data_5LLA
# 
_entry.id   5LLA 
# 
_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   5LLA         pdb_00005lla 10.2210/pdb5lla/pdb 
WWPDB D_1200000945 ?            ?                   
# 
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 2017-08-16 
2 'Structure model' 1 1 2017-11-29 
3 'Structure model' 1 2 2024-01-10 
# 
_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' 'Database references'    
2 3 'Structure model' 'Data collection'        
3 3 'Structure model' 'Database references'    
4 3 'Structure model' 'Derived calculations'   
5 3 'Structure model' 'Refinement description' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' pdbx_database_related         
2 3 'Structure model' chem_comp_atom                
3 3 'Structure model' chem_comp_bond                
4 3 'Structure model' database_2                    
5 3 'Structure model' diffrn_radiation_wavelength   
6 3 'Structure model' pdbx_initial_refinement_model 
7 3 '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  3 'Structure model' '_database_2.pdbx_DOI'                
2  3 'Structure model' '_database_2.pdbx_database_accession' 
3  3 'Structure model' '_struct_conn.pdbx_dist_value'        
4  3 'Structure model' '_struct_conn.ptnr1_auth_asym_id'     
5  3 'Structure model' '_struct_conn.ptnr1_auth_comp_id'     
6  3 'Structure model' '_struct_conn.ptnr1_auth_seq_id'      
7  3 'Structure model' '_struct_conn.ptnr1_label_asym_id'    
8  3 'Structure model' '_struct_conn.ptnr1_label_atom_id'    
9  3 'Structure model' '_struct_conn.ptnr1_label_comp_id'    
10 3 'Structure model' '_struct_conn.ptnr1_label_seq_id'     
11 3 'Structure model' '_struct_conn.ptnr2_auth_asym_id'     
12 3 'Structure model' '_struct_conn.ptnr2_auth_comp_id'     
13 3 'Structure model' '_struct_conn.ptnr2_auth_seq_id'      
14 3 'Structure model' '_struct_conn.ptnr2_label_asym_id'    
15 3 'Structure model' '_struct_conn.ptnr2_label_atom_id'    
16 3 '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                        5LLA 
_pdbx_database_status.recvd_initial_deposition_date   2016-07-27 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_nmr_data            ? 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.details 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
PDB . 5LL4 unspecified 
PDB . 5LL5 unspecified 
PDB . 5LL9 unspecified 
# 
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                   DE 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Chemistryselect 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2365-6549 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
'Combinatorial Design of Isoform-Selective N-Alkylated Benzimidazole-Based Inhibitors of Carbonic Anhydrases' 
_citation.year                      2017 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1002/slct.201700531 
_citation.pdbx_database_id_PubMed   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Capkauskaite, E.'   1 ? 
primary 'Linkuviene, V.'     2 ? 
primary 'Smirnov, A.'        3 ? 
primary 'Milinaviciute, G.'  4 ? 
primary 'Timm, D.'           5 ? 
primary 'Kasiliauskaite, 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   ?       ? ? ? 
3 non-polymer syn '4-[2-(benzimidazol-1-yl)ethanoyl]-2-chloranyl-benzenesulfonamide' 349.792   2   ?       ? ? ? 
4 non-polymer syn 'CITRIC ACID'                                                      192.124   2   ?       ? ? ? 
5 non-polymer syn 1,2-ETHANEDIOL                                                     62.068    2   ?       ? ? ? 
6 water       nat water                                                              18.015    550 ?       ? ? ? 
# 
_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 '4-[2-(benzimidazol-1-yl)ethanoyl]-2-chloranyl-benzenesulfonamide' 6YQ 
4 'CITRIC ACID'                                                      CIT 
5 1,2-ETHANEDIOL                                                     EDO 
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' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               'BL21(DE3)' 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pET15b 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
6YQ non-polymer         . '4-[2-(benzimidazol-1-yl)ethanoyl]-2-chloranyl-benzenesulfonamide' ?                 
'C15 H12 Cl N3 O3 S' 349.792 
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  
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 2   ZN  ZN  B . 
D 3 6YQ 1   302 1   6YQ E16 B . 
E 4 CIT 1   303 1   CIT CIT B . 
F 5 EDO 1   304 3   EDO EDO B . 
G 2 ZN  1   301 1   ZN  ZN  A . 
H 3 6YQ 1   302 2   6YQ E16 A . 
I 4 CIT 1   303 2   CIT CIT A . 
J 5 EDO 1   304 4   EDO EDO A . 
K 6 HOH 1   401 487 HOH HOH B . 
K 6 HOH 2   402 62  HOH HOH B . 
K 6 HOH 3   403 51  HOH HOH B . 
K 6 HOH 4   404 54  HOH HOH B . 
K 6 HOH 5   405 157 HOH HOH B . 
K 6 HOH 6   406 488 HOH HOH B . 
K 6 HOH 7   407 43  HOH HOH B . 
K 6 HOH 8   408 541 HOH HOH B . 
K 6 HOH 9   409 165 HOH HOH B . 
K 6 HOH 10  410 486 HOH HOH B . 
K 6 HOH 11  411 221 HOH HOH B . 
K 6 HOH 12  412 152 HOH HOH B . 
K 6 HOH 13  413 491 HOH HOH B . 
K 6 HOH 14  414 103 HOH HOH B . 
K 6 HOH 15  415 394 HOH HOH B . 
K 6 HOH 16  416 489 HOH HOH B . 
K 6 HOH 17  417 415 HOH HOH B . 
K 6 HOH 18  418 110 HOH HOH B . 
K 6 HOH 19  419 434 HOH HOH B . 
K 6 HOH 20  420 387 HOH HOH B . 
K 6 HOH 21  421 245 HOH HOH B . 
K 6 HOH 22  422 426 HOH HOH B . 
K 6 HOH 23  423 48  HOH HOH B . 
K 6 HOH 24  424 154 HOH HOH B . 
K 6 HOH 25  425 57  HOH HOH B . 
K 6 HOH 26  426 359 HOH HOH B . 
K 6 HOH 27  427 72  HOH HOH B . 
K 6 HOH 28  428 25  HOH HOH B . 
K 6 HOH 29  429 416 HOH HOH B . 
K 6 HOH 30  430 41  HOH HOH B . 
K 6 HOH 31  431 492 HOH HOH B . 
K 6 HOH 32  432 187 HOH HOH B . 
K 6 HOH 33  433 274 HOH HOH B . 
K 6 HOH 34  434 243 HOH HOH B . 
K 6 HOH 35  435 58  HOH HOH B . 
K 6 HOH 36  436 167 HOH HOH B . 
K 6 HOH 37  437 193 HOH HOH B . 
K 6 HOH 38  438 534 HOH HOH B . 
K 6 HOH 39  439 246 HOH HOH B . 
K 6 HOH 40  440 346 HOH HOH B . 
K 6 HOH 41  441 106 HOH HOH B . 
K 6 HOH 42  442 11  HOH HOH B . 
K 6 HOH 43  443 82  HOH HOH B . 
K 6 HOH 44  444 109 HOH HOH B . 
K 6 HOH 45  445 93  HOH HOH B . 
K 6 HOH 46  446 234 HOH HOH B . 
K 6 HOH 47  447 20  HOH HOH B . 
K 6 HOH 48  448 535 HOH HOH B . 
K 6 HOH 49  449 101 HOH HOH B . 
K 6 HOH 50  450 39  HOH HOH B . 
K 6 HOH 51  451 382 HOH HOH B . 
K 6 HOH 52  452 497 HOH HOH B . 
K 6 HOH 53  453 388 HOH HOH B . 
K 6 HOH 54  454 231 HOH HOH B . 
K 6 HOH 55  455 155 HOH HOH B . 
K 6 HOH 56  456 482 HOH HOH B . 
K 6 HOH 57  457 540 HOH HOH B . 
K 6 HOH 58  458 148 HOH HOH B . 
K 6 HOH 59  459 392 HOH HOH B . 
K 6 HOH 60  460 433 HOH HOH B . 
K 6 HOH 61  461 213 HOH HOH B . 
K 6 HOH 62  462 337 HOH HOH B . 
K 6 HOH 63  463 68  HOH HOH B . 
K 6 HOH 64  464 277 HOH HOH B . 
K 6 HOH 65  465 104 HOH HOH B . 
K 6 HOH 66  466 34  HOH HOH B . 
K 6 HOH 67  467 21  HOH HOH B . 
K 6 HOH 68  468 14  HOH HOH B . 
K 6 HOH 69  469 56  HOH HOH B . 
K 6 HOH 70  470 172 HOH HOH B . 
K 6 HOH 71  471 216 HOH HOH B . 
K 6 HOH 72  472 186 HOH HOH B . 
K 6 HOH 73  473 218 HOH HOH B . 
K 6 HOH 74  474 173 HOH HOH B . 
K 6 HOH 75  475 518 HOH HOH B . 
K 6 HOH 76  476 12  HOH HOH B . 
K 6 HOH 77  477 113 HOH HOH B . 
K 6 HOH 78  478 71  HOH HOH B . 
K 6 HOH 79  479 349 HOH HOH B . 
K 6 HOH 80  480 395 HOH HOH B . 
K 6 HOH 81  481 208 HOH HOH B . 
K 6 HOH 82  482 79  HOH HOH B . 
K 6 HOH 83  483 237 HOH HOH B . 
K 6 HOH 84  484 525 HOH HOH B . 
K 6 HOH 85  485 379 HOH HOH B . 
K 6 HOH 86  486 100 HOH HOH B . 
K 6 HOH 87  487 404 HOH HOH B . 
K 6 HOH 88  488 126 HOH HOH B . 
K 6 HOH 89  489 80  HOH HOH B . 
K 6 HOH 90  490 65  HOH HOH B . 
K 6 HOH 91  491 421 HOH HOH B . 
K 6 HOH 92  492 180 HOH HOH B . 
K 6 HOH 93  493 40  HOH HOH B . 
K 6 HOH 94  494 232 HOH HOH B . 
K 6 HOH 95  495 212 HOH HOH B . 
K 6 HOH 96  496 24  HOH HOH B . 
K 6 HOH 97  497 191 HOH HOH B . 
K 6 HOH 98  498 50  HOH HOH B . 
K 6 HOH 99  499 399 HOH HOH B . 
K 6 HOH 100 500 350 HOH HOH B . 
K 6 HOH 101 501 149 HOH HOH B . 
K 6 HOH 102 502 131 HOH HOH B . 
K 6 HOH 103 503 312 HOH HOH B . 
K 6 HOH 104 504 296 HOH HOH B . 
K 6 HOH 105 505 67  HOH HOH B . 
K 6 HOH 106 506 83  HOH HOH B . 
K 6 HOH 107 507 222 HOH HOH B . 
K 6 HOH 108 508 31  HOH HOH B . 
K 6 HOH 109 509 35  HOH HOH B . 
K 6 HOH 110 510 485 HOH HOH B . 
K 6 HOH 111 511 9   HOH HOH B . 
K 6 HOH 112 512 230 HOH HOH B . 
K 6 HOH 113 513 33  HOH HOH B . 
K 6 HOH 114 514 37  HOH HOH B . 
K 6 HOH 115 515 202 HOH HOH B . 
K 6 HOH 116 516 95  HOH HOH B . 
K 6 HOH 117 517 248 HOH HOH B . 
K 6 HOH 118 518 183 HOH HOH B . 
K 6 HOH 119 519 86  HOH HOH B . 
K 6 HOH 120 520 28  HOH HOH B . 
K 6 HOH 121 521 94  HOH HOH B . 
K 6 HOH 122 522 390 HOH HOH B . 
K 6 HOH 123 523 32  HOH HOH B . 
K 6 HOH 124 524 8   HOH HOH B . 
K 6 HOH 125 525 78  HOH HOH B . 
K 6 HOH 126 526 200 HOH HOH B . 
K 6 HOH 127 527 23  HOH HOH B . 
K 6 HOH 128 528 174 HOH HOH B . 
K 6 HOH 129 529 215 HOH HOH B . 
K 6 HOH 130 530 539 HOH HOH B . 
K 6 HOH 131 531 7   HOH HOH B . 
K 6 HOH 132 532 258 HOH HOH B . 
K 6 HOH 133 533 351 HOH HOH B . 
K 6 HOH 134 534 64  HOH HOH B . 
K 6 HOH 135 535 519 HOH HOH B . 
K 6 HOH 136 536 63  HOH HOH B . 
K 6 HOH 137 537 259 HOH HOH B . 
K 6 HOH 138 538 22  HOH HOH B . 
K 6 HOH 139 539 38  HOH HOH B . 
K 6 HOH 140 540 402 HOH HOH B . 
K 6 HOH 141 541 135 HOH HOH B . 
K 6 HOH 142 542 273 HOH HOH B . 
K 6 HOH 143 543 207 HOH HOH B . 
K 6 HOH 144 544 430 HOH HOH B . 
K 6 HOH 145 545 320 HOH HOH B . 
K 6 HOH 146 546 431 HOH HOH B . 
K 6 HOH 147 547 90  HOH HOH B . 
K 6 HOH 148 548 297 HOH HOH B . 
K 6 HOH 149 549 26  HOH HOH B . 
K 6 HOH 150 550 480 HOH HOH B . 
K 6 HOH 151 551 3   HOH HOH B . 
K 6 HOH 152 552 385 HOH HOH B . 
K 6 HOH 153 553 490 HOH HOH B . 
K 6 HOH 154 554 30  HOH HOH B . 
K 6 HOH 155 555 418 HOH HOH B . 
K 6 HOH 156 556 278 HOH HOH B . 
K 6 HOH 157 557 536 HOH HOH B . 
K 6 HOH 158 558 15  HOH HOH B . 
K 6 HOH 159 559 2   HOH HOH B . 
K 6 HOH 160 560 236 HOH HOH B . 
K 6 HOH 161 561 226 HOH HOH B . 
K 6 HOH 162 562 224 HOH HOH B . 
K 6 HOH 163 563 315 HOH HOH B . 
K 6 HOH 164 564 252 HOH HOH B . 
K 6 HOH 165 565 300 HOH HOH B . 
K 6 HOH 166 566 182 HOH HOH B . 
K 6 HOH 167 567 363 HOH HOH B . 
K 6 HOH 168 568 47  HOH HOH B . 
K 6 HOH 169 569 283 HOH HOH B . 
K 6 HOH 170 570 210 HOH HOH B . 
K 6 HOH 171 571 130 HOH HOH B . 
K 6 HOH 172 572 279 HOH HOH B . 
K 6 HOH 173 573 443 HOH HOH B . 
K 6 HOH 174 574 282 HOH HOH B . 
K 6 HOH 175 575 129 HOH HOH B . 
K 6 HOH 176 576 108 HOH HOH B . 
K 6 HOH 177 577 419 HOH HOH B . 
K 6 HOH 178 578 151 HOH HOH B . 
K 6 HOH 179 579 143 HOH HOH B . 
K 6 HOH 180 580 205 HOH HOH B . 
K 6 HOH 181 581 73  HOH HOH B . 
K 6 HOH 182 582 201 HOH HOH B . 
K 6 HOH 183 583 133 HOH HOH B . 
K 6 HOH 184 584 325 HOH HOH B . 
K 6 HOH 185 585 268 HOH HOH B . 
K 6 HOH 186 586 287 HOH HOH B . 
K 6 HOH 187 587 189 HOH HOH B . 
K 6 HOH 188 588 117 HOH HOH B . 
K 6 HOH 189 589 327 HOH HOH B . 
K 6 HOH 190 590 168 HOH HOH B . 
K 6 HOH 191 591 513 HOH HOH B . 
K 6 HOH 192 592 481 HOH HOH B . 
K 6 HOH 193 593 440 HOH HOH B . 
K 6 HOH 194 594 317 HOH HOH B . 
K 6 HOH 195 595 515 HOH HOH B . 
K 6 HOH 196 596 264 HOH HOH B . 
K 6 HOH 197 597 66  HOH HOH B . 
K 6 HOH 198 598 139 HOH HOH B . 
K 6 HOH 199 599 112 HOH HOH B . 
K 6 HOH 200 600 422 HOH HOH B . 
K 6 HOH 201 601 199 HOH HOH B . 
K 6 HOH 202 602 383 HOH HOH B . 
K 6 HOH 203 603 380 HOH HOH B . 
K 6 HOH 204 604 194 HOH HOH B . 
K 6 HOH 205 605 530 HOH HOH B . 
K 6 HOH 206 606 233 HOH HOH B . 
K 6 HOH 207 607 124 HOH HOH B . 
K 6 HOH 208 608 520 HOH HOH B . 
K 6 HOH 209 609 401 HOH HOH B . 
K 6 HOH 210 610 147 HOH HOH B . 
K 6 HOH 211 611 227 HOH HOH B . 
K 6 HOH 212 612 429 HOH HOH B . 
K 6 HOH 213 613 98  HOH HOH B . 
K 6 HOH 214 614 272 HOH HOH B . 
K 6 HOH 215 615 381 HOH HOH B . 
K 6 HOH 216 616 427 HOH HOH B . 
K 6 HOH 217 617 360 HOH HOH B . 
K 6 HOH 218 618 407 HOH HOH B . 
K 6 HOH 219 619 484 HOH HOH B . 
K 6 HOH 220 620 241 HOH HOH B . 
K 6 HOH 221 621 432 HOH HOH B . 
K 6 HOH 222 622 495 HOH HOH B . 
K 6 HOH 223 623 406 HOH HOH B . 
K 6 HOH 224 624 138 HOH HOH B . 
K 6 HOH 225 625 142 HOH HOH B . 
K 6 HOH 226 626 413 HOH HOH B . 
K 6 HOH 227 627 533 HOH HOH B . 
K 6 HOH 228 628 496 HOH HOH B . 
K 6 HOH 229 629 365 HOH HOH B . 
K 6 HOH 230 630 494 HOH HOH B . 
K 6 HOH 231 631 478 HOH HOH B . 
K 6 HOH 232 632 439 HOH HOH B . 
K 6 HOH 233 633 393 HOH HOH B . 
K 6 HOH 234 634 290 HOH HOH B . 
K 6 HOH 235 635 414 HOH HOH B . 
K 6 HOH 236 636 262 HOH HOH B . 
K 6 HOH 237 637 345 HOH HOH B . 
K 6 HOH 238 638 318 HOH HOH B . 
K 6 HOH 239 639 225 HOH HOH B . 
K 6 HOH 240 640 403 HOH HOH B . 
K 6 HOH 241 641 206 HOH HOH B . 
K 6 HOH 242 642 417 HOH HOH B . 
K 6 HOH 243 643 361 HOH HOH B . 
K 6 HOH 244 644 119 HOH HOH B . 
K 6 HOH 245 645 441 HOH HOH B . 
K 6 HOH 246 646 184 HOH HOH B . 
K 6 HOH 247 647 146 HOH HOH B . 
K 6 HOH 248 648 339 HOH HOH B . 
K 6 HOH 249 649 479 HOH HOH B . 
K 6 HOH 250 650 309 HOH HOH B . 
K 6 HOH 251 651 400 HOH HOH B . 
K 6 HOH 252 652 444 HOH HOH B . 
K 6 HOH 253 653 516 HOH HOH B . 
K 6 HOH 254 654 428 HOH HOH B . 
K 6 HOH 255 655 391 HOH HOH B . 
K 6 HOH 256 656 389 HOH HOH B . 
K 6 HOH 257 657 328 HOH HOH B . 
K 6 HOH 258 658 340 HOH HOH B . 
K 6 HOH 259 659 410 HOH HOH B . 
K 6 HOH 260 660 84  HOH HOH B . 
K 6 HOH 261 661 537 HOH HOH B . 
K 6 HOH 262 662 306 HOH HOH B . 
K 6 HOH 263 663 352 HOH HOH B . 
K 6 HOH 264 664 386 HOH HOH B . 
K 6 HOH 265 665 281 HOH HOH B . 
K 6 HOH 266 666 323 HOH HOH B . 
K 6 HOH 267 667 493 HOH HOH B . 
K 6 HOH 268 668 271 HOH HOH B . 
K 6 HOH 269 669 384 HOH HOH B . 
K 6 HOH 270 670 408 HOH HOH B . 
K 6 HOH 271 671 435 HOH HOH B . 
K 6 HOH 272 672 247 HOH HOH B . 
K 6 HOH 273 673 522 HOH HOH B . 
K 6 HOH 274 674 412 HOH HOH B . 
K 6 HOH 275 675 150 HOH HOH B . 
K 6 HOH 276 676 240 HOH HOH B . 
K 6 HOH 277 677 378 HOH HOH B . 
K 6 HOH 278 678 341 HOH HOH B . 
K 6 HOH 279 679 314 HOH HOH B . 
K 6 HOH 280 680 256 HOH HOH B . 
K 6 HOH 281 681 538 HOH HOH B . 
K 6 HOH 282 682 512 HOH HOH B . 
K 6 HOH 283 683 517 HOH HOH B . 
K 6 HOH 284 684 542 HOH HOH B . 
K 6 HOH 285 685 308 HOH HOH B . 
K 6 HOH 286 686 333 HOH HOH B . 
K 6 HOH 287 687 344 HOH HOH B . 
K 6 HOH 288 688 464 HOH HOH B . 
K 6 HOH 289 689 336 HOH HOH B . 
K 6 HOH 290 690 276 HOH HOH B . 
L 6 HOH 1   401 299 HOH HOH A . 
L 6 HOH 2   402 528 HOH HOH A . 
L 6 HOH 3   403 288 HOH HOH A . 
L 6 HOH 4   404 449 HOH HOH A . 
L 6 HOH 5   405 107 HOH HOH A . 
L 6 HOH 6   406 249 HOH HOH A . 
L 6 HOH 7   407 446 HOH HOH A . 
L 6 HOH 8   408 284 HOH HOH A . 
L 6 HOH 9   409 76  HOH HOH A . 
L 6 HOH 10  410 524 HOH HOH A . 
L 6 HOH 11  411 244 HOH HOH A . 
L 6 HOH 12  412 457 HOH HOH A . 
L 6 HOH 13  413 367 HOH HOH A . 
L 6 HOH 14  414 250 HOH HOH A . 
L 6 HOH 15  415 228 HOH HOH A . 
L 6 HOH 16  416 114 HOH HOH A . 
L 6 HOH 17  417 166 HOH HOH A . 
L 6 HOH 18  418 136 HOH HOH A . 
L 6 HOH 19  419 425 HOH HOH A . 
L 6 HOH 20  420 501 HOH HOH A . 
L 6 HOH 21  421 134 HOH HOH A . 
L 6 HOH 22  422 451 HOH HOH A . 
L 6 HOH 23  423 348 HOH HOH A . 
L 6 HOH 24  424 462 HOH HOH A . 
L 6 HOH 25  425 354 HOH HOH A . 
L 6 HOH 26  426 81  HOH HOH A . 
L 6 HOH 27  427 529 HOH HOH A . 
L 6 HOH 28  428 303 HOH HOH A . 
L 6 HOH 29  429 87  HOH HOH A . 
L 6 HOH 30  430 330 HOH HOH A . 
L 6 HOH 31  431 438 HOH HOH A . 
L 6 HOH 32  432 140 HOH HOH A . 
L 6 HOH 33  433 75  HOH HOH A . 
L 6 HOH 34  434 158 HOH HOH A . 
L 6 HOH 35  435 298 HOH HOH A . 
L 6 HOH 36  436 121 HOH HOH A . 
L 6 HOH 37  437 178 HOH HOH A . 
L 6 HOH 38  438 411 HOH HOH A . 
L 6 HOH 39  439 223 HOH HOH A . 
L 6 HOH 40  440 153 HOH HOH A . 
L 6 HOH 41  441 448 HOH HOH A . 
L 6 HOH 42  442 96  HOH HOH A . 
L 6 HOH 43  443 177 HOH HOH A . 
L 6 HOH 44  444 137 HOH HOH A . 
L 6 HOH 45  445 61  HOH HOH A . 
L 6 HOH 46  446 159 HOH HOH A . 
L 6 HOH 47  447 305 HOH HOH A . 
L 6 HOH 48  448 10  HOH HOH A . 
L 6 HOH 49  449 332 HOH HOH A . 
L 6 HOH 50  450 474 HOH HOH A . 
L 6 HOH 51  451 466 HOH HOH A . 
L 6 HOH 52  452 471 HOH HOH A . 
L 6 HOH 53  453 204 HOH HOH A . 
L 6 HOH 54  454 514 HOH HOH A . 
L 6 HOH 55  455 329 HOH HOH A . 
L 6 HOH 56  456 74  HOH HOH A . 
L 6 HOH 57  457 219 HOH HOH A . 
L 6 HOH 58  458 19  HOH HOH A . 
L 6 HOH 59  459 286 HOH HOH A . 
L 6 HOH 60  460 13  HOH HOH A . 
L 6 HOH 61  461 442 HOH HOH A . 
L 6 HOH 62  462 331 HOH HOH A . 
L 6 HOH 63  463 55  HOH HOH A . 
L 6 HOH 64  464 4   HOH HOH A . 
L 6 HOH 65  465 5   HOH HOH A . 
L 6 HOH 66  466 465 HOH HOH A . 
L 6 HOH 67  467 59  HOH HOH A . 
L 6 HOH 68  468 128 HOH HOH A . 
L 6 HOH 69  469 156 HOH HOH A . 
L 6 HOH 70  470 370 HOH HOH A . 
L 6 HOH 71  471 120 HOH HOH A . 
L 6 HOH 72  472 49  HOH HOH A . 
L 6 HOH 73  473 405 HOH HOH A . 
L 6 HOH 74  474 97  HOH HOH A . 
L 6 HOH 75  475 251 HOH HOH A . 
L 6 HOH 76  476 88  HOH HOH A . 
L 6 HOH 77  477 353 HOH HOH A . 
L 6 HOH 78  478 188 HOH HOH A . 
L 6 HOH 79  479 36  HOH HOH A . 
L 6 HOH 80  480 122 HOH HOH A . 
L 6 HOH 81  481 115 HOH HOH A . 
L 6 HOH 82  482 69  HOH HOH A . 
L 6 HOH 83  483 358 HOH HOH A . 
L 6 HOH 84  484 263 HOH HOH A . 
L 6 HOH 85  485 293 HOH HOH A . 
L 6 HOH 86  486 190 HOH HOH A . 
L 6 HOH 87  487 506 HOH HOH A . 
L 6 HOH 88  488 302 HOH HOH A . 
L 6 HOH 89  489 366 HOH HOH A . 
L 6 HOH 90  490 132 HOH HOH A . 
L 6 HOH 91  491 161 HOH HOH A . 
L 6 HOH 92  492 211 HOH HOH A . 
L 6 HOH 93  493 92  HOH HOH A . 
L 6 HOH 94  494 265 HOH HOH A . 
L 6 HOH 95  495 257 HOH HOH A . 
L 6 HOH 96  496 292 HOH HOH A . 
L 6 HOH 97  497 472 HOH HOH A . 
L 6 HOH 98  498 17  HOH HOH A . 
L 6 HOH 99  499 483 HOH HOH A . 
L 6 HOH 100 500 319 HOH HOH A . 
L 6 HOH 101 501 195 HOH HOH A . 
L 6 HOH 102 502 18  HOH HOH A . 
L 6 HOH 103 503 238 HOH HOH A . 
L 6 HOH 104 504 295 HOH HOH A . 
L 6 HOH 105 505 16  HOH HOH A . 
L 6 HOH 106 506 44  HOH HOH A . 
L 6 HOH 107 507 52  HOH HOH A . 
L 6 HOH 108 508 459 HOH HOH A . 
L 6 HOH 109 509 209 HOH HOH A . 
L 6 HOH 110 510 162 HOH HOH A . 
L 6 HOH 111 511 6   HOH HOH A . 
L 6 HOH 112 512 500 HOH HOH A . 
L 6 HOH 113 513 356 HOH HOH A . 
L 6 HOH 114 514 269 HOH HOH A . 
L 6 HOH 115 515 118 HOH HOH A . 
L 6 HOH 116 516 470 HOH HOH A . 
L 6 HOH 117 517 548 HOH HOH A . 
L 6 HOH 118 518 372 HOH HOH A . 
L 6 HOH 119 519 326 HOH HOH A . 
L 6 HOH 120 520 436 HOH HOH A . 
L 6 HOH 121 521 362 HOH HOH A . 
L 6 HOH 122 522 342 HOH HOH A . 
L 6 HOH 123 523 267 HOH HOH A . 
L 6 HOH 124 524 220 HOH HOH A . 
L 6 HOH 125 525 253 HOH HOH A . 
L 6 HOH 126 526 203 HOH HOH A . 
L 6 HOH 127 527 454 HOH HOH A . 
L 6 HOH 128 528 105 HOH HOH A . 
L 6 HOH 129 529 235 HOH HOH A . 
L 6 HOH 130 530 197 HOH HOH A . 
L 6 HOH 131 531 373 HOH HOH A . 
L 6 HOH 132 532 396 HOH HOH A . 
L 6 HOH 133 533 544 HOH HOH A . 
L 6 HOH 134 534 450 HOH HOH A . 
L 6 HOH 135 535 527 HOH HOH A . 
L 6 HOH 136 536 291 HOH HOH A . 
L 6 HOH 137 537 229 HOH HOH A . 
L 6 HOH 138 538 355 HOH HOH A . 
L 6 HOH 139 539 469 HOH HOH A . 
L 6 HOH 140 540 145 HOH HOH A . 
L 6 HOH 141 541 89  HOH HOH A . 
L 6 HOH 142 542 175 HOH HOH A . 
L 6 HOH 143 543 27  HOH HOH A . 
L 6 HOH 144 544 46  HOH HOH A . 
L 6 HOH 145 545 102 HOH HOH A . 
L 6 HOH 146 546 545 HOH HOH A . 
L 6 HOH 147 547 170 HOH HOH A . 
L 6 HOH 148 548 160 HOH HOH A . 
L 6 HOH 149 549 116 HOH HOH A . 
L 6 HOH 150 550 127 HOH HOH A . 
L 6 HOH 151 551 503 HOH HOH A . 
L 6 HOH 152 552 42  HOH HOH A . 
L 6 HOH 153 553 275 HOH HOH A . 
L 6 HOH 154 554 255 HOH HOH A . 
L 6 HOH 155 555 531 HOH HOH A . 
L 6 HOH 156 556 294 HOH HOH A . 
L 6 HOH 157 557 509 HOH HOH A . 
L 6 HOH 158 558 144 HOH HOH A . 
L 6 HOH 159 559 198 HOH HOH A . 
L 6 HOH 160 560 1   HOH HOH A . 
L 6 HOH 161 561 375 HOH HOH A . 
L 6 HOH 162 562 452 HOH HOH A . 
L 6 HOH 163 563 242 HOH HOH A . 
L 6 HOH 164 564 169 HOH HOH A . 
L 6 HOH 165 565 60  HOH HOH A . 
L 6 HOH 166 566 307 HOH HOH A . 
L 6 HOH 167 567 192 HOH HOH A . 
L 6 HOH 168 568 468 HOH HOH A . 
L 6 HOH 169 569 460 HOH HOH A . 
L 6 HOH 170 570 364 HOH HOH A . 
L 6 HOH 171 571 176 HOH HOH A . 
L 6 HOH 172 572 409 HOH HOH A . 
L 6 HOH 173 573 123 HOH HOH A . 
L 6 HOH 174 574 77  HOH HOH A . 
L 6 HOH 175 575 310 HOH HOH A . 
L 6 HOH 176 576 111 HOH HOH A . 
L 6 HOH 177 577 377 HOH HOH A . 
L 6 HOH 178 578 260 HOH HOH A . 
L 6 HOH 179 579 91  HOH HOH A . 
L 6 HOH 180 580 321 HOH HOH A . 
L 6 HOH 181 581 357 HOH HOH A . 
L 6 HOH 182 582 456 HOH HOH A . 
L 6 HOH 183 583 502 HOH HOH A . 
L 6 HOH 184 584 163 HOH HOH A . 
L 6 HOH 185 585 29  HOH HOH A . 
L 6 HOH 186 586 141 HOH HOH A . 
L 6 HOH 187 587 376 HOH HOH A . 
L 6 HOH 188 588 164 HOH HOH A . 
L 6 HOH 189 589 217 HOH HOH A . 
L 6 HOH 190 590 125 HOH HOH A . 
L 6 HOH 191 591 324 HOH HOH A . 
L 6 HOH 192 592 546 HOH HOH A . 
L 6 HOH 193 593 374 HOH HOH A . 
L 6 HOH 194 594 313 HOH HOH A . 
L 6 HOH 195 595 547 HOH HOH A . 
L 6 HOH 196 596 85  HOH HOH A . 
L 6 HOH 197 597 467 HOH HOH A . 
L 6 HOH 198 598 179 HOH HOH A . 
L 6 HOH 199 599 70  HOH HOH A . 
L 6 HOH 200 600 543 HOH HOH A . 
L 6 HOH 201 601 99  HOH HOH A . 
L 6 HOH 202 602 505 HOH HOH A . 
L 6 HOH 203 603 45  HOH HOH A . 
L 6 HOH 204 604 437 HOH HOH A . 
L 6 HOH 205 605 181 HOH HOH A . 
L 6 HOH 206 606 266 HOH HOH A . 
L 6 HOH 207 607 196 HOH HOH A . 
L 6 HOH 208 608 185 HOH HOH A . 
L 6 HOH 209 609 261 HOH HOH A . 
L 6 HOH 210 610 477 HOH HOH A . 
L 6 HOH 211 611 476 HOH HOH A . 
L 6 HOH 212 612 347 HOH HOH A . 
L 6 HOH 213 613 550 HOH HOH A . 
L 6 HOH 214 614 504 HOH HOH A . 
L 6 HOH 215 615 508 HOH HOH A . 
L 6 HOH 216 616 270 HOH HOH A . 
L 6 HOH 217 617 311 HOH HOH A . 
L 6 HOH 218 618 53  HOH HOH A . 
L 6 HOH 219 619 322 HOH HOH A . 
L 6 HOH 220 620 463 HOH HOH A . 
L 6 HOH 221 621 445 HOH HOH A . 
L 6 HOH 222 622 521 HOH HOH A . 
L 6 HOH 223 623 458 HOH HOH A . 
L 6 HOH 224 624 239 HOH HOH A . 
L 6 HOH 225 625 304 HOH HOH A . 
L 6 HOH 226 626 549 HOH HOH A . 
L 6 HOH 227 627 424 HOH HOH A . 
L 6 HOH 228 628 371 HOH HOH A . 
L 6 HOH 229 629 285 HOH HOH A . 
L 6 HOH 230 630 423 HOH HOH A . 
L 6 HOH 231 631 316 HOH HOH A . 
L 6 HOH 232 632 171 HOH HOH A . 
L 6 HOH 233 633 368 HOH HOH A . 
L 6 HOH 234 634 473 HOH HOH A . 
L 6 HOH 235 635 334 HOH HOH A . 
L 6 HOH 236 636 397 HOH HOH A . 
L 6 HOH 237 637 461 HOH HOH A . 
L 6 HOH 238 638 301 HOH HOH A . 
L 6 HOH 239 639 338 HOH HOH A . 
L 6 HOH 240 640 447 HOH HOH A . 
L 6 HOH 241 641 420 HOH HOH A . 
L 6 HOH 242 642 499 HOH HOH A . 
L 6 HOH 243 643 510 HOH HOH A . 
L 6 HOH 244 644 526 HOH HOH A . 
L 6 HOH 245 645 214 HOH HOH A . 
L 6 HOH 246 646 475 HOH HOH A . 
L 6 HOH 247 647 343 HOH HOH A . 
L 6 HOH 248 648 280 HOH HOH A . 
L 6 HOH 249 649 455 HOH HOH A . 
L 6 HOH 250 650 453 HOH HOH A . 
L 6 HOH 251 651 532 HOH HOH A . 
L 6 HOH 252 652 254 HOH HOH A . 
L 6 HOH 253 653 398 HOH HOH A . 
L 6 HOH 254 654 289 HOH HOH A . 
L 6 HOH 255 655 369 HOH HOH A . 
L 6 HOH 256 656 511 HOH HOH A . 
L 6 HOH 257 657 335 HOH HOH A . 
L 6 HOH 258 658 523 HOH HOH A . 
L 6 HOH 259 659 498 HOH HOH A . 
L 6 HOH 260 660 507 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      ? ? ? 5.6.0117 1 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? SCALA       ? ? ? 3.3.20   2 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.20     3 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? XDS         ? ? ? .        4 
? phasing           ? ? ? ? ? ? ? ? ? ? ? MOLREP      ? ? ? .        5 
# 
_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                     5LLA 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     56.023 
_cell.length_a_esd                 ? 
_cell.length_b                     57.276 
_cell.length_b_esd                 ? 
_cell.length_c                     159.284 
_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                         5LLA 
_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                   5LLA 
_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            2.16 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         42.99 
_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              0.170 
_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          EVAPORATION 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp            291 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
'Crystallization buffer: 0.1M ammonium citrate (pH 7), 0.1M sodium acetate (pH 4.5) and 26% PEG3350' 
_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                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2012-11-30 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.826606 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'PETRA III, EMBL c/o DESY BEAMLINE P13 (MX1)' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.826606 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'P13 (MX1)' 
_diffrn_source.pdbx_synchrotron_site       'PETRA III, EMBL c/o DESY' 
# 
_reflns.B_iso_Wilson_estimate            ? 
_reflns.entry_id                         5LLA 
_reflns.data_reduction_details           ? 
_reflns.data_reduction_method            ? 
_reflns.d_resolution_high                1.500 
_reflns.d_resolution_low                 159.284 
_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                       82297 
_reflns.number_obs                       82297 
_reflns.observed_criterion               ? 
_reflns.observed_criterion_F_max         ? 
_reflns.observed_criterion_F_min         ? 
_reflns.observed_criterion_I_max         ? 
_reflns.observed_criterion_I_min         ? 
_reflns.observed_criterion_sigma_F       ? 
_reflns.observed_criterion_sigma_I       ? 
_reflns.percent_possible_obs             99.300 
_reflns.R_free_details                   ? 
_reflns.Rmerge_F_all                     ? 
_reflns.Rmerge_F_obs                     ? 
_reflns.Friedel_coverage                 ? 
_reflns.number_gt                        ? 
_reflns.threshold_expression             ? 
_reflns.pdbx_redundancy                  6.400 
_reflns.pdbx_Rmerge_I_obs                ? 
_reflns.pdbx_Rmerge_I_all                ? 
_reflns.pdbx_Rsym_value                  0.033 
_reflns.pdbx_netI_over_av_sigmaI         15.123 
_reflns.pdbx_netI_over_sigmaI            26.800 
_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                  0.040 
_reflns.pdbx_Rpim_I_all                  0.016 
_reflns.pdbx_d_opt                       ? 
_reflns.pdbx_number_measured_all         524723 
_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 
1.500 1.580   ? 2.200  ? ? ? ? ? 99.200 ? ? ? ? 0.358 ? ? ? ? ? ? ? ? 6.600 ? ? ? ? ? ? ? 1  1 ? ? 
1.580 1.680   ? 3.000  ? ? ? ? ? 99.400 ? ? ? ? 0.249 ? ? ? ? ? ? ? ? 6.400 ? ? ? ? ? ? ? 2  1 ? ? 
1.680 1.790   ? 4.900  ? ? ? ? ? 99.300 ? ? ? ? 0.151 ? ? ? ? ? ? ? ? 6.400 ? ? ? ? ? ? ? 3  1 ? ? 
1.790 1.940   ? 8.900  ? ? ? ? ? 99.800 ? ? ? ? 0.084 ? ? ? ? ? ? ? ? 6.600 ? ? ? ? ? ? ? 4  1 ? ? 
1.940 2.120   ? 14.500 ? ? ? ? ? 99.200 ? ? ? ? 0.051 ? ? ? ? ? ? ? ? 6.200 ? ? ? ? ? ? ? 5  1 ? ? 
2.120 2.370   ? 19.600 ? ? ? ? ? 99.700 ? ? ? ? 0.037 ? ? ? ? ? ? ? ? 6.600 ? ? ? ? ? ? ? 6  1 ? ? 
2.370 2.740   ? 23.800 ? ? ? ? ? 99.400 ? ? ? ? 0.029 ? ? ? ? ? ? ? ? 6.100 ? ? ? ? ? ? ? 7  1 ? ? 
2.740 3.350   ? 27.200 ? ? ? ? ? 99.100 ? ? ? ? 0.023 ? ? ? ? ? ? ? ? 6.400 ? ? ? ? ? ? ? 8  1 ? ? 
3.350 4.740   ? 31.500 ? ? ? ? ? 98.500 ? ? ? ? 0.019 ? ? ? ? ? ? ? ? 5.900 ? ? ? ? ? ? ? 9  1 ? ? 
4.740 159.284 ? 32.700 ? ? ? ? ? 98.200 ? ? ? ? 0.017 ? ? ? ? ? ? ? ? 5.800 ? ? ? ? ? ? ? 10 1 ? ? 
# 
_refine.aniso_B[1][1]                            0.5100 
_refine.aniso_B[1][2]                            0.0000 
_refine.aniso_B[1][3]                            0.0000 
_refine.aniso_B[2][2]                            0.5700 
_refine.aniso_B[2][3]                            0.0000 
_refine.aniso_B[3][3]                            -1.0900 
_refine.B_iso_max                                82.810 
_refine.B_iso_mean                               20.0790 
_refine.B_iso_min                                7.840 
_refine.correlation_coeff_Fo_to_Fc               0.9660 
_refine.correlation_coeff_Fo_to_Fc_free          0.9540 
_refine.details                                  
'HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT U VALUES      : REFINED INDIVIDUALLY' 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 5LLA 
_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                            1.5000 
_refine.ls_d_res_low                             79.6400 
_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                     74022 
_refine.ls_number_reflns_R_free                  8196 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.1000 
_refine.ls_percent_reflns_R_free                 10.0000 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1821 
_refine.ls_R_factor_R_free                       0.2125 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1787 
_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                      4KNN 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.0830 
_refine.pdbx_overall_ESU_R_Free                  0.0850 
_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             0.0830 
_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.cycle_id                         final 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.d_res_high                       1.5000 
_refine_hist.d_res_low                        79.6400 
_refine_hist.pdbx_number_atoms_ligand         82 
_refine_hist.number_atoms_solvent             550 
_refine_hist.number_atoms_total               4740 
_refine_hist.pdbx_number_residues_total       516 
_refine_hist.pdbx_B_iso_mean_ligand           41.03 
_refine_hist.pdbx_B_iso_mean_solvent          28.89 
_refine_hist.pdbx_number_atoms_protein        4108 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
# 
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' ? 0.025  0.020  4440 ? r_bond_refined_d       ? ? 
'X-RAY DIFFRACTION' ? 2.452  1.962  6067 ? r_angle_refined_deg    ? ? 
'X-RAY DIFFRACTION' ? 6.599  5.000  542  ? r_dihedral_angle_1_deg ? ? 
'X-RAY DIFFRACTION' ? 32.967 24.039 203  ? r_dihedral_angle_2_deg ? ? 
'X-RAY DIFFRACTION' ? 12.706 15.000 705  ? r_dihedral_angle_3_deg ? ? 
'X-RAY DIFFRACTION' ? 13.343 15.000 22   ? r_dihedral_angle_4_deg ? ? 
'X-RAY DIFFRACTION' ? 0.233  0.200  632  ? r_chiral_restr         ? ? 
'X-RAY DIFFRACTION' ? 0.014  0.021  3490 ? r_gen_planes_refined   ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.5000 
_refine_ls_shell.d_res_low                        1.5390 
_refine_ls_shell.number_reflns_all                5989 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             591 
_refine_ls_shell.number_reflns_R_work             5398 
_refine_ls_shell.percent_reflns_obs               98.9900 
_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                  0.3620 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.3520 
_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                     5LLA 
_struct.title                        
'Crystal structure of human carbonic anhydrase isozyme XIII with 4-(1H-benzimidazol-1-ylacetyl)-2-chlorobenzenesulfonamide' 
_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        5LLA 
_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 5 ? 
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 5LLA B 2 ? 263 ? Q8N1Q1 1 ? 262 ? 2 263 
2 1 5LLA 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 5LLA MET B 1 ? UNP Q8N1Q1 ? ? 'initiating methionine' 1 1 
2 5LLA 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 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 GLY A 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 SER A 132 ? ALA A 137 ? SER B 132 ALA B 137 1 ? 6 
HELX_P HELX_P5  AA5 ASN A 156 ? ASP A 164 ? ASN B 156 ASP B 164 1 ? 9 
HELX_P HELX_P6  AA6 THR A 165 ? LYS A 170 ? THR B 165 LYS B 170 5 ? 6 
HELX_P HELX_P7  AA7 ASP A 182 ? LEU A 187 ? ASP B 182 LEU B 187 1 ? 6 
HELX_P HELX_P8  AA8 SER A 221 ? ARG A 229 ? SER B 221 ARG B 229 1 ? 9 
HELX_P HELX_P9  AA9 GLY B 14  ? PHE B 21  ? GLY A 14  PHE A 21  5 ? 8 
HELX_P HELX_P10 AB1 PHE B 22  ? GLY B 27  ? PHE A 22  GLY A 27  5 ? 6 
HELX_P HELX_P11 AB2 LYS B 36  ? VAL B 40  ? LYS A 36  VAL A 40  5 ? 5 
HELX_P HELX_P12 AB3 SER B 132 ? ALA B 137 ? SER A 132 ALA A 137 1 ? 6 
HELX_P HELX_P13 AB4 ASN B 156 ? GLN B 158 ? ASN A 156 GLN A 158 5 ? 3 
HELX_P HELX_P14 AB5 LEU B 159 ? ASP B 164 ? LEU A 159 ASP A 164 1 ? 6 
HELX_P HELX_P15 AB6 THR B 165 ? LYS B 170 ? THR A 165 LYS A 170 5 ? 6 
HELX_P HELX_P16 AB7 LEU B 183 ? LEU B 187 ? LEU A 183 LEU A 187 5 ? 5 
HELX_P HELX_P17 AB8 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 ? ? ? ? ? ? ? 2.039 ? ? 
metalc2  metalc ? ? A HIS 98  NE2 ? ? ? 1_555 C ZN  . ZN  ? ? B HIS 98  B ZN  301 1_555 ? ? ? ? ? ? ? 2.035 ? ? 
metalc3  metalc ? ? A HIS 121 ND1 ? ? ? 1_555 C ZN  . ZN  ? ? B HIS 121 B ZN  301 1_555 ? ? ? ? ? ? ? 2.017 ? ? 
metalc4  metalc ? ? C ZN  .   ZN  ? ? ? 1_555 D 6YQ . O8  ? ? B ZN  301 B 6YQ 302 1_555 ? ? ? ? ? ? ? 2.543 ? ? 
metalc5  metalc ? ? C ZN  .   ZN  ? ? ? 1_555 D 6YQ . N10 ? ? B ZN  301 B 6YQ 302 1_555 ? ? ? ? ? ? ? 1.897 ? ? 
metalc6  metalc ? ? B HIS 96  NE2 ? ? ? 1_555 G ZN  . ZN  ? ? A HIS 96  A ZN  301 1_555 ? ? ? ? ? ? ? 2.034 ? ? 
metalc7  metalc ? ? B HIS 98  NE2 ? ? ? 1_555 G ZN  . ZN  ? ? A HIS 98  A ZN  301 1_555 ? ? ? ? ? ? ? 2.013 ? ? 
metalc8  metalc ? ? B HIS 121 ND1 ? ? ? 1_555 G ZN  . ZN  ? ? A HIS 121 A ZN  301 1_555 ? ? ? ? ? ? ? 2.051 ? ? 
metalc9  metalc ? ? G ZN  .   ZN  ? ? ? 1_555 H 6YQ . S7  ? ? A ZN  301 A 6YQ 302 1_555 ? ? ? ? ? ? ? 2.951 ? ? 
metalc10 metalc ? ? G ZN  .   ZN  ? ? ? 1_555 H 6YQ . N10 ? ? A ZN  301 A 6YQ 302 1_555 ? ? ? ? ? ? ? 1.797 ? ? 
metalc11 metalc ? ? G ZN  .   ZN  ? ? ? 1_555 H 6YQ . O8  ? ? A ZN  301 A 6YQ 302 1_555 ? ? ? ? ? ? ? 2.685 ? ? 
# 
_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_555 101.3 ? 
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_555 114.3 ? 
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 95.5  ? 
4  NE2 ? A HIS 96  ? B HIS 96  ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 O8  ? D 6YQ .   ? B 6YQ 302 ? 1_555 87.6  ? 
5  NE2 ? A HIS 98  ? B HIS 98  ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 O8  ? D 6YQ .   ? B 6YQ 302 ? 1_555 170.9 ? 
6  ND1 ? A HIS 121 ? B HIS 121 ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 O8  ? D 6YQ .   ? B 6YQ 302 ? 1_555 82.5  ? 
7  NE2 ? A HIS 96  ? B HIS 96  ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 N10 ? D 6YQ .   ? B 6YQ 302 ? 1_555 106.8 ? 
8  NE2 ? A HIS 98  ? B HIS 98  ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 N10 ? D 6YQ .   ? B 6YQ 302 ? 1_555 111.9 ? 
9  ND1 ? A HIS 121 ? B HIS 121 ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 N10 ? D 6YQ .   ? B 6YQ 302 ? 1_555 124.3 ? 
10 O8  ? D 6YQ .   ? B 6YQ 302 ? 1_555 ZN ? C ZN . ? B ZN 301 ? 1_555 N10 ? D 6YQ .   ? B 6YQ 302 ? 1_555 62.9  ? 
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_555 104.7 ? 
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_555 109.9 ? 
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 93.7  ? 
14 NE2 ? B HIS 96  ? A HIS 96  ? 1_555 ZN ? G ZN . ? A ZN 301 ? 1_555 S7  ? H 6YQ .   ? A 6YQ 302 ? 1_555 98.1  ? 
15 NE2 ? B HIS 98  ? A HIS 98  ? 1_555 ZN ? G ZN . ? A ZN 301 ? 1_555 S7  ? H 6YQ .   ? A 6YQ 302 ? 1_555 146.5 ? 
16 ND1 ? B HIS 121 ? A HIS 121 ? 1_555 ZN ? G ZN . ? A ZN 301 ? 1_555 S7  ? H 6YQ .   ? A 6YQ 302 ? 1_555 101.3 ? 
17 NE2 ? B HIS 96  ? A HIS 96  ? 1_555 ZN ? G ZN . ? A ZN 301 ? 1_555 N10 ? H 6YQ .   ? A 6YQ 302 ? 1_555 113.7 ? 
18 NE2 ? B HIS 98  ? A HIS 98  ? 1_555 ZN ? G ZN . ? A ZN 301 ? 1_555 N10 ? H 6YQ .   ? A 6YQ 302 ? 1_555 111.2 ? 
19 ND1 ? B HIS 121 ? A HIS 121 ? 1_555 ZN ? G ZN . ? A ZN 301 ? 1_555 N10 ? H 6YQ .   ? A 6YQ 302 ? 1_555 120.7 ? 
20 S7  ? H 6YQ .   ? A 6YQ 302 ? 1_555 ZN ? G ZN . ? A ZN 301 ? 1_555 N10 ? H 6YQ .   ? A 6YQ 302 ? 1_555 35.8  ? 
21 NE2 ? B HIS 96  ? A HIS 96  ? 1_555 ZN ? G ZN . ? A ZN 301 ? 1_555 O8  ? H 6YQ .   ? A 6YQ 302 ? 1_555 87.3  ? 
22 NE2 ? B HIS 98  ? A HIS 98  ? 1_555 ZN ? G ZN . ? A ZN 301 ? 1_555 O8  ? H 6YQ .   ? A 6YQ 302 ? 1_555 167.9 ? 
23 ND1 ? B HIS 121 ? A HIS 121 ? 1_555 ZN ? G ZN . ? A ZN 301 ? 1_555 O8  ? H 6YQ .   ? A 6YQ 302 ? 1_555 80.6  ? 
24 S7  ? H 6YQ .   ? A 6YQ 302 ? 1_555 ZN ? G ZN . ? A ZN 301 ? 1_555 O8  ? H 6YQ .   ? A 6YQ 302 ? 1_555 28.3  ? 
25 N10 ? H 6YQ .   ? A 6YQ 302 ? 1_555 ZN ? G ZN . ? A ZN 301 ? 1_555 O8  ? H 6YQ .   ? A 6YQ 302 ? 1_555 63.9  ? 
# 
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 0.39  
2 PRO 203 A . ? PRO 203 B PRO 204 A ? PRO 204 B 1 9.25  
3 SER 31  B . ? SER 31  A PRO 32  B ? PRO 32  A 1 -4.31 
4 PRO 203 B . ? PRO 203 A PRO 204 B ? PRO 204 A 1 17.47 
# 
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  TYR A 90  ? TRP A 99  ? TYR B 90  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  TYR A 90  ? TRP A 99  ? TYR B 90  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 ILE A 212 ? O ILE B 212 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 VAL A 123 ? O VAL B 123 N GLN A 94  ? N GLN B 94  
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 SER A 50  ? N SER B 50  O ARG A 82  ? O ARG B 82  
AA3 2 3  N LEU A 81  ? N LEU B 81  O TYR A 90  ? O TYR B 90  
AA3 3 4  N GLN A 94  ? N GLN B 94  O VAL A 123 ? O VAL B 123 
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 VAL B 123 ? O VAL A 123 N ARG B 93  ? N ARG A 93  
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 LYS B 59  ? N LYS A 59  
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 93  ? N ARG A 93  O VAL B 123 ? O VAL A 123 
AA6 4 5  N LEU B 120 ? N LEU A 120 O VAL B 148 ? O VAL A 148 
AA6 5 6  N GLN B 151 ? N GLN A 151 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 ? 5  'binding site for residue ZN B 301'  
AC2 Software B 6YQ 302 ? 10 'binding site for residue 6YQ B 302' 
AC3 Software B CIT 303 ? 9  'binding site for residue CIT B 303' 
AC4 Software B EDO 304 ? 5  'binding site for residue EDO B 304' 
AC5 Software A ZN  301 ? 4  'binding site for residue ZN A 301'  
AC6 Software A 6YQ 302 ? 12 'binding site for residue 6YQ A 302' 
AC7 Software A CIT 303 ? 7  'binding site for residue CIT A 303' 
AC8 Software A EDO 304 ? 5  'binding site for residue EDO 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 5  HIS A 96  ? HIS B 96  . ? 1_555 ? 
