11.042 22.451  -36.559 1.00 15.64 ? 166 LEU A CD1 1 
ATOM   3367 C  CD2 . LEU B 1 166 ? -12.198 23.094  -34.390 1.00 17.17 ? 166 LEU A CD2 1 
ATOM   3368 N  N   . ASP B 1 167 ? -15.921 19.511  -36.227 1.00 19.51 ? 167 ASP A N   1 
ATOM   3369 C  CA  . ASP B 1 167 ? -17.303 19.286  -36.754 1.00 21.14 ? 167 ASP A CA  1 
ATOM   3370 C  C   . ASP B 1 167 ? -18.279 19.087  -35.649 1.00 20.63 ? 167 ASP A C   1 
ATOM   3371 O  O   . ASP B 1 167 ? -19.425 19.561  -35.756 1.00 20.37 ? 167 ASP A O   1 
ATOM   3372 C  CB  . ASP B 1 167 ? -17.361 18.104  -37.703 1.00 24.39 ? 167 ASP A CB  1 
ATOM   3373 C  CG  . ASP B 1 167 ? -16.988 18.509  -39.073 1.00 29.21 ? 167 ASP A CG  1 
ATOM   3374 O  OD1 . ASP B 1 167 ? -17.259 19.700  -39.444 1.00 33.03 ? 167 ASP A OD1 1 
ATOM   3375 O  OD2 . ASP B 1 167 ? -16.417 17.642  -39.737 1.00 29.82 ? 167 ASP A OD2 1 
ATOM   3376 N  N   . SER B 1 168 ? -17.815 18.459  -34.550 1.00 20.40 ? 168 SER A N   1 
ATOM   3377 C  CA  . SER B 1 168 ? -18.694 18.273  -33.399 1.00 18.92 ? 168 SER A CA  1 
ATOM   3378 C  C   . SER B 1 168 ? -18.963 19.589  -32.656 1.00 17.37 ? 168 SER A C   1 
ATOM   3379 O  O   . SER B 1 168 ? -19.886 19.630  -31.888 1.00 17.24 ? 168 SER A O   1 
ATOM   3380 C  CB  . SER B 1 168 ? -18.155 17.189  -32.480 1.00 20.50 ? 168 SER A CB  1 
ATOM   3381 O  OG  . SER B 1 168 ? -17.083 17.694  -31.692 1.00 22.60 ? 168 SER A OG  1 
ATOM   3382 N  N   . ILE B 1 169 ? -18.185 20.657  -32.875 1.00 15.82 ? 169 ILE A N   1 
ATOM   3383 C  CA  . ILE B 1 169 ? -18.468 21.965  -32.193 1.00 15.27 ? 169 ILE A CA  1 
ATOM   3384 C  C   . ILE B 1 169 ? -18.707 23.073  -33.215 1.00 15.50 ? 169 ILE A C   1 
ATOM   3385 O  O   . ILE B 1 169 ? -18.342 24.179  -33.020 1.00 15.78 ? 169 ILE A O   1 
ATOM   3386 C  CB  . ILE B 1 169 ? -17.386 22.289  -31.127 1.00 14.58 ? 169 ILE A CB  1 
ATOM   3387 C  CG1 . ILE B 1 169 ? -15.976 22.315  -31.774 1.00 14.04 ? 169 ILE A CG1 1 
ATOM   3388 C  CG2 . ILE B 1 169 ? -17.380 21.167  -30.083 1.00 15.04 ? 169 ILE A CG2 1 
ATOM   3389 C  CD1 . ILE B 1 169 ? -15.000 23.181  -30.956 1.00 14.83 ? 169 ILE A CD1 1 
ATOM   3390 N  N   . LYS B 1 170 ? -19.308 22.721  -34.347 1.00 17.83 ? 170 LYS A N   1 
ATOM   3391 C  CA  . LYS B 1 170 ? -19.557 23.706  -35.354 1.00 17.64 ? 170 LYS A CA  1 
ATOM   3392 C  C   . LYS B 1 170 ? -20.345 24.911  -34.957 1.00 16.82 ? 170 LYS A C   1 
ATOM   3393 O  O   . LYS B 1 170 ? -20.024 26.018  -35.328 1.00 18.03 ? 170 LYS A O   1 
ATOM   3394 C  CB  . LYS B 1 170 ? -20.277 23.030  -36.584 1.00 19.94 ? 170 LYS A CB  1 
ATOM   3395 C  CG  . LYS B 1 170 ? -20.469 24.034  -37.713 1.00 21.60 ? 170 LYS A CG  1 
ATOM   3396 C  CD  . LYS B 1 170 ? -20.767 23.369  -39.073 1.00 27.47 ? 170 LYS A CD  1 
ATOM   3397 C  CE  . LYS B 1 170 ? -20.785 24.385  -40.209 1.00 28.64 ? 170 LYS A CE  1 
ATOM   3398 N  NZ  . LYS B 1 170 ? -19.458 24.604  -40.851 1.00 27.18 ? 170 LYS A NZ  1 
ATOM   3399 N  N   . GLU B 1 171 ? -21.386 24.700  -34.151 1.00 18.51 ? 171 GLU A N   1 
ATOM   3400 C  CA  . GLU B 1 171 ? -22.251 25.776  -33.678 1.00 19.05 ? 171 GLU A CA  1 
ATOM   3401 C  C   . GLU B 1 171 ? -21.759 26.307  -32.305 1.00 17.78 ? 171 GLU A C   1 
ATOM   3402 O  O   . GLU B 1 171 ? -21.268 25.546  -31.495 1.00 18.58 ? 171 GLU A O   1 
ATOM   3403 C  CB  . GLU B 1 171 ? -23.742 25.314  -33.593 1.00 23.10 ? 171 GLU A CB  1 
ATOM   3404 C  CG  . GLU B 1 171 ? -24.354 24.781  -34.891 1.00 25.93 ? 171 GLU A CG  1 
ATOM   3405 C  CD  . GLU B 1 171 ? -23.863 23.379  -35.271 1.00 36.02 ? 171 GLU A CD  1 
ATOM   3406 O  OE1 . GLU B 1 171 ? -24.014 23.036  -36.482 1.00 43.66 ? 171 GLU A OE1 1 
ATOM   3407 O  OE2 . GLU B 1 171 ? -23.316 22.596  -34.406 1.00 37.94 ? 171 GLU A OE2 1 
ATOM   3408 N  N   . LYS B 1 172 ? -21.798 27.623  -32.110 1.00 16.65 ? 172 LYS A N   1 
ATOM   3409 C  CA  . LYS B 1 172 ? -21.592 28.234  -30.815 1.00 18.28 ? 172 LYS A CA  1 
ATOM   3410 C  C   . LYS B 1 172 ? -22.425 27.518  -29.735 1.00 19.65 ? 172 LYS A C   1 
ATOM   3411 O  O   . LYS B 1 172 ? -23.623 27.237  -29.951 1.00 18.30 ? 172 LYS A O   1 
ATOM   3412 C  CB  . LYS B 1 172 ? -22.040 29.702  -30.875 1.00 18.36 ? 172 LYS A CB  1 
ATOM   3413 C  CG  . LYS B 1 172 ? -21.918 30.453  -29.562 1.00 17.75 ? 172 LYS A CG  1 
ATOM   3414 C  CD  . LYS B 1 172 ? -22.375 31.875  -29.768 1.00 20.18 ? 172 LYS A CD  1 
ATOM   3415 C  CE  . LYS B 1 172 ? -22.354 32.685  -28.463 1.00 23.32 ? 172 LYS A CE  1 
ATOM   3416 N  NZ  . LYS B 1 172 ? -22.434 34.146  -28.755 1.00 25.61 ? 172 LYS A NZ  1 
ATOM   3417 N  N   . GLY B 1 173 ? -21.814 27.219  -28.602 1.00 18.72 ? 173 GLY A N   1 
ATOM   3418 C  CA  . GLY B 1 173 ? -22.532 26.535  -27.554 1.00 18.36 ? 173 GLY A CA  1 
ATOM   3419 C  C   . GLY B 1 173 ? -22.208 25.060  -27.481 1.00 17.81 ? 173 GLY A C   1 
ATOM   3420 O  O   . GLY B 1 173 ? -22.314 24.490  -26.423 1.00 18.43 ? 173 GLY A O   1 
ATOM   3421 N  N   . LYS B 1 174 ? -21.733 24.459  -28.562 1.00 17.03 ? 174 LYS A N   1 
ATOM   3422 C  CA  . LYS B 1 174 ? -21.467 23.032  -28.599 1.00 16.87 ? 174 LYS A CA  1 
ATOM   3423 C  C   . LYS B 1 174 ? -20.166 22.736  -27.846 1.00 17.25 ? 174 LYS A C   1 
ATOM   3424 O  O   . LYS B 1 174 ? -19.247 23.611  -27.750 1.00 16.67 ? 174 LYS A O   1 
ATOM   3425 C  CB  . LYS B 1 174 ? -21.333 22.573  -30.043 1.00 20.55 ? 174 LYS A CB  1 
ATOM   3426 C  CG  . LYS B 1 174 ? -22.629 22.492  -30.828 1.00 25.42 ? 174 LYS A CG  1 
ATOM   3427 C  CD  . LYS B 1 174 ? -23.226 21.074  -30.765 1.00 27.47 ? 174 LYS A CD  1 
ATOM   3428 C  CE  . LYS B 1 174 ? -24.412 20.922  -31.725 1.00 36.71 ? 174 LYS A CE  1 
ATOM   3429 N  NZ  . LYS B 1 174 ? -25.476 21.836  -31.213 1.00 37.89 ? 174 LYS A NZ  1 
ATOM   3430 N  N   . GLN B 1 175 ? -20.112 21.555  -27.243 1.00 15.95 ? 175 GLN A N   1 
ATOM   3431 C  CA  . GLN B 1 175 ? -18.901 21.149  -26.494 1.00 14.67 ? 175 GLN A CA  1 
ATOM   3432 C  C   . GLN B 1 175 ? -18.773 19.637  -26.488 1.00 15.72 ? 175 GLN A C   1 
ATOM   3433 O  O   . GLN B 1 175 ? -19.797 18.918  -26.722 1.00 17.21 ? 175 GLN A O   1 
ATOM   3434 C  CB  . GLN B 1 175 ? -18.914 21.657  -25.086 1.00 14.09 ? 175 GLN A CB  1 
ATOM   3435 C  CG  . GLN B 1 175 ? -19.919 20.933  -24.168 1.00 14.75 ? 175 GLN A CG  1 
ATOM   3436 C  CD  . GLN B 1 175 ? -19.946 21.480  -22.769 1.00 15.94 ? 175 GLN A CD  1 
ATOM   3437 O  OE1 . GLN B 1 175 ? -19.874 20.726  -21.756 1.00 19.34 ? 175 GLN A OE1 1 
ATOM   3438 N  NE2 . GLN B 1 175 ? -20.052 22.784  -22.675 1.00 14.69 ? 175 GLN A NE2 1 
ATOM   3439 N  N   . THR B 1 176 ? -17.546 19.159  -26.350 1.00 13.43 ? 176 THR A N   1 
ATOM   3440 C  CA  . THR B 1 176 ? -17.269 17.744  -26.362 1.00 15.58 ? 176 THR A CA  1 
ATOM   3441 C  C   . THR B 1 176 ? -16.178 17.401  -25.372 1.00 14.81 ? 176 THR A C   1 
ATOM   3442 O  O   . THR B 1 176 ? -15.294 18.261  -25.107 1.00 15.10 ? 176 THR A O   1 
ATOM   3443 C  CB  . THR B 1 176 ? -17.051 17.135  -27.786 1.00 19.38 ? 176 THR A CB  1 
ATOM   3444 O  OG1 . THR B 1 176 ? -15.688 17.133  -28.157 1.00 23.48 ? 176 THR A OG1 1 
ATOM   3445 C  CG2 . THR B 1 176 ? -17.765 17.895  -28.808 1.00 19.00 ? 176 THR A CG2 1 
ATOM   3446 N  N   . ARG B 1 177 ? -16.216 16.171  -24.834 1.00 14.63 ? 177 ARG A N   1 
ATOM   3447 C  CA  . ARG B 1 177 ? -15.153 15.733  -23.909 1.00 15.72 ? 177 ARG A CA  1 
ATOM   3448 C  C   . ARG B 1 177 ? -13.802 15.870  -24.677 1.00 14.32 ? 177 ARG A C   1 
ATOM   3449 O  O   . ARG B 1 177 ? -13.665 15.467  -25.838 1.00 15.47 ? 177 ARG A O   1 
ATOM   3450 C  CB  . ARG B 1 177 ? -15.378 14.328  -23.376 1.00 16.16 ? 177 ARG A CB  1 
ATOM   3451 C  CG  . ARG B 1 177 ? -14.223 13.790  -22.520 1.00 17.95 ? 177 ARG A CG  1 
ATOM   3452 C  CD  . ARG B 1 177 ? -14.579 12.536  -21.709 1.00 21.16 ? 177 ARG A CD  1 
ATOM   3453 N  NE  . ARG B 1 177 ? -13.579 12.113  -20.686 1.00 23.58 ? 177 ARG A NE  1 
ATOM   3454 C  CZ  . ARG B 1 177 ? -13.294 12.693  -19.506 1.00 23.83 ? 177 ARG A CZ  1 
ATOM   3455 N  NH1 . ARG B 1 177 ? -13.886 13.807  -19.097 1.00 24.31 ? 177 ARG A NH1 1 
ATOM   3456 N  NH2 . ARG B 1 177 ? -12.374 12.143  -18.716 1.00 25.41 ? 177 ARG A NH2 1 
ATOM   3457 N  N   . PHE B 1 178 ? -12.788 16.357  -23.964 1.00 13.46 ? 178 PHE A N   1 
ATOM   3458 C  CA  . PHE B 1 178 ? -11.484 16.580  -24.576 1.00 12.23 ? 178 PHE A CA  1 
ATOM   3459 C  C   . PHE B 1 178 ? -10.458 16.415  -23.484 1.00 13.59 ? 178 PHE A C   1 
ATOM   3460 O  O   . PHE B 1 178 ? -10.220 17.348  -22.725 1.00 13.68 ? 178 PHE A O   1 
ATOM   3461 C  CB  . PHE B 1 178 ? -11.442 18.045  -25.168 1.00 11.74 ? 178 PHE A CB  1 
ATOM   3462 C  CG  . PHE B 1 178 ? -10.281 18.270  -26.094 1.00 10.53 ? 178 PHE A CG  1 
ATOM   3463 C  CD1 . PHE B 1 178 ? -10.376 17.935  -27.443 1.00 10.59 ? 178 PHE A CD1 1 
ATOM   3464 C  CD2 . PHE B 1 178 ? -9.098  18.899  -25.626 1.00 10.20 ? 178 PHE A CD2 1 
ATOM   3465 C  CE1 . PHE B 1 178 ? -9.315  18.213  -28.292 1.00 11.07 ? 178 PHE A CE1 1 
ATOM   3466 C  CE2 . PHE B 1 178 ? -8.048  19.168  -26.509 1.00 10.77 ? 178 PHE A CE2 1 
ATOM   3467 C  CZ  . PHE B 1 178 ? -8.173  18.828  -27.835 1.00 10.58 ? 178 PHE A CZ  1 
ATOM   3468 N  N   . THR B 1 179 ? -9.821  15.234  -23.390 1.00 14.00 ? 179 THR A N   1 
ATOM   3469 C  CA  . THR B 1 179 ? -8.772  15.050  -22.364 1.00 14.67 ? 179 THR A CA  1 
ATOM   3470 C  C   . THR B 1 179 ? -7.557  14.338  -22.908 1.00 14.51 ? 179 THR A C   1 
ATOM   3471 O  O   . THR B 1 179 ? -7.534  13.971  -24.124 1.00 16.24 ? 179 THR A O   1 
ATOM   3472 C  CB  . THR B 1 179 ? -9.279  14.382  -21.094 1.00 18.28 ? 179 THR A CB  1 
ATOM   3473 O  OG1 . THR B 1 179 ? -8.297  14.546  -19.978 1.00 18.21 ? 179 THR A OG1 1 
ATOM   3474 C  CG2 . THR B 1 179 ? -9.662  12.904  -21.432 1.00 19.85 ? 179 THR A CG2 1 
ATOM   3475 N  N   . ASN B 1 180 ? -6.557  14.131  -22.059 0.50 10.69 ? 180 ASN A N   1 
ATOM   3476 C  CA  . ASN B 1 180 ? -5.309  13.561  -22.494 0.50 10.21 ? 180 ASN A CA  1 
ATOM   3477 C  C   . ASN B 1 180 ? -4.673  14.350  -23.677 0.50 9.28  ? 180 ASN A C   1 
ATOM   3478 O  O   . ASN B 1 180 ? -4.252  13.818  -24.696 0.50 7.65  ? 180 ASN A O   1 
ATOM   3479 C  CB  . ASN B 1 180 ? -5.575  12.066  -22.787 0.50 10.81 ? 180 ASN A CB  1 
ATOM   3480 C  CG  . ASN B 1 180 ? -6.123  11.341  -21.555 0.50 12.17 ? 180 ASN A CG  1 
ATOM   3481 O  OD1 . ASN B 1 180 ? -5.754  11.663  -20.433 0.50 13.24 ? 180 ASN A OD1 1 
ATOM   3482 N  ND2 . ASN B 1 180 ? -7.063  10.394  -21.761 0.50 13.68 ? 180 ASN A ND2 1 
ATOM   3483 N  N   . PHE B 1 181 ? -4.627  15.663  -23.486 1.00 11.05 ? 181 PHE A N   1 
ATOM   3484 C  CA  . PHE B 1 181 ? -4.166  16.635  -24.454 1.00 11.22 ? 181 PHE A CA  1 
ATOM   3485 C  C   . PHE B 1 181 ? -2.705  17.011  -24.161 1.00 11.88 ? 181 PHE A C   1 
ATOM   3486 O  O   . PHE B 1 181 ? -2.444  17.604  -23.130 1.00 12.50 ? 181 PHE A O   1 
ATOM   3487 C  CB  . PHE B 1 181 ? -5.090  17.896  -24.319 1.00 11.62 ? 181 PHE A CB  1 
ATOM   3488 C  CG  . PHE B 1 181 ? -4.733  19.069  -25.217 1.00 12.04 ? 181 PHE A CG  1 
ATOM   3489 C  CD1 . PHE B 1 181 ? -4.223  18.866  -26.507 1.00 12.74 ? 181 PHE A CD1 1 
ATOM   3490 C  CD2 . PHE B 1 181 ? -4.988  20.379  -24.797 1.00 11.94 ? 181 PHE A CD2 1 
ATOM   3491 C  CE1 . PHE B 1 181 ? -3.870  19.949  -27.322 1.00 13.51 ? 181 PHE A CE1 1 
ATOM   3492 C  CE2 . PHE B 1 181 ? -4.673  21.457  -25.619 1.00 13.00 ? 181 PHE A CE2 1 
ATOM   3493 C  CZ  . PHE B 1 181 ? -4.085  21.234  -26.885 1.00 12.52 ? 181 PHE A CZ  1 
ATOM   3494 N  N   . ASP B 1 182 ? -1.823  16.731  -25.107 1.00 12.23 ? 182 ASP A N   1 
ATOM   3495 C  CA  . ASP B 1 182 ? -0.367  16.959  -25.041 1.00 13.20 ? 182 ASP A CA  1 
ATOM   3496 C  C   . ASP B 1 182 ? -0.142  18.416  -25.452 1.00 12.60 ? 182 ASP A C   1 
ATOM   3497 O  O   . ASP B 1 182 ? 0.304   18.706  -26.567 1.00 14.02 ? 182 ASP A O   1 
ATOM   3498 C  CB  . ASP B 1 182 ? 0.383   15.975  -25.980 1.00 16.38 ? 182 ASP A CB  1 
ATOM   3499 C  CG  . ASP B 1 182 ? 1.932   16.164  -25.965 1.00 17.64 ? 182 ASP A CG  1 
ATOM   3500 O  OD1 . ASP B 1 182 ? 2.508   17.017  -25.196 1.00 18.78 ? 182 ASP A OD1 1 
ATOM   3501 O  OD2 . ASP B 1 182 ? 2.615   15.450  -26.718 1.00 19.32 ? 182 ASP A OD2 1 
ATOM   3502 N  N   . LEU B 1 183 ? -0.479  19.321  -24.564 1.00 12.90 ? 183 LEU A N   1 
ATOM   3503 C  CA  . LEU B 1 183 ? -0.376  20.783  -24.834 1.00 11.59 ? 183 LEU A CA  1 
ATOM   3504 C  C   . LEU B 1 183 ? 1.089   21.186  -25.001 1.00 11.37 ? 183 LEU A C   1 
ATOM   3505 O  O   . LEU B 1 183 ? 1.406   22.043  -25.876 1.00 10.62 ? 183 LEU A O   1 
ATOM   3506 C  CB  . LEU B 1 183 ? -1.086  21.585  -23.719 1.00 11.03 ? 183 LEU A CB  1 
ATOM   3507 C  CG  . LEU B 1 183 ? -1.009  23.117  -23.848 1.00 10.09 ? 183 LEU A CG  1 
ATOM   3508 C  CD1 . LEU B 1 183 ? -1.539  23.611  -25.228 1.00 10.02 ? 183 LEU A CD1 1 
ATOM   3509 C  CD2 . LEU B 1 183 ? -1.759  23.740  -22.678 1.00 10.77 ? 183 LEU A CD2 1 
ATOM   3510 N  N   . LEU B 1 184 ? 1.987   20.569  -24.216 1.00 11.02 ? 184 LEU A N   1 
ATOM   3511 C  CA  . LEU B 1 184 ? 3.387   20.901  -24.415 1.00 12.94 ? 184 LEU A CA  1 
ATOM   3512 C  C   . LEU B 1 184 ? 3.824   20.705  -25.851 1.00 13.71 ? 184 LEU A C   1 
ATOM   3513 O  O   . LEU B 1 184 ? 4.734   21.375  -26.320 1.00 14.80 ? 184 LEU A O   1 
ATOM   3514 C  CB  . LEU B 1 184 ? 4.261   20.056  -23.485 1.00 13.09 ? 184 LEU A CB  1 
ATOM   3515 C  CG  . LEU B 1 184 ? 4.265   20.470  -22.017 1.00 14.15 ? 184 LEU A CG  1 
ATOM   3516 C  CD1 . LEU B 1 184 ? 5.181   19.472  -21.288 1.00 12.76 ? 184 LEU A CD1 1 
ATOM   3517 C  CD2 . LEU B 1 184 ? 4.801   21.925  -21.832 1.00 13.53 ? 184 LEU A CD2 1 
ATOM   3518 N  N   . SER B 1 185 ? 3.239   19.710  -26.554 1.00 14.01 ? 185 SER A N   1 
ATOM   3519 C  CA  . SER B 1 185 ? 3.626   19.451  -27.948 1.00 17.58 ? 185 SER A CA  1 
ATOM   3520 C  C   . SER B 1 185 ? 3.339   20.554  -28.962 1.00 17.81 ? 185 SER A C   1 
ATOM   3521 O  O   . SER B 1 185 ? 3.889   20.542  -30.079 1.00 18.69 ? 185 SER A O   1 
ATOM   3522 C  CB  . SER B 1 185 ? 3.034   18.132  -28.488 1.00 18.56 ? 185 SER A CB  1 
ATOM   3523 O  OG  . SER B 1 185 ? 1.624   18.218  -28.745 1.00 20.30 ? 185 SER A OG  1 
ATOM   3524 N  N   . LEU B 1 186 ? 2.476   21.491  -28.582 1.00 15.94 ? 186 LEU A N   1 
ATOM   3525 C  CA  . LEU B 1 186 ? 2.212   22.689  -29.384 1.00 15.15 ? 186 LEU A CA  1 
ATOM   3526 C  C   . LEU B 1 186 ? 3.153   23.839  -29.078 1.00 15.66 ? 186 LEU A C   1 
ATOM   3527 O  O   . LEU B 1 186 ? 2.940   25.012  -29.541 1.00 16.04 ? 186 LEU A O   1 
ATOM   3528 C  CB  . LEU B 1 186 ? 0.735   23.128  -29.155 1.00 15.38 ? 186 LEU A CB  1 
ATOM   3529 C  CG  . LEU B 1 186 ? -0.285  22.035  -29.637 1.00 17.36 ? 186 LEU A CG  1 
ATOM   3530 C  CD1 . LEU B 1 186 ? -1.718  22.428  -29.395 1.00 16.52 ? 186 LEU A CD1 1 
ATOM   3531 C  CD2 . LEU B 1 186 ? -0.161  21.754  -31.117 1.00 17.60 ? 186 LEU A CD2 1 
ATOM   3532 N  N   . LEU B 1 187 ? 4.112   23.610  -28.179 1.00 13.58 ? 187 LEU A N   1 
ATOM   3533 C  CA  . LEU B 1 187 ? 5.105   24.646  -27.991 1.00 11.84 ? 187 LEU A CA  1 
ATOM   3534 C  C   . LEU B 1 187 ? 6.270   24.350  -28.944 1.00 11.64 ? 187 LEU A C   1 
ATOM   3535 O  O   . LEU B 1 187 ? 6.562   23.158  -29.223 1.00 12.16 ? 187 LEU A O   1 
ATOM   3536 C  CB  . LEU B 1 187 ? 5.610   24.742  -26.534 1.00 12.22 ? 187 LEU A CB  1 
ATOM   3537 C  CG  . LEU B 1 187 ? 4.454   24.952  -25.542 1.00 13.18 ? 187 LEU A CG  1 
ATOM   3538 C  CD1 . LEU B 1 187 ? 5.026   25.015  -24.098 1.00 12.19 ? 187 LEU A CD1 1 
ATOM   3539 C  CD2 . LEU B 1 187 ? 3.674   26.179  -25.842 1.00 14.80 ? 187 LEU A CD2 1 
ATOM   3540 N  N   . PRO B 1 188 ? 6.901   25.415  -29.456 1.00 10.91 ? 188 PRO A N   1 
ATOM   3541 C  CA  . PRO B 1 188 ? 8.090   25.248  -30.296 1.00 10.52 ? 188 PRO A CA  1 
ATOM   3542 C  C   . PRO B 1 188 ? 9.281   24.764  -29.423 1.00 10.25 ? 188 PRO A C   1 
ATOM   3543 O  O   . PRO B 1 188 ? 9.210   24.840  -28.192 1.00 10.39 ? 188 PRO A O   1 
ATOM   3544 C  CB  . PRO B 1 188 ? 8.372   26.681  -30.789 1.00 10.30 ? 188 PRO A CB  1 
ATOM   3545 C  CG  . PRO B 1 188 ? 7.814   27.566  -29.653 1.00 9.98  ? 188 PRO A CG  1 
ATOM   3546 C  CD  . PRO B 1 188 ? 6.560   26.865  -29.254 1.00 10.94 ? 188 PRO A CD  1 
ATOM   3547 N  N   . PRO B 1 189 ? 10.369  24.290  -30.040 1.00 11.81 ? 189 PRO A N   1 
ATOM   3548 C  CA  . PRO B 1 189 ? 11.465  23.766  -29.251 1.00 11.31 ? 189 PRO A CA  1 
ATOM   3549 C  C   . PRO B 1 189 ? 12.164  24.817  -28.379 1.00 12.03 ? 189 PRO A C   1 
ATOM   3550 O  O   . PRO B 1 189 ? 12.625  24.503  -27.254 1.00 9.90  ? 189 PRO A O   1 
ATOM   3551 C  CB  . PRO B 1 189 ? 12.422  23.222  -30.293 1.00 13.11 ? 189 PRO A CB  1 
ATOM   3552 C  CG  . PRO B 1 189 ? 11.601  22.972  -31.516 1.00 14.37 ? 189 PRO A CG  1 
ATOM   3553 C  CD  . PRO B 1 189 ? 10.434  23.887  -31.464 1.00 13.84 ? 189 PRO A CD  1 
ATOM   3554 N  N   . SER B 1 190 ? 12.265  26.058  -28.852 1.00 11.16 ? 190 SER A N   1 
ATOM   3555 C  CA  . SER B 1 190 ? 12.830  27.119  -28.059 1.00 11.07 ? 190 SER A CA  1 
ATOM   3556 C  C   . SER B 1 190 ? 11.711  27.911  -27.390 1.00 10.42 ? 190 SER A C   1 
ATOM   3557 O  O   . SER B 1 190 ? 10.705  28.194  -28.035 1.00 9.20  ? 190 SER A O   1 
ATOM   3558 C  CB  . SER B 1 190 ? 13.681  28.065  -28.929 1.00 12.12 ? 190 SER A CB  1 
ATOM   3559 O  OG  . SER B 1 190 ? 14.036  29.301  -28.238 1.00 14.51 ? 190 SER A OG  1 
ATOM   3560 N  N   . TRP B 1 191 ? 11.886  28.230  -26.118 1.00 9.46  ? 191 TRP A N   1 
ATOM   3561 C  CA  . TRP B 1 191 ? 10.935  29.088  -25.462 1.00 10.34 ? 191 TRP A CA  1 
ATOM   3562 C  C   . TRP B 1 191 ? 11.432  30.493  -25.309 1.00 11.04 ? 191 TRP A C   1 
ATOM   3563 O  O   . TRP B 1 191 ? 10.905  31.251  -24.465 1.00 11.91 ? 191 TRP A O   1 
ATOM   3564 C  CB  . TRP B 1 191 ? 10.462  28.532  -24.082 1.00 9.33  ? 191 TRP A CB  1 
ATOM   3565 C  CG  . TRP B 1 191 ? 9.867   27.148  -24.095 1.00 9.64  ? 191 TRP A CG  1 
ATOM   3566 C  CD1 . TRP B 1 191 ? 9.377   26.408  -25.186 1.00 10.07 ? 191 TRP A CD1 1 
ATOM   3567 C  CD2 . TRP B 1 191 ? 9.617   26.357  -22.942 1.00 9.57  ? 191 TRP A CD2 1 
ATOM   3568 N  NE1 . TRP B 1 191 ? 8.882   25.174  -24.713 1.00 11.44 ? 191 TRP A NE1 1 
ATOM   3569 C  CE2 . TRP B 1 191 ? 9.060   25.124  -23.362 1.00 9.97  ? 191 TRP A CE2 1 
ATOM   3570 C  CE3 . TRP B 1 191 ? 9.872   26.562  -21.562 1.00 9.70  ? 191 TRP A CE3 1 
ATOM   3571 C  CZ2 . TRP B 1 191 ? 8.731   24.061  -22.433 1.00 10.73 ? 191 TRP A CZ2 1 
ATOM   3572 C  CZ3 . TRP B 1 191 ? 9.554   25.506  -20.647 1.00 10.71 ? 191 TRP A CZ3 1 
ATOM   3573 C  CH2 . TRP B 1 191 ? 8.998   24.309  -21.087 1.00 10.36 ? 191 TRP A CH2 1 
ATOM   3574 N  N   . ASP B 1 192 ? 12.384  30.920  -26.146 1.00 11.01 ? 192 ASP A N   1 
ATOM   3575 C  CA  . ASP B 1 192 ? 12.756  32.339  -26.104 1.00 11.41 ? 192 ASP A CA  1 
ATOM   3576 C  C   . ASP B 1 192 ? 11.520  33.193  -26.376 1.00 9.58  ? 192 ASP A C   1 
ATOM   3577 O  O   . ASP B 1 192 ? 10.650  32.827  -27.211 1.00 8.66  ? 192 ASP A O   1 
ATOM   3578 C  CB  . ASP B 1 192 ? 13.827  32.609  -27.172 1.00 14.26 ? 192 ASP A CB  1 
ATOM   3579 C  CG  . ASP B 1 192 ? 15.191  32.011  -26.803 1.00 17.39 ? 192 ASP A CG  1 
ATOM   3580 O  OD1 . ASP B 1 192 ? 15.393  31.541  -25.686 1.00 20.38 ? 192 ASP A OD1 1 
ATOM   3581 O  OD2 . ASP B 1 192 ? 16.027  31.974  -27.713 1.00 21.65 ? 192 ASP A OD2 1 
ATOM   3582 N  N   . TYR B 1 193 ? 11.413  34.299  -25.641 1.00 9.69  ? 193 TYR A N   1 
ATOM   3583 C  CA  . TYR B 1 193 ? 10.172  35.104  -25.693 1.00 9.24  ? 193 TYR A CA  1 
ATOM   3584 C  C   . TYR B 1 193 ? 10.382  36.579  -25.484 1.00 9.21  ? 193 TYR A C   1 
ATOM   3585 O  O   . TYR B 1 193 ? 11.441  37.008  -24.992 1.00 11.11 ? 193 TYR A O   1 
ATOM   3586 C  CB  . TYR B 1 193 ? 9.151   34.579  -24.616 1.00 8.56  ? 193 TYR A CB  1 
ATOM   3587 C  CG  . TYR B 1 193 ? 9.681   34.788  -23.137 1.00 9.61  ? 193 TYR A CG  1 
ATOM   3588 C  CD1 . TYR B 1 193 ? 9.489   36.013  -22.481 1.00 9.47  ? 193 TYR A CD1 1 
ATOM   3589 C  CD2 . TYR B 1 193 ? 10.357  33.803  -22.498 1.00 10.05 ? 193 TYR A CD2 1 
ATOM   3590 C  CE1 . TYR B 1 193 ? 9.964   36.232  -21.182 1.00 10.39 ? 193 TYR A CE1 1 
ATOM   3591 C  CE2 . TYR B 1 193 ? 10.868  33.989  -21.209 1.00 9.85  ? 193 TYR A CE2 1 
ATOM   3592 C  CZ  . TYR B 1 193 ? 10.654  35.207  -20.557 1.00 9.90  ? 193 TYR A CZ  1 
ATOM   3593 O  OH  . TYR B 1 193 ? 11.212  35.417  -19.286 1.00 9.68  ? 193 TYR A OH  1 
ATOM   3594 N  N   . TRP B 1 194 ? 9.338   37.332  -25.821 1.00 9.73  ? 194 TRP A N   1 
ATOM   3595 C  CA  . TRP B 1 194 ? 9.222   38.765  -25.476 1.00 9.27  ? 194 TRP A CA  1 
ATOM   3596 C  C   . TRP B 1 194 ? 8.128   38.849  -24.395 1.00 9.83  ? 194 TRP A C   1 
ATOM   3597 O  O   . TRP B 1 194 ? 7.157   38.061  -24.414 1.00 8.85  ? 194 TRP A O   1 
ATOM   3598 C  CB  . TRP B 1 194 ? 8.740   39.547  -26.684 1.00 10.61 ? 194 TRP A CB  1 
ATOM   3599 C  CG  . TRP B 1 194 ? 9.787   39.533  -27.796 1.00 11.07 ? 194 TRP A CG  1 
ATOM   3600 C  CD1 . TRP B 1 194 ? 11.046  40.184  -27.812 1.00 12.19 ? 194 TRP A CD1 1 
ATOM   3601 C  CD2 . TRP B 1 194 ? 9.668   38.860  -29.047 1.00 11.25 ? 194 TRP A CD2 1 
ATOM   3602 N  NE1 . TRP B 1 194 ? 11.689  39.897  -29.000 1.00 12.27 ? 194 TRP A NE1 1 
ATOM   3603 C  CE2 . TRP B 1 194 ? 10.870  39.097  -29.775 1.00 12.10 ? 194 TRP A CE2 1 
ATOM   3604 C  CE3 . TRP B 1 194 ? 8.665   38.088  -29.640 1.00 11.41 ? 194 TRP A CE3 1 
ATOM   3605 C  CZ2 . TRP B 1 194 ? 11.062  38.606  -31.102 1.00 11.92 ? 194 TRP A CZ2 1 
ATOM   3606 C  CZ3 . TRP B 1 194 ? 8.880   37.586  -30.964 1.00 12.20 ? 194 TRP A CZ3 1 
ATOM   3607 C  CH2 . TRP B 1 194 ? 10.080  37.822  -31.642 1.00 12.17 ? 194 TRP A CH2 1 
ATOM   3608 N  N   . THR B 1 195 ? 8.282   39.796  -23.486 1.00 8.55  ? 195 THR A N   1 
ATOM   3609 C  CA  . THR B 1 195 ? 7.254   40.000  -22.484 1.00 8.48  ? 195 THR A CA  1 
ATOM   3610 C  C   . THR B 1 195 ? 6.925   41.483  -22.305 1.00 9.84  ? 195 THR A C   1 
ATOM   3611 O  O   . THR B 1 195 ? 7.800   42.352  -22.415 1.00 9.34  ? 195 THR A O   1 
ATOM   3612 C  CB  . THR B 1 195 ? 7.655   39.367  -21.134 1.00 7.99  ? 195 THR A CB  1 
ATOM   3613 O  OG1 . THR B 1 195 ? 6.548   39.483  -20.226 1.00 8.51  ? 195 THR A OG1 1 
ATOM   3614 C  CG2 . THR B 1 195 ? 8.935   39.990  -20.494 1.00 8.03  ? 195 THR A CG2 1 
ATOM   3615 N  N   . TYR B 1 196 ? 5.693   41.761  -21.974 1.00 8.74  ? 196 TYR A N   1 
ATOM   3616 C  CA  . TYR B 1 196 ? 5.279   43.147  -21.773 1.00 8.59  ? 196 TYR A CA  1 
ATOM   3617 C  C   . TYR B 1 196 ? 3.951   43.124  -21.023 1.00 9.10  ? 196 TYR A C   1 
ATOM   3618 O  O   . TYR B 1 196 ? 3.243   42.080  -21.027 1.00 8.04  ? 196 TYR A O   1 
ATOM   3619 C  CB  . TYR B 1 196 ? 5.122   43.833  -23.143 1.00 8.69  ? 196 TYR A CB  1 
ATOM   3620 C  CG  . TYR B 1 196 ? 3.909   43.445  -23.923 1.00 8.12  ? 196 TYR A CG  1 
ATOM   3621 C  CD1 . TYR B 1 196 ? 3.930   42.278  -24.760 1.00 7.76  ? 196 TYR A CD1 1 
ATOM   3622 C  CD2 . TYR B 1 196 ? 2.693   44.172  -23.787 1.00 7.57  ? 196 TYR A CD2 1 
ATOM   3623 C  CE1 . TYR B 1 196 ? 2.803   41.934  -25.486 1.00 7.85  ? 196 TYR A CE1 1 
ATOM   3624 C  CE2 . TYR B 1 196 ? 1.551   43.815  -24.524 1.00 7.62  ? 196 TYR A CE2 1 
ATOM   3625 C  CZ  . TYR B 1 196 ? 1.633   42.667  -25.350 1.00 7.62  ? 196 TYR A CZ  1 
ATOM   3626 O  OH  . TYR B 1 196 ? 0.490   42.319  -26.034 1.00 7.55  ? 196 TYR A OH  1 
ATOM   3627 N  N   . PRO B 1 197 ? 3.628   44.226  -20.339 1.00 9.03  ? 197 PRO A N   1 
ATOM   3628 C  CA  . PRO B 1 197 ? 2.308   44.263  -19.694 1.00 9.29  ? 197 PRO A CA  1 
ATOM   3629 C  C   . PRO B 1 197 ? 1.167   44.638  -20.630 1.00 9.00  ? 197 PRO A C   1 
ATOM   3630 O  O   . PRO B 1 197 ? 1.261   45.633  -21.340 1.00 10.01 ? 197 PRO A O   1 
ATOM   3631 C  CB  . PRO B 1 197 ? 2.467   45.369  -18.618 1.00 9.22  ? 197 PRO A CB  1 
ATOM   3632 C  CG  . PRO B 1 197 ? 3.494   46.333  -19.211 1.00 9.37  ? 197 PRO A CG  1 
ATOM   3633 C  CD  . PRO B 1 197 ? 4.386   45.480  -20.141 1.00 10.34 ? 197 PRO A CD  1 
ATOM   3634 N  N   . GLY B 1 198 ? 0.086   43.888  -20.605 1.00 8.68  ? 198 GLY A N   1 
ATOM   3635 C  CA  . GLY B 1 198 ? -1.014  44.231  -21.534 1.00 9.07  ? 198 GLY A CA  1 
ATOM   3636 C  C   . GLY B 1 198 ? -2.321  43.716  -21.039 1.00 9.82  ? 198 GLY A C   1 
ATOM   3637 O  O   . GLY B 1 198 ? -2.598  43.748  -19.854 1.00 9.41  ? 198 GLY A O   1 
ATOM   3638 N  N   . SER B 1 199 ? -3.164  43.309  -21.999 1.00 9.67  ? 199 SER A N   1 
ATOM   3639 C  CA  . SER B 1 199 ? -4.621  43.211  -21.671 1.00 9.29  ? 199 SER A CA  1 
ATOM   3640 C  C   . SER B 1 199 ? -5.166  41.933  -22.333 1.00 8.86  ? 199 SER A C   1 
ATOM   3641 O  O   . SER B 1 199 ? -4.523  41.351  -23.183 1.00 8.42  ? 199 SER A O   1 
ATOM   3642 C  CB  . SER B 1 199 ? -5.349  44.449  -22.202 1.00 8.65  ? 199 SER A CB  1 
ATOM   3643 O  OG  . SER B 1 199 ? -5.520  44.281  -23.629 1.00 9.70  ? 199 SER A OG  1 
ATOM   3644 N  N   . LEU B 1 200 ? -6.380  41.550  -21.949 1.00 8.74  ? 200 LEU A N   1 
ATOM   3645 C  CA  . LEU B 1 200 ? -7.170  40.615  -22.819 1.00 8.22  ? 200 LEU A CA  1 
ATOM   3646 C  C   . LEU B 1 200 ? -7.291  41.265  -24.179 1.00 9.14  ? 200 LEU A C   1 
ATOM   3647 O  O   . LEU B 1 200 ? -7.459  42.499  -24.260 1.00 8.19  ? 200 LEU A O   1 
ATOM   3648 C  CB  . LEU B 1 200 ? -8.579  40.516  -22.318 1.00 9.58  ? 200 LEU A CB  1 
ATOM   3649 C  CG  . LEU B 1 200 ? -8.902  39.449  -21.265 1.00 9.70  ? 200 LEU A CG  1 
ATOM   3650 C  CD1 . LEU B 1 200 ? -8.041  39.624  -20.011 1.00 10.15 ? 200 LEU A CD1 1 
ATOM   3651 C  CD2 . LEU B 1 200 ? -10.384 39.473  -20.878 1.00 10.14 ? 200 LEU A CD2 1 
ATOM   3652 N  N   . THR B 1 201 ? -7.211  40.440  -25.221 1.00 7.78  ? 201 THR A N   1 
ATOM   3653 C  CA  . THR B 1 201 ? -7.386  40.998  -26.583 1.00 8.38  ? 201 THR A CA  1 
ATOM   3654 C  C   . THR B 1 201 ? -8.836  40.922  -27.082 1.00 9.30  ? 201 THR A C   1 
ATOM   3655 O  O   . THR B 1 201 ? -9.134  41.222  -28.287 1.00 9.78  ? 201 THR A O   1 
ATOM   3656 C  CB  . THR B 1 201 ? -6.518  40.278  -27.603 1.00 8.06  ? 201 THR A CB  1 
ATOM   3657 O  OG1 . THR B 1 201 ? -6.980  38.935  -27.700 1.00 8.10  ? 201 THR A OG1 1 
ATOM   3658 C  CG2 . THR B 1 201 ? -5.045  40.301  -27.193 1.00 9.21  ? 201 THR A CG2 1 
ATOM   3659 N  N   . VAL B 1 202 ? -9.741  40.576  -26.174 1.00 8.92  ? 202 VAL A N   1 
ATOM   3660 C  CA  . VAL B 1 202 ? -11.195 40.504  -26.417 1.00 9.57  ? 202 VAL A CA  1 
ATOM   3661 C  C   . VAL B 1 202 ? -11.871 41.212  -25.249 1.00 10.19 ? 202 VAL A C   1 
ATOM   3662 O  O   . VAL B 1 202 ? -11.307 41.296  -24.156 1.00 10.15 ? 202 VAL A O   1 
ATOM   3663 C  CB  . VAL B 1 202 ? -11.721 39.043  -26.456 1.00 9.53  ? 202 VAL A CB  1 
ATOM   3664 C  CG1 . VAL B 1 202 ? -11.073 38.275  -27.623 1.00 10.42 ? 202 VAL A CG1 1 
ATOM   3665 C  CG2 . VAL B 1 202 ? -11.409 38.306  -25.159 1.00 10.09 ? 202 VAL A CG2 1 
ATOM   3666 N  N   . PRO B 1 203 ? -13.049 41.796  -25.477 1.00 10.46 ? 203 PRO A N   1 
ATOM   3667 C  CA  . PRO B 1 203 ? -13.884 42.243  -24.377 1.00 10.21 ? 203 PRO A CA  1 
ATOM   3668 C  C   . PRO B 1 203 ? -13.918 41.237  -23.248 1.00 10.73 ? 203 PRO A C   1 
ATOM   3669 O  O   . PRO B 1 203 ? -14.110 40.039  -23.454 1.00 10.11 ? 203 PRO A O   1 
ATOM   3670 C  CB  . PRO B 1 203 ? -15.279 42.340  -25.057 1.00 9.93  ? 203 PRO A CB  1 
ATOM   3671 C  CG  . PRO B 1 203 ? -14.907 42.859  -26.408 1.00 10.91 ? 203 PRO A CG  1 
ATOM   3672 C  CD  . PRO B 1 203 ? -13.803 41.881  -26.767 1.00 10.33 ? 203 PRO A CD  1 
ATOM   3673 N  N   . PRO B 1 204 ? -13.766 41.690  -22.009 1.00 12.50 ? 204 PRO A N   1 
ATOM   3674 C  CA  . PRO B 1 204 ? -13.793 43.063  -21.565 1.00 12.28 ? 204 PRO A CA  1 
ATOM   3675 C  C   . PRO B 1 204 ? -12.458 43.856  -21.642 1.00 11.50 ? 204 PRO A C   1 
ATOM   3676 O  O   . PRO B 1 204 ? -12.385 44.987  -21.049 1.00 11.46 ? 204 PRO A O   1 
ATOM   3677 C  CB  . PRO B 1 204 ? -14.288 42.910  -20.086 1.00 14.00 ? 204 PRO A CB  1 
ATOM   3678 C  CG  . PRO B 1 204 ? -13.765 41.535  -19.668 1.00 12.99 ? 204 PRO A CG  1 
ATOM   3679 C  CD  . PRO B 1 204 ? -13.874 40.707  -20.917 1.00 13.40 ? 204 PRO A CD  1 
ATOM   3680 N  N   . LEU B 1 205 ? -11.408 43.287  -22.289 1.00 11.46 ? 205 LEU A N   1 
ATOM   3681 C  CA  . LEU B 1 205 ? -10.147 43.995  -22.589 1.00 10.40 ? 205 LEU A CA  1 
ATOM   3682 C  C   . LEU B 1 205 ? -9.381  44.445  -21.325 1.00 11.59 ? 205 LEU A C   1 
ATOM   3683 O  O   . LEU B 1 205 ? -8.681  45.456  -21.342 1.00 9.71  ? 205 LEU A O   1 
ATOM   3684 C  CB  . LEU B 1 205 ? -10.416 45.230  -23.489 1.00 10.52 ? 205 LEU A CB  1 
ATOM   3685 C  CG  . LEU B 1 205 ? -11.016 44.756  -24.824 1.00 10.79 ? 205 LEU A CG  1 
ATOM   3686 C  CD1 . LEU B 1 205 ? -11.652 45.943  -25.569 1.00 13.17 ? 205 LEU A CD1 1 
ATOM   3687 C  CD2 . LEU B 1 205 ? -9.989  44.160  -25.793 1.00 11.32 ? 205 LEU A CD2 1 
ATOM   3688 N  N   . LEU B 1 206 ? -9.566  43.697  -20.241 1.00 11.90 ? 206 LEU A N   1 
ATOM   3689 C  CA  . LEU B 1 206 ? -9.040  44.121  -18.910 1.00 11.99 ? 206 LEU A CA  1 
ATOM   3690 C  C   . LEU B 1 206 ? -7.497  44.108  -18.945 1.00 11.17 ? 206 LEU A C   1 
ATOM   3691 O  O   . LEU B 1 206 ? -6.903  43.185  -19.533 1.00 10.40 ? 206 LEU A O   1 
ATOM   3692 C  CB  . LEU B 1 206 ? -9.536  43.180  -17.790 1.00 13.04 ? 206 LEU A CB  1 
ATOM   3693 C  CG  . LEU B 1 206 ? -11.052 43.160  -17.632 1.00 13.25 ? 206 LEU A CG  1 
ATOM   3694 C  CD1 . LEU B 1 206 ? -11.458 41.968  -16.786 1.00 13.98 ? 206 LEU A CD1 1 
ATOM   3695 C  CD2 . LEU B 1 206 ? -11.624 44.436  -17.014 1.00 14.75 ? 206 LEU A CD2 1 
ATOM   3696 N  N   . GLU B 1 207 ? -6.888  45.111  -18.293 1.00 9.98  ? 207 GLU A N   1 
ATOM   3697 C  CA  . GLU B 1 207 ? -5.393  45.264  -18.263 1.00 9.89  ? 207 GLU A CA  1 
ATOM   3698 C  C   . GLU B 1 207 ? -4.863  44.485  -17.117 1.00 9.46  ? 207 GLU A C   1 
ATOM   3699 O  O   . GLU B 1 207 ? -4.448  45.040  -16.121 1.00 9.99  ? 207 GLU A O   1 
ATOM   3700 C  CB  . GLU B 1 207 ? -5.031  46.789  -18.251 1.00 10.31 ? 207 GLU A CB  1 
ATOM   3701 C  CG  . GLU B 1 207 ? -5.517  47.391  -19.563 1.00 10.19 ? 207 GLU A CG  1 
ATOM   3702 C  CD  . GLU B 1 207 ? -5.246  48.846  -19.708 1.00 10.01 ? 207 GLU A CD  1 
ATOM   3703 O  OE1 . GLU B 1 207 ? -5.127  49.557  -18.652 1.00 11.78 ? 207 GLU A OE1 1 
ATOM   3704 O  OE2 . GLU B 1 207 ? -5.222  49.267  -20.903 1.00 12.33 ? 207 GLU A OE2 1 
ATOM   3705 N  N   . SER B 1 208 ? -4.911  43.144  -17.258 1.00 8.95  ? 208 SER A N   1 
ATOM   3706 C  CA  . SER B 1 208 ? -4.523  42.209  -16.198 1.00 9.71  ? 208 SER A CA  1 
ATOM   3707 C  C   . SER B 1 208 ? -3.515  41.128  -16.656 1.00 9.35  ? 208 SER A C   1 
ATOM   3708 O  O   . SER B 1 208 ? -3.266  40.131  -15.931 1.00 9.18  ? 208 SER A O   1 
ATOM   3709 C  CB  . SER B 1 208 ? -5.811  41.508  -15.736 1.00 10.49 ? 208 SER A CB  1 
ATOM   3710 O  OG  . SER B 1 208 ? -6.427  40.929  -16.876 1.00 13.16 ? 208 SER A OG  1 
ATOM   3711 N  N   . VAL B 1 209 ? -2.933  41.304  -17.851 1.00 8.87  ? 209 VAL A N   1 
ATOM   3712 C  CA  . VAL B 1 209 ? -2.169  40.209  -18.502 1.00 8.28  ? 209 VAL A CA  1 
ATOM   3713 C  C   . VAL B 1 209 ? -0.658  40.529  -18.600 1.00 9.12  ? 209 VAL A C   1 
ATOM   3714 O  O   . VAL B 1 209 ? -0.269  41.560  -19.170 1.00 9.53  ? 209 VAL A O   1 
ATOM   3715 C  CB  . VAL B 1 209 ? -2.692  39.927  -19.965 1.00 7.82  ? 209 VAL A CB  1 
ATOM   3716 C  CG1 . VAL B 1 209 ? -1.879  38.737  -20.519 1.00 7.74  ? 209 VAL A CG1 1 
ATOM   3717 C  CG2 . VAL B 1 209 ? -4.213  39.567  -19.934 1.00 7.72  ? 209 VAL A CG2 1 
ATOM   3718 N  N   . THR B 1 210 ? 0.157   39.620  -18.055 1.00 9.08  ? 210 THR A N   1 
ATOM   3719 C  CA  . THR B 1 210 ? 1.569   39.557  -18.392 1.00 8.52  ? 210 THR A CA  1 
ATOM   3720 C  C   . THR B 1 210 ? 1.676   38.656  -19.629 1.00 8.38  ? 210 THR A C   1 
ATOM   3721 O  O   . THR B 1 210 ? 1.443   37.439  -19.607 1.00 9.20  ? 210 THR A O   1 
ATOM   3722 C  CB  . THR B 1 210 ? 2.354   38.974  -17.193 1.00 8.67  ? 210 THR A CB  1 
ATOM   3723 O  OG1 . THR B 1 210 ? 2.092   39.841  -16.075 1.00 8.42  ? 210 THR A OG1 1 
ATOM   3724 C  CG2 . THR B 1 210 ? 3.813   38.988  -17.534 1.00 7.56  ? 210 THR A CG2 1 
ATOM   3725 N  N   . TRP B 1 211 ? 1.937   39.302  -20.744 1.00 8.53  ? 211 TRP A N   1 
ATOM   3726 C  CA  . TRP B 1 211 ? 2.166   38.632  -22.019 1.00 7.87  ? 211 TRP A CA  1 
ATOM   3727 C  C   . TRP B 1 211 ? 3.576   38.044  -22.150 1.00 8.62  ? 211 TRP A C   1 
ATOM   3728 O  O   . TRP B 1 211 ? 4.578   38.687  -21.807 1.00 7.63  ? 211 TRP A O   1 
ATOM   3729 C  CB  . TRP B 1 211 ? 1.925   39.632  -23.190 1.00 8.01  ? 211 TRP A CB  1 
ATOM   3730 C  CG  . TRP B 1 211 ? 0.464   39.728  -23.470 1.00 7.91  ? 211 TRP A CG  1 
ATOM   3731 C  CD1 . TRP B 1 211 ? -0.425  40.689  -23.021 1.00 8.25  ? 211 TRP A CD1 1 
ATOM   3732 C  CD2 . TRP B 1 211 ? -0.303  38.778  -24.203 1.00 8.23  ? 211 TRP A CD2 1 
ATOM   3733 N  NE1 . TRP B 1 211 ? -1.701  40.351  -23.406 1.00 7.45  ? 211 TRP A NE1 1 