2  AC1 5  HIS A 98  ? HIS B 98  . ? 1_555 ? 
3  AC1 5  HIS A 121 ? HIS B 121 . ? 1_555 ? 
4  AC1 5  THR A 201 ? THR B 201 . ? 1_555 ? 
5  AC1 5  6YQ D .   ? 6YQ B 302 . ? 1_555 ? 
6  AC2 10 HIS A 96  ? HIS B 96  . ? 1_555 ? 
7  AC2 10 HIS A 98  ? HIS B 98  . ? 1_555 ? 
8  AC2 10 HIS A 121 ? HIS B 121 . ? 1_555 ? 
9  AC2 10 PHE A 133 ? PHE B 133 . ? 1_555 ? 
10 AC2 10 VAL A 145 ? VAL B 145 . ? 1_555 ? 
11 AC2 10 LEU A 200 ? LEU B 200 . ? 1_555 ? 
12 AC2 10 THR A 201 ? THR B 201 . ? 1_555 ? 
13 AC2 10 VAL A 202 ? VAL B 202 . ? 1_555 ? 
14 AC2 10 TRP A 211 ? TRP B 211 . ? 1_555 ? 
15 AC2 10 ZN  C .   ? ZN  B 301 . ? 1_555 ? 
16 AC3 9  HOH L .   ? HOH A 434 . ? 4_545 ? 
17 AC3 9  GLY A 100 ? GLY B 100 . ? 1_555 ? 
18 AC3 9  SER A 101 ? SER B 101 . ? 1_555 ? 
19 AC3 9  HIS A 105 ? HIS B 105 . ? 1_555 ? 
20 AC3 9  SER A 245 ? SER B 245 . ? 1_555 ? 
21 AC3 9  HIS A 247 ? HIS B 247 . ? 1_555 ? 
22 AC3 9  HOH K .   ? HOH B 514 . ? 1_555 ? 
23 AC3 9  HOH K .   ? HOH B 569 . ? 1_555 ? 
24 AC3 9  HOH K .   ? HOH B 605 . ? 1_555 ? 
25 AC4 5  SER B 50  ? SER A 50  . ? 1_555 ? 
26 AC4 5  ARG B 82  ? ARG A 82  . ? 1_555 ? 
27 AC4 5  PRO A 189 ? PRO B 189 . ? 1_555 ? 
28 AC4 5  SER A 190 ? SER B 190 . ? 1_555 ? 
29 AC4 5  HOH K .   ? HOH B 483 . ? 1_555 ? 
30 AC5 4  HIS B 96  ? HIS A 96  . ? 1_555 ? 
31 AC5 4  HIS B 98  ? HIS A 98  . ? 1_555 ? 
32 AC5 4  HIS B 121 ? HIS A 121 . ? 1_555 ? 
33 AC5 4  6YQ H .   ? 6YQ A 302 . ? 1_555 ? 
34 AC6 12 HIS B 96  ? HIS A 96  . ? 1_555 ? 
35 AC6 12 HIS B 98  ? HIS A 98  . ? 1_555 ? 
36 AC6 12 HIS B 121 ? HIS A 121 . ? 1_555 ? 
37 AC6 12 PHE B 133 ? PHE A 133 . ? 1_555 ? 
38 AC6 12 VAL B 145 ? VAL A 145 . ? 1_555 ? 
39 AC6 12 LEU B 200 ? LEU A 200 . ? 1_555 ? 
40 AC6 12 THR B 201 ? THR A 201 . ? 1_555 ? 
41 AC6 12 VAL B 202 ? VAL A 202 . ? 1_555 ? 
42 AC6 12 TRP B 211 ? TRP A 211 . ? 1_555 ? 
43 AC6 12 ZN  G .   ? ZN  A 301 . ? 1_555 ? 
44 AC6 12 HOH L .   ? HOH A 470 . ? 1_555 ? 
45 AC6 12 HOH L .   ? HOH A 613 . ? 1_555 ? 
46 AC7 7  GLY B 100 ? GLY A 100 . ? 1_555 ? 
47 AC7 7  SER B 101 ? SER A 101 . ? 1_555 ? 
48 AC7 7  HIS B 105 ? HIS A 105 . ? 1_555 ? 
49 AC7 7  SER B 245 ? SER A 245 . ? 1_555 ? 
50 AC7 7  HIS B 247 ? HIS A 247 . ? 1_555 ? 
51 AC7 7  HOH L .   ? HOH A 428 . ? 1_555 ? 
52 AC7 7  HOH L .   ? HOH A 462 . ? 1_555 ? 
53 AC8 5  LYS B 215 ? LYS A 215 . ? 1_555 ? 
54 AC8 5  GLN B 216 ? GLN A 216 . ? 1_555 ? 
55 AC8 5  HOH L .   ? HOH A 427 . ? 1_555 ? 
56 AC8 5  HOH L .   ? HOH A 516 . ? 1_555 ? 
57 AC8 5  HOH L .   ? HOH A 598 . ? 1_555 ? 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O  B HOH 557 ? ? O B HOH 619 ? ? 2.00 
2 1 O  B HOH 453 ? ? O B HOH 656 ? ? 2.07 
3 1 OG A SER 230 ? A O A HOH 401 ? ? 2.14 
4 1 O  B HOH 484 ? ? O B HOH 560 ? ? 2.19 
# 
loop_
_pdbx_validate_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1 1 CG B HIS 105 ? ? CD2 B HIS 105 ? ? 1.424 1.354 0.070 0.009 N 
2 1 CG A HIS 263 ? ? CD2 A HIS 263 ? ? 1.412 1.354 0.058 0.009 N 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             N 
_pdbx_validate_rmsd_angle.auth_asym_id_1             B 
_pdbx_validate_rmsd_angle.auth_comp_id_1             GLN 
_pdbx_validate_rmsd_angle.auth_seq_id_1              94 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CA 
_pdbx_validate_rmsd_angle.auth_asym_id_2             B 
_pdbx_validate_rmsd_angle.auth_comp_id_2             GLN 
_pdbx_validate_rmsd_angle.auth_seq_id_2              94 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             CB 
_pdbx_validate_rmsd_angle.auth_asym_id_3             B 
_pdbx_validate_rmsd_angle.auth_comp_id_3             GLN 
_pdbx_validate_rmsd_angle.auth_seq_id_3              94 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                96.48 
_pdbx_validate_rmsd_angle.angle_target_value         110.60 
_pdbx_validate_rmsd_angle.angle_deviation            -14.12 
_pdbx_validate_rmsd_angle.angle_standard_deviation   1.80 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 SER B 67  ? ? -174.56 -177.52 
2 1 ASN B 77  ? ? -92.05  48.80   
3 1 PHE B 178 ? ? -163.15 117.61  
4 1 ASN B 246 ? ? -154.55 50.88   
5 1 SER A 67  ? ? -179.23 -178.89 
6 1 ASP A 73  ? B -39.85  130.13  
7 1 ASN A 77  ? ? -99.64  34.90   
8 1 ASN A 246 ? ? -151.28 41.24   
# 
_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 
6YQ CL1  CL N N 1   
6YQ C6   C  Y N 2   
6YQ C1   C  Y N 3   
6YQ S7   S  N N 4   
6YQ O9   O  N N 5   
6YQ N10  N  N N 6   
6YQ O8   O  N N 7   
6YQ C5   C  Y N 8   
6YQ C4   C  Y N 9   
6YQ C3   C  Y N 10  
6YQ C2   C  Y N 11  
6YQ C11  C  N N 12  
6YQ O12  O  N N 13  
6YQ C13  C  N N 14  
6YQ N14  N  Y N 15  
6YQ C18  C  Y N 16  
6YQ C20  C  Y N 17  
6YQ C21  C  Y N 18  
6YQ C22  C  Y N 19  
6YQ C23  C  Y N 20  
6YQ C19  C  Y N 21  
6YQ N17  N  Y N 22  
6YQ C16  C  Y N 23  
6YQ H1   H  N N 24  
6YQ H2   H  N N 25  
6YQ H3   H  N N 26  
6YQ H4   H  N N 27  
6YQ H5   H  N N 28  
6YQ H6   H  N N 29  
6YQ H7   H  N N 30  
6YQ H8   H  N N 31  
6YQ H9   H  N N 32  
6YQ H10  H  N N 33  
6YQ H11  H  N N 34  
6YQ H12  H  N N 35  
ALA N    N  N N 36  
ALA CA   C  N S 37  
ALA C    C  N N 38  
ALA O    O  N N 39  
ALA CB   C  N N 40  
ALA OXT  O  N N 41  
ALA H    H  N N 42  
ALA H2   H  N N 43  
ALA HA   H  N N 44  
ALA HB1  H  N N 45  
ALA HB2  H  N N 46  
ALA HB3  H  N N 47  
ALA HXT  H  N N 48  
ARG N    N  N N 49  
ARG CA   C  N S 50  
ARG C    C  N N 51  
ARG O    O  N N 52  
ARG CB   C  N N 53  
ARG CG   C  N N 54  
ARG CD   C  N N 55  
ARG NE   N  N N 56  
ARG CZ   C  N N 57  
ARG NH1  N  N N 58  
ARG NH2  N  N N 59  
ARG OXT  O  N N 60  
ARG H    H  N N 61  
ARG H2   H  N N 62  
ARG HA   H  N N 63  
ARG HB2  H  N N 64  
ARG HB3  H  N N 65  
ARG HG2  H  N N 66  
ARG HG3  H  N N 67  
ARG HD2  H  N N 68  
ARG HD3  H  N N 69  
ARG HE   H  N N 70  
ARG HH11 H  N N 71  
ARG HH12 H  N N 72  
ARG HH21 H  N N 73  
ARG HH22 H  N N 74  
ARG HXT  H  N N 75  
ASN N    N  N N 76  
ASN CA   C  N S 77  
ASN C    C  N N 78  
ASN O    O  N N 79  
ASN CB   C  N N 80  
ASN CG   C  N N 81  
ASN OD1  O  N N 82  
ASN ND2  N  N N 83  
ASN OXT  O  N N 84  
ASN H    H  N N 85  
ASN H2   H  N N 86  
ASN HA   H  N N 87  
ASN HB2  H  N N 88  
ASN HB3  H  N N 89  
ASN HD21 H  N N 90  
ASN HD22 H  N N 91  
ASN HXT  H  N N 92  
ASP N    N  N N 93  
ASP CA   C  N S 94  
ASP C    C  N N 95  
ASP O    O  N N 96  
ASP CB   C  N N 97  
ASP CG   C  N N 98  
ASP OD1  O  N N 99  
ASP OD2  O  N N 100 
ASP OXT  O  N N 101 
ASP H    H  N N 102 
ASP H2   H  N N 103 
ASP HA   H  N N 104 
ASP HB2  H  N N 105 
ASP HB3  H  N N 106 
ASP HD2  H  N N 107 
ASP HXT  H  N N 108 
CIT C1   C  N N 109 
CIT O1   O  N N 110 
CIT O2   O  N N 111 
CIT C2   C  N N 112 
CIT C3   C  N N 113 
CIT O7   O  N N 114 
CIT C4   C  N N 115 
CIT C5   C  N N 116 
CIT O3   O  N N 117 
CIT O4   O  N N 118 
CIT C6   C  N N 119 
CIT O5   O  N N 120 
CIT O6   O  N N 121 
CIT HO2  H  N N 122 
CIT H21  H  N N 123 
CIT H22  H  N N 124 
CIT HO7  H  N N 125 
CIT H41  H  N N 126 
CIT H42  H  N N 127 
CIT HO4  H  N N 128 
CIT HO6  H  N N 129 
CYS N    N  N N 130 
CYS CA   C  N R 131 
CYS C    C  N N 132 
CYS O    O  N N 133 
CYS CB   C  N N 134 
CYS SG   S  N N 135 
CYS OXT  O  N N 136 
CYS H    H  N N 137 
CYS H2   H  N N 138 
CYS HA   H  N N 139 
CYS HB2  H  N N 140 
CYS HB3  H  N N 141 
CYS HG   H  N N 142 
CYS HXT  H  N N 143 
EDO C1   C  N N 144 
EDO O1   O  N N 145 
EDO C2   C  N N 146 
EDO O2   O  N N 147 
EDO H11  H  N N 148 
EDO H12  H  N N 149 
EDO HO1  H  N N 150 
EDO H21  H  N N 151 
EDO H22  H  N N 152 
EDO HO2  H  N N 153 
GLN N    N  N N 154 
GLN CA   C  N S 155 
GLN C    C  N N 156 
GLN O    O  N N 157 
GLN CB   C  N N 158 
GLN CG   C  N N 159 
GLN CD   C  N N 160 
GLN OE1  O  N N 161 
GLN NE2  N  N N 162 
GLN OXT  O  N N 163 
GLN H    H  N N 164 
GLN H2   H  N N 165 
GLN HA   H  N N 166 
GLN HB2  H  N N 167 
GLN HB3  H  N N 168 
GLN HG2  H  N N 169 
GLN HG3  H  N N 170 
GLN HE21 H  N N 171 
GLN HE22 H  N N 172 
GLN HXT  H  N N 173 
GLU N    N  N N 174 
GLU CA   C  N S 175 
GLU C    C  N N 176 
GLU O    O  N N 177 
GLU CB   C  N N 178 
GLU CG   C  N N 179 
GLU CD   C  N N 180 
GLU OE1  O  N N 181 
GLU OE2  O  N N 182 
GLU OXT  O  N N 183 
GLU H    H  N N 184 
GLU H2   H  N N 185 
GLU HA   H  N N 186 
GLU HB2  H  N N 187 
GLU HB3  H  N N 188 
GLU HG2  H  N N 189 
GLU HG3  H  N N 190 
GLU HE2  H  N N 191 
GLU HXT  H  N N 192 
GLY N    N  N N 193 
GLY CA   C  N N 194 
GLY C    C  N N 195 
GLY O    O  N N 196 
GLY OXT  O  N N 197 
GLY H    H  N N 198 
GLY H2   H  N N 199 
GLY HA2  H  N N 200 
GLY HA3  H  N N 201 
GLY HXT  H  N N 202 
HIS N    N  N N 203 
HIS CA   C  N S 204 
HIS C    C  N N 205 
HIS O    O  N N 206 
HIS CB   C  N N 207 
HIS CG   C  Y N 208 
HIS ND1  N  Y N 209 
HIS CD2  C  Y N 210 
HIS CE1  C  Y N 211 
HIS NE2  N  Y N 212 
HIS OXT  O  N N 213 
HIS H    H  N N 214 
HIS H2   H  N N 215 
HIS HA   H  N N 216 
HIS HB2  H  N N 217 
HIS HB3  H  N N 218 
HIS HD1  H  N N 219 
HIS HD2  H  N N 220 
HIS HE1  H  N N 221 
HIS HE2  H  N N 222 
HIS HXT  H  N N 223 
HOH O    O  N N 224 
HOH H1   H  N N 225 
HOH H2   H  N N 226 
ILE N    N  N N 227 
ILE CA   C  N S 228 
ILE C    C  N N 229 
ILE O    O  N N 230 
ILE CB   C  N S 231 
ILE CG1  C  N N 232 
ILE CG2  C  N N 233 
ILE CD1  C  N N 234 
ILE OXT  O  N N 235 
ILE H    H  N N 236 
ILE H2   H  N N 237 
ILE HA   H  N N 238 
ILE HB   H  N N 239 
ILE HG12 H  N N 240 
ILE HG13 H  N N 241 
ILE HG21 H  N N 242 
ILE HG22 H  N N 243 
ILE HG23 H  N N 244 
ILE HD11 H  N N 245 
ILE HD12 H  N N 246 
ILE HD13 H  N N 247 
ILE HXT  H  N N 248 
LEU N    N  N N 249 
LEU CA   C  N S 250 
LEU C    C  N N 251 
LEU O    O  N N 252 
LEU CB   C  N N 253 
LEU CG   C  N N 254 
LEU CD1  C  N N 255 
LEU CD2  C  N N 256 
LEU OXT  O  N N 257 
LEU H    H  N N 258 
LEU H2   H  N N 259 
LEU HA   H  N N 260 
LEU HB2  H  N N 261 
LEU HB3  H  N N 262 
LEU HG   H  N N 263 
LEU HD11 H  N N 264 
LEU HD12 H  N N 265 
LEU HD13 H  N N 266 
LEU HD21 H  N N 267 
LEU HD22 H  N N 268 
LEU HD23 H  N N 269 
LEU HXT  H  N N 270 
LYS N    N  N N 271 
LYS CA   C  N S 272 
LYS C    C  N N 273 
LYS O    O  N N 274 
LYS CB   C  N N 275 
LYS CG   C  N N 276 
LYS CD   C  N N 277 
LYS CE   C  N N 278 
LYS NZ   N  N N 279 
LYS OXT  O  N N 280 
LYS H    H  N N 281 
LYS H2   H  N N 282 
LYS HA   H  N N 283 
LYS HB2  H  N N 284 
LYS HB3  H  N N 285 
LYS HG2  H  N N 286 
LYS HG3  H  N N 287 
LYS HD2  H  N N 288 
LYS HD3  H  N N 289 
LYS HE2  H  N N 290 
LYS HE3  H  N N 291 
LYS HZ1  H  N N 292 
LYS HZ2  H  N N 293 
LYS HZ3  H  N N 294 
LYS HXT  H  N N 295 
MET N    N  N N 296 
MET CA   C  N S 297 
MET C    C  N N 298 
MET O    O  N N 299 
MET CB   C  N N 300 
MET CG   C  N N 301 
MET SD   S  N N 302 
MET CE   C  N N 303 
MET OXT  O  N N 304 
MET H    H  N N 305 
MET H2   H  N N 306 
MET HA   H  N N 307 
MET HB2  H  N N 308 
MET HB3  H  N N 309 
MET HG2  H  N N 310 
MET HG3  H  N N 311 
MET HE1  H  N N 312 
MET HE2  H  N N 313 
MET HE3  H  N N 314 
MET HXT  H  N N 315 
PHE N    N  N N 316 
PHE CA   C  N S 317 
PHE C    C  N N 318 
PHE O    O  N N 319 
PHE CB   C  N N 320 
PHE CG   C  Y N 321 
PHE CD1  C  Y N 322 
PHE CD2  C  Y N 323 
PHE CE1  C  Y N 324 
PHE CE2  C  Y N 325 
PHE CZ   C  Y N 326 
PHE OXT  O  N N 327 
PHE H    H  N N 328 
PHE H2   H  N N 329 
PHE HA   H  N N 330 
PHE HB2  H  N N 331 
PHE HB3  H  N N 332 
PHE HD1  H  N N 333 
PHE HD2  H  N N 334 
PHE HE1  H  N N 335 
PHE HE2  H  N N 336 
PHE HZ   H  N N 337 
PHE HXT  H  N N 338 
PRO N    N  N N 339 
PRO CA   C  N S 340 
PRO C    C  N N 341 
PRO O    O  N N 342 
PRO CB   C  N N 343 
PRO CG   C  N N 344 
PRO CD   C  N N 345 
PRO OXT  O  N N 346 
PRO H    H  N N 347 
PRO HA   H  N N 348 
PRO HB2  H  N N 349 
PRO HB3  H  N N 350 
PRO HG2  H  N N 351 
PRO HG3  H  N N 352 
PRO HD2  H  N N 353 
PRO HD3  H  N N 354 
PRO HXT  H  N N 355 
SER N    N  N N 356 
SER CA   C  N S 357 
SER C    C  N N 358 
SER O    O  N N 359 
SER CB   C  N N 360 
SER OG   O  N N 361 
SER OXT  O  N N 362 
SER H    H  N N 363 
SER H2   H  N N 364 
SER HA   H  N N 365 
SER HB2  H  N N 366 
SER HB3  H  N N 367 
SER HG   H  N N 368 
SER HXT  H  N N 369 
THR N    N  N N 370 
THR CA   C  N S 371 
THR C    C  N N 372 
THR O    O  N N 373 
THR CB   C  N R 374 
THR OG1  O  N N 375 
THR CG2  C  N N 376 
THR OXT  O  N N 377 
THR H    H  N N 378 
THR H2   H  N N 379 
THR HA   H  N N 380 
THR HB   H  N N 381 
THR HG1  H  N N 382 
THR HG21 H  N N 383 
THR HG22 H  N N 384 
THR HG23 H  N N 385 
THR HXT  H  N N 386 
TRP N    N  N N 387 
TRP CA   C  N S 388 
TRP C    C  N N 389 
TRP O    O  N N 390 
TRP CB   C  N N 391 
TRP CG   C  Y N 392 
TRP CD1  C  Y N 393 
TRP CD2  C  Y N 394 
TRP NE1  N  Y N 395 
TRP CE2  C  Y N 396 
TRP CE3  C  Y N 397 
TRP CZ2  C  Y N 398 
TRP CZ3  C  Y N 399 
TRP CH2  C  Y N 400 
TRP OXT  O  N N 401 
TRP H    H  N N 402 
TRP H2   H  N N 403 
TRP HA   H  N N 404 
TRP HB2  H  N N 405 
TRP HB3  H  N N 406 
TRP HD1  H  N N 407 
TRP HE1  H  N N 408 
TRP HE3  H  N N 409 
TRP HZ2  H  N N 410 
TRP HZ3  H  N N 411 
TRP HH2  H  N N 412 
TRP HXT  H  N N 413 
TYR N    N  N N 414 
TYR CA   C  N S 415 
TYR C    C  N N 416 
TYR O    O  N N 417 
TYR CB   C  N N 418 
TYR CG   C  Y N 419 
TYR CD1  C  Y N 420 
TYR CD2  C  Y N 421 
TYR CE1  C  Y N 422 
TYR CE2  C  Y N 423 
TYR CZ   C  Y N 424 
TYR OH   O  N N 425 
TYR OXT  O  N N 426 
TYR H    H  N N 427 
TYR H2   H  N N 428 
TYR HA   H  N N 429 
TYR HB2  H  N N 430 
TYR HB3  H  N N 431 
TYR HD1  H  N N 432 
TYR HD2  H  N N 433 
TYR HE1  H  N N 434 
TYR HE2  H  N N 435 
TYR HH   H  N N 436 
TYR HXT  H  N N 437 
VAL N    N  N N 438 
VAL CA   C  N S 439 
VAL C    C  N N 440 
VAL O    O  N N 441 
VAL CB   C  N N 442 
VAL CG1  C  N N 443 
VAL CG2  C  N N 444 
VAL OXT  O  N N 445 
VAL H    H  N N 446 
VAL H2   H  N N 447 
VAL HA   H  N N 448 
VAL HB   H  N N 449 
VAL HG11 H  N N 450 
VAL HG12 H  N N 451 
VAL HG13 H  N N 452 
VAL HG21 H  N N 453 
VAL HG22 H  N N 454 
VAL HG23 H  N N 455 
VAL HXT  H  N N 456 
ZN  ZN   ZN N N 457 
# 
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 
6YQ C13 N14  sing N N 1   
6YQ C13 C11  sing N N 2   
6YQ C3  C2   doub Y N 3   
6YQ C3  C4   sing Y N 4   
6YQ C16 N14  sing Y N 5   
6YQ C16 N17  doub Y N 6   
6YQ N14 C18  sing Y N 7   
6YQ C2  C1   sing Y N 8   
6YQ N10 S7   sing N N 9   
6YQ N17 C19  sing Y N 10  
6YQ C18 C19  doub Y N 11  
6YQ C18 C20  sing Y N 12  
6YQ C19 C23  sing Y N 13  
6YQ C20 C21  doub Y N 14  
6YQ C11 C4   sing N N 15  
6YQ C11 O12  doub N N 16  
6YQ C4  C5   doub Y N 17  
6YQ C23 C22  doub Y N 18  
6YQ C21 C22  sing Y N 19  
6YQ C1  S7   sing N N 20  
6YQ C1  C6   doub Y N 21  
6YQ S7  O8   doub N N 22  
6YQ S7  O9   doub N N 23  
6YQ C5  C6   sing Y N 24  
6YQ C6  CL1  sing N N 25  
6YQ N10 H1   sing N N 26  
6YQ N10 H2   sing N N 27  
6YQ C5  H3   sing N N 28  
6YQ C3  H4   sing N N 29  
6YQ C2  H5   sing N N 30  
6YQ C13 H6   sing N N 31  
6YQ C13 H7   sing N N 32  
6YQ C20 H8   sing N N 33  
6YQ C21 H9   sing N N 34  
6YQ C22 H10  sing N N 35  
6YQ C23 H11  sing N N 36  
6YQ C16 H12  sing N N 37  
ALA N   CA   sing N N 38  
ALA N   H    sing N N 39  
ALA N   H2   sing N N 40  
ALA CA  C    sing N N 41  
ALA CA  CB   sing N N 42  
ALA CA  HA   sing N N 43  
ALA C   O    doub N N 44  
ALA C   OXT  sing N N 45  
ALA CB  HB1  sing N N 46  
ALA CB  HB2  sing N N 47  
ALA CB  HB3  sing N N 48  
ALA OXT HXT  sing N N 49  
ARG N   CA   sing N N 50  
ARG N   H    sing N N 51  
ARG N   H2   sing N N 52  
ARG CA  C    sing N N 53  
ARG CA  CB   sing N N 54  
ARG CA  HA   sing N N 55  
ARG C   O    doub N N 56  
ARG C   OXT  sing N N 57  
ARG CB  CG   sing N N 58  
ARG CB  HB2  sing N N 59  
ARG CB  HB3  sing N N 60  
ARG CG  CD   sing N N 61  
ARG CG  HG2  sing N N 62  
ARG CG  HG3  sing N N 63  
ARG CD  NE   sing N N 64  
ARG CD  HD2  sing N N 65  
ARG CD  HD3  sing N N 66  
ARG NE  CZ   sing N N 67  
ARG NE  HE   sing N N 68  
ARG CZ  NH1  sing N N 69  
ARG CZ  NH2  doub N N 70  
ARG NH1 HH11 sing N N 71  
ARG NH1 HH12 sing N N 72  
ARG NH2 HH21 sing N N 73  
ARG NH2 HH22 sing N N 74  
ARG OXT HXT  sing N N 75  
ASN N   CA   sing N N 76  
ASN N   H    sing N N 77  
ASN N   H2   sing N N 78  
ASN CA  C    sing N N 79  
ASN CA  CB   sing N N 80  
ASN CA  HA   sing N N 81  
ASN C   O    doub N N 82  
ASN C   OXT  sing N N 83  
ASN CB  CG   sing N N 84  
ASN CB  HB2  sing N N 85  
ASN CB  HB3  sing N N 86  
ASN CG  OD1  doub N N 87  
ASN CG  ND2  sing N N 88  
ASN ND2 HD21 sing N N 89  
ASN ND2 HD22 sing N N 90  
ASN OXT HXT  sing N N 91  
ASP N   CA   sing N N 92  
ASP N   H    sing N N 93  
ASP N   H2   sing N N 94  
ASP CA  C    sing N N 95  
ASP CA  CB   sing N N 96  
ASP CA  HA   sing N N 97  
ASP C   O    doub N N 98  
ASP C   OXT  sing N N 99  
ASP CB  CG   sing N N 100 
ASP CB  HB2  sing N N 101 
ASP CB  HB3  sing N N 102 
ASP CG  OD1  doub N N 103 
ASP CG  OD2  sing N N 104 
ASP OD2 HD2  sing N N 105 
ASP OXT HXT  sing N N 106 
CIT C1  O1   doub N N 107 
CIT C1  O2   sing N N 108 
CIT C1  C2   sing N N 109 
CIT O2  HO2  sing N N 110 
CIT C2  C3   sing N N 111 
CIT C2  H21  sing N N 112 
CIT C2  H22  sing N N 113 
CIT C3  O7   sing N N 114 
CIT C3  C4   sing N N 115 
CIT C3  C6   sing N N 116 
CIT O7  HO7  sing N N 117 
CIT C4  C5   sing N N 118 
CIT C4  H41  sing N N 119 
CIT C4  H42  sing N N 120 
CIT C5  O3   doub N N 121 
CIT C5  O4   sing N N 122 
CIT O4  HO4  sing N N 123 
CIT C6  O5   doub N N 124 
CIT C6  O6   sing N N 125 
CIT O6  HO6  sing N N 126 
CYS N   CA   sing N N 127 
CYS N   H    sing N N 128 
CYS N   H2   sing N N 129 
CYS CA  C    sing N N 130 
CYS CA  CB   sing N N 131 
CYS CA  HA   sing N N 132 
CYS C   O    doub N N 133 
CYS C   OXT  sing N N 134 
CYS CB  SG   sing N N 135 
CYS CB  HB2  sing N N 136 
CYS CB  HB3  sing N N 137 
CYS SG  HG   sing N N 138 
CYS OXT HXT  sing N N 139 
EDO C1  O1   sing N N 140 
EDO C1  C2   sing N N 141 
EDO C1  H11  sing N N 142 
EDO C1  H12  sing N N 143 
EDO O1  HO1  sing N N 144 
EDO C2  O2   sing N N 145 
EDO C2  H21  sing N N 146 
EDO C2  H22  sing N N 147 
EDO O2  HO2  sing N N 148 
GLN N   CA   sing N N 149 
GLN N   H    sing N N 150 
GLN N   H2   sing N N 151 
GLN CA  C    sing N N 152 
GLN CA  CB   sing N N 153 
GLN CA  HA   sing N N 154 
GLN C   O    doub N N 155 
GLN C   OXT  sing N N 156 
GLN CB  CG   sing N N 157 
GLN CB  HB2  sing N N 158 
GLN CB  HB3  sing N N 159 
GLN CG  CD   sing N N 160 
GLN CG  HG2  sing N N 161 
GLN CG  HG3  sing N N 162 
GLN CD  OE1  doub N N 163 
GLN CD  NE2  sing N N 164 
GLN NE2 HE21 sing N N 165 
GLN NE2 HE22 sing N N 166 
GLN OXT HXT  sing N N 167 
GLU N   CA   sing N N 168 
GLU N   H    sing N N 169 
GLU N   H2   sing N N 170 
GLU CA  C    sing N N 171 
GLU CA  CB   sing N N 172 
GLU CA  HA   sing N N 173 
GLU C   O    doub N N 174 
GLU C   OXT  sing N N 175 
GLU CB  CG   sing N N 176 
GLU CB  HB2  sing N N 177 
GLU CB  HB3  sing N N 178 
GLU CG  CD   sing N N 179 
GLU CG  HG2  sing N N 180 
GLU CG  HG3  sing N N 181 
GLU CD  OE1  doub N N 182 
GLU CD  OE2  sing N N 183 
GLU OE2 HE2  sing N N 184 
GLU OXT HXT  sing N N 185 
GLY N   CA   sing N N 186 
GLY N   H    sing N N 187 
GLY N   H2   sing N N 188 
GLY CA  C    sing N N 189 
GLY CA  HA2  sing N N 190 
GLY CA  HA3  sing N N 191 
GLY C   O    doub N N 192 
GLY C   OXT  sing N N 193 
GLY OXT HXT  sing N N 194 
HIS N   CA   sing N N 195 
HIS N   H    sing N N 196 
HIS N   H2   sing N N 197 
HIS CA  C    sing N N 198 
HIS CA  CB   sing N N 199 
HIS CA  HA   sing N N 200 
HIS C   O    doub N N 201 
HIS C   OXT  sing N N 202 
HIS CB  CG   sing N N 203 
HIS CB  HB2  sing N N 204 
HIS CB  HB3  sing N N 205 
HIS CG  ND1  sing Y N 206 
HIS CG  CD2  doub Y N 207 
HIS ND1 CE1  doub Y N 208 
HIS ND1 HD1  sing N N 209 
HIS CD2 NE2  sing Y N 210 
HIS CD2 HD2  sing N N 211 
HIS CE1 NE2  sing Y N 212 
HIS CE1 HE1  sing N N 213 
HIS NE2 HE2  sing N N 214 
HIS OXT HXT  sing N N 215 
HOH O   H1   sing N N 216 
HOH O   H2   sing N N 217 
ILE N   CA   sing N N 218 
ILE N   H    sing N N 219 
ILE N   H2   sing N N 220 
ILE CA  C    sing N N 221 
ILE CA  CB   sing N N 222 
ILE CA  HA   sing N N 223 
ILE C   O    doub N N 224 
ILE C   OXT  sing N N 225 
ILE CB  CG1  sing N N 226 
ILE CB  CG2  sing N N 227 
ILE CB  HB   sing N N 228 
ILE CG1 CD1  sing N N 229 
ILE CG1 HG12 sing N N 230 
ILE CG1 HG13 sing N N 231 
ILE CG2 HG21 sing N N 232 
ILE CG2 HG22 sing N N 233 
ILE CG2 HG23 sing N N 234 
ILE CD1 HD11 sing N N 235 
ILE CD1 HD12 sing N N 236 
ILE CD1 HD13 sing N N 237 
ILE OXT HXT  sing N N 238 
LEU N   CA   sing N N 239 
LEU N   H    sing N N 240 
LEU N   H2   sing N N 241 
LEU CA  C    sing N N 242 
LEU CA  CB   sing N N 243 
LEU CA  HA   sing N N 244 
LEU C   O    doub N N 245 
LEU C   OXT  sing N N 246 
LEU CB  CG   sing N N 247 
LEU CB  HB2  sing N N 248 
LEU CB  HB3  sing N N 249 
LEU CG  CD1  sing N N 250 
LEU CG  CD2  sing N N 251 
LEU CG  HG   sing N N 252 
LEU CD1 HD11 sing N N 253 
LEU CD1 HD12 sing N N 254 
LEU CD1 HD13 sing N N 255 
LEU CD2 HD21 sing N N 256 
LEU CD2 HD22 sing N N 257 
LEU CD2 HD23 sing N N 258 
LEU OXT HXT  sing N N 259 
LYS N   CA   sing N N 260 
LYS N   H    sing N N 261 
LYS N   H2   sing N N 262 
LYS CA  C    sing N N 263 
LYS CA  CB   sing N N 264 
LYS CA  HA   sing N N 265 
LYS C   O    doub N N 266 
LYS C   OXT  sing N N 267 
LYS CB  CG   sing N N 268 
LYS CB  HB2  sing N N 269 
LYS CB  HB3  sing N N 270 
LYS CG  CD   sing N N 271 
LYS CG  HG2  sing N N 272 
LYS CG  HG3  sing N N 273 
LYS CD  CE   sing N N 274 
LYS CD  HD2  sing N N 275 
LYS CD  HD3  sing N N 276 
LYS CE  NZ   sing N N 277 
LYS CE  HE2  sing N N 278 
LYS CE  HE3  sing N N 279 
LYS NZ  HZ1  sing N N 280 
LYS NZ  HZ2  sing N N 281 
LYS NZ  HZ3  sing N N 282 
LYS OXT HXT  sing N N 283 
MET N   CA   sing N N 284 
MET N   H    sing N N 285 
MET N   H2   sing N N 286 
MET CA  C    sing N N 287 
MET CA  CB   sing N N 288 
MET CA  HA   sing N N 289 
MET C   O    doub N N 290 
MET C   OXT  sing N N 291 
MET CB  CG   sing N N 292 
MET CB  HB2  sing N N 293 
MET CB  HB3  sing N N 294 
MET CG  SD   sing N N 295 
MET CG  HG2  sing N N 296 
MET CG  HG3  sing N N 297 
MET SD  CE   sing N N 298 
MET CE  HE1  sing N N 299 
MET CE  HE2  sing N N 300 
MET CE  HE3  sing N N 301 
MET OXT HXT  sing N N 302 
PHE N   CA   sing N N 303 
PHE N   H    sing N N 304 
PHE N   H2   sing N N 305 
PHE CA  C    sing N N 306 
PHE CA  CB   sing N N 307 
PHE CA  HA   sing N N 308 
PHE C   O    doub N N 309 
PHE C   OXT  sing N N 310 
PHE CB  CG   sing N N 311 
PHE CB  HB2  sing N N 312 
PHE CB  HB3  sing N N 313 
PHE CG  CD1  doub Y N 314 
PHE CG  CD2  sing Y N 315 
PHE CD1 CE1  sing Y N 316 
PHE CD1 HD1  sing N N 317 
PHE CD2 CE2  doub Y N 318 
PHE CD2 HD2  sing N N 319 
PHE CE1 CZ   doub Y N 320 
PHE CE1 HE1  sing N N 321 
PHE CE2 CZ   sing Y N 322 
PHE CE2 HE2  sing N N 323 
PHE CZ  HZ   sing N N 324 
PHE OXT HXT  sing N N 325 
PRO N   CA   sing N N 326 
PRO N   CD   sing N N 327 
PRO N   H    sing N N 328 
PRO CA  C    sing N N 329 
PRO CA  CB   sing N N 330 
PRO CA  HA   sing N N 331 
PRO C   O    doub N N 332 
PRO C   OXT  sing N N 333 
PRO CB  CG   sing N N 334 
PRO CB  HB2  sing N N 335 
PRO CB  HB3  sing N N 336 
PRO CG  CD   sing N N 337 
PRO CG  HG2  sing N N 338 
PRO CG  HG3  sing N N 339 
PRO CD  HD2  sing N N 340 
PRO CD  HD3  sing N N 341 
PRO OXT HXT  sing N N 342 
SER N   CA   sing N N 343 
SER N   H    sing N N 344 
SER N   H2   sing N N 345 
SER CA  C    sing N N 346 
SER CA  CB   sing N N 347 
SER CA  HA   sing N N 348 
SER C   O    doub N N 349 
SER C   OXT  sing N N 350 
SER CB  OG   sing N N 351 
SER CB  HB2  sing N N 352 
SER CB  HB3  sing N N 353 
SER OG  HG   sing N N 354 
SER OXT HXT  sing N N 355 
THR N   CA   sing N N 356 
THR N   H    sing N N 357 
THR N   H2   sing N N 358 
THR CA  C    sing N N 359 
THR CA  CB   sing N N 360 
THR CA  HA   sing N N 361 
THR C   O    doub N N 362 
THR C   OXT  sing N N 363 
THR CB  OG1  sing N N 364 
THR CB  CG2  sing N N 365 
THR CB  HB   sing N N 366 
THR OG1 HG1  sing N N 367 
THR CG2 HG21 sing N N 368 
THR CG2 HG22 sing N N 369 
THR CG2 HG23 sing N N 370 
THR OXT HXT  sing N N 371 
TRP N   CA   sing N N 372 
TRP N   H    sing N N 373 
TRP N   H2   sing N N 374 
TRP CA  C    sing N N 375 
TRP CA  CB   sing N N 376 
TRP CA  HA   sing N N 377 
TRP C   O    doub N N 378 
TRP C   OXT  sing N N 379 
TRP CB  CG   sing N N 380 
TRP CB  HB2  sing N N 381 
TRP CB  HB3  sing N N 382 
TRP CG  CD1  doub Y N 383 
TRP CG  CD2  sing Y N 384 
TRP CD1 NE1  sing Y N 385 
TRP CD1 HD1  sing N N 386 
TRP CD2 CE2  doub Y N 387 
TRP CD2 CE3  sing Y N 388 
TRP NE1 CE2  sing Y N 389 
TRP NE1 HE1  sing N N 390 
TRP CE2 CZ2  sing Y N 391 
TRP CE3 CZ3  doub Y N 392 
TRP CE3 HE3  sing N N 393 
TRP CZ2 CH2  doub Y N 394 
TRP CZ2 HZ2  sing N N 395 
TRP CZ3 CH2  sing Y N 396 
TRP CZ3 HZ3  sing N N 397 
TRP CH2 HH2  sing N N 398 
TRP OXT HXT  sing N N 399 
TYR N   CA   sing N N 400 
TYR N   H    sing N N 401 
TYR N   H2   sing N N 402 
TYR CA  C    sing N N 403 
TYR CA  CB   sing N N 404 
TYR CA  HA   sing N N 405 
TYR C   O    doub N N 406 
TYR C   OXT  sing N N 407 
TYR CB  CG   sing N N 408 
TYR CB  HB2  sing N N 409 
TYR CB  HB3  sing N N 410 
TYR CG  CD1  doub Y N 411 
TYR CG  CD2  sing Y N 412 
TYR CD1 CE1  sing Y N 413 
TYR CD1 HD1  sing N N 414 
TYR CD2 CE2  doub Y N 415 
TYR CD2 HD2  sing N N 416 
TYR CE1 CZ   doub Y N 417 
TYR CE1 HE1  sing N N 418 
TYR CE2 CZ   sing Y N 419 
TYR CE2 HE2  sing N N 420 
TYR CZ  OH   sing N N 421 
TYR OH  HH   sing N N 422 
TYR OXT HXT  sing N N 423 
VAL N   CA   sing N N 424 
VAL N   H    sing N N 425 
VAL N   H2   sing N N 426 
VAL CA  C    sing N N 427 
VAL CA  CB   sing N N 428 
VAL CA  HA   sing N N 429 
VAL C   O    doub N N 430 
VAL C   OXT  sing N N 431 
VAL CB  CG1  sing N N 432 
VAL CB  CG2  sing N N 433 
VAL CB  HB   sing N N 434 
VAL CG1 HG11 sing N N 435 
VAL CG1 HG12 sing N N 436 
VAL CG1 HG13 sing N N 437 
VAL CG2 HG21 sing N N 438 
VAL CG2 HG22 sing N N 439 
VAL CG2 HG23 sing N N 440 
VAL OXT HXT  sing N N 441 
# 
_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   4KNN 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    5LLA 
_atom_sites.fract_transf_matrix[1][1]   0.017850 
_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]   0.017459 
_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]   0.006278 
_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   ? 1.456   12.668  12.585  1.00 41.64 ? 6   SER B N   1 
ATOM   2    C  CA  . SER A 1 6   ? 1.092   11.524  13.469  1.00 44.30 ? 6   SER B CA  1 
ATOM   3    C  C   . SER A 1 6   ? 1.173   10.286  12.591  1.00 41.64 ? 6   SER B C   1 
ATOM   4    O  O   . SER A 1 6   ? 1.439   10.382  11.381  1.00 41.92 ? 6   SER B O   1 
ATOM   5    C  CB  . SER A 1 6   ? -0.329  11.705  14.004  1.00 46.11 ? 6   SER B CB  1 
ATOM   6    O  OG  . SER A 1 6   ? -0.440  11.359  15.374  1.00 49.42 ? 6   SER B OG  1 
ATOM   7    N  N   . TRP A 1 7   ? 0.930   9.127   13.171  1.00 31.40 ? 7   TRP B N   1 
ATOM   8    C  CA  . TRP A 1 7   ? 1.095   7.870   12.415  1.00 27.00 ? 7   TRP B CA  1 
ATOM   9    C  C   . TRP A 1 7   ? 0.098   7.562   11.311  1.00 25.09 ? 7   TRP B C   1 
ATOM   10   O  O   . TRP A 1 7   ? -1.027  8.033   11.355  1.00 25.93 ? 7   TRP B O   1 
ATOM   11   C  CB  . TRP A 1 7   ? 1.208   6.675   13.430  1.00 25.60 ? 7   TRP B CB  1 
ATOM   12   C  CG  . TRP A 1 7   ? -0.130  6.254   14.005  1.00 22.43 ? 7   TRP B CG  1 
ATOM   13   C  CD1 . TRP A 1 7   ? -0.781  6.741   15.142  1.00 22.28 ? 7   TRP B CD1 1 
ATOM   14   C  CD2 . TRP A 1 7   ? -1.025  5.228   13.468  1.00 21.53 ? 7   TRP B CD2 1 
ATOM   15   N  NE1 . TRP A 1 7   ? -1.982  6.098   15.331  1.00 23.48 ? 7   TRP B NE1 1 
ATOM   16   C  CE2 . TRP A 1 7   ? -2.187  5.179   14.360  1.00 21.48 ? 7   TRP B CE2 1 
ATOM   17   C  CE3 . TRP A 1 7   ? -0.980  4.378   12.376  1.00 20.24 ? 7   TRP B CE3 1 
ATOM   18   C  CZ2 . TRP A 1 7   ? -3.242  4.307   14.140  1.00 21.27 ? 7   TRP B CZ2 1 
ATOM   19   C  CZ3 . TRP A 1 7   ? -2.046  3.505   12.164  1.00 21.38 ? 7   TRP B CZ3 1 
ATOM   20   C  CH2 . TRP A 1 7   ? -3.150  3.470   13.025  1.00 22.61 ? 7   TRP B CH2 1 
ATOM   21   N  N   . GLY A 1 8   ? 0.476   6.692   10.349  1.00 21.74 ? 8   GLY B N   1 
ATOM   22   C  CA  . GLY A 1 8   ? -0.435  6.318   9.282   1.00 24.00 ? 8   GLY B CA  1 
ATOM   23   C  C   . GLY A 1 8   ? 0.155   5.198   8.455   1.00 20.50 ? 8   GLY B C   1 
ATOM   24   O  O   . GLY A 1 8   ? 0.921   4.373   8.973   1.00 20.34 ? 8   GLY B O   1 
ATOM   25   N  N   . TYR A 1 9   ? -0.164  5.137   7.150   1.00 19.34 ? 9   TYR B N   1 
ATOM   26   C  CA  . TYR A 1 9   ? 0.360   4.121   6.296   1.00 21.36 ? 9   TYR B CA  1 
ATOM   27   C  C   . TYR A 1 9   ? 1.008   4.703   5.025   1.00 24.90 ? 9   TYR B C   1 
ATOM   28   O  O   . TYR A 1 9   ? 1.269   3.934   4.047   1.00 25.29 ? 9   TYR B O   1 
ATOM   29   C  CB  . TYR A 1 9   ? -0.783  3.204   5.867   1.00 22.05 ? 9   TYR B CB  1 
ATOM   30   C  CG  . TYR A 1 9   ? -1.341  2.391   7.002   1.00 17.83 ? 9   TYR B CG  1 
ATOM   31   C  CD1 . TYR A 1 9   ? -0.772  1.173   7.357   1.00 16.90 ? 9   TYR B CD1 1 
ATOM   32   C  CD2 . TYR A 1 9   ? -2.427  2.849   7.732   1.00 17.76 ? 9   TYR B CD2 1 
ATOM   33   C  CE1 . TYR A 1 9   ? -1.278  0.433   8.409   1.00 15.58 ? 9   TYR B CE1 1 
ATOM   34   C  CE2 . TYR A 1 9   ? -2.937  2.119   8.781   1.00 18.12 ? 9   TYR B CE2 1 
ATOM   35   C  CZ  . TYR A 1 9   ? -2.362  0.908   9.115   1.00 15.68 ? 9   TYR B CZ  1 
ATOM   36   O  OH  . TYR A 1 9   ? -2.877  0.179   10.164  1.00 14.77 ? 9   TYR B OH  1 
ATOM   37   N  N   . ARG A 1 10  ? 1.277   6.022   5.088   1.00 25.58 ? 10  ARG B N   1 
ATOM   38   C  CA  . ARG A 1 10  ? 1.911   6.703   3.939   1.00 29.34 ? 10  ARG B CA  1 
ATOM   39   C  C   . ARG A 1 10  ? 3.408   6.569   4.077   1.00 29.38 ? 10  ARG B C   1 
ATOM   40   O  O   . ARG A 1 10  ? 3.896   5.974   5.044   1.00 26.34 ? 10  ARG B O   1 
ATOM   41   C  CB  . ARG A 1 10  ? 1.493   8.176   3.903   1.00 29.79 ? 10  ARG B CB  1 
ATOM   42   C  CG  . ARG A 1 10  ? -0.004  8.401   3.727   1.00 36.79 ? 10  ARG B CG  1 
ATOM   43   C  CD  . ARG A 1 10  ? -0.376  9.818   4.156   1.00 35.40 ? 10  ARG B CD  1 
ATOM   44   N  NE  . ARG A 1 10  ? -0.246  10.735  3.034   1.00 41.08 ? 10  ARG B NE  1 
ATOM   45   C  CZ  . ARG A 1 10  ? -0.716  11.985  2.982   1.00 40.76 ? 10  ARG B CZ  1 
ATOM   46   N  NH1 . ARG A 1 10  ? -1.411  12.523  3.990   1.00 43.44 ? 10  ARG B NH1 1 
ATOM   47   N  NH2 . ARG A 1 10  ? -0.513  12.685  1.877   1.00 44.24 ? 10  ARG B NH2 1 
ATOM   48   N  N   . GLU A 1 11  ? 4.175   7.139   3.136   1.00 31.35 ? 11  GLU B N   1 
ATOM   49   C  CA  . GLU A 1 11  ? 5.621   6.890   3.115   1.00 32.50 ? 11  GLU B CA  1 
ATOM   50   C  C   . GLU A 1 11  ? 6.402   7.290   4.391   1.00 29.74 ? 11  GLU B C   1 
ATOM   51   O  O   . GLU A 1 11  ? 7.243   6.525   4.881   1.00 30.15 ? 11  GLU B O   1 
ATOM   52   C  CB  . GLU A 1 11  ? 6.251   7.523   1.873   1.00 36.76 ? 11  GLU B CB  1 
ATOM   53   C  CG  . GLU A 1 11  ? 7.744   7.185   1.741   1.00 43.81 ? 11  GLU B CG  1 
ATOM   54   C  CD  . GLU A 1 11  ? 8.520   8.071   0.750   1.00 54.42 ? 11  GLU B CD  1 
ATOM   55   O  OE1 . GLU A 1 11  ? 9.534   7.574   0.198   1.00 54.53 ? 11  GLU B OE1 1 
ATOM   56   O  OE2 . GLU A 1 11  ? 8.138   9.254   0.526   1.00 52.37 ? 11  GLU B OE2 1 
ATOM   57   N  N   . HIS A 1 12  ? 6.095   8.480   4.883   1.00 31.52 ? 12  HIS B N   1 
ATOM   58   C  CA  . HIS A 1 12  ? 6.768   9.160   5.988   1.00 35.08 ? 12  HIS B CA  1 
ATOM   59   C  C   . HIS A 1 12  ? 6.305   8.717   7.343   1.00 32.42 ? 12  HIS B C   1 
ATOM   60   O  O   . HIS A 1 12  ? 7.030   8.854   8.341   1.00 36.15 ? 12  HIS B O   1 
ATOM   61   C  CB  . HIS A 1 12  ? 6.506   10.660  5.845   1.00 45.53 ? 12  HIS B CB  1 
ATOM   62   C  CG  . HIS A 1 12  ? 5.059   11.015  5.442   1.00 53.80 ? 12  HIS B CG  1 
ATOM   63   N  ND1 . HIS A 1 12  ? 4.168   11.595  6.307   1.00 51.67 ? 12  HIS B ND1 1 
ATOM   64   C  CD2 . HIS A 1 12  ? 4.380   10.863  4.219   1.00 51.38 ? 12  HIS B CD2 1 
ATOM   65   C  CE1 . HIS A 1 12  ? 2.995   11.801  5.673   1.00 53.00 ? 12  HIS B CE1 1 
ATOM   66   N  NE2 . HIS A 1 12  ? 3.126   11.359  4.391   1.00 60.03 ? 12  HIS B NE2 1 
ATOM   67   N  N   . ASN A 1 13  ? 5.088   8.154   7.398   1.00 26.98 ? 13  ASN B N   1 
ATOM   68   C  CA  . ASN A 1 13  ? 4.504   7.865   8.691   1.00 24.90 ? 13  ASN B CA  1 
ATOM   69   C  C   . ASN A 1 13  ? 4.090   6.402   8.814   1.00 21.26 ? 13  ASN B C   1 
ATOM   70   O  O   . ASN A 1 13  ? 3.393   6.094   9.802   1.00 24.23 ? 13  ASN B O   1 
ATOM   71   C  CB  . ASN A 1 13  ? 3.334   8.833   9.007   1.00 24.15 ? 13  ASN B CB  1 
ATOM   72   C  CG  . ASN A 1 13  ? 2.098   8.634   8.116   1.00 22.64 ? 13  ASN B CG  1 
ATOM   73   O  OD1 . ASN A 1 13  ? 2.097   7.757   7.249   1.00 27.04 ? 13  ASN B OD1 1 
ATOM   74   N  ND2 . ASN A 1 13  ? 1.099   9.476   8.262   1.00 25.24 ? 13  ASN B ND2 1 
ATOM   75   N  N   . GLY A 1 14  ? 4.472   5.593   7.831   1.00 23.65 ? 14  GLY B N   1 
ATOM   76   C  CA  . GLY A 1 14  ? 3.982   4.178   7.719   1.00 24.85 ? 14  GLY B CA  1 
ATOM   77   C  C   . GLY A 1 14  ? 4.679   3.201   8.643   1.00 24.46 ? 14  GLY B C   1 
ATOM   78   O  O   . GLY A 1 14  ? 5.571   3.564   9.416   1.00 21.75 ? 14  GLY B O   1 
ATOM   79   N  N   . PRO A 1 15  ? 4.244   1.937   8.617   1.00 20.05 ? 15  PRO B N   1 
ATOM   80   C  CA  . PRO A 1 15  ? 4.739   0.865   9.488   1.00 19.67 ? 15  PRO B CA  1 
ATOM   81   C  C   . PRO A 1 15  ? 6.264   0.864   9.715   1.00 23.73 ? 15  PRO B C   1 
ATOM   82   O  O   . PRO A 1 15  ? 6.700   0.689   10.852  1.00 23.06 ? 15  PRO B O   1 
ATOM   83   C  CB  . PRO A 1 15  ? 4.217   -0.401  8.779   1.00 18.19 ? 15  PRO B CB  1 
ATOM   84   C  CG  . PRO A 1 15  ? 2.911   0.033   8.237   1.00 17.99 ? 15  PRO B CG  1 
ATOM   85   C  CD  . PRO A 1 15  ? 3.058   1.509   7.824   1.00 21.52 ? 15  PRO B CD  1 
ATOM   86   N  N   . ILE A 1 16  ? 7.086   1.035   8.662   1.00 26.80 ? 16  ILE B N   1 
ATOM   87   C  CA  . ILE A 1 16  ? 8.549   1.052   8.855   1.00 30.55 ? 16  ILE B CA  1 
ATOM   88   C  C   . ILE A 1 16  ? 9.022   2.168   9.813   1.00 27.12 ? 16  ILE B C   1 
ATOM   89   O  O   . ILE A 1 16  ? 10.042  2.025   10.486  1.00 29.81 ? 16  ILE B O   1 
ATOM   90   C  CB  . ILE A 1 16  ? 9.300   1.061   7.476   1.00 32.18 ? 16  ILE B CB  1 
ATOM   91   C  CG1 . ILE A 1 16  ? 10.653  0.340   7.556   1.00 38.77 ? 16  ILE B CG1 1 
ATOM   92   C  CG2 . ILE A 1 16  ? 9.486   2.459   6.969   1.00 33.67 ? 16  ILE B CG2 1 
ATOM   93   C  CD1 . ILE A 1 16  ? 10.550  -1.184  7.634   1.00 42.94 ? 16  ILE B CD1 1 
ATOM   94   N  N   . HIS A 1 17  ? 8.238   3.226   9.944   1.00 26.37 ? 17  HIS B N   1 
ATOM   95   C  CA  . HIS A 1 17  ? 8.586   4.327   10.843  1.00 27.68 ? 17  HIS B CA  1 
ATOM   96   C  C   . HIS A 1 17  ? 7.945   4.292   12.190  1.00 30.75 ? 17  HIS B C   1 
ATOM   97   O  O   . HIS A 1 17  ? 8.292   5.060   13.079  1.00 26.50 ? 17  HIS B O   1 
ATOM   98   C  CB  . HIS A 1 17  ? 8.247   5.658   10.223  1.00 29.42 ? 17  HIS B CB  1 
ATOM   99   C  CG  . HIS A 1 17  ? 8.971   5.904   8.914   1.00 32.71 ? 17  HIS B CG  1 
ATOM   100  N  ND1 . HIS A 1 17  ? 10.350  5.936   8.812   1.00 34.52 ? 17  HIS B ND1 1 
ATOM   101  C  CD2 . HIS A 1 17  ? 8.483   6.137   7.653   1.00 34.00 ? 17  HIS B CD2 1 
ATOM   102  C  CE1 . HIS A 1 17  ? 10.689  6.168   7.521   1.00 34.24 ? 17  HIS B CE1 1 
ATOM   103  N  NE2 . HIS A 1 17  ? 9.558   6.302   6.812   1.00 38.78 ? 17  HIS B NE2 1 
ATOM   104  N  N   . TRP A 1 18  ? 6.992   3.394   12.421  1.00 23.15 ? 18  TRP B N   1 
ATOM   105  C  CA  . TRP A 1 18  ? 6.394   3.418   13.725  1.00 23.29 ? 18  TRP B CA  1 
ATOM   106  C  C   . TRP A 1 18  ? 7.353   3.235   14.901  1.00 24.13 ? 18  TRP B C   1 
ATOM   107  O  O   . TRP A 1 18  ? 7.041   3.840   15.960  1.00 27.77 ? 18  TRP B O   1 
ATOM   108  C  CB  . TRP A 1 18  ? 5.251   2.368   13.815  1.00 20.70 ? 18  TRP B CB  1 
ATOM   109  C  CG  . TRP A 1 18  ? 4.122   2.620   12.867  1.00 19.14 ? 18  TRP B CG  1 
ATOM   110  C  CD1 . TRP A 1 18  ? 3.874   3.737   12.062  1.00 19.40 ? 18  TRP B CD1 1 
ATOM   111  C  CD2 . TRP A 1 18  ? 3.058   1.668   12.542  1.00 15.88 ? 18  TRP B CD2 1 
ATOM   112  N  NE1 . TRP A 1 18  ? 2.704   3.597   11.381  1.00 19.93 ? 18  TRP B NE1 1 