ATOM   3734 C  CE2 . TRP B 1 211 ? -1.661  39.197  -24.136 1.00 7.97  ? 211 TRP A CE2 1 
ATOM   3735 C  CE3 . TRP B 1 211 ? 0.024   37.600  -24.922 1.00 7.32  ? 211 TRP A CE3 1 
ATOM   3736 C  CZ2 . TRP B 1 211 ? -2.715  38.473  -24.746 1.00 7.17  ? 211 TRP A CZ2 1 
ATOM   3737 C  CZ3 . TRP B 1 211 ? -1.008  36.907  -25.570 1.00 7.40  ? 211 TRP A CZ3 1 
ATOM   3738 C  CH2 . TRP B 1 211 ? -2.351  37.300  -25.431 1.00 7.67  ? 211 TRP A CH2 1 
ATOM   3739 N  N   . ILE B 1 212 ? 3.605   36.780  -22.624 1.00 7.58  ? 212 ILE A N   1 
ATOM   3740 C  CA  . ILE B 1 212 ? 4.865   36.076  -22.867 1.00 7.18  ? 212 ILE A CA  1 
ATOM   3741 C  C   . ILE B 1 212 ? 4.649   35.520  -24.272 1.00 7.79  ? 212 ILE A C   1 
ATOM   3742 O  O   . ILE B 1 212 ? 3.966   34.542  -24.441 1.00 8.37  ? 212 ILE A O   1 
ATOM   3743 C  CB  . ILE B 1 212 ? 5.094   34.946  -21.789 1.00 7.22  ? 212 ILE A CB  1 
ATOM   3744 C  CG1 . ILE B 1 212 ? 5.270   35.591  -20.400 1.00 7.89  ? 212 ILE A CG1 1 
ATOM   3745 C  CG2 . ILE B 1 212 ? 6.325   34.073  -22.100 1.00 7.11  ? 212 ILE A CG2 1 
ATOM   3746 C  CD1 . ILE B 1 212 ? 5.114   34.670  -19.185 1.00 7.58  ? 212 ILE A CD1 1 
ATOM   3747 N  N   . VAL B 1 213 ? 5.282   36.147  -25.271 1.00 7.86  ? 213 VAL A N   1 
ATOM   3748 C  CA  . VAL B 1 213 ? 5.037   35.790  -26.679 1.00 8.27  ? 213 VAL A CA  1 
ATOM   3749 C  C   . VAL B 1 213 ? 6.293   35.086  -27.135 1.00 8.42  ? 213 VAL A C   1 
ATOM   3750 O  O   . VAL B 1 213 ? 7.340   35.677  -27.120 1.00 8.78  ? 213 VAL A O   1 
ATOM   3751 C  CB  . VAL B 1 213 ? 4.816   37.044  -27.503 1.00 7.97  ? 213 VAL A CB  1 
ATOM   3752 C  CG1 . VAL B 1 213 ? 4.696   36.688  -29.016 1.00 7.99  ? 213 VAL A CG1 1 
ATOM   3753 C  CG2 . VAL B 1 213 ? 3.569   37.866  -27.047 1.00 9.57  ? 213 VAL A CG2 1 
ATOM   3754 N  N   . LEU B 1 214 ? 6.165   33.845  -27.569 1.00 8.04  ? 214 LEU A N   1 
ATOM   3755 C  CA  . LEU B 1 214 ? 7.373   33.081  -27.977 1.00 8.61  ? 214 LEU A CA  1 
ATOM   3756 C  C   . LEU B 1 214 ? 7.775   33.504  -29.372 1.00 8.44  ? 214 LEU A C   1 
ATOM   3757 O  O   . LEU B 1 214 ? 6.912   33.700  -30.252 1.00 8.76  ? 214 LEU A O   1 
ATOM   3758 C  CB  . LEU B 1 214 ? 7.093   31.575  -27.943 1.00 8.92  ? 214 LEU A CB  1 
ATOM   3759 C  CG  . LEU B 1 214 ? 7.144   30.970  -26.503 1.00 10.96 ? 214 LEU A CG  1 
ATOM   3760 C  CD1 . LEU B 1 214 ? 6.317   31.587  -25.414 1.00 14.17 ? 214 LEU A CD1 1 
ATOM   3761 C  CD2 . LEU B 1 214 ? 6.710   29.485  -26.621 1.00 11.62 ? 214 LEU A CD2 1 
ATOM   3762 N  N   . LYS B 1 215 ? 9.074   33.635  -29.563 1.00 7.96  ? 215 LYS A N   1 
ATOM   3763 C  CA  . LYS B 1 215 ? 9.654   34.038  -30.871 1.00 9.18  ? 215 LYS A CA  1 
ATOM   3764 C  C   . LYS B 1 215 ? 9.464   32.982  -31.965 1.00 10.30 ? 215 LYS A C   1 
ATOM   3765 O  O   . LYS B 1 215 ? 9.100   33.336  -33.138 1.00 11.57 ? 215 LYS A O   1 
ATOM   3766 C  CB  . LYS B 1 215 ? 11.141  34.322  -30.681 1.00 9.67  ? 215 LYS A CB  1 
ATOM   3767 C  CG  . LYS B 1 215 ? 11.845  34.634  -31.970 1.00 10.86 ? 215 LYS A CG  1 
ATOM   3768 C  CD  . LYS B 1 215 ? 13.236  35.186  -31.671 1.00 12.64 ? 215 LYS A CD  1 
ATOM   3769 C  CE  . LYS B 1 215 ? 14.086  35.168  -32.980 1.00 15.90 ? 215 LYS A CE  1 
ATOM   3770 N  NZ  . LYS B 1 215 ? 15.400  35.851  -32.654 1.00 22.64 ? 215 LYS A NZ  1 
ATOM   3771 N  N   . GLN B 1 216 ? 9.681   31.705  -31.600 1.00 9.31  ? 216 GLN A N   1 
ATOM   3772 C  CA  . GLN B 1 216 ? 9.687   30.638  -32.611 1.00 10.65 ? 216 GLN A CA  1 
ATOM   3773 C  C   . GLN B 1 216 ? 8.272   30.158  -32.933 1.00 10.40 ? 216 GLN A C   1 
ATOM   3774 O  O   . GLN B 1 216 ? 7.594   29.663  -32.052 1.00 10.12 ? 216 GLN A O   1 
ATOM   3775 C  CB  . GLN B 1 216 ? 10.539  29.470  -32.135 1.00 10.23 ? 216 GLN A CB  1 
ATOM   3776 C  CG  . GLN B 1 216 ? 10.603  28.406  -33.205 1.00 11.36 ? 216 GLN A CG  1 
ATOM   3777 C  CD  . GLN B 1 216 ? 11.529  27.223  -32.915 1.00 12.66 ? 216 GLN A CD  1 
ATOM   3778 O  OE1 . GLN B 1 216 ? 12.068  27.040  -31.808 1.00 12.74 ? 216 GLN A OE1 1 
ATOM   3779 N  NE2 . GLN B 1 216 ? 11.723  26.405  -33.948 1.00 13.62 ? 216 GLN A NE2 1 
ATOM   3780 N  N   . PRO B 1 217 ? 7.861   30.217  -34.176 1.00 10.18 ? 217 PRO A N   1 
ATOM   3781 C  CA  . PRO B 1 217 ? 6.525   29.713  -34.475 1.00 10.68 ? 217 PRO A CA  1 
ATOM   3782 C  C   . PRO B 1 217 ? 6.479   28.183  -34.590 1.00 10.67 ? 217 PRO A C   1 
ATOM   3783 O  O   . PRO B 1 217 ? 7.550   27.533  -34.736 1.00 11.03 ? 217 PRO A O   1 
ATOM   3784 C  CB  . PRO B 1 217 ? 6.234   30.205  -35.920 1.00 11.71 ? 217 PRO A CB  1 
ATOM   3785 C  CG  . PRO B 1 217 ? 7.533   30.731  -36.413 1.00 14.11 ? 217 PRO A CG  1 
ATOM   3786 C  CD  . PRO B 1 217 ? 8.563   30.821  -35.337 1.00 11.06 ? 217 PRO A CD  1 
ATOM   3787 N  N   . ILE B 1 218 ? 5.255   27.656  -34.529 1.00 10.20 ? 218 ILE A N   1 
ATOM   3788 C  CA  . ILE B 1 218 ? 5.006   26.261  -34.927 1.00 10.78 ? 218 ILE A CA  1 
ATOM   3789 C  C   . ILE B 1 218 ? 4.295   26.238  -36.304 1.00 11.05 ? 218 ILE A C   1 
ATOM   3790 O  O   . ILE B 1 218 ? 3.874   27.278  -36.770 1.00 10.61 ? 218 ILE A O   1 
ATOM   3791 C  CB  . ILE B 1 218 ? 4.114   25.528  -33.868 1.00 10.88 ? 218 ILE A CB  1 
ATOM   3792 C  CG1 . ILE B 1 218 ? 2.714   26.096  -33.803 1.00 11.43 ? 218 ILE A CG1 1 
ATOM   3793 C  CG2 . ILE B 1 218 ? 4.836   25.542  -32.492 1.00 10.59 ? 218 ILE A CG2 1 
ATOM   3794 C  CD1 . ILE B 1 218 ? 1.755   25.249  -33.039 1.00 11.31 ? 218 ILE A CD1 1 
ATOM   3795 N  N   . ASN B 1 219 ? 4.286   25.087  -36.980 1.00 11.57 ? 219 ASN A N   1 
ATOM   3796 C  CA  . ASN B 1 219 ? 3.663   25.002  -38.318 1.00 11.85 ? 219 ASN A CA  1 
ATOM   3797 C  C   . ASN B 1 219 ? 2.166   24.702  -38.279 1.00 12.04 ? 219 ASN A C   1 
ATOM   3798 O  O   . ASN B 1 219 ? 1.673   24.029  -37.364 1.00 12.96 ? 219 ASN A O   1 
ATOM   3799 C  CB  . ASN B 1 219 ? 4.329   23.863  -39.114 1.00 13.51 ? 219 ASN A CB  1 
ATOM   3800 C  CG  . ASN B 1 219 ? 5.720   24.191  -39.568 1.00 16.50 ? 219 ASN A CG  1 
ATOM   3801 O  OD1 . ASN B 1 219 ? 6.474   23.293  -39.995 1.00 21.39 ? 219 ASN A OD1 1 
ATOM   3802 N  ND2 . ASN B 1 219 ? 6.048   25.441  -39.613 1.00 15.78 ? 219 ASN A ND2 1 
ATOM   3803 N  N   . ILE B 1 220 ? 1.472   25.130  -39.340 1.00 10.17 ? 220 ILE A N   1 
ATOM   3804 C  CA  . ILE B 1 220 ? 0.098   24.664  -39.569 1.00 10.99 ? 220 ILE A CA  1 
ATOM   3805 C  C   . ILE B 1 220 ? -0.040  24.707  -41.107 1.00 10.62 ? 220 ILE A C   1 
ATOM   3806 O  O   . ILE B 1 220 ? 0.470   25.650  -41.713 1.00 11.33 ? 220 ILE A O   1 
ATOM   3807 C  CB  . ILE B 1 220 ? -0.974  25.558  -38.896 1.00 10.31 ? 220 ILE A CB  1 
ATOM   3808 C  CG1 . ILE B 1 220 ? -2.349  24.938  -39.071 1.00 10.14 ? 220 ILE A CG1 1 
ATOM   3809 C  CG2 . ILE B 1 220 ? -0.985  27.053  -39.380 1.00 11.03 ? 220 ILE A CG2 1 
ATOM   3810 C  CD1 . ILE B 1 220 ? -3.444  25.609  -38.152 1.00 11.26 ? 220 ILE A CD1 1 
ATOM   3811 N  N   . SER B 1 221 ? -0.761  23.740  -41.692 1.00 10.37 ? 221 SER A N   1 
ATOM   3812 C  CA  . SER B 1 221 ? -0.924  23.826  -43.162 1.00 10.42 ? 221 SER A CA  1 
ATOM   3813 C  C   . SER B 1 221 ? -2.113  24.707  -43.487 1.00 11.09 ? 221 SER A C   1 
ATOM   3814 O  O   . SER B 1 221 ? -3.020  24.899  -42.621 1.00 11.17 ? 221 SER A O   1 
ATOM   3815 C  CB  . SER B 1 221 ? -1.118  22.418  -43.814 1.00 9.35  ? 221 SER A CB  1 
ATOM   3816 O  OG  . SER B 1 221 ? -2.438  21.933  -43.544 1.00 9.98  ? 221 SER A OG  1 
ATOM   3817 N  N   A SER B 1 222 ? -2.145  25.197  -44.723 0.50 10.26 ? 222 SER A N   1 
ATOM   3818 N  N   B SER B 1 222 ? -2.178  25.212  -44.722 0.50 10.64 ? 222 SER A N   1 
ATOM   3819 C  CA  A SER B 1 222 ? -3.296  25.964  -45.151 0.50 10.09 ? 222 SER A CA  1 
ATOM   3820 C  CA  B SER B 1 222 ? -3.371  25.969  -45.130 0.50 10.62 ? 222 SER A CA  1 
ATOM   3821 C  C   A SER B 1 222 ? -4.613  25.185  -44.961 0.50 9.80  ? 222 SER A C   1 
ATOM   3822 C  C   B SER B 1 222 ? -4.648  25.169  -44.931 0.50 10.12 ? 222 SER A C   1 
ATOM   3823 O  O   A SER B 1 222 ? -5.599  25.748  -44.463 0.50 10.16 ? 222 SER A O   1 
ATOM   3824 O  O   B SER B 1 222 ? -5.641  25.693  -44.405 0.50 10.28 ? 222 SER A O   1 
ATOM   3825 C  CB  A SER B 1 222 ? -3.134  26.361  -46.625 0.50 9.41  ? 222 SER A CB  1 
ATOM   3826 C  CB  B SER B 1 222 ? -3.265  26.372  -46.607 0.50 10.49 ? 222 SER A CB  1 
ATOM   3827 O  OG  A SER B 1 222 ? -4.278  27.060  -47.010 0.50 9.07  ? 222 SER A OG  1 
ATOM   3828 O  OG  B SER B 1 222 ? -2.188  27.246  -46.744 0.50 11.18 ? 222 SER A OG  1 
ATOM   3829 N  N   . GLN B 1 223 ? -4.628  23.890  -45.357 1.00 10.19 ? 223 GLN A N   1 
ATOM   3830 C  CA  . GLN B 1 223 ? -5.809  23.010  -45.165 1.00 9.99  ? 223 GLN A CA  1 
ATOM   3831 C  C   . GLN B 1 223 ? -6.217  22.813  -43.701 1.00 9.50  ? 223 GLN A C   1 
ATOM   3832 O  O   . GLN B 1 223 ? -7.386  22.897  -43.389 1.00 10.99 ? 223 GLN A O   1 
ATOM   3833 C  CB  . GLN B 1 223 ? -5.539  21.645  -45.834 1.00 11.20 ? 223 GLN A CB  1 
ATOM   3834 C  CG  . GLN B 1 223 ? -5.732  21.676  -47.355 1.00 13.59 ? 223 GLN A CG  1 
ATOM   3835 C  CD  . GLN B 1 223 ? -5.748  20.257  -47.932 1.00 15.47 ? 223 GLN A CD  1 
ATOM   3836 O  OE1 . GLN B 1 223 ? -6.452  19.358  -47.423 1.00 17.22 ? 223 GLN A OE1 1 
ATOM   3837 N  NE2 . GLN B 1 223 ? -4.926  20.023  -48.893 1.00 18.15 ? 223 GLN A NE2 1 
ATOM   3838 N  N   . GLN B 1 224 ? -5.257  22.692  -42.790 1.00 9.71  ? 224 GLN A N   1 
ATOM   3839 C  CA  . GLN B 1 224 ? -5.610  22.597  -41.392 1.00 10.05 ? 224 GLN A CA  1 
ATOM   3840 C  C   . GLN B 1 224 ? -6.244  23.934  -40.930 1.00 10.26 ? 224 GLN A C   1 
ATOM   3841 O  O   . GLN B 1 224 ? -7.312  23.925  -40.239 1.00 9.80  ? 224 GLN A O   1 
ATOM   3842 C  CB  . GLN B 1 224 ? -4.389  22.309  -40.532 1.00 9.68  ? 224 GLN A CB  1 
ATOM   3843 C  CG  . GLN B 1 224 ? -3.803  20.882  -40.709 1.00 9.74  ? 224 GLN A CG  1 
ATOM   3844 C  CD  . GLN B 1 224 ? -2.554  20.683  -39.830 1.00 11.20 ? 224 GLN A CD  1 
ATOM   3845 O  OE1 . GLN B 1 224 ? -1.554  21.399  -39.919 1.00 11.59 ? 224 GLN A OE1 1 
ATOM   3846 N  NE2 . GLN B 1 224 ? -2.603  19.687  -38.976 1.00 12.56 ? 224 GLN A NE2 1 
ATOM   3847 N  N   . LEU B 1 225 ? -5.631  25.048  -41.313 1.00 9.36  ? 225 LEU A N   1 
ATOM   3848 C  CA  . LEU B 1 225 ? -6.077  26.325  -40.732 1.00 9.53  ? 225 LEU A CA  1 
ATOM   3849 C  C   . LEU B 1 225 ? -7.456  26.623  -41.292 1.00 10.24 ? 225 LEU A C   1 
ATOM   3850 O  O   . LEU B 1 225 ? -8.308  27.170  -40.618 1.00 10.10 ? 225 LEU A O   1 
ATOM   3851 C  CB  . LEU B 1 225 ? -5.121  27.430  -41.132 1.00 9.54  ? 225 LEU A CB  1 
ATOM   3852 C  CG  . LEU B 1 225 ? -5.414  28.861  -40.655 1.00 9.67  ? 225 LEU A CG  1 
ATOM   3853 C  CD1 . LEU B 1 225 ? -5.755  28.850  -39.144 1.00 10.31 ? 225 LEU A CD1 1 
ATOM   3854 C  CD2 . LEU B 1 225 ? -4.236  29.762  -41.042 1.00 9.95  ? 225 LEU A CD2 1 
ATOM   3855 N  N   . ALA B 1 226 ? -7.684  26.313  -42.580 1.00 9.61  ? 226 ALA A N   1 
ATOM   3856 C  CA  . ALA B 1 226 ? -9.013  26.547  -43.116 1.00 11.10 ? 226 ALA A CA  1 
ATOM   3857 C  C   . ALA B 1 226 ? -10.190 25.866  -42.375 1.00 12.58 ? 226 ALA A C   1 
ATOM   3858 O  O   . ALA B 1 226 ? -11.311 26.370  -42.434 1.00 13.57 ? 226 ALA A O   1 
ATOM   3859 C  CB  . ALA B 1 226 ? -9.051  26.171  -44.603 1.00 9.88  ? 226 ALA A CB  1 
ATOM   3860 N  N   . LYS B 1 227 ? -9.934  24.708  -41.742 1.00 12.67 ? 227 LYS A N   1 
ATOM   3861 C  CA  . LYS B 1 227 ? -10.957 24.039  -40.910 1.00 13.51 ? 227 LYS A CA  1 
ATOM   3862 C  C   . LYS B 1 227 ? -11.488 24.913  -39.760 1.00 13.13 ? 227 LYS A C   1 
ATOM   3863 O  O   . LYS B 1 227 ? -12.697 24.847  -39.442 1.00 13.00 ? 227 LYS A O   1 
ATOM   3864 C  CB  . LYS B 1 227 ? -10.463 22.705  -40.345 1.00 14.89 ? 227 LYS A CB  1 
ATOM   3865 C  CG  . LYS B 1 227 ? -10.009 21.750  -41.449 1.00 17.97 ? 227 LYS A CG  1 
ATOM   3866 C  CD  . LYS B 1 227 ? -9.367  20.495  -40.907 1.00 20.46 ? 227 LYS A CD  1 
ATOM   3867 C  CE  . LYS B 1 227 ? -10.326 19.296  -40.820 1.00 24.53 ? 227 LYS A CE  1 
ATOM   3868 N  NZ  . LYS B 1 227 ? -9.496  18.045  -40.930 1.00 22.33 ? 227 LYS A NZ  1 
ATOM   3869 N  N   . PHE B 1 228 ? -10.625 25.760  -39.175 1.00 13.14 ? 228 PHE A N   1 
ATOM   3870 C  CA  . PHE B 1 228 ? -11.093 26.706  -38.113 1.00 12.16 ? 228 PHE A CA  1 
ATOM   3871 C  C   . PHE B 1 228 ? -12.092 27.702  -38.630 1.00 13.17 ? 228 PHE A C   1 
ATOM   3872 O  O   . PHE B 1 228 ? -13.011 28.079  -37.955 1.00 11.58 ? 228 PHE A O   1 
ATOM   3873 C  CB  . PHE B 1 228 ? -9.904  27.361  -37.409 1.00 11.75 ? 228 PHE A CB  1 
ATOM   3874 C  CG  . PHE B 1 228 ? -9.049  26.357  -36.707 1.00 11.26 ? 228 PHE A CG  1 
ATOM   3875 C  CD1 . PHE B 1 228 ? -9.447  25.850  -35.482 1.00 10.42 ? 228 PHE A CD1 1 
ATOM   3876 C  CD2 . PHE B 1 228 ? -7.881  25.858  -37.288 1.00 12.19 ? 228 PHE A CD2 1 
ATOM   3877 C  CE1 . PHE B 1 228 ? -8.710  24.910  -34.814 1.00 10.36 ? 228 PHE A CE1 1 
ATOM   3878 C  CE2 . PHE B 1 228 ? -7.125  24.872  -36.638 1.00 12.63 ? 228 PHE A CE2 1 
ATOM   3879 C  CZ  . PHE B 1 228 ? -7.567  24.369  -35.386 1.00 12.13 ? 228 PHE A CZ  1 
ATOM   3880 N  N   . ARG B 1 229 ? -11.888 28.135  -39.874 1.00 14.07 ? 229 ARG A N   1 
ATOM   3881 C  CA  . ARG B 1 229 ? -12.766 29.138  -40.470 1.00 14.87 ? 229 ARG A CA  1 
ATOM   3882 C  C   . ARG B 1 229 ? -14.173 28.692  -40.760 1.00 15.80 ? 229 ARG A C   1 
ATOM   3883 O  O   . ARG B 1 229 ? -15.027 29.543  -41.050 1.00 16.95 ? 229 ARG A O   1 
ATOM   3884 C  CB  . ARG B 1 229 ? -12.164 29.717  -41.740 1.00 13.29 ? 229 ARG A CB  1 
ATOM   3885 C  CG  . ARG B 1 229 ? -10.750 30.241  -41.614 1.00 12.16 ? 229 ARG A CG  1 
ATOM   3886 C  CD  . ARG B 1 229 ? -10.452 31.261  -42.724 1.00 12.60 ? 229 ARG A CD  1 
ATOM   3887 N  NE  . ARG B 1 229 ? -9.027  31.607  -42.693 1.00 11.61 ? 229 ARG A NE  1 
ATOM   3888 C  CZ  . ARG B 1 229 ? -8.009  30.965  -43.248 1.00 10.27 ? 229 ARG A CZ  1 
ATOM   3889 N  NH1 . ARG B 1 229 ? -8.251  29.920  -44.095 1.00 10.69 ? 229 ARG A NH1 1 
ATOM   3890 N  NH2 . ARG B 1 229 ? -6.764  31.404  -43.020 1.00 9.89  ? 229 ARG A NH2 1 
ATOM   3891 N  N   A SER B 1 230 ? -14.447 27.390  -40.690 0.50 17.07 ? 230 SER A N   1 
ATOM   3892 N  N   B SER B 1 230 ? -14.428 27.384  -40.680 0.50 16.23 ? 230 SER A N   1 
ATOM   3893 C  CA  A SER B 1 230 ? -15.840 26.914  -40.821 0.50 17.06 ? 230 SER A CA  1 
ATOM   3894 C  CA  B SER B 1 230 ? -15.798 26.842  -40.809 0.50 15.83 ? 230 SER A CA  1 
ATOM   3895 C  C   A SER B 1 230 ? -16.566 26.716  -39.497 0.50 16.79 ? 230 SER A C   1 
ATOM   3896 C  C   B SER B 1 230 ? -16.574 26.771  -39.503 0.50 15.87 ? 230 SER A C   1 
ATOM   3897 O  O   A SER B 1 230 ? -17.709 26.276  -39.501 0.50 18.31 ? 230 SER A O   1 
ATOM   3898 O  O   B SER B 1 230 ? -17.765 26.482  -39.520 0.50 16.97 ? 230 SER A O   1 
ATOM   3899 C  CB  A SER B 1 230 ? -15.931 25.642  -41.684 0.50 20.19 ? 230 SER A CB  1 
ATOM   3900 C  CB  B SER B 1 230 ? -15.784 25.456  -41.487 0.50 17.41 ? 230 SER A CB  1 
ATOM   3901 O  OG  A SER B 1 230 ? -15.181 24.590  -41.108 0.50 21.38 ? 230 SER A OG  1 
ATOM   3902 O  OG  B SER B 1 230 ? -15.312 25.551  -42.819 0.50 16.53 ? 230 SER A OG  1 
ATOM   3903 N  N   . LEU B 1 231 ? -15.909 27.028  -38.366 1.00 14.24 ? 231 LEU A N   1 
ATOM   3904 C  CA  . LEU B 1 231 ? -16.647 27.201  -37.134 1.00 13.92 ? 231 LEU A CA  1 
ATOM   3905 C  C   . LEU B 1 231 ? -17.636 28.334  -37.340 1.00 13.81 ? 231 LEU A C   1 
ATOM   3906 O  O   . LEU B 1 231 ? -17.341 29.337  -38.082 1.00 14.26 ? 231 LEU A O   1 
ATOM   3907 C  CB  . LEU B 1 231 ? -15.741 27.522  -35.918 1.00 12.46 ? 231 LEU A CB  1 
ATOM   3908 C  CG  . LEU B 1 231 ? -14.794 26.396  -35.582 1.00 13.01 ? 231 LEU A CG  1 
ATOM   3909 C  CD1 . LEU B 1 231 ? -13.790 26.936  -34.594 1.00 12.02 ? 231 LEU A CD1 1 
ATOM   3910 C  CD2 . LEU B 1 231 ? -15.665 25.286  -34.973 1.00 13.36 ? 231 LEU A CD2 1 
ATOM   3911 N  N   . LEU B 1 232 ? -18.797 28.219  -36.697 1.00 14.10 ? 232 LEU A N   1 
ATOM   3912 C  CA  . LEU B 1 232 ? -19.746 29.352  -36.650 1.00 15.63 ? 232 LEU A CA  1 
ATOM   3913 C  C   . LEU B 1 232 ? -19.589 30.234  -35.437 1.00 16.45 ? 232 LEU A C   1 
ATOM   3914 O  O   . LEU B 1 232 ? -19.220 29.755  -34.352 1.00 16.40 ? 232 LEU A O   1 
ATOM   3915 C  CB  . LEU B 1 232 ? -21.199 28.849  -36.738 1.00 14.85 ? 232 LEU A CB  1 
ATOM   3916 C  CG  . LEU B 1 232 ? -21.473 27.884  -37.912 1.00 15.84 ? 232 LEU A CG  1 
ATOM   3917 C  CD1 . LEU B 1 232 ? -22.945 27.483  -37.847 1.00 16.37 ? 232 LEU A CD1 1 
ATOM   3918 C  CD2 . LEU B 1 232 ? -21.076 28.466  -39.283 1.00 15.80 ? 232 LEU A CD2 1 
ATOM   3919 N  N   . CYS B 1 233 ? -19.934 31.514  -35.612 1.00 16.07 ? 233 CYS A N   1 
ATOM   3920 C  CA  . CYS B 1 233 ? -20.060 32.407  -34.486 1.00 16.70 ? 233 CYS A CA  1 
ATOM   3921 C  C   . CYS B 1 233 ? -21.486 32.453  -33.975 1.00 15.89 ? 233 CYS A C   1 
ATOM   3922 O  O   . CYS B 1 233 ? -21.810 33.257  -33.152 1.00 17.31 ? 233 CYS A O   1 
ATOM   3923 C  CB  . CYS B 1 233 ? -19.504 33.799  -34.848 1.00 17.47 ? 233 CYS A CB  1 
ATOM   3924 S  SG  . CYS B 1 233 ? -20.436 34.638  -36.211 1.00 19.63 ? 233 CYS A SG  1 
ATOM   3925 N  N   . THR B 1 234 ? -22.344 31.611  -34.548 1.00 15.78 ? 234 THR A N   1 
ATOM   3926 C  CA  . THR B 1 234 ? -23.794 31.591  -34.251 1.00 17.85 ? 234 THR A CA  1 
ATOM   3927 C  C   . THR B 1 234 ? -24.212 30.223  -33.700 1.00 20.27 ? 234 THR A C   1 
ATOM   3928 O  O   . THR B 1 234 ? -23.580 29.183  -33.997 1.00 18.69 ? 234 THR A O   1 
ATOM   3929 C  CB  . THR B 1 234 ? -24.556 31.880  -35.555 1.00 15.69 ? 234 THR A CB  1 
ATOM   3930 O  OG1 . THR B 1 234 ? -24.055 31.001  -36.546 1.00 16.87 ? 234 THR A OG1 1 
ATOM   3931 C  CG2 . THR B 1 234 ? -24.293 33.333  -36.027 1.00 16.97 ? 234 THR A CG2 1 
ATOM   3932 N  N   . ALA B 1 235 ? -25.222 30.231  -32.849 1.00 22.89 ? 235 ALA A N   1 
ATOM   3933 C  CA  . ALA B 1 235 ? -25.728 28.991  -32.197 1.00 25.77 ? 235 ALA A CA  1 
ATOM   3934 C  C   . ALA B 1 235 ? -26.720 28.246  -33.151 1.00 30.03 ? 235 ALA A C   1 
ATOM   3935 O  O   . ALA B 1 235 ? -27.173 28.832  -34.149 1.00 27.73 ? 235 ALA A O   1 
ATOM   3936 C  CB  . ALA B 1 235 ? -26.395 29.357  -30.863 1.00 26.41 ? 235 ALA A CB  1 
ATOM   3937 N  N   . GLU B 1 236 ? -27.016 26.971  -32.849 1.00 32.58 ? 236 GLU A N   1 
ATOM   3938 C  CA  . GLU B 1 236 ? -27.986 26.144  -33.574 1.00 39.35 ? 236 GLU A CA  1 
ATOM   3939 C  C   . GLU B 1 236 ? -29.318 26.868  -33.702 1.00 40.59 ? 236 GLU A C   1 
ATOM   3940 O  O   . GLU B 1 236 ? -29.792 27.443  -32.716 1.00 38.45 ? 236 GLU A O   1 
ATOM   3941 C  CB  . GLU B 1 236 ? -28.209 24.831  -32.821 1.00 48.88 ? 236 GLU A CB  1 
ATOM   3942 C  CG  . GLU B 1 236 ? -28.865 23.729  -33.653 1.00 53.33 ? 236 GLU A CG  1 
ATOM   3943 C  CD  . GLU B 1 236 ? -28.291 22.351  -33.346 1.00 59.78 ? 236 GLU A CD  1 
ATOM   3944 O  OE1 . GLU B 1 236 ? -27.735 21.701  -34.280 1.00 53.75 ? 236 GLU A OE1 1 
ATOM   3945 O  OE2 . GLU B 1 236 ? -28.378 21.935  -32.162 1.00 62.68 ? 236 GLU A OE2 1 
ATOM   3946 N  N   . GLY B 1 237 ? -29.885 26.866  -34.922 1.00 45.19 ? 237 GLY A N   1 
ATOM   3947 C  CA  . GLY B 1 237 ? -31.115 27.609  -35.252 1.00 48.01 ? 237 GLY A CA  1 
ATOM   3948 C  C   . GLY B 1 237 ? -31.061 29.142  -35.350 1.00 54.66 ? 237 GLY A C   1 
ATOM   3949 O  O   . GLY B 1 237 ? -32.038 29.753  -35.813 1.00 56.93 ? 237 GLY A O   1 
ATOM   3950 N  N   . GLU B 1 238 ? -29.970 29.777  -34.886 1.00 47.66 ? 238 GLU A N   1 
ATOM   3951 C  CA  . GLU B 1 238 ? -29.720 31.205  -35.118 1.00 41.97 ? 238 GLU A CA  1 
ATOM   3952 C  C   . GLU B 1 238 ? -29.148 31.298  -36.550 1.00 40.51 ? 238 GLU A C   1 
ATOM   3953 O  O   . GLU B 1 238 ? -28.511 30.351  -37.009 1.00 39.47 ? 238 GLU A O   1 
ATOM   3954 C  CB  . GLU B 1 238 ? -28.777 31.770  -34.025 1.00 45.43 ? 238 GLU A CB  1 
ATOM   3955 C  CG  . GLU B 1 238 ? -28.403 33.273  -34.098 1.00 43.86 ? 238 GLU A CG  1 
ATOM   3956 C  CD  . GLU B 1 238 ? -27.155 33.687  -33.255 1.00 44.97 ? 238 GLU A CD  1 
ATOM   3957 O  OE1 . GLU B 1 238 ? -26.641 32.882  -32.409 1.00 35.06 ? 238 GLU A OE1 1 
ATOM   3958 O  OE2 . GLU B 1 238 ? -26.664 34.839  -33.456 1.00 39.79 ? 238 GLU A OE2 1 
ATOM   3959 N  N   . ALA B 1 239 ? -29.405 32.402  -37.273 1.00 39.63 ? 239 ALA A N   1 
ATOM   3960 C  CA  . ALA B 1 239 ? -28.928 32.587  -38.677 1.00 39.62 ? 239 ALA A CA  1 
ATOM   3961 C  C   . ALA B 1 239 ? -27.391 32.390  -38.814 1.00 35.05 ? 239 ALA A C   1 
ATOM   3962 O  O   . ALA B 1 239 ? -26.643 33.120  -38.182 1.00 43.66 ? 239 ALA A O   1 
ATOM   3963 C  CB  . ALA B 1 239 ? -29.324 33.974  -39.198 1.00 39.07 ? 239 ALA A CB  1 
ATOM   3964 N  N   . ALA B 1 240 ? -26.962 31.430  -39.631 1.00 31.59 ? 240 ALA A N   1 
ATOM   3965 C  CA  . ALA B 1 240 ? -25.532 30.985  -39.705 1.00 27.77 ? 240 ALA A CA  1 
ATOM   3966 C  C   . ALA B 1 240 ? -24.518 32.039  -40.201 1.00 25.71 ? 240 ALA A C   1 
ATOM   3967 O  O   . ALA B 1 240 ? -24.683 32.656  -41.262 1.00 23.91 ? 240 ALA A O   1 
ATOM   3968 C  CB  . ALA B 1 240 ? -25.400 29.724  -40.539 1.00 30.24 ? 240 ALA A CB  1 
ATOM   3969 N  N   . ALA B 1 241 ? -23.428 32.209  -39.446 1.00 20.51 ? 241 ALA A N   1 
ATOM   3970 C  CA  . ALA B 1 241 ? -22.372 33.122  -39.890 1.00 17.46 ? 241 ALA A CA  1 
ATOM   3971 C  C   . ALA B 1 241 ? -21.069 32.532  -39.398 1.00 16.34 ? 241 ALA A C   1 
ATOM   3972 O  O   . ALA B 1 241 ? -21.016 31.898  -38.328 1.00 15.80 ? 241 ALA A O   1 
ATOM   3973 C  CB  . ALA B 1 241 ? -22.613 34.514  -39.379 1.00 15.86 ? 241 ALA A CB  1 
ATOM   3974 N  N   . PHE B 1 242 ? -20.075 32.626  -40.266 1.00 14.88 ? 242 PHE A N   1 
ATOM   3975 C  CA  . PHE B 1 242 ? -18.806 31.951  -40.024 1.00 14.95 ? 242 PHE A CA  1 
ATOM   3976 C  C   . PHE B 1 242 ? -17.793 32.776  -39.280 1.00 14.49 ? 242 PHE A C   1 
ATOM   3977 O  O   . PHE B 1 242 ? -17.694 33.998  -39.482 1.00 16.27 ? 242 PHE A O   1 
ATOM   3978 C  CB  . PHE B 1 242 ? -18.163 31.527  -41.354 1.00 14.90 ? 242 PHE A CB  1 
ATOM   3979 C  CG  . PHE B 1 242 ? -18.991 30.573  -42.101 1.00 17.31 ? 242 PHE A CG  1 
ATOM   3980 C  CD1 . PHE B 1 242 ? -19.938 31.037  -43.028 1.00 19.73 ? 242 PHE A CD1 1 
ATOM   3981 C  CD2 . PHE B 1 242 ? -18.817 29.200  -41.915 1.00 18.56 ? 242 PHE A CD2 1 
ATOM   3982 C  CE1 . PHE B 1 242 ? -20.737 30.106  -43.724 1.00 22.69 ? 242 PHE A CE1 1 
ATOM   3983 C  CE2 . PHE B 1 242 ? -19.598 28.269  -42.622 1.00 21.44 ? 242 PHE A CE2 1 
ATOM   3984 C  CZ  . PHE B 1 242 ? -20.579 28.736  -43.509 1.00 21.18 ? 242 PHE A CZ  1 
ATOM   3985 N  N   . LEU B 1 243 ? -16.963 32.061  -38.501 1.00 13.26 ? 243 LEU A N   1 
ATOM   3986 C  CA  . LEU B 1 243 ? -15.822 32.676  -37.801 1.00 13.38 ? 243 LEU A CA  1 
ATOM   3987 C  C   . LEU B 1 243 ? -14.594 32.681  -38.743 1.00 12.67 ? 243 LEU A C   1 
ATOM   3988 O  O   . LEU B 1 243 ? -13.597 31.964  -38.501 1.00 11.76 ? 243 LEU A O   1 
ATOM   3989 C  CB  . LEU B 1 243 ? -15.505 31.883  -36.504 1.00 13.80 ? 243 LEU A CB  1 
ATOM   3990 C  CG  . LEU B 1 243 ? -14.695 32.528  -35.360 1.00 16.64 ? 243 LEU A CG  1 
ATOM   3991 C  CD1 . LEU B 1 243 ? -15.327 33.858  -34.996 1.00 14.13 ? 243 LEU A CD1 1 
ATOM   3992 C  CD2 . LEU B 1 243 ? -14.876 31.613  -34.152 1.00 16.60 ? 243 LEU A CD2 1 
ATOM   3993 N  N   . VAL B 1 244 ? -14.663 33.440  -39.858 1.00 10.85 ? 244 VAL A N   1 
ATOM   3994 C  CA  . VAL B 1 244 ? -13.529 33.346  -40.785 1.00 11.92 ? 244 VAL A CA  1 
ATOM   3995 C  C   . VAL B 1 244 ? -12.340 34.172  -40.252 1.00 11.02 ? 244 VAL A C   1 
ATOM   3996 O  O   . VAL B 1 244 ? -11.236 34.000  -40.709 1.00 12.62 ? 244 VAL A O   1 
ATOM   3997 C  CB  . VAL B 1 244 ? -13.855 33.784  -42.260 1.00 13.46 ? 244 VAL A CB  1 
ATOM   3998 C  CG1 . VAL B 1 244 ? -14.872 32.803  -42.831 1.00 15.95 ? 244 VAL A CG1 1 
ATOM   3999 C  CG2 . VAL B 1 244 ? -14.391 35.184  -42.281 1.00 15.58 ? 244 VAL A CG2 1 
ATOM   4000 N  N   . SER B 1 245 ? -12.593 35.095  -39.310 1.00 11.33 ? 245 SER A N   1 
ATOM   4001 C  CA  . SER B 1 245 ? -11.496 35.938  -38.750 1.00 10.42 ? 245 SER A CA  1 
ATOM   4002 C  C   . SER B 1 245 ? -11.874 36.309  -37.313 1.00 9.51  ? 245 SER A C   1 
ATOM   4003 O  O   . SER B 1 245 ? -13.037 36.638  -37.000 1.00 10.51 ? 245 SER A O   1 
ATOM   4004 C  CB  . SER B 1 245 ? -11.258 37.174  -39.653 1.00 10.99 ? 245 SER A CB  1 
ATOM   4005 O  OG  . SER B 1 245 ? -10.143 37.913  -39.192 1.00 11.84 ? 245 SER A OG  1 
ATOM   4006 N  N   . ASN B 1 246 ? -10.892 36.287  -36.409 1.00 9.64  ? 246 ASN A N   1 
ATOM   4007 C  CA  . ASN B 1 246 ? -11.170 36.568  -35.011 1.00 9.33  ? 246 ASN A CA  1 
ATOM   4008 C  C   . ASN B 1 246 ? -9.897  37.159  -34.320 1.00 9.97  ? 246 ASN A C   1 
ATOM   4009 O  O   . ASN B 1 246 ? -9.573  36.792  -33.216 1.00 10.43 ? 246 ASN A O   1 
ATOM   4010 C  CB  . ASN B 1 246 ? -11.708 35.258  -34.354 1.00 9.68  ? 246 ASN A CB  1 
ATOM   4011 C  CG  . ASN B 1 246 ? -10.663 34.149  -34.314 1.00 11.35 ? 246 ASN A CG  1 
ATOM   4012 O  OD1 . ASN B 1 246 ? -9.595  34.251  -34.944 1.00 11.54 ? 246 ASN A OD1 1 
ATOM   4013 N  ND2 . ASN B 1 246 ? -10.965 33.068  -33.609 1.00 10.39 ? 246 ASN A ND2 1 
ATOM   4014 N  N   . HIS B 1 247 ? -9.174  38.023  -35.020 1.00 9.74  ? 247 HIS A N   1 
ATOM   4015 C  CA  . HIS B 1 247 ? -7.955  38.683  -34.434 1.00 10.25 ? 247 HIS A CA  1 
ATOM   4016 C  C   . HIS B 1 247 ? -8.167  40.192  -34.245 1.00 11.02 ? 247 HIS A C   1 
ATOM   4017 O  O   . HIS B 1 247 ? -8.732  40.879  -35.122 1.00 12.89 ? 247 HIS A O   1 
ATOM   4018 C  CB  . HIS B 1 247 ? -6.665  38.401  -35.232 1.00 10.56 ? 247 HIS A CB  1 
ATOM   4019 C  CG  . HIS B 1 247 ? -6.714  38.875  -36.652 1.00 10.83 ? 247 HIS A CG  1 
ATOM   4020 N  ND1 . HIS B 1 247 ? -6.063  40.025  -37.084 1.00 12.61 ? 247 HIS A ND1 1 
ATOM   4021 C  CD2 . HIS B 1 247 ? -7.442  38.436  -37.697 1.00 11.48 ? 247 HIS A CD2 1 
ATOM   4022 C  CE1 . HIS B 1 247 ? -6.328  40.216  -38.371 1.00 12.61 ? 247 HIS A CE1 1 
ATOM   4023 N  NE2 . HIS B 1 247 ? -7.137  39.249  -38.777 1.00 12.79 ? 247 HIS A NE2 1 
ATOM   4024 N  N   . ARG B 1 248 ? -7.671  40.720  -33.127 1.00 9.94  ? 248 ARG A N   1 
ATOM   4025 C  CA  . ARG B 1 248 ? -7.724  42.175  -32.922 1.00 10.93 ? 248 ARG A CA  1 
ATOM   4026 C  C   . ARG B 1 248 ? -6.445  42.773  -33.493 1.00 10.36 ? 248 ARG A C   1 
ATOM   4027 O  O   . ARG B 1 248 ? -5.408  42.159  -33.351 1.00 12.29 ? 248 ARG A O   1 
ATOM   4028 C  CB  . ARG B 1 248 ? -7.841  42.464  -31.438 1.00 10.15 ? 248 ARG A CB  1 
ATOM   4029 C  CG  . ARG B 1 248 ? -7.890  43.963  -31.109 1.00 9.69  ? 248 ARG A CG  1 
ATOM   4030 C  CD  . ARG B 1 248 ? -7.824  44.205  -29.615 1.00 9.71  ? 248 ARG A CD  1 
ATOM   4031 N  NE  . ARG B 1 248 ? -8.329  45.564  -29.389 1.00 10.38 ? 248 ARG A NE  1 
ATOM   4032 C  CZ  . ARG B 1 248 ? -8.116  46.306  -28.322 1.00 10.84 ? 248 ARG A CZ  1 
ATOM   4033 N  NH1 . ARG B 1 248 ? -7.249  45.890  -27.391 1.00 9.30  ? 248 ARG A NH1 1 
ATOM   4034 N  NH2 . ARG B 1 248 ? -8.677  47.568  -28.271 1.00 11.74 ? 248 ARG A NH2 1 
ATOM   4035 N  N   . PRO B 1 249 ? -6.509  43.976  -34.127 1.00 11.39 ? 249 PRO A N   1 
ATOM   4036 C  CA  . PRO B 1 249 ? -5.281  44.618  -34.656 1.00 11.34 ? 249 PRO A CA  1 
ATOM   4037 C  C   . PRO B 1 249 ? -4.393  45.070  -33.479 1.00 11.18 ? 249 PRO A C   1 
ATOM   4038 O  O   . PRO B 1 249 ? -4.935  45.320  -32.383 1.00 12.36 ? 249 PRO A O   1 
ATOM   4039 C  CB  . PRO B 1 249 ? -5.801  45.950  -35.307 1.00 12.10 ? 249 PRO A CB  1 
ATOM   4040 C  CG  . PRO B 1 249 ? -7.214  45.627  -35.668 1.00 13.95 ? 249 PRO A CG  1 
ATOM   4041 C  CD  . PRO B 1 249 ? -7.730  44.670  -34.579 1.00 12.48 ? 249 PRO A CD  1 
ATOM   4042 N  N   . PRO B 1 250 ? -3.090  45.132  -33.676 1.00 11.48 ? 250 PRO A N   1 
ATOM   4043 C  CA  . PRO B 1 250 ? -2.196  45.676  -32.657 1.00 11.71 ? 250 PRO A CA  1 
ATOM   4044 C  C   . PRO B 1 250 ? -2.653  47.072  -32.240 1.00 11.29 ? 250 PRO A C   1 
ATOM   4045 O  O   . PRO B 1 250 ? -3.138  47.858  -33.100 1.00 13.57 ? 250 PRO A O   1 
ATOM   4046 C  CB  . PRO B 1 250 ? -0.821  45.677  -33.330 1.00 11.68 ? 250 PRO A CB  1 
ATOM   4047 C  CG  . PRO B 1 250 ? -0.925  44.498  -34.286 1.00 12.55 ? 250 PRO A CG  1 
ATOM   4048 C  CD  . PRO B 1 250 ? -2.343  44.545  -34.808 1.00 13.24 ? 250 PRO A CD  1 
ATOM   4049 N  N   . GLN B 1 251 ? -2.476  47.372  -30.942 1.00 11.02 ? 251 GLN A N   1 
ATOM   4050 C  CA  . GLN B 1 251 ? -2.777  48.669  -30.310 1.00 11.09 ? 251 GLN A CA  1 
ATOM   4051 C  C   . GLN B 1 251 ? -1.462  49.325  -29.929 1.00 10.39 ? 251 GLN A C   1 
ATOM   4052 O  O   . GLN B 1 251 ? -0.502  48.650  -29.781 1.00 10.26 ? 251 GLN A O   1 
ATOM   4053 C  CB  . GLN B 1 251 ? -3.657  48.484  -29.062 1.00 12.07 ? 251 GLN A CB  1 
ATOM   4054 C  CG  . GLN B 1 251 ? -5.002  47.789  -29.419 1.00 12.81 ? 251 GLN A CG  1 
ATOM   4055 C  CD  . GLN B 1 251 ? -5.715  48.455  -30.558 1.00 14.96 ? 251 GLN A CD  1 
ATOM   4056 O  OE1 . GLN B 1 251 ? -6.104  47.838  -31.563 1.00 16.29 ? 251 GLN A OE1 1 
ATOM   4057 N  NE2 . GLN B 1 251 ? -5.893  49.736  -30.417 1.00 13.21 ? 251 GLN A NE2 1 
ATOM   4058 N  N   . PRO B 1 252 ? -1.434  50.665  -29.779 1.00 10.48 ? 252 PRO A N   1 
ATOM   4059 C  CA  . PRO B 1 252 ? -0.181  51.378  -29.573 1.00 10.89 ? 252 PRO A CA  1 
ATOM   4060 C  C   . PRO B 1 252 ? 0.478   51.044  -28.229 1.00 11.05 ? 252 PRO A C   1 
ATOM   4061 O  O   . PRO B 1 252 ? -0.180  50.819  -27.230 1.00 10.13 ? 252 PRO A O   1 
ATOM   4062 C  CB  . PRO B 1 252 ? -0.614  52.872  -29.592 1.00 12.13 ? 252 PRO A CB  1 
ATOM   4063 C  CG  . PRO B 1 252 ? -2.017  52.864  -30.287 1.00 12.59 ? 252 PRO A CG  1 
ATOM   4064 C  CD  . PRO B 1 252 ? -2.619  51.526  -29.965 1.00 11.60 ? 252 PRO A CD  1 
ATOM   4065 N  N   . LEU B 1 253 ? 1.786   51.043  -28.213 1.00 11.54 ? 253 LEU A N   1 
ATOM   4066 C  CA  . LEU B 1 253 ? 2.555   50.672  -26.990 1.00 11.74 ? 253 LEU A CA  1 
ATOM   4067 C  C   . LEU B 1 253 ? 2.395   51.690  -25.866 1.00 12.26 ? 253 LEU A C   1 
ATOM   4068 O  O   . LEU B 1 253 ? 2.395   51.355  -24.678 1.00 10.65 ? 253 LEU A O   1 
ATOM   4069 C  CB  . LEU B 1 253 ? 4.029   50.612  -27.333 1.00 15.01 ? 253 LEU A CB  1 
ATOM   4070 C  CG  . LEU B 1 253 ? 4.692   49.270  -27.535 1.00 21.12 ? 253 LEU A CG  1 
ATOM   4071 C  CD1 . LEU B 1 253 ? 6.190   49.581  -27.702 1.00 23.45 ? 253 LEU A CD1 1 
ATOM   4072 C  CD2 . LEU B 1 253 ? 4.347   48.193  -26.468 1.00 17.02 ? 253 LEU A CD2 1 
ATOM   4073 N  N   A LYS B 1 254 ? 2.238   52.962  -26.247 0.50 10.77 ? 254 LYS A N   1 
ATOM   4074 N  N   B LYS B 1 254 ? 2.254   52.952  -26.286 0.50 10.97 ? 254 LYS A N   1 
ATOM   4075 C  CA  A LYS B 1 254 ? 2.025   54.040  -25.274 0.50 10.89 ? 254 LYS A CA  1 
ATOM   4076 C  CA  B LYS B 1 254 ? 2.058   54.076  -25.384 0.50 11.29 ? 254 LYS A CA  1 
ATOM   4077 C  C   A LYS B 1 254 ? 3.088   54.115  -24.190 0.50 11.10 ? 254 LYS A C   1 
ATOM   4078 C  C   B LYS B 1 254 ? 3.068   54.127  -24.234 0.50 11.36 ? 254 LYS A C   1 
ATOM   4079 O  O   A LYS B 1 254 ? 2.775   54.344  -23.046 0.50 11.98 ? 254 LYS A O   1 
ATOM   4080 O  O   B LYS B 1 254 ? 2.697   54.343  -23.099 0.50 12.22 ? 254 LYS A O   1 
ATOM   4081 C  CB  A LYS B 1 254 ? 0.621   53.995  -24.678 0.50 10.09 ? 254 LYS A CB  1 
ATOM   4082 C  CB  B LYS B 1 254 ? 0.594   54.192  -24.934 0.50 10.72 ? 254 LYS A CB  1 
ATOM   4083 C  CG  A LYS B 1 254 ? -0.404  54.247  -25.769 0.50 10.65 ? 254 LYS A CG  1 
ATOM   4084 C  CG  B LYS B 1 254 ? -0.346  54.422  -26.148 0.50 11.11 ? 254 LYS A CG  1 
ATOM   4085 C  CD  A LYS B 1 254 ? -1.801  54.244  -25.264 0.50 9.96  ? 254 LYS A CD  1 
ATOM   4086 C  CD  B LYS B 1 254 ? -1.248  55.629  -25.984 0.50 10.96 ? 254 LYS A CD  1 
ATOM   4087 C  CE  A LYS B 1 254 ? -2.660  54.815  -26.415 0.50 10.91 ? 254 LYS A CE  1 
ATOM   4088 C  CE  B LYS B 1 254 ? -2.260  55.816  -27.120 0.50 11.41 ? 254 LYS A CE  1 
ATOM   4089 N  NZ  A LYS B 1 254 ? -4.075  54.835  -25.963 0.50 10.45 ? 254 LYS A NZ  1 
ATOM   4090 N  NZ  B LYS B 1 254 ? -1.976  57.052  -27.943 0.50 11.18 ? 254 LYS A NZ  1 
ATOM   4091 N  N   . GLY B 1 255 ? 4.341   53.947  -24.563 1.00 11.61 ? 255 GLY A N   1 
ATOM   4092 C  CA  . GLY B 1 255 ? 5.432   54.069  -23.521 1.00 12.47 ? 255 GLY A CA  1 
ATOM   4093 C  C   . GLY B 1 255 ? 5.825   52.766  -22.891 1.00 12.86 ? 255 GLY A C   1 
ATOM   4094 O  O   . GLY B 1 255 ? 6.885   52.690  -22.224 1.00 14.32 ? 255 GLY A O   1 
ATOM   4095 N  N   . ARG B 1 256 ? 5.029   51.704  -23.055 1.00 11.82 ? 256 ARG A N   1 
ATOM   4096 C  CA  . ARG B 1 256 ? 5.480   50.384  -22.510 1.00 11.67 ? 256 ARG A CA  1 
ATOM   4097 C  C   . ARG B 1 256 ? 6.803   49.887  -23.120 1.00 12.14 ? 256 ARG A C   1 
ATOM   4098 O  O   . ARG B 1 256 ? 7.081   50.128  -24.308 1.00 12.90 ? 256 ARG A O   1 
ATOM   4099 C  CB  . ARG B 1 256 ? 4.399   49.305  -22.723 1.00 10.65 ? 256 ARG A CB  1 
ATOM   4100 C  CG  . ARG B 1 256 ? 3.177   49.525  -21.841 1.00 10.47 ? 256 ARG A CG  1 
ATOM   4101 C  CD  . ARG B 1 256 ? 2.044   48.581  -22.253 1.00 9.22  ? 256 ARG A CD  1 