ATOM   113  C  CE2 . TRP A 1 18  ? 2.180   2.327   11.578  1.00 18.21 ? 18  TRP B CE2 1 
ATOM   114  C  CE3 . TRP A 1 18  ? 2.740   0.362   13.007  1.00 15.86 ? 18  TRP B CE3 1 
ATOM   115  C  CZ2 . TRP A 1 18  ? 1.050   1.731   11.079  1.00 18.55 ? 18  TRP B CZ2 1 
ATOM   116  C  CZ3 . TRP A 1 18  ? 1.601   -0.241  12.471  1.00 15.82 ? 18  TRP B CZ3 1 
ATOM   117  C  CH2 . TRP A 1 18  ? 0.786   0.418   11.526  1.00 16.64 ? 18  TRP B CH2 1 
ATOM   118  N  N   . LYS A 1 19  ? 8.416   2.430   14.731  1.00 28.75 ? 19  LYS B N   1 
ATOM   119  C  CA  . LYS A 1 19  ? 9.455   2.107   15.776  1.00 29.98 ? 19  LYS B CA  1 
ATOM   120  C  C   . LYS A 1 19  ? 10.254  3.315   16.236  1.00 41.83 ? 19  LYS B C   1 
ATOM   121  O  O   . LYS A 1 19  ? 10.828  3.310   17.334  1.00 42.67 ? 19  LYS B O   1 
ATOM   122  C  CB  . LYS A 1 19  ? 10.468  1.063   15.290  1.00 32.29 ? 19  LYS B CB  1 
ATOM   123  C  CG  . LYS A 1 19  ? 11.536  1.564   14.294  1.00 34.35 ? 19  LYS B CG  1 
ATOM   124  C  CD  . LYS A 1 19  ? 12.508  0.415   14.014  1.00 39.16 ? 19  LYS B CD  1 
ATOM   125  C  CE  . LYS A 1 19  ? 13.628  0.756   13.037  1.00 44.94 ? 19  LYS B CE  1 
ATOM   126  N  NZ  . LYS A 1 19  ? 14.854  -0.028  13.394  1.00 54.24 ? 19  LYS B NZ  1 
ATOM   127  N  N   . GLU A 1 20  ? 10.344  4.304   15.348  1.00 40.18 ? 20  GLU B N   1 
ATOM   128  C  CA  . GLU A 1 20  ? 10.944  5.593   15.664  1.00 42.18 ? 20  GLU B CA  1 
ATOM   129  C  C   . GLU A 1 20  ? 10.181  6.295   16.777  1.00 43.73 ? 20  GLU B C   1 
ATOM   130  O  O   . GLU A 1 20  ? 10.805  6.954   17.610  1.00 36.68 ? 20  GLU B O   1 
ATOM   131  C  CB  . GLU A 1 20  ? 10.986  6.475   14.409  1.00 42.24 ? 20  GLU B CB  1 
ATOM   132  C  CG  . GLU A 1 20  ? 11.944  5.948   13.329  1.00 41.31 ? 20  GLU B CG  1 
ATOM   133  C  CD  . GLU A 1 20  ? 11.604  6.485   11.942  1.00 40.05 ? 20  GLU B CD  1 
ATOM   134  O  OE1 . GLU A 1 20  ? 10.888  7.493   11.878  1.00 35.50 ? 20  GLU B OE1 1 
ATOM   135  O  OE2 . GLU A 1 20  ? 12.059  5.909   10.930  1.00 43.10 ? 20  GLU B OE2 1 
ATOM   136  N  N   . PHE A 1 21  ? 8.853   6.136   16.813  1.00 46.35 ? 21  PHE B N   1 
ATOM   137  C  CA  . PHE A 1 21  ? 8.043   6.839   17.834  1.00 51.00 ? 21  PHE B CA  1 
ATOM   138  C  C   . PHE A 1 21  ? 7.142   6.042   18.809  1.00 52.25 ? 21  PHE B C   1 
ATOM   139  O  O   . PHE A 1 21  ? 6.591   6.608   19.766  1.00 48.83 ? 21  PHE B O   1 
ATOM   140  C  CB  . PHE A 1 21  ? 7.343   8.086   17.270  1.00 60.33 ? 21  PHE B CB  1 
ATOM   141  C  CG  . PHE A 1 21  ? 6.610   7.878   15.963  1.00 69.20 ? 21  PHE B CG  1 
ATOM   142  C  CD1 . PHE A 1 21  ? 5.196   7.943   15.917  1.00 67.89 ? 21  PHE B CD1 1 
ATOM   143  C  CD2 . PHE A 1 21  ? 7.309   7.694   14.758  1.00 64.66 ? 21  PHE B CD2 1 
ATOM   144  C  CE1 . PHE A 1 21  ? 4.504   7.788   14.708  1.00 64.36 ? 21  PHE B CE1 1 
ATOM   145  C  CE2 . PHE A 1 21  ? 6.611   7.535   13.546  1.00 71.86 ? 21  PHE B CE2 1 
ATOM   146  C  CZ  . PHE A 1 21  ? 5.211   7.587   13.519  1.00 66.08 ? 21  PHE B CZ  1 
ATOM   147  N  N   . PHE A 1 22  ? 7.004   4.732   18.561  1.00 43.46 ? 22  PHE B N   1 
ATOM   148  C  CA  . PHE A 1 22  ? 6.445   3.779   19.522  1.00 42.49 ? 22  PHE B CA  1 
ATOM   149  C  C   . PHE A 1 22  ? 7.434   2.631   19.602  1.00 35.36 ? 22  PHE B C   1 
ATOM   150  O  O   . PHE A 1 22  ? 7.316   1.669   18.856  1.00 33.24 ? 22  PHE B O   1 
ATOM   151  C  CB  . PHE A 1 22  ? 5.078   3.241   19.048  1.00 41.21 ? 22  PHE B CB  1 
ATOM   152  C  CG  . PHE A 1 22  ? 3.993   4.265   19.025  1.00 41.48 ? 22  PHE B CG  1 
ATOM   153  C  CD1 . PHE A 1 22  ? 3.168   4.433   20.122  1.00 38.36 ? 22  PHE B CD1 1 
ATOM   154  C  CD2 . PHE A 1 22  ? 3.788   5.072   17.886  1.00 41.37 ? 22  PHE B CD2 1 
ATOM   155  C  CE1 . PHE A 1 22  ? 2.150   5.370   20.103  1.00 41.00 ? 22  PHE B CE1 1 
ATOM   156  C  CE2 . PHE A 1 22  ? 2.800   6.020   17.873  1.00 42.21 ? 22  PHE B CE2 1 
ATOM   157  C  CZ  . PHE A 1 22  ? 1.964   6.164   18.983  1.00 41.62 ? 22  PHE B CZ  1 
ATOM   158  N  N   . PRO A 1 23  ? 8.428   2.705   20.518  1.00 31.97 ? 23  PRO B N   1 
ATOM   159  C  CA  . PRO A 1 23  ? 9.529   1.752   20.573  1.00 30.88 ? 23  PRO B CA  1 
ATOM   160  C  C   . PRO A 1 23  ? 9.132   0.269   20.720  1.00 25.61 ? 23  PRO B C   1 
ATOM   161  O  O   . PRO A 1 23  ? 9.883   -0.660  20.333  1.00 27.34 ? 23  PRO B O   1 
ATOM   162  C  CB  . PRO A 1 23  ? 10.299  2.208   21.788  1.00 29.67 ? 23  PRO B CB  1 
ATOM   163  C  CG  . PRO A 1 23  ? 10.119  3.665   21.739  1.00 36.45 ? 23  PRO B CG  1 
ATOM   164  C  CD  . PRO A 1 23  ? 8.676   3.865   21.402  1.00 31.99 ? 23  PRO B CD  1 
ATOM   165  N  N   . ILE A 1 24  ? 7.921   0.046   21.281  1.00 25.89 ? 24  ILE B N   1 
ATOM   166  C  CA  . ILE A 1 24  ? 7.497   -1.328  21.462  1.00 22.79 ? 24  ILE B CA  1 
ATOM   167  C  C   . ILE A 1 24  ? 7.232   -1.933  20.066  1.00 21.50 ? 24  ILE B C   1 
ATOM   168  O  O   . ILE A 1 24  ? 7.093   -3.121  19.965  1.00 22.23 ? 24  ILE B O   1 
ATOM   169  C  CB  . ILE A 1 24  ? 6.193   -1.420  22.329  1.00 21.60 ? 24  ILE B CB  1 
ATOM   170  C  CG1 . ILE A 1 24  ? 5.980   -2.838  22.866  1.00 21.77 ? 24  ILE B CG1 1 
ATOM   171  C  CG2 . ILE A 1 24  ? 4.947   -0.891  21.578  1.00 21.04 ? 24  ILE B CG2 1 
ATOM   172  C  CD1 . ILE A 1 24  ? 7.099   -3.361  23.765  1.00 29.08 ? 24  ILE B CD1 1 
ATOM   173  N  N   . ALA A 1 25  ? 7.244   -1.101  19.017  1.00 22.72 ? 25  ALA B N   1 
ATOM   174  C  CA  . ALA A 1 25  ? 7.152   -1.650  17.629  1.00 22.21 ? 25  ALA B CA  1 
ATOM   175  C  C   . ALA A 1 25  ? 8.173   -2.721  17.361  1.00 20.49 ? 25  ALA B C   1 
ATOM   176  O  O   . ALA A 1 25  ? 7.937   -3.641  16.558  1.00 23.07 ? 25  ALA B O   1 
ATOM   177  C  CB  . ALA A 1 25  ? 7.324   -0.524  16.619  1.00 21.63 ? 25  ALA B CB  1 
ATOM   178  N  N   . ASP A 1 26  ? 9.336   -2.663  18.047  1.00 22.64 ? 26  ASP B N   1 
ATOM   179  C  CA  . ASP A 1 26  ? 10.377  -3.615  17.999  1.00 27.08 ? 26  ASP B CA  1 
ATOM   180  C  C   . ASP A 1 26  ? 10.422  -4.577  19.200  1.00 24.81 ? 26  ASP B C   1 
ATOM   181  O  O   . ASP A 1 26  ? 11.455  -5.205  19.460  1.00 24.88 ? 26  ASP B O   1 
ATOM   182  C  CB  . ASP A 1 26  ? 11.748  -2.859  17.916  1.00 32.00 ? 26  ASP B CB  1 
ATOM   183  C  CG  . ASP A 1 26  ? 12.168  -2.526  16.467  1.00 39.27 ? 26  ASP B CG  1 
ATOM   184  O  OD1 . ASP A 1 26  ? 11.365  -2.635  15.506  1.00 42.23 ? 26  ASP B OD1 1 
ATOM   185  O  OD2 . ASP A 1 26  ? 13.344  -2.174  16.279  1.00 40.63 ? 26  ASP B OD2 1 
ATOM   186  N  N   . GLY A 1 27  ? 9.275   -4.749  19.843  1.00 23.74 ? 27  GLY B N   1 
ATOM   187  C  CA  . GLY A 1 27  ? 9.166   -5.681  20.964  1.00 23.67 ? 27  GLY B CA  1 
ATOM   188  C  C   . GLY A 1 27  ? 9.184   -7.158  20.593  1.00 23.13 ? 27  GLY B C   1 
ATOM   189  O  O   . GLY A 1 27  ? 9.249   -7.579  19.424  1.00 25.89 ? 27  GLY B O   1 
ATOM   190  N  N   . ASP A 1 28  ? 9.049   -7.968  21.634  1.00 21.43 ? 28  ASP B N   1 
ATOM   191  C  CA  . ASP A 1 28  ? 9.144   -9.356  21.519  1.00 21.22 ? 28  ASP B CA  1 
ATOM   192  C  C   . ASP A 1 28  ? 7.836   -10.099 21.164  1.00 18.57 ? 28  ASP B C   1 
ATOM   193  O  O   . ASP A 1 28  ? 7.901   -11.299 20.850  1.00 20.95 ? 28  ASP B O   1 
ATOM   194  C  CB  . ASP A 1 28  ? 9.539   -9.884  22.930  1.00 29.33 ? 28  ASP B CB  1 
ATOM   195  C  CG  . ASP A 1 28  ? 11.069  -9.748  23.253  1.00 37.51 ? 28  ASP B CG  1 
ATOM   196  O  OD1 . ASP A 1 28  ? 11.870  -9.214  22.455  1.00 35.74 ? 28  ASP B OD1 1 
ATOM   197  O  OD2 . ASP A 1 28  ? 11.439  -10.244 24.329  1.00 38.40 ? 28  ASP B OD2 1 
ATOM   198  N  N   . GLN A 1 29  ? 6.722   -9.365  21.271  1.00 19.04 ? 29  GLN B N   1 
ATOM   199  C  CA  . GLN A 1 29  ? 5.396   -10.012 21.048  1.00 17.56 ? 29  GLN B CA  1 
ATOM   200  C  C   . GLN A 1 29  ? 4.499   -9.184  20.095  1.00 14.87 ? 29  GLN B C   1 
ATOM   201  O  O   . GLN A 1 29  ? 3.378   -8.816  20.392  1.00 15.08 ? 29  GLN B O   1 
ATOM   202  C  CB  . GLN A 1 29  ? 4.665   -10.358 22.334  1.00 18.50 ? 29  GLN B CB  1 
ATOM   203  C  CG  . GLN A 1 29  ? 5.599   -11.178 23.249  1.00 21.61 ? 29  GLN B CG  1 
ATOM   204  C  CD  . GLN A 1 29  ? 4.851   -12.133 24.181  1.00 25.00 ? 29  GLN B CD  1 
ATOM   205  O  OE1 . GLN A 1 29  ? 5.403   -13.201 24.572  1.00 27.92 ? 29  GLN B OE1 1 
ATOM   206  N  NE2 . GLN A 1 29  ? 3.662   -11.770 24.557  1.00 21.13 ? 29  GLN B NE2 1 
ATOM   207  N  N   . GLN A 1 30  ? 5.148   -8.843  18.951  1.00 16.56 ? 30  GLN B N   1 
ATOM   208  C  CA  . GLN A 1 30  ? 4.475   -7.994  17.949  1.00 16.29 ? 30  GLN B CA  1 
ATOM   209  C  C   . GLN A 1 30  ? 3.701   -8.821  16.907  1.00 11.81 ? 30  GLN B C   1 
ATOM   210  O  O   . GLN A 1 30  ? 4.018   -9.933  16.592  1.00 13.70 ? 30  GLN B O   1 
ATOM   211  C  CB  . GLN A 1 30  ? 5.524   -7.081  17.303  1.00 16.03 ? 30  GLN B CB  1 
ATOM   212  C  CG  . GLN A 1 30  ? 6.008   -6.007  18.273  1.00 16.13 ? 30  GLN B CG  1 
ATOM   213  C  CD  . GLN A 1 30  ? 4.940   -5.003  18.568  1.00 16.77 ? 30  GLN B CD  1 
ATOM   214  O  OE1 . GLN A 1 30  ? 4.514   -4.251  17.723  1.00 15.15 ? 30  GLN B OE1 1 
ATOM   215  N  NE2 . GLN A 1 30  ? 4.474   -4.943  19.871  1.00 14.33 ? 30  GLN B NE2 1 
ATOM   216  N  N   . SER A 1 31  ? 2.639   -8.173  16.457  1.00 12.32 ? 31  SER B N   1 
ATOM   217  C  CA  . SER A 1 31  ? 1.755   -8.749  15.450  1.00 11.99 ? 31  SER B CA  1 
ATOM   218  C  C   . SER A 1 31  ? 1.658   -7.794  14.239  1.00 11.79 ? 31  SER B C   1 
ATOM   219  O  O   . SER A 1 31  ? 1.808   -6.591  14.370  1.00 13.34 ? 31  SER B O   1 
ATOM   220  C  CB  . SER A 1 31  ? 0.378   -8.826  16.087  1.00 13.11 ? 31  SER B CB  1 
ATOM   221  O  OG  . SER A 1 31  ? 0.412   -9.853  17.108  1.00 12.70 ? 31  SER B OG  1 
ATOM   222  N  N   . PRO A 1 32  ? 1.282   -8.350  13.068  1.00 11.77 ? 32  PRO B N   1 
ATOM   223  C  CA  . PRO A 1 32  ? 0.939   -9.738  12.763  1.00 11.54 ? 32  PRO B CA  1 
ATOM   224  C  C   . PRO A 1 32  ? 2.149   -10.551 12.530  1.00 11.98 ? 32  PRO B C   1 
ATOM   225  O  O   . PRO A 1 32  ? 3.260   -10.063 12.719  1.00 13.31 ? 32  PRO B O   1 
ATOM   226  C  CB  . PRO A 1 32  ? 0.092   -9.588  11.462  1.00 11.91 ? 32  PRO B CB  1 
ATOM   227  C  CG  . PRO A 1 32  ? 0.884   -8.423  10.752  1.00 11.67 ? 32  PRO B CG  1 
ATOM   228  C  CD  . PRO A 1 32  ? 1.238   -7.439  11.864  1.00 11.88 ? 32  PRO B CD  1 
ATOM   229  N  N   . ILE A 1 33  ? 1.957   -11.796 12.131  1.00 13.44 ? 33  ILE B N   1 
ATOM   230  C  CA  . ILE A 1 33  ? 3.072   -12.750 11.941  1.00 13.24 ? 33  ILE B CA  1 
ATOM   231  C  C   . ILE A 1 33  ? 2.820   -13.555 10.707  1.00 13.93 ? 33  ILE B C   1 
ATOM   232  O  O   . ILE A 1 33  ? 1.696   -13.639 10.203  1.00 13.94 ? 33  ILE B O   1 
ATOM   233  C  CB  . ILE A 1 33  ? 3.319   -13.748 13.176  1.00 14.32 ? 33  ILE B CB  1 
ATOM   234  C  CG1 . ILE A 1 33  ? 2.080   -14.622 13.442  1.00 16.53 ? 33  ILE B CG1 1 
ATOM   235  C  CG2 . ILE A 1 33  ? 3.802   -12.944 14.405  1.00 15.35 ? 33  ILE B CG2 1 
ATOM   236  C  CD1 . ILE A 1 33  ? 2.364   -15.806 14.359  1.00 16.29 ? 33  ILE B CD1 1 
ATOM   237  N  N   . GLU A 1 34  ? 3.872   -14.242 10.273  1.00 14.69 ? 34  GLU B N   1 
ATOM   238  C  CA  . GLU A 1 34  ? 3.731   -15.329 9.321   1.00 14.68 ? 34  GLU B CA  1 
ATOM   239  C  C   . GLU A 1 34  ? 3.268   -16.612 10.062  1.00 15.96 ? 34  GLU B C   1 
ATOM   240  O  O   . GLU A 1 34  ? 3.949   -17.017 11.056  1.00 17.54 ? 34  GLU B O   1 
ATOM   241  C  CB  . GLU A 1 34  ? 5.064   -15.678 8.758   1.00 16.07 ? 34  GLU B CB  1 
ATOM   242  C  CG  . GLU A 1 34  ? 5.819   -14.538 8.117   1.00 22.47 ? 34  GLU B CG  1 
ATOM   243  C  CD  . GLU A 1 34  ? 5.347   -14.123 6.744   1.00 21.37 ? 34  GLU B CD  1 
ATOM   244  O  OE1 . GLU A 1 34  ? 4.611   -14.893 6.089   1.00 21.69 ? 34  GLU B OE1 1 
ATOM   245  O  OE2 . GLU A 1 34  ? 5.763   -13.010 6.347   1.00 24.87 ? 34  GLU B OE2 1 
ATOM   246  N  N   . ILE A 1 35  ? 2.194   -17.237 9.574   1.00 13.80 ? 35  ILE B N   1 
ATOM   247  C  CA  . ILE A 1 35  ? 1.755   -18.525 10.094  1.00 14.84 ? 35  ILE B CA  1 
ATOM   248  C  C   . ILE A 1 35  ? 2.232   -19.637 9.135   1.00 15.91 ? 35  ILE B C   1 
ATOM   249  O  O   . ILE A 1 35  ? 1.874   -19.661 7.998   1.00 17.83 ? 35  ILE B O   1 
ATOM   250  C  CB  . ILE A 1 35  ? 0.217   -18.511 10.169  1.00 15.33 ? 35  ILE B CB  1 
ATOM   251  C  CG1 . ILE A 1 35  ? -0.175  -17.429 11.211  1.00 15.71 ? 35  ILE B CG1 1 
ATOM   252  C  CG2 . ILE A 1 35  ? -0.294  -19.874 10.654  1.00 18.35 ? 35  ILE B CG2 1 
ATOM   253  C  CD1 . ILE A 1 35  ? -1.640  -17.099 11.260  1.00 19.46 ? 35  ILE B CD1 1 
ATOM   254  N  N   . LYS A 1 36  ? 3.168   -20.447 9.638   1.00 16.34 ? 36  LYS B N   1 
ATOM   255  C  CA  . LYS A 1 36  ? 3.764   -21.551 8.917   1.00 16.26 ? 36  LYS B CA  1 
ATOM   256  C  C   . LYS A 1 36  ? 3.111   -22.798 9.465   1.00 16.06 ? 36  LYS B C   1 
ATOM   257  O  O   . LYS A 1 36  ? 3.436   -23.152 10.616  1.00 19.16 ? 36  LYS B O   1 
ATOM   258  C  CB  . LYS A 1 36  ? 5.275   -21.575 9.139   1.00 17.10 ? 36  LYS B CB  1 
ATOM   259  C  CG  . LYS A 1 36  ? 6.061   -20.369 8.566   1.00 18.70 ? 36  LYS B CG  1 
ATOM   260  C  CD  . LYS A 1 36  ? 7.535   -20.461 8.841   1.00 19.66 ? 36  LYS B CD  1 
ATOM   261  C  CE  . LYS A 1 36  ? 8.350   -19.281 8.371   1.00 21.94 ? 36  LYS B CE  1 
ATOM   262  N  NZ  . LYS A 1 36  ? 9.750   -19.434 8.833   1.00 22.58 ? 36  LYS B NZ  1 
ATOM   263  N  N   . THR A 1 37  ? 2.231   -23.382 8.650   1.00 21.05 ? 37  THR B N   1 
ATOM   264  C  CA  . THR A 1 37  ? 1.325   -24.455 9.166   1.00 23.42 ? 37  THR B CA  1 
ATOM   265  C  C   . THR A 1 37  ? 2.097   -25.698 9.638   1.00 27.21 ? 37  THR B C   1 
ATOM   266  O  O   . THR A 1 37  ? 1.619   -26.411 10.504  1.00 26.11 ? 37  THR B O   1 
ATOM   267  C  CB  . THR A 1 37  ? 0.231   -24.831 8.172   1.00 28.45 ? 37  THR B CB  1 
ATOM   268  O  OG1 . THR A 1 37  ? 0.828   -25.282 6.946   1.00 26.97 ? 37  THR B OG1 1 
ATOM   269  C  CG2 . THR A 1 37  ? -0.629  -23.666 7.904   1.00 25.08 ? 37  THR B CG2 1 
ATOM   270  N  N   . LYS A 1 38  ? 3.261   -25.982 9.056   1.00 27.95 ? 38  LYS B N   1 
ATOM   271  C  CA  . LYS A 1 38  ? 4.148   -27.085 9.516   1.00 28.31 ? 38  LYS B CA  1 
ATOM   272  C  C   . LYS A 1 38  ? 4.889   -26.851 10.841  1.00 26.67 ? 38  LYS B C   1 
ATOM   273  O  O   . LYS A 1 38  ? 5.420   -27.825 11.433  1.00 28.84 ? 38  LYS B O   1 
ATOM   274  C  CB  . LYS A 1 38  ? 5.155   -27.496 8.392   1.00 31.12 ? 38  LYS B CB  1 
ATOM   275  C  CG  . LYS A 1 38  ? 4.695   -28.659 7.485   1.00 40.21 ? 38  LYS B CG  1 
ATOM   276  C  CD  . LYS A 1 38  ? 5.445   -29.943 7.904   1.00 45.61 ? 38  LYS B CD  1 
ATOM   277  C  CE  . LYS A 1 38  ? 4.568   -31.190 8.099   1.00 51.00 ? 38  LYS B CE  1 
ATOM   278  N  NZ  . LYS A 1 38  ? 4.352   -32.060 6.886   1.00 49.70 ? 38  LYS B NZ  1 
ATOM   279  N  N   . GLU A 1 39  ? 4.978   -25.604 11.301  1.00 21.73 ? 39  GLU B N   1 
ATOM   280  C  CA  . GLU A 1 39  ? 5.630   -25.266 12.537  1.00 23.20 ? 39  GLU B CA  1 
ATOM   281  C  C   . GLU A 1 39  ? 4.646   -25.073 13.675  1.00 21.44 ? 39  GLU B C   1 
ATOM   282  O  O   . GLU A 1 39  ? 5.028   -24.879 14.835  1.00 24.07 ? 39  GLU B O   1 
ATOM   283  C  CB  . GLU A 1 39  ? 6.410   -23.961 12.340  1.00 26.13 ? 39  GLU B CB  1 
ATOM   284  C  CG  . GLU A 1 39  ? 7.353   -24.035 11.118  1.00 27.15 ? 39  GLU B CG  1 
ATOM   285  C  CD  . GLU A 1 39  ? 8.285   -25.197 11.233  1.00 33.53 ? 39  GLU B CD  1 
ATOM   286  O  OE1 . GLU A 1 39  ? 8.910   -25.325 12.329  1.00 38.79 ? 39  GLU B OE1 1 
ATOM   287  O  OE2 . GLU A 1 39  ? 8.323   -26.015 10.289  1.00 32.75 ? 39  GLU B OE2 1 
ATOM   288  N  N   . VAL A 1 40  ? 3.357   -25.012 13.330  1.00 20.59 ? 40  VAL B N   1 
ATOM   289  C  CA  . VAL A 1 40  ? 2.399   -24.754 14.383  1.00 19.65 ? 40  VAL B CA  1 
ATOM   290  C  C   . VAL A 1 40  ? 2.265   -26.027 15.208  1.00 20.71 ? 40  VAL B C   1 
ATOM   291  O  O   . VAL A 1 40  ? 2.492   -27.112 14.683  1.00 21.69 ? 40  VAL B O   1 
ATOM   292  C  CB  . VAL A 1 40  ? 1.037   -24.246 13.867  1.00 19.67 ? 40  VAL B CB  1 
ATOM   293  C  CG1 . VAL A 1 40  ? 1.243   -22.923 13.120  1.00 21.64 ? 40  VAL B CG1 1 
ATOM   294  C  CG2 . VAL A 1 40  ? 0.264   -25.286 13.093  1.00 23.86 ? 40  VAL B CG2 1 
ATOM   295  N  N   . LYS A 1 41  ? 2.027   -25.865 16.495  1.00 20.98 ? 41  LYS B N   1 
ATOM   296  C  CA  . LYS A 1 41  ? 1.825   -26.980 17.391  1.00 22.48 ? 41  LYS B CA  1 
ATOM   297  C  C   . LYS A 1 41  ? 0.324   -27.237 17.624  1.00 17.74 ? 41  LYS B C   1 
ATOM   298  O  O   . LYS A 1 41  ? -0.321  -26.383 18.257  1.00 18.92 ? 41  LYS B O   1 
ATOM   299  C  CB  . LYS A 1 41  ? 2.488   -26.592 18.756  1.00 26.24 ? 41  LYS B CB  1 
ATOM   300  C  CG  . LYS A 1 41  ? 3.991   -26.361 18.728  1.00 39.77 ? 41  LYS B CG  1 
ATOM   301  C  CD  . LYS A 1 41  ? 4.700   -27.588 18.136  1.00 43.78 ? 41  LYS B CD  1 
ATOM   302  C  CE  . LYS A 1 41  ? 6.003   -27.884 18.883  1.00 55.18 ? 41  LYS B CE  1 
ATOM   303  N  NZ  . LYS A 1 41  ? 7.054   -28.300 17.914  1.00 62.57 ? 41  LYS B NZ  1 
ATOM   304  N  N   . TYR A 1 42  ? -0.193  -28.408 17.218  1.00 19.18 ? 42  TYR B N   1 
ATOM   305  C  CA  . TYR A 1 42  ? -1.502  -28.811 17.679  1.00 20.44 ? 42  TYR B CA  1 
ATOM   306  C  C   . TYR A 1 42  ? -1.574  -28.924 19.197  1.00 20.01 ? 42  TYR B C   1 
ATOM   307  O  O   . TYR A 1 42  ? -0.684  -29.474 19.833  1.00 21.02 ? 42  TYR B O   1 
ATOM   308  C  CB  . TYR A 1 42  ? -1.926  -30.154 17.107  1.00 21.29 ? 42  TYR B CB  1 
ATOM   309  C  CG  . TYR A 1 42  ? -3.226  -30.619 17.684  1.00 22.12 ? 42  TYR B CG  1 
ATOM   310  C  CD1 . TYR A 1 42  ? -4.448  -29.976 17.349  1.00 22.84 ? 42  TYR B CD1 1 
ATOM   311  C  CD2 . TYR A 1 42  ? -3.276  -31.775 18.534  1.00 24.36 ? 42  TYR B CD2 1 
ATOM   312  C  CE1 . TYR A 1 42  ? -5.671  -30.436 17.860  1.00 23.11 ? 42  TYR B CE1 1 
ATOM   313  C  CE2 . TYR A 1 42  ? -4.478  -32.227 19.051  1.00 23.89 ? 42  TYR B CE2 1 
ATOM   314  C  CZ  . TYR A 1 42  ? -5.673  -31.598 18.706  1.00 25.56 ? 42  TYR B CZ  1 
ATOM   315  O  OH  . TYR A 1 42  ? -6.900  -32.019 19.186  1.00 27.04 ? 42  TYR B OH  1 
ATOM   316  N  N   . ASP A 1 43  ? -2.601  -28.322 19.786  1.00 19.29 ? 43  ASP B N   1 
ATOM   317  C  CA  . ASP A 1 43  ? -2.724  -28.319 21.209  1.00 18.50 ? 43  ASP B CA  1 
ATOM   318  C  C   . ASP A 1 43  ? -4.122  -28.825 21.589  1.00 20.01 ? 43  ASP B C   1 
ATOM   319  O  O   . ASP A 1 43  ? -5.151  -28.098 21.399  1.00 18.45 ? 43  ASP B O   1 
ATOM   320  C  CB  . ASP A 1 43  ? -2.456  -26.944 21.810  1.00 18.52 ? 43  ASP B CB  1 
ATOM   321  C  CG  . ASP A 1 43  ? -2.375  -26.978 23.304  1.00 20.22 ? 43  ASP B CG  1 
ATOM   322  O  OD1 . ASP A 1 43  ? -2.911  -27.957 23.920  1.00 21.39 ? 43  ASP B OD1 1 
ATOM   323  O  OD2 . ASP A 1 43  ? -1.836  -26.037 23.862  1.00 22.29 ? 43  ASP B OD2 1 
ATOM   324  N  N   . SER A 1 44  ? -4.179  -30.072 22.142  1.00 21.59 ? 44  SER B N   1 
ATOM   325  C  CA  . SER A 1 44  ? -5.459  -30.690 22.510  1.00 24.51 ? 44  SER B CA  1 
ATOM   326  C  C   . SER A 1 44  ? -6.132  -29.988 23.692  1.00 23.11 ? 44  SER B C   1 
ATOM   327  O  O   . SER A 1 44  ? -7.343  -30.169 23.870  1.00 28.21 ? 44  SER B O   1 
ATOM   328  C  CB  . SER A 1 44  ? -5.299  -32.239 22.721  1.00 26.44 ? 44  SER B CB  1 
ATOM   329  O  OG  . SER A 1 44  ? -4.488  -32.444 23.846  1.00 28.20 ? 44  SER B OG  1 
ATOM   330  N  N   . SER A 1 45  ? -5.435  -29.129 24.446  1.00 19.76 ? 45  SER B N   1 
ATOM   331  C  CA  . SER A 1 45  ? -6.009  -28.372 25.540  1.00 22.47 ? 45  SER B CA  1 
ATOM   332  C  C   . SER A 1 45  ? -6.848  -27.119 25.035  1.00 19.35 ? 45  SER B C   1 
ATOM   333  O  O   . SER A 1 45  ? -7.706  -26.593 25.777  1.00 22.27 ? 45  SER B O   1 
ATOM   334  C  CB  . SER A 1 45  ? -4.947  -27.968 26.573  1.00 24.47 ? 45  SER B CB  1 
ATOM   335  O  OG  . SER A 1 45  ? -4.125  -26.852 26.220  1.00 23.98 ? 45  SER B OG  1 
ATOM   336  N  N   . LEU A 1 46  ? -6.634  -26.693 23.790  1.00 17.95 ? 46  LEU B N   1 
ATOM   337  C  CA  . LEU A 1 46  ? -7.418  -25.576 23.271  1.00 18.26 ? 46  LEU B CA  1 
ATOM   338  C  C   . LEU A 1 46  ? -8.867  -26.000 23.103  1.00 18.17 ? 46  LEU B C   1 
ATOM   339  O  O   . LEU A 1 46  ? -9.175  -27.120 22.622  1.00 20.57 ? 46  LEU B O   1 
ATOM   340  C  CB  . LEU A 1 46  ? -6.921  -25.199 21.855  1.00 16.34 ? 46  LEU B CB  1 
ATOM   341  C  CG  . LEU A 1 46  ? -5.571  -24.438 21.876  1.00 15.82 ? 46  LEU B CG  1 
ATOM   342  C  CD1 . LEU A 1 46  ? -4.946  -24.260 20.458  1.00 15.34 ? 46  LEU B CD1 1 
ATOM   343  C  CD2 . LEU A 1 46  ? -5.820  -23.083 22.548  1.00 17.04 ? 46  LEU B CD2 1 
ATOM   344  N  N   . ARG A 1 47  ? -9.729  -25.037 23.260  1.00 14.51 ? 47  ARG B N   1 
ATOM   345  C  CA  . ARG A 1 47  ? -11.148 -25.297 23.229  1.00 14.53 ? 47  ARG B CA  1 
ATOM   346  C  C   . ARG A 1 47  ? -11.771 -24.772 21.932  1.00 14.70 ? 47  ARG B C   1 
ATOM   347  O  O   . ARG A 1 47  ? -11.203 -23.884 21.327  1.00 16.00 ? 47  ARG B O   1 
ATOM   348  C  CB  . ARG A 1 47  ? -11.862 -24.617 24.394  1.00 16.08 ? 47  ARG B CB  1 
ATOM   349  C  CG  . ARG A 1 47  ? -11.516 -25.420 25.664  1.00 18.48 ? 47  ARG B CG  1 
ATOM   350  C  CD  . ARG A 1 47  ? -12.173 -24.772 26.824  1.00 20.20 ? 47  ARG B CD  1 
ATOM   351  N  NE  . ARG A 1 47  ? -11.837 -25.574 28.033  1.00 23.90 ? 47  ARG B NE  1 
ATOM   352  C  CZ  . ARG A 1 47  ? -12.031 -25.077 29.258  1.00 25.79 ? 47  ARG B CZ  1 
ATOM   353  N  NH1 . ARG A 1 47  ? -12.532 -23.835 29.393  1.00 29.48 ? 47  ARG B NH1 1 
ATOM   354  N  NH2 . ARG A 1 47  ? -11.704 -25.801 30.316  1.00 27.15 ? 47  ARG B NH2 1 
ATOM   355  N  N   . PRO A 1 48  ? -12.890 -25.337 21.510  1.00 13.89 ? 48  PRO B N   1 
ATOM   356  C  CA  . PRO A 1 48  ? -13.642 -24.618 20.413  1.00 13.87 ? 48  PRO B CA  1 
ATOM   357  C  C   . PRO A 1 48  ? -14.017 -23.220 20.831  1.00 13.48 ? 48  PRO B C   1 
ATOM   358  O  O   . PRO A 1 48  ? -14.184 -22.889 22.011  1.00 13.59 ? 48  PRO B O   1 
ATOM   359  C  CB  . PRO A 1 48  ? -14.902 -25.433 20.231  1.00 13.45 ? 48  PRO B CB  1 
ATOM   360  C  CG  . PRO A 1 48  ? -14.551 -26.877 20.743  1.00 14.19 ? 48  PRO B CG  1 
ATOM   361  C  CD  . PRO A 1 48  ? -13.643 -26.525 21.937  1.00 14.84 ? 48  PRO B CD  1 
ATOM   362  N  N   . LEU A 1 49  ? -14.198 -22.337 19.858  1.00 13.16 ? 49  LEU B N   1 
ATOM   363  C  CA  . LEU A 1 49  ? -14.623 -20.989 20.251  1.00 12.84 ? 49  LEU B CA  1 
ATOM   364  C  C   . LEU A 1 49  ? -16.095 -21.056 20.655  1.00 12.57 ? 49  LEU B C   1 
ATOM   365  O  O   . LEU A 1 49  ? -16.916 -21.689 19.981  1.00 13.24 ? 49  LEU B O   1 
ATOM   366  C  CB  . LEU A 1 49  ? -14.500 -20.078 19.020  1.00 13.59 ? 49  LEU B CB  1 
ATOM   367  C  CG  . LEU A 1 49  ? -13.055 -19.954 18.502  1.00 13.01 ? 49  LEU B CG  1 
ATOM   368  C  CD1 . LEU A 1 49  ? -13.067 -19.095 17.230  1.00 14.34 ? 49  LEU B CD1 1 
ATOM   369  C  CD2 . LEU A 1 49  ? -12.212 -19.383 19.676  1.00 15.45 ? 49  LEU B CD2 1 
ATOM   370  N  N   . SER A 1 50  ? -16.416 -20.282 21.719  1.00 12.54 ? 50  SER B N   1 
ATOM   371  C  CA  . SER A 1 50  ? -17.770 -20.094 22.179  1.00 12.98 ? 50  SER B CA  1 
ATOM   372  C  C   . SER A 1 50  ? -18.168 -18.613 21.897  1.00 12.16 ? 50  SER B C   1 
ATOM   373  O  O   . SER A 1 50  ? -17.626 -17.702 22.518  1.00 13.22 ? 50  SER B O   1 
ATOM   374  C  CB  . SER A 1 50  ? -17.779 -20.326 23.717  1.00 12.77 ? 50  SER B CB  1 
ATOM   375  O  OG  . SER A 1 50  ? -19.052 -19.884 24.256  1.00 16.84 ? 50  SER B OG  1 
ATOM   376  N  N   . ILE A 1 51  ? -19.032 -18.425 20.899  1.00 11.76 ? 51  ILE B N   1 
ATOM   377  C  CA  . ILE A 1 51  ? -19.254 -17.076 20.298  1.00 11.27 ? 51  ILE B CA  1 
ATOM   378  C  C   . ILE A 1 51  ? -20.691 -16.683 20.462  1.00 12.76 ? 51  ILE B C   1 
ATOM   379  O  O   . ILE A 1 51  ? -21.579 -17.377 20.063  1.00 12.65 ? 51  ILE B O   1 
ATOM   380  C  CB  . ILE A 1 51  ? -18.852 -17.143 18.806  1.00 12.33 ? 51  ILE B CB  1 
ATOM   381  C  CG1 . ILE A 1 51  ? -17.427 -17.717 18.639  1.00 12.58 ? 51  ILE B CG1 1 
ATOM   382  C  CG2 . ILE A 1 51  ? -18.876 -15.685 18.265  1.00 16.61 ? 51  ILE B CG2 1 
ATOM   383  C  CD1 . ILE A 1 51  ? -17.074 -17.631 17.121  1.00 13.23 ? 51  ILE B CD1 1 
ATOM   384  N  N   . LYS A 1 52  ? -20.930 -15.530 21.071  1.00 13.10 ? 52  LYS B N   1 
ATOM   385  C  CA  . LYS A 1 52  ? -22.213 -14.946 21.170  1.00 13.80 ? 52  LYS B CA  1 
ATOM   386  C  C   . LYS A 1 52  ? -22.173 -13.499 20.772  1.00 14.07 ? 52  LYS B C   1 
ATOM   387  O  O   . LYS A 1 52  ? -21.550 -12.681 21.447  1.00 13.37 ? 52  LYS B O   1 
ATOM   388  C  CB  . LYS A 1 52  ? -22.739 -15.003 22.635  1.00 12.50 ? 52  LYS B CB  1 
ATOM   389  C  CG  . LYS A 1 52  ? -24.156 -14.514 22.766  1.00 13.88 ? 52  LYS B CG  1 
ATOM   390  C  CD  . LYS A 1 52  ? -24.517 -14.406 24.275  1.00 13.97 ? 52  LYS B CD  1 
ATOM   391  C  CE  . LYS A 1 52  ? -26.019 -13.998 24.334  1.00 15.28 ? 52  LYS B CE  1 
ATOM   392  N  NZ  . LYS A 1 52  ? -26.346 -12.631 23.629  1.00 15.02 ? 52  LYS B NZ  1 
ATOM   393  N  N   . TYR A 1 53  ? -22.836 -13.182 19.631  1.00 13.75 ? 53  TYR B N   1 
ATOM   394  C  CA  . TYR A 1 53  ? -22.791 -11.803 19.120  1.00 13.22 ? 53  TYR B CA  1 
ATOM   395  C  C   . TYR A 1 53  ? -24.226 -11.382 18.840  1.00 11.91 ? 53  TYR B C   1 
ATOM   396  O  O   . TYR A 1 53  ? -24.920 -11.964 17.991  1.00 15.03 ? 53  TYR B O   1 
ATOM   397  C  CB  . TYR A 1 53  ? -21.970 -11.724 17.823  1.00 12.24 ? 53  TYR B CB  1 
ATOM   398  C  CG  . TYR A 1 53  ? -20.483 -11.886 17.935  1.00 10.88 ? 53  TYR B CG  1 
ATOM   399  C  CD1 . TYR A 1 53  ? -19.754 -11.562 19.113  1.00 12.29 ? 53  TYR B CD1 1 
ATOM   400  C  CD2 . TYR A 1 53  ? -19.735 -12.477 16.860  1.00 11.74 ? 53  TYR B CD2 1 
ATOM   401  C  CE1 . TYR A 1 53  ? -18.359 -11.758 19.152  1.00 10.79 ? 53  TYR B CE1 1 
ATOM   402  C  CE2 . TYR A 1 53  ? -18.386 -12.662 16.928  1.00 11.25 ? 53  TYR B CE2 1 
ATOM   403  C  CZ  . TYR A 1 53  ? -17.635 -12.296 18.069  1.00 10.35 ? 53  TYR B CZ  1 
ATOM   404  O  OH  . TYR A 1 53  ? -16.283 -12.456 18.180  1.00 11.79 ? 53  TYR B OH  1 
ATOM   405  N  N   . ASP A 1 54  ? -24.691 -10.335 19.561  1.00 13.83 ? 54  ASP B N   1 
ATOM   406  C  CA  . ASP A 1 54  ? -26.043 -9.800  19.404  1.00 14.61 ? 54  ASP B CA  1 
ATOM   407  C  C   . ASP A 1 54  ? -26.027 -8.743  18.261  1.00 16.46 ? 54  ASP B C   1 
ATOM   408  O  O   . ASP A 1 54  ? -25.369 -7.716  18.398  1.00 17.13 ? 54  ASP B O   1 
ATOM   409  C  CB  . ASP A 1 54  ? -26.441 -9.137  20.749  1.00 16.67 ? 54  ASP B CB  1 
ATOM   410  C  CG  . ASP A 1 54  ? -27.894 -8.704  20.790  1.00 22.42 ? 54  ASP B CG  1 
ATOM   411  O  OD1 . ASP A 1 54  ? -28.444 -8.331  19.733  1.00 19.96 ? 54  ASP B OD1 1 
ATOM   412  O  OD2 . ASP A 1 54  ? -28.485 -8.727  21.891  1.00 24.08 ? 54  ASP B OD2 1 
ATOM   413  N  N   . PRO A 1 55  ? -26.765 -9.015  17.162  1.00 17.64 ? 55  PRO B N   1 
ATOM   414  C  CA  . PRO A 1 55  ? -26.808 -8.018  16.042  1.00 16.80 ? 55  PRO B CA  1 
ATOM   415  C  C   . PRO A 1 55  ? -27.191 -6.577  16.504  1.00 19.34 ? 55  PRO B C   1 
ATOM   416  O  O   . PRO A 1 55  ? -26.820 -5.632  15.810  1.00 19.68 ? 55  PRO B O   1 
ATOM   417  C  CB  . PRO A 1 55  ? -27.896 -8.552  15.126  1.00 18.38 ? 55  PRO B CB  1 
ATOM   418  C  CG  . PRO A 1 55  ? -27.907 -10.073 15.473  1.00 19.09 ? 55  PRO B CG  1 
ATOM   419  C  CD  . PRO A 1 55  ? -27.776 -10.054 16.972  1.00 17.46 ? 55  PRO B CD  1 
ATOM   420  N  N   . SER A 1 56  ? -27.901 -6.445  17.622  1.00 18.36 ? 56  SER B N   1 
ATOM   421  C  CA  . SER A 1 56  ? -28.314 -5.109  18.126  1.00 19.89 ? 56  SER B CA  1 
ATOM   422  C  C   . SER A 1 56  ? -27.162 -4.445  18.866  1.00 19.84 ? 56  SER B C   1 
ATOM   423  O  O   . SER A 1 56  ? -27.213 -3.223  19.152  1.00 21.67 ? 56  SER B O   1 
ATOM   424  C  CB  . SER A 1 56  ? -29.547 -5.263  19.027  1.00 23.67 ? 56  SER B CB  1 
ATOM   425  O  OG  . SER A 1 56  ? -29.184 -5.765  20.312  1.00 28.86 ? 56  SER B OG  1 
ATOM   426  N  N   . SER A 1 57  ? -26.048 -5.165  19.132  1.00 17.15 ? 57  SER B N   1 
ATOM   427  C  CA  . SER A 1 57  ? -24.888 -4.588  19.785  1.00 17.14 ? 57  SER B CA  1 
ATOM   428  C  C   . SER A 1 57  ? -24.225 -3.543  18.932  1.00 14.89 ? 57  SER B C   1 
ATOM   429  O  O   . SER A 1 57  ? -23.601 -2.651  19.520  1.00 15.60 ? 57  SER B O   1 
ATOM   430  C  CB  . SER A 1 57  ? -23.805 -5.662  20.172  1.00 18.47 ? 57  SER B CB  1 
ATOM   431  O  OG  . SER A 1 57  ? -24.340 -6.375  21.236  1.00 18.97 ? 57  SER B OG  1 
ATOM   432  N  N   . ALA A 1 58  ? -24.188 -3.718  17.582  1.00 14.10 ? 58  ALA B N   1 
ATOM   433  C  CA  . ALA A 1 58  ? -23.548 -2.700  16.773  1.00 14.55 ? 58  ALA B CA  1 
ATOM   434  C  C   . ALA A 1 58  ? -24.331 -1.373  16.814  1.00 13.34 ? 58  ALA B C   1 
ATOM   435  O  O   . ALA A 1 58  ? -25.514 -1.413  16.761  1.00 15.58 ? 58  ALA B O   1 
ATOM   436  C  CB  . ALA A 1 58  ? -23.463 -3.206  15.324  1.00 15.69 ? 58  ALA B CB  1 
ATOM   437  N  N   . LYS A 1 59  ? -23.613 -0.279  16.992  1.00 13.46 ? 59  LYS B N   1 
ATOM   438  C  CA  . LYS A 1 59  ? -24.315 1.021   17.088  1.00 14.57 ? 59  LYS B CA  1 
ATOM   439  C  C   . LYS A 1 59  ? -23.849 2.101   16.101  1.00 13.14 ? 59  LYS B C   1 
ATOM   440  O  O   . LYS A 1 59  ? -24.729 2.857   15.683  1.00 15.99 ? 59  LYS B O   1 
ATOM   441  C  CB  . LYS A 1 59  ? -24.146 1.546   18.517  1.00 13.02 ? 59  LYS B CB  1 
ATOM   442  C  CG  . LYS A 1 59  ? -24.624 0.617   19.639  1.00 14.86 ? 59  LYS B CG  1 
ATOM   443  C  CD  . LYS A 1 59  ? -26.096 0.360   19.557  1.00 15.23 ? 59  LYS B CD  1 
ATOM   444  C  CE  . LYS A 1 59  ? -26.624 -0.533  20.719  1.00 17.44 ? 59  LYS B CE  1 
ATOM   445  N  NZ  . LYS A 1 59  ? -28.022 -0.939  20.452  1.00 18.04 ? 59  LYS B NZ  1 
ATOM   446  N  N   . ILE A 1 60  ? -22.535 2.169   15.860  1.00 14.30 ? 60  ILE B N   1 
ATOM   447  C  CA  . ILE A 1 60  ? -21.976 3.285   15.090  1.00 17.02 ? 60  ILE B CA  1 
ATOM   448  C  C   . ILE A 1 60  ? -20.911 2.755   14.201  1.00 17.22 ? 60  ILE B C   1 
ATOM   449  O  O   . ILE A 1 60  ? -20.165 1.809   14.556  1.00 15.97 ? 60  ILE B O   1 
ATOM   450  C  CB  . ILE A 1 60  ? -21.420 4.326   16.087  1.00 18.35 ? 60  ILE B CB  1 
ATOM   451  C  CG1 . ILE A 1 60  ? -22.633 4.969   16.801  1.00 22.52 ? 60  ILE B CG1 1 
ATOM   452  C  CG2 . ILE A 1 60  ? -20.568 5.407   15.412  1.00 17.44 ? 60  ILE B CG2 1 
ATOM   453  C  CD1 . ILE A 1 60  ? -22.240 5.763   17.986  1.00 27.75 ? 60  ILE B CD1 1 
ATOM   454  N  N   . ILE A 1 61  ? -20.826 3.329   13.000  1.00 15.36 ? 61  ILE B N   1 
ATOM   455  C  CA  . ILE A 1 61  ? -19.639 3.131   12.164  1.00 14.74 ? 61  ILE B CA  1 
ATOM   456  C  C   . ILE A 1 61  ? -18.919 4.443   11.925  1.00 15.00 ? 61  ILE B C   1 
ATOM   457  O  O   . ILE A 1 61  ? -19.604 5.438   11.707  1.00 17.60 ? 61  ILE B O   1 
ATOM   458  C  CB  . ILE A 1 61  ? -20.011 2.388   10.875  1.00 15.34 ? 61  ILE B CB  1 
ATOM   459  C  CG1 . ILE A 1 61  ? -18.705 1.902   10.176  1.00 14.53 ? 61  ILE B CG1 1 
ATOM   460  C  CG2 . ILE A 1 61  ? -20.969 3.238   9.963   1.00 15.89 ? 61  ILE B CG2 1 
ATOM   461  C  CD1 . ILE A 1 61  ? -19.059 0.965   9.019   1.00 16.99 ? 61  ILE B CD1 1 
ATOM   462  N  N   . SER A 1 62  ? -17.609 4.446   11.985  1.00 15.14 ? 62  SER B N   1 
ATOM   463  C  CA  . SER A 1 62  ? -16.869 5.721   11.817  1.00 16.70 ? 62  SER B CA  1 
ATOM   464  C  C   . SER A 1 62  ? -15.592 5.488   11.037  1.00 17.85 ? 62  SER B C   1 
ATOM   465  O  O   . SER A 1 62  ? -15.183 4.366   10.841  1.00 15.62 ? 62  SER B O   1 
ATOM   466  C  CB  . SER A 1 62  ? -16.534 6.331   13.146  1.00 20.02 ? 62  SER B CB  1 
ATOM   467  O  OG  . SER A 1 62  ? -15.790 5.401   13.917  1.00 20.53 ? 62  SER B OG  1 
ATOM   468  N  N   . ASN A 1 63  ? -15.077 6.573   10.461  1.00 15.73 ? 63  ASN B N   1 
ATOM   469  C  CA  . ASN A 1 63  ? -13.813 6.518   9.807   1.00 14.94 ? 63  ASN B CA  1 
ATOM   470  C  C   . ASN A 1 63  ? -12.772 7.061   10.725  1.00 16.75 ? 63  ASN B C   1 
ATOM   471  O  O   . ASN A 1 63  ? -12.802 8.305   11.074  1.00 17.35 ? 63  ASN B O   1 
ATOM   472  C  CB  . ASN A 1 63  ? -13.873 7.247   8.451   1.00 17.19 ? 63  ASN B CB  1 
ATOM   473  C  CG  . ASN A 1 63  ? -12.523 7.374   7.798   1.00 15.02 ? 63  ASN B CG  1 
ATOM   474  O  OD1 . ASN A 1 63  ? -11.538 6.820   8.205   1.00 16.07 ? 63  ASN B OD1 1 
ATOM   475  N  ND2 . ASN A 1 63  ? -12.487 8.111   6.656   1.00 15.77 ? 63  ASN B ND2 1 
ATOM   476  N  N   . SER A 1 64  ? -11.834 6.220   11.208  1.00 15.88 ? 64  SER B N   1 
ATOM   477  C  CA  . SER A 1 64  ? -10.787 6.705   12.051  1.00 15.92 ? 64  SER B CA  1 
ATOM   478  C  C   . SER A 1 64  ? -9.605  7.466   11.396  1.00 16.45 ? 64  SER B C   1 
ATOM   479  O  O   . SER A 1 64  ? -8.725  8.059   12.036  1.00 21.48 ? 64  SER B O   1 
ATOM   480  C  CB  . SER A 1 64  ? -10.240 5.539   12.841  1.00 19.53 ? 64  SER B CB  1 
ATOM   481  O  OG  . SER A 1 64  ? -9.500  4.635   11.973  1.00 19.21 ? 64  SER B OG  1 
ATOM   482  N  N   . GLY A 1 65  ? -9.608  7.347   10.058  1.00 15.27 ? 65  GLY B N   1 
ATOM   483  C  CA  . GLY A 1 65  ? -8.421  7.781   9.280   1.00 17.95 ? 65  GLY B CA  1 
ATOM   484  C  C   . GLY A 1 65  ? -7.534  6.565   9.006   1.00 17.55 ? 65  GLY B C   1 
ATOM   485  O  O   . GLY A 1 65  ? -6.748  6.628   8.089   1.00 18.42 ? 65  GLY B O   1 
ATOM   486  N  N   . HIS A 1 66  ? -7.669  5.456   9.781   1.00 14.65 ? 66  HIS B N   1 
ATOM   487  C  CA  . HIS A 1 66  ? -6.841  4.259   9.658   1.00 14.64 ? 66  HIS B CA  1 
ATOM   488  C  C   . HIS A 1 66  ? -7.583  3.009   9.215   1.00 11.84 ? 66  HIS B C   1 
ATOM   489  O  O   . HIS A 1 66  ? -6.939  2.041   8.838   1.00 13.54 ? 66  HIS B O   1 
ATOM   490  C  CB  . HIS A 1 66  ? -6.225  4.002   11.053  1.00 16.85 ? 66  HIS B CB  1 
ATOM   491  C  CG  . HIS A 1 66  ? -5.695  5.224   11.707  1.00 21.94 ? 66  HIS B CG  1 
ATOM   492  N  ND1 . HIS A 1 66  ? -4.699  5.971   11.161  1.00 23.37 ? 66  HIS B ND1 1 
ATOM   493  C  CD2 . HIS A 1 66  ? -6.033  5.812   12.927  1.00 24.66 ? 66  HIS B CD2 1 
ATOM   494  C  CE1 . HIS A 1 66  ? -4.396  7.016   12.012  1.00 22.35 ? 66  HIS B CE1 1 
ATOM   495  N  NE2 . HIS A 1 66  ? -5.192  6.883   13.111  1.00 24.55 ? 66  HIS B NE2 1 
ATOM   496  N  N   . SER A 1 67  ? -8.895  3.018   9.330   1.00 12.22 ? 67  SER B N   1 
ATOM   497  C  CA  . SER A 1 67  ? -9.785  1.967   8.867   1.00 13.27 ? 67  SER B CA  1 
ATOM   498  C  C   . SER A 1 67  ? -11.211 2.490   9.097   1.00 13.11 ? 67  SER B C   1 
ATOM   499  O  O   . SER A 1 67  ? -11.397 3.661   9.559   1.00 14.06 ? 67  SER B O   1 
ATOM   500  C  CB  . SER A 1 67  ? -9.624  0.658   9.716   1.00 12.34 ? 67  SER B CB  1 
ATOM   501  O  OG  . SER A 1 67  ? -10.460 -0.368  9.105   1.00 14.10 ? 67  SER B OG  1 
ATOM   502  N  N   . PHE A 1 68  ? -12.247 1.720   8.812   1.00 12.90 ? 68  PHE B N   1 
ATOM   503  C  CA  . PHE A 1 68  ? -13.553 2.019   9.463   1.00 13.57 ? 68  PHE B CA  1 
ATOM   504  C  C   . PHE A 1 68  ? -13.510 1.275   10.842  1.00 14.21 ? 68  PHE B C   1 
ATOM   505  O  O   . PHE A 1 68  ? -12.888 0.256   10.988  1.00 16.23 ? 68  PHE B O   1 
ATOM   506  C  CB  . PHE A 1 68  ? -14.784 1.577   8.631   1.00 13.68 ? 68  PHE B CB  1 
ATOM   507  C  CG  . PHE A 1 68  ? -14.944 0.096   8.561   1.00 15.36 ? 68  PHE B CG  1 
ATOM   508  C  CD1 . PHE A 1 68  ? -14.362 -0.630  7.480   1.00 17.11 ? 68  PHE B CD1 1 
ATOM   509  C  CD2 . PHE A 1 68  ? -15.580 -0.632  9.582   1.00 16.64 ? 68  PHE B CD2 1 
ATOM   510  C  CE1 . PHE A 1 68  ? -14.433 -2.011  7.441   1.00 15.80 ? 68  PHE B CE1 1 
ATOM   511  C  CE2 . PHE A 1 68  ? -15.696 -2.042  9.494   1.00 17.00 ? 68  PHE B CE2 1 
ATOM   512  C  CZ  . PHE A 1 68  ? -15.071 -2.734  8.434   1.00 17.09 ? 68  PHE B CZ  1 
ATOM   513  N  N   . ASN A 1 69  ? -14.336 1.776   11.770  1.00 13.79 ? 69  ASN B N   1 
ATOM   514  C  CA  . ASN A 1 69  ? -14.651 0.912   12.949  1.00 15.19 ? 69  ASN B CA  1 
ATOM   515  C  C   . ASN A 1 69  ? -16.114 0.846   13.189  1.00 14.96 ? 69  ASN B C   1 
ATOM   516  O  O   . ASN A 1 69  ? -16.785 1.917   13.187  1.00 16.35 ? 69  ASN B O   1 
ATOM   517  C  CB  . ASN A 1 69  ? -14.124 1.601   14.171  1.00 17.55 ? 69  ASN B CB  1 
ATOM   518  C  CG  . ASN A 1 69  ? -12.648 1.519   14.268  1.00 22.17 ? 69  ASN B CG  1 
ATOM   519  O  OD1 . ASN A 1 69  ? -12.070 0.469   14.612  1.00 26.56 ? 69  ASN B OD1 1 
ATOM   520  N  ND2 . ASN A 1 69  ? -12.051 2.589   14.048  1.00 23.19 ? 69  ASN B ND2 1 
ATOM   521  N  N   . VAL A 1 70  ? -16.620 -0.356  13.397  1.00 15.25 ? 70  VAL B N   1 
ATOM   522  C  CA  . VAL A 1 70  ? -17.924 -0.522  13.852  1.00 14.14 ? 70  VAL B CA  1 
ATOM   523  C  C   . VAL A 1 70  ? -17.800 -0.633  15.378  1.00 14.87 ? 70  VAL B C   1 
ATOM   524  O  O   . VAL A 1 70  ? -17.051 -1.484  15.859  1.00 17.07 ? 70  VAL B O   1 
ATOM   525  C  CB  . VAL A 1 70  ? -18.579 -1.823  13.292  1.00 15.80 ? 70  VAL B CB  1 
ATOM   526  C  CG1 . VAL A 1 70  ? -19.933 -2.109  13.908  1.00 18.16 ? 70  VAL B CG1 1 
ATOM   527  C  CG2 . VAL A 1 70  ? -18.815 -1.640  11.772  1.00 18.52 ? 70  VAL B CG2 1 
ATOM   528  N  N   . ASP A 1 71  ? -18.412 0.309   16.126  1.00 14.37 ? 71  ASP B N   1 
ATOM   529  C  CA  . ASP A 1 71  ? -18.379 0.261   17.617  1.00 15.92 ? 71  ASP B CA  1 
ATOM   530  C  C   . ASP A 1 71  ? -19.673 -0.387  18.066  1.00 13.15 ? 71  ASP B C   1 
ATOM   531  O  O   . ASP A 1 71  ? -20.778 -0.133  17.610  1.00 14.11 ? 71  ASP B O   1 
ATOM   532  C  CB  . ASP A 1 71  ? -18.340 1.714   18.136  1.00 16.57 ? 71  ASP B CB  1 
ATOM   533  C  CG  . ASP A 1 71  ? -17.081 2.406   17.788  1.00 23.62 ? 71  ASP B CG  1 
ATOM   534  O  OD1 . ASP A 1 71  ? -16.031 1.745   17.518  1.00 25.40 ? 71  ASP B OD1 1 
ATOM   535  O  OD2 . ASP A 1 71  ? -17.149 3.664   17.816  1.00 25.59 ? 71  ASP B OD2 1 
ATOM   536  N  N   . PHE A 1 72  ? -19.439 -1.259  19.081  1.00 14.18 ? 72  PHE B N   1 
ATOM   537  C  CA  . PHE A 1 72  ? -20.479 -2.060  19.758  1.00 14.02 ? 72  PHE B CA  1 
ATOM   538  C  C   . PHE A 1 72  ? -20.651 -1.480  21.161  1.00 13.28 ? 72  PHE B C   1 
ATOM   539  O  O   . PHE A 1 72  ? -19.682 -1.038  21.812  1.00 17.84 ? 72  PHE B O   1 
ATOM   540  C  CB  . PHE A 1 72  ? -20.085 -3.534  19.810  1.00 13.49 ? 72  PHE B CB  1 
ATOM   541  C  CG  . PHE A 1 72  ? -19.982 -4.176  18.426  1.00 13.78 ? 72  PHE B CG  1 
ATOM   542  C  CD1 . PHE A 1 72  ? -18.796 -3.963  17.696  1.00 16.92 ? 72  PHE B CD1 1 
ATOM   543  C  CD2 . PHE A 1 72  ? -21.029 -4.865  17.896  1.00 14.87 ? 72  PHE B CD2 1 
ATOM   544  C  CE1 . PHE A 1 72  ? -18.710 -4.480  16.375  1.00 15.20 ? 72  PHE B CE1 1 
ATOM   545  C  CE2 . PHE A 1 72  ? -20.902 -5.505  16.618  1.00 15.79 ? 72  PHE B CE2 1 
ATOM   546  C  CZ  . PHE A 1 72  ? -19.709 -5.251  15.907  1.00 15.22 ? 72  PHE B CZ  1 
ATOM   547  N  N   . ASP A 1 73  ? -21.888 -1.544  21.581  1.00 15.27 ? 73  ASP B N   1 
ATOM   548  C  CA  . ASP A 1 73  ? -22.212 -1.067  22.996  1.00 14.66 ? 73  ASP B CA  1 
ATOM   549  C  C   . ASP A 1 73  ? -21.657 -2.197  23.873  1.00 16.17 ? 73  ASP B C   1 
ATOM   550  O  O   . ASP A 1 73  ? -22.161 -3.356  23.836  1.00 18.58 ? 73  ASP B O   1 
ATOM   551  C  CB  . ASP A 1 73  ? -23.720 -1.018  23.120  1.00 15.57 ? 73  ASP B CB  1 
ATOM   552  C  CG  . ASP A 1 73  ? -24.170 -0.662  24.509  1.00 16.49 ? 73  ASP B CG  1 
ATOM   553  O  OD1 . ASP A 1 73  ? -23.302 -0.421  25.365  1.00 20.49 ? 73  ASP B OD1 1 
ATOM   554  O  OD2 . ASP A 1 73  ? -25.398 -0.621  24.743  1.00 20.32 ? 73  ASP B OD2 1 
ATOM   555  N  N   . ASP A 1 74  ? -20.599 -1.868  24.571  1.00 15.30 ? 74  ASP B N   1 
ATOM   556  C  CA  . ASP A 1 74  ? -19.917 -2.860  25.439  1.00 16.76 ? 74  ASP B CA  1 
ATOM   557  C  C   . ASP A 1 74  ? -20.260 -2.529  26.940  1.00 17.29 ? 74  ASP B C   1 
ATOM   558  O  O   . ASP A 1 74  ? -19.435 -2.716  27.787  1.00 17.45 ? 74  ASP B O   1 
ATOM   559  C  CB  . ASP A 1 74  ? -18.406 -2.895  25.195  1.00 15.61 ? 74  ASP B CB  1 
ATOM   560  C  CG  . ASP A 1 74  ? -17.689 -1.641  25.607  1.00 20.73 ? 74  ASP B CG  1 
ATOM   561  O  OD1 . ASP A 1 74  ? -18.375 -0.599  25.828  1.00 20.65 ? 74  ASP B OD1 1 
ATOM   562  O  OD2 . ASP A 1 74  ? -16.482 -1.697  25.699  1.00 20.28 ? 74  ASP B OD2 1 
ATOM   563  N  N   . THR A 1 75  ? -21.437 -2.003  27.133  1.00 19.90 ? 75  THR B N   1 
ATOM   564  C  CA  . THR A 1 75  ? -21.927 -1.701  28.528  1.00 19.80 ? 75  THR B CA  1 
ATOM   565  C  C   . THR A 1 75  ? -22.113 -2.960  29.334  1.00 20.51 ? 75  THR B C   1 
ATOM   566  O  O   . THR A 1 75  ? -21.943 -2.868  30.537  1.00 18.62 ? 75  THR B O   1 
ATOM   567  C  CB  . THR A 1 75  ? -23.280 -0.958  28.481  1.00 18.79 ? 75  THR B CB  1 
ATOM   568  O  OG1 . THR A 1 75  ? -23.141 0.248   27.745  1.00 21.28 ? 75  THR B OG1 1 
ATOM   569  C  CG2 . THR A 1 75  ? -23.877 -0.632  29.886  1.00 19.77 ? 75  THR B CG2 1 
ATOM   570  N  N   . GLU A 1 76  ? -22.636 -4.051  28.765  1.00 20.87 ? 76  GLU B N   1 
ATOM   571  C  CA  . GLU A 1 76  ? -22.707 -5.312  29.495  1.00 21.67 ? 76  GLU B CA  1 
ATOM   572  C  C   . GLU A 1 76  ? -22.337 -6.472  28.585  1.00 21.15 ? 76  GLU B C   1 
ATOM   573  O  O   . GLU A 1 76  ? -21.605 -6.233  27.603  1.00 19.48 ? 76  GLU B O   1 
ATOM   574  C  CB  . GLU A 1 76  ? -24.044 -5.504  30.232  1.00 27.92 ? 76  GLU B CB  1 
ATOM   575  C  CG  . GLU A 1 76  ? -25.291 -5.566  29.363  1.00 28.32 ? 76  GLU B CG  1 
ATOM   576  C  CD  . GLU A 1 76  ? -26.493 -6.109  30.142  1.00 32.27 ? 76  GLU B CD  1 
ATOM   577  O  OE1 . GLU A 1 76  ? -26.371 -6.243  31.363  1.00 32.67 ? 76  GLU B OE1 1 
ATOM   578  O  OE2 . GLU A 1 76  ? -27.570 -6.402  29.577  1.00 41.93 ? 76  GLU B OE2 1 
ATOM   579  N  N   . ASN A 1 77  ? -22.577 -7.697  29.058  1.00 19.48 ? 77  ASN B N   1 
ATOM   580  C  CA  . ASN A 1 77  ? -22.124 -8.886  28.433  1.00 16.82 ? 77  ASN B CA  1 
ATOM   581  C  C   . ASN A 1 77  ? -23.112 -9.451  27.486  1.00 17.60 ? 77  ASN B C   1 
ATOM   582  O  O   . ASN A 1 77  ? -23.299 -10.655 27.446  1.00 19.18 ? 77  ASN B O   1 
ATOM   583  C  CB  . ASN A 1 77  ? -21.800 -9.960  29.517  1.00 20.08 ? 77  ASN B CB  1 
ATOM   584  C  CG  . ASN A 1 77  ? -20.406 -9.833  30.016  1.00 17.78 ? 77  ASN B CG  1 
ATOM   585  O  OD1 . ASN A 1 77  ? -19.543 -9.183  29.396  1.00 15.12 ? 77  ASN B OD1 1 
ATOM   586  N  ND2 . ASN A 1 77  ? -20.115 -10.515 31.182  1.00 18.96 ? 77  ASN B ND2 1 
ATOM   587  N  N   . LYS A 1 78  ? -23.677 -8.648  26.582  1.00 13.72 ? 78  LYS B N   1 
ATOM   588  C  CA  . LYS A 1 78  ? -24.587 -9.204  25.565  1.00 16.15 ? 78  LYS B CA  1 
ATOM   589  C  C   . LYS A 1 78  ? -23.786 -9.926  24.452  1.00 14.19 ? 78  LYS B C   1 
ATOM   590  O  O   . LYS A 1 78  ? -24.237 -10.950 23.921  1.00 14.93 ? 78  LYS B O   1 
ATOM   591  C  CB  . LYS A 1 78  ? -25.411 -8.101  24.919  1.00 15.97 ? 78  LYS B CB  1 
ATOM   592  C  CG  . LYS A 1 78  ? -26.494 -7.613  25.883  1.00 21.31 ? 78  LYS B CG  1 
ATOM   593  C  CD  . LYS A 1 78  ? -27.205 -6.410  25.223  1.00 22.92 ? 78  LYS B CD  1 
ATOM   594  C  CE  . LYS A 1 78  ? -28.350 -5.843  26.125  1.00 29.08 ? 78  LYS B CE  1 
ATOM   595  N  NZ  . LYS A 1 78  ? -28.711 -4.432  25.718  1.00 31.34 ? 78  LYS B NZ  1 
ATOM   596  N  N   . SER A 1 79  ? -22.596 -9.440  24.152  1.00 13.46 ? 79  SER B N   1 
ATOM   597  C  CA  . SER A 1 79  ? -21.800 -10.047 23.010  1.00 11.48 ? 79  SER B CA  1 
ATOM   598  C  C   . SER A 1 79  ? -20.420 -10.332 23.562  1.00 11.44 ? 79  SER B C   1 
ATOM   599  O  O   . SER A 1 79  ? -19.672 -9.441  24.009  1.00 10.85 ? 79  SER B O   1 
ATOM   600  C  CB  . SER A 1 79  ? -21.686 -9.013  21.917  1.00 11.65 ? 79  SER B CB  1 
ATOM   601  O  OG  . SER A 1 79  ? -22.921 -8.823  21.319  1.00 12.77 ? 79  SER B OG  1 
ATOM   602  N  N   . VAL A 1 80  ? -20.108 -11.656 23.629  1.00 11.52 ? 80  VAL B N   1 
ATOM   603  C  CA  . VAL A 1 80  ? -18.880 -12.076 24.290  1.00 11.22 ? 80  VAL B CA  1 
ATOM   604  C  C   . VAL A 1 80  ? -18.283 -13.267 23.531  1.00 12.16 ? 80  VAL B C   1 
ATOM   605  O  O   . VAL A 1 80  ? -18.979 -14.063 22.897  1.00 13.86 ? 80  VAL B O   1 
ATOM   606  C  CB  . VAL A 1 80  ? -19.059 -12.499 25.790  1.00 12.35 ? 80  VAL B CB  1 
ATOM   607  C  CG1 . VAL A 1 80  ? -19.628 -11.368 26.640  1.00 14.01 ? 80  VAL B CG1 1 
ATOM   608  C  CG2 . VAL A 1 80  ? -20.051 -13.645 25.898  1.00 15.88 ? 80  VAL B CG2 1 
ATOM   609  N  N   . LEU A 1 81  ? -16.976 -13.313 23.675  1.00 10.64 ? 81  LEU B N   1 
ATOM   610  C  CA  . LEU A 1 81  ? -16.202 -14.444 23.199  1.00 11.40 ? 81  LEU B CA  1 
ATOM   611  C  C   . LEU A 1 81  ? -15.625 -15.175 24.374  1.00 11.69 ? 81  LEU B C   1 
ATOM   612  O  O   . LEU A 1 81  ? -14.984 -14.557 25.229  1.00 11.65 ? 81  LEU B O   1 
ATOM   613  C  CB  . LEU A 1 81  ? -15.014 -13.927 22.258  1.00 13.14 ? 81  LEU B CB  1 
ATOM   614  C  CG  . LEU A 1 81  ? -14.096 -14.997 21.656  1.00 13.68 ? 81  LEU B CG  1 
ATOM   615  C  CD1 . LEU A 1 81  ? -14.843 -15.926 20.650  1.00 13.37 ? 81  LEU B CD1 1 
ATOM   616  C  CD2 . LEU A 1 81  ? -13.020 -14.198 20.900  1.00 15.14 ? 81  LEU B CD2 1 
ATOM   617  N  N   . ARG A 1 82  ? -15.745 -16.518 24.347  1.00 11.93 ? 82  ARG B N   1 
ATOM   618  C  CA  . ARG A 1 82  ? -15.184 -17.388 25.390  1.00 13.68 ? 82  ARG B CA  1 
ATOM   619  C  C   . ARG A 1 82  ? -14.592 -18.612 24.683  1.00 13.34 ? 82  ARG B C   1 
ATOM   620  O  O   . ARG A 1 82  ? -14.723 -18.779 23.448  1.00 12.87 ? 82  ARG B O   1 
ATOM   621  C  CB  . ARG A 1 82  ? -16.311 -17.825 26.349  1.00 12.72 ? 82  ARG B CB  1 
ATOM   622  C  CG  . ARG A 1 82  ? -16.774 -16.678 27.236  1.00 14.68 ? 82  ARG B CG  1 
ATOM   623  C  CD  . ARG A 1 82  ? -18.015 -17.045 28.056  1.00 16.39 ? 82  ARG B CD  1 
ATOM   624  N  NE  . ARG A 1 82  ? -19.173 -17.145 27.160  1.00 17.91 ? 82  ARG B NE  1 
ATOM   625  C  CZ  . ARG A 1 82  ? -20.455 -17.329 27.498  1.00 23.78 ? 82  ARG B CZ  1 
ATOM   626  N  NH1 . ARG A 1 82  ? -20.786 -17.411 28.801  1.00 27.00 ? 82  ARG B NH1 1 
ATOM   627  N  NH2 . ARG A 1 82  ? -21.388 -17.453 26.548  1.00 22.77 ? 82  ARG B NH2 1 
ATOM   628  N  N   . GLY A 1 83  ? -14.002 -19.503 25.470  1.00 13.65 ? 83  GLY B N   1 
ATOM   629  C  CA  . GLY A 1 83  ? -13.415 -20.748 24.952  1.00 12.80 ? 83  GLY B CA  1 
ATOM   630  C  C   . GLY A 1 83  ? -12.169 -20.446 24.161  1.00 13.39 ? 83  GLY B C   1 
ATOM   631  O  O   . GLY A 1 83  ? -11.484 -19.468 24.481  1.00 13.30 ? 83  GLY B O   1 
ATOM   632  N  N   . GLY A 1 84  ? -11.931 -21.233 23.091  1.00 13.64 ? 84  GLY B N   1 
ATOM   633  C  CA  . GLY A 1 84  ? -10.643 -21.031 22.380  1.00 14.61 ? 84  GLY B CA  1 
ATOM   634  C  C   . GLY A 1 84  ? -9.476  -21.164 23.356  1.00 15.01 ? 84  GLY B C   1 
ATOM   635  O  O   . GLY A 1 84  ? -9.521  -22.054 24.209  1.00 15.18 ? 84  GLY B O   1 
ATOM   636  N  N   . PRO A 1 85  ? -8.469  -20.294 23.299  1.00 15.14 ? 85  PRO B N   1 
ATOM   637  C  CA  . PRO A 1 85  ? -7.369  -20.235 24.287  1.00 13.76 ? 85  PRO B CA  1 
ATOM   638  C  C   . PRO A 1 85  ? -7.683  -19.453 25.582  1.00 13.41 ? 85  PRO B C   1 
ATOM   639  O  O   . PRO A 1 85  ? -6.785  -19.296 26.420  1.00 15.22 ? 85  PRO B O   1 
ATOM   640  C  CB  . PRO A 1 85  ? -6.230  -19.494 23.496  1.00 15.19 ? 85  PRO B CB  1 
ATOM   641  C  CG  . PRO A 1 85  ? -7.076  -18.474 22.678  1.00 13.38 ? 85  PRO B CG  1 
ATOM   642  C  CD  . PRO A 1 85  ? -8.243  -19.328 22.169  1.00 13.56 ? 85  PRO B CD  1 
ATOM   643  N  N   . LEU A 1 86  ? -8.861  -18.823 25.687  1.00 12.65 ? 86  LEU B N   1 
ATOM   644  C  CA  . LEU A 1 86  ? -9.088  -17.787 26.669  1.00 13.18 ? 86  LEU B CA  1 
ATOM   645  C  C   . LEU A 1 86  ? -9.547  -18.339 28.004  1.00 15.48 ? 86  LEU B C   1 
ATOM   646  O  O   . LEU A 1 86  ? -10.349 -19.284 28.037  1.00 16.05 ? 86  LEU B O   1 
ATOM   647  C  CB  . LEU A 1 86  ? -10.242 -16.916 26.116  1.00 13.05 ? 86  LEU B CB  1 
ATOM   648  C  CG  . LEU A 1 86  ? -9.966  -16.269 24.709  1.00 12.91 ? 86  LEU B CG  1 
ATOM   649  C  CD1 . LEU A 1 86  ? -11.228 -15.614 24.218  1.00 13.84 ? 86  LEU B CD1 1 
ATOM   650  C  CD2 . LEU A 1 86  ? -8.752  -15.310 24.798  1.00 15.60 ? 86  LEU B CD2 1 
ATOM   651  N  N   . THR A 1 87  ? -9.101  -17.638 29.037  1.00 14.87 ? 87  THR B N   1 
ATOM   652  C  CA  . THR A 1 87  ? -9.653  -17.831 30.403  1.00 18.11 ? 87  THR B CA  1 
ATOM   653  C  C   . THR A 1 87  ? -10.636 -16.739 30.624  1.00 16.74 ? 87  THR B C   1 
ATOM   654  O  O   . THR A 1 87  ? -10.257 -15.554 30.519  1.00 17.24 ? 87  THR B O   1 
ATOM   655  C  CB  . THR A 1 87  ? -8.493  -17.761 31.349  1.00 19.77 ? 87  THR B CB  1 
ATOM   656  O  OG1 . THR A 1 87  ? -7.723  -18.920 31.066  1.00 23.61 ? 87  THR B OG1 1 
ATOM   657  C  CG2 . THR A 1 87  ? -8.965  -17.872 32.841  1.00 24.26 ? 87  THR B CG2 1 
ATOM   658  N  N   . GLY A 1 88  ? -11.902 -17.097 30.886  1.00 15.11 ? 88  GLY B N   1 
ATOM   659  C  CA  . GLY A 1 88  ? -12.824 -16.014 31.220  1.00 18.14 ? 88  GLY B CA  1 
ATOM   660  C  C   . GLY A 1 88  ? -13.499 -15.443 29.945  1.00 15.90 ? 88  GLY B C   1 
ATOM   661  O  O   . GLY A 1 88  ? -13.329 -15.994 28.843  1.00 16.82 ? 88  GLY B O   1 
ATOM   662  N  N   . SER A 1 89  ? -14.232 -14.374 30.134  1.00 14.47 ? 89  SER B N   1 
ATOM   663  C  CA  . SER A 1 89  ? -15.146 -13.826 29.073  1.00 14.77 ? 89  SER B CA  1 
ATOM   664  C  C   . SER A 1 89  ? -14.661 -12.537 28.588  1.00 13.48 ? 89  SER B C   1 
ATOM   665  O  O   . SER A 1 89  ? -14.316 -11.639 29.346  1.00 14.39 ? 89  SER B O   1 
ATOM   666  C  CB  . SER A 1 89  ? -16.553 -13.661 29.720  1.00 15.86 ? 89  SER B CB  1 
ATOM   667  O  OG  . SER A 1 89  ? -17.530 -13.233 28.822  1.00 16.95 ? 89  SER B OG  1 
ATOM   668  N  N   . TYR A 1 90  ? -14.588 -12.441 27.262  1.00 13.27 ? 90  TYR B N   1 
ATOM   669  C  CA  . TYR A 1 90  ? -14.067 -11.236 26.543  1.00 11.85 ? 90  TYR B CA  1 
ATOM   670  C  C   . TYR A 1 90  ? -15.184 -10.565 25.805  1.00 12.43 ? 90  TYR B C   1 
ATOM   671  O  O   . TYR A 1 90  ? -15.830 -11.134 24.912  1.00 13.36 ? 90  TYR B O   1 
ATOM   672  C  CB  . TYR A 1 90  ? -12.936 -11.672 25.630  1.00 11.65 ? 90  TYR B CB  1 
ATOM   673  C  CG  . TYR A 1 90  ? -11.640 -12.006 26.360  1.00 10.38 ? 90  TYR B CG  1 
ATOM   674  C  CD1 . TYR A 1 90  ? -11.541 -13.132 27.173  1.00 10.77 ? 90  TYR B CD1 1 
ATOM   675  C  CD2 . TYR A 1 90  ? -10.518 -11.192 26.236  1.00 11.57 ? 90  TYR B CD2 1 
ATOM   676  C  CE1 . TYR A 1 90  ? -10.366 -13.435 27.836  1.00 11.74 ? 90  TYR B CE1 1 
ATOM   677  C  CE2 . TYR A 1 90  ? -9.337  -11.489 26.897  1.00 12.49 ? 90  TYR B CE2 1 
ATOM   678  C  CZ  . TYR A 1 90  ? -9.267  -12.612 27.696  1.00 11.89 ? 90  TYR B CZ  1 
ATOM   679  O  OH  . TYR A 1 90  ? -8.100  -12.919 28.361  1.00 13.28 ? 90  TYR B OH  1 
ATOM   680  N  N   . ARG A 1 91  ? -15.493 -9.313  26.145  1.00 11.40 ? 91  ARG B N   1 
ATOM   681  C  CA  . ARG A 1 91  ? -16.586 -8.561  25.621  1.00 11.24 ? 91  ARG B CA  1 
ATOM   682  C  C   . ARG A 1 91  ? -16.293 -7.856  24.298  1.00 10.58 ? 91  ARG B C   1 
ATOM   683  O  O   . ARG A 1 91  ? -15.223 -7.191  24.177  1.00 11.36 ? 91  ARG B O   1 
ATOM   684  C  CB  . ARG A 1 91  ? -16.944 -7.457  26.692  1.00 11.69 ? 91  ARG B CB  1 
ATOM   685  C  CG  . ARG A 1 91  ? -18.291 -6.886  26.480  1.00 14.28 ? 91  ARG B CG  1 
ATOM   686  C  CD  . ARG A 1 91  ? -18.532 -5.821  27.536  1.00 14.31 ? 91  ARG B CD  1 
ATOM   687  N  NE  . ARG A 1 91  ? -18.659 -6.475  28.833  1.00 15.23 ? 91  ARG B NE  1 
ATOM   688  C  CZ  . ARG A 1 91  ? -18.818 -5.833  29.979  1.00 16.28 ? 91  ARG B CZ  1 
ATOM   689  N  NH1 . ARG A 1 91  ? -18.868 -4.506  29.990  1.00 16.80 ? 91  ARG B NH1 1 
ATOM   690  N  NH2 . ARG A 1 91  ? -18.926 -6.514  31.108  1.00 14.38 ? 91  ARG B NH2 1 
ATOM   691  N  N   . LEU A 1 92  ? -17.219 -8.093  23.359  1.00 10.96 ? 92  LEU B N   1 
ATOM   692  C  CA  . LEU A 1 92  ? -17.072 -7.379  22.071  1.00 12.52 ? 92  LEU B CA  1 
ATOM   693  C  C   . LEU A 1 92  ? -17.059 -5.849  22.185  1.00 12.57 ? 92  LEU B C   1 
ATOM   694  O  O   . LEU A 1 92  ? -17.965 -5.247  22.721  1.00 13.78 ? 92  LEU B O   1 
ATOM   695  C  CB  . LEU A 1 92  ? -18.197 -7.841  21.216  1.00 12.16 ? 92  LEU B CB  1 
ATOM   696  C  CG  . LEU A 1 92  ? -18.218 -7.242  19.774  1.00 10.03 ? 92  LEU B CG  1 
ATOM   697  C  CD1 . LEU A 1 92  ? -16.932 -7.563  18.984  1.00 15.70 ? 92  LEU B CD1 1 
ATOM   698  C  CD2 . LEU A 1 92  ? -19.520 -7.723  19.101  1.00 11.54 ? 92  LEU B CD2 1 
ATOM   699  N  N   . ARG A 1 93  ? -16.047 -5.268  21.561  1.00 11.20 ? 93  ARG B N   1 
ATOM   700  C  CA  . ARG A 1 93  ? -15.877 -3.775  21.540  1.00 12.69 ? 93  ARG B CA  1 
ATOM   701  C  C   . ARG A 1 93  ? -15.988 -3.170  20.104  1.00 12.40 ? 93  ARG B C   1 
ATOM   702  O  O   . ARG A 1 93  ? -16.724 -2.195  19.968  1.00 14.23 ? 93  ARG B O   1 
ATOM   703  C  CB  . ARG A 1 93  ? -14.515 -3.450  22.135  1.00 15.85 ? 93  ARG B CB  1 
ATOM   704  C  CG  . ARG A 1 93  ? -14.025 -2.011  21.959  1.00 19.96 ? 93  ARG B CG  1 
ATOM   705  C  CD  . ARG A 1 93  ? -14.331 -1.227  23.170  1.00 22.42 ? 93  ARG B CD  1 
ATOM   706  N  NE  . ARG A 1 93  ? -13.781 0.121   23.105  1.00 20.84 ? 93  ARG B NE  1 
ATOM   707  C  CZ  . ARG A 1 93  ? -14.121 1.091   23.944  1.00 19.45 ? 93  ARG B CZ  1 
ATOM   708  N  NH1 . ARG A 1 93  ? -15.004 0.846   24.901  1.00 21.48 ? 93  ARG B NH1 1 
ATOM   709  N  NH2 . ARG A 1 93  ? -13.584 2.298   23.831  1.00 21.80 ? 93  ARG B NH2 1 
ATOM   710  N  N   . GLN A 1 94  ? -15.210 -3.710  19.139  1.00 12.89 ? 94  GLN B N   1 
ATOM   711  C  CA  . GLN A 1 94  ? -15.208 -3.047  17.834  1.00 14.68 ? 94  GLN B CA  1 
ATOM   712  C  C   . GLN A 1 94  ? -14.762 -4.012  16.794  1.00 13.94 ? 94  GLN B C   1 
ATOM   713  O  O   . GLN A 1 94  ? -14.127 -5.019  17.087  1.00 11.44 ? 94  GLN B O   1 
ATOM   714  C  CB  . GLN A 1 94  ? -14.178 -1.930  18.205  1.00 17.14 ? 94  GLN B CB  1 
ATOM   715  C  CG  . GLN A 1 94  ? -13.408 -1.110  17.194  1.00 24.90 ? 94  GLN B CG  1 
ATOM   716  C  CD  . GLN A 1 94  ? -12.112 -1.769  16.756  1.00 22.94 ? 94  GLN B CD  1 
ATOM   717  O  OE1 . GLN A 1 94  ? -12.136 -2.591  15.858  1.00 20.27 ? 94  GLN B OE1 1 
ATOM   718  N  NE2 . GLN A 1 94  ? -10.996 -1.400  17.380  1.00 21.52 ? 94  GLN B NE2 1 
ATOM   719  N  N   . VAL A 1 95  ? -15.118 -3.686  15.517  1.00 12.60 ? 95  VAL B N   1 
ATOM   720  C  CA  . VAL A 1 95  ? -14.672 -4.493  14.346  1.00 12.38 ? 95  VAL B CA  1 
ATOM   721  C  C   . VAL A 1 95  ? -14.074 -3.495  13.357  1.00 12.40 ? 95  VAL B C   1 
ATOM   722  O  O   . VAL A 1 95  ? -14.613 -2.408  13.160  1.00 13.58 ? 95  VAL B O   1 
ATOM   723  C  CB  . VAL A 1 95  ? -15.904 -5.136  13.698  1.00 11.20 ? 95  VAL B CB  1 
ATOM   724  C  CG1 . VAL A 1 95  ? -15.670 -5.627  12.269  1.00 13.19 ? 95  VAL B CG1 1 
ATOM   725  C  CG2 . VAL A 1 95  ? -16.325 -6.378  14.545  1.00 13.67 ? 95  VAL B CG2 1 
ATOM   726  N  N   . HIS A 1 96  ? -12.958 -3.901  12.753  1.00 11.85 ? 96  HIS B N   1 
ATOM   727  C  CA  . HIS A 1 96  ? -12.440 -3.060  11.651  1.00 11.36 ? 96  HIS B CA  1 
ATOM   728  C  C   . HIS A 1 96  ? -11.812 -3.978  10.652  1.00 11.21 ? 96  HIS B C   1 
ATOM   729  O  O   . HIS A 1 96  ? -11.874 -5.204  10.772  1.00 10.24 ? 96  HIS B O   1 
ATOM   730  C  CB  . HIS A 1 96  ? -11.483 -2.011  12.171  1.00 10.79 ? 96  HIS B CB  1 
ATOM   731  C  CG  . HIS A 1 96  ? -10.325 -2.636  12.860  1.00 10.48 ? 96  HIS B CG  1 
ATOM   732  N  ND1 . HIS A 1 96  ? -10.348 -2.950  14.222  1.00 11.17 ? 96  HIS B ND1 1 
ATOM   733  C  CD2 . HIS A 1 96  ? -9.117  -3.114  12.411  1.00 11.26 ? 96  HIS B CD2 1 
ATOM   734  C  CE1 . HIS A 1 96  ? -9.183  -3.494  14.539  1.00 12.53 ? 96  HIS B CE1 1 
ATOM   735  N  NE2 . HIS A 1 96  ? -8.440  -3.664  13.436  1.00 15.18 ? 96  HIS B NE2 1 
ATOM   736  N  N   . LEU A 1 97  ? -11.241 -3.404  9.550   1.00 10.74 ? 97  LEU B N   1 
ATOM   737  C  CA  . LEU A 1 97  ? -10.745 -4.209  8.405   1.00 11.44 ? 97  LEU B CA  1 
ATOM   738  C  C   . LEU A 1 97  ? -9.381  -3.644  7.959   1.00 10.76 ? 97  LEU B C   1 
ATOM   739  O  O   . LEU A 1 97  ? -9.134  -2.436  8.013   1.00 10.76 ? 97  LEU B O   1 
ATOM   740  C  CB  . LEU A 1 97  ? -11.745 -4.056  7.245   1.00 12.62 ? 97  LEU B CB  1 
ATOM   741  C  CG  . LEU A 1 97  ? -11.421 -4.927  6.066   1.00 11.92 ? 97  LEU B CG  1 
ATOM   742  C  CD1 . LEU A 1 97  ? -11.718 -6.403  6.362   1.00 13.05 ? 97  LEU B CD1 1 
ATOM   743  C  CD2 . LEU A 1 97  ? -12.321 -4.579  4.935   1.00 13.61 ? 97  LEU B CD2 1 
ATOM   744  N  N   . HIS A 1 98  ? -8.537  -4.528  7.468   1.00 10.59 ? 98  HIS B N   1 
ATOM   745  C  CA  . HIS A 1 98  ? -7.308  -4.163  6.808   1.00 10.01 ? 98  HIS B CA  1 
ATOM   746  C  C   . HIS A 1 98  ? -7.272  -4.728  5.425   1.00 10.31 ? 98  HIS B C   1 
ATOM   747  O  O   . HIS A 1 98  ? -7.724  -5.802  5.175   1.00 11.50 ? 98  HIS B O   1 
ATOM   748  C  CB  . HIS A 1 98  ? -6.089  -4.729  7.591   1.00 11.90 ? 98  HIS B CB  1 
ATOM   749  C  CG  . HIS A 1 98  ? -6.015  -4.297  9.054   1.00 11.82 ? 98  HIS B CG  1 
ATOM   750  N  ND1 . HIS A 1 98  ? -5.364  -3.204  9.456   1.00 12.94 ? 98  HIS B ND1 1 
ATOM   751  C  CD2 . HIS A 1 98  ? -6.514  -4.922  10.166  1.00 14.70 ? 98  HIS B CD2 1 
ATOM   752  C  CE1 . HIS A 1 98  ? -5.467  -3.081  10.830  1.00 12.62 ? 98  HIS B CE1 1 
ATOM   753  N  NE2 . HIS A 1 98  ? -6.201  -4.107  11.265  1.00 9.09  ? 98  HIS B NE2 1 
ATOM   754  N  N   . TRP A 1 99  ? -6.672  -3.925  4.563   1.00 9.78  ? 99  TRP B N   1 
ATOM   755  C  CA  . TRP A 1 99  ? -6.693  -4.296  3.105   1.00 10.53 ? 99  TRP B CA  1 
ATOM   756  C  C   . TRP A 1 99  ? -5.413  -3.666  2.569   1.00 10.64 ? 99  TRP B C   1 
ATOM   757  O  O   . TRP A 1 99  ? -4.546  -3.090  3.219   1.00 10.89 ? 99  TRP B O   1 
ATOM   758  C  CB  . TRP A 1 99  ? -7.909  -3.727  2.392   1.00 9.94  ? 99  TRP B CB  1 
ATOM   759  C  CG  . TRP A 1 99  ? -8.063  -2.271  2.509   1.00 11.58 ? 99  TRP B CG  1 
ATOM   760  C  CD1 . TRP A 1 99  ? -7.458  -1.288  1.712   1.00 11.56 ? 99  TRP B CD1 1 
ATOM   761  C  CD2 . TRP A 1 99  ? -8.879  -1.541  3.454   1.00 11.96 ? 99  TRP B CD2 1 
ATOM   762  N  NE1 . TRP A 1 99  ? -7.818  -0.017  2.106   1.00 11.51 ? 99  TRP B NE1 1 
ATOM   763  C  CE2 . TRP A 1 99  ? -8.662  -0.118  3.201   1.00 12.07 ? 99  TRP B CE2 1 
ATOM   764  C  CE3 . TRP A 1 99  ? -9.725  -1.927  4.531   1.00 12.85 ? 99  TRP B CE3 1 
ATOM   765  C  CZ2 . TRP A 1 99  ? -9.320  0.866   3.912   1.00 10.27 ? 99  TRP B CZ2 1 
ATOM   766  C  CZ3 . TRP A 1 99  ? -10.330 -0.926  5.293   1.00 10.58 ? 99  TRP B CZ3 1 
ATOM   767  C  CH2 . TRP A 1 99  ? -10.168 0.449   4.981   1.00 11.30 ? 99  TRP B CH2 1 
ATOM   768  N  N   . GLY A 1 100 ? -5.252  -3.951  1.244   1.00 10.72 ? 100 GLY B N   1 
ATOM   769  C  CA  . GLY A 1 100 ? -4.059  -3.433  0.486   1.00 12.87 ? 100 GLY B CA  1 
ATOM   770  C  C   . GLY A 1 100 ? -4.549  -2.710  -0.747  1.00 10.96 ? 100 GLY B C   1 
ATOM   771  O  O   . GLY A 1 100 ? -5.727  -2.627  -1.001  1.00 10.54 ? 100 GLY B O   1 
ATOM   772  N  N   . SER A 1 101 ? -3.557  -2.221  -1.518  1.00 13.42 ? 101 SER B N   1 
ATOM   773  C  CA  . SER A 1 101 ? -3.988  -1.531  -2.779  1.00 13.17 ? 101 SER B CA  1 
ATOM   774  C  C   . SER A 1 101 ? -4.327  -2.492  -3.867  1.00 14.31 ? 101 SER B C   1 
ATOM   775  O  O   . SER A 1 101 ? -5.043  -2.024  -4.816  1.00 13.68 ? 101 SER B O   1 
ATOM   776  C  CB  . SER A 1 101 ? -2.926  -0.537  -3.293  1.00 13.70 ? 101 SER B CB  1 
ATOM   777  O  OG  . SER A 1 101 ? -1.805  -1.245  -3.749  1.00 15.64 ? 101 SER B OG  1 
ATOM   778  N  N   . ALA A 1 102 ? -4.033  -3.751  -3.721  1.00 13.60 ? 102 ALA B N   1 
ATOM   779  C  CA  . ALA A 1 102 ? -4.417  -4.725  -4.715  1.00 14.37 ? 102 ALA B CA  1 
ATOM   780  C  C   . ALA A 1 102 ? -4.935  -5.947  -3.971  1.00 12.54 ? 102 ALA B C   1 
ATOM   781  O  O   . ALA A 1 102 ? -4.568  -6.229  -2.781  1.00 13.12 ? 102 ALA B O   1 
ATOM   782  C  CB  . ALA A 1 102 ? -3.219  -5.117  -5.512  1.00 17.94 ? 102 ALA B CB  1 
ATOM   783  N  N   . ASP A 1 103 ? -5.768  -6.677  -4.666  1.00 12.38 ? 103 ASP B N   1 
ATOM   784  C  CA  . ASP A 1 103 ? -6.448  -7.816  -4.033  1.00 14.02 ? 103 ASP B CA  1 
ATOM   785  C  C   . ASP A 1 103 ? -5.401  -8.902  -3.741  1.00 17.97 ? 103 ASP B C   1 
ATOM   786  O  O   . ASP A 1 103 ? -5.662  -9.801  -2.910  1.00 21.64 ? 103 ASP B O   1 
ATOM   787  C  CB  . ASP A 1 103 ? -7.493  -8.404  -4.994  1.00 14.75 ? 103 ASP B CB  1 
ATOM   788  C  CG  . ASP A 1 103 ? -8.654  -7.533  -5.240  1.00 15.79 ? 103 ASP B CG  1 
ATOM   789  O  OD1 . ASP A 1 103 ? -8.916  -6.570  -4.524  1.00 15.02 ? 103 ASP B OD1 1 
ATOM   790  O  OD2 . ASP A 1 103 ? -9.399  -7.903  -6.228  1.00 18.36 ? 103 ASP B OD2 1 
ATOM   791  N  N   . ASP A 1 104 ? -4.236  -8.814  -4.435  1.00 18.98 ? 104 ASP B N   1 
ATOM   792  C  CA  . ASP A 1 104 ? -3.160  -9.761  -4.298  1.00 23.68 ? 104 ASP B CA  1 
ATOM   793  C  C   . ASP A 1 104 ? -2.567  -9.836  -2.882  1.00 20.91 ? 104 ASP B C   1 
ATOM   794  O  O   . ASP A 1 104 ? -1.996  -10.845 -2.472  1.00 21.29 ? 104 ASP B O   1 
ATOM   795  C  CB  . ASP A 1 104 ? -1.979  -9.565  -5.324  1.00 23.36 ? 104 ASP B CB  1 
ATOM   796  C  CG  . ASP A 1 104 ? -2.224  -8.649  -6.593  1.00 28.39 ? 104 ASP B CG  1 
ATOM   797  O  OD1 . ASP A 1 104 ? -3.389  -8.316  -6.892  1.00 21.08 ? 104 ASP B OD1 1 
ATOM   798  O  OD2 . ASP A 1 104 ? -1.224  -8.295  -7.253  1.00 30.25 ? 104 ASP B OD2 1 
ATOM   799  N  N   . HIS A 1 105 ? -2.676  -8.749  -2.132  1.00 18.75 ? 105 HIS B N   1 
ATOM   800  C  CA  . HIS A 1 105 ? -1.900  -8.639  -0.920  1.00 18.37 ? 105 HIS B CA  1 
ATOM   801  C  C   . HIS A 1 105 ? -2.519  -7.608  0.009   1.00 17.79 ? 105 HIS B C   1 
ATOM   802  O  O   . HIS A 1 105 ? -2.154  -6.418  -0.019  1.00 20.52 ? 105 HIS B O   1 
ATOM   803  C  CB  . HIS A 1 105 ? -0.530  -8.157  -1.421  1.00 23.61 ? 105 HIS B CB  1 
ATOM   804  C  CG  . HIS A 1 105 ? 0.620   -8.345  -0.512  1.00 26.04 ? 105 HIS B CG  1 
ATOM   805  N  ND1 . HIS A 1 105 ? 1.185   -7.303  0.141   1.00 30.55 ? 105 HIS B ND1 1 
ATOM   806  C  CD2 . HIS A 1 105 ? 1.412   -9.490  -0.212  1.00 27.63 ? 105 HIS B CD2 1 
ATOM   807  C  CE1 . HIS A 1 105 ? 2.251   -7.750  0.863   1.00 30.97 ? 105 HIS B CE1 1 
ATOM   808  N  NE2 . HIS A 1 105 ? 2.364   -9.084  0.673   1.00 31.16 ? 105 HIS B NE2 1 
ATOM   809  N  N   . GLY A 1 106 ? -3.417  -8.026  0.901   1.00 14.44 ? 106 GLY B N   1 
ATOM   810  C  CA  . GLY A 1 106 ? -4.091  -7.093  1.792   1.00 14.65 ? 106 GLY B CA  1 
ATOM   811  C  C   . GLY A 1 106 ? -4.170  -7.495  3.251   1.00 14.09 ? 106 GLY B C   1 
ATOM   812  O  O   . GLY A 1 106 ? -4.549  -6.641  4.047   1.00 15.58 ? 106 GLY B O   1 
ATOM   813  N  N   . SER A 1 107 ? -3.936  -8.763  3.555   1.00 13.10 ? 107 SER B N   1 
ATOM   814  C  CA  . SER A 1 107 ? -4.107  -9.200  4.938   1.00 11.69 ? 107 SER B CA  1 
ATOM   815  C  C   . SER A 1 107 ? -2.877  -8.829  5.730   1.00 12.96 ? 107 SER B C   1 
ATOM   816  O  O   . SER A 1 107 ? -1.801  -8.443  5.258   1.00 14.56 ? 107 SER B O   1 
ATOM   817  C  CB  . SER A 1 107 ? -4.376  -10.701 4.997   1.00 12.10 ? 107 SER B CB  1 
ATOM   818  O  OG  . SER A 1 107 ? -3.312  -11.519 4.556   1.00 12.04 ? 107 SER B OG  1 
ATOM   819  N  N   . GLU A 1 108 ? -3.022  -8.973  7.069   1.00 11.40 ? 108 GLU B N   1 
ATOM   820  C  CA  . GLU A 1 108 ? -1.898  -8.755  7.995   1.00 11.84 ? 108 GLU B CA  1 
ATOM   821  C  C   . GLU A 1 108 ? -1.188  -10.040 8.340   1.00 11.59 ? 108 GLU B C   1 
ATOM   822  O  O   . GLU A 1 108 ? -0.011  -10.164 8.058   1.00 12.66 ? 108 GLU B O   1 
ATOM   823  C  CB  . GLU A 1 108 ? -2.465  -8.081  9.302   1.00 11.69 ? 108 GLU B CB  1 
ATOM   824  C  CG  . GLU A 1 108 ? -2.895  -6.664  8.925   1.00 14.46 ? 108 GLU B CG  1 
ATOM   825  C  CD  . GLU A 1 108 ? -2.811  -5.688  10.034  1.00 14.27 ? 108 GLU B CD  1 
ATOM   826  O  OE1 . GLU A 1 108 ? -3.293  -6.026  11.131  1.00 13.62 ? 108 GLU B OE1 1 
ATOM   827  O  OE2 . GLU A 1 108 ? -2.413  -4.554  9.839   1.00 13.22 ? 108 GLU B OE2 1 
ATOM   828  N  N   . HIS A 1 109 ? -1.901  -11.016 8.864   1.00 13.19 ? 109 HIS B N   1 
ATOM   829  C  CA  . HIS A 1 109 ? -1.350  -12.387 8.953   1.00 12.96 ? 109 HIS B CA  1 
ATOM   830  C  C   . HIS A 1 109 ? -1.270  -12.952 7.541   1.00 14.11 ? 109 HIS B C   1 
ATOM   831  O  O   . HIS A 1 109 ? -2.108  -12.647 6.638   1.00 11.84 ? 109 HIS B O   1 
ATOM   832  C  CB  . HIS A 1 109 ? -2.246  -13.258 9.858   1.00 12.05 ? 109 HIS B CB  1 
ATOM   833  C  CG  . HIS A 1 109 ? -2.244  -12.737 11.291  1.00 11.85 ? 109 HIS B CG  1 
ATOM   834  N  ND1 . HIS A 1 109 ? -3.135  -11.824 11.742  1.00 10.86 ? 109 HIS B ND1 1 
ATOM   835  C  CD2 . HIS A 1 109 ? -1.357  -12.993 12.307  1.00 11.90 ? 109 HIS B CD2 1 
ATOM   836  C  CE1 . HIS A 1 109 ? -2.783  -11.479 13.026  1.00 12.46 ? 109 HIS B CE1 1 
ATOM   837  N  NE2 . HIS A 1 109 ? -1.741  -12.223 13.366  1.00 12.43 ? 109 HIS B NE2 1 
ATOM   838  N  N   . ILE A 1 110 ? -0.245  -13.806 7.350   1.00 12.97 ? 110 ILE B N   1 
ATOM   839  C  CA  . ILE A 1 110 ? 0.092   -14.410 6.034   1.00 13.47 ? 110 ILE B CA  1 
ATOM   840  C  C   . ILE A 1 110 ? 0.280   -15.918 6.291   1.00 14.07 ? 110 ILE B C   1 
ATOM   841  O  O   . ILE A 1 110 ? 0.858   -16.235 7.315   1.00 15.82 ? 110 ILE B O   1 
ATOM   842  C  CB  . ILE A 1 110 ? 1.447   -13.848 5.582   1.00 15.76 ? 110 ILE B CB  1 
ATOM   843  C  CG1 . ILE A 1 110 ? 1.537   -12.305 5.600   1.00 21.18 ? 110 ILE B CG1 1 
ATOM   844  C  CG2 . ILE A 1 110 ? 1.813   -14.458 4.173   1.00 16.69 ? 110 ILE B CG2 1 
ATOM   845  C  CD1 . ILE A 1 110 ? 0.638   -11.689 4.635   1.00 21.84 ? 110 ILE B CD1 1 
ATOM   846  N  N   . VAL A 1 111 ? -0.311  -16.790 5.482   1.00 14.90 ? 111 VAL B N   1 
ATOM   847  C  CA  . VAL A 1 111 ? -0.349  -18.211 5.819   1.00 12.90 ? 111 VAL B CA  1 
ATOM   848  C  C   . VAL A 1 111 ? 0.465   -18.946 4.740   1.00 14.16 ? 111 VAL B C   1 
ATOM   849  O  O   . VAL A 1 111 ? 0.069   -19.018 3.592   1.00 16.64 ? 111 VAL B O   1 
ATOM   850  C  CB  . VAL A 1 111 ? -1.794  -18.756 5.855   1.00 15.57 ? 111 VAL B CB  1 
ATOM   851  C  CG1 . VAL A 1 111 ? -1.769  -20.261 6.235   1.00 18.29 ? 111 VAL B CG1 1 
ATOM   852  C  CG2 . VAL A 1 111 ? -2.644  -18.005 6.885   1.00 17.33 ? 111 VAL B CG2 1 
ATOM   853  N  N   . ASP A 1 112 ? 1.596   -19.451 5.174   1.00 14.13 ? 112 ASP B N   1 
ATOM   854  C  CA  . ASP A 1 112 ? 2.546   -20.124 4.279   1.00 15.00 ? 112 ASP B CA  1 
ATOM   855  C  C   . ASP A 1 112 ? 2.735   -19.263 3.024   1.00 16.39 ? 112 ASP B C   1 
ATOM   856  O  O   . ASP A 1 112 ? 2.720   -19.714 1.866   1.00 16.56 ? 112 ASP B O   1 
ATOM   857  C  CB  . ASP A 1 112 ? 2.033   -21.551 3.931   1.00 18.57 ? 112 ASP B CB  1 
ATOM   858  C  CG  . ASP A 1 112 ? 2.200   -22.504 5.111   1.00 20.10 ? 112 ASP B CG  1 
ATOM   859  O  OD1 . ASP A 1 112 ? 3.281   -22.485 5.708   1.00 20.87 ? 112 ASP B OD1 1 
ATOM   860  O  OD2 . ASP A 1 112 ? 1.226   -23.250 5.327   1.00 25.62 ? 112 ASP B OD2 1 
ATOM   861  N  N   . GLY A 1 113 ? 2.917   -17.965 3.261   1.00 14.63 ? 113 GLY B N   1 
ATOM   862  C  CA  . GLY A 1 113 ? 3.166   -17.055 2.133   1.00 15.04 ? 113 GLY B CA  1 
ATOM   863  C  C   . GLY A 1 113 ? 1.941   -16.493 1.456   1.00 13.09 ? 113 GLY B C   1 
ATOM   864  O  O   . GLY A 1 113 ? 2.068   -15.607 0.608   1.00 15.44 ? 113 GLY B O   1 
ATOM   865  N  N   . VAL A 1 114 ? 0.732   -16.979 1.812   1.00 15.00 ? 114 VAL B N   1 
ATOM   866  C  CA  . VAL A 1 114 ? -0.458  -16.520 1.150   1.00 16.17 ? 114 VAL B CA  1 
ATOM   867  C  C   . VAL A 1 114 ? -0.969  -15.262 1.928   1.00 17.41 ? 114 VAL B C   1 
ATOM   868  O  O   . VAL A 1 114 ? -1.229  -15.395 3.123   1.00 17.20 ? 114 VAL B O   1 
ATOM   869  C  CB  . VAL A 1 114 ? -1.515  -17.611 1.122   1.00 18.70 ? 114 VAL B CB  1 
ATOM   870  C  CG1 . VAL A 1 114 ? -2.832  -16.978 0.685   1.00 20.66 ? 114 VAL B CG1 1 
ATOM   871  C  CG2 . VAL A 1 114 ? -1.099  -18.702 0.147   1.00 19.85 ? 114 VAL B CG2 1 
ATOM   872  N  N   . SER A 1 115 ? -1.010  -14.100 1.269   1.00 16.60 ? 115 SER B N   1 
ATOM   873  C  CA  . SER A 1 115 ? -1.682  -12.879 1.789   1.00 16.13 ? 115 SER B CA  1 
ATOM   874  C  C   . SER A 1 115 ? -3.062  -12.874 1.149   1.00 18.91 ? 115 SER B C   1 
ATOM   875  O  O   . SER A 1 115 ? -3.198  -13.030 -0.093  1.00 22.29 ? 115 SER B O   1 
ATOM   876  C  CB  . SER A 1 115 ? -0.810  -11.615 1.514   1.00 18.29 ? 115 SER B CB  1 
ATOM   877  O  OG  . SER A 1 115 ? -1.493  -10.333 1.725   1.00 21.98 ? 115 SER B OG  1 
ATOM   878  N  N   . TYR A 1 116 ? -4.102  -12.689 1.955   1.00 12.72 ? 116 TYR B N   1 
ATOM   879  C  CA  . TYR A 1 116 ? -5.423  -12.662 1.478   1.00 12.06 ? 116 TYR B CA  1 
ATOM   880  C  C   . TYR A 1 116 ? -5.809  -11.254 1.005   1.00 11.33 ? 116 TYR B C   1 
ATOM   881  O  O   . TYR A 1 116 ? -5.026  -10.392 1.205   1.00 12.57 ? 116 TYR B O   1 
ATOM   882  C  CB  . TYR A 1 116 ? -6.410  -13.214 2.613   1.00 11.39 ? 116 TYR B CB  1 
ATOM   883  C  CG  . TYR A 1 116 ? -6.138  -14.638 2.806   1.00 12.80 ? 116 TYR B CG  1 
ATOM   884  C  CD1 . TYR A 1 116 ? -6.850  -15.601 2.064   1.00 14.52 ? 116 TYR B CD1 1 
ATOM   885  C  CD2 . TYR A 1 116 ? -5.208  -15.048 3.737   1.00 13.05 ? 116 TYR B CD2 1 
ATOM   886  C  CE1 . TYR A 1 116 ? -6.580  -16.991 2.284   1.00 16.53 ? 116 TYR B CE1 1 
ATOM   887  C  CE2 . TYR A 1 116 ? -4.983  -16.406 3.974   1.00 15.41 ? 116 TYR B CE2 1 
ATOM   888  C  CZ  . TYR A 1 116 ? -5.635  -17.336 3.242   1.00 16.50 ? 116 TYR B CZ  1 
ATOM   889  O  OH  . TYR A 1 116 ? -5.401  -18.731 3.410   1.00 22.21 ? 116 TYR B OH  1 
ATOM   890  N  N   . ALA A 1 117 ? -7.002  -11.068 0.455   1.00 10.57 ? 117 ALA B N   1 
ATOM   891  C  CA  . ALA A 1 117 ? -7.369  -9.729  -0.037  1.00 11.68 ? 117 ALA B CA  1 
ATOM   892  C  C   . ALA A 1 117 ? -7.573  -8.778  1.119   1.00 11.98 ? 117 ALA B C   1 
ATOM   893  O  O   . ALA A 1 117 ? -7.380  -7.596  0.963   1.00 13.10 ? 117 ALA B O   1 
ATOM   894  C  CB  . ALA A 1 117 ? -8.638  -9.860  -0.883  1.00 12.80 ? 117 ALA B CB  1 
ATOM   895  N  N   . ALA A 1 118 ? -8.021  -9.283  2.308   1.00 9.98  ? 118 ALA B N   1 
ATOM   896  C  CA  . ALA A 1 118 ? -8.255  -8.291  3.436   1.00 9.74  ? 118 ALA B CA  1 
ATOM   897  C  C   . ALA A 1 118 ? -8.292  -9.211  4.655   1.00 8.60  ? 118 ALA B C   1 
ATOM   898  O  O   . ALA A 1 118 ? -8.270  -10.444 4.600   1.00 10.21 ? 118 ALA B O   1 
ATOM   899  C  CB  . ALA A 1 118 ? -9.575  -7.494  3.230   1.00 10.05 ? 118 ALA B CB  1 
ATOM   900  N  N   . GLU A 1 119 ? -8.373  -8.472  5.781   1.00 9.13  ? 119 GLU B N   1 
ATOM   901  C  CA  . GLU A 1 119 ? -8.447  -9.229  7.089   1.00 8.95  ? 119 GLU B CA  1 
ATOM   902  C  C   . GLU A 1 119 ? -9.293  -8.425  8.101   1.00 9.23  ? 119 GLU B C   1 
ATOM   903  O  O   . GLU A 1 119 ? -8.944  -7.269  8.391   1.00 10.29 ? 119 GLU B O   1 
ATOM   904  C  CB  . GLU A 1 119 ? -7.070  -9.434  7.614   1.00 8.00  ? 119 GLU B CB  1 
ATOM   905  C  CG  . GLU A 1 119 ? -7.122  -10.299 8.939   1.00 9.59  ? 119 GLU B CG  1 
ATOM   906  C  CD  . GLU A 1 119 ? -5.717  -10.600 9.412   1.00 10.58 ? 119 GLU B CD  1 
ATOM   907  O  OE1 . GLU A 1 119 ? -4.824  -10.709 8.545   1.00 10.75 ? 119 GLU B OE1 1 
ATOM   908  O  OE2 . GLU A 1 119 ? -5.496  -10.702 10.635  1.00 11.53 ? 119 GLU B OE2 1 
ATOM   909  N  N   . LEU A 1 120 ? -10.334 -9.074  8.570   1.00 9.29  ? 120 LEU B N   1 
ATOM   910  C  CA  . LEU A 1 120 ? -11.236 -8.491  9.585   1.00 9.15  ? 120 LEU B CA  1 
ATOM   911  C  C   . LEU A 1 120 ? -10.693 -8.771  10.987  1.00 10.14 ? 120 LEU B C   1 
ATOM   912  O  O   . LEU A 1 120 ? -10.319 -9.864  11.251  1.00 10.68 ? 120 LEU B O   1 
ATOM   913  C  CB  . LEU A 1 120 ? -12.612 -9.063  9.461   1.00 10.75 ? 120 LEU B CB  1 
ATOM   914  C  CG  . LEU A 1 120 ? -13.823 -8.327  10.116  1.00 12.20 ? 120 LEU B CG  1 
ATOM   915  C  CD1 . LEU A 1 120 ? -14.209 -7.094  9.313   1.00 12.13 ? 120 LEU B CD1 1 
ATOM   916  C  CD2 . LEU A 1 120 ? -14.924 -9.339  10.333  1.00 14.76 ? 120 LEU B CD2 1 
ATOM   917  N  N   . HIS A 1 121 ? -10.697 -7.723  11.812  1.00 9.88  ? 121 HIS B N   1 
ATOM   918  C  CA  . HIS A 1 121 ? -10.352 -7.879  13.247  1.00 10.48 ? 121 HIS B CA  1 
ATOM   919  C  C   . HIS A 1 121 ? -11.581 -7.578  14.090  1.00 9.53  ? 121 HIS B C   1 
ATOM   920  O  O   . HIS A 1 121 ? -12.214 -6.555  13.993  1.00 10.50 ? 121 HIS B O   1 
ATOM   921  C  CB  . HIS A 1 121 ? -9.190  -6.920  13.598  1.00 11.00 ? 121 HIS B CB  1 
ATOM   922  C  CG  . HIS A 1 121 ? -7.951  -7.344  12.989  1.00 8.86  ? 121 HIS B CG  1 
ATOM   923  N  ND1 . HIS A 1 121 ? -6.798  -6.589  12.839  1.00 10.17 ? 121 HIS B ND1 1 
ATOM   924  C  CD2 . HIS A 1 121 ? -7.689  -8.597  12.457  1.00 9.27  ? 121 HIS B CD2 1 