ATOM   4102 N  NE  . ARG B 1 256 ? 1.447   48.944  -23.521 1.00 8.95  ? 256 ARG A NE  1 
ATOM   4103 C  CZ  . ARG B 1 256 ? 0.575   48.163  -24.162 1.00 10.32 ? 256 ARG A CZ  1 
ATOM   4104 N  NH1 . ARG B 1 256 ? 0.228   46.942  -23.706 1.00 9.49  ? 256 ARG A NH1 1 
ATOM   4105 N  NH2 . ARG B 1 256 ? 0.052   48.599  -25.307 1.00 8.92  ? 256 ARG A NH2 1 
ATOM   4106 N  N   . LYS B 1 257 ? 7.573   49.147  -22.312 1.00 13.88 ? 257 LYS A N   1 
ATOM   4107 C  CA  . LYS B 1 257 ? 8.766   48.490  -22.809 1.00 15.04 ? 257 LYS A CA  1 
ATOM   4108 C  C   . LYS B 1 257 ? 8.593   46.986  -22.937 1.00 13.13 ? 257 LYS A C   1 
ATOM   4109 O  O   . LYS B 1 257 ? 8.019   46.312  -22.063 1.00 13.24 ? 257 LYS A O   1 
ATOM   4110 C  CB  . LYS B 1 257 ? 9.970   48.811  -21.895 1.00 18.01 ? 257 LYS A CB  1 
ATOM   4111 C  CG  . LYS B 1 257 ? 10.391  50.308  -22.067 1.00 23.57 ? 257 LYS A CG  1 
ATOM   4112 C  CD  . LYS B 1 257 ? 11.499  50.706  -21.117 1.00 29.17 ? 257 LYS A CD  1 
ATOM   4113 C  CE  . LYS B 1 257 ? 11.948  52.115  -21.461 1.00 34.79 ? 257 LYS A CE  1 
ATOM   4114 N  NZ  . LYS B 1 257 ? 12.222  52.801  -20.179 1.00 40.36 ? 257 LYS A NZ  1 
ATOM   4115 N  N   . VAL B 1 258 ? 9.007   46.503  -24.087 1.00 11.81 ? 258 VAL A N   1 
ATOM   4116 C  CA  . VAL B 1 258 ? 9.000   45.075  -24.311 1.00 10.57 ? 258 VAL A CA  1 
ATOM   4117 C  C   . VAL B 1 258 ? 10.379  44.528  -23.984 1.00 10.81 ? 258 VAL A C   1 
ATOM   4118 O  O   . VAL B 1 258 ? 11.383  45.088  -24.436 1.00 13.45 ? 258 VAL A O   1 
ATOM   4119 C  CB  . VAL B 1 258 ? 8.633   44.768  -25.779 1.00 10.04 ? 258 VAL A CB  1 
ATOM   4120 C  CG1 . VAL B 1 258 ? 8.582   43.250  -26.011 1.00 10.65 ? 258 VAL A CG1 1 
ATOM   4121 C  CG2 . VAL B 1 258 ? 7.323   45.474  -26.158 1.00 10.43 ? 258 VAL A CG2 1 
ATOM   4122 N  N   . ARG B 1 259 ? 10.455  43.420  -23.252 1.00 9.99  ? 259 ARG A N   1 
ATOM   4123 C  CA  . ARG B 1 259 ? 11.756  42.896  -22.834 1.00 9.72  ? 259 ARG A CA  1 
ATOM   4124 C  C   . ARG B 1 259 ? 11.940  41.545  -23.518 1.00 9.96  ? 259 ARG A C   1 
ATOM   4125 O  O   . ARG B 1 259 ? 10.970  40.853  -23.791 1.00 10.72 ? 259 ARG A O   1 
ATOM   4126 C  CB  . ARG B 1 259 ? 11.730  42.665  -21.326 1.00 11.11 ? 259 ARG A CB  1 
ATOM   4127 C  CG  . ARG B 1 259 ? 11.723  44.026  -20.553 1.00 12.16 ? 259 ARG A CG  1 
ATOM   4128 C  CD  . ARG B 1 259 ? 11.625  43.747  -19.068 1.00 13.72 ? 259 ARG A CD  1 
ATOM   4129 N  NE  . ARG B 1 259 ? 10.386  43.140  -18.628 1.00 12.73 ? 259 ARG A NE  1 
ATOM   4130 C  CZ  . ARG B 1 259 ? 10.253  42.432  -17.513 1.00 13.21 ? 259 ARG A CZ  1 
ATOM   4131 N  NH1 . ARG B 1 259 ? 11.315  42.173  -16.726 1.00 13.91 ? 259 ARG A NH1 1 
ATOM   4132 N  NH2 . ARG B 1 259 ? 9.071   41.957  -17.177 1.00 14.37 ? 259 ARG A NH2 1 
ATOM   4133 N  N   . ALA B 1 260 ? 13.186  41.169  -23.753 1.00 9.86  ? 260 ALA A N   1 
ATOM   4134 C  CA  . ALA B 1 260 ? 13.509  39.856  -24.320 1.00 10.28 ? 260 ALA A CA  1 
ATOM   4135 C  C   . ALA B 1 260 ? 14.145  38.959  -23.300 1.00 10.36 ? 260 ALA A C   1 
ATOM   4136 O  O   . ALA B 1 260 ? 14.975  39.402  -22.482 1.00 10.74 ? 260 ALA A O   1 
ATOM   4137 C  CB  . ALA B 1 260 ? 14.479  40.040  -25.478 1.00 11.70 ? 260 ALA A CB  1 
ATOM   4138 N  N   . SER B 1 261 ? 13.866  37.670  -23.434 1.00 10.31 ? 261 SER A N   1 
ATOM   4139 C  CA  . SER B 1 261 ? 14.411  36.690  -22.556 1.00 10.01 ? 261 SER A CA  1 
ATOM   4140 C  C   . SER B 1 261 ? 15.778  36.200  -23.086 1.00 11.17 ? 261 SER A C   1 
ATOM   4141 O  O   . SER B 1 261 ? 16.470  35.285  -22.475 1.00 12.56 ? 261 SER A O   1 
ATOM   4142 C  CB  . SER B 1 261 ? 13.449  35.488  -22.512 1.00 10.14 ? 261 SER A CB  1 
ATOM   4143 O  OG  . SER B 1 261 ? 13.578  34.674  -23.667 1.00 9.58  ? 261 SER A OG  1 
ATOM   4144 N  N   . PHE B 1 262 ? 16.156  36.720  -24.256 1.00 11.73 ? 262 PHE A N   1 
ATOM   4145 C  CA  . PHE B 1 262 ? 17.283  36.148  -24.976 1.00 13.89 ? 262 PHE A CA  1 
ATOM   4146 C  C   . PHE B 1 262 ? 18.094  37.299  -25.559 1.00 15.25 ? 262 PHE A C   1 
ATOM   4147 O  O   . PHE B 1 262 ? 17.583  38.423  -25.724 1.00 15.75 ? 262 PHE A O   1 
ATOM   4148 C  CB  . PHE B 1 262 ? 16.789  35.240  -26.146 1.00 12.50 ? 262 PHE A CB  1 
ATOM   4149 C  CG  . PHE B 1 262 ? 15.876  35.953  -27.108 1.00 13.15 ? 262 PHE A CG  1 
ATOM   4150 C  CD1 . PHE B 1 262 ? 14.500  36.133  -26.846 1.00 13.09 ? 262 PHE A CD1 1 
ATOM   4151 C  CD2 . PHE B 1 262 ? 16.406  36.525  -28.287 1.00 14.50 ? 262 PHE A CD2 1 
ATOM   4152 C  CE1 . PHE B 1 262 ? 13.692  36.832  -27.774 1.00 13.32 ? 262 PHE A CE1 1 
ATOM   4153 C  CE2 . PHE B 1 262 ? 15.598  37.245  -29.189 1.00 15.67 ? 262 PHE A CE2 1 
ATOM   4154 C  CZ  . PHE B 1 262 ? 14.230  37.436  -28.918 1.00 14.77 ? 262 PHE A CZ  1 
ATOM   4155 N  N   . HIS B 1 263 ? 19.363  37.038  -25.864 1.00 19.93 ? 263 HIS A N   1 
ATOM   4156 C  CA  . HIS B 1 263 ? 20.112  38.062  -26.587 1.00 28.45 ? 263 HIS A CA  1 
ATOM   4157 C  C   . HIS B 1 263 ? 20.796  37.459  -27.756 1.00 38.28 ? 263 HIS A C   1 
ATOM   4158 O  O   . HIS B 1 263 ? 21.522  36.467  -27.599 1.00 39.02 ? 263 HIS A O   1 
ATOM   4159 C  CB  . HIS B 1 263 ? 21.082  38.934  -25.793 1.00 30.78 ? 263 HIS A CB  1 
ATOM   4160 C  CG  . HIS B 1 263 ? 21.822  38.278  -24.680 1.00 33.68 ? 263 HIS A CG  1 
ATOM   4161 N  ND1 . HIS B 1 263 ? 22.626  39.024  -23.839 1.00 40.61 ? 263 HIS A ND1 1 
ATOM   4162 C  CD2 . HIS B 1 263 ? 21.900  37.003  -24.237 1.00 37.82 ? 263 HIS A CD2 1 
ATOM   4163 C  CE1 . HIS B 1 263 ? 23.171  38.232  -22.930 1.00 40.94 ? 263 HIS A CE1 1 
ATOM   4164 N  NE2 . HIS B 1 263 ? 22.741  37.003  -23.145 1.00 39.12 ? 263 HIS A NE2 1 
ATOM   4165 O  OXT . HIS B 1 263 ? 20.577  37.973  -28.854 1.00 50.67 ? 263 HIS A OXT 1 
HETATM 4166 ZN ZN  . ZN  C 2 .   ? 20.479  3.901   -13.268 1.00 9.77  ? 301 ZN  B ZN  1 
HETATM 4167 C  C5  . ENN D 3 .   ? 20.471  1.268   -16.398 1.00 13.81 ? 302 ENN B C5  1 
HETATM 4168 C  C4  . ENN D 3 .   ? 19.942  0.141   -17.021 1.00 16.56 ? 302 ENN B C4  1 
HETATM 4169 C  C6  . ENN D 3 .   ? 20.746  2.398   -17.081 1.00 12.82 ? 302 ENN B C6  1 
HETATM 4170 C  C2  . ENN D 3 .   ? 20.077  1.325   -19.116 1.00 16.78 ? 302 ENN B C2  1 
HETATM 4171 O  O14 . ENN D 3 .   ? 18.875  -0.817  -15.155 1.00 20.19 ? 302 ENN B O14 1 
HETATM 4172 C  C13 . ENN D 3 .   ? 19.599  -1.008  -16.157 1.00 18.88 ? 302 ENN B C13 1 
HETATM 4173 N  N15 . ENN D 3 .   ? 19.998  -2.222  -16.484 1.00 22.70 ? 302 ENN B N15 1 
HETATM 4174 C  C16 . ENN D 3 .   ? 19.665  -3.348  -15.590 1.00 26.23 ? 302 ENN B C16 1 
HETATM 4175 C  C17 . ENN D 3 .   ? 20.063  -4.658  -16.220 1.00 38.46 ? 302 ENN B C17 1 
HETATM 4176 C  C18 . ENN D 3 .   ? 18.877  -5.215  -16.992 1.00 43.40 ? 302 ENN B C18 1 
HETATM 4177 C  C19 . ENN D 3 .   ? 17.859  -5.852  -16.050 1.00 42.92 ? 302 ENN B C19 1 
HETATM 4178 C  C3  . ENN D 3 .   ? 19.785  0.176   -18.387 1.00 18.56 ? 302 ENN B C3  1 
HETATM 4179 CL CL1 . ENN D 3 .   ? 19.152  -1.188  -19.318 1.00 32.32 ? 302 ENN B CL1 1 
HETATM 4180 C  C1  . ENN D 3 .   ? 20.573  2.434   -18.476 1.00 13.86 ? 302 ENN B C1  1 
HETATM 4181 CL CL2 . ENN D 3 .   ? 20.919  3.879   -19.374 1.00 15.03 ? 302 ENN B CL2 1 
HETATM 4182 S  S7  . ENN D 3 .   ? 21.373  3.807   -16.118 1.00 12.17 ? 302 ENN B S7  1 
HETATM 4183 O  O9  . ENN D 3 .   ? 22.582  4.275   -16.826 1.00 11.02 ? 302 ENN B O9  1 
HETATM 4184 O  O10 . ENN D 3 .   ? 20.325  4.833   -16.078 1.00 12.35 ? 302 ENN B O10 1 
HETATM 4185 N  N8  . ENN D 3 .   ? 21.798  3.520   -14.543 1.00 10.56 ? 302 ENN B N8  1 
HETATM 4186 C  C1  . EDO E 4 .   ? -3.839  4.819   -17.114 1.00 33.94 ? 303 EDO B C1  1 
HETATM 4187 O  O1  . EDO E 4 .   ? -3.853  3.347   -17.111 1.00 40.14 ? 303 EDO B O1  1 
HETATM 4188 C  C2  . EDO E 4 .   ? -4.661  5.203   -18.358 1.00 37.58 ? 303 EDO B C2  1 
HETATM 4189 O  O2  . EDO E 4 .   ? -4.708  6.609   -18.599 1.00 45.64 ? 303 EDO B O2  1 
HETATM 4190 C  C1  . EDO F 4 .   ? 24.301  -9.109  1.648   1.00 25.24 ? 304 EDO B C1  1 
HETATM 4191 O  O1  . EDO F 4 .   ? 23.135  -9.303  2.500   1.00 18.41 ? 304 EDO B O1  1 
HETATM 4192 C  C2  . EDO F 4 .   ? 24.319  -7.764  0.880   1.00 29.05 ? 304 EDO B C2  1 
HETATM 4193 O  O2  . EDO F 4 .   ? 24.445  -7.898  -0.579  1.00 31.81 ? 304 EDO B O2  1 
HETATM 4194 ZN ZN  . ZN  G 2 .   ? -6.532  35.169  -27.330 1.00 8.53  ? 301 ZN  A ZN  1 
HETATM 4195 C  C5  . ENN H 3 .   ? -9.115  35.585  -24.251 1.00 11.69 ? 302 ENN A C5  1 
HETATM 4196 C  C4  . ENN H 3 .   ? -10.228 35.185  -23.531 1.00 15.28 ? 302 ENN A C4  1 
HETATM 4197 C  C6  . ENN H 3 .   ? -8.002  36.076  -23.574 1.00 10.46 ? 302 ENN A C6  1 
HETATM 4198 C  C2  . ENN H 3 .   ? -9.010  35.660  -21.460 1.00 14.44 ? 302 ENN A C2  1 
HETATM 4199 O  O14 . ENN H 3 .   ? -11.181 33.686  -25.042 1.00 20.63 ? 302 ENN A O14 1 
HETATM 4200 C  C13 . ENN H 3 .   ? -11.413 34.647  -24.260 1.00 19.30 ? 302 ENN A C13 1 
HETATM 4201 N  N15 . ENN H 3 .   ? -12.645 35.113  -24.011 1.00 22.48 ? 302 ENN A N15 1 
HETATM 4202 C  C16 . ENN H 3 .   ? -13.811 34.587  -24.685 1.00 28.90 ? 302 ENN A C16 1 
HETATM 4203 C  C17 . ENN H 3 .   ? -14.638 33.789  -23.692 1.00 34.82 ? 302 ENN A C17 1 
HETATM 4204 C  C18 . ENN H 3 .   ? -15.899 33.477  -24.459 1.00 38.24 ? 302 ENN A C18 1 
HETATM 4205 C  C19 . ENN H 3 .   ? -17.076 34.143  -23.778 1.00 46.60 ? 302 ENN A C19 1 
HETATM 4206 C  C3  . ENN H 3 .   ? -10.159 35.258  -22.157 1.00 15.90 ? 302 ENN A C3  1 
HETATM 4207 CL CL1 . ENN H 3 .   ? -11.553 34.789  -21.189 1.00 28.88 ? 302 ENN A CL1 1 
HETATM 4208 C  C1  . ENN H 3 .   ? -7.915  36.069  -22.187 1.00 12.33 ? 302 ENN A C1  1 
HETATM 4209 CL CL2 . ENN H 3 .   ? -6.531  36.578  -21.341 1.00 12.74 ? 302 ENN A CL2 1 
HETATM 4210 S  S7  . ENN H 3 .   ? -6.613  36.587  -24.604 1.00 10.17 ? 302 ENN A S7  1 
HETATM 4211 O  O9  . ENN H 3 .   ? -6.187  37.948  -24.162 1.00 10.12 ? 302 ENN A O9  1 
HETATM 4212 O  O10 . ENN H 3 .   ? -5.579  35.519  -24.539 1.00 10.16 ? 302 ENN A O10 1 
HETATM 4213 N  N8  . ENN H 3 .   ? -7.046  36.732  -26.229 1.00 8.57  ? 302 ENN A N8  1 
HETATM 4214 C  C1  . EDO I 4 .   ? -2.740  11.400  -22.631 1.00 41.25 ? 303 EDO A C1  1 
HETATM 4215 O  O1  . EDO I 4 .   ? -3.322  10.559  -23.674 1.00 40.32 ? 303 EDO A O1  1 
HETATM 4216 C  C2  . EDO I 4 .   ? -1.238  11.163  -22.406 1.00 45.88 ? 303 EDO A C2  1 
HETATM 4217 O  O2  . EDO I 4 .   ? -1.009  11.165  -20.971 1.00 44.59 ? 303 EDO A O2  1 
HETATM 4218 C  C1  . CIT J 5 .   ? -8.541  44.458  -40.527 1.00 32.89 ? 304 CIT A C1  1 
HETATM 4219 O  O1  . CIT J 5 .   ? -7.470  44.540  -41.163 1.00 34.62 ? 304 CIT A O1  1 
HETATM 4220 O  O2  . CIT J 5 .   ? -8.967  45.459  -39.881 1.00 30.64 ? 304 CIT A O2  1 
HETATM 4221 C  C2  . CIT J 5 .   ? -9.324  43.134  -40.527 1.00 28.10 ? 304 CIT A C2  1 
HETATM 4222 C  C3  . CIT J 5 .   ? -8.649  41.943  -41.267 1.00 25.92 ? 304 CIT A C3  1 
HETATM 4223 O  O7  . CIT J 5 .   ? -7.241  41.890  -40.912 1.00 23.23 ? 304 CIT A O7  1 
HETATM 4224 C  C4  . CIT J 5 .   ? -9.490  40.669  -40.935 1.00 25.30 ? 304 CIT A C4  1 
HETATM 4225 C  C5  . CIT J 5 .   ? -9.058  39.414  -41.719 1.00 23.46 ? 304 CIT A C5  1 
HETATM 4226 O  O3  . CIT J 5 .   ? -9.692  39.011  -42.722 1.00 24.78 ? 304 CIT A O3  1 
HETATM 4227 O  O4  . CIT J 5 .   ? -8.053  38.819  -41.290 1.00 21.79 ? 304 CIT A O4  1 
HETATM 4228 C  C6  . CIT J 5 .   ? -8.707  42.179  -42.760 1.00 29.00 ? 304 CIT A C6  1 
HETATM 4229 O  O5  . CIT J 5 .   ? -7.633  42.028  -43.413 1.00 25.31 ? 304 CIT A O5  1 
HETATM 4230 O  O6  . CIT J 5 .   ? -9.835  42.530  -43.266 1.00 28.93 ? 304 CIT A O6  1 
HETATM 4231 O  O   . HOH K 6 .   ? -0.786  8.985   -24.948 1.00 40.05 ? 401 HOH B O   1 
HETATM 4232 O  O   . HOH K 6 .   ? 0.718   12.365  -18.695 1.00 27.11 ? 402 HOH B O   1 
HETATM 4233 O  O   . HOH K 6 .   ? 35.894  18.883  -17.994 1.00 23.86 ? 403 HOH B O   1 
HETATM 4234 O  O   . HOH K 6 .   ? -0.841  4.886   -33.393 1.00 24.34 ? 404 HOH B O   1 
HETATM 4235 O  O   . HOH K 6 .   ? 41.827  8.638   -20.908 1.00 30.57 ? 405 HOH B O   1 
HETATM 4236 O  O   . HOH K 6 .   ? 32.571  27.076  -3.465  1.00 36.28 ? 406 HOH B O   1 
HETATM 4237 O  O   . HOH K 6 .   ? 7.571   17.169  9.631   1.00 25.00 ? 407 HOH B O   1 
HETATM 4238 O  O   . HOH K 6 .   ? -2.997  5.983   -24.030 1.00 27.20 ? 408 HOH B O   1 
HETATM 4239 O  O   . HOH K 6 .   ? 1.081   16.096  -12.668 1.00 20.42 ? 409 HOH B O   1 
HETATM 4240 O  O   . HOH K 6 .   ? 26.922  24.490  -27.296 1.00 28.67 ? 410 HOH B O   1 
HETATM 4241 O  O   . HOH K 6 .   ? 35.974  3.078   -12.348 1.00 30.66 ? 411 HOH B O   1 
HETATM 4242 O  O   . HOH K 6 .   ? 1.584   1.256   -26.782 1.00 19.65 ? 412 HOH B O   1 
HETATM 4243 O  O   . HOH K 6 .   ? 3.226   16.510  -20.107 1.00 21.11 ? 413 HOH B O   1 
HETATM 4244 O  O   . HOH K 6 .   ? 16.359  25.879  -17.230 1.00 14.01 ? 414 HOH B O   1 
HETATM 4245 O  O   . HOH K 6 .   ? -3.637  7.703   -20.678 1.00 24.42 ? 415 HOH B O   1 
HETATM 4246 O  O   . HOH K 6 .   ? 26.628  8.252   6.644   1.00 21.04 ? 416 HOH B O   1 
HETATM 4247 O  O   . HOH K 6 .   ? 12.349  26.153  -13.039 1.00 30.21 ? 417 HOH B O   1 
HETATM 4248 O  O   . HOH K 6 .   ? 17.203  15.649  4.315   1.00 36.02 ? 418 HOH B O   1 
HETATM 4249 O  O   . HOH K 6 .   ? -2.005  13.605  -12.990 1.00 20.96 ? 419 HOH B O   1 
HETATM 4250 O  O   . HOH K 6 .   ? 22.493  10.048  -26.438 1.00 17.26 ? 420 HOH B O   1 
HETATM 4251 O  O   . HOH K 6 .   ? 20.504  12.563  3.075   1.00 29.83 ? 421 HOH B O   1 
HETATM 4252 O  O   . HOH K 6 .   ? 25.200  1.508   -10.855 1.00 11.98 ? 422 HOH B O   1 
HETATM 4253 O  O   . HOH K 6 .   ? 17.701  26.792  -29.314 1.00 33.36 ? 423 HOH B O   1 
HETATM 4254 O  O   . HOH K 6 .   ? 1.011   -0.348  -5.757  1.00 14.36 ? 424 HOH B O   1 
HETATM 4255 O  O   . HOH K 6 .   ? 21.429  16.905  -29.933 1.00 16.06 ? 425 HOH B O   1 
HETATM 4256 O  O   . HOH K 6 .   ? 3.433   16.220  -8.451  1.00 26.68 ? 426 HOH B O   1 
HETATM 4257 O  O   . HOH K 6 .   ? 0.490   0.896   -29.234 1.00 20.22 ? 427 HOH B O   1 
HETATM 4258 O  O   . HOH K 6 .   ? 17.326  -2.828  -12.438 1.00 23.60 ? 428 HOH B O   1 
HETATM 4259 O  O   . HOH K 6 .   ? -1.554  11.041  -10.240 1.00 15.79 ? 429 HOH B O   1 
HETATM 4260 O  O   . HOH K 6 .   ? 13.943  -2.500  4.840   1.00 26.78 ? 430 HOH B O   1 
HETATM 4261 O  O   . HOH K 6 .   ? 16.956  20.065  -28.082 1.00 15.93 ? 431 HOH B O   1 
HETATM 4262 O  O   . HOH K 6 .   ? 29.314  12.689  -1.429  1.00 19.27 ? 432 HOH B O   1 
HETATM 4263 O  O   . HOH K 6 .   ? 36.153  5.081   -15.422 1.00 21.76 ? 433 HOH B O   1 
HETATM 4264 O  O   . HOH K 6 .   ? 29.287  21.281  -0.788  1.00 23.88 ? 434 HOH B O   1 
HETATM 4265 O  O   . HOH K 6 .   ? 24.308  -3.977  -2.091  1.00 15.15 ? 435 HOH B O   1 
HETATM 4266 O  O   . HOH K 6 .   ? 25.822  23.136  -5.309  1.00 29.84 ? 436 HOH B O   1 
HETATM 4267 O  O   . HOH K 6 .   ? 17.890  12.191  -33.081 1.00 31.01 ? 437 HOH B O   1 
HETATM 4268 O  O   . HOH K 6 .   ? 32.672  7.441   -26.057 1.00 28.90 ? 438 HOH B O   1 
HETATM 4269 O  O   . HOH K 6 .   ? 6.866   16.625  -3.228  1.00 27.93 ? 439 HOH B O   1 
HETATM 4270 O  O   . HOH K 6 .   ? 13.341  -8.629  2.423   1.00 28.45 ? 440 HOH B O   1 
HETATM 4271 O  O   . HOH K 6 .   ? 15.593  23.627  -10.481 1.00 19.43 ? 441 HOH B O   1 
HETATM 4272 O  O   . HOH K 6 .   ? 39.933  5.943   -21.022 1.00 45.59 ? 442 HOH B O   1 
HETATM 4273 O  O   . HOH K 6 .   ? 9.872   -4.854  -15.046 1.00 19.66 ? 443 HOH B O   1 
HETATM 4274 O  O   . HOH K 6 .   ? 17.363  -15.550 -2.353  1.00 23.30 ? 444 HOH B O   1 
HETATM 4275 O  O   . HOH K 6 .   ? 25.428  12.808  -25.332 1.00 15.33 ? 445 HOH B O   1 
HETATM 4276 O  O   . HOH K 6 .   ? 26.752  0.457   -4.081  1.00 12.79 ? 446 HOH B O   1 
HETATM 4277 O  O   . HOH K 6 .   ? 38.607  -1.031  -11.111 1.00 41.39 ? 447 HOH B O   1 
HETATM 4278 O  O   . HOH K 6 .   ? 15.373  20.798  -30.102 1.00 25.56 ? 448 HOH B O   1 
HETATM 4279 O  O   . HOH K 6 .   ? 13.520  -2.709  -20.474 1.00 31.32 ? 449 HOH B O   1 
HETATM 4280 O  O   . HOH K 6 .   ? 14.093  13.652  -35.433 1.00 19.13 ? 450 HOH B O   1 
HETATM 4281 O  O   . HOH K 6 .   ? 2.674   10.303  -16.214 1.00 12.14 ? 451 HOH B O   1 
HETATM 4282 O  O   . HOH K 6 .   ? -0.586  12.609  -16.117 1.00 19.01 ? 452 HOH B O   1 
HETATM 4283 O  O   . HOH K 6 .   ? 7.827   -2.747  -24.875 1.00 27.47 ? 453 HOH B O   1 
HETATM 4284 O  O   . HOH K 6 .   ? 29.536  2.877   -4.643  1.00 22.08 ? 454 HOH B O   1 
HETATM 4285 O  O   . HOH K 6 .   ? 24.403  -9.871  -9.044  1.00 19.48 ? 455 HOH B O   1 