ATOM   925  C  CE1 . HIS A 1 121 ? -5.837  -7.352  12.241  1.00 12.11 ? 121 HIS B CE1 1 
ATOM   926  N  NE2 . HIS A 1 121 ? -6.344  -8.564  12.025  1.00 9.31  ? 121 HIS B NE2 1 
ATOM   927  N  N   . VAL A 1 122 ? -11.846 -8.545  14.991  1.00 10.31 ? 122 VAL B N   1 
ATOM   928  C  CA  . VAL A 1 122 ? -12.963 -8.373  15.945  1.00 10.08 ? 122 VAL B CA  1 
ATOM   929  C  C   . VAL A 1 122 ? -12.296 -8.293  17.328  1.00 10.13 ? 122 VAL B C   1 
ATOM   930  O  O   . VAL A 1 122 ? -11.666 -9.239  17.798  1.00 11.19 ? 122 VAL B O   1 
ATOM   931  C  CB  . VAL A 1 122 ? -13.882 -9.594  15.942  1.00 8.93  ? 122 VAL B CB  1 
ATOM   932  C  CG1 . VAL A 1 122 ? -15.156 -9.343  16.743  1.00 12.06 ? 122 VAL B CG1 1 
ATOM   933  C  CG2 . VAL A 1 122 ? -14.288 -9.952  14.445  1.00 11.23 ? 122 VAL B CG2 1 
ATOM   934  N  N   . VAL A 1 123 ? -12.406 -7.105  17.961  1.00 10.23 ? 123 VAL B N   1 
ATOM   935  C  CA  . VAL A 1 123 ? -11.642 -6.795  19.154  1.00 10.66 ? 123 VAL B CA  1 
ATOM   936  C  C   . VAL A 1 123 ? -12.533 -6.929  20.434  1.00 9.12  ? 123 VAL B C   1 
ATOM   937  O  O   . VAL A 1 123 ? -13.648 -6.447  20.453  1.00 9.95  ? 123 VAL B O   1 
ATOM   938  C  CB  . VAL A 1 123 ? -11.118 -5.341  19.047  1.00 10.83 ? 123 VAL B CB  1 
ATOM   939  C  CG1 . VAL A 1 123 ? -10.360 -4.983  20.303  1.00 12.41 ? 123 VAL B CG1 1 
ATOM   940  C  CG2 . VAL A 1 123 ? -10.281 -5.121  17.767  1.00 11.25 ? 123 VAL B CG2 1 
ATOM   941  N  N   . HIS A 1 124 ? -11.948 -7.722  21.406  1.00 10.52 ? 124 HIS B N   1 
ATOM   942  C  CA  . HIS A 1 124 ? -12.705 -7.961  22.653  1.00 10.10 ? 124 HIS B CA  1 
ATOM   943  C  C   . HIS A 1 124 ? -11.772 -7.675  23.810  1.00 9.60  ? 124 HIS B C   1 
ATOM   944  O  O   . HIS A 1 124 ? -10.568 -7.759  23.739  1.00 10.18 ? 124 HIS B O   1 
ATOM   945  C  CB  . HIS A 1 124 ? -13.100 -9.444  22.742  1.00 10.70 ? 124 HIS B CB  1 
ATOM   946  C  CG  . HIS A 1 124 ? -13.739 -10.026 21.496  1.00 11.01 ? 124 HIS B CG  1 
ATOM   947  N  ND1 . HIS A 1 124 ? -12.947 -10.331 20.410  1.00 10.68 ? 124 HIS B ND1 1 
ATOM   948  C  CD2 . HIS A 1 124 ? -15.006 -10.502 21.251  1.00 10.96 ? 124 HIS B CD2 1 
ATOM   949  C  CE1 . HIS A 1 124 ? -13.777 -10.959 19.485  1.00 11.34 ? 124 HIS B CE1 1 
ATOM   950  N  NE2 . HIS A 1 124 ? -15.018 -11.047 19.960  1.00 11.43 ? 124 HIS B NE2 1 
ATOM   951  N  N   . TRP A 1 125 ? -12.400 -7.440  24.978  1.00 12.24 ? 125 TRP B N   1 
ATOM   952  C  CA  . TRP A 1 125 ? -11.607 -7.188  26.220  1.00 11.91 ? 125 TRP B CA  1 
ATOM   953  C  C   . TRP A 1 125 ? -12.108 -7.979  27.424  1.00 11.10 ? 125 TRP B C   1 
ATOM   954  O  O   . TRP A 1 125 ? -13.299 -8.220  27.561  1.00 11.97 ? 125 TRP B O   1 
ATOM   955  C  CB  . TRP A 1 125 ? -11.549 -5.662  26.537  1.00 12.94 ? 125 TRP B CB  1 
ATOM   956  C  CG  . TRP A 1 125 ? -12.885 -4.991  26.795  1.00 13.71 ? 125 TRP B CG  1 
ATOM   957  C  CD1 . TRP A 1 125 ? -13.762 -4.467  25.864  1.00 14.65 ? 125 TRP B CD1 1 
ATOM   958  C  CD2 . TRP A 1 125 ? -13.490 -4.658  28.105  1.00 12.70 ? 125 TRP B CD2 1 
ATOM   959  N  NE1 . TRP A 1 125 ? -14.862 -3.908  26.430  1.00 14.62 ? 125 TRP B NE1 1 
ATOM   960  C  CE2 . TRP A 1 125 ? -14.732 -4.032  27.842  1.00 15.17 ? 125 TRP B CE2 1 
ATOM   961  C  CE3 . TRP A 1 125 ? -13.120 -4.910  29.427  1.00 16.03 ? 125 TRP B CE3 1 
ATOM   962  C  CZ2 . TRP A 1 125 ? -15.537 -3.541  28.835  1.00 16.15 ? 125 TRP B CZ2 1 
ATOM   963  C  CZ3 . TRP A 1 125 ? -13.947 -4.413  30.422  1.00 16.05 ? 125 TRP B CZ3 1 
ATOM   964  C  CH2 . TRP A 1 125 ? -15.132 -3.843  30.142  1.00 16.38 ? 125 TRP B CH2 1 
ATOM   965  N  N   . ASN A 1 126 ? -11.164 -8.324  28.238  1.00 12.20 ? 126 ASN B N   1 
ATOM   966  C  CA  . ASN A 1 126 ? -11.457 -9.190  29.420  1.00 13.62 ? 126 ASN B CA  1 
ATOM   967  C  C   . ASN A 1 126 ? -12.179 -8.435  30.565  1.00 12.69 ? 126 ASN B C   1 
ATOM   968  O  O   . ASN A 1 126 ? -11.491 -7.799  31.383  1.00 14.07 ? 126 ASN B O   1 
ATOM   969  C  CB  . ASN A 1 126 ? -10.140 -9.697  29.916  1.00 12.71 ? 126 ASN B CB  1 
ATOM   970  C  CG  . ASN A 1 126 ? -10.279 -10.741 31.054  1.00 12.89 ? 126 ASN B CG  1 
ATOM   971  O  OD1 . ASN A 1 126 ? -11.356 -10.907 31.587  1.00 13.95 ? 126 ASN B OD1 1 
ATOM   972  N  ND2 . ASN A 1 126 ? -9.218  -11.515 31.216  1.00 15.87 ? 126 ASN B ND2 1 
ATOM   973  N  N   . SER A 1 127 ? -13.497 -8.506  30.590  1.00 13.20 ? 127 SER B N   1 
ATOM   974  C  CA  . SER A 1 127 ? -14.318 -7.796  31.614  1.00 13.76 ? 127 SER B CA  1 
ATOM   975  C  C   . SER A 1 127 ? -14.370 -8.655  32.868  1.00 15.90 ? 127 SER B C   1 
ATOM   976  O  O   . SER A 1 127 ? -14.834 -8.126  33.885  1.00 16.09 ? 127 SER B O   1 
ATOM   977  C  CB  . SER A 1 127 ? -15.715 -7.441  31.102  1.00 14.58 ? 127 SER B CB  1 
ATOM   978  O  OG  . SER A 1 127 ? -16.385 -8.636  30.749  1.00 17.63 ? 127 SER B OG  1 
ATOM   979  N  N   . ASP A 1 128 ? -13.908 -9.894  32.836  1.00 14.71 ? 128 ASP B N   1 
ATOM   980  C  CA  . ASP A 1 128 ? -13.876 -10.702 34.115  1.00 16.51 ? 128 ASP B CA  1 
ATOM   981  C  C   . ASP A 1 128 ? -12.708 -10.240 35.021  1.00 16.86 ? 128 ASP B C   1 
ATOM   982  O  O   . ASP A 1 128 ? -12.733 -10.546 36.253  1.00 20.14 ? 128 ASP B O   1 
ATOM   983  C  CB  . ASP A 1 128 ? -13.671 -12.131 33.813  1.00 16.62 ? 128 ASP B CB  1 
ATOM   984  C  CG  . ASP A 1 128 ? -14.937 -12.847 33.346  1.00 16.87 ? 128 ASP B CG  1 
ATOM   985  O  OD1 . ASP A 1 128 ? -14.798 -14.003 32.890  1.00 18.08 ? 128 ASP B OD1 1 
ATOM   986  O  OD2 . ASP A 1 128 ? -16.052 -12.282 33.436  1.00 20.83 ? 128 ASP B OD2 1 
ATOM   987  N  N   . LYS A 1 129 ? -11.671 -9.567  34.486  1.00 14.80 ? 129 LYS B N   1 
ATOM   988  C  CA  . LYS A 1 129 ? -10.503 -9.133  35.264  1.00 15.06 ? 129 LYS B CA  1 
ATOM   989  C  C   . LYS A 1 129 ? -10.387 -7.655  35.305  1.00 14.99 ? 129 LYS B C   1 
ATOM   990  O  O   . LYS A 1 129 ? -9.710  -7.119  36.178  1.00 17.93 ? 129 LYS B O   1 
ATOM   991  C  CB  . LYS A 1 129 ? -9.186  -9.768  34.789  1.00 17.39 ? 129 LYS B CB  1 
ATOM   992  C  CG  . LYS A 1 129 ? -9.098  -11.287 35.034  1.00 19.66 ? 129 LYS B CG  1 
ATOM   993  C  CD  . LYS A 1 129 ? -7.661  -11.702 34.790  1.00 21.78 ? 129 LYS B CD  1 
ATOM   994  C  CE  . LYS A 1 129 ? -6.616  -11.076 35.715  1.00 21.73 ? 129 LYS B CE  1 
ATOM   995  N  NZ  . LYS A 1 129 ? -5.150  -11.343 35.378  1.00 24.21 ? 129 LYS B NZ  1 
ATOM   996  N  N   . TYR A 1 130 ? -10.846 -6.944  34.262  1.00 13.82 ? 130 TYR B N   1 
ATOM   997  C  CA  . TYR A 1 130 ? -10.625 -5.527  34.121  1.00 13.81 ? 130 TYR B CA  1 
ATOM   998  C  C   . TYR A 1 130 ? -11.896 -4.772  34.035  1.00 12.48 ? 130 TYR B C   1 
ATOM   999  O  O   . TYR A 1 130 ? -12.917 -5.278  33.579  1.00 13.63 ? 130 TYR B O   1 
ATOM   1000 C  CB  . TYR A 1 130 ? -9.723  -5.222  32.834  1.00 13.53 ? 130 TYR B CB  1 
ATOM   1001 C  CG  . TYR A 1 130 ? -8.436  -5.992  32.923  1.00 14.22 ? 130 TYR B CG  1 
ATOM   1002 C  CD1 . TYR A 1 130 ? -7.488  -5.718  33.964  1.00 17.26 ? 130 TYR B CD1 1 
ATOM   1003 C  CD2 . TYR A 1 130 ? -8.174  -7.140  32.141  1.00 14.48 ? 130 TYR B CD2 1 
ATOM   1004 C  CE1 . TYR A 1 130 ? -6.394  -6.528  34.159  1.00 17.47 ? 130 TYR B CE1 1 
ATOM   1005 C  CE2 . TYR A 1 130 ? -7.040  -7.915  32.325  1.00 16.22 ? 130 TYR B CE2 1 
ATOM   1006 C  CZ  . TYR A 1 130 ? -6.116  -7.615  33.338  1.00 17.26 ? 130 TYR B CZ  1 
ATOM   1007 O  OH  . TYR A 1 130 ? -5.037  -8.392  33.501  1.00 19.31 ? 130 TYR B OH  1 
ATOM   1008 N  N   . PRO A 1 131 ? -11.885 -3.474  34.500  1.00 14.52 ? 131 PRO B N   1 
ATOM   1009 C  CA  . PRO A 1 131 ? -13.138 -2.761  34.547  1.00 14.43 ? 131 PRO B CA  1 
ATOM   1010 C  C   . PRO A 1 131 ? -13.560 -2.020  33.250  1.00 14.15 ? 131 PRO B C   1 
ATOM   1011 O  O   . PRO A 1 131 ? -14.688 -1.572  33.135  1.00 15.91 ? 131 PRO B O   1 
ATOM   1012 C  CB  . PRO A 1 131 ? -12.897 -1.723  35.683  1.00 15.18 ? 131 PRO B CB  1 
ATOM   1013 C  CG  . PRO A 1 131 ? -11.464 -1.447  35.612  1.00 13.72 ? 131 PRO B CG  1 
ATOM   1014 C  CD  . PRO A 1 131 ? -10.798 -2.755  35.233  1.00 13.63 ? 131 PRO B CD  1 
ATOM   1015 N  N   . SER A 1 132 ? -12.589 -1.972  32.344  1.00 14.51 ? 132 SER B N   1 
ATOM   1016 C  CA  . SER A 1 132 ? -12.846 -1.210  31.103  1.00 16.04 ? 132 SER B CA  1 
ATOM   1017 C  C   . SER A 1 132 ? -11.825 -1.697  30.035  1.00 14.72 ? 132 SER B C   1 
ATOM   1018 O  O   . SER A 1 132 ? -10.789 -2.257  30.331  1.00 15.34 ? 132 SER B O   1 
ATOM   1019 C  CB  . SER A 1 132 ? -12.586 0.269   31.343  1.00 16.27 ? 132 SER B CB  1 
ATOM   1020 O  OG  . SER A 1 132 ? -11.254 0.528   31.604  1.00 19.39 ? 132 SER B OG  1 
ATOM   1021 N  N   . PHE A 1 133 ? -12.193 -1.400  28.770  1.00 15.33 ? 133 PHE B N   1 
ATOM   1022 C  CA  . PHE A 1 133 ? -11.287 -1.692  27.695  1.00 16.46 ? 133 PHE B CA  1 
ATOM   1023 C  C   . PHE A 1 133 ? -9.956  -1.037  27.878  1.00 15.33 ? 133 PHE B C   1 
ATOM   1024 O  O   . PHE A 1 133 ? -8.941  -1.618  27.625  1.00 15.29 ? 133 PHE B O   1 
ATOM   1025 C  CB  . PHE A 1 133 ? -11.911 -1.140  26.437  1.00 16.17 ? 133 PHE B CB  1 
ATOM   1026 C  CG  . PHE A 1 133 ? -11.004 -1.228  25.247  1.00 18.54 ? 133 PHE B CG  1 
ATOM   1027 C  CD1 . PHE A 1 133 ? -10.763 -2.449  24.613  1.00 20.56 ? 133 PHE B CD1 1 
ATOM   1028 C  CD2 . PHE A 1 133 ? -10.315 -0.109  24.826  1.00 22.46 ? 133 PHE B CD2 1 
ATOM   1029 C  CE1 . PHE A 1 133 ? -9.874  -2.519  23.523  1.00 25.07 ? 133 PHE B CE1 1 
ATOM   1030 C  CE2 . PHE A 1 133 ? -9.456  -0.162  23.732  1.00 22.86 ? 133 PHE B CE2 1 
ATOM   1031 C  CZ  . PHE A 1 133 ? -9.197  -1.385  23.140  1.00 23.99 ? 133 PHE B CZ  1 
ATOM   1032 N  N   . VAL A 1 134 ? -9.981  0.261   28.304  1.00 17.10 ? 134 VAL B N   1 
ATOM   1033 C  CA  . VAL A 1 134 ? -8.700  0.949   28.419  1.00 19.03 ? 134 VAL B CA  1 
ATOM   1034 C  C   . VAL A 1 134 ? -7.761  0.322   29.402  1.00 17.17 ? 134 VAL B C   1 
ATOM   1035 O  O   . VAL A 1 134 ? -6.582  0.172   29.116  1.00 19.47 ? 134 VAL B O   1 
ATOM   1036 C  CB  . VAL A 1 134 ? -8.832  2.483   28.678  1.00 23.06 ? 134 VAL B CB  1 
ATOM   1037 C  CG1 . VAL A 1 134 ? -7.403  3.127   28.603  1.00 26.12 ? 134 VAL B CG1 1 
ATOM   1038 C  CG2 . VAL A 1 134 ? -9.778  3.170   27.689  1.00 27.62 ? 134 VAL B CG2 1 
ATOM   1039 N  N   . GLU A 1 135 ? -8.282  -0.183  30.565  1.00 17.45 ? 135 GLU B N   1 
ATOM   1040 C  CA  . GLU A 1 135 ? -7.394  -0.928  31.457  1.00 17.40 ? 135 GLU B CA  1 
ATOM   1041 C  C   . GLU A 1 135 ? -6.923  -2.305  30.911  1.00 16.96 ? 135 GLU B C   1 
ATOM   1042 O  O   . GLU A 1 135 ? -5.779  -2.702  30.991  1.00 15.37 ? 135 GLU B O   1 
ATOM   1043 C  CB  . GLU A 1 135 ? -8.102  -1.181  32.818  1.00 16.06 ? 135 GLU B CB  1 
ATOM   1044 C  CG  . GLU A 1 135 ? -8.354  0.148   33.581  1.00 21.12 ? 135 GLU B CG  1 
ATOM   1045 C  CD  . GLU A 1 135 ? -7.102  0.802   34.084  1.00 24.08 ? 135 GLU B CD  1 
ATOM   1046 O  OE1 . GLU A 1 135 ? -7.261  1.894   34.673  1.00 27.99 ? 135 GLU B OE1 1 
ATOM   1047 O  OE2 . GLU A 1 135 ? -5.996  0.259   33.971  1.00 23.65 ? 135 GLU B OE2 1 
ATOM   1048 N  N   . ALA A 1 136 ? -7.872  -2.998  30.302  1.00 14.63 ? 136 ALA B N   1 
ATOM   1049 C  CA  . ALA A 1 136 ? -7.565  -4.279  29.682  1.00 14.63 ? 136 ALA B CA  1 
ATOM   1050 C  C   . ALA A 1 136 ? -6.439  -4.165  28.598  1.00 15.71 ? 136 ALA B C   1 
ATOM   1051 O  O   . ALA A 1 136 ? -5.604  -5.075  28.437  1.00 15.24 ? 136 ALA B O   1 
ATOM   1052 C  CB  . ALA A 1 136 ? -8.803  -4.902  29.091  1.00 13.08 ? 136 ALA B CB  1 
ATOM   1053 N  N   . ALA A 1 137 ? -6.513  -3.066  27.861  1.00 16.13 ? 137 ALA B N   1 
ATOM   1054 C  CA  . ALA A 1 137 ? -5.575  -2.903  26.749  1.00 16.22 ? 137 ALA B CA  1 
ATOM   1055 C  C   . ALA A 1 137 ? -4.080  -2.864  27.113  1.00 17.14 ? 137 ALA B C   1 
ATOM   1056 O  O   . ALA A 1 137 ? -3.168  -3.007  26.266  1.00 15.78 ? 137 ALA B O   1 
ATOM   1057 C  CB  . ALA A 1 137 ? -5.968  -1.650  25.925  1.00 15.13 ? 137 ALA B CB  1 
ATOM   1058 N  N   . HIS A 1 138 ? -3.788  -2.680  28.428  1.00 17.62 ? 138 HIS B N   1 
ATOM   1059 C  CA  . HIS A 1 138 ? -2.416  -2.585  28.911  1.00 19.64 ? 138 HIS B CA  1 
ATOM   1060 C  C   . HIS A 1 138 ? -1.985  -3.783  29.711  1.00 20.07 ? 138 HIS B C   1 
ATOM   1061 O  O   . HIS A 1 138 ? -1.051  -3.687  30.497  1.00 25.69 ? 138 HIS B O   1 
ATOM   1062 C  CB  . HIS A 1 138 ? -2.388  -1.343  29.805  1.00 20.35 ? 138 HIS B CB  1 
ATOM   1063 C  CG  . HIS A 1 138 ? -2.462  -0.059  29.013  1.00 22.34 ? 138 HIS B CG  1 
ATOM   1064 N  ND1 . HIS A 1 138 ? -3.607  0.568   28.729  1.00 27.99 ? 138 HIS B ND1 1 
ATOM   1065 C  CD2 . HIS A 1 138 ? -1.454  0.667   28.397  1.00 23.67 ? 138 HIS B CD2 1 
ATOM   1066 C  CE1 . HIS A 1 138 ? -3.361  1.673   27.961  1.00 24.68 ? 138 HIS B CE1 1 
ATOM   1067 N  NE2 . HIS A 1 138 ? -2.058  1.724   27.754  1.00 24.74 ? 138 HIS B NE2 1 
ATOM   1068 N  N   . GLU A 1 139 ? -2.648  -4.949  29.544  1.00 17.53 ? 139 GLU B N   1 
ATOM   1069 C  CA  . GLU A 1 139 ? -2.337  -6.158  30.271  1.00 19.90 ? 139 GLU B CA  1 
ATOM   1070 C  C   . GLU A 1 139 ? -2.215  -7.285  29.315  1.00 17.82 ? 139 GLU B C   1 
ATOM   1071 O  O   . GLU A 1 139 ? -3.019  -7.352  28.371  1.00 16.46 ? 139 GLU B O   1 
ATOM   1072 C  CB  . GLU A 1 139 ? -3.503  -6.509  31.238  1.00 23.37 ? 139 GLU B CB  1 
ATOM   1073 C  CG  . GLU A 1 139 ? -3.761  -5.471  32.302  1.00 28.68 ? 139 GLU B CG  1 
ATOM   1074 C  CD  . GLU A 1 139 ? -2.881  -5.658  33.490  1.00 34.80 ? 139 GLU B CD  1 
ATOM   1075 O  OE1 . GLU A 1 139 ? -1.710  -6.117  33.364  1.00 40.64 ? 139 GLU B OE1 1 
ATOM   1076 O  OE2 . GLU A 1 139 ? -3.369  -5.282  34.571  1.00 40.82 ? 139 GLU B OE2 1 
ATOM   1077 N  N   . PRO A 1 140 ? -1.295  -8.219  29.524  1.00 17.87 ? 140 PRO B N   1 
ATOM   1078 C  CA  . PRO A 1 140 ? -1.060  -9.339  28.582  1.00 16.99 ? 140 PRO B CA  1 
ATOM   1079 C  C   . PRO A 1 140 ? -2.266  -10.159 28.318  1.00 16.81 ? 140 PRO B C   1 
ATOM   1080 O  O   . PRO A 1 140 ? -2.412  -10.727 27.200  1.00 17.43 ? 140 PRO B O   1 
ATOM   1081 C  CB  . PRO A 1 140 ? 0.058   -10.157 29.227  1.00 16.81 ? 140 PRO B CB  1 
ATOM   1082 C  CG  . PRO A 1 140 ? 0.767   -9.131  30.070  1.00 24.27 ? 140 PRO B CG  1 
ATOM   1083 C  CD  . PRO A 1 140 ? -0.316  -8.268  30.644  1.00 19.66 ? 140 PRO B CD  1 
ATOM   1084 N  N   . ASP A 1 141 ? -3.118  -10.337 29.311  1.00 14.27 ? 141 ASP B N   1 
ATOM   1085 C  CA  . ASP A 1 141 ? -4.333  -11.108 29.176  1.00 14.00 ? 141 ASP B CA  1 
ATOM   1086 C  C   . ASP A 1 141 ? -5.580  -10.243 28.911  1.00 12.35 ? 141 ASP B C   1 
ATOM   1087 O  O   . ASP A 1 141 ? -6.705  -10.725 29.062  1.00 13.61 ? 141 ASP B O   1 
ATOM   1088 C  CB  . ASP A 1 141 ? -4.592  -12.033 30.397  1.00 16.34 ? 141 ASP B CB  1 
ATOM   1089 C  CG  . ASP A 1 141 ? -4.765  -11.239 31.651  1.00 17.01 ? 141 ASP B CG  1 
ATOM   1090 O  OD1 . ASP A 1 141 ? -4.479  -10.027 31.663  1.00 18.93 ? 141 ASP B OD1 1 
ATOM   1091 O  OD2 . ASP A 1 141 ? -5.315  -11.824 32.636  1.00 22.24 ? 141 ASP B OD2 1 
ATOM   1092 N  N   . GLY A 1 142 ? -5.365  -8.948  28.514  1.00 12.22 ? 142 GLY B N   1 
ATOM   1093 C  CA  . GLY A 1 142 ? -6.460  -8.006  28.423  1.00 13.20 ? 142 GLY B CA  1 
ATOM   1094 C  C   . GLY A 1 142 ? -7.379  -8.130  27.223  1.00 11.39 ? 142 GLY B C   1 
ATOM   1095 O  O   . GLY A 1 142 ? -8.602  -7.912  27.329  1.00 12.54 ? 142 GLY B O   1 
ATOM   1096 N  N   . LEU A 1 143 ? -6.748  -8.358  26.054  1.00 13.71 ? 143 LEU B N   1 
ATOM   1097 C  CA  . LEU A 1 143 ? -7.563  -8.315  24.815  1.00 12.20 ? 143 LEU B CA  1 
ATOM   1098 C  C   . LEU A 1 143 ? -7.519  -9.646  24.069  1.00 11.35 ? 143 LEU B C   1 
ATOM   1099 O  O   . LEU A 1 143 ? -6.574  -10.413 24.167  1.00 11.25 ? 143 LEU B O   1 
ATOM   1100 C  CB  . LEU A 1 143 ? -6.962  -7.231  23.861  1.00 12.68 ? 143 LEU B CB  1 
ATOM   1101 C  CG  . LEU A 1 143 ? -6.894  -5.827  24.448  1.00 12.70 ? 143 LEU B CG  1 
ATOM   1102 C  CD1 . LEU A 1 143 ? -6.466  -4.866  23.285  1.00 14.81 ? 143 LEU B CD1 1 
ATOM   1103 C  CD2 . LEU A 1 143 ? -8.271  -5.390  24.958  1.00 13.68 ? 143 LEU B CD2 1 
ATOM   1104 N  N   . ALA A 1 144 ? -8.607  -9.900  23.310  1.00 12.24 ? 144 ALA B N   1 
ATOM   1105 C  CA  . ALA A 1 144 ? -8.666  -11.091 22.430  1.00 11.60 ? 144 ALA B CA  1 
ATOM   1106 C  C   . ALA A 1 144 ? -9.136  -10.491 21.085  1.00 10.37 ? 144 ALA B C   1 
ATOM   1107 O  O   . ALA A 1 144 ? -10.167 -9.854  21.068  1.00 12.10 ? 144 ALA B O   1 
ATOM   1108 C  CB  . ALA A 1 144 ? -9.654  -12.167 22.916  1.00 11.43 ? 144 ALA B CB  1 
ATOM   1109 N  N   . VAL A 1 145 ? -8.409  -10.905 20.025  1.00 10.65 ? 145 VAL B N   1 
ATOM   1110 C  CA  . VAL A 1 145 ? -8.826  -10.420 18.661  1.00 10.47 ? 145 VAL B CA  1 
ATOM   1111 C  C   . VAL A 1 145 ? -9.023  -11.664 17.810  1.00 10.78 ? 145 VAL B C   1 
ATOM   1112 O  O   . VAL A 1 145 ? -8.110  -12.492 17.723  1.00 11.09 ? 145 VAL B O   1 
ATOM   1113 C  CB  . VAL A 1 145 ? -7.792  -9.471  18.045  1.00 12.26 ? 145 VAL B CB  1 
ATOM   1114 C  CG1 . VAL A 1 145 ? -8.312  -9.003  16.647  1.00 14.74 ? 145 VAL B CG1 1 
ATOM   1115 C  CG2 . VAL A 1 145 ? -7.609  -8.261  19.005  1.00 13.74 ? 145 VAL B CG2 1 
ATOM   1116 N  N   . LEU A 1 146 ? -10.202 -11.718 17.216  1.00 10.58 ? 146 LEU B N   1 
ATOM   1117 C  CA  . LEU A 1 146 ? -10.494 -12.710 16.188  1.00 10.73 ? 146 LEU B CA  1 
ATOM   1118 C  C   . LEU A 1 146 ? -10.120 -12.126 14.824  1.00 11.37 ? 146 LEU B C   1 
ATOM   1119 O  O   . LEU A 1 146 ? -10.654 -11.036 14.443  1.00 13.50 ? 146 LEU B O   1 
ATOM   1120 C  CB  . LEU A 1 146 ? -11.984 -13.051 16.252  1.00 12.50 ? 146 LEU B CB  1 
ATOM   1121 C  CG  . LEU A 1 146 ? -12.552 -14.167 15.451  1.00 15.81 ? 146 LEU B CG  1 
ATOM   1122 C  CD1 . LEU A 1 146 ? -11.930 -15.586 15.742  1.00 14.78 ? 146 LEU B CD1 1 
ATOM   1123 C  CD2 . LEU A 1 146 ? -14.059 -14.184 15.673  1.00 15.34 ? 146 LEU B CD2 1 
ATOM   1124 N  N   . GLY A 1 147 ? -9.200  -12.783 14.155  1.00 10.94 ? 147 GLY B N   1 
ATOM   1125 C  CA  . GLY A 1 147 ? -8.943  -12.374 12.752  1.00 10.15 ? 147 GLY B CA  1 
ATOM   1126 C  C   . GLY A 1 147 ? -9.567  -13.323 11.764  1.00 11.07 ? 147 GLY B C   1 
ATOM   1127 O  O   . GLY A 1 147 ? -9.560  -14.549 11.886  1.00 10.92 ? 147 GLY B O   1 
ATOM   1128 N  N   . VAL A 1 148 ? -10.176 -12.725 10.750  1.00 11.23 ? 148 VAL B N   1 
ATOM   1129 C  CA  . VAL A 1 148 ? -10.881 -13.479 9.700   1.00 10.02 ? 148 VAL B CA  1 
ATOM   1130 C  C   . VAL A 1 148 ? -10.402 -12.963 8.333   1.00 10.64 ? 148 VAL B C   1 
ATOM   1131 O  O   . VAL A 1 148 ? -10.480 -11.752 8.050   1.00 10.75 ? 148 VAL B O   1 
ATOM   1132 C  CB  . VAL A 1 148 ? -12.395 -13.248 9.765   1.00 10.58 ? 148 VAL B CB  1 
ATOM   1133 C  CG1 . VAL A 1 148 ? -13.150 -14.139 8.763   1.00 12.03 ? 148 VAL B CG1 1 
ATOM   1134 C  CG2 . VAL A 1 148 ? -12.908 -13.502 11.243  1.00 13.17 ? 148 VAL B CG2 1 
ATOM   1135 N  N   . PHE A 1 149 ? -9.913  -13.899 7.539   1.00 11.27 ? 149 PHE B N   1 
ATOM   1136 C  CA  . PHE A 1 149 ? -9.422  -13.508 6.191   1.00 9.80  ? 149 PHE B CA  1 
ATOM   1137 C  C   . PHE A 1 149 ? -10.595 -13.372 5.267   1.00 10.15 ? 149 PHE B C   1 
ATOM   1138 O  O   . PHE A 1 149 ? -11.632 -14.020 5.400   1.00 10.68 ? 149 PHE B O   1 
ATOM   1139 C  CB  . PHE A 1 149 ? -8.536  -14.643 5.634   1.00 9.63  ? 149 PHE B CB  1 
ATOM   1140 C  CG  . PHE A 1 149 ? -7.276  -14.825 6.447   1.00 9.77  ? 149 PHE B CG  1 
ATOM   1141 C  CD1 . PHE A 1 149 ? -6.385  -13.753 6.642   1.00 8.96  ? 149 PHE B CD1 1 
ATOM   1142 C  CD2 . PHE A 1 149 ? -6.981  -16.082 7.003   1.00 10.67 ? 149 PHE B CD2 1 
ATOM   1143 C  CE1 . PHE A 1 149 ? -5.173  -13.944 7.353   1.00 9.54  ? 149 PHE B CE1 1 
ATOM   1144 C  CE2 . PHE A 1 149 ? -5.784  -16.286 7.712   1.00 11.53 ? 149 PHE B CE2 1 
ATOM   1145 C  CZ  . PHE A 1 149 ? -4.903  -15.232 7.871   1.00 9.74  ? 149 PHE B CZ  1 
ATOM   1146 N  N   . LEU A 1 150 ? -10.411 -12.405 4.335   1.00 11.13 ? 150 LEU B N   1 
ATOM   1147 C  CA  . LEU A 1 150 ? -11.343 -12.207 3.163   1.00 11.91 ? 150 LEU B CA  1 
ATOM   1148 C  C   . LEU A 1 150 ? -10.592 -12.535 1.884   1.00 11.99 ? 150 LEU B C   1 
ATOM   1149 O  O   . LEU A 1 150 ? -9.483  -12.063 1.671   1.00 11.62 ? 150 LEU B O   1 
ATOM   1150 C  CB  . LEU A 1 150 ? -11.836 -10.760 3.119   1.00 11.87 ? 150 LEU B CB  1 
ATOM   1151 C  CG  . LEU A 1 150 ? -12.862 -10.301 4.106   1.00 13.62 ? 150 LEU B CG  1 
ATOM   1152 C  CD1 . LEU A 1 150 ? -12.366 -10.329 5.589   1.00 13.63 ? 150 LEU B CD1 1 
ATOM   1153 C  CD2 . LEU A 1 150 ? -13.393 -8.843  3.815   1.00 13.24 ? 150 LEU B CD2 1 
ATOM   1154 N  N   . GLN A 1 151 ? -11.269 -13.345 1.065   1.00 11.76 ? 151 GLN B N   1 
ATOM   1155 C  CA  . GLN A 1 151 ? -10.794 -13.611 -0.313  1.00 11.89 ? 151 GLN B CA  1 
ATOM   1156 C  C   . GLN A 1 151 ? -11.817 -13.117 -1.273  1.00 12.87 ? 151 GLN B C   1 
ATOM   1157 O  O   . GLN A 1 151 ? -12.988 -13.003 -0.943  1.00 11.96 ? 151 GLN B O   1 
ATOM   1158 C  CB  . GLN A 1 151 ? -10.477 -15.074 -0.536  1.00 15.41 ? 151 GLN B CB  1 
ATOM   1159 C  CG  . GLN A 1 151 ? -11.677 -15.898 -0.405  1.00 16.89 ? 151 GLN B CG  1 
ATOM   1160 C  CD  . GLN A 1 151 ? -11.343 -17.368 -0.455  1.00 21.18 ? 151 GLN B CD  1 
ATOM   1161 O  OE1 . GLN A 1 151 ? -10.148 -17.780 -0.495  1.00 24.12 ? 151 GLN B OE1 1 
ATOM   1162 N  NE2 . GLN A 1 151 ? -12.390 -18.139 -0.479  1.00 24.77 ? 151 GLN B NE2 1 
ATOM   1163 N  N   . ILE A 1 152 ? -11.378 -12.845 -2.524  1.00 14.34 ? 152 ILE B N   1 
ATOM   1164 C  CA  . ILE A 1 152 ? -12.319 -12.325 -3.521  1.00 15.51 ? 152 ILE B CA  1 
ATOM   1165 C  C   . ILE A 1 152 ? -13.194 -13.461 -4.022  1.00 14.56 ? 152 ILE B C   1 
ATOM   1166 O  O   . ILE A 1 152 ? -12.706 -14.573 -4.256  1.00 16.97 ? 152 ILE B O   1 
ATOM   1167 C  CB  . ILE A 1 152 ? -11.564 -11.706 -4.727  1.00 15.70 ? 152 ILE B CB  1 
ATOM   1168 C  CG1 . ILE A 1 152 ? -10.687 -10.546 -4.237  1.00 15.76 ? 152 ILE B CG1 1 
ATOM   1169 C  CG2 . ILE A 1 152 ? -12.588 -11.277 -5.782  1.00 16.65 ? 152 ILE B CG2 1 
ATOM   1170 C  CD1 . ILE A 1 152 ? -11.469 -9.516  -3.502  1.00 16.78 ? 152 ILE B CD1 1 
ATOM   1171 N  N   . GLY A 1 153 ? -14.476 -13.199 -4.041  1.00 13.88 ? 153 GLY B N   1 
ATOM   1172 C  CA  . GLY A 1 153 ? -15.451 -14.192 -4.513  1.00 15.77 ? 153 GLY B CA  1 
ATOM   1173 C  C   . GLY A 1 153 ? -16.808 -13.509 -4.579  1.00 14.38 ? 153 GLY B C   1 
ATOM   1174 O  O   . GLY A 1 153 ? -16.886 -12.305 -5.020  1.00 16.14 ? 153 GLY B O   1 
ATOM   1175 N  N   . GLU A 1 154 ? -17.850 -14.235 -4.164  1.00 15.21 ? 154 GLU B N   1 
ATOM   1176 C  CA  . GLU A 1 154 ? -19.207 -13.764 -4.292  1.00 18.95 ? 154 GLU B CA  1 
ATOM   1177 C  C   . GLU A 1 154 ? -19.377 -12.550 -3.356  1.00 16.57 ? 154 GLU B C   1 
ATOM   1178 O  O   . GLU A 1 154 ? -18.771 -12.545 -2.268  1.00 16.54 ? 154 GLU B O   1 
ATOM   1179 C  CB  . GLU A 1 154 ? -20.167 -14.842 -3.734  1.00 21.39 ? 154 GLU B CB  1 
ATOM   1180 C  CG  . GLU A 1 154 ? -21.609 -14.492 -3.239  1.00 24.52 ? 154 GLU B CG  1 
ATOM   1181 C  CD  . GLU A 1 154 ? -22.506 -15.758 -3.071  1.00 28.51 ? 154 GLU B CD  1 
ATOM   1182 O  OE1 . GLU A 1 154 ? -22.844 -16.379 -4.121  1.00 27.31 ? 154 GLU B OE1 1 
ATOM   1183 O  OE2 . GLU A 1 154 ? -22.882 -16.177 -1.927  1.00 25.90 ? 154 GLU B OE2 1 
ATOM   1184 N  N   . PRO A 1 155 ? -20.156 -11.541 -3.714  1.00 16.05 ? 155 PRO B N   1 
ATOM   1185 C  CA  . PRO A 1 155 ? -20.440 -10.409 -2.818  1.00 13.95 ? 155 PRO B CA  1 
ATOM   1186 C  C   . PRO A 1 155 ? -20.960 -10.948 -1.499  1.00 13.49 ? 155 PRO B C   1 
ATOM   1187 O  O   . PRO A 1 155 ? -21.715 -11.926 -1.451  1.00 15.00 ? 155 PRO B O   1 
ATOM   1188 C  CB  . PRO A 1 155 ? -21.535 -9.602  -3.570  1.00 14.93 ? 155 PRO B CB  1 
ATOM   1189 C  CG  . PRO A 1 155 ? -21.361 -10.011 -5.009  1.00 15.93 ? 155 PRO B CG  1 
ATOM   1190 C  CD  . PRO A 1 155 ? -20.857 -11.401 -5.022  1.00 15.21 ? 155 PRO B CD  1 
ATOM   1191 N  N   . ASN A 1 156 ? -20.608 -10.258 -0.430  1.00 13.87 ? 156 ASN B N   1 
ATOM   1192 C  CA  . ASN A 1 156 ? -21.084 -10.644 0.868   1.00 14.29 ? 156 ASN B CA  1 
ATOM   1193 C  C   . ASN A 1 156 ? -22.208 -9.747  1.340   1.00 13.87 ? 156 ASN B C   1 
ATOM   1194 O  O   . ASN A 1 156 ? -22.056 -8.549  1.455   1.00 14.21 ? 156 ASN B O   1 
ATOM   1195 C  CB  . ASN A 1 156 ? -19.869 -10.552 1.792   1.00 16.52 ? 156 ASN B CB  1 
ATOM   1196 C  CG  . ASN A 1 156 ? -20.107 -11.162 3.091   1.00 18.32 ? 156 ASN B CG  1 
ATOM   1197 O  OD1 . ASN A 1 156 ? -21.055 -10.755 3.850   1.00 18.68 ? 156 ASN B OD1 1 
ATOM   1198 N  ND2 . ASN A 1 156 ? -19.217 -12.097 3.437   1.00 16.63 ? 156 ASN B ND2 1 
ATOM   1199 N  N   . SER A 1 157 ? -23.378 -10.368 1.556   1.00 15.69 ? 157 SER B N   1 
ATOM   1200 C  CA  . SER A 1 157 ? -24.524 -9.541  1.863   1.00 16.86 ? 157 SER B CA  1 
ATOM   1201 C  C   . SER A 1 157 ? -24.418 -8.776  3.182   1.00 17.00 ? 157 SER B C   1 
ATOM   1202 O  O   . SER A 1 157 ? -24.939 -7.658  3.264   1.00 20.77 ? 157 SER B O   1 
ATOM   1203 C  CB  . SER A 1 157 ? -25.849 -10.348 1.749   1.00 18.00 ? 157 SER B CB  1 
ATOM   1204 O  OG  . SER A 1 157 ? -25.835 -11.338 2.773   1.00 20.75 ? 157 SER B OG  1 
ATOM   1205 N  N   A GLN A 1 158 ? -23.777 -9.343  4.208   0.50 15.16 ? 158 GLN B N   1 
ATOM   1206 N  N   B GLN A 1 158 ? -23.728 -9.320  4.167   0.50 15.21 ? 158 GLN B N   1 
ATOM   1207 C  CA  A GLN A 1 158 ? -23.565 -8.553  5.453   0.50 15.48 ? 158 GLN B CA  1 
ATOM   1208 C  CA  B GLN A 1 158 ? -23.524 -8.586  5.422   0.50 15.99 ? 158 GLN B CA  1 
ATOM   1209 C  C   A GLN A 1 158 ? -22.578 -7.427  5.222   0.50 15.69 ? 158 GLN B C   1 
ATOM   1210 C  C   B GLN A 1 158 ? -22.455 -7.506  5.341   0.50 16.42 ? 158 GLN B C   1 
ATOM   1211 O  O   A GLN A 1 158 ? -22.826 -6.267  5.702   0.50 14.22 ? 158 GLN B O   1 
ATOM   1212 O  O   B GLN A 1 158 ? -22.512 -6.453  6.011   0.50 17.80 ? 158 GLN B O   1 
ATOM   1213 C  CB  A GLN A 1 158 ? -23.089 -9.395  6.647   0.50 16.77 ? 158 GLN B CB  1 
ATOM   1214 C  CB  B GLN A 1 158 ? -23.183 -9.601  6.473   0.50 16.76 ? 158 GLN B CB  1 
ATOM   1215 C  CG  A GLN A 1 158 ? -24.136 -10.228 7.397   0.50 17.14 ? 158 GLN B CG  1 
ATOM   1216 C  CG  B GLN A 1 158 ? -24.269 -10.642 6.560   0.50 17.48 ? 158 GLN B CG  1 
ATOM   1217 C  CD  A GLN A 1 158 ? -25.373 -9.525  7.951   0.50 16.43 ? 158 GLN B CD  1 
ATOM   1218 C  CD  B GLN A 1 158 ? -23.966 -11.589 7.657   0.50 17.96 ? 158 GLN B CD  1 
ATOM   1219 O  OE1 A GLN A 1 158 ? -26.461 -9.905  7.537   0.50 21.93 ? 158 GLN B OE1 1 
ATOM   1220 O  OE1 B GLN A 1 158 ? -23.454 -12.683 7.408   0.50 19.76 ? 158 GLN B OE1 1 
ATOM   1221 N  NE2 A GLN A 1 158 ? -25.247 -8.622  8.955   0.50 14.13 ? 158 GLN B NE2 1 
ATOM   1222 N  NE2 B GLN A 1 158 ? -24.176 -11.123 8.923   0.50 18.76 ? 158 GLN B NE2 1 
ATOM   1223 N  N   . LEU A 1 159 ? -21.509 -7.703  4.448   1.00 14.75 ? 159 LEU B N   1 
ATOM   1224 C  CA  . LEU A 1 159 ? -20.518 -6.626  4.166   1.00 14.34 ? 159 LEU B CA  1 
ATOM   1225 C  C   . LEU A 1 159 ? -21.107 -5.490  3.323   1.00 15.17 ? 159 LEU B C   1 
ATOM   1226 O  O   . LEU A 1 159 ? -20.633 -4.364  3.419   1.00 15.93 ? 159 LEU B O   1 
ATOM   1227 C  CB  . LEU A 1 159 ? -19.159 -7.103  3.605   1.00 14.43 ? 159 LEU B CB  1 
ATOM   1228 C  CG  . LEU A 1 159 ? -18.516 -8.161  4.512   1.00 17.04 ? 159 LEU B CG  1 
ATOM   1229 C  CD1 . LEU A 1 159 ? -17.340 -8.686  3.734   1.00 17.84 ? 159 LEU B CD1 1 
ATOM   1230 C  CD2 . LEU A 1 159 ? -18.175 -7.494  5.852   1.00 17.42 ? 159 LEU B CD2 1 
ATOM   1231 N  N   . GLN A 1 160 ? -22.108 -5.816  2.513   1.00 16.85 ? 160 GLN B N   1 
ATOM   1232 C  CA  . GLN A 1 160 ? -22.794 -4.797  1.716   1.00 17.16 ? 160 GLN B CA  1 
ATOM   1233 C  C   . GLN A 1 160 ? -23.371 -3.734  2.648   1.00 17.60 ? 160 GLN B C   1 
ATOM   1234 O  O   . GLN A 1 160 ? -23.360 -2.540  2.320   1.00 17.89 ? 160 GLN B O   1 
ATOM   1235 C  CB  . GLN A 1 160 ? -23.879 -5.442  0.838   1.00 19.64 ? 160 GLN B CB  1 
ATOM   1236 C  CG  . GLN A 1 160 ? -24.497 -4.406  -0.119  1.00 20.75 ? 160 GLN B CG  1 
ATOM   1237 C  CD  . GLN A 1 160 ? -23.768 -4.342  -1.465  1.00 24.17 ? 160 GLN B CD  1 
ATOM   1238 O  OE1 . GLN A 1 160 ? -22.702 -4.880  -1.665  1.00 20.75 ? 160 GLN B OE1 1 
ATOM   1239 N  NE2 . GLN A 1 160 ? -24.343 -3.575  -2.385  1.00 25.23 ? 160 GLN B NE2 1 
ATOM   1240 N  N   . LYS A 1 161 ? -23.855 -4.125  3.835   1.00 18.69 ? 161 LYS B N   1 
ATOM   1241 C  CA  . LYS A 1 161 ? -24.380 -3.136  4.761   1.00 18.80 ? 161 LYS B CA  1 
ATOM   1242 C  C   . LYS A 1 161 ? -23.331 -2.113  5.161   1.00 18.02 ? 161 LYS B C   1 
ATOM   1243 O  O   . LYS A 1 161 ? -23.675 -0.935  5.388   1.00 18.96 ? 161 LYS B O   1 
ATOM   1244 C  CB  . LYS A 1 161 ? -24.879 -3.870  6.023   1.00 20.32 ? 161 LYS B CB  1 
ATOM   1245 C  CG  . LYS A 1 161 ? -25.969 -4.909  5.750   1.00 27.22 ? 161 LYS B CG  1 
ATOM   1246 C  CD  . LYS A 1 161 ? -26.371 -5.740  6.983   1.00 33.49 ? 161 LYS B CD  1 
ATOM   1247 C  CE  . LYS A 1 161 ? -27.598 -6.584  6.678   1.00 37.43 ? 161 LYS B CE  1 
ATOM   1248 N  NZ  . LYS A 1 161 ? -28.416 -6.828  7.908   1.00 42.19 ? 161 LYS B NZ  1 
ATOM   1249 N  N   . ILE A 1 162 ? -22.073 -2.599  5.332   1.00 16.08 ? 162 ILE B N   1 
ATOM   1250 C  CA  . ILE A 1 162 ? -20.975 -1.707  5.651   1.00 15.47 ? 162 ILE B CA  1 
ATOM   1251 C  C   . ILE A 1 162 ? -20.654 -0.887  4.400   1.00 15.75 ? 162 ILE B C   1 
ATOM   1252 O  O   . ILE A 1 162 ? -20.497 0.317   4.507   1.00 15.88 ? 162 ILE B O   1 
ATOM   1253 C  CB  . ILE A 1 162 ? -19.724 -2.511  6.119   1.00 14.50 ? 162 ILE B CB  1 
ATOM   1254 C  CG1 . ILE A 1 162 ? -20.086 -3.130  7.511   1.00 15.31 ? 162 ILE B CG1 1 
ATOM   1255 C  CG2 . ILE A 1 162 ? -18.561 -1.570  6.243   1.00 15.50 ? 162 ILE B CG2 1 
ATOM   1256 C  CD1 . ILE A 1 162 ? -18.938 -4.021  8.031   1.00 16.89 ? 162 ILE B CD1 1 
ATOM   1257 N  N   . THR A 1 163 ? -20.507 -1.520  3.239   1.00 16.52 ? 163 THR B N   1 
ATOM   1258 C  CA  . THR A 1 163 ? -20.128 -0.686  2.094   1.00 16.87 ? 163 THR B CA  1 
ATOM   1259 C  C   . THR A 1 163 ? -21.198 0.366   1.755   1.00 17.40 ? 163 THR B C   1 
ATOM   1260 O  O   . THR A 1 163 ? -20.842 1.454   1.301   1.00 17.67 ? 163 THR B O   1 
ATOM   1261 C  CB  . THR A 1 163 ? -19.680 -1.504  0.861   1.00 20.29 ? 163 THR B CB  1 
ATOM   1262 O  OG1 . THR A 1 163 ? -20.727 -2.349  0.520   1.00 21.71 ? 163 THR B OG1 1 
ATOM   1263 C  CG2 . THR A 1 163 ? -18.491 -2.432  1.146   1.00 21.49 ? 163 THR B CG2 1 
ATOM   1264 N  N   . ASP A 1 164 ? -22.467 0.064   2.008   1.00 16.24 ? 164 ASP B N   1 
ATOM   1265 C  CA  . ASP A 1 164 ? -23.514 1.086   1.770   1.00 19.63 ? 164 ASP B CA  1 
ATOM   1266 C  C   . ASP A 1 164 ? -23.365 2.323   2.652   1.00 20.85 ? 164 ASP B C   1 
ATOM   1267 O  O   . ASP A 1 164 ? -23.903 3.379   2.291   1.00 25.82 ? 164 ASP B O   1 
ATOM   1268 C  CB  . ASP A 1 164 ? -24.873 0.504   1.972   1.00 20.75 ? 164 ASP B CB  1 
ATOM   1269 C  CG  . ASP A 1 164 ? -25.319 -0.367  0.793   1.00 23.06 ? 164 ASP B CG  1 
ATOM   1270 O  OD1 . ASP A 1 164 ? -24.693 -0.323  -0.258  1.00 27.04 ? 164 ASP B OD1 1 
ATOM   1271 O  OD2 . ASP A 1 164 ? -26.289 -1.105  1.007   1.00 27.05 ? 164 ASP B OD2 1 
ATOM   1272 N  N   . THR A 1 165 ? -22.604 2.261   3.744   1.00 19.29 ? 165 THR B N   1 
ATOM   1273 C  CA  . THR A 1 165 ? -22.452 3.450   4.604   1.00 18.44 ? 165 THR B CA  1 
ATOM   1274 C  C   . THR A 1 165 ? -21.263 4.258   4.234   1.00 17.41 ? 165 THR B C   1 
ATOM   1275 O  O   . THR A 1 165 ? -21.076 5.330   4.808   1.00 19.68 ? 165 THR B O   1 
ATOM   1276 C  CB  . THR A 1 165 ? -22.286 3.075   6.108   1.00 20.67 ? 165 THR B CB  1 
ATOM   1277 O  OG1 . THR A 1 165 ? -20.973 2.476   6.319   1.00 20.00 ? 165 THR B OG1 1 
ATOM   1278 C  CG2 . THR A 1 165 ? -23.440 2.104   6.582   1.00 24.47 ? 165 THR B CG2 1 
ATOM   1279 N  N   . LEU A 1 166 ? -20.350 3.750   3.391   1.00 15.05 ? 166 LEU B N   1 
ATOM   1280 C  CA  . LEU A 1 166 ? -19.005 4.364   3.329   1.00 14.75 ? 166 LEU B CA  1 
ATOM   1281 C  C   . LEU A 1 166 ? -19.089 5.782   2.755   1.00 17.21 ? 166 LEU B C   1 
ATOM   1282 O  O   . LEU A 1 166 ? -18.327 6.635   3.206   1.00 17.57 ? 166 LEU B O   1 
ATOM   1283 C  CB  . LEU A 1 166 ? -17.985 3.515   2.514   1.00 17.03 ? 166 LEU B CB  1 
ATOM   1284 C  CG  . LEU A 1 166 ? -17.743 2.161   3.147   1.00 17.08 ? 166 LEU B CG  1 
ATOM   1285 C  CD1 . LEU A 1 166 ? -16.846 1.333   2.283   1.00 18.30 ? 166 LEU B CD1 1 
ATOM   1286 C  CD2 . LEU A 1 166 ? -17.061 2.279   4.539   1.00 19.30 ? 166 LEU B CD2 1 
ATOM   1287 N  N   . ASP A 1 167 ? -20.032 6.007   1.845   1.00 19.73 ? 167 ASP B N   1 
ATOM   1288 C  CA  . ASP A 1 167 ? -20.187 7.382   1.280   1.00 22.09 ? 167 ASP B CA  1 
ATOM   1289 C  C   . ASP A 1 167 ? -20.447 8.390   2.373   1.00 21.82 ? 167 ASP B C   1 
ATOM   1290 O  O   . ASP A 1 167 ? -20.013 9.532   2.281   1.00 27.22 ? 167 ASP B O   1 
ATOM   1291 C  CB  . ASP A 1 167 ? -21.229 7.450   0.158   1.00 23.14 ? 167 ASP B CB  1 
ATOM   1292 C  CG  . ASP A 1 167 ? -20.715 6.837   -1.139  1.00 24.02 ? 167 ASP B CG  1 
ATOM   1293 O  OD1 . ASP A 1 167 ? -19.504 6.599   -1.291  1.00 28.35 ? 167 ASP B OD1 1 
ATOM   1294 O  OD2 . ASP A 1 167 ? -21.528 6.591   -2.040  1.00 31.86 ? 167 ASP B OD2 1 
ATOM   1295 N  N   A SER A 1 168 ? -21.134 8.006   3.434   0.50 19.86 ? 168 SER B N   1 
ATOM   1296 N  N   B SER A 1 168 ? -21.146 7.957   3.416   0.50 20.68 ? 168 SER B N   1 
ATOM   1297 C  CA  A SER A 1 168 ? -21.360 8.980   4.492   0.50 19.67 ? 168 SER B CA  1 
ATOM   1298 C  CA  B SER A 1 168 ? -21.450 8.807   4.557   0.50 21.10 ? 168 SER B CA  1 
ATOM   1299 C  C   A SER A 1 168 ? -20.199 9.230   5.453   0.50 19.48 ? 168 SER B C   1 
ATOM   1300 C  C   B SER A 1 168 ? -20.340 9.071   5.549   0.50 19.91 ? 168 SER B C   1 
ATOM   1301 O  O   A SER A 1 168 ? -20.152 10.239  6.190   0.50 20.26 ? 168 SER B O   1 
ATOM   1302 O  O   B SER A 1 168 ? -20.516 9.922   6.442   0.50 21.31 ? 168 SER B O   1 
ATOM   1303 C  CB  A SER A 1 168 ? -22.640 8.635   5.229   0.50 20.19 ? 168 SER B CB  1 
ATOM   1304 C  CB  B SER A 1 168 ? -22.639 8.223   5.298   0.50 22.89 ? 168 SER B CB  1 
ATOM   1305 O  OG  A SER A 1 168 ? -22.483 7.476   6.030   0.50 18.00 ? 168 SER B OG  1 
ATOM   1306 O  OG  B SER A 1 168 ? -23.761 8.248   4.460   0.50 23.53 ? 168 SER B OG  1 
ATOM   1307 N  N   . ILE A 1 169 ? -19.222 8.334   5.440   1.00 17.30 ? 169 ILE B N   1 
ATOM   1308 C  CA  . ILE A 1 169 ? -18.075 8.496   6.333   1.00 17.63 ? 169 ILE B CA  1 
ATOM   1309 C  C   . ILE A 1 169 ? -16.719 8.617   5.622   1.00 16.74 ? 169 ILE B C   1 
ATOM   1310 O  O   . ILE A 1 169 ? -15.677 8.228   6.121   1.00 15.99 ? 169 ILE B O   1 
ATOM   1311 C  CB  . ILE A 1 169 ? -18.031 7.391   7.422   1.00 16.01 ? 169 ILE B CB  1 
ATOM   1312 C  CG1 . ILE A 1 169 ? -17.885 5.980   6.792   1.00 17.57 ? 169 ILE B CG1 1 
ATOM   1313 C  CG2 . ILE A 1 169 ? -19.318 7.394   8.251   1.00 18.33 ? 169 ILE B CG2 1 
ATOM   1314 C  CD1 . ILE A 1 169 ? -17.502 4.921   7.853   1.00 19.82 ? 169 ILE B CD1 1 
ATOM   1315 N  N   A LYS A 1 170 ? -16.749 9.224   4.434   0.50 16.77 ? 170 LYS B N   1 
ATOM   1316 N  N   B LYS A 1 170 ? -16.752 9.235   4.436   0.50 16.91 ? 170 LYS B N   1 
ATOM   1317 C  CA  A LYS A 1 170 ? -15.543 9.312   3.648   0.50 18.24 ? 170 LYS B CA  1 
ATOM   1318 C  CA  B LYS A 1 170 ? -15.540 9.370   3.656   0.50 18.56 ? 170 LYS B CA  1 
ATOM   1319 C  C   A LYS A 1 170 ? -14.415 10.100  4.349   0.50 17.30 ? 170 LYS B C   1 
ATOM   1320 C  C   B LYS A 1 170 ? -14.415 10.094  4.375   0.50 17.62 ? 170 LYS B C   1 
ATOM   1321 O  O   A LYS A 1 170 ? -13.277 9.714   4.282   0.50 18.53 ? 170 LYS B O   1 
ATOM   1322 O  O   B LYS A 1 170 ? -13.286 9.676   4.330   0.50 19.23 ? 170 LYS B O   1 
ATOM   1323 C  CB  A LYS A 1 170 ? -15.880 9.922   2.273   0.50 19.98 ? 170 LYS B CB  1 
ATOM   1324 C  CB  B LYS A 1 170 ? -15.844 10.099  2.339   0.50 19.59 ? 170 LYS B CB  1 
ATOM   1325 C  CG  A LYS A 1 170 ? -14.714 10.546  1.551   0.50 20.85 ? 170 LYS B CG  1 
ATOM   1326 C  CG  B LYS A 1 170 ? -16.572 9.173   1.391   0.50 20.31 ? 170 LYS B CG  1 
ATOM   1327 C  CD  A LYS A 1 170 ? -15.159 11.102  0.205   0.50 23.20 ? 170 LYS B CD  1 
ATOM   1328 C  CD  B LYS A 1 170 ? -15.881 7.801   1.293   0.50 21.34 ? 170 LYS B CD  1 
ATOM   1329 C  CE  A LYS A 1 170 ? -14.013 11.788  -0.508  0.50 21.75 ? 170 LYS B CE  1 
ATOM   1330 C  CE  B LYS A 1 170 ? -16.550 6.903   0.260   0.50 20.47 ? 170 LYS B CE  1 
ATOM   1331 N  NZ  A LYS A 1 170 ? -14.322 11.817  -1.967  0.50 27.39 ? 170 LYS B NZ  1 
ATOM   1332 N  NZ  B LYS A 1 170 ? -16.788 7.739   -0.985  0.50 22.01 ? 170 LYS B NZ  1 
ATOM   1333 N  N   . GLU A 1 171 ? -14.749 11.198  5.044   1.00 20.13 ? 171 GLU B N   1 
ATOM   1334 C  CA  . GLU A 1 171 ? -13.754 11.987  5.702   1.00 21.43 ? 171 GLU B CA  1 
ATOM   1335 C  C   . GLU A 1 171 ? -13.363 11.474  7.041   1.00 20.15 ? 171 GLU B C   1 
ATOM   1336 O  O   . GLU A 1 171 ? -14.253 10.959  7.772   1.00 20.40 ? 171 GLU B O   1 
ATOM   1337 C  CB  . GLU A 1 171 ? -14.254 13.447  5.864   1.00 24.94 ? 171 GLU B CB  1 
ATOM   1338 C  CG  . GLU A 1 171 ? -14.270 14.201  4.545   1.00 30.26 ? 171 GLU B CG  1 
ATOM   1339 C  CD  . GLU A 1 171 ? -15.515 13.921  3.737   1.00 31.57 ? 171 GLU B CD  1 
ATOM   1340 O  OE1 . GLU A 1 171 ? -15.452 14.153  2.486   1.00 38.14 ? 171 GLU B OE1 1 
ATOM   1341 O  OE2 . GLU A 1 171 ? -16.538 13.433  4.294   1.00 35.19 ? 171 GLU B OE2 1 
ATOM   1342 N  N   . LYS A 1 172 ? -12.088 11.588  7.363   1.00 21.36 ? 172 LYS B N   1 
ATOM   1343 C  CA  . LYS A 1 172 ? -11.606 11.225  8.668   1.00 21.48 ? 172 LYS B CA  1 
ATOM   1344 C  C   . LYS A 1 172 ? -12.436 11.898  9.781   1.00 23.99 ? 172 LYS B C   1 
ATOM   1345 O  O   . LYS A 1 172 ? -12.783 13.121  9.734   1.00 24.29 ? 172 LYS B O   1 
ATOM   1346 C  CB  . LYS A 1 172 ? -10.122 11.549  8.843   1.00 24.86 ? 172 LYS B CB  1 
ATOM   1347 C  CG  . LYS A 1 172 ? -9.587  11.324  10.242  1.00 22.30 ? 172 LYS B CG  1 
ATOM   1348 C  CD  . LYS A 1 172 ? -8.067  11.494  10.248  1.00 30.22 ? 172 LYS B CD  1 
ATOM   1349 C  CE  . LYS A 1 172 ? -7.570  11.451  11.691  1.00 26.61 ? 172 LYS B CE  1 
ATOM   1350 N  NZ  . LYS A 1 172 ? -6.112  11.293  11.823  1.00 32.87 ? 172 LYS B NZ  1 
ATOM   1351 N  N   . GLY A 1 173 ? -12.823 11.075  10.741  1.00 19.59 ? 173 GLY B N   1 
ATOM   1352 C  CA  . GLY A 1 173 ? -13.683 11.516  11.904  1.00 18.38 ? 173 GLY B CA  1 
ATOM   1353 C  C   . GLY A 1 173 ? -15.190 11.412  11.715  1.00 18.86 ? 173 GLY B C   1 
ATOM   1354 O  O   . GLY A 1 173 ? -15.958 11.562  12.675  1.00 23.17 ? 173 GLY B O   1 
ATOM   1355 N  N   . LYS A 1 174 ? -15.690 11.190  10.513  1.00 17.57 ? 174 LYS B N   1 
ATOM   1356 C  CA  . LYS A 1 174 ? -17.140 11.108  10.293  1.00 19.02 ? 174 LYS B CA  1 
ATOM   1357 C  C   . LYS A 1 174 ? -17.671 9.809   10.924  1.00 18.50 ? 174 LYS B C   1 
ATOM   1358 O  O   . LYS A 1 174 ? -16.945 8.781   10.944  1.00 18.49 ? 174 LYS B O   1 
ATOM   1359 C  CB  . LYS A 1 174 ? -17.467 11.127  8.794   1.00 21.32 ? 174 LYS B CB  1 
ATOM   1360 C  CG  . LYS A 1 174 ? -17.206 12.495  8.098   1.00 28.46 ? 174 LYS B CG  1 
ATOM   1361 C  CD  . LYS A 1 174 ? -18.168 13.571  8.503   1.00 33.93 ? 174 LYS B CD  1 
ATOM   1362 C  CE  . LYS A 1 174 ? -18.197 14.641  7.406   1.00 39.36 ? 174 LYS B CE  1 
ATOM   1363 N  NZ  . LYS A 1 174 ? -18.624 14.071  6.079   1.00 46.84 ? 174 LYS B NZ  1 
ATOM   1364 N  N   . GLN A 1 175 ? -18.908 9.874   11.372  1.00 18.65 ? 175 GLN B N   1 
ATOM   1365 C  CA  . GLN A 1 175 ? -19.661 8.760   11.975  1.00 20.43 ? 175 GLN B CA  1 
ATOM   1366 C  C   . GLN A 1 175 ? -21.053 8.705   11.507  1.00 22.19 ? 175 GLN B C   1 
ATOM   1367 O  O   . GLN A 1 175 ? -21.690 9.713   11.074  1.00 21.98 ? 175 GLN B O   1 
ATOM   1368 C  CB  . GLN A 1 175 ? -19.662 8.754   13.518  1.00 21.13 ? 175 GLN B CB  1 
ATOM   1369 C  CG  . GLN A 1 175 ? -20.613 9.720   14.213  1.00 27.45 ? 175 GLN B CG  1 
ATOM   1370 C  CD  . GLN A 1 175 ? -20.434 9.639   15.744  1.00 32.92 ? 175 GLN B CD  1 
ATOM   1371 O  OE1 . GLN A 1 175 ? -21.148 8.881   16.415  1.00 31.79 ? 175 GLN B OE1 1 
ATOM   1372 N  NE2 . GLN A 1 175 ? -19.475 10.428  16.296  1.00 32.38 ? 175 GLN B NE2 1 
ATOM   1373 N  N   . THR A 1 176 ? -21.584 7.502   11.521  1.00 18.37 ? 176 THR B N   1 
ATOM   1374 C  CA  . THR A 1 176 ? -22.966 7.406   11.304  1.00 17.61 ? 176 THR B CA  1 
ATOM   1375 C  C   . THR A 1 176 ? -23.568 6.197   12.023  1.00 18.91 ? 176 THR B C   1 
ATOM   1376 O  O   . THR A 1 176 ? -22.821 5.294   12.435  1.00 18.44 ? 176 THR B O   1 
ATOM   1377 C  CB  . THR A 1 176 ? -23.329 7.404   9.787   1.00 21.30 ? 176 THR B CB  1 
ATOM   1378 O  OG1 . THR A 1 176 ? -24.721 7.666   9.595   1.00 23.28 ? 176 THR B OG1 1 
ATOM   1379 C  CG2 . THR A 1 176 ? -22.981 6.115   9.208   1.00 22.11 ? 176 THR B CG2 1 
ATOM   1380 N  N   A ARG A 1 177 ? -24.871 6.172   12.196  0.50 16.66 ? 177 ARG B N   1 
ATOM   1381 N  N   B ARG A 1 177 ? -24.894 6.192   12.173  0.50 18.22 ? 177 ARG B N   1 
ATOM   1382 C  CA  A ARG A 1 177 ? -25.426 5.048   12.915  0.50 15.32 ? 177 ARG B CA  1 
ATOM   1383 C  CA  B ARG A 1 177 ? -25.637 5.101   12.855  0.50 17.85 ? 177 ARG B CA  1 
ATOM   1384 C  C   A ARG A 1 177 ? -25.368 3.802   12.099  0.50 15.20 ? 177 ARG B C   1 
ATOM   1385 C  C   B ARG A 1 177 ? -25.587 3.794   12.110  0.50 17.60 ? 177 ARG B C   1 
ATOM   1386 O  O   A ARG A 1 177 ? -25.404 3.848   10.863  0.50 15.93 ? 177 ARG B O   1 
ATOM   1387 O  O   B ARG A 1 177 ? -25.837 3.797   10.887  0.50 17.86 ? 177 ARG B O   1 
ATOM   1388 C  CB  A ARG A 1 177 ? -26.822 5.351   13.394  0.50 15.65 ? 177 ARG B CB  1 
ATOM   1389 C  CB  B ARG A 1 177 ? -27.105 5.542   13.053  0.50 19.49 ? 177 ARG B CB  1 
ATOM   1390 C  CG  A ARG A 1 177 ? -26.682 6.543   14.307  0.50 15.78 ? 177 ARG B CG  1 
ATOM   1391 C  CG  B ARG A 1 177 ? -28.029 4.454   13.511  0.50 22.21 ? 177 ARG B CG  1 
ATOM   1392 C  CD  A ARG A 1 177 ? -28.011 6.984   14.792  0.50 17.04 ? 177 ARG B CD  1 
ATOM   1393 C  CD  B ARG A 1 177 ? -29.507 4.860   13.362  0.50 22.10 ? 177 ARG B CD  1 
ATOM   1394 N  NE  A ARG A 1 177 ? -28.805 5.883   15.329  0.50 21.90 ? 177 ARG B NE  1 
ATOM   1395 N  NE  B ARG A 1 177 ? -29.829 6.058   14.183  0.50 21.19 ? 177 ARG B NE  1 
ATOM   1396 C  CZ  A ARG A 1 177 ? -29.944 6.043   15.997  0.50 19.90 ? 177 ARG B CZ  1 
ATOM   1397 C  CZ  B ARG A 1 177 ? -30.344 6.072   15.429  0.50 21.32 ? 177 ARG B CZ  1 
ATOM   1398 N  NH1 A ARG A 1 177 ? -30.423 7.260   16.211  0.50 18.23 ? 177 ARG B NH1 1 
ATOM   1399 N  NH1 B ARG A 1 177 ? -30.706 4.972   16.042  0.50 23.89 ? 177 ARG B NH1 1 
ATOM   1400 N  NH2 A ARG A 1 177 ? -30.604 4.986   16.451  0.50 23.18 ? 177 ARG B NH2 1 
ATOM   1401 N  NH2 B ARG A 1 177 ? -30.540 7.221   16.035  0.50 21.00 ? 177 ARG B NH2 1 
ATOM   1402 N  N   . PHE A 1 178 ? -25.272 2.694   12.816  1.00 16.06 ? 178 PHE B N   1 
ATOM   1403 C  CA  . PHE A 1 178 ? -25.135 1.360   12.148  1.00 17.35 ? 178 PHE B CA  1 
ATOM   1404 C  C   . PHE A 1 178 ? -25.459 0.294   13.142  1.00 16.79 ? 178 PHE B C   1 
ATOM   1405 O  O   . PHE A 1 178 ? -24.745 0.103   14.176  1.00 18.21 ? 178 PHE B O   1 
ATOM   1406 C  CB  . PHE A 1 178 ? -23.693 1.222   11.689  1.00 20.55 ? 178 PHE B CB  1 
ATOM   1407 C  CG  . PHE A 1 178 ? -23.420 -0.052  10.943  1.00 21.54 ? 178 PHE B CG  1 
ATOM   1408 C  CD1 . PHE A 1 178 ? -23.693 -0.142  9.593   1.00 20.78 ? 178 PHE B CD1 1 
ATOM   1409 C  CD2 . PHE A 1 178 ? -22.920 -1.156  11.611  1.00 22.04 ? 178 PHE B CD2 1 
ATOM   1410 C  CE1 . PHE A 1 178 ? -23.432 -1.308  8.876   1.00 24.12 ? 178 PHE B CE1 1 
ATOM   1411 C  CE2 . PHE A 1 178 ? -22.632 -2.317  10.903  1.00 22.95 ? 178 PHE B CE2 1 
ATOM   1412 C  CZ  . PHE A 1 178 ? -22.892 -2.394  9.537   1.00 23.87 ? 178 PHE B CZ  1 
ATOM   1413 N  N   . THR A 1 179 ? -26.507 -0.431  12.810  1.00 17.48 ? 179 THR B N   1 
ATOM   1414 C  CA  . THR A 1 179 ? -26.923 -1.473  13.790  1.00 19.07 ? 179 THR B CA  1 
ATOM   1415 C  C   . THR A 1 179 ? -27.477 -2.664  13.026  1.00 20.99 ? 179 THR B C   1 
ATOM   1416 O  O   . THR A 1 179 ? -27.406 -2.684  11.814  1.00 21.98 ? 179 THR B O   1 
ATOM   1417 C  CB  . THR A 1 179 ? -27.855 -0.943  14.903  1.00 22.05 ? 179 THR B CB  1 
ATOM   1418 O  OG1 . THR A 1 179 ? -28.018 -1.965  15.942  1.00 20.54 ? 179 THR B OG1 1 
ATOM   1419 C  CG2 . THR A 1 179 ? -29.220 -0.568  14.329  1.00 20.94 ? 179 THR B CG2 1 
ATOM   1420 N  N   . ASN A 1 180 ? -27.897 -3.687  13.770  1.00 22.61 ? 180 ASN B N   1 
ATOM   1421 C  CA  . ASN A 1 180 ? -28.459 -4.931  13.224  1.00 21.79 ? 180 ASN B CA  1 
ATOM   1422 C  C   . ASN A 1 180 ? -27.429 -5.586  12.315  1.00 20.33 ? 180 ASN B C   1 
ATOM   1423 O  O   . ASN A 1 180 ? -27.692 -5.806  11.143  1.00 23.11 ? 180 ASN B O   1 
ATOM   1424 C  CB  . ASN A 1 180 ? -29.727 -4.693  12.364  1.00 25.01 ? 180 ASN B CB  1 
ATOM   1425 C  CG  . ASN A 1 180 ? -30.457 -6.006  12.090  1.00 32.44 ? 180 ASN B CG  1 
ATOM   1426 O  OD1 . ASN A 1 180 ? -30.489 -6.895  12.979  1.00 34.07 ? 180 ASN B OD1 1 
ATOM   1427 N  ND2 . ASN A 1 180 ? -30.978 -6.166  10.886  1.00 37.79 ? 180 ASN B ND2 1 
ATOM   1428 N  N   . PHE A 1 181 ? -26.249 -5.843  12.854  1.00 17.17 ? 181 PHE B N   1 
ATOM   1429 C  CA  . PHE A 1 181 ? -25.131 -6.391  12.072  1.00 17.78 ? 181 PHE B CA  1 
ATOM   1430 C  C   . PHE A 1 181 ? -24.873 -7.799  12.623  1.00 17.22 ? 181 PHE B C   1 
ATOM   1431 O  O   . PHE A 1 181 ? -24.508 -7.932  13.783  1.00 17.67 ? 181 PHE B O   1 
ATOM   1432 C  CB  . PHE A 1 181 ? -23.935 -5.481  12.289  1.00 18.81 ? 181 PHE B CB  1 
ATOM   1433 C  CG  . PHE A 1 181 ? -22.676 -5.974  11.636  1.00 19.57 ? 181 PHE B CG  1 
ATOM   1434 C  CD1 . PHE A 1 181 ? -22.611 -6.251  10.246  1.00 21.54 ? 181 PHE B CD1 1 
ATOM   1435 C  CD2 . PHE A 1 181 ? -21.532 -6.022  12.394  1.00 23.53 ? 181 PHE B CD2 1 
ATOM   1436 C  CE1 . PHE A 1 181 ? -21.374 -6.702  9.679   1.00 20.79 ? 181 PHE B CE1 1 
ATOM   1437 C  CE2 . PHE A 1 181 ? -20.316 -6.394  11.847  1.00 24.16 ? 181 PHE B CE2 1 
ATOM   1438 C  CZ  . PHE A 1 181 ? -20.241 -6.789  10.486  1.00 21.67 ? 181 PHE B CZ  1 
ATOM   1439 N  N   . ASP A 1 182 ? -25.106 -8.821  11.799  1.00 16.96 ? 182 ASP B N   1 
ATOM   1440 C  CA  . ASP A 1 182 ? -25.146 -10.172 12.367  1.00 16.87 ? 182 ASP B CA  1 
ATOM   1441 C  C   . ASP A 1 182 ? -23.746 -10.760 12.144  1.00 15.77 ? 182 ASP B C   1 
ATOM   1442 O  O   . ASP A 1 182 ? -23.478 -11.466 11.154  1.00 18.52 ? 182 ASP B O   1 
ATOM   1443 C  CB  . ASP A 1 182 ? -26.199 -10.989 11.612  1.00 15.59 ? 182 ASP B CB  1 
ATOM   1444 C  CG  . ASP A 1 182 ? -26.394 -12.397 12.187  1.00 19.06 ? 182 ASP B CG  1 
ATOM   1445 O  OD1 . ASP A 1 182 ? -25.663 -12.822 13.064  1.00 17.33 ? 182 ASP B OD1 1 
ATOM   1446 O  OD2 . ASP A 1 182 ? -27.370 -12.991 11.773  1.00 19.45 ? 182 ASP B OD2 1 
ATOM   1447 N  N   . LEU A 1 183 ? -22.845 -10.360 13.050  1.00 15.29 ? 183 LEU B N   1 
ATOM   1448 C  CA  . LEU A 1 183 ? -21.449 -10.725 13.010  1.00 13.76 ? 183 LEU B CA  1 
ATOM   1449 C  C   . LEU A 1 183 ? -21.297 -12.225 13.128  1.00 16.33 ? 183 LEU B C   1 
ATOM   1450 O  O   . LEU A 1 183 ? -20.399 -12.769 12.495  1.00 14.59 ? 183 LEU B O   1 
ATOM   1451 C  CB  . LEU A 1 183 ? -20.730 -9.981  14.129  1.00 13.70 ? 183 LEU B CB  1 
ATOM   1452 C  CG  . LEU A 1 183 ? -19.236 -10.153 14.218  1.00 13.10 ? 183 LEU B CG  1 
ATOM   1453 C  CD1 . LEU A 1 183 ? -18.467 -9.701  12.973  1.00 14.98 ? 183 LEU B CD1 1 
ATOM   1454 C  CD2 . LEU A 1 183 ? -18.762 -9.377  15.472  1.00 12.82 ? 183 LEU B CD2 1 
ATOM   1455 N  N   . LEU A 1 184 ? -22.191 -12.882 13.906  1.00 15.95 ? 184 LEU B N   1 
ATOM   1456 C  CA  . LEU A 1 184 ? -22.043 -14.318 14.056  1.00 15.32 ? 184 LEU B CA  1 
ATOM   1457 C  C   . LEU A 1 184 ? -22.230 -14.970 12.713  1.00 15.39 ? 184 LEU B C   1 
ATOM   1458 O  O   . LEU A 1 184 ? -21.461 -15.909 12.376  1.00 14.76 ? 184 LEU B O   1 
ATOM   1459 C  CB  . LEU A 1 184 ? -23.033 -14.878 15.124  1.00 13.70 ? 184 LEU B CB  1 
ATOM   1460 C  CG  . LEU A 1 184 ? -22.839 -16.353 15.470  1.00 14.40 ? 184 LEU B CG  1 
ATOM   1461 C  CD1 . LEU A 1 184 ? -21.559 -16.584 16.199  1.00 17.02 ? 184 LEU B CD1 1 
ATOM   1462 C  CD2 . LEU A 1 184 ? -24.025 -16.790 16.333  1.00 15.88 ? 184 LEU B CD2 1 
ATOM   1463 N  N   A SER A 1 185 ? -23.202 -14.494 11.930  0.50 14.61 ? 185 SER B N   1 
ATOM   1464 N  N   B SER A 1 185 ? -23.206 -14.548 11.918  0.50 15.03 ? 185 SER B N   1 
ATOM   1465 C  CA  A SER A 1 185 ? -23.476 -15.110 10.620  0.50 14.99 ? 185 SER B CA  1 
ATOM   1466 C  CA  B SER A 1 185 ? -23.384 -15.233 10.629  0.50 15.18 ? 185 SER B CA  1 
ATOM   1467 C  C   A SER A 1 185 ? -22.440 -14.789 9.579   0.50 14.73 ? 185 SER B C   1 
ATOM   1468 C  C   B SER A 1 185 ? -22.278 -14.902 9.657   0.50 14.67 ? 185 SER B C   1 
ATOM   1469 O  O   A SER A 1 185 ? -22.492 -15.399 8.504   0.50 16.11 ? 185 SER B O   1 
ATOM   1470 O  O   B SER A 1 185 ? -22.089 -15.615 8.703   0.50 16.62 ? 185 SER B O   1 
ATOM   1471 C  CB  A SER A 1 185 ? -24.841 -14.634 10.053  0.50 15.61 ? 185 SER B CB  1 
ATOM   1472 C  CB  B SER A 1 185 ? -24.718 -14.821 9.970   0.50 17.07 ? 185 SER B CB  1 
ATOM   1473 O  OG  A SER A 1 185 ? -24.795 -13.311 9.516   0.50 16.58 ? 185 SER B OG  1 
ATOM   1474 O  OG  B SER A 1 185 ? -25.803 -15.180 10.804  0.50 19.74 ? 185 SER B OG  1 
ATOM   1475 N  N   . LEU A 1 186 ? -21.604 -13.770 9.842   1.00 13.46 ? 186 LEU B N   1 
ATOM   1476 C  CA  . LEU A 1 186 ? -20.531 -13.369 8.922   1.00 13.88 ? 186 LEU B CA  1 
ATOM   1477 C  C   . LEU A 1 186 ? -19.365 -14.318 8.976   1.00 14.95 ? 186 LEU B C   1 
ATOM   1478 O  O   . LEU A 1 186 ? -18.642 -14.437 8.013   1.00 13.09 ? 186 LEU B O   1 
ATOM   1479 C  CB  . LEU A 1 186 ? -20.118 -11.890 9.274   1.00 13.92 ? 186 LEU B CB  1 
ATOM   1480 C  CG  . LEU A 1 186 ? -18.986 -11.303 8.470   1.00 14.93 ? 186 LEU B CG  1 
ATOM   1481 C  CD1 . LEU A 1 186 ? -19.534 -10.985 7.066   1.00 17.66 ? 186 LEU B CD1 1 
ATOM   1482 C  CD2 . LEU A 1 186 ? -18.500 -9.968  9.078   1.00 16.04 ? 186 LEU B CD2 1 
ATOM   1483 N  N   . LEU A 1 187 ? -19.172 -15.029 10.117  1.00 12.81 ? 187 LEU B N   1 
ATOM   1484 C  CA  . LEU A 1 187 ? -18.023 -15.835 10.266  1.00 11.42 ? 187 LEU B CA  1 
ATOM   1485 C  C   . LEU A 1 187 ? -18.108 -17.091 9.344   1.00 11.65 ? 187 LEU B C   1 
ATOM   1486 O  O   . LEU A 1 187 ? -19.174 -17.493 8.923   1.00 12.38 ? 187 LEU B O   1 
ATOM   1487 C  CB  . LEU A 1 187 ? -17.949 -16.295 11.784  1.00 12.00 ? 187 LEU B CB  1 
ATOM   1488 C  CG  . LEU A 1 187 ? -17.815 -15.147 12.781  1.00 12.99 ? 187 LEU B CG  1 
ATOM   1489 C  CD1 . LEU A 1 187 ? -17.756 -15.812 14.176  1.00 13.73 ? 187 LEU B CD1 1 
ATOM   1490 C  CD2 . LEU A 1 187 ? -16.560 -14.298 12.545  1.00 14.54 ? 187 LEU B CD2 1 
ATOM   1491 N  N   . PRO A 1 188 ? -16.956 -17.632 8.953   1.00 10.85 ? 188 PRO B N   1 
ATOM   1492 C  CA  . PRO A 1 188 ? -16.956 -18.771 7.993   1.00 11.88 ? 188 PRO B CA  1 
ATOM   1493 C  C   . PRO A 1 188 ? -17.492 -20.021 8.615   1.00 12.77 ? 188 PRO B C   1 
ATOM   1494 O  O   . PRO A 1 188 ? -17.681 -20.090 9.806   1.00 14.03 ? 188 PRO B O   1 
ATOM   1495 C  CB  . PRO A 1 188 ? -15.475 -18.996 7.722   1.00 11.63 ? 188 PRO B CB  1 
ATOM   1496 C  CG  . PRO A 1 188 ? -14.737 -18.444 8.955   1.00 11.89 ? 188 PRO B CG  1 
ATOM   1497 C  CD  . PRO A 1 188 ? -15.587 -17.272 9.383   1.00 10.81 ? 188 PRO B CD  1 
ATOM   1498 N  N   . PRO A 1 189 ? -17.830 -21.014 7.822   1.00 12.49 ? 189 PRO B N   1 
ATOM   1499 C  CA  . PRO A 1 189 ? -18.385 -22.233 8.367   1.00 13.36 ? 189 PRO B CA  1 
ATOM   1500 C  C   . PRO A 1 189 ? -17.515 -22.916 9.415   1.00 14.25 ? 189 PRO B C   1 
ATOM   1501 O  O   . PRO A 1 189 ? -18.065 -23.361 10.499  1.00 15.78 ? 189 PRO B O   1 
ATOM   1502 C  CB  . PRO A 1 189 ? -18.438 -23.145 7.100   1.00 14.18 ? 189 PRO B CB  1 
ATOM   1503 C  CG  . PRO A 1 189 ? -18.698 -22.142 5.987   1.00 13.87 ? 189 PRO B CG  1 
ATOM   1504 C  CD  . PRO A 1 189 ? -17.903 -20.934 6.329   1.00 13.95 ? 189 PRO B CD  1 
ATOM   1505 N  N   . SER A 1 190 ? -16.186 -22.993 9.185   1.00 12.95 ? 190 SER B N   1 
ATOM   1506 C  CA  . SER A 1 190 ? -15.297 -23.627 10.167  1.00 12.65 ? 190 SER B CA  1 
ATOM   1507 C  C   . SER A 1 190 ? -14.665 -22.605 11.042  1.00 13.80 ? 190 SER B C   1 
ATOM   1508 O  O   . SER A 1 190 ? -14.261 -21.524 10.573  1.00 12.53 ? 190 SER B O   1 
ATOM   1509 C  CB  . SER A 1 190 ? -14.171 -24.386 9.428   1.00 15.24 ? 190 SER B CB  1 
ATOM   1510 O  OG  . SER A 1 190 ? -13.242 -24.878 10.390  1.00 16.21 ? 190 SER B OG  1 
ATOM   1511 N  N   . TRP A 1 191 ? -14.625 -22.871 12.345  1.00 12.95 ? 191 TRP B N   1 
ATOM   1512 C  CA  . TRP A 1 191 ? -14.000 -21.970 13.286  1.00 13.73 ? 191 TRP B CA  1 
ATOM   1513 C  C   . TRP A 1 191 ? -12.676 -22.541 13.805  1.00 14.71 ? 191 TRP B C   1 
ATOM   1514 O  O   . TRP A 1 191 ? -12.212 -22.135 14.925  1.00 15.57 ? 191 TRP B O   1 
ATOM   1515 C  CB  . TRP A 1 191 ? -14.899 -21.610 14.458  1.00 13.39 ? 191 TRP B CB  1 
ATOM   1516 C  CG  . TRP A 1 191 ? -16.114 -20.851 14.028  1.00 13.21 ? 191 TRP B CG  1 
ATOM   1517 C  CD1 . TRP A 1 191 ? -16.354 -20.232 12.805  1.00 11.85 ? 191 TRP B CD1 1 
ATOM   1518 C  CD2 . TRP A 1 191 ? -17.313 -20.628 14.820  1.00 13.33 ? 191 TRP B CD2 1 
ATOM   1519 N  NE1 . TRP A 1 191 ? -17.595 -19.647 12.797  1.00 12.71 ? 191 TRP B NE1 1 
ATOM   1520 C  CE2 . TRP A 1 191 ? -18.221 -19.853 13.982  1.00 13.12 ? 191 TRP B CE2 1 
ATOM   1521 C  CE3 . TRP A 1 191 ? -17.708 -20.981 16.099  1.00 13.39 ? 191 TRP B CE3 1 
ATOM   1522 C  CZ2 . TRP A 1 191 ? -19.469 -19.457 14.429  1.00 16.04 ? 191 TRP B CZ2 1 
ATOM   1523 C  CZ3 . TRP A 1 191 ? -18.965 -20.580 16.541  1.00 15.86 ? 191 TRP B CZ3 1 
ATOM   1524 C  CH2 . TRP A 1 191 ? -19.826 -19.838 15.726  1.00 16.24 ? 191 TRP B CH2 1 
ATOM   1525 N  N   . ASP A 1 192 ? -12.054 -23.428 13.049  1.00 13.09 ? 192 ASP B N   1 
ATOM   1526 C  CA  . ASP A 1 192 ? -10.726 -23.908 13.399  1.00 15.03 ? 192 ASP B CA  1 
ATOM   1527 C  C   . ASP A 1 192 ? -9.745  -22.707 13.267  1.00 13.16 ? 192 ASP B C   1 
ATOM   1528 O  O   . ASP A 1 192 ? -9.850  -21.819 12.395  1.00 11.86 ? 192 ASP B O   1 
ATOM   1529 C  CB  . ASP A 1 192 ? -10.321 -25.086 12.545  1.00 18.26 ? 192 ASP B CB  1 
ATOM   1530 C  CG  . ASP A 1 192 ? -11.174 -26.289 12.815  1.00 17.74 ? 192 ASP B CG  1 
ATOM   1531 O  OD1 . ASP A 1 192 ? -11.851 -26.312 13.870  1.00 19.60 ? 192 ASP B OD1 1 
ATOM   1532 O  OD2 . ASP A 1 192 ? -11.168 -27.209 11.980  1.00 21.48 ? 192 ASP B OD2 1 
ATOM   1533 N  N   . TYR A 1 193 ? -8.835  -22.642 14.211  1.00 12.22 ? 193 TYR B N   1 
ATOM   1534 C  CA  . TYR A 1 193 ? -8.015  -21.440 14.350  1.00 11.73 ? 193 TYR B CA  1 
ATOM   1535 C  C   . TYR A 1 193 ? -6.591  -21.692 14.759  1.00 12.55 ? 193 TYR B C   1 
ATOM   1536 O  O   . TYR A 1 193 ? -6.294  -22.782 15.308  1.00 12.43 ? 193 TYR B O   1 
ATOM   1537 C  CB  . TYR A 1 193 ? -8.658  -20.424 15.390  1.00 12.07 ? 193 TYR B CB  1 
ATOM   1538 C  CG  . TYR A 1 193 ? -8.728  -21.043 16.839  1.00 12.19 ? 193 TYR B CG  1 
ATOM   1539 C  CD1 . TYR A 1 193 ? -7.635  -20.945 17.688  1.00 13.95 ? 193 TYR B CD1 1 
ATOM   1540 C  CD2 . TYR A 1 193 ? -9.867  -21.676 17.264  1.00 11.84 ? 193 TYR B CD2 1 
ATOM   1541 C  CE1 . TYR A 1 193 ? -7.673  -21.521 18.977  1.00 12.95 ? 193 TYR B CE1 1 
ATOM   1542 C  CE2 . TYR A 1 193 ? -9.895  -22.286 18.549  1.00 11.12 ? 193 TYR B CE2 1 
ATOM   1543 C  CZ  . TYR A 1 193 ? -8.813  -22.141 19.336  1.00 12.77 ? 193 TYR B CZ  1 
ATOM   1544 O  OH  . TYR A 1 193 ? -8.856  -22.753 20.598  1.00 13.63 ? 193 TYR B OH  1 
ATOM   1545 N  N   . TRP A 1 194 ? -5.733  -20.720 14.550  1.00 11.78 ? 194 TRP B N   1 
ATOM   1546 C  CA  . TRP A 1 194 ? -4.408  -20.657 15.157  1.00 12.32 ? 194 TRP B CA  1 
ATOM   1547 C  C   . TRP A 1 194 ? -4.445  -19.613 16.225  1.00 12.29 ? 194 TRP B C   1 
ATOM   1548 O  O   . TRP A 1 194 ? -5.205  -18.597 16.158  1.00 12.12 ? 194 TRP B O   1 
ATOM   1549 C  CB  . TRP A 1 194 ? -3.328  -20.301 14.156  1.00 12.70 ? 194 TRP B CB  1 
ATOM   1550 C  CG  . TRP A 1 194 ? -3.241  -21.248 12.978  1.00 11.99 ? 194 TRP B CG  1 
ATOM   1551 C  CD1 . TRP A 1 194 ? -2.746  -22.550 12.977  1.00 13.79 ? 194 TRP B CD1 1 
ATOM   1552 C  CD2 . TRP A 1 194 ? -3.770  -21.036 11.633  1.00 12.32 ? 194 TRP B CD2 1 
ATOM   1553 N  NE1 . TRP A 1 194 ? -2.835  -23.090 11.731  1.00 14.27 ? 194 TRP B NE1 1 
ATOM   1554 C  CE2 . TRP A 1 194 ? -3.453  -22.198 10.878  1.00 13.25 ? 194 TRP B CE2 1 
ATOM   1555 C  CE3 . TRP A 1 194 ? -4.354  -19.958 11.009  1.00 12.83 ? 194 TRP B CE3 1 
ATOM   1556 C  CZ2 . TRP A 1 194 ? -3.732  -22.313 9.520   1.00 14.79 ? 194 TRP B CZ2 1 
ATOM   1557 C  CZ3 . TRP A 1 194 ? -4.652  -20.061 9.648   1.00 12.34 ? 194 TRP B CZ3 1 
ATOM   1558 C  CH2 . TRP A 1 194 ? -4.352  -21.206 8.924   1.00 13.65 ? 194 TRP B CH2 1 
ATOM   1559 N  N   . THR A 1 195 ? -3.556  -19.744 17.223  1.00 12.06 ? 195 THR B N   1 
ATOM   1560 C  CA  . THR A 1 195 ? -3.483  -18.759 18.275  1.00 11.58 ? 195 THR B CA  1 
ATOM   1561 C  C   . THR A 1 195 ? -2.059  -18.511 18.758  1.00 11.57 ? 195 THR B C   1 
ATOM   1562 O  O   . THR A 1 195 ? -1.279  -19.456 18.808  1.00 12.38 ? 195 THR B O   1 
ATOM   1563 C  CB  . THR A 1 195 ? -4.484  -19.112 19.442  1.00 12.23 ? 195 THR B CB  1 
ATOM   1564 O  OG1 . THR A 1 195 ? -4.380  -18.119 20.456  1.00 12.42 ? 195 THR B OG1 1 
ATOM   1565 C  CG2 . THR A 1 195 ? -4.035  -20.543 20.045  1.00 12.67 ? 195 THR B CG2 1 
ATOM   1566 N  N   . TYR A 1 196 ? -1.778  -17.270 19.090  1.00 11.64 ? 196 TYR B N   1 
ATOM   1567 C  CA  . TYR A 1 196 ? -0.464  -16.888 19.665  1.00 12.03 ? 196 TYR B CA  1 
ATOM   1568 C  C   . TYR A 1 196 ? -0.597  -15.603 20.428  1.00 13.11 ? 196 TYR B C   1 
ATOM   1569 O  O   . TYR A 1 196 ? -1.542  -14.864 20.198  1.00 13.31 ? 196 TYR B O   1 
ATOM   1570 C  CB  . TYR A 1 196 ? 0.599   -16.781 18.522  1.00 12.77 ? 196 TYR B CB  1 
ATOM   1571 C  CG  . TYR A 1 196 ? 0.396   -15.559 17.673  1.00 12.91 ? 196 TYR B CG  1 
ATOM   1572 C  CD1 . TYR A 1 196 ? -0.611  -15.520 16.673  1.00 11.86 ? 196 TYR B CD1 1 
ATOM   1573 C  CD2 . TYR A 1 196 ? 1.201   -14.415 17.894  1.00 12.53 ? 196 TYR B CD2 1 
ATOM   1574 C  CE1 . TYR A 1 196 ? -0.778  -14.376 15.893  1.00 11.39 ? 196 TYR B CE1 1 
ATOM   1575 C  CE2 . TYR A 1 196 ? 1.005   -13.232 17.133  1.00 11.97 ? 196 TYR B CE2 1 
ATOM   1576 C  CZ  . TYR A 1 196 ? -0.026  -13.281 16.153  1.00 12.29 ? 196 TYR B CZ  1 
ATOM   1577 O  OH  . TYR A 1 196 ? -0.090  -12.050 15.462  1.00 11.74 ? 196 TYR B OH  1 
ATOM   1578 N  N   . PRO A 1 197 ? 0.338   -15.310 21.342  1.00 12.31 ? 197 PRO B N   1 
ATOM   1579 C  CA  . PRO A 1 197 ? 0.306   -14.052 22.053  1.00 11.77 ? 197 PRO B CA  1 
ATOM   1580 C  C   . PRO A 1 197 ? 0.967   -12.944 21.225  1.00 13.99 ? 197 PRO B C   1 
ATOM   1581 O  O   . PRO A 1 197 ? 2.095   -13.128 20.737  1.00 13.39 ? 197 PRO B O   1 
ATOM   1582 C  CB  . PRO A 1 197 ? 1.106   -14.367 23.387  1.00 13.98 ? 197 PRO B CB  1 
ATOM   1583 C  CG  . PRO A 1 197 ? 2.177   -15.369 22.891  1.00 13.69 ? 197 PRO B CG  1 
ATOM   1584 C  CD  . PRO A 1 197 ? 1.409   -16.247 21.850  1.00 14.79 ? 197 PRO B CD  1 
ATOM   1585 N  N   . GLY A 1 198 ? 0.316   -11.798 21.173  1.00 12.94 ? 198 GLY B N   1 
ATOM   1586 C  CA  . GLY A 1 198 ? 0.865   -10.722 20.403  1.00 12.93 ? 198 GLY B CA  1 
ATOM   1587 C  C   . GLY A 1 198 ? 0.394   -9.400  20.746  1.00 12.93 ? 198 GLY B C   1 
ATOM   1588 O  O   . GLY A 1 198 ? 0.089   -9.046  21.915  1.00 13.45 ? 198 GLY B O   1 
ATOM   1589 N  N   . SER A 1 199 ? 0.252   -8.503  19.737  1.00 11.97 ? 199 SER B N   1 
ATOM   1590 C  CA  . SER A 1 199 ? 0.005   -7.121  20.004  1.00 14.57 ? 199 SER B CA  1 
ATOM   1591 C  C   . SER A 1 199 ? -1.079  -6.507  19.144  1.00 13.26 ? 199 SER B C   1 
ATOM   1592 O  O   . SER A 1 199 ? -1.583  -7.134  18.184  1.00 13.73 ? 199 SER B O   1 
ATOM   1593 C  CB  . SER A 1 199 ? 1.304   -6.265  19.725  1.00 12.59 ? 199 SER B CB  1 
ATOM   1594 O  OG  . SER A 1 199 ? 1.513   -6.257  18.328  1.00 13.77 ? 199 SER B OG  1 
ATOM   1595 N  N   . LEU A 1 200 ? -1.449  -5.280  19.491  1.00 12.16 ? 200 LEU B N   1 
ATOM   1596 C  CA  . LEU A 1 200 ? -2.190  -4.442  18.506  1.00 13.76 ? 200 LEU B CA  1 
ATOM   1597 C  C   . LEU A 1 200 ? -1.275  -4.313  17.285  1.00 14.33 ? 200 LEU B C   1 
ATOM   1598 O  O   . LEU A 1 200 ? -0.084  -4.253  17.384  1.00 13.95 ? 200 LEU B O   1 
ATOM   1599 C  CB  . LEU A 1 200 ? -2.422  -3.042  19.031  1.00 14.09 ? 200 LEU B CB  1 
ATOM   1600 C  CG  . LEU A 1 200 ? -3.517  -2.742  19.972  1.00 18.45 ? 200 LEU B CG  1 
ATOM   1601 C  CD1 . LEU A 1 200 ? -3.536  -3.677  21.063  1.00 18.72 ? 200 LEU B CD1 1 
ATOM   1602 C  CD2 . LEU A 1 200 ? -3.358  -1.314  20.534  1.00 17.71 ? 200 LEU B CD2 1 
ATOM   1603 N  N   . THR A 1 201 ? -1.913  -4.285  16.094  1.00 13.83 ? 201 THR B N   1 
ATOM   1604 C  CA  . THR A 1 201 ? -1.161  -4.051  14.841  1.00 12.71 ? 201 THR B CA  1 
ATOM   1605 C  C   . THR A 1 201 ? -1.147  -2.646  14.452  1.00 14.24 ? 201 THR B C   1 
ATOM   1606 O  O   . THR A 1 201 ? -0.700  -2.356  13.306  1.00 14.54 ? 201 THR B O   1 
ATOM   1607 C  CB  . THR A 1 201 ? -1.750  -4.907  13.659  1.00 11.42 ? 201 THR B CB  1 
ATOM   1608 O  OG1 . THR A 1 201 ? -3.029  -4.475  13.314  1.00 11.97 ? 201 THR B OG1 1 
ATOM   1609 C  CG2 . THR A 1 201 ? -1.759  -6.414  14.124  1.00 12.75 ? 201 THR B CG2 1 
ATOM   1610 N  N   . VAL A 1 202 ? -1.587  -1.723  15.317  1.00 14.26 ? 202 VAL B N   1 
ATOM   1611 C  CA  . VAL A 1 202 ? -1.532  -0.267  15.055  1.00 14.20 ? 202 VAL B CA  1 
ATOM   1612 C  C   . VAL A 1 202 ? -0.975  0.354   16.320  1.00 16.60 ? 202 VAL B C   1 
ATOM   1613 O  O   . VAL A 1 202 ? -1.156  -0.200  17.410  1.00 15.45 ? 202 VAL B O   1 
ATOM   1614 C  CB  . VAL A 1 202 ? -2.890  0.364   14.763  1.00 16.26 ? 202 VAL B CB  1 
ATOM   1615 C  CG1 . VAL A 1 202 ? -3.383  -0.142  13.398  1.00 15.69 ? 202 VAL B CG1 1 
ATOM   1616 C  CG2 . VAL A 1 202 ? -3.935  0.089   15.824  1.00 16.75 ? 202 VAL B CG2 1 
ATOM   1617 N  N   . PRO A 1 203 ? -0.346  1.505   16.216  1.00 15.68 ? 203 PRO B N   1 
ATOM   1618 C  CA  . PRO A 1 203 ? 0.042   2.291   17.408  1.00 17.21 ? 203 PRO B CA  1 
ATOM   1619 C  C   . PRO A 1 203 ? -1.193  2.416   18.288  1.00 14.50 ? 203 PRO B C   1 
ATOM   1620 O  O   . PRO A 1 203 ? -2.321  2.673   17.860  1.00 16.83 ? 203 PRO B O   1 
ATOM   1621 C  CB  . PRO A 1 203 ? 0.456   3.612   16.811  1.00 17.56 ? 203 PRO B CB  1 
ATOM   1622 C  CG  . PRO A 1 203 ? 1.038   3.202   15.473  1.00 16.32 ? 203 PRO B CG  1 
ATOM   1623 C  CD  . PRO A 1 203 ? 0.070   2.167   14.946  1.00 16.63 ? 203 PRO B CD  1 
ATOM   1624 N  N   . PRO A 1 204 ? -0.997  2.236   19.642  1.00 16.89 ? 204 PRO B N   1 
ATOM   1625 C  CA  . PRO A 1 204 ? 0.203   2.122   20.375  1.00 17.59 ? 204 PRO B CA  1 
ATOM   1626 C  C   . PRO A 1 204 ? 0.921   0.756   20.467  1.00 14.09 ? 204 PRO B C   1 
ATOM   1627 O  O   . PRO A 1 204 ? 1.941   0.593   21.129  1.00 15.67 ? 204 PRO B O   1 
ATOM   1628 C  CB  . PRO A 1 204 ? -0.274  2.491   21.814  1.00 17.39 ? 204 PRO B CB  1 
ATOM   1629 C  CG  . PRO A 1 204 ? -1.627  2.002   21.864  1.00 18.98 ? 204 PRO B CG  1 
ATOM   1630 C  CD  . PRO A 1 204 ? -2.193  2.322   20.487  1.00 19.09 ? 204 PRO B CD  1 
ATOM   1631 N  N   . LEU A 1 205 ? 0.453   -0.274  19.679  1.00 14.28 ? 205 LEU B N   1 
ATOM   1632 C  CA  . LEU A 1 205 ? 1.188   -1.513  19.498  1.00 13.29 ? 205 LEU B CA  1 
ATOM   1633 C  C   . LEU A 1 205 ? 1.378   -2.323  20.815  1.00 13.51 ? 205 LEU B C   1 
ATOM   1634 O  O   . LEU A 1 205 ? 2.261   -3.118  20.920  1.00 13.27 ? 205 LEU B O   1 
ATOM   1635 C  CB  . LEU A 1 205 ? 2.559   -1.301  18.775  1.00 16.06 ? 205 LEU B CB  1 
ATOM   1636 C  CG  . LEU A 1 205 ? 2.391   -0.649  17.351  1.00 15.81 ? 205 LEU B CG  1 
ATOM   1637 C  CD1 . LEU A 1 205 ? 3.803   -0.121  16.934  1.00 16.69 ? 205 LEU B CD1 1 
ATOM   1638 C  CD2 . LEU A 1 205 ? 1.778   -1.573  16.295  1.00 17.13 ? 205 LEU B CD2 1 
ATOM   1639 N  N   . LEU A 1 206 ? 0.435   -2.083  21.735  1.00 16.55 ? 206 LEU B N   1 
ATOM   1640 C  CA  . LEU A 1 206 ? 0.472   -2.720  23.069  1.00 16.59 ? 206 LEU B CA  1 
ATOM   1641 C  C   . LEU A 1 206 ? 0.434   -4.246  22.942  1.00 16.65 ? 206 LEU B C   1 
ATOM   1642 O  O   . LEU A 1 206 ? -0.380  -4.804  22.211  1.00 13.75 ? 206 LEU B O   1 
ATOM   1643 C  CB  . LEU A 1 206 ? -0.716  -2.218  23.894  1.00 16.96 ? 206 LEU B CB  1 
ATOM   1644 C  CG  . LEU A 1 206 ? -0.734  -0.711  24.146  1.00 17.34 ? 206 LEU B CG  1 
ATOM   1645 C  CD1 . LEU A 1 206 ? -2.050  -0.302  24.762  1.00 17.25 ? 206 LEU B CD1 1 
ATOM   1646 C  CD2 . LEU A 1 206 ? 0.536   -0.344  24.954  1.00 21.98 ? 206 LEU B CD2 1 
ATOM   1647 N  N   . GLU A 1 207 ? 1.241   -4.921  23.754  1.00 14.09 ? 207 GLU B N   1 
ATOM   1648 C  CA  . GLU A 1 207 ? 1.383   -6.397  23.757  1.00 14.71 ? 207 GLU B CA  1 
ATOM   1649 C  C   . GLU A 1 207 ? 0.387   -6.962  24.762  1.00 15.85 ? 207 GLU B C   1 
ATOM   1650 O  O   . GLU A 1 207 ? 0.745   -7.558  25.810  1.00 15.50 ? 207 GLU B O   1 
ATOM   1651 C  CB  . GLU A 1 207 ? 2.839   -6.803  23.992  1.00 16.59 ? 207 GLU B CB  1 
ATOM   1652 C  CG  . GLU A 1 207 ? 3.718   -6.273  22.847  1.00 17.97 ? 207 GLU B CG  1 
ATOM   1653 C  CD  . GLU A 1 207 ? 5.216   -6.623  22.967  1.00 23.34 ? 207 GLU B CD  1 
ATOM   1654 O  OE1 . GLU A 1 207 ? 5.738   -6.856  24.135  1.00 20.59 ? 207 GLU B OE1 1 
ATOM   1655 O  OE2 . GLU A 1 207 ? 5.902   -6.688  21.915  1.00 18.85 ? 207 GLU B OE2 1 
ATOM   1656 N  N   . SER A 1 208 ? -0.877  -6.874  24.376  1.00 13.63 ? 208 SER B N   1 
ATOM   1657 C  CA  . SER A 1 208 ? -1.996  -7.235  25.259  1.00 13.91 ? 208 SER B CA  1 
ATOM   1658 C  C   . SER A 1 208 ? -3.019  -8.190  24.583  1.00 13.06 ? 208 SER B C   1 
ATOM   1659 O  O   . SER A 1 208 ? -4.123  -8.425  25.075  1.00 13.74 ? 208 SER B O   1 
ATOM   1660 C  CB  . SER A 1 208 ? -2.756  -6.022  25.662  1.00 15.84 ? 208 SER B CB  1 
ATOM   1661 O  OG  . SER A 1 208 ? -3.070  -5.163  24.504  1.00 16.90 ? 208 SER B OG  1 
ATOM   1662 N  N   . VAL A 1 209 ? -2.628  -8.681  23.381  1.00 12.90 ? 209 VAL B N   1 
ATOM   1663 C  CA  . VAL A 1 209 ? -3.563  -9.448  22.595  1.00 12.22 ? 209 VAL B CA  1 
ATOM   1664 C  C   . VAL A 1 209 ? -3.341  -10.929 22.473  1.00 11.39 ? 209 VAL B C   1 
ATOM   1665 O  O   . VAL A 1 209 ? -2.242  -11.391 22.117  1.00 12.92 ? 209 VAL B O   1 
ATOM   1666 C  CB  . VAL A 1 209 ? -3.592  -8.865  21.135  1.00 10.00 ? 209 VAL B CB  1 
ATOM   1667 C  CG1 . VAL A 1 209 ? -4.644  -9.614  20.298  1.00 11.99 ? 209 VAL B CG1 1 
ATOM   1668 C  CG2 . VAL A 1 209 ? -3.912  -7.374  21.150  1.00 13.60 ? 209 VAL B CG2 1 
ATOM   1669 N  N   . THR A 1 210 ? -4.405  -11.688 22.806  1.00 10.97 ? 210 THR B N   1 
ATOM   1670 C  CA  . THR A 1 210 ? -4.474  -13.078 22.511  1.00 11.43 ? 210 THR B CA  1 
ATOM   1671 C  C   . THR A 1 210 ? -5.080  -13.111 21.067  1.00 9.85  ? 210 THR B C   1 
ATOM   1672 O  O   . THR A 1 210 ? -6.285  -12.871 20.898  1.00 10.57 ? 210 THR B O   1 
ATOM   1673 C  CB  . THR A 1 210 ? -5.324  -13.917 23.465  1.00 11.06 ? 210 THR B CB  1 
ATOM   1674 O  OG1 . THR A 1 210 ? -4.708  -13.785 24.775  1.00 14.71 ? 210 THR B OG1 1 
ATOM   1675 C  CG2 . THR A 1 210 ? -5.232  -15.361 23.084  1.00 12.20 ? 210 THR B CG2 1 
ATOM   1676 N  N   . TRP A 1 211 ? -4.187  -13.468 20.129  1.00 11.40 ? 211 TRP B N   1 
ATOM   1677 C  CA  . TRP A 1 211 ? -4.703  -13.577 18.716  1.00 10.58 ? 211 TRP B CA  1 
ATOM   1678 C  C   . TRP A 1 211 ? -5.315  -14.939 18.426  1.00 11.32 ? 211 TRP B C   1 
ATOM   1679 O  O   . TRP A 1 211 ? -4.780  -16.000 18.787  1.00 13.17 ? 211 TRP B O   1 
ATOM   1680 C  CB  . TRP A 1 211 ? -3.510  -13.419 17.754  1.00 10.85 ? 211 TRP B CB  1 
ATOM   1681 C  CG  . TRP A 1 211 ? -3.299  -11.959 17.526  1.00 10.71 ? 211 TRP B CG  1 
ATOM   1682 C  CD1 . TRP A 1 211 ? -2.388  -11.111 18.146  1.00 12.14 ? 211 TRP B CD1 1 
ATOM   1683 C  CD2 . TRP A 1 211 ? -4.094  -11.106 16.658  1.00 10.42 ? 211 TRP B CD2 1 
ATOM   1684 N  NE1 . TRP A 1 211 ? -2.541  -9.825  17.693  1.00 11.46 ? 211 TRP B NE1 1 
ATOM   1685 C  CE2 . TRP A 1 211 ? -3.551  -9.757  16.797  1.00 9.95  ? 211 TRP B CE2 1 
ATOM   1686 C  CE3 . TRP A 1 211 ? -5.149  -11.324 15.792  1.00 11.56 ? 211 TRP B CE3 1 
ATOM   1687 C  CZ2 . TRP A 1 211 ? -4.062  -8.689  16.086  1.00 10.58 ? 211 TRP B CZ2 1 
ATOM   1688 C  CZ3 . TRP A 1 211 ? -5.657  -10.243 15.081  1.00 10.63 ? 211 TRP B CZ3 1 
ATOM   1689 C  CH2 . TRP A 1 211 ? -5.126  -8.957  15.225  1.00 11.26 ? 211 TRP B CH2 1 
ATOM   1690 N  N   . ILE A 1 212 ? -6.478  -14.891 17.782  1.00 10.15 ? 212 ILE B N   1 
ATOM   1691 C  CA  . ILE A 1 212 ? -7.205  -16.108 17.393  1.00 10.01 ? 212 ILE B CA  1 
ATOM   1692 C  C   . ILE A 1 212 ? -7.476  -15.859 15.852  1.00 10.12 ? 212 ILE B C   1 
ATOM   1693 O  O   . ILE A 1 212 ? -8.411  -15.106 15.488  1.00 10.18 ? 212 ILE B O   1 
ATOM   1694 C  CB  . ILE A 1 212 ? -8.558  -16.209 18.130  1.00 10.54 ? 212 ILE B CB  1 
ATOM   1695 C  CG1 . ILE A 1 212 ? -8.228  -16.396 19.652  1.00 12.26 ? 212 ILE B CG1 1 
ATOM   1696 C  CG2 . ILE A 1 212 ? -9.330  -17.481 17.649  1.00 12.10 ? 212 ILE B CG2 1 
ATOM   1697 C  CD1 . ILE A 1 212 ? -9.482  -16.197 20.538  1.00 13.16 ? 212 ILE B CD1 1 
ATOM   1698 N  N   . VAL A 1 213 ? -6.695  -16.592 15.021  1.00 10.87 ? 213 VAL B N   1 
ATOM   1699 C  CA  . VAL A 1 213 ? -6.818  -16.327 13.532  1.00 11.25 ? 213 VAL B CA  1 
ATOM   1700 C  C   . VAL A 1 213 ? -7.542  -17.492 12.918  1.00 9.74  ? 213 VAL B C   1 
ATOM   1701 O  O   . VAL A 1 213 ? -7.054  -18.623 13.012  1.00 10.43 ? 213 VAL B O   1 
ATOM   1702 C  CB  . VAL A 1 213 ? -5.432  -16.165 12.972  1.00 11.28 ? 213 VAL B CB  1 
ATOM   1703 C  CG1 . VAL A 1 213 ? -5.555  -16.008 11.435  1.00 12.82 ? 213 VAL B CG1 1 
ATOM   1704 C  CG2 . VAL A 1 213 ? -4.795  -14.899 13.607  1.00 11.32 ? 213 VAL B CG2 1 
ATOM   1705 N  N   . LEU A 1 214 ? -8.762  -17.344 12.361  1.00 11.26 ? 214 LEU B N   1 
ATOM   1706 C  CA  . LEU A 1 214 ? -9.413  -18.433 11.682  1.00 11.40 ? 214 LEU B CA  1 
ATOM   1707 C  C   . LEU A 1 214 ? -8.727  -18.864 10.389  1.00 12.48 ? 214 LEU B C   1 
ATOM   1708 O  O   . LEU A 1 214 ? -8.333  -18.040 9.564   1.00 12.24 ? 214 LEU B O   1 
ATOM   1709 C  CB  . LEU A 1 214 ? -10.888 -18.052 11.351  1.00 11.67 ? 214 LEU B CB  1 
ATOM   1710 C  CG  . LEU A 1 214 ? -11.706 -17.681 12.581  1.00 12.96 ? 214 LEU B CG  1 
ATOM   1711 C  CD1 . LEU A 1 214 ? -13.191 -17.492 12.191  1.00 11.93 ? 214 LEU B CD1 1 
ATOM   1712 C  CD2 . LEU A 1 214 ? -11.673 -18.760 13.651  1.00 14.97 ? 214 LEU B CD2 1 
ATOM   1713 N  N   . LYS A 1 215 ? -8.642  -20.181 10.216  1.00 11.94 ? 215 LYS B N   1 
ATOM   1714 C  CA  . LYS A 1 215 ? -8.075  -20.701 8.971   1.00 12.60 ? 215 LYS B CA  1 
ATOM   1715 C  C   . LYS A 1 215 ? -8.954  -20.432 7.703   1.00 11.79 ? 215 LYS B C   1 
ATOM   1716 O  O   . LYS A 1 215 ? -8.350  -20.104 6.630   1.00 13.78 ? 215 LYS B O   1 
ATOM   1717 C  CB  . LYS A 1 215 ? -7.863  -22.218 9.147   1.00 11.85 ? 215 LYS B CB  1 
ATOM   1718 C  CG  . LYS A 1 215 ? -7.356  -22.875 7.837   1.00 15.18 ? 215 LYS B CG  1 
ATOM   1719 C  CD  . LYS A 1 215 ? -7.009  -24.351 8.064   1.00 14.39 ? 215 LYS B CD  1 
ATOM   1720 C  CE  . LYS A 1 215 ? -6.846  -24.990 6.687   1.00 22.11 ? 215 LYS B CE  1 
ATOM   1721 N  NZ  . LYS A 1 215 ? -6.338  -26.367 6.888   1.00 26.72 ? 215 LYS B NZ  1 
ATOM   1722 N  N   . GLN A 1 216 ? -10.253 -20.495 7.813   1.00 11.07 ? 216 GLN B N   1 
ATOM   1723 C  CA  . GLN A 1 216 ? -11.098 -20.482 6.615   1.00 11.12 ? 216 GLN B CA  1 
ATOM   1724 C  C   . GLN A 1 216 ? -11.456 -19.018 6.319   1.00 12.53 ? 216 GLN B C   1 
ATOM   1725 O  O   . GLN A 1 216 ? -12.070 -18.328 7.146   1.00 12.46 ? 216 GLN B O   1 
ATOM   1726 C  CB  . GLN A 1 216 ? -12.390 -21.241 6.797   1.00 11.67 ? 216 GLN B CB  1 
ATOM   1727 C  CG  . GLN A 1 216 ? -13.183 -21.242 5.500   1.00 11.53 ? 216 GLN B CG  1 
ATOM   1728 C  CD  . GLN A 1 216 ? -14.422 -22.167 5.494   1.00 15.18 ? 216 GLN B CD  1 
ATOM   1729 O  OE1 . GLN A 1 216 ? -14.992 -22.479 4.410   1.00 20.16 ? 216 GLN B OE1 1 
ATOM   1730 N  NE2 . GLN A 1 216 ? -14.808 -22.688 6.600   1.00 12.87 ? 216 GLN B NE2 1 
ATOM   1731 N  N   . PRO A 1 217 ? -11.120 -18.496 5.095   1.00 12.60 ? 217 PRO B N   1 
ATOM   1732 C  CA  . PRO A 1 217 ? -11.559 -17.184 4.682   1.00 13.28 ? 217 PRO B CA  1 
ATOM   1733 C  C   . PRO A 1 217 ? -13.047 -17.076 4.382   1.00 11.84 ? 217 PRO B C   1 
ATOM   1734 O  O   . PRO A 1 217 ? -13.717 -18.089 4.155   1.00 14.26 ? 217 PRO B O   1 
ATOM   1735 C  CB  . PRO A 1 217 ? -10.819 -16.947 3.364   1.00 14.83 ? 217 PRO B CB  1 
ATOM   1736 C  CG  . PRO A 1 217 ? -9.896  -18.079 3.183   1.00 20.19 ? 217 PRO B CG  1 