HETATM 4286 O  O   . HOH K 6 .   ? 16.176  -4.679  -32.819 1.00 35.15 ? 456 HOH B O   1 
HETATM 4287 O  O   . HOH K 6 .   ? 10.907  14.391  -33.430 1.00 21.83 ? 457 HOH B O   1 
HETATM 4288 O  O   . HOH K 6 .   ? 3.058   3.146   -23.969 1.00 12.42 ? 458 HOH B O   1 
HETATM 4289 O  O   . HOH K 6 .   ? 20.672  1.122   6.074   1.00 13.88 ? 459 HOH B O   1 
HETATM 4290 O  O   . HOH K 6 .   ? 5.564   5.092   -25.622 1.00 11.97 ? 460 HOH B O   1 
HETATM 4291 O  O   . HOH K 6 .   ? 30.486  -2.830  -22.977 1.00 20.38 ? 461 HOH B O   1 
HETATM 4292 O  O   . HOH K 6 .   ? 23.413  -11.829 3.309   1.00 23.46 ? 462 HOH B O   1 
HETATM 4293 O  O   . HOH K 6 .   ? 13.737  -7.135  -14.101 1.00 32.07 ? 463 HOH B O   1 
HETATM 4294 O  O   . HOH K 6 .   ? 4.972   5.322   -6.988  1.00 15.82 ? 464 HOH B O   1 
HETATM 4295 O  O   . HOH K 6 .   ? 19.911  -1.606  -12.823 1.00 28.67 ? 465 HOH B O   1 
HETATM 4296 O  O   . HOH K 6 .   ? 16.460  4.835   5.127   1.00 18.67 ? 466 HOH B O   1 
HETATM 4297 O  O   . HOH K 6 .   ? 10.677  1.188   6.379   1.00 18.70 ? 467 HOH B O   1 
HETATM 4298 O  O   . HOH K 6 .   ? 28.712  9.179   -24.442 1.00 16.42 ? 468 HOH B O   1 
HETATM 4299 O  O   . HOH K 6 .   ? 4.379   0.880   0.934   1.00 20.64 ? 469 HOH B O   1 
HETATM 4300 O  O   . HOH K 6 .   ? 14.417  17.157  -29.119 1.00 14.14 ? 470 HOH B O   1 
HETATM 4301 O  O   . HOH K 6 .   ? 5.274   16.548  -11.078 1.00 28.20 ? 471 HOH B O   1 
HETATM 4302 O  O   . HOH K 6 .   ? 28.630  29.331  -17.410 1.00 29.02 ? 472 HOH B O   1 
HETATM 4303 O  O   . HOH K 6 .   ? 4.008   11.509  -29.024 1.00 27.43 ? 473 HOH B O   1 
HETATM 4304 O  O   . HOH K 6 .   ? 15.225  17.952  -32.835 1.00 19.59 ? 474 HOH B O   1 
HETATM 4305 O  O   . HOH K 6 .   ? 0.082   9.549   -8.743  1.00 22.08 ? 475 HOH B O   1 
HETATM 4306 O  O   . HOH K 6 .   ? 5.421   4.811   0.753   1.00 17.89 ? 476 HOH B O   1 
HETATM 4307 O  O   . HOH K 6 .   ? 35.291  7.357   -7.560  1.00 26.15 ? 477 HOH B O   1 
HETATM 4308 O  O   . HOH K 6 .   ? 7.495   12.568  -30.241 1.00 20.85 ? 478 HOH B O   1 
HETATM 4309 O  O   . HOH K 6 .   ? 22.871  0.168   -33.401 1.00 27.41 ? 479 HOH B O   1 
HETATM 4310 O  O   . HOH K 6 .   ? 7.414   20.704  -26.799 1.00 16.88 ? 480 HOH B O   1 
HETATM 4311 O  O   . HOH K 6 .   ? 18.571  27.009  -9.967  1.00 42.71 ? 481 HOH B O   1 
HETATM 4312 O  O   . HOH K 6 .   ? 6.076   2.708   -33.353 1.00 15.80 ? 482 HOH B O   1 
HETATM 4313 O  O   . HOH K 6 .   ? 1.310   -3.214  -8.940  1.00 18.71 ? 483 HOH B O   1 
HETATM 4314 O  O   . HOH K 6 .   ? -0.091  -0.827  -8.310  1.00 16.65 ? 484 HOH B O   1 
HETATM 4315 O  O   . HOH K 6 .   ? -0.643  1.201   -4.130  1.00 20.25 ? 485 HOH B O   1 
HETATM 4316 O  O   . HOH K 6 .   ? 35.871  5.762   -24.090 1.00 18.06 ? 486 HOH B O   1 
HETATM 4317 O  O   . HOH K 6 .   ? -0.896  -6.230  -10.172 1.00 25.42 ? 487 HOH B O   1 
HETATM 4318 O  O   . HOH K 6 .   ? 2.403   -3.787  -28.771 1.00 13.19 ? 488 HOH B O   1 
HETATM 4319 O  O   . HOH K 6 .   ? 33.668  15.237  -12.360 1.00 27.79 ? 489 HOH B O   1 
HETATM 4320 O  O   . HOH K 6 .   ? 14.186  27.882  -12.007 1.00 33.22 ? 490 HOH B O   1 
HETATM 4321 O  O   . HOH K 6 .   ? 5.505   -11.107 -7.564  1.00 43.25 ? 491 HOH B O   1 
HETATM 4322 O  O   . HOH K 6 .   ? 31.794  24.108  -7.622  1.00 16.25 ? 492 HOH B O   1 
HETATM 4323 O  O   . HOH K 6 .   ? 18.598  13.989  1.986   1.00 25.46 ? 493 HOH B O   1 
HETATM 4324 O  O   . HOH K 6 .   ? 7.224   7.301   5.983   1.00 16.54 ? 494 HOH B O   1 
HETATM 4325 O  O   . HOH K 6 .   ? 33.627  12.616  -11.394 1.00 15.47 ? 495 HOH B O   1 
HETATM 4326 O  O   . HOH K 6 .   ? 4.942   14.573  -3.821  1.00 31.05 ? 496 HOH B O   1 
HETATM 4327 O  O   . HOH K 6 .   ? -2.790  8.363   -13.530 1.00 23.08 ? 497 HOH B O   1 
HETATM 4328 O  O   . HOH K 6 .   ? 32.054  18.603  -12.704 1.00 21.50 ? 498 HOH B O   1 
HETATM 4329 O  O   . HOH K 6 .   ? -1.577  2.550   -0.245  1.00 27.49 ? 499 HOH B O   1 
HETATM 4330 O  O   . HOH K 6 .   ? 22.628  -13.224 -7.242  1.00 27.11 ? 500 HOH B O   1 
HETATM 4331 O  O   . HOH K 6 .   ? 6.357   20.806  4.251   1.00 41.02 ? 501 HOH B O   1 
HETATM 4332 O  O   . HOH K 6 .   ? 26.825  8.665   -3.335  1.00 16.32 ? 502 HOH B O   1 
HETATM 4333 O  O   . HOH K 6 .   ? 37.915  6.523   -16.980 1.00 20.64 ? 503 HOH B O   1 
HETATM 4334 O  O   . HOH K 6 .   ? 15.283  21.053  -11.643 1.00 12.43 ? 504 HOH B O   1 
HETATM 4335 O  O   . HOH K 6 .   ? 39.497  13.295  -15.809 1.00 26.32 ? 505 HOH B O   1 
HETATM 4336 O  O   . HOH K 6 .   ? 28.617  8.007   -7.060  1.00 12.77 ? 506 HOH B O   1 
HETATM 4337 O  O   . HOH K 6 .   ? 9.487   12.280  7.193   1.00 20.70 ? 507 HOH B O   1 
HETATM 4338 O  O   . HOH K 6 .   ? -0.193  -0.305  -23.981 1.00 23.95 ? 508 HOH B O   1 
HETATM 4339 O  O   . HOH K 6 .   ? 10.391  9.018   -29.281 1.00 9.65  ? 509 HOH B O   1 
HETATM 4340 O  O   . HOH K 6 .   ? 5.692   -12.924 -16.421 1.00 34.33 ? 510 HOH B O   1 
HETATM 4341 O  O   . HOH K 6 .   ? 35.703  -1.651  -12.864 1.00 16.32 ? 511 HOH B O   1 
HETATM 4342 O  O   . HOH K 6 .   ? 30.300  7.404   -27.196 1.00 21.32 ? 512 HOH B O   1 
HETATM 4343 O  O   . HOH K 6 .   ? 31.339  15.603  0.481   1.00 15.00 ? 513 HOH B O   1 
HETATM 4344 O  O   . HOH K 6 .   ? 16.814  28.507  -18.366 1.00 24.12 ? 514 HOH B O   1 
HETATM 4345 O  O   . HOH K 6 .   ? 16.773  16.056  -9.184  1.00 8.69  ? 515 HOH B O   1 
HETATM 4346 O  O   . HOH K 6 .   ? 7.762   13.908  -6.264  1.00 12.10 ? 516 HOH B O   1 
HETATM 4347 O  O   . HOH K 6 .   ? 20.731  5.792   0.489   1.00 6.90  ? 517 HOH B O   1 
HETATM 4348 O  O   . HOH K 6 .   ? 10.072  -1.928  -21.705 1.00 22.86 ? 518 HOH B O   1 
HETATM 4349 O  O   . HOH K 6 .   ? 14.034  22.281  -18.863 1.00 10.36 ? 519 HOH B O   1 
HETATM 4350 O  O   . HOH K 6 .   ? 33.054  0.748   -11.811 1.00 16.26 ? 520 HOH B O   1 
HETATM 4351 O  O   . HOH K 6 .   ? 25.568  20.864  -3.488  1.00 17.71 ? 521 HOH B O   1 
HETATM 4352 O  O   . HOH K 6 .   ? 0.546   -5.287  -16.985 1.00 21.32 ? 522 HOH B O   1 
HETATM 4353 O  O   . HOH K 6 .   ? 22.936  -6.372  -7.787  1.00 14.16 ? 523 HOH B O   1 
HETATM 4354 O  O   . HOH K 6 .   ? 20.307  13.768  -29.396 1.00 10.49 ? 524 HOH B O   1 
HETATM 4355 O  O   . HOH K 6 .   ? 28.686  29.982  -20.451 1.00 39.12 ? 525 HOH B O   1 
HETATM 4356 O  O   . HOH K 6 .   ? 3.671   3.097   -27.064 1.00 15.62 ? 526 HOH B O   1 
HETATM 4357 O  O   . HOH K 6 .   ? 12.959  -15.816 -8.004  1.00 23.50 ? 527 HOH B O   1 
HETATM 4358 O  O   . HOH K 6 .   ? 1.120   14.851  -4.960  1.00 27.92 ? 528 HOH B O   1 
HETATM 4359 O  O   . HOH K 6 .   ? 27.636  18.750  -22.461 1.00 15.11 ? 529 HOH B O   1 
HETATM 4360 O  O   . HOH K 6 .   ? 26.403  2.262   0.560   1.00 19.05 ? 530 HOH B O   1 
HETATM 4361 O  O   . HOH K 6 .   ? 7.922   -2.337  -28.298 1.00 34.85 ? 531 HOH B O   1 
HETATM 4362 O  O   . HOH K 6 .   ? 6.790   4.125   -23.414 1.00 10.91 ? 532 HOH B O   1 
HETATM 4363 O  O   . HOH K 6 .   ? 4.149   5.301   3.247   1.00 44.01 ? 533 HOH B O   1 
HETATM 4364 O  O   . HOH K 6 .   ? -1.713  5.788   -9.832  1.00 31.26 ? 534 HOH B O   1 
HETATM 4365 O  O   . HOH K 6 .   ? 12.514  26.091  -15.639 1.00 25.42 ? 535 HOH B O   1 
HETATM 4366 O  O   . HOH K 6 .   ? 9.199   11.716  -34.658 1.00 23.01 ? 536 HOH B O   1 
HETATM 4367 O  O   . HOH K 6 .   ? 28.731  -1.509  -3.663  1.00 36.33 ? 537 HOH B O   1 
HETATM 4368 O  O   . HOH K 6 .   ? -3.115  0.915   -18.475 1.00 25.04 ? 538 HOH B O   1 
HETATM 4369 O  O   . HOH K 6 .   ? 8.207   -10.105 0.915   1.00 32.19 ? 539 HOH B O   1 
HETATM 4370 O  O   . HOH K 6 .   ? -0.564  10.936  -4.161  1.00 36.33 ? 540 HOH B O   1 
HETATM 4371 O  O   . HOH K 6 .   ? 25.652  4.809   1.662   1.00 17.98 ? 541 HOH B O   1 
HETATM 4372 O  O   . HOH K 6 .   ? 10.015  8.262   -32.987 1.00 12.85 ? 542 HOH B O   1 
HETATM 4373 O  O   . HOH K 6 .   ? 0.188   9.692   -27.596 1.00 44.52 ? 543 HOH B O   1 
HETATM 4374 O  O   . HOH K 6 .   ? 8.078   13.959  8.537   1.00 29.74 ? 544 HOH B O   1 
HETATM 4375 O  O   . HOH K 6 .   ? 25.248  24.933  -12.150 1.00 20.68 ? 545 HOH B O   1 
HETATM 4376 O  O   . HOH K 6 .   ? 2.862   13.889  -19.390 1.00 15.18 ? 546 HOH B O   1 
HETATM 4377 O  O   . HOH K 6 .   ? -2.443  1.481   -28.635 1.00 28.71 ? 547 HOH B O   1 
HETATM 4378 O  O   . HOH K 6 .   ? 33.504  -2.459  -5.933  1.00 19.62 ? 548 HOH B O   1 
HETATM 4379 O  O   . HOH K 6 .   ? 0.764   -9.355  -11.226 1.00 23.30 ? 549 HOH B O   1 
HETATM 4380 O  O   . HOH K 6 .   ? 25.250  17.252  -23.057 1.00 9.99  ? 550 HOH B O   1 
HETATM 4381 O  O   . HOH K 6 .   ? 3.665   -6.072  -2.342  1.00 20.40 ? 551 HOH B O   1 
HETATM 4382 O  O   . HOH K 6 .   ? 1.892   6.625   -5.582  1.00 13.81 ? 552 HOH B O   1 
HETATM 4383 O  O   . HOH K 6 .   ? 22.063  -2.993  -18.393 1.00 31.82 ? 553 HOH B O   1 
HETATM 4384 O  O   . HOH K 6 .   ? 3.734   9.165   -9.375  1.00 15.51 ? 554 HOH B O   1 
HETATM 4385 O  O   . HOH K 6 .   ? 39.421  -1.837  -18.781 1.00 31.91 ? 555 HOH B O   1 
HETATM 4386 O  O   . HOH K 6 .   ? 11.296  22.575  -19.344 1.00 15.24 ? 556 HOH B O   1 
HETATM 4387 O  O   . HOH K 6 .   ? 21.363  -0.815  -10.353 1.00 17.09 ? 557 HOH B O   1 
HETATM 4388 O  O   . HOH K 6 .   ? 27.043  10.710  -26.052 1.00 17.87 ? 558 HOH B O   1 
HETATM 4389 O  O   . HOH K 6 .   ? 28.461  4.408   -0.169  1.00 36.16 ? 559 HOH B O   1 
HETATM 4390 O  O   . HOH K 6 .   ? 3.203   5.096   -17.113 1.00 11.08 ? 560 HOH B O   1 
HETATM 4391 O  O   . HOH K 6 .   ? 10.989  -6.610  -0.471  1.00 18.20 ? 561 HOH B O   1 
HETATM 4392 O  O   . HOH K 6 .   ? 31.535  17.241  -23.542 1.00 19.90 ? 562 HOH B O   1 
HETATM 4393 O  O   . HOH K 6 .   ? 21.611  -10.100 -9.044  1.00 14.97 ? 563 HOH B O   1 
HETATM 4394 O  O   . HOH K 6 .   ? 35.048  8.439   -18.012 1.00 19.19 ? 564 HOH B O   1 
HETATM 4395 O  O   . HOH K 6 .   ? 0.593   7.107   -10.136 1.00 16.32 ? 565 HOH B O   1 
HETATM 4396 O  O   . HOH K 6 .   ? 21.178  19.715  -7.038  1.00 17.35 ? 566 HOH B O   1 
HETATM 4397 O  O   . HOH K 6 .   ? 10.840  1.218   -34.481 1.00 18.79 ? 567 HOH B O   1 
HETATM 4398 O  O   . HOH K 6 .   ? 36.405  9.542   -10.400 1.00 32.67 ? 568 HOH B O   1 
HETATM 4399 O  O   . HOH K 6 .   ? 13.077  20.262  -3.672  1.00 28.17 ? 569 HOH B O   1 
HETATM 4400 O  O   . HOH K 6 .   ? 29.952  -8.361  -0.125  1.00 40.33 ? 570 HOH B O   1 
HETATM 4401 O  O   . HOH K 6 .   ? 24.590  -7.055  -5.774  1.00 15.12 ? 571 HOH B O   1 
HETATM 4402 O  O   . HOH K 6 .   ? 26.553  13.630  1.081   1.00 15.72 ? 572 HOH B O   1 
HETATM 4403 O  O   . HOH K 6 .   ? 19.298  20.498  -3.449  1.00 35.17 ? 573 HOH B O   1 
HETATM 4404 O  O   . HOH K 6 .   ? 24.229  -9.977  -12.773 1.00 30.49 ? 574 HOH B O   1 
HETATM 4405 O  O   . HOH K 6 .   ? 36.798  0.614   -13.413 1.00 25.11 ? 575 HOH B O   1 
HETATM 4406 O  O   . HOH K 6 .   ? 20.397  5.399   -37.985 1.00 23.60 ? 576 HOH B O   1 
HETATM 4407 O  O   . HOH K 6 .   ? -1.450  -1.348  -11.485 1.00 13.83 ? 577 HOH B O   1 
HETATM 4408 O  O   . HOH K 6 .   ? 14.109  17.934  3.056   1.00 33.26 ? 578 HOH B O   1 
HETATM 4409 O  O   . HOH K 6 .   ? 23.111  22.705  -27.237 1.00 33.71 ? 579 HOH B O   1 
HETATM 4410 O  O   . HOH K 6 .   ? 11.836  -4.669  -26.704 1.00 28.74 ? 580 HOH B O   1 
HETATM 4411 O  O   . HOH K 6 .   ? 33.334  -3.354  -22.408 1.00 22.02 ? 581 HOH B O   1 
HETATM 4412 O  O   . HOH K 6 .   ? 2.298   14.394  -3.045  1.00 32.51 ? 582 HOH B O   1 
HETATM 4413 O  O   . HOH K 6 .   ? 34.665  23.722  -7.961  1.00 21.77 ? 583 HOH B O   1 
HETATM 4414 O  O   . HOH K 6 .   ? 5.598   -3.662  0.002   1.00 17.48 ? 584 HOH B O   1 
HETATM 4415 O  O   . HOH K 6 .   ? 11.891  3.665   -34.767 1.00 17.96 ? 585 HOH B O   1 
HETATM 4416 O  O   . HOH K 6 .   ? 21.305  -9.145  -14.739 1.00 35.62 ? 586 HOH B O   1 
HETATM 4417 O  O   . HOH K 6 .   ? 37.128  14.027  -12.885 1.00 32.09 ? 587 HOH B O   1 
HETATM 4418 O  O   . HOH K 6 .   ? 10.414  18.516  -5.657  1.00 13.61 ? 588 HOH B O   1 
HETATM 4419 O  O   . HOH K 6 .   ? 25.556  30.380  -23.919 1.00 35.63 ? 589 HOH B O   1 
HETATM 4420 O  O   . HOH K 6 .   ? 7.021   -0.897  -32.761 1.00 22.26 ? 590 HOH B O   1 
HETATM 4421 O  O   . HOH K 6 .   ? 37.849  17.048  -16.833 1.00 21.55 ? 591 HOH B O   1 
HETATM 4422 O  O   . HOH K 6 .   ? 30.490  1.984   -25.479 1.00 15.85 ? 592 HOH B O   1 
HETATM 4423 O  O   . HOH K 6 .   ? 18.260  -20.115 -7.472  1.00 46.60 ? 593 HOH B O   1 
HETATM 4424 O  O   . HOH K 6 .   ? 26.728  -4.323  -1.196  1.00 27.56 ? 594 HOH B O   1 
HETATM 4425 O  O   . HOH K 6 .   ? 12.249  10.677  7.312   1.00 16.71 ? 595 HOH B O   1 
HETATM 4426 O  O   . HOH K 6 .   ? 22.097  14.474  -27.236 1.00 14.92 ? 596 HOH B O   1 
HETATM 4427 O  O   . HOH K 6 .   ? 34.485  2.610   -10.120 1.00 26.75 ? 597 HOH B O   1 
HETATM 4428 O  O   . HOH K 6 .   ? 10.073  17.307  2.437   1.00 22.95 ? 598 HOH B O   1 
HETATM 4429 O  O   . HOH K 6 .   ? 38.394  1.446   -21.395 1.00 38.89 ? 599 HOH B O   1 
HETATM 4430 O  O   . HOH K 6 .   ? 23.338  19.191  -27.230 1.00 17.59 ? 600 HOH B O   1 
HETATM 4431 O  O   . HOH K 6 .   ? 28.657  -0.555  -28.801 1.00 33.68 ? 601 HOH B O   1 
HETATM 4432 O  O   . HOH K 6 .   ? 32.318  20.779  -16.389 1.00 36.60 ? 602 HOH B O   1 
HETATM 4433 O  O   . HOH K 6 .   ? 23.729  -6.503  -3.096  1.00 17.00 ? 603 HOH B O   1 
HETATM 4434 O  O   . HOH K 6 .   ? 20.854  -15.029 -9.808  1.00 24.58 ? 604 HOH B O   1 
HETATM 4435 O  O   . HOH K 6 .   ? 32.574  21.712  -5.066  1.00 19.77 ? 605 HOH B O   1 
HETATM 4436 O  O   . HOH K 6 .   ? 32.586  3.699   -26.383 1.00 27.96 ? 606 HOH B O   1 
HETATM 4437 O  O   . HOH K 6 .   ? 7.028   -13.243 -10.631 1.00 37.65 ? 607 HOH B O   1 
HETATM 4438 O  O   . HOH K 6 .   ? 25.017  -9.819  -6.639  1.00 23.20 ? 608 HOH B O   1 
HETATM 4439 O  O   . HOH K 6 .   ? 12.518  -1.379  -28.440 1.00 14.91 ? 609 HOH B O   1 
HETATM 4440 O  O   . HOH K 6 .   ? 23.632  -6.363  -17.465 1.00 39.73 ? 610 HOH B O   1 
HETATM 4441 O  O   . HOH K 6 .   ? 27.922  4.177   -28.219 1.00 19.81 ? 611 HOH B O   1 
HETATM 4442 O  O   . HOH K 6 .   ? 8.948   2.235   -33.541 1.00 24.38 ? 612 HOH B O   1 
HETATM 4443 O  O   . HOH K 6 .   ? 30.957  20.491  -13.833 1.00 27.77 ? 613 HOH B O   1 
HETATM 4444 O  O   . HOH K 6 .   ? 40.651  5.823   -16.806 1.00 31.23 ? 614 HOH B O   1 
HETATM 4445 O  O   . HOH K 6 .   ? 32.614  15.076  -25.051 1.00 30.24 ? 615 HOH B O   1 
HETATM 4446 O  O   . HOH K 6 .   ? 24.858  -12.252 -5.823  1.00 32.59 ? 616 HOH B O   1 
HETATM 4447 O  O   . HOH K 6 .   ? 10.875  4.274   11.816  1.00 39.61 ? 617 HOH B O   1 
HETATM 4448 O  O   . HOH K 6 .   ? 2.766   6.862   -8.397  1.00 15.36 ? 618 HOH B O   1 
HETATM 4449 O  O   . HOH K 6 .   ? 19.385  27.345  -22.070 1.00 24.90 ? 619 HOH B O   1 
HETATM 4450 O  O   . HOH K 6 .   ? 27.709  -10.872 1.337   1.00 30.56 ? 620 HOH B O   1 
HETATM 4451 O  O   . HOH K 6 .   ? 14.191  4.342   8.499   1.00 26.89 ? 621 HOH B O   1 
HETATM 4452 O  O   . HOH K 6 .   ? 39.364  -10.948 -13.369 1.00 35.33 ? 622 HOH B O   1 
HETATM 4453 O  O   . HOH K 6 .   ? -4.689  2.392   -10.717 1.00 24.70 ? 623 HOH B O   1 
HETATM 4454 O  O   . HOH K 6 .   ? 24.583  27.381  -13.773 1.00 41.03 ? 624 HOH B O   1 
HETATM 4455 O  O   . HOH K 6 .   ? 39.851  -4.031  -18.398 1.00 40.90 ? 625 HOH B O   1 
HETATM 4456 O  O   . HOH K 6 .   ? 28.984  25.191  -4.098  1.00 34.61 ? 626 HOH B O   1 
HETATM 4457 O  O   . HOH K 6 .   ? 14.540  -3.239  -27.979 1.00 20.07 ? 627 HOH B O   1 
HETATM 4458 O  O   . HOH K 6 .   ? 5.269   15.294  -0.676  1.00 24.30 ? 628 HOH B O   1 
HETATM 4459 O  O   . HOH K 6 .   ? 11.483  -1.727  -30.935 1.00 26.20 ? 629 HOH B O   1 
HETATM 4460 O  O   . HOH K 6 .   ? 9.272   23.812  -5.218  1.00 33.46 ? 630 HOH B O   1 
HETATM 4461 O  O   . HOH K 6 .   ? 31.341  9.290   -3.571  1.00 25.89 ? 631 HOH B O   1 
HETATM 4462 O  O   . HOH K 6 .   ? 2.974   -4.215  1.166   1.00 35.58 ? 632 HOH B O   1 
HETATM 4463 O  O   . HOH K 6 .   ? -1.096  2.269   -33.564 1.00 33.68 ? 633 HOH B O   1 
HETATM 4464 O  O   . HOH K 6 .   ? 1.815   -6.076  -4.944  1.00 29.95 ? 634 HOH B O   1 
HETATM 4465 O  O   . HOH K 6 .   ? 23.685  25.446  -9.432  1.00 20.80 ? 635 HOH B O   1 
HETATM 4466 O  O   . HOH K 6 .   ? 13.147  -9.757  -13.433 1.00 31.71 ? 636 HOH B O   1 
HETATM 4467 O  O   . HOH K 6 .   ? 16.566  19.961  -32.679 1.00 34.33 ? 637 HOH B O   1 
HETATM 4468 O  O   . HOH K 6 .   ? 16.987  28.175  -26.663 1.00 51.70 ? 638 HOH B O   1 
HETATM 4469 O  O   . HOH K 6 .   ? 14.497  21.706  -34.002 1.00 34.26 ? 639 HOH B O   1 
HETATM 4470 O  O   . HOH K 6 .   ? 0.773   1.811   -23.253 1.00 27.05 ? 640 HOH B O   1 
HETATM 4471 O  O   . HOH K 6 .   ? 16.122  -14.678 -11.274 1.00 23.16 ? 641 HOH B O   1 
HETATM 4472 O  O   . HOH K 6 .   ? -3.370  -4.368  -15.112 1.00 30.07 ? 642 HOH B O   1 
HETATM 4473 O  O   . HOH K 6 .   ? 29.887  -11.237 -0.941  1.00 39.45 ? 643 HOH B O   1 
HETATM 4474 O  O   . HOH K 6 .   ? 23.908  16.342  -27.029 1.00 19.27 ? 644 HOH B O   1 
HETATM 4475 O  O   . HOH K 6 .   ? 16.615  25.857  -21.195 1.00 34.90 ? 645 HOH B O   1 
HETATM 4476 O  O   . HOH K 6 .   ? 34.870  25.500  -4.514  1.00 35.52 ? 646 HOH B O   1 
HETATM 4477 O  O   . HOH K 6 .   ? 22.112  14.162  -31.349 1.00 24.96 ? 647 HOH B O   1 
HETATM 4478 O  O   . HOH K 6 .   ? 10.428  -5.310  -24.632 1.00 37.14 ? 648 HOH B O   1 
HETATM 4479 O  O   . HOH K 6 .   ? 11.163  20.177  -27.936 1.00 17.75 ? 649 HOH B O   1 
HETATM 4480 O  O   . HOH K 6 .   ? 30.547  5.500   -4.160  1.00 21.17 ? 650 HOH B O   1 
HETATM 4481 O  O   . HOH K 6 .   ? 26.112  -5.162  -24.991 1.00 32.29 ? 651 HOH B O   1 
HETATM 4482 O  O   . HOH K 6 .   ? -3.898  -0.120  -11.903 1.00 35.75 ? 652 HOH B O   1 
HETATM 4483 O  O   . HOH K 6 .   ? 36.146  -1.078  -24.444 1.00 30.88 ? 653 HOH B O   1 
HETATM 4484 O  O   . HOH K 6 .   ? 0.485   -2.878  -4.741  1.00 18.62 ? 654 HOH B O   1 
HETATM 4485 O  O   . HOH K 6 .   ? 10.341  -8.031  1.526   1.00 31.17 ? 655 HOH B O   1 
HETATM 4486 O  O   . HOH K 6 .   ? 24.263  -12.702 -9.718  1.00 31.29 ? 656 HOH B O   1 
HETATM 4487 O  O   . HOH K 6 .   ? -3.434  -9.633  -13.325 1.00 32.59 ? 657 HOH B O   1 
HETATM 4488 O  O   . HOH K 6 .   ? 14.587  22.303  -3.737  1.00 31.55 ? 658 HOH B O   1 
HETATM 4489 O  O   . HOH K 6 .   ? 28.271  1.809   -27.300 1.00 24.77 ? 659 HOH B O   1 
HETATM 4490 O  O   . HOH K 6 .   ? 20.856  21.494  -27.533 1.00 33.09 ? 660 HOH B O   1 
HETATM 4491 O  O   . HOH K 6 .   ? 13.127  19.521  -29.839 1.00 17.92 ? 661 HOH B O   1 
HETATM 4492 O  O   . HOH K 6 .   ? 10.707  15.777  -31.089 1.00 34.18 ? 662 HOH B O   1 
HETATM 4493 O  O   . HOH K 6 .   ? 28.078  5.218   2.782   1.00 41.50 ? 663 HOH B O   1 
HETATM 4494 O  O   . HOH K 6 .   ? 8.396   16.702  -5.342  1.00 27.78 ? 664 HOH B O   1 
HETATM 4495 O  O   . HOH K 6 .   ? 29.145  7.859   -4.496  1.00 16.29 ? 665 HOH B O   1 
HETATM 4496 O  O   . HOH K 6 .   ? 40.484  17.404  -17.542 1.00 16.59 ? 666 HOH B O   1 
HETATM 4497 O  O   . HOH K 6 .   ? 9.891   -11.254 -18.466 1.00 31.89 ? 667 HOH B O   1 
HETATM 4498 O  O   . HOH K 6 .   ? 0.924   8.162   -29.633 1.00 39.27 ? 668 HOH B O   1 
HETATM 4499 O  O   . HOH K 6 .   ? 21.779  22.031  -6.156  1.00 21.98 ? 669 HOH B O   1 
HETATM 4500 O  O   . HOH K 6 .   ? 9.000   20.248  -4.243  1.00 26.00 ? 670 HOH B O   1 
HETATM 4501 O  O   . HOH K 6 .   ? -1.095  12.889  -27.540 1.00 24.30 ? 671 HOH B O   1 
HETATM 4502 O  O   . HOH K 6 .   ? 8.577   19.441  -28.635 1.00 27.69 ? 672 HOH B O   1 
HETATM 4503 O  O   . HOH K 6 .   ? 29.194  18.191  -24.473 1.00 17.45 ? 673 HOH B O   1 
HETATM 4504 O  O   . HOH K 6 .   ? -1.090  6.921   1.306   1.00 26.06 ? 674 HOH B O   1 
HETATM 4505 O  O   . HOH K 6 .   ? 24.168  29.068  -11.671 1.00 35.09 ? 675 HOH B O   1 
HETATM 4506 O  O   . HOH K 6 .   ? 23.469  23.635  -7.175  1.00 25.75 ? 676 HOH B O   1 
HETATM 4507 O  O   . HOH K 6 .   ? 14.877  24.880  -19.211 1.00 19.09 ? 677 HOH B O   1 
HETATM 4508 O  O   . HOH K 6 .   ? 25.795  15.488  -25.171 1.00 17.49 ? 678 HOH B O   1 
HETATM 4509 O  O   . HOH K 6 .   ? 14.374  16.324  -35.477 1.00 24.72 ? 679 HOH B O   1 
HETATM 4510 O  O   . HOH K 6 .   ? 15.585  10.409  9.103   1.00 33.78 ? 680 HOH B O   1 
HETATM 4511 O  O   . HOH K 6 .   ? 19.449  21.045  -29.414 1.00 34.88 ? 681 HOH B O   1 
HETATM 4512 O  O   . HOH K 6 .   ? 17.316  11.427  -38.339 1.00 32.34 ? 682 HOH B O   1 
HETATM 4513 O  O   . HOH K 6 .   ? 26.914  28.433  -10.080 1.00 49.40 ? 683 HOH B O   1 
HETATM 4514 O  O   . HOH K 6 .   ? -0.802  6.122   -5.438  1.00 28.09 ? 684 HOH B O   1 
HETATM 4515 O  O   . HOH K 6 .   ? 15.027  -15.911 -0.887  1.00 33.35 ? 685 HOH B O   1 
HETATM 4516 O  O   . HOH K 6 .   ? 25.412  12.885  -29.386 1.00 42.96 ? 686 HOH B O   1 
HETATM 4517 O  O   . HOH K 6 .   ? 18.725  -15.923 -11.222 1.00 27.04 ? 687 HOH B O   1 
HETATM 4518 O  O   . HOH K 6 .   ? 34.664  19.536  -13.168 1.00 29.22 ? 688 HOH B O   1 
HETATM 4519 O  O   . HOH K 6 .   ? 15.403  27.925  -22.281 1.00 31.62 ? 689 HOH B O   1 
HETATM 4520 O  O   . HOH K 6 .   ? 16.749  12.766  -35.448 1.00 24.77 ? 690 HOH B O   1 
HETATM 4521 O  O   . HOH K 6 .   ? -1.440  3.499   -5.529  1.00 32.90 ? 691 HOH B O   1 
HETATM 4522 O  O   . HOH K 6 .   ? 12.475  2.101   8.489   1.00 23.29 ? 692 HOH B O   1 
HETATM 4523 O  O   . HOH K 6 .   ? -2.403  9.349   -2.719  1.00 34.94 ? 693 HOH B O   1 
HETATM 4524 O  O   . HOH K 6 .   ? 29.860  14.398  -27.154 1.00 27.29 ? 694 HOH B O   1 
HETATM 4525 O  O   . HOH K 6 .   ? 37.684  3.658   -24.510 1.00 33.49 ? 695 HOH B O   1 
HETATM 4526 O  O   . HOH K 6 .   ? 31.343  0.547   -4.807  1.00 30.45 ? 696 HOH B O   1 
HETATM 4527 O  O   . HOH K 6 .   ? 30.581  -2.031  -27.480 1.00 28.21 ? 697 HOH B O   1 
HETATM 4528 O  O   . HOH K 6 .   ? 18.400  -3.477  -20.507 1.00 37.28 ? 698 HOH B O   1 
HETATM 4529 O  O   . HOH K 6 .   ? 15.690  24.365  -7.822  1.00 30.71 ? 699 HOH B O   1 
HETATM 4530 O  O   . HOH K 6 .   ? 37.756  16.886  -14.191 1.00 29.79 ? 700 HOH B O   1 
HETATM 4531 O  O   . HOH K 6 .   ? -6.735  -4.302  -18.290 1.00 33.38 ? 701 HOH B O   1 
HETATM 4532 O  O   . HOH K 6 .   ? 28.104  16.403  -26.132 1.00 18.17 ? 702 HOH B O   1 
HETATM 4533 O  O   . HOH K 6 .   ? 27.431  17.962  -28.430 1.00 27.25 ? 703 HOH B O   1 
HETATM 4534 O  O   . HOH K 6 .   ? 12.814  19.737  -32.390 1.00 36.33 ? 704 HOH B O   1 
HETATM 4535 O  O   . HOH K 6 .   ? 34.135  -0.362  -25.860 1.00 33.93 ? 705 HOH B O   1 
HETATM 4536 O  O   . HOH K 6 .   ? 34.352  1.897   -27.393 1.00 34.66 ? 706 HOH B O   1 
HETATM 4537 O  O   . HOH K 6 .   ? 31.546  -0.691  -25.252 1.00 25.29 ? 707 HOH B O   1 
HETATM 4538 O  O   . HOH L 6 .   ? -13.511 25.707  -43.814 1.00 27.04 ? 401 HOH A O   1 
HETATM 4539 O  O   . HOH L 6 .   ? -4.524  52.896  -27.061 1.00 20.71 ? 402 HOH A O   1 
HETATM 4540 O  O   . HOH L 6 .   ? -4.665  55.789  -23.981 1.00 30.22 ? 403 HOH A O   1 
HETATM 4541 O  O   . HOH L 6 .   ? -7.568  53.617  -29.976 1.00 24.88 ? 404 HOH A O   1 
HETATM 4542 O  O   . HOH L 6 .   ? -1.870  58.427  -25.968 1.00 35.46 ? 405 HOH A O   1 
HETATM 4543 O  O   . HOH L 6 .   ? 1.594   13.912  -28.332 1.00 28.79 ? 406 HOH A O   1 
HETATM 4544 O  O   . HOH L 6 .   ? -13.006 31.393  -27.478 1.00 28.03 ? 407 HOH A O   1 
HETATM 4545 O  O   . HOH L 6 .   ? -8.934  17.223  -6.763  1.00 30.55 ? 408 HOH A O   1 
HETATM 4546 O  O   . HOH L 6 .   ? -8.445  16.458  -38.283 1.00 22.66 ? 409 HOH A O   1 
HETATM 4547 O  O   . HOH L 6 .   ? 19.740  42.647  -18.482 1.00 26.56 ? 410 HOH A O   1 
HETATM 4548 O  O   . HOH L 6 .   ? 4.191   29.654  -5.856  1.00 20.73 ? 411 HOH A O   1 
HETATM 4549 O  O   . HOH L 6 .   ? -7.879  17.590  -10.097 1.00 30.28 ? 412 HOH A O   1 
HETATM 4550 O  O   . HOH L 6 .   ? -11.634 30.964  -25.254 1.00 19.85 ? 413 HOH A O   1 
HETATM 4551 O  O   . HOH L 6 .   ? -9.884  44.601  -44.645 1.00 29.25 ? 414 HOH A O   1 
HETATM 4552 O  O   . HOH L 6 .   ? -12.269 42.206  -42.789 1.00 30.61 ? 415 HOH A O   1 
HETATM 4553 O  O   . HOH L 6 .   ? -5.277  19.509  -13.618 1.00 38.23 ? 416 HOH A O   1 
HETATM 4554 O  O   . HOH L 6 .   ? 12.273  40.410  -36.469 1.00 23.52 ? 417 HOH A O   1 
HETATM 4555 O  O   . HOH L 6 .   ? -2.940  36.123  -48.913 1.00 22.40 ? 418 HOH A O   1 
HETATM 4556 O  O   . HOH L 6 .   ? 2.449   37.276  -44.313 1.00 24.29 ? 419 HOH A O   1 
HETATM 4557 O  O   . HOH L 6 .   ? -0.138  39.757  -14.890 1.00 10.70 ? 420 HOH A O   1 
HETATM 4558 O  O   . HOH L 6 .   ? -3.311  19.274  -21.431 1.00 33.10 ? 421 HOH A O   1 
HETATM 4559 O  O   . HOH L 6 .   ? 9.890   19.068  -46.968 1.00 22.41 ? 422 HOH A O   1 
HETATM 4560 O  O   . HOH L 6 .   ? 12.932  49.267  -25.068 1.00 31.42 ? 423 HOH A O   1 
HETATM 4561 O  O   . HOH L 6 .   ? -20.875 24.853  -24.355 1.00 24.50 ? 424 HOH A O   1 
HETATM 4562 O  O   . HOH L 6 .   ? 8.003   51.889  -25.918 1.00 29.35 ? 425 HOH A O   1 
HETATM 4563 O  O   . HOH L 6 .   ? -3.509  22.637  -12.878 1.00 12.86 ? 426 HOH A O   1 
HETATM 4564 O  O   . HOH L 6 .   ? 18.478  32.496  -27.054 1.00 45.39 ? 427 HOH A O   1 
HETATM 4565 O  O   . HOH L 6 .   ? -14.917 16.061  -19.903 1.00 17.95 ? 428 HOH A O   1 
HETATM 4566 O  O   . HOH L 6 .   ? 15.037  32.487  -23.275 1.00 25.67 ? 429 HOH A O   1 
HETATM 4567 O  O   . HOH L 6 .   ? -15.134 36.593  -38.563 1.00 17.34 ? 430 HOH A O   1 
HETATM 4568 O  O   . HOH L 6 .   ? 8.814   35.646  -34.332 1.00 15.57 ? 431 HOH A O   1 
HETATM 4569 O  O   . HOH L 6 .   ? -1.820  13.146  -34.827 1.00 44.54 ? 432 HOH A O   1 
HETATM 4570 O  O   . HOH L 6 .   ? 13.019  26.735  -19.371 1.00 29.88 ? 433 HOH A O   1 
HETATM 4571 O  O   . HOH L 6 .   ? -14.232 22.727  -39.521 1.00 27.86 ? 434 HOH A O   1 
HETATM 4572 O  O   . HOH L 6 .   ? -1.167  13.122  -8.581  1.00 36.34 ? 435 HOH A O   1 
HETATM 4573 O  O   . HOH L 6 .   ? -21.148 53.995  -24.807 1.00 34.42 ? 436 HOH A O   1 
HETATM 4574 O  O   . HOH L 6 .   ? 13.330  33.838  -18.913 1.00 11.73 ? 437 HOH A O   1 
HETATM 4575 O  O   . HOH L 6 .   ? -1.387  28.232  -6.300  1.00 17.27 ? 438 HOH A O   1 
HETATM 4576 O  O   . HOH L 6 .   ? -6.712  49.456  -16.550 1.00 20.34 ? 439 HOH A O   1 
HETATM 4577 O  O   . HOH L 6 .   ? 1.399   49.582  -33.207 1.00 13.43 ? 440 HOH A O   1 
HETATM 4578 O  O   . HOH L 6 .   ? -8.359  12.858  -17.951 1.00 31.29 ? 441 HOH A O   1 
HETATM 4579 O  O   . HOH L 6 .   ? 5.071   30.270  -43.905 1.00 29.86 ? 442 HOH A O   1 
HETATM 4580 O  O   . HOH L 6 .   ? 10.263  34.932  -12.274 1.00 16.71 ? 443 HOH A O   1 
HETATM 4581 O  O   . HOH L 6 .   ? 2.350   39.427  -7.906  1.00 19.17 ? 444 HOH A O   1 
HETATM 4582 O  O   . HOH L 6 .   ? 22.578  37.237  -18.442 1.00 28.30 ? 445 HOH A O   1 
HETATM 4583 O  O   . HOH L 6 .   ? -10.104 19.263  -7.361  1.00 21.29 ? 446 HOH A O   1 
HETATM 4584 O  O   . HOH L 6 .   ? -25.815 25.842  -30.438 1.00 28.75 ? 447 HOH A O   1 
HETATM 4585 O  O   . HOH L 6 .   ? -10.800 13.923  -38.937 1.00 36.13 ? 448 HOH A O   1 
HETATM 4586 O  O   . HOH L 6 .   ? -9.227  39.423  -30.428 1.00 10.26 ? 449 HOH A O   1 
HETATM 4587 O  O   . HOH L 6 .   ? 22.638  34.717  -21.794 1.00 33.91 ? 450 HOH A O   1 
HETATM 4588 O  O   . HOH L 6 .   ? -8.242  12.774  -32.529 1.00 28.08 ? 451 HOH A O   1 
HETATM 4589 O  O   . HOH L 6 .   ? -10.208 50.830  -32.422 1.00 26.32 ? 452 HOH A O   1 
HETATM 4590 O  O   . HOH L 6 .   ? -14.798 34.238  -8.360  1.00 20.59 ? 453 HOH A O   1 
HETATM 4591 O  O   . HOH L 6 .   ? -12.816 49.661  -30.212 1.00 19.47 ? 454 HOH A O   1 
HETATM 4592 O  O   . HOH L 6 .   ? 13.226  46.222  -35.335 1.00 21.38 ? 455 HOH A O   1 
HETATM 4593 O  O   . HOH L 6 .   ? 4.126   17.275  -41.875 1.00 24.80 ? 456 HOH A O   1 
HETATM 4594 O  O   . HOH L 6 .   ? -18.383 35.977  -41.143 1.00 27.40 ? 457 HOH A O   1 
HETATM 4595 O  O   . HOH L 6 .   ? -9.755  14.601  -31.198 1.00 18.01 ? 458 HOH A O   1 
HETATM 4596 O  O   . HOH L 6 .   ? 1.691   42.195  -41.107 1.00 18.27 ? 459 HOH A O   1 
HETATM 4597 O  O   . HOH L 6 .   ? 3.088   46.168  -39.087 1.00 24.27 ? 460 HOH A O   1 
HETATM 4598 O  O   . HOH L 6 .   ? -5.088  18.140  -38.649 1.00 17.92 ? 461 HOH A O   1 
HETATM 4599 O  O   . HOH L 6 .   ? -13.219 46.800  -19.246 1.00 20.33 ? 462 HOH A O   1 
HETATM 4600 O  O   . HOH L 6 .   ? -14.469 24.552  -23.330 1.00 13.50 ? 463 HOH A O   1 
HETATM 4601 O  O   . HOH L 6 .   ? -5.110  52.182  -19.252 1.00 16.56 ? 464 HOH A O   1 
HETATM 4602 O  O   . HOH L 6 .   ? -3.402  10.214  -37.547 1.00 23.45 ? 465 HOH A O   1 
HETATM 4603 O  O   . HOH L 6 .   ? 1.302   52.792  -21.395 1.00 14.15 ? 466 HOH A O   1 
HETATM 4604 O  O   . HOH L 6 .   ? -5.182  33.322  -41.104 1.00 12.16 ? 467 HOH A O   1 
HETATM 4605 O  O   . HOH L 6 .   ? 5.822   25.367  -13.925 1.00 13.70 ? 468 HOH A O   1 
HETATM 4606 O  O   . HOH L 6 .   ? -23.057 37.141  -34.788 1.00 26.84 ? 469 HOH A O   1 
HETATM 4607 O  O   . HOH L 6 .   ? 17.146  36.519  -18.086 1.00 14.78 ? 470 HOH A O   1 
HETATM 4608 O  O   . HOH L 6 .   ? -6.370  37.668  -43.066 1.00 15.39 ? 471 HOH A O   1 
HETATM 4609 O  O   . HOH L 6 .   ? 8.895   53.191  -32.812 1.00 24.20 ? 472 HOH A O   1 
HETATM 4610 O  O   . HOH L 6 .   ? 5.627   31.541  -31.281 1.00 7.84  ? 473 HOH A O   1 
HETATM 4611 O  O   . HOH L 6 .   ? 10.840  24.220  -15.220 1.00 19.15 ? 474 HOH A O   1 
HETATM 4612 O  O   . HOH L 6 .   ? -13.970 37.418  -22.788 1.00 31.22 ? 475 HOH A O   1 
HETATM 4613 O  O   . HOH L 6 .   ? -6.125  28.324  -45.133 1.00 16.57 ? 476 HOH A O   1 
HETATM 4614 O  O   . HOH L 6 .   ? -9.889  28.421  -6.066  1.00 22.04 ? 477 HOH A O   1 
HETATM 4615 O  O   . HOH L 6 .   ? -0.033  40.595  -45.112 1.00 33.86 ? 478 HOH A O   1 
HETATM 4616 O  O   . HOH L 6 .   ? -0.585  27.901  -10.051 1.00 10.78 ? 479 HOH A O   1 
HETATM 4617 O  O   . HOH L 6 .   ? 2.018   51.675  -19.068 1.00 15.20 ? 480 HOH A O   1 
HETATM 4618 O  O   . HOH L 6 .   ? -4.073  41.335  -35.575 1.00 12.87 ? 481 HOH A O   1 
HETATM 4619 O  O   . HOH L 6 .   ? 5.248   20.611  -40.031 1.00 19.30 ? 482 HOH A O   1 
HETATM 4620 O  O   . HOH L 6 .   ? 9.816   47.098  -36.593 1.00 25.45 ? 483 HOH A O   1 
HETATM 4621 O  O   . HOH L 6 .   ? -20.865 37.715  -40.813 1.00 34.62 ? 484 HOH A O   1 
HETATM 4622 O  O   . HOH L 6 .   ? 2.076   23.361  -46.456 1.00 14.99 ? 485 HOH A O   1 
HETATM 4623 O  O   . HOH L 6 .   ? 10.835  30.847  -29.076 1.00 10.57 ? 486 HOH A O   1 
HETATM 4624 O  O   . HOH L 6 .   ? -1.578  45.248  -17.810 1.00 10.82 ? 487 HOH A O   1 
HETATM 4625 O  O   . HOH L 6 .   ? 19.311  43.897  -25.368 1.00 29.02 ? 488 HOH A O   1 
HETATM 4626 O  O   . HOH L 6 .   ? -17.177 36.028  -32.535 1.00 15.78 ? 489 HOH A O   1 
HETATM 4627 O  O   . HOH L 6 .   ? 12.908  47.095  -23.370 1.00 25.63 ? 490 HOH A O   1 
HETATM 4628 O  O   . HOH L 6 .   ? 6.521   48.894  -19.795 1.00 26.24 ? 491 HOH A O   1 
HETATM 4629 O  O   . HOH L 6 .   ? 7.194   32.482  -10.907 1.00 13.90 ? 492 HOH A O   1 
HETATM 4630 O  O   . HOH L 6 .   ? -10.694 39.729  -37.214 1.00 14.28 ? 493 HOH A O   1 
HETATM 4631 O  O   . HOH L 6 .   ? 9.390   23.439  -17.615 1.00 10.06 ? 494 HOH A O   1 
HETATM 4632 O  O   . HOH L 6 .   ? -7.900  16.496  -13.436 1.00 29.39 ? 495 HOH A O   1 
HETATM 4633 O  O   . HOH L 6 .   ? -18.471 14.647  -25.201 1.00 25.06 ? 496 HOH A O   1 
HETATM 4634 O  O   . HOH L 6 .   ? -11.143 56.268  -29.428 1.00 32.11 ? 497 HOH A O   1 
HETATM 4635 O  O   . HOH L 6 .   ? 9.899   39.738  -37.988 1.00 27.19 ? 498 HOH A O   1 
HETATM 4636 O  O   . HOH L 6 .   ? 2.994   25.695  -8.500  1.00 18.96 ? 499 HOH A O   1 
HETATM 4637 O  O   . HOH L 6 .   ? -15.987 16.422  -34.862 1.00 21.34 ? 500 HOH A O   1 
HETATM 4638 O  O   . HOH L 6 .   ? 0.257   56.242  -29.341 1.00 17.92 ? 501 HOH A O   1 
HETATM 4639 O  O   . HOH L 6 .   ? -12.388 14.990  -28.237 1.00 28.08 ? 502 HOH A O   1 
HETATM 4640 O  O   . HOH L 6 .   ? -5.779  50.864  -27.857 1.00 25.25 ? 503 HOH A O   1 
HETATM 4641 O  O   . HOH L 6 .   ? -5.155  39.170  -47.242 1.00 16.34 ? 504 HOH A O   1 
HETATM 4642 O  O   . HOH L 6 .   ? 11.805  22.157  -26.044 1.00 13.02 ? 505 HOH A O   1 
HETATM 4643 O  O   . HOH L 6 .   ? 10.082  30.801  -39.054 1.00 24.87 ? 506 HOH A O   1 
HETATM 4644 O  O   . HOH L 6 .   ? -12.284 54.747  -25.238 1.00 26.63 ? 507 HOH A O   1 
HETATM 4645 O  O   . HOH L 6 .   ? -4.864  23.538  -14.935 1.00 10.84 ? 508 HOH A O   1 
HETATM 4646 O  O   . HOH L 6 .   ? 13.333  31.207  -10.576 1.00 29.86 ? 509 HOH A O   1 
HETATM 4647 O  O   . HOH L 6 .   ? 17.710  44.064  -15.335 1.00 30.84 ? 510 HOH A O   1 
HETATM 4648 O  O   . HOH L 6 .   ? -1.950  39.751  -38.453 1.00 16.02 ? 511 HOH A O   1 
HETATM 4649 O  O   . HOH L 6 .   ? -0.796  29.702  -47.710 1.00 19.30 ? 512 HOH A O   1 
HETATM 4650 O  O   . HOH L 6 .   ? 2.122   36.714  -7.294  1.00 18.47 ? 513 HOH A O   1 
HETATM 4651 O  O   . HOH L 6 .   ? -9.468  54.185  -22.128 1.00 27.66 ? 514 HOH A O   1 
HETATM 4652 O  O   . HOH L 6 .   ? 9.816   27.119  -36.283 1.00 16.84 ? 515 HOH A O   1 
HETATM 4653 O  O   . HOH L 6 .   ? 13.676  44.523  -14.919 1.00 30.56 ? 516 HOH A O   1 