ATOM   1737 C  CD  . PRO A 1 217 ? -10.395 -19.230 4.027   1.00 14.11 ? 217 PRO B CD  1 
ATOM   1738 N  N   . ILE A 1 218 ? -13.572 -15.843 4.435   1.00 10.69 ? 218 ILE B N   1 
ATOM   1739 C  CA  . ILE A 1 218 ? -14.921 -15.493 3.925   1.00 12.63 ? 218 ILE B CA  1 
ATOM   1740 C  C   . ILE A 1 218 ? -14.752 -14.754 2.605   1.00 12.86 ? 218 ILE B C   1 
ATOM   1741 O  O   . ILE A 1 218 ? -13.614 -14.421 2.261   1.00 12.86 ? 218 ILE B O   1 
ATOM   1742 C  CB  . ILE A 1 218 ? -15.732 -14.681 4.971   1.00 11.48 ? 218 ILE B CB  1 
ATOM   1743 C  CG1 . ILE A 1 218 ? -15.116 -13.342 5.245   1.00 12.11 ? 218 ILE B CG1 1 
ATOM   1744 C  CG2 . ILE A 1 218 ? -15.848 -15.563 6.265   1.00 12.58 ? 218 ILE B CG2 1 
ATOM   1745 C  CD1 . ILE A 1 218 ? -15.968 -12.384 6.040   1.00 14.57 ? 218 ILE B CD1 1 
ATOM   1746 N  N   . ASN A 1 219 ? -15.887 -14.569 1.918   1.00 12.54 ? 219 ASN B N   1 
ATOM   1747 C  CA  . ASN A 1 219 ? -15.762 -13.961 0.559   1.00 12.36 ? 219 ASN B CA  1 
ATOM   1748 C  C   . ASN A 1 219 ? -16.198 -12.498 0.587   1.00 13.84 ? 219 ASN B C   1 
ATOM   1749 O  O   . ASN A 1 219 ? -17.022 -12.065 1.412   1.00 13.99 ? 219 ASN B O   1 
ATOM   1750 C  CB  . ASN A 1 219 ? -16.590 -14.758 -0.456  1.00 17.33 ? 219 ASN B CB  1 
ATOM   1751 C  CG  . ASN A 1 219 ? -16.075 -16.206 -0.565  1.00 22.71 ? 219 ASN B CG  1 
ATOM   1752 O  OD1 . ASN A 1 219 ? -16.663 -17.128 0.043   1.00 31.80 ? 219 ASN B OD1 1 
ATOM   1753 N  ND2 . ASN A 1 219 ? -14.909 -16.397 -1.209  1.00 22.55 ? 219 ASN B ND2 1 
ATOM   1754 N  N   . ILE A 1 220 ? -15.631 -11.704 -0.332  1.00 10.36 ? 220 ILE B N   1 
ATOM   1755 C  CA  . ILE A 1 220 ? -16.066 -10.341 -0.592  1.00 11.11 ? 220 ILE B CA  1 
ATOM   1756 C  C   . ILE A 1 220 ? -15.902 -10.171 -2.121  1.00 10.73 ? 220 ILE B C   1 
ATOM   1757 O  O   . ILE A 1 220 ? -14.959 -10.754 -2.674  1.00 12.46 ? 220 ILE B O   1 
ATOM   1758 C  CB  . ILE A 1 220 ? -15.191 -9.329  0.232   1.00 12.39 ? 220 ILE B CB  1 
ATOM   1759 C  CG1 . ILE A 1 220 ? -15.826 -7.922  0.136   1.00 10.16 ? 220 ILE B CG1 1 
ATOM   1760 C  CG2 . ILE A 1 220 ? -13.692 -9.432  -0.115  1.00 12.93 ? 220 ILE B CG2 1 
ATOM   1761 C  CD1 . ILE A 1 220 ? -15.159 -6.812  1.046   1.00 11.87 ? 220 ILE B CD1 1 
ATOM   1762 N  N   . SER A 1 221 ? -16.741 -9.291  -2.694  1.00 10.70 ? 221 SER B N   1 
ATOM   1763 C  CA  . SER A 1 221 ? -16.467 -9.075  -4.156  1.00 11.20 ? 221 SER B CA  1 
ATOM   1764 C  C   . SER A 1 221 ? -15.320 -8.086  -4.302  1.00 12.83 ? 221 SER B C   1 
ATOM   1765 O  O   . SER A 1 221 ? -15.062 -7.297  -3.378  1.00 12.35 ? 221 SER B O   1 
ATOM   1766 C  CB  . SER A 1 221 ? -17.706 -8.520  -4.880  1.00 12.21 ? 221 SER B CB  1 
ATOM   1767 O  OG  . SER A 1 221 ? -17.996 -7.228  -4.470  1.00 12.09 ? 221 SER B OG  1 
ATOM   1768 N  N   . SER A 1 222 ? -14.715 -8.046  -5.512  1.00 12.17 ? 222 SER B N   1 
ATOM   1769 C  CA  . SER A 1 222 ? -13.677 -7.025  -5.762  1.00 12.42 ? 222 SER B CA  1 
ATOM   1770 C  C   . SER A 1 222 ? -14.280 -5.627  -5.675  1.00 10.98 ? 222 SER B C   1 
ATOM   1771 O  O   . SER A 1 222 ? -13.571 -4.736  -5.161  1.00 11.53 ? 222 SER B O   1 
ATOM   1772 C  CB  . SER A 1 222 ? -12.902 -7.232  -7.093  1.00 14.34 ? 222 SER B CB  1 
ATOM   1773 O  OG  . SER A 1 222 ? -13.912 -7.161  -8.066  1.00 20.20 ? 222 SER B OG  1 
ATOM   1774 N  N   . GLN A 1 223 ? -15.527 -5.433  -6.158  1.00 13.71 ? 223 GLN B N   1 
ATOM   1775 C  CA  . GLN A 1 223 ? -16.142 -4.086  -6.079  1.00 15.85 ? 223 GLN B CA  1 
ATOM   1776 C  C   . GLN A 1 223 ? -16.411 -3.643  -4.607  1.00 13.90 ? 223 GLN B C   1 
ATOM   1777 O  O   . GLN A 1 223 ? -16.233 -2.464  -4.263  1.00 16.26 ? 223 GLN B O   1 
ATOM   1778 C  CB  . GLN A 1 223 ? -17.415 -4.053  -6.923  1.00 15.93 ? 223 GLN B CB  1 
ATOM   1779 C  CG  . GLN A 1 223 ? -17.170 -4.329  -8.420  1.00 18.36 ? 223 GLN B CG  1 
ATOM   1780 C  CD  . GLN A 1 223 ? -17.039 -5.768  -8.816  1.00 22.89 ? 223 GLN B CD  1 
ATOM   1781 O  OE1 . GLN A 1 223 ? -17.193 -6.774  -8.027  1.00 17.21 ? 223 GLN B OE1 1 
ATOM   1782 N  NE2 . GLN A 1 223 ? -16.821 -5.925  -10.130 1.00 22.56 ? 223 GLN B NE2 1 
ATOM   1783 N  N   . GLN A 1 224 ? -16.910 -4.584  -3.777  1.00 13.21 ? 224 GLN B N   1 
ATOM   1784 C  CA  . GLN A 1 224 ? -17.150 -4.205  -2.366  1.00 13.51 ? 224 GLN B CA  1 
ATOM   1785 C  C   . GLN A 1 224 ? -15.782 -3.831  -1.734  1.00 12.67 ? 224 GLN B C   1 
ATOM   1786 O  O   . GLN A 1 224 ? -15.653 -2.813  -1.017  1.00 12.19 ? 224 GLN B O   1 
ATOM   1787 C  CB  . GLN A 1 224 ? -17.712 -5.398  -1.568  1.00 12.79 ? 224 GLN B CB  1 
ATOM   1788 C  CG  . GLN A 1 224 ? -19.181 -5.679  -1.880  1.00 13.77 ? 224 GLN B CG  1 
ATOM   1789 C  CD  . GLN A 1 224 ? -19.664 -6.895  -1.117  1.00 11.60 ? 224 GLN B CD  1 
ATOM   1790 O  OE1 . GLN A 1 224 ? -18.958 -7.924  -1.026  1.00 12.50 ? 224 GLN B OE1 1 
ATOM   1791 N  NE2 . GLN A 1 224 ? -20.910 -6.798  -0.670  1.00 14.68 ? 224 GLN B NE2 1 
ATOM   1792 N  N   . LEU A 1 225 ? -14.746 -4.655  -1.939  1.00 12.09 ? 225 LEU B N   1 
ATOM   1793 C  CA  . LEU A 1 225 ? -13.450 -4.388  -1.307  1.00 10.68 ? 225 LEU B CA  1 
ATOM   1794 C  C   . LEU A 1 225 ? -12.909 -3.008  -1.714  1.00 11.17 ? 225 LEU B C   1 
ATOM   1795 O  O   . LEU A 1 225 ? -12.386 -2.228  -0.945  1.00 11.72 ? 225 LEU B O   1 
ATOM   1796 C  CB  . LEU A 1 225 ? -12.492 -5.533  -1.556  1.00 11.38 ? 225 LEU B CB  1 
ATOM   1797 C  CG  . LEU A 1 225 ? -11.134 -5.262  -0.864  1.00 11.20 ? 225 LEU B CG  1 
ATOM   1798 C  CD1 . LEU A 1 225 ? -11.250 -5.106  0.688   1.00 12.25 ? 225 LEU B CD1 1 
ATOM   1799 C  CD2 . LEU A 1 225 ? -10.178 -6.415  -1.128  1.00 12.01 ? 225 LEU B CD2 1 
ATOM   1800 N  N   . ALA A 1 226 ? -13.046 -2.730  -3.018  1.00 12.45 ? 226 ALA B N   1 
ATOM   1801 C  CA  . ALA A 1 226 ? -12.562 -1.466  -3.555  1.00 11.37 ? 226 ALA B CA  1 
ATOM   1802 C  C   . ALA A 1 226 ? -13.190 -0.246  -2.896  1.00 12.97 ? 226 ALA B C   1 
ATOM   1803 O  O   . ALA A 1 226 ? -12.480 0.728   -2.820  1.00 13.39 ? 226 ALA B O   1 
ATOM   1804 C  CB  . ALA A 1 226 ? -12.817 -1.450  -5.099  1.00 12.06 ? 226 ALA B CB  1 
ATOM   1805 N  N   . LYS A 1 227 ? -14.469 -0.327  -2.443  1.00 11.71 ? 227 LYS B N   1 
ATOM   1806 C  CA  . LYS A 1 227 ? -15.058 0.812   -1.818  1.00 13.16 ? 227 LYS B CA  1 
ATOM   1807 C  C   . LYS A 1 227 ? -14.285 1.243   -0.563  1.00 13.42 ? 227 LYS B C   1 
ATOM   1808 O  O   . LYS A 1 227 ? -14.266 2.446   -0.205  1.00 14.88 ? 227 LYS B O   1 
ATOM   1809 C  CB  . LYS A 1 227 ? -16.511 0.540   -1.494  1.00 16.14 ? 227 LYS B CB  1 
ATOM   1810 C  CG  . LYS A 1 227 ? -17.284 1.884   -1.394  1.00 24.13 ? 227 LYS B CG  1 
ATOM   1811 C  CD  . LYS A 1 227 ? -18.751 1.749   -1.767  1.00 24.32 ? 227 LYS B CD  1 
ATOM   1812 C  CE  . LYS A 1 227 ? -19.394 3.122   -1.897  1.00 30.68 ? 227 LYS B CE  1 
ATOM   1813 N  NZ  . LYS A 1 227 ? -20.881 3.066   -1.829  1.00 42.20 ? 227 LYS B NZ  1 
ATOM   1814 N  N   . PHE A 1 228 ? -13.635 0.271   0.125   1.00 12.89 ? 228 PHE B N   1 
ATOM   1815 C  CA  . PHE A 1 228 ? -12.918 0.722   1.293   1.00 12.13 ? 228 PHE B CA  1 
ATOM   1816 C  C   . PHE A 1 228 ? -11.748 1.612   1.043   1.00 12.32 ? 228 PHE B C   1 
ATOM   1817 O  O   . PHE A 1 228 ? -11.388 2.493   1.861   1.00 12.39 ? 228 PHE B O   1 
ATOM   1818 C  CB  . PHE A 1 228 ? -12.415 -0.467  2.156   1.00 12.01 ? 228 PHE B CB  1 
ATOM   1819 C  CG  . PHE A 1 228 ? -13.538 -1.264  2.722   1.00 12.84 ? 228 PHE B CG  1 
ATOM   1820 C  CD1 . PHE A 1 228 ? -13.929 -2.444  2.156   1.00 12.40 ? 228 PHE B CD1 1 
ATOM   1821 C  CD2 . PHE A 1 228 ? -14.271 -0.774  3.823   1.00 14.17 ? 228 PHE B CD2 1 
ATOM   1822 C  CE1 . PHE A 1 228 ? -15.051 -3.143  2.636   1.00 15.72 ? 228 PHE B CE1 1 
ATOM   1823 C  CE2 . PHE A 1 228 ? -15.379 -1.461  4.305   1.00 13.24 ? 228 PHE B CE2 1 
ATOM   1824 C  CZ  . PHE A 1 228 ? -15.759 -2.649  3.759   1.00 13.35 ? 228 PHE B CZ  1 
ATOM   1825 N  N   . ARG A 1 229 ? -11.125 1.503   -0.151  1.00 12.52 ? 229 ARG B N   1 
ATOM   1826 C  CA  . ARG A 1 229 ? -9.929  2.284   -0.497  1.00 13.22 ? 229 ARG B CA  1 
ATOM   1827 C  C   . ARG A 1 229 ? -10.293 3.744   -0.777  1.00 12.44 ? 229 ARG B C   1 
ATOM   1828 O  O   . ARG A 1 229 ? -9.394  4.563   -0.863  1.00 14.76 ? 229 ARG B O   1 
ATOM   1829 C  CB  . ARG A 1 229 ? -9.234  1.676   -1.723  1.00 11.93 ? 229 ARG B CB  1 
ATOM   1830 C  CG  . ARG A 1 229 ? -8.910  0.226   -1.540  1.00 11.21 ? 229 ARG B CG  1 
ATOM   1831 C  CD  . ARG A 1 229 ? -8.080  -0.280  -2.774  1.00 12.12 ? 229 ARG B CD  1 
ATOM   1832 N  NE  . ARG A 1 229 ? -7.687  -1.702  -2.655  1.00 12.15 ? 229 ARG B NE  1 
ATOM   1833 C  CZ  . ARG A 1 229 ? -8.319  -2.727  -3.229  1.00 13.61 ? 229 ARG B CZ  1 
ATOM   1834 N  NH1 . ARG A 1 229 ? -9.286  -2.541  -4.129  1.00 13.94 ? 229 ARG B NH1 1 
ATOM   1835 N  NH2 . ARG A 1 229 ? -7.988  -4.005  -2.868  1.00 14.11 ? 229 ARG B NH2 1 
ATOM   1836 N  N   . SER A 1 230 ? -11.581 4.013   -0.883  1.00 14.54 ? 230 SER B N   1 
ATOM   1837 C  CA  . SER A 1 230 ? -12.091 5.423   -1.075  1.00 16.41 ? 230 SER B CA  1 
ATOM   1838 C  C   . SER A 1 230 ? -12.276 6.209   0.213   1.00 15.42 ? 230 SER B C   1 
ATOM   1839 O  O   . SER A 1 230 ? -12.463 7.456   0.151   1.00 17.20 ? 230 SER B O   1 
ATOM   1840 C  CB  . SER A 1 230 ? -13.313 5.442   -1.928  1.00 18.91 ? 230 SER B CB  1 
ATOM   1841 O  OG  . SER A 1 230 ? -14.452 4.977   -1.276  1.00 23.31 ? 230 SER B OG  1 
ATOM   1842 N  N   . LEU A 1 231 ? -12.066 5.555   1.400   1.00 14.19 ? 231 LEU B N   1 
ATOM   1843 C  CA  . LEU A 1 231 ? -12.049 6.333   2.592   1.00 14.42 ? 231 LEU B CA  1 
ATOM   1844 C  C   . LEU A 1 231 ? -10.849 7.216   2.607   1.00 15.76 ? 231 LEU B C   1 
ATOM   1845 O  O   . LEU A 1 231 ? -9.725  6.848   2.079   1.00 16.49 ? 231 LEU B O   1 
ATOM   1846 C  CB  . LEU A 1 231 ? -11.886 5.350   3.791   1.00 16.18 ? 231 LEU B CB  1 
ATOM   1847 C  CG  . LEU A 1 231 ? -13.170 4.565   4.016   1.00 15.54 ? 231 LEU B CG  1 
ATOM   1848 C  CD1 . LEU A 1 231 ? -12.873 3.434   5.049   1.00 15.60 ? 231 LEU B CD1 1 
ATOM   1849 C  CD2 . LEU A 1 231 ? -14.364 5.402   4.448   1.00 14.67 ? 231 LEU B CD2 1 
ATOM   1850 N  N   . LEU A 1 232 ? -11.001 8.399   3.226   1.00 16.49 ? 232 LEU B N   1 
ATOM   1851 C  CA  . LEU A 1 232 ? -9.876  9.294   3.307   1.00 17.50 ? 232 LEU B CA  1 
ATOM   1852 C  C   . LEU A 1 232 ? -9.087  9.103   4.654   1.00 17.01 ? 232 LEU B C   1 
ATOM   1853 O  O   . LEU A 1 232 ? -9.693  8.777   5.666   1.00 18.15 ? 232 LEU B O   1 
ATOM   1854 C  CB  . LEU A 1 232 ? -10.306 10.748  3.264   1.00 19.50 ? 232 LEU B CB  1 
ATOM   1855 C  CG  . LEU A 1 232 ? -11.123 11.153  2.042   1.00 22.61 ? 232 LEU B CG  1 
ATOM   1856 C  CD1 . LEU A 1 232 ? -11.339 12.653  2.105   1.00 24.53 ? 232 LEU B CD1 1 
ATOM   1857 C  CD2 . LEU A 1 232 ? -10.382 10.768  0.770   1.00 24.53 ? 232 LEU B CD2 1 
ATOM   1858 N  N   . CYS A 1 233 ? -7.769  9.319   4.632   1.00 17.11 ? 233 CYS B N   1 
ATOM   1859 C  CA  . CYS A 1 233 ? -6.967  9.254   5.866   1.00 19.22 ? 233 CYS B CA  1 
ATOM   1860 C  C   . CYS A 1 233 ? -6.789  10.673  6.390   1.00 22.34 ? 233 CYS B C   1 
ATOM   1861 O  O   . CYS A 1 233 ? -6.201  10.863  7.471   1.00 23.40 ? 233 CYS B O   1 
ATOM   1862 C  CB  . CYS A 1 233 ? -5.606  8.539   5.765   1.00 16.43 ? 233 CYS B CB  1 
ATOM   1863 S  SG  . CYS A 1 233 ? -4.576  9.098   4.421   1.00 25.92 ? 233 CYS B SG  1 
ATOM   1864 N  N   . THR A 1 234 ? -7.262  11.622  5.580   1.00 21.14 ? 234 THR B N   1 
ATOM   1865 C  CA  . THR A 1 234 ? -7.320  13.062  5.925   1.00 25.96 ? 234 THR B CA  1 
ATOM   1866 C  C   . THR A 1 234 ? -8.707  13.567  6.393   1.00 25.75 ? 234 THR B C   1 
ATOM   1867 O  O   . THR A 1 234 ? -9.822  13.086  5.991   1.00 29.67 ? 234 THR B O   1 
ATOM   1868 C  CB  . THR A 1 234 ? -6.851  13.891  4.671   1.00 24.56 ? 234 THR B CB  1 
ATOM   1869 O  OG1 . THR A 1 234 ? -7.633  13.491  3.552   1.00 25.49 ? 234 THR B OG1 1 
ATOM   1870 C  CG2 . THR A 1 234 ? -5.426  13.614  4.334   1.00 26.56 ? 234 THR B CG2 1 
ATOM   1871 N  N   . ALA A 1 235 ? -8.698  14.591  7.259   1.00 36.29 ? 235 ALA B N   1 
ATOM   1872 C  CA  . ALA A 1 235 ? -9.981  15.193  7.759   1.00 39.79 ? 235 ALA B CA  1 
ATOM   1873 C  C   . ALA A 1 235 ? -10.710 16.105  6.763   1.00 42.70 ? 235 ALA B C   1 
ATOM   1874 O  O   . ALA A 1 235 ? -10.135 16.532  5.743   1.00 39.70 ? 235 ALA B O   1 
ATOM   1875 C  CB  . ALA A 1 235 ? -9.772  15.934  9.095   1.00 42.88 ? 235 ALA B CB  1 
ATOM   1876 N  N   . GLU A 1 236 ? -11.972 16.408  7.063   1.00 47.07 ? 236 GLU B N   1 
ATOM   1877 C  CA  . GLU A 1 236 ? -12.780 17.325  6.222   1.00 54.55 ? 236 GLU B CA  1 
ATOM   1878 C  C   . GLU A 1 236 ? -12.076 18.690  6.085   1.00 53.25 ? 236 GLU B C   1 
ATOM   1879 O  O   . GLU A 1 236 ? -11.462 19.162  7.041   1.00 43.29 ? 236 GLU B O   1 
ATOM   1880 C  CB  . GLU A 1 236 ? -14.206 17.458  6.778   1.00 59.72 ? 236 GLU B CB  1 
ATOM   1881 C  CG  . GLU A 1 236 ? -15.255 17.882  5.745   1.00 72.89 ? 236 GLU B CG  1 
ATOM   1882 C  CD  . GLU A 1 236 ? -16.672 17.936  6.310   1.00 73.61 ? 236 GLU B CD  1 
ATOM   1883 O  OE1 . GLU A 1 236 ? -16.838 18.233  7.518   1.00 80.36 ? 236 GLU B OE1 1 
ATOM   1884 O  OE2 . GLU A 1 236 ? -17.626 17.688  5.540   1.00 68.69 ? 236 GLU B OE2 1 
ATOM   1885 N  N   . GLY A 1 237 ? -12.140 19.278  4.887   1.00 55.19 ? 237 GLY B N   1 
ATOM   1886 C  CA  . GLY A 1 237 ? -11.307 20.440  4.506   1.00 59.05 ? 237 GLY B CA  1 
ATOM   1887 C  C   . GLY A 1 237 ? -9.793  20.431  4.685   1.00 57.48 ? 237 GLY B C   1 
ATOM   1888 O  O   . GLY A 1 237 ? -9.258  21.279  5.378   1.00 57.94 ? 237 GLY B O   1 
ATOM   1889 N  N   . GLU A 1 238 ? -9.115  19.455  4.075   1.00 56.44 ? 238 GLU B N   1 
ATOM   1890 C  CA  . GLU A 1 238 ? -7.650  19.258  4.184   1.00 53.57 ? 238 GLU B CA  1 
ATOM   1891 C  C   . GLU A 1 238 ? -7.173  18.533  2.924   1.00 47.96 ? 238 GLU B C   1 
ATOM   1892 O  O   . GLU A 1 238 ? -7.990  17.943  2.213   1.00 48.12 ? 238 GLU B O   1 
ATOM   1893 C  CB  . GLU A 1 238 ? -7.429  18.385  5.423   1.00 59.11 ? 238 GLU B CB  1 
ATOM   1894 C  CG  . GLU A 1 238 ? -6.025  17.842  5.615   1.00 65.13 ? 238 GLU B CG  1 
ATOM   1895 C  CD  . GLU A 1 238 ? -5.943  16.895  6.798   1.00 73.62 ? 238 GLU B CD  1 
ATOM   1896 O  OE1 . GLU A 1 238 ? -4.863  16.303  7.008   1.00 82.81 ? 238 GLU B OE1 1 
ATOM   1897 O  OE2 . GLU A 1 238 ? -6.951  16.739  7.527   1.00 70.79 ? 238 GLU B OE2 1 
ATOM   1898 N  N   . ALA A 1 239 ? -5.876  18.579  2.621   1.00 44.03 ? 239 ALA B N   1 
ATOM   1899 C  CA  . ALA A 1 239 ? -5.408  17.982  1.367   1.00 47.33 ? 239 ALA B CA  1 
ATOM   1900 C  C   . ALA A 1 239 ? -5.822  16.465  1.308   1.00 40.66 ? 239 ALA B C   1 
ATOM   1901 O  O   . ALA A 1 239 ? -5.267  15.662  2.072   1.00 44.02 ? 239 ALA B O   1 
ATOM   1902 C  CB  . ALA A 1 239 ? -3.889  18.146  1.250   1.00 45.13 ? 239 ALA B CB  1 
ATOM   1903 N  N   . ALA A 1 240 ? -6.765  16.094  0.425   1.00 34.88 ? 240 ALA B N   1 
ATOM   1904 C  CA  . ALA A 1 240 ? -7.267  14.684  0.392   1.00 31.73 ? 240 ALA B CA  1 
ATOM   1905 C  C   . ALA A 1 240 ? -6.163  13.642  0.111   1.00 30.75 ? 240 ALA B C   1 
ATOM   1906 O  O   . ALA A 1 240 ? -5.352  13.765  -0.834  1.00 24.96 ? 240 ALA B O   1 
ATOM   1907 C  CB  . ALA A 1 240 ? -8.465  14.508  -0.559  1.00 32.78 ? 240 ALA B CB  1 
ATOM   1908 N  N   . ALA A 1 241 ? -6.135  12.593  0.950   1.00 22.55 ? 241 ALA B N   1 
ATOM   1909 C  CA  . ALA A 1 241 ? -5.327  11.427  0.627   1.00 21.06 ? 241 ALA B CA  1 
ATOM   1910 C  C   . ALA A 1 241 ? -6.162  10.232  0.970   1.00 19.34 ? 241 ALA B C   1 
ATOM   1911 O  O   . ALA A 1 241 ? -7.010  10.284  1.869   1.00 18.41 ? 241 ALA B O   1 
ATOM   1912 C  CB  . ALA A 1 241 ? -4.027  11.390  1.370   1.00 19.94 ? 241 ALA B CB  1 
ATOM   1913 N  N   . PHE A 1 242 ? -6.004  9.199   0.165   1.00 16.41 ? 242 PHE B N   1 
ATOM   1914 C  CA  . PHE A 1 242 ? -6.848  8.018   0.282   1.00 14.81 ? 242 PHE B CA  1 
ATOM   1915 C  C   . PHE A 1 242 ? -6.216  6.849   0.970   1.00 12.24 ? 242 PHE B C   1 
ATOM   1916 O  O   . PHE A 1 242 ? -5.051  6.597   0.811   1.00 13.56 ? 242 PHE B O   1 
ATOM   1917 C  CB  . PHE A 1 242 ? -7.296  7.522   -1.158  1.00 15.03 ? 242 PHE B CB  1 
ATOM   1918 C  CG  . PHE A 1 242 ? -8.111  8.534   -1.885  1.00 15.93 ? 242 PHE B CG  1 
ATOM   1919 C  CD1 . PHE A 1 242 ? -7.438  9.481   -2.734  1.00 17.05 ? 242 PHE B CD1 1 
ATOM   1920 C  CD2 . PHE A 1 242 ? -9.515  8.543   -1.820  1.00 16.91 ? 242 PHE B CD2 1 
ATOM   1921 C  CE1 . PHE A 1 242 ? -8.222  10.448  -3.410  1.00 16.11 ? 242 PHE B CE1 1 
ATOM   1922 C  CE2 . PHE A 1 242 ? -10.248 9.495   -2.509  1.00 21.71 ? 242 PHE B CE2 1 
ATOM   1923 C  CZ  . PHE A 1 242 ? -9.578  10.444  -3.286  1.00 18.43 ? 242 PHE B CZ  1 
ATOM   1924 N  N   . LEU A 1 243 ? -7.082  6.177   1.762   1.00 13.02 ? 243 LEU B N   1 
ATOM   1925 C  CA  . LEU A 1 243 ? -6.578  5.015   2.517   1.00 13.22 ? 243 LEU B CA  1 
ATOM   1926 C  C   . LEU A 1 243 ? -6.562  3.746   1.616   1.00 12.05 ? 243 LEU B C   1 
ATOM   1927 O  O   . LEU A 1 243 ? -7.403  2.834   1.833   1.00 12.33 ? 243 LEU B O   1 
ATOM   1928 C  CB  . LEU A 1 243 ? -7.459  4.918   3.814   1.00 13.80 ? 243 LEU B CB  1 
ATOM   1929 C  CG  . LEU A 1 243 ? -7.009  3.833   4.799   1.00 14.18 ? 243 LEU B CG  1 
ATOM   1930 C  CD1 . LEU A 1 243 ? -5.693  4.197   5.398   1.00 13.73 ? 243 LEU B CD1 1 
ATOM   1931 C  CD2 . LEU A 1 243 ? -8.161  3.757   5.850   1.00 14.79 ? 243 LEU B CD2 1 
ATOM   1932 N  N   . VAL A 1 244 ? -5.624  3.738   0.629   1.00 11.96 ? 244 VAL B N   1 
ATOM   1933 C  CA  . VAL A 1 244 ? -5.670  2.645   -0.330  1.00 12.56 ? 244 VAL B CA  1 
ATOM   1934 C  C   . VAL A 1 244 ? -5.112  1.334   0.255   1.00 12.40 ? 244 VAL B C   1 
ATOM   1935 O  O   . VAL A 1 244 ? -5.317  0.240   -0.258  1.00 11.40 ? 244 VAL B O   1 
ATOM   1936 C  CB  . VAL A 1 244 ? -4.993  3.009   -1.654  1.00 13.78 ? 244 VAL B CB  1 
ATOM   1937 C  CG1 . VAL A 1 244 ? -5.692  4.224   -2.242  1.00 14.69 ? 244 VAL B CG1 1 
ATOM   1938 C  CG2 . VAL A 1 244 ? -3.505  3.238   -1.426  1.00 14.46 ? 244 VAL B CG2 1 
ATOM   1939 N  N   . SER A 1 245 ? -4.411  1.464   1.382   1.00 12.28 ? 245 SER B N   1 
ATOM   1940 C  CA  . SER A 1 245 ? -3.723  0.297   1.972   1.00 11.45 ? 245 SER B CA  1 
ATOM   1941 C  C   . SER A 1 245 ? -3.525  0.614   3.456   1.00 11.52 ? 245 SER B C   1 
ATOM   1942 O  O   . SER A 1 245 ? -3.130  1.722   3.819   1.00 12.12 ? 245 SER B O   1 
ATOM   1943 C  CB  . SER A 1 245 ? -2.360  0.048   1.252   1.00 12.90 ? 245 SER B CB  1 
ATOM   1944 O  OG  . SER A 1 245 ? -1.746  -1.147  1.777   1.00 13.87 ? 245 SER B OG  1 
ATOM   1945 N  N   . ASN A 1 246 ? -3.751  -0.401  4.324   1.00 10.75 ? 246 ASN B N   1 
ATOM   1946 C  CA  . ASN A 1 246 ? -3.651  -0.104  5.797   1.00 10.90 ? 246 ASN B CA  1 
ATOM   1947 C  C   . ASN A 1 246 ? -3.315  -1.405  6.441   1.00 11.64 ? 246 ASN B C   1 
ATOM   1948 O  O   . ASN A 1 246 ? -3.919  -1.739  7.504   1.00 12.28 ? 246 ASN B O   1 
ATOM   1949 C  CB  . ASN A 1 246 ? -4.986  0.498   6.301   1.00 10.41 ? 246 ASN B CB  1 
ATOM   1950 C  CG  . ASN A 1 246 ? -6.141  -0.438  6.215   1.00 10.18 ? 246 ASN B CG  1 
ATOM   1951 O  OD1 . ASN A 1 246 ? -6.095  -1.419  5.425   1.00 11.52 ? 246 ASN B OD1 1 
ATOM   1952 N  ND2 . ASN A 1 246 ? -7.232  -0.179  6.911   1.00 12.25 ? 246 ASN B ND2 1 
ATOM   1953 N  N   . HIS A 1 247 ? -2.303  -2.103  5.965   1.00 13.12 ? 247 HIS B N   1 
ATOM   1954 C  CA  . HIS A 1 247 ? -1.863  -3.373  6.681   1.00 11.43 ? 247 HIS B CA  1 
ATOM   1955 C  C   . HIS A 1 247 ? -0.460  -3.261  7.080   1.00 13.91 ? 247 HIS B C   1 
ATOM   1956 O  O   . HIS A 1 247 ? 0.394   -2.693  6.366   1.00 16.12 ? 247 HIS B O   1 
ATOM   1957 C  CB  . HIS A 1 247 ? -2.091  -4.630  5.833   1.00 11.82 ? 247 HIS B CB  1 
ATOM   1958 C  CG  . HIS A 1 247 ? -1.430  -4.562  4.431   1.00 14.00 ? 247 HIS B CG  1 
ATOM   1959 N  ND1 . HIS A 1 247 ? -0.186  -5.061  4.112   1.00 19.57 ? 247 HIS B ND1 1 
ATOM   1960 C  CD2 . HIS A 1 247 ? -1.907  -3.961  3.318   1.00 12.28 ? 247 HIS B CD2 1 
ATOM   1961 C  CE1 . HIS A 1 247 ? 0.053   -4.779  2.763   1.00 14.74 ? 247 HIS B CE1 1 
ATOM   1962 N  NE2 . HIS A 1 247 ? -0.972  -4.134  2.318   1.00 17.65 ? 247 HIS B NE2 1 
ATOM   1963 N  N   . ARG A 1 248 ? -0.132  -3.776  8.264   1.00 12.98 ? 248 ARG B N   1 
ATOM   1964 C  CA  . ARG A 1 248 ? 1.201   -3.791  8.740   1.00 11.69 ? 248 ARG B CA  1 
ATOM   1965 C  C   . ARG A 1 248 ? 1.929   -5.087  8.296   1.00 13.27 ? 248 ARG B C   1 
ATOM   1966 O  O   . ARG A 1 248 ? 1.320   -6.142  8.253   1.00 13.29 ? 248 ARG B O   1 
ATOM   1967 C  CB  . ARG A 1 248 ? 1.079   -3.740  10.337  1.00 13.85 ? 248 ARG B CB  1 
ATOM   1968 C  CG  . ARG A 1 248 ? 2.396   -3.717  10.974  1.00 13.87 ? 248 ARG B CG  1 
ATOM   1969 C  CD  . ARG A 1 248 ? 2.376   -3.839  12.546  1.00 13.83 ? 248 ARG B CD  1 
ATOM   1970 N  NE  . ARG A 1 248 ? 3.713   -3.402  12.999  1.00 16.08 ? 248 ARG B NE  1 
ATOM   1971 C  CZ  . ARG A 1 248 ? 4.218   -3.688  14.233  1.00 16.92 ? 248 ARG B CZ  1 
ATOM   1972 N  NH1 . ARG A 1 248 ? 3.598   -4.518  15.037  1.00 15.16 ? 248 ARG B NH1 1 
ATOM   1973 N  NH2 . ARG A 1 248 ? 5.358   -3.170  14.629  1.00 17.46 ? 248 ARG B NH2 1 
ATOM   1974 N  N   . PRO A 1 249 ? 3.229   -4.990  7.939   1.00 15.31 ? 249 PRO B N   1 
ATOM   1975 C  CA  . PRO A 1 249 ? 3.955   -6.166  7.547   1.00 17.83 ? 249 PRO B CA  1 
ATOM   1976 C  C   . PRO A 1 249 ? 4.078   -7.177  8.678   1.00 17.04 ? 249 PRO B C   1 
ATOM   1977 O  O   . PRO A 1 249 ? 3.992   -6.775  9.841   1.00 17.94 ? 249 PRO B O   1 
ATOM   1978 C  CB  . PRO A 1 249 ? 5.391   -5.603  7.282   1.00 19.24 ? 249 PRO B CB  1 
ATOM   1979 C  CG  . PRO A 1 249 ? 5.180   -4.230  6.845   1.00 21.29 ? 249 PRO B CG  1 
ATOM   1980 C  CD  . PRO A 1 249 ? 3.996   -3.760  7.734   1.00 17.83 ? 249 PRO B CD  1 
ATOM   1981 N  N   . PRO A 1 250 ? 4.351   -8.429  8.383   1.00 17.70 ? 250 PRO B N   1 
ATOM   1982 C  CA  . PRO A 1 250 ? 4.575   -9.437  9.479   1.00 17.17 ? 250 PRO B CA  1 
ATOM   1983 C  C   . PRO A 1 250 ? 5.837   -9.130  10.314  1.00 17.76 ? 250 PRO B C   1 
ATOM   1984 O  O   . PRO A 1 250 ? 6.800   -8.522  9.811   1.00 19.11 ? 250 PRO B O   1 
ATOM   1985 C  CB  . PRO A 1 250 ? 4.775   -10.768 8.726   1.00 17.45 ? 250 PRO B CB  1 
ATOM   1986 C  CG  . PRO A 1 250 ? 4.443   -10.428 7.265   1.00 24.44 ? 250 PRO B CG  1 
ATOM   1987 C  CD  . PRO A 1 250 ? 4.585   -8.972  7.033   1.00 20.81 ? 250 PRO B CD  1 
ATOM   1988 N  N   . GLN A 1 251 ? 5.815   -9.482  11.623  1.00 14.72 ? 251 GLN B N   1 
ATOM   1989 C  CA  . GLN A 1 251 ? 6.860   -9.098  12.551  1.00 15.11 ? 251 GLN B CA  1 
ATOM   1990 C  C   . GLN A 1 251 ? 7.487   -10.408 13.016  1.00 15.15 ? 251 GLN B C   1 
ATOM   1991 O  O   . GLN A 1 251 ? 6.957   -11.487 12.928  1.00 16.04 ? 251 GLN B O   1 
ATOM   1992 C  CB  . GLN A 1 251 ? 6.206   -8.353  13.755  1.00 15.61 ? 251 GLN B CB  1 
ATOM   1993 C  CG  . GLN A 1 251 ? 5.502   -7.128  13.311  1.00 17.41 ? 251 GLN B CG  1 
ATOM   1994 C  CD  . GLN A 1 251 ? 6.423   -6.168  12.574  1.00 22.96 ? 251 GLN B CD  1 
ATOM   1995 O  OE1 . GLN A 1 251 ? 6.075   -5.670  11.473  1.00 21.70 ? 251 GLN B OE1 1 
ATOM   1996 N  NE2 . GLN A 1 251 ? 7.557   -5.853  13.169  1.00 19.16 ? 251 GLN B NE2 1 
ATOM   1997 N  N   . PRO A 1 252 ? 8.721   -10.321 13.514  1.00 16.63 ? 252 PRO B N   1 
ATOM   1998 C  CA  . PRO A 1 252 ? 9.449   -11.526 13.963  1.00 18.10 ? 252 PRO B CA  1 
ATOM   1999 C  C   . PRO A 1 252 ? 8.751   -12.293 15.078  1.00 17.69 ? 252 PRO B C   1 
ATOM   2000 O  O   . PRO A 1 252 ? 8.243   -11.700 16.026  1.00 19.31 ? 252 PRO B O   1 
ATOM   2001 C  CB  . PRO A 1 252 ? 10.801  -10.980 14.464  1.00 18.82 ? 252 PRO B CB  1 
ATOM   2002 C  CG  . PRO A 1 252 ? 10.824  -9.580  13.948  1.00 20.21 ? 252 PRO B CG  1 
ATOM   2003 C  CD  . PRO A 1 252 ? 9.399   -9.057  13.821  1.00 16.75 ? 252 PRO B CD  1 
ATOM   2004 N  N   . LEU A 1 253 ? 8.782   -13.584 14.918  1.00 18.72 ? 253 LEU B N   1 
ATOM   2005 C  CA  . LEU A 1 253 ? 8.112   -14.492 15.868  1.00 18.71 ? 253 LEU B CA  1 
ATOM   2006 C  C   . LEU A 1 253 ? 8.795   -14.504 17.233  1.00 20.99 ? 253 LEU B C   1 
ATOM   2007 O  O   . LEU A 1 253 ? 8.162   -14.547 18.268  1.00 17.95 ? 253 LEU B O   1 
ATOM   2008 C  CB  . LEU A 1 253 ? 8.020   -15.903 15.295  1.00 20.53 ? 253 LEU B CB  1 
ATOM   2009 C  CG  . LEU A 1 253 ? 6.988   -16.824 16.031  1.00 21.32 ? 253 LEU B CG  1 
ATOM   2010 C  CD1 . LEU A 1 253 ? 5.578   -16.255 16.203  1.00 22.18 ? 253 LEU B CD1 1 
ATOM   2011 C  CD2 . LEU A 1 253 ? 6.861   -18.183 15.327  1.00 22.76 ? 253 LEU B CD2 1 
ATOM   2012 N  N   . LYS A 1 254 ? 10.118  -14.321 17.242  1.00 21.00 ? 254 LYS B N   1 
ATOM   2013 C  CA  . LYS A 1 254 ? 10.866  -14.243 18.475  1.00 20.82 ? 254 LYS B CA  1 
ATOM   2014 C  C   . LYS A 1 254 ? 10.534  -15.377 19.496  1.00 19.02 ? 254 LYS B C   1 
ATOM   2015 O  O   . LYS A 1 254 ? 10.430  -15.117 20.725  1.00 19.91 ? 254 LYS B O   1 
ATOM   2016 C  CB  . LYS A 1 254 ? 10.810  -12.853 19.066  1.00 20.86 ? 254 LYS B CB  1 
ATOM   2017 C  CG  . LYS A 1 254 ? 11.621  -11.939 18.105  1.00 24.01 ? 254 LYS B CG  1 
ATOM   2018 C  CD  . LYS A 1 254 ? 11.758  -10.598 18.694  1.00 27.13 ? 254 LYS B CD  1 
ATOM   2019 C  CE  . LYS A 1 254 ? 12.645  -9.684  17.868  1.00 30.27 ? 254 LYS B CE  1 
ATOM   2020 N  NZ  . LYS A 1 254 ? 12.428  -8.311  18.422  1.00 34.08 ? 254 LYS B NZ  1 
ATOM   2021 N  N   . GLY A 1 255 ? 10.433  -16.567 18.956  1.00 19.78 ? 255 GLY B N   1 
ATOM   2022 C  CA  . GLY A 1 255 ? 10.342  -17.782 19.843  1.00 19.78 ? 255 GLY B CA  1 
ATOM   2023 C  C   . GLY A 1 255 ? 8.997   -18.003 20.494  1.00 19.78 ? 255 GLY B C   1 
ATOM   2024 O  O   . GLY A 1 255 ? 8.831   -18.930 21.327  1.00 20.92 ? 255 GLY B O   1 
ATOM   2025 N  N   . ARG A 1 256 ? 7.986   -17.227 20.125  1.00 17.15 ? 256 ARG B N   1 
ATOM   2026 C  CA  . ARG A 1 256 ? 6.600   -17.555 20.534  1.00 16.84 ? 256 ARG B CA  1 
ATOM   2027 C  C   . ARG A 1 256 ? 6.109   -18.873 19.891  1.00 17.04 ? 256 ARG B C   1 
ATOM   2028 O  O   . ARG A 1 256 ? 6.510   -19.322 18.800  1.00 18.68 ? 256 ARG B O   1 
ATOM   2029 C  CB  . ARG A 1 256 ? 5.653   -16.398 20.092  1.00 15.71 ? 256 ARG B CB  1 
ATOM   2030 C  CG  . ARG A 1 256 ? 5.876   -15.202 20.864  1.00 15.16 ? 256 ARG B CG  1 
ATOM   2031 C  CD  . ARG A 1 256 ? 5.049   -13.992 20.421  1.00 16.35 ? 256 ARG B CD  1 
ATOM   2032 N  NE  . ARG A 1 256 ? 5.644   -13.428 19.213  1.00 16.10 ? 256 ARG B NE  1 
ATOM   2033 C  CZ  . ARG A 1 256 ? 5.085   -12.484 18.465  1.00 15.46 ? 256 ARG B CZ  1 
ATOM   2034 N  NH1 . ARG A 1 256 ? 3.908   -11.979 18.800  1.00 16.32 ? 256 ARG B NH1 1 
ATOM   2035 N  NH2 . ARG A 1 256 ? 5.705   -12.037 17.384  1.00 15.27 ? 256 ARG B NH2 1 
ATOM   2036 N  N   . LYS A 1 257 ? 5.161   -19.511 20.584  1.00 17.15 ? 257 LYS B N   1 
ATOM   2037 C  CA  . LYS A 1 257 ? 4.562   -20.728 20.126  1.00 18.88 ? 257 LYS B CA  1 
ATOM   2038 C  C   . LYS A 1 257 ? 3.233   -20.404 19.425  1.00 17.77 ? 257 LYS B C   1 
ATOM   2039 O  O   . LYS A 1 257 ? 2.366   -19.752 20.062  1.00 17.01 ? 257 LYS B O   1 
ATOM   2040 C  CB  . LYS A 1 257 ? 4.236   -21.625 21.377  1.00 20.01 ? 257 LYS B CB  1 
ATOM   2041 C  CG  . LYS A 1 257 ? 3.828   -23.011 20.938  1.00 22.57 ? 257 LYS B CG  1 
ATOM   2042 C  CD  . LYS A 1 257 ? 3.321   -24.013 22.022  1.00 23.70 ? 257 LYS B CD  1 
ATOM   2043 C  CE  . LYS A 1 257 ? 4.248   -24.117 23.253  1.00 24.22 ? 257 LYS B CE  1 
ATOM   2044 N  NZ  . LYS A 1 257 ? 3.607   -25.102 24.237  1.00 23.49 ? 257 LYS B NZ  1 
ATOM   2045 N  N   . VAL A 1 258 ? 3.132   -20.758 18.134  1.00 16.65 ? 258 VAL B N   1 
ATOM   2046 C  CA  . VAL A 1 258 ? 1.803   -20.629 17.469  1.00 15.92 ? 258 VAL B CA  1 
ATOM   2047 C  C   . VAL A 1 258 ? 1.148   -22.000 17.610  1.00 15.38 ? 258 VAL B C   1 
ATOM   2048 O  O   . VAL A 1 258 ? 1.753   -23.025 17.206  1.00 16.88 ? 258 VAL B O   1 
ATOM   2049 C  CB  . VAL A 1 258 ? 1.937   -20.288 15.964  1.00 16.42 ? 258 VAL B CB  1 
ATOM   2050 C  CG1 . VAL A 1 258 ? 0.537   -20.043 15.396  1.00 16.32 ? 258 VAL B CG1 1 
ATOM   2051 C  CG2 . VAL A 1 258 ? 2.823   -19.045 15.839  1.00 18.34 ? 258 VAL B CG2 1 
ATOM   2052 N  N   . ARG A 1 259 ? -0.095  -22.058 18.137  1.00 14.64 ? 259 ARG B N   1 
ATOM   2053 C  CA  . ARG A 1 259 ? -0.767  -23.335 18.361  1.00 15.05 ? 259 ARG B CA  1 
ATOM   2054 C  C   . ARG A 1 259 ? -1.962  -23.425 17.374  1.00 15.32 ? 259 ARG B C   1 
ATOM   2055 O  O   . ARG A 1 259 ? -2.547  -22.384 16.961  1.00 14.78 ? 259 ARG B O   1 
ATOM   2056 C  CB  . ARG A 1 259 ? -1.283  -23.320 19.806  1.00 15.00 ? 259 ARG B CB  1 
ATOM   2057 C  CG  . ARG A 1 259 ? -0.125  -23.364 20.794  1.00 16.52 ? 259 ARG B CG  1 
ATOM   2058 C  CD  . ARG A 1 259 ? -0.676  -23.454 22.250  1.00 16.68 ? 259 ARG B CD  1 
ATOM   2059 N  NE  . ARG A 1 259 ? -1.319  -22.215 22.646  1.00 15.34 ? 259 ARG B NE  1 
ATOM   2060 C  CZ  . ARG A 1 259 ? -2.255  -22.141 23.601  1.00 14.54 ? 259 ARG B CZ  1 
ATOM   2061 N  NH1 . ARG A 1 259 ? -2.673  -23.256 24.244  1.00 16.27 ? 259 ARG B NH1 1 
ATOM   2062 N  NH2 . ARG A 1 259 ? -2.736  -20.956 23.930  1.00 14.41 ? 259 ARG B NH2 1 
ATOM   2063 N  N   . ALA A 1 260 ? -2.342  -24.640 17.076  1.00 13.92 ? 260 ALA B N   1 
ATOM   2064 C  CA  . ALA A 1 260 ? -3.535  -24.945 16.187  1.00 15.83 ? 260 ALA B CA  1 
ATOM   2065 C  C   . ALA A 1 260 ? -4.569  -25.618 17.030  1.00 15.59 ? 260 ALA B C   1 
ATOM   2066 O  O   . ALA A 1 260 ? -4.243  -26.512 17.904  1.00 15.18 ? 260 ALA B O   1 
ATOM   2067 C  CB  . ALA A 1 260 ? -3.145  -25.805 14.986  1.00 18.30 ? 260 ALA B CB  1 
ATOM   2068 N  N   . SER A 1 261 ? -5.812  -25.283 16.812  1.00 15.83 ? 261 SER B N   1 
ATOM   2069 C  CA  . SER A 1 261 ? -6.953  -25.943 17.456  1.00 15.09 ? 261 SER B CA  1 
ATOM   2070 C  C   . SER A 1 261 ? -7.363  -27.261 16.771  1.00 16.37 ? 261 SER B C   1 
ATOM   2071 O  O   . SER A 1 261 ? -8.364  -27.883 17.147  1.00 18.07 ? 261 SER B O   1 
ATOM   2072 C  CB  . SER A 1 261 ? -8.121  -24.904 17.536  1.00 13.46 ? 261 SER B CB  1 
ATOM   2073 O  OG  . SER A 1 261 ? -8.724  -24.855 16.232  1.00 13.95 ? 261 SER B OG  1 
ATOM   2074 N  N   . PHE A 1 262 ? -6.691  -27.603 15.674  1.00 16.25 ? 262 PHE B N   1 
ATOM   2075 C  CA  . PHE A 1 262 ? -7.117  -28.654 14.776  1.00 18.68 ? 262 PHE B CA  1 
ATOM   2076 C  C   . PHE A 1 262 ? -5.828  -29.313 14.212  1.00 18.34 ? 262 PHE B C   1 
ATOM   2077 O  O   . PHE A 1 262 ? -4.750  -28.723 14.240  1.00 19.37 ? 262 PHE B O   1 
ATOM   2078 C  CB  . PHE A 1 262 ? -7.965  -28.072 13.626  1.00 18.78 ? 262 PHE B CB  1 
ATOM   2079 C  CG  . PHE A 1 262 ? -7.156  -27.075 12.786  1.00 16.97 ? 262 PHE B CG  1 
ATOM   2080 C  CD1 . PHE A 1 262 ? -6.524  -27.494 11.614  1.00 19.72 ? 262 PHE B CD1 1 
ATOM   2081 C  CD2 . PHE A 1 262 ? -6.929  -25.740 13.238  1.00 15.67 ? 262 PHE B CD2 1 
ATOM   2082 C  CE1 . PHE A 1 262 ? -5.722  -26.644 10.861  1.00 21.10 ? 262 PHE B CE1 1 
ATOM   2083 C  CE2 . PHE A 1 262 ? -6.094  -24.895 12.478  1.00 16.50 ? 262 PHE B CE2 1 
ATOM   2084 C  CZ  . PHE A 1 262 ? -5.529  -25.316 11.296  1.00 17.35 ? 262 PHE B CZ  1 
ATOM   2085 N  N   . HIS A 1 263 ? -5.954  -30.561 13.772  1.00 23.79 ? 263 HIS B N   1 
ATOM   2086 C  CA  . HIS A 1 263 ? -4.883  -31.222 12.957  1.00 28.11 ? 263 HIS B CA  1 
ATOM   2087 C  C   . HIS A 1 263 ? -5.487  -32.236 12.072  1.00 38.22 ? 263 HIS B C   1 
ATOM   2088 O  O   . HIS A 1 263 ? -4.760  -32.989 11.374  1.00 34.04 ? 263 HIS B O   1 
ATOM   2089 C  CB  . HIS A 1 263 ? -3.804  -31.894 13.801  1.00 31.07 ? 263 HIS B CB  1 
ATOM   2090 C  CG  . HIS A 1 263 ? -4.298  -32.985 14.737  1.00 36.85 ? 263 HIS B CG  1 
ATOM   2091 N  ND1 . HIS A 1 263 ? -5.596  -33.286 14.919  1.00 39.43 ? 263 HIS B ND1 1 
ATOM   2092 C  CD2 . HIS A 1 263 ? -3.584  -33.805 15.614  1.00 38.40 ? 263 HIS B CD2 1 
ATOM   2093 C  CE1 . HIS A 1 263 ? -5.717  -34.245 15.859  1.00 42.26 ? 263 HIS B CE1 1 
ATOM   2094 N  NE2 . HIS A 1 263 ? -4.481  -34.559 16.286  1.00 44.83 ? 263 HIS B NE2 1 
ATOM   2095 O  OXT . HIS A 1 263 ? -6.718  -32.304 12.067  1.00 33.21 ? 263 HIS B OXT 1 
ATOM   2096 N  N   . SER B 1 6   ? -51.845 -43.191 28.375  1.00 39.11 ? 6   SER A N   1 
ATOM   2097 C  CA  . SER B 1 6   ? -50.539 -43.013 27.651  1.00 46.26 ? 6   SER A CA  1 
ATOM   2098 C  C   . SER B 1 6   ? -49.336 -42.904 28.605  1.00 34.38 ? 6   SER A C   1 
ATOM   2099 O  O   . SER B 1 6   ? -49.462 -42.815 29.858  1.00 33.32 ? 6   SER A O   1 
ATOM   2100 C  CB  . SER B 1 6   ? -50.557 -41.806 26.697  1.00 45.05 ? 6   SER A CB  1 
ATOM   2101 O  OG  . SER B 1 6   ? -51.854 -41.265 26.587  1.00 54.80 ? 6   SER A OG  1 
ATOM   2102 N  N   . TRP B 1 7   ? -48.160 -42.903 27.989  1.00 30.40 ? 7   TRP A N   1 
ATOM   2103 C  CA  . TRP B 1 7   ? -46.922 -43.081 28.741  1.00 26.41 ? 7   TRP A CA  1 
ATOM   2104 C  C   . TRP B 1 7   ? -46.591 -41.878 29.618  1.00 21.20 ? 7   TRP A C   1 
ATOM   2105 O  O   . TRP B 1 7   ? -47.026 -40.786 29.383  1.00 21.97 ? 7   TRP A O   1 
ATOM   2106 C  CB  . TRP B 1 7   ? -45.789 -43.427 27.769  1.00 21.90 ? 7   TRP A CB  1 
ATOM   2107 C  CG  . TRP B 1 7   ? -45.379 -42.224 26.970  1.00 22.19 ? 7   TRP A CG  1 
ATOM   2108 C  CD1 . TRP B 1 7   ? -45.822 -41.828 25.682  1.00 23.22 ? 7   TRP A CD1 1 
ATOM   2109 C  CD2 . TRP B 1 7   ? -44.343 -41.266 27.327  1.00 19.01 ? 7   TRP A CD2 1 
ATOM   2110 N  NE1 . TRP B 1 7   ? -45.138 -40.691 25.293  1.00 21.15 ? 7   TRP A NE1 1 
ATOM   2111 C  CE2 . TRP B 1 7   ? -44.254 -40.299 26.230  1.00 20.41 ? 7   TRP A CE2 1 
ATOM   2112 C  CE3 . TRP B 1 7   ? -43.480 -41.096 28.445  1.00 18.93 ? 7   TRP A CE3 1 
ATOM   2113 C  CZ2 . TRP B 1 7   ? -43.371 -39.246 26.272  1.00 18.46 ? 7   TRP A CZ2 1 
ATOM   2114 C  CZ3 . TRP B 1 7   ? -42.580 -40.045 28.440  1.00 17.82 ? 7   TRP A CZ3 1 
ATOM   2115 C  CH2 . TRP B 1 7   ? -42.528 -39.125 27.377  1.00 19.62 ? 7   TRP A CH2 1 
ATOM   2116 N  N   . GLY B 1 8   ? -45.816 -42.121 30.673  1.00 19.43 ? 8   GLY A N   1 
ATOM   2117 C  CA  . GLY B 1 8   ? -45.340 -41.044 31.570  1.00 18.40 ? 8   GLY A CA  1 
ATOM   2118 C  C   . GLY B 1 8   ? -44.342 -41.643 32.510  1.00 17.13 ? 8   GLY A C   1 
ATOM   2119 O  O   . GLY B 1 8   ? -43.569 -42.512 32.123  1.00 15.87 ? 8   GLY A O   1 
ATOM   2120 N  N   . TYR B 1 9   ? -44.308 -41.150 33.767  1.00 15.78 ? 9   TYR A N   1 
ATOM   2121 C  CA  . TYR B 1 9   ? -43.302 -41.557 34.709  1.00 16.85 ? 9   TYR A CA  1 
ATOM   2122 C  C   . TYR B 1 9   ? -43.900 -41.930 36.041  1.00 18.33 ? 9   TYR A C   1 
ATOM   2123 O  O   . TYR B 1 9   ? -43.227 -42.001 37.056  1.00 21.55 ? 9   TYR A O   1 
ATOM   2124 C  CB  . TYR B 1 9   ? -42.381 -40.335 34.926  1.00 15.27 ? 9   TYR A CB  1 
ATOM   2125 C  CG  . TYR B 1 9   ? -41.524 -40.017 33.714  1.00 13.60 ? 9   TYR A CG  1 
ATOM   2126 C  CD1 . TYR B 1 9   ? -40.317 -40.681 33.470  1.00 14.73 ? 9   TYR A CD1 1 
ATOM   2127 C  CD2 . TYR B 1 9   ? -41.934 -39.057 32.807  1.00 14.42 ? 9   TYR A CD2 1 
ATOM   2128 C  CE1 . TYR B 1 9   ? -39.545 -40.370 32.363  1.00 13.23 ? 9   TYR A CE1 1 
ATOM   2129 C  CE2 . TYR B 1 9   ? -41.173 -38.746 31.702  1.00 12.46 ? 9   TYR A CE2 1 
ATOM   2130 C  CZ  . TYR B 1 9   ? -39.986 -39.405 31.486  1.00 14.88 ? 9   TYR A CZ  1 
ATOM   2131 O  OH  . TYR B 1 9   ? -39.242 -39.084 30.383  1.00 14.22 ? 9   TYR A OH  1 
ATOM   2132 N  N   . ARG B 1 10  ? -45.222 -42.131 35.974  1.00 21.57 ? 10  ARG A N   1 
ATOM   2133 C  CA  . ARG B 1 10  ? -45.991 -42.680 37.140  1.00 25.36 ? 10  ARG A CA  1 
ATOM   2134 C  C   . ARG B 1 10  ? -45.851 -44.222 37.265  1.00 28.05 ? 10  ARG A C   1 
ATOM   2135 O  O   . ARG B 1 10  ? -45.245 -44.911 36.430  1.00 24.92 ? 10  ARG A O   1 
ATOM   2136 C  CB  . ARG B 1 10  ? -47.418 -42.188 37.005  1.00 27.63 ? 10  ARG A CB  1 
ATOM   2137 C  CG  . ARG B 1 10  ? -47.510 -40.664 37.090  1.00 28.38 ? 10  ARG A CG  1 
ATOM   2138 C  CD  . ARG B 1 10  ? -48.808 -40.051 36.593  1.00 38.20 ? 10  ARG A CD  1 
ATOM   2139 N  NE  . ARG B 1 10  ? -49.821 -40.013 37.643  1.00 44.49 ? 10  ARG A NE  1 
ATOM   2140 C  CZ  . ARG B 1 10  ? -51.082 -39.586 37.472  1.00 55.21 ? 10  ARG A CZ  1 
ATOM   2141 N  NH1 . ARG B 1 10  ? -51.505 -39.085 36.297  1.00 53.34 ? 10  ARG A NH1 1 
ATOM   2142 N  NH2 . ARG B 1 10  ? -51.926 -39.617 38.507  1.00 50.96 ? 10  ARG A NH2 1 