HETATM 4654 O  O   . HOH L 6 .   ? -6.765  18.437  -40.599 1.00 23.80 ? 517 HOH A O   1 
HETATM 4655 O  O   . HOH L 6 .   ? -0.948  35.414  -1.406  1.00 36.64 ? 518 HOH A O   1 
HETATM 4656 O  O   . HOH L 6 .   ? 6.747   39.877  -11.321 1.00 19.33 ? 519 HOH A O   1 
HETATM 4657 O  O   . HOH L 6 .   ? -13.508 17.915  -37.577 1.00 24.86 ? 520 HOH A O   1 
HETATM 4658 O  O   . HOH L 6 .   ? 3.771   38.253  -11.741 1.00 13.31 ? 521 HOH A O   1 
HETATM 4659 O  O   . HOH L 6 .   ? -23.664 35.311  -32.812 1.00 30.14 ? 522 HOH A O   1 
HETATM 4660 O  O   . HOH L 6 .   ? -14.356 28.018  -13.022 1.00 44.38 ? 523 HOH A O   1 
HETATM 4661 O  O   . HOH L 6 .   ? 9.181   54.057  -23.042 1.00 24.31 ? 524 HOH A O   1 
HETATM 4662 O  O   . HOH L 6 .   ? -1.426  17.739  -29.304 1.00 32.18 ? 525 HOH A O   1 
HETATM 4663 O  O   . HOH L 6 .   ? -1.763  54.508  -17.465 1.00 18.83 ? 526 HOH A O   1 
HETATM 4664 O  O   . HOH L 6 .   ? -6.266  30.319  -5.290  1.00 14.52 ? 527 HOH A O   1 
HETATM 4665 O  O   . HOH L 6 .   ? 2.079   48.377  -30.832 1.00 13.90 ? 528 HOH A O   1 
HETATM 4666 O  O   . HOH L 6 .   ? 9.024   22.727  -26.361 1.00 12.10 ? 529 HOH A O   1 
HETATM 4667 O  O   . HOH L 6 .   ? -20.721 37.396  -31.341 1.00 26.54 ? 530 HOH A O   1 
HETATM 4668 O  O   . HOH L 6 .   ? -16.843 23.030  -37.780 1.00 24.69 ? 531 HOH A O   1 
HETATM 4669 O  O   . HOH L 6 .   ? 2.410   42.598  -16.504 1.00 13.29 ? 532 HOH A O   1 
HETATM 4670 O  O   . HOH L 6 .   ? 8.208   44.453  -19.965 1.00 20.07 ? 533 HOH A O   1 
HETATM 4671 O  O   . HOH L 6 .   ? 6.587   41.961  -18.900 1.00 13.55 ? 534 HOH A O   1 
HETATM 4672 O  O   . HOH L 6 .   ? 17.046  40.163  -27.867 1.00 35.05 ? 535 HOH A O   1 
HETATM 4673 O  O   . HOH L 6 .   ? -12.851 41.364  -37.715 1.00 24.93 ? 536 HOH A O   1 
HETATM 4674 O  O   . HOH L 6 .   ? -12.121 34.225  -27.639 1.00 26.46 ? 537 HOH A O   1 
HETATM 4675 O  O   . HOH L 6 .   ? -12.483 39.282  -42.472 1.00 19.97 ? 538 HOH A O   1 
HETATM 4676 O  O   . HOH L 6 .   ? -5.602  21.146  -11.736 1.00 35.40 ? 539 HOH A O   1 
HETATM 4677 O  O   . HOH L 6 .   ? -10.221 13.862  -28.603 1.00 21.97 ? 540 HOH A O   1 
HETATM 4678 O  O   . HOH L 6 .   ? -5.439  15.960  -13.488 1.00 26.90 ? 541 HOH A O   1 
HETATM 4679 O  O   . HOH L 6 .   ? 7.598   47.429  -30.045 1.00 27.60 ? 542 HOH A O   1 
HETATM 4680 O  O   . HOH L 6 .   ? -18.036 37.333  -34.761 1.00 17.90 ? 543 HOH A O   1 
HETATM 4681 O  O   . HOH L 6 .   ? -7.099  18.013  -45.016 1.00 18.91 ? 544 HOH A O   1 
HETATM 4682 O  O   . HOH L 6 .   ? 8.691   41.092  -14.506 1.00 20.40 ? 545 HOH A O   1 
HETATM 4683 O  O   . HOH L 6 .   ? 15.830  34.791  -19.757 1.00 12.61 ? 546 HOH A O   1 
HETATM 4684 O  O   . HOH L 6 .   ? 6.014   48.541  -37.329 1.00 15.72 ? 547 HOH A O   1 
HETATM 4685 O  O   . HOH L 6 .   ? 20.118  34.439  -25.010 1.00 24.94 ? 548 HOH A O   1 
HETATM 4686 O  O   . HOH L 6 .   ? 12.314  29.690  -12.605 1.00 29.17 ? 549 HOH A O   1 
HETATM 4687 O  O   . HOH L 6 .   ? -0.058  43.903  -16.104 1.00 10.28 ? 550 HOH A O   1 
HETATM 4688 O  O   . HOH L 6 .   ? 6.973   18.922  -41.610 1.00 19.67 ? 551 HOH A O   1 
HETATM 4689 O  O   . HOH L 6 .   ? -10.981 29.669  -11.613 1.00 13.21 ? 552 HOH A O   1 
HETATM 4690 O  O   . HOH L 6 .   ? -2.582  47.069  -15.356 1.00 14.25 ? 553 HOH A O   1 
HETATM 4691 O  O   . HOH L 6 .   ? 8.767   21.536  -30.056 1.00 23.95 ? 554 HOH A O   1 
HETATM 4692 O  O   . HOH L 6 .   ? -5.693  54.689  -28.319 1.00 31.14 ? 555 HOH A O   1 
HETATM 4693 O  O   . HOH L 6 .   ? -2.741  15.673  -27.606 1.00 16.61 ? 556 HOH A O   1 
HETATM 4694 O  O   . HOH L 6 .   ? -2.550  50.521  -25.367 1.00 11.67 ? 557 HOH A O   1 
HETATM 4695 O  O   . HOH L 6 .   ? -20.596 34.679  -30.896 1.00 20.07 ? 558 HOH A O   1 
HETATM 4696 O  O   . HOH L 6 .   ? -8.617  46.922  -16.886 1.00 14.38 ? 559 HOH A O   1 
HETATM 4697 O  O   . HOH L 6 .   ? 2.395   17.948  -10.405 1.00 39.22 ? 560 HOH A O   1 
HETATM 4698 O  O   . HOH L 6 .   ? -20.490 38.133  -27.556 1.00 26.07 ? 561 HOH A O   1 
HETATM 4699 O  O   . HOH L 6 .   ? 18.487  39.386  -30.238 1.00 30.01 ? 562 HOH A O   1 
HETATM 4700 O  O   . HOH L 6 .   ? 4.548   18.986  -34.420 1.00 41.19 ? 563 HOH A O   1 
HETATM 4701 O  O   . HOH L 6 .   ? -25.941 28.836  -36.792 1.00 21.08 ? 564 HOH A O   1 
HETATM 4702 O  O   . HOH L 6 .   ? 5.353   45.052  -36.076 1.00 16.33 ? 565 HOH A O   1 
HETATM 4703 O  O   . HOH L 6 .   ? -11.368 25.871  -17.236 1.00 17.42 ? 566 HOH A O   1 
HETATM 4704 O  O   . HOH L 6 .   ? -1.292  50.072  -33.255 1.00 20.39 ? 567 HOH A O   1 
HETATM 4705 O  O   . HOH L 6 .   ? 9.542   26.071  -11.606 1.00 22.04 ? 568 HOH A O   1 
HETATM 4706 O  O   . HOH L 6 .   ? -10.558 13.060  -25.154 1.00 23.01 ? 569 HOH A O   1 
HETATM 4707 O  O   . HOH L 6 .   ? -6.064  44.993  -13.717 1.00 22.77 ? 570 HOH A O   1 
HETATM 4708 O  O   . HOH L 6 .   ? -2.783  15.497  -32.136 1.00 25.57 ? 571 HOH A O   1 
HETATM 4709 O  O   . HOH L 6 .   ? 13.679  31.011  -19.904 1.00 27.93 ? 572 HOH A O   1 
HETATM 4710 O  O   . HOH L 6 .   ? 4.167   39.512  -14.065 1.00 15.58 ? 573 HOH A O   1 
HETATM 4711 O  O   . HOH L 6 .   ? -22.081 34.925  -25.971 1.00 41.08 ? 574 HOH A O   1 
HETATM 4712 O  O   . HOH L 6 .   ? -11.632 16.338  -39.908 1.00 34.08 ? 575 HOH A O   1 
HETATM 4713 O  O   . HOH L 6 .   ? 14.247  40.943  -29.950 1.00 21.21 ? 576 HOH A O   1 
HETATM 4714 O  O   . HOH L 6 .   ? -13.425 13.340  -36.263 1.00 33.10 ? 577 HOH A O   1 
HETATM 4715 O  O   . HOH L 6 .   ? -4.294  56.372  -29.590 1.00 25.94 ? 578 HOH A O   1 
HETATM 4716 O  O   . HOH L 6 .   ? -10.304 47.115  -30.930 1.00 17.61 ? 579 HOH A O   1 
HETATM 4717 O  O   . HOH L 6 .   ? -6.554  25.608  -48.148 1.00 18.94 ? 580 HOH A O   1 
HETATM 4718 O  O   . HOH L 6 .   ? 12.355  40.406  -14.384 1.00 27.53 ? 581 HOH A O   1 
HETATM 4719 O  O   . HOH L 6 .   ? 11.304  54.342  -32.095 1.00 27.12 ? 582 HOH A O   1 
HETATM 4720 O  O   . HOH L 6 .   ? 3.258   45.231  -41.929 1.00 22.84 ? 583 HOH A O   1 
HETATM 4721 O  O   . HOH L 6 .   ? 1.498   18.593  -22.092 1.00 22.94 ? 584 HOH A O   1 
HETATM 4722 O  O   . HOH L 6 .   ? -12.682 29.396  -19.224 1.00 23.83 ? 585 HOH A O   1 
HETATM 4723 O  O   . HOH L 6 .   ? 8.259   34.036  -7.676  1.00 28.16 ? 586 HOH A O   1 
HETATM 4724 O  O   . HOH L 6 .   ? 14.384  28.512  -24.579 1.00 16.82 ? 587 HOH A O   1 
HETATM 4725 O  O   . HOH L 6 .   ? 3.173   52.259  -30.513 1.00 15.64 ? 588 HOH A O   1 
HETATM 4726 O  O   . HOH L 6 .   ? 5.806   53.830  -27.123 1.00 26.61 ? 589 HOH A O   1 
HETATM 4727 O  O   . HOH L 6 .   ? -0.144  24.793  -46.858 1.00 11.59 ? 590 HOH A O   1 
HETATM 4728 O  O   . HOH L 6 .   ? -11.438 26.326  -9.845  1.00 36.35 ? 591 HOH A O   1 
HETATM 4729 O  O   . HOH L 6 .   ? 3.904   22.048  -32.716 1.00 16.67 ? 592 HOH A O   1 
HETATM 4730 O  O   . HOH L 6 .   ? 8.332   24.817  -33.840 1.00 12.89 ? 593 HOH A O   1 
HETATM 4731 O  O   . HOH L 6 .   ? -24.396 35.401  -42.356 1.00 40.08 ? 594 HOH A O   1 
HETATM 4732 O  O   . HOH L 6 .   ? -1.378  13.118  -24.993 1.00 27.10 ? 595 HOH A O   1 
HETATM 4733 O  O   . HOH L 6 .   ? 5.801   22.649  -36.198 1.00 14.75 ? 596 HOH A O   1 
HETATM 4734 O  O   . HOH L 6 .   ? -23.338 51.905  -28.883 1.00 35.24 ? 597 HOH A O   1 
HETATM 4735 O  O   . HOH L 6 .   ? -11.376 35.180  -29.996 1.00 19.63 ? 598 HOH A O   1 
HETATM 4736 O  O   . HOH L 6 .   ? 12.690  30.931  -22.099 1.00 30.74 ? 599 HOH A O   1 
HETATM 4737 O  O   . HOH L 6 .   ? -13.819 49.406  -20.284 1.00 21.23 ? 600 HOH A O   1 
HETATM 4738 O  O   . HOH L 6 .   ? -20.913 17.998  -29.340 1.00 34.15 ? 601 HOH A O   1 
HETATM 4739 O  O   . HOH L 6 .   ? 10.353  48.225  -26.138 1.00 22.44 ? 602 HOH A O   1 
HETATM 4740 O  O   . HOH L 6 .   ? -10.210 44.675  -37.268 1.00 23.44 ? 603 HOH A O   1 
HETATM 4741 O  O   . HOH L 6 .   ? 14.148  52.882  -26.382 1.00 35.14 ? 604 HOH A O   1 
HETATM 4742 O  O   . HOH L 6 .   ? -20.329 28.889  -25.847 1.00 34.32 ? 605 HOH A O   1 
HETATM 4743 O  O   . HOH L 6 .   ? -5.502  12.177  -26.895 1.00 32.15 ? 606 HOH A O   1 
HETATM 4744 O  O   . HOH L 6 .   ? 17.736  42.582  -27.141 1.00 40.14 ? 607 HOH A O   1 
HETATM 4745 O  O   . HOH L 6 .   ? 0.296   27.094  -48.433 1.00 14.18 ? 608 HOH A O   1 
HETATM 4746 O  O   . HOH L 6 .   ? -9.927  50.381  -29.767 1.00 25.35 ? 609 HOH A O   1 
HETATM 4747 O  O   . HOH L 6 .   ? 3.725   33.553  -4.590  1.00 16.90 ? 610 HOH A O   1 
HETATM 4748 O  O   . HOH L 6 .   ? -20.620 37.670  -34.032 1.00 21.10 ? 611 HOH A O   1 
HETATM 4749 O  O   . HOH L 6 .   ? -22.821 20.190  -27.023 1.00 27.42 ? 612 HOH A O   1 
HETATM 4750 O  O   . HOH L 6 .   ? 7.325   23.122  -43.440 1.00 21.61 ? 613 HOH A O   1 
HETATM 4751 O  O   . HOH L 6 .   ? -11.113 45.713  -13.216 1.00 20.54 ? 614 HOH A O   1 
HETATM 4752 O  O   . HOH L 6 .   ? -12.341 32.063  -20.795 1.00 26.79 ? 615 HOH A O   1 
HETATM 4753 O  O   . HOH L 6 .   ? -22.348 18.851  -25.030 1.00 31.23 ? 616 HOH A O   1 
HETATM 4754 O  O   . HOH L 6 .   ? 20.404  40.046  -13.474 1.00 39.45 ? 617 HOH A O   1 
HETATM 4755 O  O   . HOH L 6 .   ? 10.334  18.441  -44.055 1.00 29.32 ? 618 HOH A O   1 
HETATM 4756 O  O   . HOH L 6 .   ? 0.306   46.353  -15.110 1.00 16.41 ? 619 HOH A O   1 
HETATM 4757 O  O   . HOH L 6 .   ? 18.185  32.830  -23.190 1.00 35.01 ? 620 HOH A O   1 
HETATM 4758 O  O   . HOH L 6 .   ? -15.648 42.667  -40.064 1.00 38.24 ? 621 HOH A O   1 
HETATM 4759 O  O   . HOH L 6 .   ? 2.670   32.300  -41.683 1.00 16.87 ? 622 HOH A O   1 
HETATM 4760 O  O   . HOH L 6 .   ? 4.017   17.019  -38.056 1.00 42.05 ? 623 HOH A O   1 
HETATM 4761 O  O   . HOH L 6 .   ? 14.690  38.837  -32.230 1.00 26.94 ? 624 HOH A O   1 
HETATM 4762 O  O   . HOH L 6 .   ? -11.902 23.257  -13.165 1.00 24.67 ? 625 HOH A O   1 
HETATM 4763 O  O   . HOH L 6 .   ? -19.748 40.996  -41.220 1.00 32.92 ? 626 HOH A O   1 
HETATM 4764 O  O   . HOH L 6 .   ? 3.089   47.861  -15.902 1.00 20.50 ? 627 HOH A O   1 
HETATM 4765 O  O   . HOH L 6 .   ? -13.207 31.532  -12.388 1.00 16.64 ? 628 HOH A O   1 
HETATM 4766 O  O   . HOH L 6 .   ? -11.410 28.829  -8.877  1.00 20.00 ? 629 HOH A O   1 
HETATM 4767 O  O   . HOH L 6 .   ? 0.420   23.024  -5.149  1.00 33.34 ? 630 HOH A O   1 
HETATM 4768 O  O   . HOH L 6 .   ? -2.315  22.982  -47.284 1.00 11.98 ? 631 HOH A O   1 
HETATM 4769 O  O   . HOH L 6 .   ? 17.782  36.119  -13.082 1.00 31.42 ? 632 HOH A O   1 
HETATM 4770 O  O   . HOH L 6 .   ? -22.693 42.377  -36.805 1.00 39.14 ? 633 HOH A O   1 
HETATM 4771 O  O   . HOH L 6 .   ? 8.560   25.641  -9.127  1.00 34.16 ? 634 HOH A O   1 
HETATM 4772 O  O   . HOH L 6 .   ? 8.079   52.065  -19.311 1.00 35.28 ? 635 HOH A O   1 
HETATM 4773 O  O   . HOH L 6 .   ? -19.368 45.389  -30.005 1.00 25.68 ? 636 HOH A O   1 
HETATM 4774 O  O   . HOH L 6 .   ? -7.329  38.917  -45.356 1.00 20.68 ? 637 HOH A O   1 
HETATM 4775 O  O   . HOH L 6 .   ? -17.610 36.250  -37.181 1.00 22.65 ? 638 HOH A O   1 
HETATM 4776 O  O   . HOH L 6 .   ? -13.901 46.082  -36.818 1.00 22.25 ? 639 HOH A O   1 
HETATM 4777 O  O   . HOH L 6 .   ? -8.830  10.639  -24.488 1.00 32.47 ? 640 HOH A O   1 
HETATM 4778 O  O   . HOH L 6 .   ? 13.184  31.427  -30.597 1.00 19.36 ? 641 HOH A O   1 
HETATM 4779 O  O   . HOH L 6 .   ? 14.136  24.164  -34.005 1.00 27.32 ? 642 HOH A O   1 
HETATM 4780 O  O   . HOH L 6 .   ? 9.364   25.280  -38.291 1.00 24.98 ? 643 HOH A O   1 
HETATM 4781 O  O   . HOH L 6 .   ? 16.439  42.313  -29.078 1.00 40.67 ? 644 HOH A O   1 
HETATM 4782 O  O   . HOH L 6 .   ? -14.102 12.401  -15.905 1.00 32.35 ? 645 HOH A O   1 
HETATM 4783 O  O   . HOH L 6 .   ? 9.488   47.170  -28.651 1.00 26.54 ? 646 HOH A O   1 
HETATM 4784 O  O   . HOH L 6 .   ? 9.002   30.771  -10.038 1.00 31.47 ? 647 HOH A O   1 
HETATM 4785 O  O   . HOH L 6 .   ? 18.387  37.067  -31.545 1.00 38.99 ? 648 HOH A O   1 
HETATM 4786 O  O   . HOH L 6 .   ? 8.447   23.002  -37.127 1.00 23.88 ? 649 HOH A O   1 
HETATM 4787 O  O   . HOH L 6 .   ? -25.992 19.231  -28.938 1.00 48.62 ? 650 HOH A O   1 
HETATM 4788 O  O   . HOH L 6 .   ? -21.680 46.192  -30.662 1.00 48.29 ? 651 HOH A O   1 
HETATM 4789 O  O   . HOH L 6 .   ? 10.164  23.521  -35.249 1.00 23.23 ? 652 HOH A O   1 
HETATM 4790 O  O   . HOH L 6 .   ? 6.095   23.964  -6.438  1.00 31.36 ? 653 HOH A O   1 
HETATM 4791 O  O   . HOH L 6 .   ? 0.656   19.359  -8.249  1.00 39.21 ? 654 HOH A O   1 
HETATM 4792 O  O   . HOH L 6 .   ? 6.213   29.928  -8.128  1.00 35.21 ? 655 HOH A O   1 
HETATM 4793 O  O   . HOH L 6 .   ? -8.713  45.236  -14.600 1.00 25.18 ? 656 HOH A O   1 
HETATM 4794 O  O   . HOH L 6 .   ? -10.332 25.953  -7.597  1.00 35.93 ? 657 HOH A O   1 
HETATM 4795 O  O   . HOH L 6 .   ? -19.079 36.191  -25.191 1.00 29.45 ? 658 HOH A O   1 
HETATM 4796 O  O   . HOH L 6 .   ? 5.957   41.685  -14.563 1.00 20.68 ? 659 HOH A O   1 
HETATM 4797 O  O   . HOH L 6 .   ? -17.447 40.962  -22.176 1.00 25.82 ? 660 HOH A O   1 
HETATM 4798 O  O   . HOH L 6 .   ? 11.659  38.572  -12.318 1.00 38.16 ? 661 HOH A O   1 
HETATM 4799 O  O   . HOH L 6 .   ? -25.488 44.410  -25.987 1.00 48.25 ? 662 HOH A O   1 
HETATM 4800 O  O   . HOH L 6 .   ? -8.109  21.648  -49.922 1.00 37.04 ? 663 HOH A O   1 
HETATM 4801 O  O   . HOH L 6 .   ? 4.831   20.432  -37.390 1.00 21.32 ? 664 HOH A O   1 
HETATM 4802 O  O   . HOH L 6 .   ? 10.209  28.764  -11.556 1.00 23.38 ? 665 HOH A O   1 
HETATM 4803 O  O   . HOH L 6 .   ? -3.489  41.997  -38.977 1.00 21.93 ? 666 HOH A O   1 
HETATM 4804 O  O   . HOH L 6 .   ? 3.883   40.372  -9.903  1.00 23.07 ? 667 HOH A O   1 
HETATM 4805 O  O   . HOH L 6 .   ? -13.340 19.952  -39.939 1.00 28.98 ? 668 HOH A O   1 
HETATM 4806 O  O   . HOH L 6 .   ? -12.300 13.642  -31.889 1.00 28.79 ? 669 HOH A O   1 
HETATM 4807 O  O   . HOH L 6 .   ? 4.983   42.936  -16.916 1.00 11.66 ? 670 HOH A O   1 
HETATM 4808 O  O   . HOH L 6 .   ? 15.936  45.091  -13.328 1.00 31.61 ? 671 HOH A O   1 
HETATM 4809 O  O   . HOH L 6 .   ? 13.039  38.455  -34.382 1.00 23.61 ? 672 HOH A O   1 
HETATM 4810 O  O   . HOH L 6 .   ? -5.170  43.741  -37.942 1.00 28.47 ? 673 HOH A O   1 
HETATM 4811 O  O   . HOH L 6 .   ? -1.105  15.630  -39.868 1.00 22.93 ? 674 HOH A O   1 
HETATM 4812 O  O   . HOH L 6 .   ? -23.545 37.165  -31.025 1.00 26.94 ? 675 HOH A O   1 
HETATM 4813 O  O   . HOH L 6 .   ? -13.854 14.121  -29.944 1.00 27.77 ? 676 HOH A O   1 
HETATM 4814 O  O   . HOH L 6 .   ? -7.945  42.426  -47.373 1.00 27.11 ? 677 HOH A O   1 
HETATM 4815 O  O   . HOH L 6 .   ? 2.570   42.605  -12.954 1.00 30.07 ? 678 HOH A O   1 
HETATM 4816 O  O   . HOH L 6 .   ? 11.153  36.663  -35.351 1.00 21.90 ? 679 HOH A O   1 
HETATM 4817 O  O   . HOH L 6 .   ? -2.497  8.420   -27.003 1.00 44.20 ? 680 HOH A O   1 
HETATM 4818 O  O   . HOH L 6 .   ? 11.506  29.179  -36.934 1.00 23.52 ? 681 HOH A O   1 
HETATM 4819 O  O   . HOH L 6 .   ? -5.750  23.814  -50.364 1.00 19.72 ? 682 HOH A O   1 
HETATM 4820 O  O   . HOH L 6 .   ? 4.323   24.549  -47.282 1.00 23.30 ? 683 HOH A O   1 
HETATM 4821 O  O   . HOH L 6 .   ? -16.122 29.515  -23.356 1.00 32.97 ? 684 HOH A O   1 
HETATM 4822 O  O   . HOH L 6 .   ? -12.455 43.913  -37.938 1.00 28.11 ? 685 HOH A O   1 
HETATM 4823 O  O   . HOH L 6 .   ? -26.477 26.531  -37.782 1.00 26.91 ? 686 HOH A O   1 
HETATM 4824 O  O   . HOH L 6 .   ? 13.753  31.315  -33.206 1.00 26.31 ? 687 HOH A O   1 
HETATM 4825 O  O   . HOH L 6 .   ? 12.256  31.046  -35.189 1.00 27.18 ? 688 HOH A O   1 
HETATM 4826 O  O   . HOH L 6 .   ? 6.505   22.639  -33.601 1.00 19.57 ? 689 HOH A O   1 
HETATM 4827 O  O   . HOH L 6 .   ? -3.403  56.159  -32.035 1.00 21.59 ? 690 HOH A O   1 
HETATM 4828 O  O   . HOH L 6 .   ? -14.043 29.370  -8.898  1.00 24.50 ? 691 HOH A O   1 
HETATM 4829 O  O   . HOH L 6 .   ? 2.742   35.832  -4.797  1.00 20.82 ? 692 HOH A O   1 
HETATM 4830 O  O   . HOH L 6 .   ? -12.048 46.468  -43.794 1.00 31.38 ? 693 HOH A O   1 
HETATM 4831 O  O   . HOH L 6 .   ? 25.430  33.405  -22.175 1.00 46.01 ? 694 HOH A O   1 
HETATM 4832 O  O   . HOH L 6 .   ? 18.149  39.658  -10.489 1.00 24.86 ? 695 HOH A O   1 
HETATM 4833 O  O   . HOH L 6 .   ? -12.290 47.409  -14.857 1.00 30.22 ? 696 HOH A O   1 
HETATM 4834 O  O   . HOH L 6 .   ? 13.526  47.271  -20.741 1.00 27.27 ? 697 HOH A O   1 
HETATM 4835 O  O   . HOH L 6 .   ? -14.591 33.812  -19.808 1.00 39.40 ? 698 HOH A O   1 
HETATM 4836 O  O   . HOH L 6 .   ? -11.211 47.794  -17.294 1.00 19.77 ? 699 HOH A O   1 
HETATM 4837 O  O   . HOH L 6 .   ? -11.540 50.567  -17.030 1.00 25.65 ? 700 HOH A O   1 
# 