ATOM   2143 N  N   . GLU B 1 11  ? -46.389 -44.804 38.356  1.00 28.87 ? 11  GLU A N   1 
ATOM   2144 C  CA  . GLU B 1 11  ? -46.144 -46.219 38.603  1.00 29.77 ? 11  GLU A CA  1 
ATOM   2145 C  C   . GLU B 1 11  ? -46.635 -47.106 37.432  1.00 31.55 ? 11  GLU A C   1 
ATOM   2146 O  O   . GLU B 1 11  ? -45.962 -48.062 37.039  1.00 31.22 ? 11  GLU A O   1 
ATOM   2147 C  CB  . GLU B 1 11  ? -46.863 -46.613 39.912  1.00 39.02 ? 11  GLU A CB  1 
ATOM   2148 C  CG  . GLU B 1 11  ? -47.220 -48.101 40.076  1.00 45.30 ? 11  GLU A CG  1 
ATOM   2149 C  CD  . GLU B 1 11  ? -46.005 -49.024 40.131  1.00 59.57 ? 11  GLU A CD  1 
ATOM   2150 O  OE1 . GLU B 1 11  ? -46.171 -50.258 39.914  1.00 58.58 ? 11  GLU A OE1 1 
ATOM   2151 O  OE2 . GLU B 1 11  ? -44.880 -48.515 40.381  1.00 67.72 ? 11  GLU A OE2 1 
ATOM   2152 N  N   . HIS B 1 12  ? -47.795 -46.737 36.916  1.00 31.04 ? 12  HIS A N   1 
ATOM   2153 C  CA  . HIS B 1 12  ? -48.611 -47.511 35.978  1.00 36.66 ? 12  HIS A CA  1 
ATOM   2154 C  C   . HIS B 1 12  ? -48.248 -47.233 34.538  1.00 33.66 ? 12  HIS A C   1 
ATOM   2155 O  O   . HIS B 1 12  ? -48.559 -48.026 33.637  1.00 29.49 ? 12  HIS A O   1 
ATOM   2156 C  CB  . HIS B 1 12  ? -50.092 -47.152 36.228  1.00 40.96 ? 12  HIS A CB  1 
ATOM   2157 C  CG  . HIS B 1 12  ? -50.305 -45.688 36.675  1.00 52.71 ? 12  HIS A CG  1 
ATOM   2158 N  ND1 . HIS B 1 12  ? -50.060 -45.258 37.954  1.00 56.84 ? 12  HIS A ND1 1 
ATOM   2159 C  CD2 . HIS B 1 12  ? -50.738 -44.555 35.960  1.00 53.14 ? 12  HIS A CD2 1 
ATOM   2160 C  CE1 . HIS B 1 12  ? -50.348 -43.944 38.053  1.00 55.75 ? 12  HIS A CE1 1 
ATOM   2161 N  NE2 . HIS B 1 12  ? -50.758 -43.510 36.831  1.00 55.74 ? 12  HIS A NE2 1 
ATOM   2162 N  N   . ASN B 1 13  ? -47.540 -46.131 34.290  1.00 27.91 ? 13  ASN A N   1 
ATOM   2163 C  CA  . ASN B 1 13  ? -47.253 -45.758 32.872  1.00 25.58 ? 13  ASN A CA  1 
ATOM   2164 C  C   . ASN B 1 13  ? -45.745 -45.431 32.652  1.00 23.68 ? 13  ASN A C   1 
ATOM   2165 O  O   . ASN B 1 13  ? -45.338 -45.076 31.540  1.00 20.18 ? 13  ASN A O   1 
ATOM   2166 C  CB  . ASN B 1 13  ? -48.163 -44.611 32.366  1.00 23.78 ? 13  ASN A CB  1 
ATOM   2167 C  CG  . ASN B 1 13  ? -47.903 -43.295 33.050  1.00 22.90 ? 13  ASN A CG  1 
ATOM   2168 O  OD1 . ASN B 1 13  ? -47.009 -43.228 33.873  1.00 23.04 ? 13  ASN A OD1 1 
ATOM   2169 N  ND2 . ASN B 1 13  ? -48.595 -42.229 32.626  1.00 22.34 ? 13  ASN A ND2 1 
ATOM   2170 N  N   . GLY B 1 14  ? -44.965 -45.634 33.686  1.00 22.67 ? 14  GLY A N   1 
ATOM   2171 C  CA  . GLY B 1 14  ? -43.534 -45.246 33.740  1.00 21.23 ? 14  GLY A CA  1 
ATOM   2172 C  C   . GLY B 1 14  ? -42.649 -46.174 32.958  1.00 19.82 ? 14  GLY A C   1 
ATOM   2173 O  O   . GLY B 1 14  ? -43.121 -47.149 32.325  1.00 20.15 ? 14  GLY A O   1 
ATOM   2174 N  N   . PRO B 1 15  ? -41.324 -45.915 32.970  1.00 19.58 ? 15  PRO A N   1 
ATOM   2175 C  CA  . PRO B 1 15  ? -40.305 -46.566 32.174  1.00 18.36 ? 15  PRO A CA  1 
ATOM   2176 C  C   . PRO B 1 15  ? -40.373 -48.072 32.102  1.00 19.61 ? 15  PRO A C   1 
ATOM   2177 O  O   . PRO B 1 15  ? -40.194 -48.618 31.018  1.00 21.47 ? 15  PRO A O   1 
ATOM   2178 C  CB  . PRO B 1 15  ? -38.964 -46.026 32.757  1.00 17.45 ? 15  PRO A CB  1 
ATOM   2179 C  CG  . PRO B 1 15  ? -39.367 -44.620 33.128  1.00 18.34 ? 15  PRO A CG  1 
ATOM   2180 C  CD  . PRO B 1 15  ? -40.782 -44.706 33.653  1.00 19.36 ? 15  PRO A CD  1 
ATOM   2181 N  N   . ILE B 1 16  ? -40.695 -48.742 33.231  1.00 23.58 ? 16  ILE A N   1 
ATOM   2182 C  CA  . ILE B 1 16  ? -40.736 -50.223 33.215  1.00 23.69 ? 16  ILE A CA  1 
ATOM   2183 C  C   . ILE B 1 16  ? -41.931 -50.743 32.347  1.00 21.45 ? 16  ILE A C   1 
ATOM   2184 O  O   . ILE B 1 16  ? -41.887 -51.913 31.810  1.00 28.08 ? 16  ILE A O   1 
ATOM   2185 C  CB  . ILE B 1 16  ? -40.713 -50.829 34.652  1.00 27.07 ? 16  ILE A CB  1 
ATOM   2186 C  CG1 . ILE B 1 16  ? -40.307 -52.329 34.645  1.00 36.30 ? 16  ILE A CG1 1 
ATOM   2187 C  CG2 . ILE B 1 16  ? -42.068 -50.724 35.292  1.00 26.87 ? 16  ILE A CG2 1 
ATOM   2188 C  CD1 . ILE B 1 16  ? -38.819 -52.642 34.540  1.00 37.87 ? 16  ILE A CD1 1 
ATOM   2189 N  N   . HIS B 1 17  ? -42.929 -49.908 32.117  1.00 22.08 ? 17  HIS A N   1 
ATOM   2190 C  CA  . HIS B 1 17  ? -44.064 -50.284 31.274  1.00 22.74 ? 17  HIS A CA  1 
ATOM   2191 C  C   . HIS B 1 17  ? -43.930 -49.881 29.806  1.00 23.50 ? 17  HIS A C   1 
ATOM   2192 O  O   . HIS B 1 17  ? -44.815 -50.258 28.985  1.00 23.61 ? 17  HIS A O   1 
ATOM   2193 C  CB  . HIS B 1 17  ? -45.351 -49.677 31.839  1.00 25.30 ? 17  HIS A CB  1 
ATOM   2194 C  CG  . HIS B 1 17  ? -45.689 -50.214 33.204  1.00 32.92 ? 17  HIS A CG  1 
ATOM   2195 N  ND1 . HIS B 1 17  ? -46.046 -51.510 33.413  1.00 33.61 ? 17  HIS A ND1 1 
ATOM   2196 C  CD2 . HIS B 1 17  ? -45.668 -49.608 34.457  1.00 29.96 ? 17  HIS A CD2 1 
ATOM   2197 C  CE1 . HIS B 1 17  ? -46.214 -51.720 34.734  1.00 31.06 ? 17  HIS A CE1 1 
ATOM   2198 N  NE2 . HIS B 1 17  ? -46.020 -50.563 35.369  1.00 30.56 ? 17  HIS A NE2 1 
ATOM   2199 N  N   . TRP B 1 18  ? -42.886 -49.087 29.448  1.00 18.34 ? 18  TRP A N   1 
ATOM   2200 C  CA  . TRP B 1 18  ? -42.839 -48.590 28.068  1.00 18.01 ? 18  TRP A CA  1 
ATOM   2201 C  C   . TRP B 1 18  ? -42.756 -49.641 27.011  1.00 18.97 ? 18  TRP A C   1 
ATOM   2202 O  O   . TRP B 1 18  ? -43.321 -49.420 25.932  1.00 20.64 ? 18  TRP A O   1 
ATOM   2203 C  CB  . TRP B 1 18  ? -41.697 -47.544 27.901  1.00 16.53 ? 18  TRP A CB  1 
ATOM   2204 C  CG  . TRP B 1 18  ? -41.867 -46.280 28.683  1.00 15.20 ? 18  TRP A CG  1 
ATOM   2205 C  CD1 . TRP B 1 18  ? -42.983 -45.850 29.392  1.00 16.20 ? 18  TRP A CD1 1 
ATOM   2206 C  CD2 . TRP B 1 18  ? -40.871 -45.229 28.856  1.00 13.71 ? 18  TRP A CD2 1 
ATOM   2207 N  NE1 . TRP B 1 18  ? -42.744 -44.634 29.978  1.00 16.10 ? 18  TRP A NE1 1 
ATOM   2208 C  CE2 . TRP B 1 18  ? -41.494 -44.205 29.693  1.00 13.72 ? 18  TRP A CE2 1 
ATOM   2209 C  CE3 . TRP B 1 18  ? -39.573 -45.042 28.420  1.00 13.72 ? 18  TRP A CE3 1 
ATOM   2210 C  CZ2 . TRP B 1 18  ? -40.822 -43.056 30.064  1.00 12.33 ? 18  TRP A CZ2 1 
ATOM   2211 C  CZ3 . TRP B 1 18  ? -38.908 -43.879 28.795  1.00 12.51 ? 18  TRP A CZ3 1 
ATOM   2212 C  CH2 . TRP B 1 18  ? -39.518 -42.912 29.598  1.00 11.58 ? 18  TRP A CH2 1 
ATOM   2213 N  N   . LYS B 1 19  ? -42.100 -50.763 27.345  1.00 21.09 ? 19  LYS A N   1 
ATOM   2214 C  CA  . LYS B 1 19  ? -41.983 -51.943 26.425  1.00 23.98 ? 19  LYS A CA  1 
ATOM   2215 C  C   . LYS B 1 19  ? -43.371 -52.490 25.999  1.00 25.12 ? 19  LYS A C   1 
ATOM   2216 O  O   . LYS B 1 19  ? -43.486 -53.083 24.908  1.00 26.01 ? 19  LYS A O   1 
ATOM   2217 C  CB  . LYS B 1 19  ? -41.130 -53.040 27.011  1.00 23.76 ? 19  LYS A CB  1 
ATOM   2218 C  CG  . LYS B 1 19  ? -41.723 -53.597 28.297  1.00 25.71 ? 19  LYS A CG  1 
ATOM   2219 C  CD  . LYS B 1 19  ? -40.917 -54.751 28.877  1.00 29.59 ? 19  LYS A CD  1 
ATOM   2220 C  CE  . LYS B 1 19  ? -39.614 -54.304 29.598  1.00 33.79 ? 19  LYS A CE  1 
ATOM   2221 N  NZ  . LYS B 1 19  ? -39.623 -53.675 30.983  1.00 31.96 ? 19  LYS A NZ  1 
ATOM   2222 N  N   . GLU B 1 20  ? -44.418 -52.235 26.797  1.00 24.96 ? 20  GLU A N   1 
ATOM   2223 C  CA  . GLU B 1 20  ? -45.802 -52.594 26.472  1.00 26.50 ? 20  GLU A CA  1 
ATOM   2224 C  C   . GLU B 1 20  ? -46.368 -51.890 25.240  1.00 26.91 ? 20  GLU A C   1 
ATOM   2225 O  O   . GLU B 1 20  ? -47.232 -52.428 24.494  1.00 29.59 ? 20  GLU A O   1 
ATOM   2226 C  CB  . GLU B 1 20  ? -46.730 -52.369 27.692  1.00 25.66 ? 20  GLU A CB  1 
ATOM   2227 C  CG  . GLU B 1 20  ? -46.400 -53.287 28.849  1.00 29.87 ? 20  GLU A CG  1 
ATOM   2228 C  CD  . GLU B 1 20  ? -46.956 -52.819 30.204  1.00 29.97 ? 20  GLU A CD  1 
ATOM   2229 O  OE1 . GLU B 1 20  ? -48.035 -52.191 30.196  1.00 37.66 ? 20  GLU A OE1 1 
ATOM   2230 O  OE2 . GLU B 1 20  ? -46.311 -53.150 31.257  1.00 29.97 ? 20  GLU A OE2 1 
ATOM   2231 N  N   . PHE B 1 21  ? -45.955 -50.666 25.037  1.00 24.51 ? 21  PHE A N   1 
ATOM   2232 C  CA  . PHE B 1 21  ? -46.434 -49.920 23.926  1.00 27.00 ? 21  PHE A CA  1 
ATOM   2233 C  C   . PHE B 1 21  ? -45.405 -49.639 22.826  1.00 24.52 ? 21  PHE A C   1 
ATOM   2234 O  O   . PHE B 1 21  ? -45.785 -49.279 21.696  1.00 24.66 ? 21  PHE A O   1 
ATOM   2235 C  CB  . PHE B 1 21  ? -47.032 -48.652 24.519  1.00 37.47 ? 21  PHE A CB  1 
ATOM   2236 C  CG  . PHE B 1 21  ? -47.926 -48.952 25.686  1.00 44.47 ? 21  PHE A CG  1 
ATOM   2237 C  CD1 . PHE B 1 21  ? -47.460 -48.802 27.005  1.00 46.24 ? 21  PHE A CD1 1 
ATOM   2238 C  CD2 . PHE B 1 21  ? -49.212 -49.501 25.471  1.00 46.09 ? 21  PHE A CD2 1 
ATOM   2239 C  CE1 . PHE B 1 21  ? -48.287 -49.129 28.085  1.00 49.64 ? 21  PHE A CE1 1 
ATOM   2240 C  CE2 . PHE B 1 21  ? -50.041 -49.823 26.553  1.00 48.43 ? 21  PHE A CE2 1 
ATOM   2241 C  CZ  . PHE B 1 21  ? -49.574 -49.645 27.859  1.00 48.27 ? 21  PHE A CZ  1 
ATOM   2242 N  N   . PHE B 1 22  ? -44.141 -49.787 23.163  1.00 21.00 ? 22  PHE A N   1 
ATOM   2243 C  CA  . PHE B 1 22  ? -43.019 -49.356 22.294  1.00 24.56 ? 22  PHE A CA  1 
ATOM   2244 C  C   . PHE B 1 22  ? -42.036 -50.474 22.419  1.00 27.54 ? 22  PHE A C   1 
ATOM   2245 O  O   . PHE B 1 22  ? -41.046 -50.451 23.234  1.00 25.79 ? 22  PHE A O   1 
ATOM   2246 C  CB  . PHE B 1 22  ? -42.416 -47.995 22.761  1.00 24.78 ? 22  PHE A CB  1 
ATOM   2247 C  CG  . PHE B 1 22  ? -43.417 -46.909 22.787  1.00 23.44 ? 22  PHE A CG  1 
ATOM   2248 C  CD1 . PHE B 1 22  ? -43.756 -46.278 21.622  1.00 25.98 ? 22  PHE A CD1 1 
ATOM   2249 C  CD2 . PHE B 1 22  ? -44.100 -46.604 23.945  1.00 23.96 ? 22  PHE A CD2 1 
ATOM   2250 C  CE1 . PHE B 1 22  ? -44.744 -45.326 21.577  1.00 26.24 ? 22  PHE A CE1 1 
ATOM   2251 C  CE2 . PHE B 1 22  ? -45.107 -45.612 23.927  1.00 23.66 ? 22  PHE A CE2 1 
ATOM   2252 C  CZ  . PHE B 1 22  ? -45.437 -44.990 22.739  1.00 23.39 ? 22  PHE A CZ  1 
ATOM   2253 N  N   . PRO B 1 23  ? -42.273 -51.489 21.591  1.00 30.66 ? 23  PRO A N   1 
ATOM   2254 C  CA  . PRO B 1 23  ? -41.393 -52.635 21.604  1.00 35.15 ? 23  PRO A CA  1 
ATOM   2255 C  C   . PRO B 1 23  ? -39.867 -52.323 21.534  1.00 33.22 ? 23  PRO A C   1 
ATOM   2256 O  O   . PRO B 1 23  ? -39.064 -53.003 22.209  1.00 28.14 ? 23  PRO A O   1 
ATOM   2257 C  CB  . PRO B 1 23  ? -41.922 -53.500 20.435  1.00 30.89 ? 23  PRO A CB  1 
ATOM   2258 C  CG  . PRO B 1 23  ? -42.749 -52.576 19.564  1.00 33.46 ? 23  PRO A CG  1 
ATOM   2259 C  CD  . PRO B 1 23  ? -43.258 -51.506 20.482  1.00 32.75 ? 23  PRO A CD  1 
ATOM   2260 N  N   . ILE B 1 24  ? -39.472 -51.266 20.815  1.00 23.34 ? 24  ILE A N   1 
ATOM   2261 C  CA  . ILE B 1 24  ? -38.025 -50.966 20.714  1.00 20.51 ? 24  ILE A CA  1 
ATOM   2262 C  C   . ILE B 1 24  ? -37.378 -50.599 22.114  1.00 18.23 ? 24  ILE A C   1 
ATOM   2263 O  O   . ILE B 1 24  ? -36.147 -50.522 22.258  1.00 18.61 ? 24  ILE A O   1 
ATOM   2264 C  CB  . ILE B 1 24  ? -37.814 -49.870 19.669  1.00 17.41 ? 24  ILE A CB  1 
ATOM   2265 C  CG1 . ILE B 1 24  ? -36.330 -49.844 19.206  1.00 17.99 ? 24  ILE A CG1 1 
ATOM   2266 C  CG2 . ILE B 1 24  ? -38.261 -48.537 20.277  1.00 17.91 ? 24  ILE A CG2 1 
ATOM   2267 C  CD1 . ILE B 1 24  ? -35.946 -51.125 18.474  1.00 21.74 ? 24  ILE A CD1 1 
ATOM   2268 N  N   . ALA B 1 25  ? -38.248 -50.473 23.144  1.00 18.71 ? 25  ALA A N   1 
ATOM   2269 C  CA  . ALA B 1 25  ? -37.692 -50.174 24.467  1.00 18.44 ? 25  ALA A CA  1 
ATOM   2270 C  C   . ALA B 1 25  ? -36.623 -51.136 24.949  1.00 18.16 ? 25  ALA A C   1 
ATOM   2271 O  O   . ALA B 1 25  ? -35.729 -50.811 25.686  1.00 19.21 ? 25  ALA A O   1 
ATOM   2272 C  CB  . ALA B 1 25  ? -38.812 -50.137 25.525  1.00 19.37 ? 25  ALA A CB  1 
ATOM   2273 N  N   . ASP B 1 26  ? -36.687 -52.401 24.465  1.00 19.58 ? 26  ASP A N   1 
ATOM   2274 C  CA  . ASP B 1 26  ? -35.660 -53.382 24.831  1.00 20.50 ? 26  ASP A CA  1 
ATOM   2275 C  C   . ASP B 1 26  ? -34.674 -53.694 23.685  1.00 21.95 ? 26  ASP A C   1 
ATOM   2276 O  O   . ASP B 1 26  ? -34.059 -54.770 23.622  1.00 22.89 ? 26  ASP A O   1 
ATOM   2277 C  CB  . ASP B 1 26  ? -36.393 -54.701 25.235  1.00 23.66 ? 26  ASP A CB  1 
ATOM   2278 C  CG  . ASP B 1 26  ? -37.263 -54.528 26.452  1.00 30.58 ? 26  ASP A CG  1 
ATOM   2279 O  OD1 . ASP B 1 26  ? -36.781 -53.978 27.457  1.00 31.87 ? 26  ASP A OD1 1 
ATOM   2280 O  OD2 . ASP B 1 26  ? -38.432 -54.928 26.387  1.00 30.60 ? 26  ASP A OD2 1 
ATOM   2281 N  N   . GLY B 1 27  ? -34.550 -52.737 22.765  1.00 19.82 ? 27  GLY A N   1 
ATOM   2282 C  CA  . GLY B 1 27  ? -33.601 -52.771 21.656  1.00 20.57 ? 27  GLY A CA  1 
ATOM   2283 C  C   . GLY B 1 27  ? -32.136 -52.821 21.978  1.00 19.69 ? 27  GLY A C   1 
ATOM   2284 O  O   . GLY B 1 27  ? -31.720 -52.803 23.149  1.00 21.03 ? 27  GLY A O   1 
ATOM   2285 N  N   . ASP B 1 28  ? -31.329 -52.888 20.911  1.00 19.36 ? 28  ASP A N   1 
ATOM   2286 C  CA  . ASP B 1 28  ? -29.886 -52.945 21.027  1.00 19.12 ? 28  ASP A CA  1 
ATOM   2287 C  C   . ASP B 1 28  ? -29.187 -51.610 21.113  1.00 13.50 ? 28  ASP A C   1 
ATOM   2288 O  O   . ASP B 1 28  ? -27.974 -51.580 21.371  1.00 15.46 ? 28  ASP A O   1 
ATOM   2289 C  CB  . ASP B 1 28  ? -29.328 -53.717 19.815  1.00 19.49 ? 28  ASP A CB  1 
ATOM   2290 C  CG  . ASP B 1 28  ? -29.692 -55.242 19.868  1.00 27.75 ? 28  ASP A CG  1 
ATOM   2291 O  OD1 . ASP B 1 28  ? -29.957 -55.782 20.942  1.00 31.41 ? 28  ASP A OD1 1 
ATOM   2292 O  OD2 . ASP B 1 28  ? -29.716 -55.838 18.812  1.00 30.05 ? 28  ASP A OD2 1 
ATOM   2293 N  N   . GLN B 1 29  ? -29.933 -50.500 20.783  1.00 14.35 ? 29  GLN A N   1 
ATOM   2294 C  CA  . GLN B 1 29  ? -29.224 -49.198 20.822  1.00 14.41 ? 29  GLN A CA  1 
ATOM   2295 C  C   . GLN B 1 29  ? -30.096 -48.242 21.586  1.00 14.55 ? 29  GLN A C   1 
ATOM   2296 O  O   . GLN B 1 29  ? -30.326 -47.084 21.145  1.00 12.87 ? 29  GLN A O   1 
ATOM   2297 C  CB  . GLN B 1 29  ? -28.893 -48.647 19.401  1.00 14.51 ? 29  GLN A CB  1 
ATOM   2298 C  CG  . GLN B 1 29  ? -28.074 -49.681 18.548  1.00 20.44 ? 29  GLN A CG  1 
ATOM   2299 C  CD  . GLN B 1 29  ? -27.125 -49.006 17.560  1.00 21.37 ? 29  GLN A CD  1 
ATOM   2300 O  OE1 . GLN B 1 29  ? -27.410 -47.876 17.140  1.00 18.41 ? 29  GLN A OE1 1 
ATOM   2301 N  NE2 . GLN B 1 29  ? -25.948 -49.669 17.220  1.00 28.51 ? 29  GLN A NE2 1 
ATOM   2302 N  N   . GLN B 1 30  ? -30.423 -48.589 22.834  1.00 14.49 ? 30  GLN A N   1 
ATOM   2303 C  CA  . GLN B 1 30  ? -31.257 -47.735 23.698  1.00 13.04 ? 30  GLN A CA  1 
ATOM   2304 C  C   . GLN B 1 30  ? -30.393 -46.850 24.574  1.00 12.10 ? 30  GLN A C   1 
ATOM   2305 O  O   . GLN B 1 30  ? -29.216 -47.089 24.860  1.00 12.50 ? 30  GLN A O   1 
ATOM   2306 C  CB  . GLN B 1 30  ? -32.187 -48.647 24.526  1.00 12.67 ? 30  GLN A CB  1 
ATOM   2307 C  CG  . GLN B 1 30  ? -33.272 -49.282 23.689  1.00 12.94 ? 30  GLN A CG  1 
ATOM   2308 C  CD  . GLN B 1 30  ? -34.296 -48.227 23.233  1.00 13.54 ? 30  GLN A CD  1 
ATOM   2309 O  OE1 . GLN B 1 30  ? -35.029 -47.629 23.973  1.00 13.44 ? 30  GLN A OE1 1 
ATOM   2310 N  NE2 . GLN B 1 30  ? -34.279 -47.957 21.929  1.00 13.30 ? 30  GLN A NE2 1 
ATOM   2311 N  N   . SER B 1 31  ? -31.049 -45.742 24.995  1.00 11.67 ? 31  SER A N   1 
ATOM   2312 C  CA  . SER B 1 31  ? -30.422 -44.732 25.787  1.00 11.23 ? 31  SER A CA  1 
ATOM   2313 C  C   . SER B 1 31  ? -31.397 -44.429 26.916  1.00 10.24 ? 31  SER A C   1 
ATOM   2314 O  O   . SER B 1 31  ? -32.574 -44.730 26.830  1.00 11.03 ? 31  SER A O   1 
ATOM   2315 C  CB  . SER B 1 31  ? -30.200 -43.471 24.943  1.00 10.18 ? 31  SER A CB  1 
ATOM   2316 O  OG  . SER B 1 31  ? -29.187 -43.655 23.960  1.00 10.45 ? 31  SER A OG  1 
ATOM   2317 N  N   . PRO B 1 32  ? -30.868 -43.811 28.008  1.00 10.28 ? 32  PRO A N   1 
ATOM   2318 C  CA  . PRO B 1 32  ? -29.478 -43.499 28.232  1.00 10.90 ? 32  PRO A CA  1 
ATOM   2319 C  C   . PRO B 1 32  ? -28.668 -44.734 28.646  1.00 12.32 ? 32  PRO A C   1 
ATOM   2320 O  O   . PRO B 1 32  ? -29.190 -45.862 28.555  1.00 12.36 ? 32  PRO A O   1 
ATOM   2321 C  CB  . PRO B 1 32  ? -29.554 -42.528 29.465  1.00 10.67 ? 32  PRO A CB  1 
ATOM   2322 C  CG  . PRO B 1 32  ? -30.719 -43.044 30.226  1.00 12.84 ? 32  PRO A CG  1 
ATOM   2323 C  CD  . PRO B 1 32  ? -31.721 -43.528 29.201  1.00 12.69 ? 32  PRO A CD  1 
ATOM   2324 N  N   . ILE B 1 33  ? -27.408 -44.529 28.943  1.00 10.89 ? 33  ILE A N   1 
ATOM   2325 C  CA  . ILE B 1 33  ? -26.483 -45.660 29.281  1.00 13.87 ? 33  ILE A CA  1 
ATOM   2326 C  C   . ILE B 1 33  ? -25.625 -45.255 30.475  1.00 13.56 ? 33  ILE A C   1 
ATOM   2327 O  O   . ILE B 1 33  ? -25.602 -44.053 30.929  1.00 13.04 ? 33  ILE A O   1 
ATOM   2328 C  CB  . ILE B 1 33  ? -25.526 -46.023 28.073  1.00 13.98 ? 33  ILE A CB  1 
ATOM   2329 C  CG1 . ILE B 1 33  ? -24.698 -44.797 27.726  1.00 13.75 ? 33  ILE A CG1 1 
ATOM   2330 C  CG2 . ILE B 1 33  ? -26.348 -46.488 26.866  1.00 16.72 ? 33  ILE A CG2 1 
ATOM   2331 C  CD1 . ILE B 1 33  ? -23.478 -45.181 26.928  1.00 15.01 ? 33  ILE A CD1 1 
ATOM   2332 N  N   . GLU B 1 34  ? -24.965 -46.274 31.061  1.00 14.89 ? 34  GLU A N   1 
ATOM   2333 C  CA  . GLU B 1 34  ? -23.861 -46.033 31.964  1.00 13.62 ? 34  GLU A CA  1 
ATOM   2334 C  C   . GLU B 1 34  ? -22.536 -45.918 31.190  1.00 12.36 ? 34  GLU A C   1 
ATOM   2335 O  O   . GLU B 1 34  ? -22.248 -46.739 30.294  1.00 15.40 ? 34  GLU A O   1 
ATOM   2336 C  CB  . GLU B 1 34  ? -23.801 -47.242 32.920  1.00 14.43 ? 34  GLU A CB  1 
ATOM   2337 C  CG  . GLU B 1 34  ? -24.936 -47.304 33.963  1.00 16.45 ? 34  GLU A CG  1 
ATOM   2338 C  CD  . GLU B 1 34  ? -24.624 -48.399 35.004  1.00 19.47 ? 34  GLU A CD  1 
ATOM   2339 O  OE1 . GLU B 1 34  ? -23.962 -48.054 36.020  1.00 22.94 ? 34  GLU A OE1 1 
ATOM   2340 O  OE2 . GLU B 1 34  ? -25.017 -49.546 34.793  1.00 17.37 ? 34  GLU A OE2 1 
ATOM   2341 N  N   . ILE B 1 35  ? -21.707 -44.948 31.539  1.00 16.00 ? 35  ILE A N   1 
ATOM   2342 C  CA  . ILE B 1 35  ? -20.434 -44.749 30.829  1.00 16.63 ? 35  ILE A CA  1 
ATOM   2343 C  C   . ILE B 1 35  ? -19.398 -45.263 31.875  1.00 17.82 ? 35  ILE A C   1 
ATOM   2344 O  O   . ILE B 1 35  ? -19.260 -44.626 32.905  1.00 17.33 ? 35  ILE A O   1 
ATOM   2345 C  CB  . ILE B 1 35  ? -20.255 -43.293 30.445  1.00 18.26 ? 35  ILE A CB  1 
ATOM   2346 C  CG1 . ILE B 1 35  ? -21.371 -42.945 29.431  1.00 18.60 ? 35  ILE A CG1 1 
ATOM   2347 C  CG2 . ILE B 1 35  ? -18.830 -43.013 29.863  1.00 19.46 ? 35  ILE A CG2 1 
ATOM   2348 C  CD1 . ILE B 1 35  ? -21.414 -41.477 29.063  1.00 20.81 ? 35  ILE A CD1 1 
ATOM   2349 N  N   . LYS B 1 36  ? -18.699 -46.343 31.489  1.00 18.58 ? 36  LYS A N   1 
ATOM   2350 C  CA  . LYS B 1 36  ? -17.551 -46.935 32.248  1.00 18.68 ? 36  LYS A CA  1 
ATOM   2351 C  C   . LYS B 1 36  ? -16.284 -46.333 31.638  1.00 18.85 ? 36  LYS A C   1 
ATOM   2352 O  O   . LYS B 1 36  ? -15.802 -46.788 30.572  1.00 22.87 ? 36  LYS A O   1 
ATOM   2353 C  CB  . LYS B 1 36  ? -17.588 -48.474 32.187  1.00 19.64 ? 36  LYS A CB  1 
ATOM   2354 C  CG  . LYS B 1 36  ? -16.450 -49.090 33.040  1.00 21.84 ? 36  LYS A CG  1 
ATOM   2355 C  CD  . LYS B 1 36  ? -16.697 -50.573 33.223  1.00 20.53 ? 36  LYS A CD  1 
ATOM   2356 C  CE  . LYS B 1 36  ? -17.828 -50.905 34.241  1.00 22.85 ? 36  LYS A CE  1 
ATOM   2357 N  NZ  . LYS B 1 36  ? -17.937 -52.385 34.703  1.00 20.72 ? 36  LYS A NZ  1 
ATOM   2358 N  N   . THR B 1 37  ? -15.755 -45.288 32.243  1.00 19.18 ? 37  THR A N   1 
ATOM   2359 C  CA  . THR B 1 37  ? -14.650 -44.555 31.630  1.00 23.42 ? 37  THR A CA  1 
ATOM   2360 C  C   . THR B 1 37  ? -13.390 -45.386 31.366  1.00 24.12 ? 37  THR A C   1 
ATOM   2361 O  O   . THR B 1 37  ? -12.610 -45.094 30.407  1.00 26.41 ? 37  THR A O   1 
ATOM   2362 C  CB  . THR B 1 37  ? -14.291 -43.249 32.353  1.00 23.30 ? 37  THR A CB  1 
ATOM   2363 O  OG1 . THR B 1 37  ? -13.787 -43.547 33.694  1.00 24.79 ? 37  THR A OG1 1 
ATOM   2364 C  CG2 . THR B 1 37  ? -15.568 -42.355 32.421  1.00 22.56 ? 37  THR A CG2 1 
ATOM   2365 N  N   . LYS B 1 38  ? -13.172 -46.410 32.201  1.00 26.61 ? 38  LYS A N   1 
ATOM   2366 C  CA  . LYS B 1 38  ? -11.974 -47.252 31.998  1.00 31.02 ? 38  LYS A CA  1 
ATOM   2367 C  C   . LYS B 1 38  ? -12.055 -47.990 30.670  1.00 32.01 ? 38  LYS A C   1 
ATOM   2368 O  O   . LYS B 1 38  ? -11.031 -48.383 30.102  1.00 34.80 ? 38  LYS A O   1 
ATOM   2369 C  CB  . LYS B 1 38  ? -11.702 -48.211 33.189  1.00 34.33 ? 38  LYS A CB  1 
ATOM   2370 C  CG  . LYS B 1 38  ? -12.695 -49.327 33.347  1.00 39.95 ? 38  LYS A CG  1 
ATOM   2371 C  CD  . LYS B 1 38  ? -12.240 -50.651 32.741  1.00 43.23 ? 38  LYS A CD  1 
ATOM   2372 C  CE  . LYS B 1 38  ? -13.020 -51.827 33.325  1.00 50.18 ? 38  LYS A CE  1 
ATOM   2373 N  NZ  . LYS B 1 38  ? -12.894 -53.066 32.495  1.00 47.02 ? 38  LYS A NZ  1 
ATOM   2374 N  N   . GLU B 1 39  ? -13.264 -48.149 30.145  1.00 28.48 ? 39  GLU A N   1 
ATOM   2375 C  CA  . GLU B 1 39  ? -13.430 -48.810 28.876  1.00 33.69 ? 39  GLU A CA  1 
ATOM   2376 C  C   . GLU B 1 39  ? -13.695 -47.903 27.696  1.00 28.42 ? 39  GLU A C   1 
ATOM   2377 O  O   . GLU B 1 39  ? -14.027 -48.395 26.601  1.00 35.79 ? 39  GLU A O   1 
ATOM   2378 C  CB  . GLU B 1 39  ? -14.505 -49.903 28.976  1.00 35.70 ? 39  GLU A CB  1 
ATOM   2379 C  CG  . GLU B 1 39  ? -13.958 -51.127 29.689  1.00 46.64 ? 39  GLU A CG  1 
ATOM   2380 C  CD  . GLU B 1 39  ? -15.029 -52.148 30.028  1.00 49.63 ? 39  GLU A CD  1 
ATOM   2381 O  OE1 . GLU B 1 39  ? -14.672 -53.214 30.607  1.00 48.41 ? 39  GLU A OE1 1 
ATOM   2382 O  OE2 . GLU B 1 39  ? -16.208 -51.865 29.720  1.00 48.28 ? 39  GLU A OE2 1 
ATOM   2383 N  N   . VAL B 1 40  ? -13.552 -46.601 27.899  1.00 25.52 ? 40  VAL A N   1 
ATOM   2384 C  CA  . VAL B 1 40  ? -13.778 -45.651 26.799  1.00 23.46 ? 40  VAL A CA  1 
ATOM   2385 C  C   . VAL B 1 40  ? -12.461 -45.438 26.057  1.00 28.12 ? 40  VAL A C   1 
ATOM   2386 O  O   . VAL B 1 40  ? -11.409 -45.312 26.696  1.00 28.03 ? 40  VAL A O   1 
ATOM   2387 C  CB  . VAL B 1 40  ? -14.256 -44.327 27.391  1.00 21.35 ? 40  VAL A CB  1 
ATOM   2388 C  CG1 . VAL B 1 40  ? -14.157 -43.218 26.350  1.00 22.44 ? 40  VAL A CG1 1 
ATOM   2389 C  CG2 . VAL B 1 40  ? -15.683 -44.490 27.834  1.00 21.09 ? 40  VAL A CG2 1 
ATOM   2390 N  N   . LYS B 1 41  ? -12.480 -45.361 24.727  1.00 29.86 ? 41  LYS A N   1 
ATOM   2391 C  CA  . LYS B 1 41  ? -11.219 -44.990 24.013  1.00 28.68 ? 41  LYS A CA  1 
ATOM   2392 C  C   . LYS B 1 41  ? -11.256 -43.550 23.499  1.00 25.44 ? 41  LYS A C   1 
ATOM   2393 O  O   . LYS B 1 41  ? -12.280 -43.177 22.945  1.00 24.83 ? 41  LYS A O   1 
ATOM   2394 C  CB  . LYS B 1 41  ? -11.028 -45.944 22.823  1.00 36.40 ? 41  LYS A CB  1 
ATOM   2395 C  CG  . LYS B 1 41  ? -10.571 -47.354 23.246  1.00 44.59 ? 41  LYS A CG  1 
ATOM   2396 C  CD  . LYS B 1 41  ? -9.958  -48.161 22.097  1.00 47.85 ? 41  LYS A CD  1 
ATOM   2397 C  CE  . LYS B 1 41  ? -8.746  -47.435 21.514  1.00 54.85 ? 41  LYS A CE  1 
ATOM   2398 N  NZ  . LYS B 1 41  ? -8.627  -47.600 20.033  1.00 56.93 ? 41  LYS A NZ  1 
ATOM   2399 N  N   . TYR B 1 42  ? -10.214 -42.745 23.726  1.00 23.08 ? 42  TYR A N   1 
ATOM   2400 C  CA  . TYR B 1 42  ? -10.038 -41.453 23.046  1.00 25.22 ? 42  TYR A CA  1 
ATOM   2401 C  C   . TYR B 1 42  ? -10.024 -41.739 21.542  1.00 26.22 ? 42  TYR A C   1 
ATOM   2402 O  O   . TYR B 1 42  ? -9.411  -42.724 21.076  1.00 27.32 ? 42  TYR A O   1 
ATOM   2403 C  CB  . TYR B 1 42  ? -8.702  -40.814 23.483  1.00 28.38 ? 42  TYR A CB  1 
ATOM   2404 C  CG  . TYR B 1 42  ? -8.271  -39.685 22.580  1.00 32.86 ? 42  TYR A CG  1 
ATOM   2405 C  CD1 . TYR B 1 42  ? -8.945  -38.469 22.591  1.00 26.80 ? 42  TYR A CD1 1 
ATOM   2406 C  CD2 . TYR B 1 42  ? -7.168  -39.826 21.697  1.00 32.55 ? 42  TYR A CD2 1 
ATOM   2407 C  CE1 . TYR B 1 42  ? -8.578  -37.420 21.754  1.00 28.87 ? 42  TYR A CE1 1 
ATOM   2408 C  CE2 . TYR B 1 42  ? -6.792  -38.773 20.874  1.00 36.22 ? 42  TYR A CE2 1 
ATOM   2409 C  CZ  . TYR B 1 42  ? -7.500  -37.564 20.923  1.00 32.35 ? 42  TYR A CZ  1 
ATOM   2410 O  OH  . TYR B 1 42  ? -7.153  -36.496 20.113  1.00 39.78 ? 42  TYR A OH  1 
ATOM   2411 N  N   . ASP B 1 43  ? -10.705 -40.899 20.753  1.00 24.79 ? 43  ASP A N   1 
ATOM   2412 C  CA  . ASP B 1 43  ? -10.715 -41.036 19.297  1.00 23.77 ? 43  ASP A CA  1 
ATOM   2413 C  C   . ASP B 1 43  ? -10.164 -39.752 18.677  1.00 29.45 ? 43  ASP A C   1 
ATOM   2414 O  O   . ASP B 1 43  ? -10.831 -38.710 18.669  1.00 24.98 ? 43  ASP A O   1 
ATOM   2415 C  CB  . ASP B 1 43  ? -12.151 -41.339 18.790  1.00 25.58 ? 43  ASP A CB  1 
ATOM   2416 C  CG  . ASP B 1 43  ? -12.208 -41.572 17.287  1.00 26.72 ? 43  ASP A CG  1 
ATOM   2417 O  OD1 . ASP B 1 43  ? -11.176 -41.311 16.631  1.00 29.18 ? 43  ASP A OD1 1 
ATOM   2418 O  OD2 . ASP B 1 43  ? -13.291 -41.939 16.775  1.00 28.97 ? 43  ASP A OD2 1 
ATOM   2419 N  N   . SER B 1 44  ? -8.904  -39.807 18.212  1.00 23.73 ? 44  SER A N   1 
ATOM   2420 C  CA  . SER B 1 44  ? -8.288  -38.641 17.642  1.00 25.02 ? 44  SER A CA  1 
ATOM   2421 C  C   . SER B 1 44  ? -8.855  -38.176 16.316  1.00 29.01 ? 44  SER A C   1 
ATOM   2422 O  O   . SER B 1 44  ? -8.577  -37.036 15.930  1.00 29.37 ? 44  SER A O   1 
ATOM   2423 C  CB  . SER B 1 44  ? -6.780  -38.948 17.505  1.00 26.92 ? 44  SER A CB  1 
ATOM   2424 O  OG  . SER B 1 44  ? -6.637  -40.019 16.584  1.00 33.47 ? 44  SER A OG  1 
ATOM   2425 N  N   . SER B 1 45  ? -9.650  -39.044 15.641  1.00 27.69 ? 45  SER A N   1 
ATOM   2426 C  CA  . SER B 1 45  ? -10.392 -38.730 14.445  1.00 27.31 ? 45  SER A CA  1 
ATOM   2427 C  C   . SER B 1 45  ? -11.667 -37.803 14.645  1.00 25.87 ? 45  SER A C   1 
ATOM   2428 O  O   . SER B 1 45  ? -12.213 -37.192 13.684  1.00 27.88 ? 45  SER A O   1 
ATOM   2429 C  CB  . SER B 1 45  ? -10.739 -40.041 13.683  1.00 28.48 ? 45  SER A CB  1 
ATOM   2430 O  OG  . SER B 1 45  ? -11.958 -40.608 14.077  1.00 33.07 ? 45  SER A OG  1 
ATOM   2431 N  N   . LEU B 1 46  ? -12.167 -37.687 15.860  1.00 24.66 ? 46  LEU A N   1 
ATOM   2432 C  CA  . LEU B 1 46  ? -13.268 -36.751 16.070  1.00 22.27 ? 46  LEU A CA  1 
ATOM   2433 C  C   . LEU B 1 46  ? -12.784 -35.315 15.765  1.00 19.95 ? 46  LEU A C   1 
ATOM   2434 O  O   . LEU B 1 46  ? -11.665 -34.916 16.159  1.00 23.83 ? 46  LEU A O   1 
ATOM   2435 C  CB  . LEU B 1 46  ? -13.731 -36.839 17.539  1.00 19.44 ? 46  LEU A CB  1 
ATOM   2436 C  CG  . LEU B 1 46  ? -14.366 -38.176 17.903  1.00 20.43 ? 46  LEU A CG  1 
ATOM   2437 C  CD1 . LEU B 1 46  ? -14.391 -38.251 19.434  1.00 19.88 ? 46  LEU A CD1 1 
ATOM   2438 C  CD2 . LEU B 1 46  ? -15.807 -38.308 17.336  1.00 21.91 ? 46  LEU A CD2 1 
ATOM   2439 N  N   . ARG B 1 47  ? -13.621 -34.562 15.018  1.00 22.90 ? 47  ARG A N   1 
ATOM   2440 C  CA  . ARG B 1 47  ? -13.256 -33.229 14.679  1.00 21.11 ? 47  ARG A CA  1 
ATOM   2441 C  C   . ARG B 1 47  ? -13.667 -32.253 15.767  1.00 20.51 ? 47  ARG A C   1 
ATOM   2442 O  O   . ARG B 1 47  ? -14.491 -32.619 16.648  1.00 23.10 ? 47  ARG A O   1 
ATOM   2443 C  CB  . ARG B 1 47  ? -13.892 -32.802 13.300  1.00 23.47 ? 47  ARG A CB  1 
ATOM   2444 C  CG  . ARG B 1 47  ? -13.715 -33.757 12.085  1.00 32.39 ? 47  ARG A CG  1 
ATOM   2445 C  CD  . ARG B 1 47  ? -12.229 -34.051 11.704  1.00 42.36 ? 47  ARG A CD  1 
ATOM   2446 N  NE  . ARG B 1 47  ? -11.398 -34.438 12.868  1.00 51.47 ? 47  ARG A NE  1 
ATOM   2447 C  CZ  . ARG B 1 47  ? -10.064 -34.397 12.954  1.00 49.53 ? 47  ARG A CZ  1 
ATOM   2448 N  NH1 . ARG B 1 47  ? -9.341  -33.981 11.919  1.00 57.80 ? 47  ARG A NH1 1 
ATOM   2449 N  NH2 . ARG B 1 47  ? -9.461  -34.758 14.091  1.00 46.14 ? 47  ARG A NH2 1 
ATOM   2450 N  N   . PRO B 1 48  ? -13.097 -31.039 15.793  1.00 18.92 ? 48  PRO A N   1 
ATOM   2451 C  CA  . PRO B 1 48  ? -13.596 -30.101 16.803  1.00 17.60 ? 48  PRO A CA  1 
ATOM   2452 C  C   . PRO B 1 48  ? -15.126 -29.956 16.736  1.00 19.16 ? 48  PRO A C   1 
ATOM   2453 O  O   . PRO B 1 48  ? -15.712 -29.820 15.638  1.00 18.33 ? 48  PRO A O   1 
ATOM   2454 C  CB  . PRO B 1 48  ? -12.893 -28.733 16.439  1.00 17.75 ? 48  PRO A CB  1 
ATOM   2455 C  CG  . PRO B 1 48  ? -11.643 -29.235 15.757  1.00 19.61 ? 48  PRO A CG  1 
ATOM   2456 C  CD  . PRO B 1 48  ? -12.073 -30.413 14.905  1.00 19.47 ? 48  PRO A CD  1 
ATOM   2457 N  N   . LEU B 1 49  ? -15.774 -29.893 17.906  1.00 20.36 ? 49  LEU A N   1 
ATOM   2458 C  CA  . LEU B 1 49  ? -17.229 -29.567 17.950  1.00 18.36 ? 49  LEU A CA  1 
ATOM   2459 C  C   . LEU B 1 49  ? -17.454 -28.095 17.606  1.00 18.87 ? 49  LEU A C   1 
ATOM   2460 O  O   . LEU B 1 49  ? -16.621 -27.245 17.931  1.00 21.65 ? 49  LEU A O   1 
ATOM   2461 C  CB  . LEU B 1 49  ? -17.688 -29.901 19.335  1.00 23.40 ? 49  LEU A CB  1 
ATOM   2462 C  CG  . LEU B 1 49  ? -19.097 -30.176 19.604  1.00 23.38 ? 49  LEU A CG  1 
ATOM   2463 C  CD1 . LEU B 1 49  ? -19.503 -31.497 18.949  1.00 23.41 ? 49  LEU A CD1 1 
ATOM   2464 C  CD2 . LEU B 1 49  ? -19.125 -30.386 21.108  1.00 26.67 ? 49  LEU A CD2 1 
ATOM   2465 N  N   . SER B 1 50  ? -18.506 -27.813 16.833  1.00 17.27 ? 50  SER A N   1 
ATOM   2466 C  CA  . SER B 1 50  ? -18.766 -26.471 16.362  1.00 15.78 ? 50  SER A CA  1 
ATOM   2467 C  C   . SER B 1 50  ? -20.178 -26.205 16.780  1.00 14.11 ? 50  SER A C   1 
ATOM   2468 O  O   . SER B 1 50  ? -21.097 -26.861 16.350  1.00 16.41 ? 50  SER A O   1 
ATOM   2469 C  CB  . SER B 1 50  ? -18.697 -26.377 14.778  1.00 17.03 ? 50  SER A CB  1 
ATOM   2470 O  OG  . SER B 1 50  ? -19.307 -25.181 14.335  1.00 19.08 ? 50  SER A OG  1 
ATOM   2471 N  N   . ILE B 1 51  ? -20.361 -25.181 17.673  1.00 13.46 ? 51  ILE A N   1 
ATOM   2472 C  CA  . ILE B 1 51  ? -21.711 -24.811 18.087  1.00 13.95 ? 51  ILE A CA  1 
ATOM   2473 C  C   . ILE B 1 51  ? -21.963 -23.354 17.698  1.00 15.54 ? 51  ILE A C   1 
ATOM   2474 O  O   . ILE B 1 51  ? -21.329 -22.458 18.236  1.00 16.05 ? 51  ILE A O   1 
ATOM   2475 C  CB  . ILE B 1 51  ? -21.845 -24.954 19.580  1.00 13.20 ? 51  ILE A CB  1 
ATOM   2476 C  CG1 . ILE B 1 51  ? -21.500 -26.389 19.942  1.00 16.50 ? 51  ILE A CG1 1 
ATOM   2477 C  CG2 . ILE B 1 51  ? -23.289 -24.683 19.995  1.00 16.28 ? 51  ILE A CG2 1 
ATOM   2478 C  CD1 . ILE B 1 51  ? -21.730 -26.776 21.428  1.00 14.76 ? 51  ILE A CD1 1 
ATOM   2479 N  N   . LYS B 1 52  ? -22.880 -23.167 16.730  1.00 12.77 ? 52  LYS A N   1 
ATOM   2480 C  CA  . LYS B 1 52  ? -23.269 -21.831 16.320  1.00 12.03 ? 52  LYS A CA  1 
ATOM   2481 C  C   . LYS B 1 52  ? -24.728 -21.692 16.707  1.00 13.02 ? 52  LYS A C   1 
ATOM   2482 O  O   . LYS B 1 52  ? -25.585 -22.321 16.174  1.00 13.43 ? 52  LYS A O   1 
ATOM   2483 C  CB  . LYS B 1 52  ? -23.117 -21.576 14.790  1.00 12.16 ? 52  LYS A CB  1 
ATOM   2484 C  CG  . LYS B 1 52  ? -23.606 -20.174 14.371  1.00 15.94 ? 52  LYS A CG  1 
ATOM   2485 C  CD  . LYS B 1 52  ? -23.226 -19.825 12.921  1.00 17.31 ? 52  LYS A CD  1 
ATOM   2486 C  CE  . LYS B 1 52  ? -23.863 -20.753 11.935  1.00 18.36 ? 52  LYS A CE  1 
ATOM   2487 N  NZ  . LYS B 1 52  ? -23.608 -20.285 10.518  1.00 22.55 ? 52  LYS A NZ  1 
ATOM   2488 N  N   A TYR B 1 53  ? -25.018 -20.831 17.696  0.50 12.96 ? 53  TYR A N   1 
ATOM   2489 N  N   B TYR B 1 53  ? -24.939 -20.688 17.584  0.50 12.66 ? 53  TYR A N   1 
ATOM   2490 C  CA  A TYR B 1 53  ? -26.400 -20.696 18.163  0.50 12.15 ? 53  TYR A CA  1 
ATOM   2491 C  CA  B TYR B 1 53  ? -26.200 -20.537 18.288  0.50 12.43 ? 53  TYR A CA  1 
ATOM   2492 C  C   A TYR B 1 53  ? -26.737 -19.240 18.199  0.50 11.81 ? 53  TYR A C   1 
ATOM   2493 C  C   B TYR B 1 53  ? -26.741 -19.126 18.266  0.50 11.76 ? 53  TYR A C   1 
ATOM   2494 O  O   A TYR B 1 53  ? -25.929 -18.425 18.566  0.50 12.63 ? 53  TYR A O   1 
ATOM   2495 O  O   B TYR B 1 53  ? -26.097 -18.209 18.704  0.50 13.13 ? 53  TYR A O   1 
ATOM   2496 C  CB  A TYR B 1 53  ? -26.636 -21.274 19.590  0.50 11.17 ? 53  TYR A CB  1 
ATOM   2497 C  CB  B TYR B 1 53  ? -26.096 -21.028 19.765  0.50 11.84 ? 53  TYR A CB  1 
ATOM   2498 C  CG  A TYR B 1 53  ? -26.540 -22.764 19.807  0.50 9.65  ? 53  TYR A CG  1 
ATOM   2499 C  CG  B TYR B 1 53  ? -27.424 -20.733 20.398  0.50 11.51 ? 53  TYR A CG  1 
ATOM   2500 C  CD1 A TYR B 1 53  ? -26.772 -23.722 18.771  0.50 9.71  ? 53  TYR A CD1 1 
ATOM   2501 C  CD1 B TYR B 1 53  ? -28.556 -21.451 20.062  0.50 11.51 ? 53  TYR A CD1 1 
ATOM   2502 C  CD2 A TYR B 1 53  ? -26.347 -23.235 21.090  0.50 10.05 ? 53  TYR A CD2 1 
ATOM   2503 C  CD2 B TYR B 1 53  ? -27.595 -19.624 21.215  0.50 11.28 ? 53  TYR A CD2 1 
ATOM   2504 C  CE1 A TYR B 1 53  ? -26.706 -25.044 19.036  0.50 10.97 ? 53  TYR A CE1 1 
ATOM   2505 C  CE1 B TYR B 1 53  ? -29.801 -21.127 20.544  0.50 11.38 ? 53  TYR A CE1 1 
ATOM   2506 C  CE2 A TYR B 1 53  ? -26.309 -24.586 21.331  0.50 10.00 ? 53  TYR A CE2 1 
ATOM   2507 C  CE2 B TYR B 1 53  ? -28.785 -19.301 21.731  0.50 10.20 ? 53  TYR A CE2 1 
ATOM   2508 C  CZ  A TYR B 1 53  ? -26.539 -25.492 20.289  0.50 10.96 ? 53  TYR A CZ  1 
ATOM   2509 C  CZ  B TYR B 1 53  ? -29.916 -20.015 21.356  0.50 9.91  ? 53  TYR A CZ  1 
ATOM   2510 O  OH  A TYR B 1 53  ? -26.436 -26.832 20.492  0.50 11.85 ? 53  TYR A OH  1 
ATOM   2511 O  OH  B TYR B 1 53  ? -31.160 -19.717 21.832  0.50 12.81 ? 53  TYR A OH  1 
ATOM   2512 N  N   . ASP B 1 54  ? -27.936 -18.956 17.717  1.00 11.55 ? 54  ASP A N   1 
ATOM   2513 C  CA  . ASP B 1 54  ? -28.493 -17.611 17.631  1.00 11.98 ? 54  ASP A CA  1 
ATOM   2514 C  C   . ASP B 1 54  ? -29.652 -17.538 18.612  1.00 13.26 ? 54  ASP A C   1 
ATOM   2515 O  O   . ASP B 1 54  ? -30.640 -18.221 18.469  1.00 12.79 ? 54  ASP A O   1 
ATOM   2516 C  CB  . ASP B 1 54  ? -29.025 -17.457 16.170  1.00 13.24 ? 54  ASP A CB  1 
ATOM   2517 C  CG  . ASP B 1 54  ? -29.490 -16.032 15.857  1.00 18.12 ? 54  ASP A CG  1 
ATOM   2518 O  OD1 . ASP B 1 54  ? -30.087 -15.331 16.719  1.00 16.27 ? 54  ASP A OD1 1 
ATOM   2519 O  OD2 . ASP B 1 54  ? -29.326 -15.618 14.703  1.00 18.46 ? 54  ASP A OD2 1 
ATOM   2520 N  N   . PRO B 1 55  ? -29.578 -16.633 19.621  1.00 11.91 ? 55  PRO A N   1 
ATOM   2521 C  CA  . PRO B 1 55  ? -30.685 -16.495 20.546  1.00 11.97 ? 55  PRO A CA  1 
ATOM   2522 C  C   . PRO B 1 55  ? -32.020 -16.199 19.986  1.00 13.00 ? 55  PRO A C   1 
ATOM   2523 O  O   . PRO B 1 55  ? -33.105 -16.503 20.596  1.00 15.79 ? 55  PRO A O   1 
ATOM   2524 C  CB  . PRO B 1 55  ? -30.184 -15.356 21.495  1.00 14.01 ? 55  PRO A CB  1 
ATOM   2525 C  CG  . PRO B 1 55  ? -28.666 -15.509 21.470  1.00 12.41 ? 55  PRO A CG  1 
ATOM   2526 C  CD  . PRO B 1 55  ? -28.420 -15.785 19.983  1.00 13.43 ? 55  PRO A CD  1 
ATOM   2527 N  N   A SER B 1 56  ? -32.052 -15.581 18.796  0.50 12.47 ? 56  SER A N   1 
ATOM   2528 N  N   B SER B 1 56  ? -32.016 -15.594 18.798  0.50 13.16 ? 56  SER A N   1 
ATOM   2529 C  CA  A SER B 1 56  ? -33.376 -15.298 18.191  0.50 13.21 ? 56  SER A CA  1 
ATOM   2530 C  CA  B SER B 1 56  ? -33.309 -15.309 18.174  0.50 14.82 ? 56  SER A CA  1 
ATOM   2531 C  C   A SER B 1 56  ? -34.041 -16.555 17.614  0.50 13.29 ? 56  SER A C   1 
ATOM   2532 C  C   B SER B 1 56  ? -34.003 -16.543 17.600  0.50 14.01 ? 56  SER A C   1 
ATOM   2533 O  O   A SER B 1 56  ? -35.220 -16.519 17.215  0.50 14.63 ? 56  SER A O   1 
ATOM   2534 O  O   B SER B 1 56  ? -35.165 -16.483 17.208  0.50 15.14 ? 56  SER A O   1 
ATOM   2535 C  CB  A SER B 1 56  ? -33.252 -14.238 17.044  0.50 12.50 ? 56  SER A CB  1 
ATOM   2536 C  CB  B SER B 1 56  ? -33.109 -14.276 17.050  0.50 15.17 ? 56  SER A CB  1 
ATOM   2537 O  OG  A SER B 1 56  ? -32.617 -14.743 15.881  0.50 12.21 ? 56  SER A OG  1 
ATOM   2538 O  OG  B SER B 1 56  ? -32.767 -13.071 17.675  0.50 19.94 ? 56  SER A OG  1 
ATOM   2539 N  N   . SER B 1 57  ? -33.303 -17.678 17.589  1.00 12.54 ? 57  SER A N   1 
ATOM   2540 C  CA  . SER B 1 57  ? -33.860 -18.903 17.026  1.00 13.48 ? 57  SER A CA  1 
ATOM   2541 C  C   . SER B 1 57  ? -34.917 -19.570 17.946  1.00 14.13 ? 57  SER A C   1 
ATOM   2542 O  O   . SER B 1 57  ? -35.782 -20.301 17.491  1.00 14.02 ? 57  SER A O   1 
ATOM   2543 C  CB  . SER B 1 57  ? -32.821 -19.943 16.736  1.00 15.23 ? 57  SER A CB  1 
ATOM   2544 O  OG  . SER B 1 57  ? -31.887 -19.539 15.723  1.00 17.78 ? 57  SER A OG  1 
ATOM   2545 N  N   . ALA B 1 58  ? -34.848 -19.231 19.232  1.00 14.24 ? 58  ALA A N   1 
ATOM   2546 C  CA  . ALA B 1 58  ? -35.854 -19.736 20.201  1.00 14.73 ? 58  ALA A CA  1 
ATOM   2547 C  C   . ALA B 1 58  ? -37.169 -19.068 19.922  1.00 14.91 ? 58  ALA A C   1 
ATOM   2548 O  O   . ALA B 1 58  ? -37.205 -17.885 19.621  1.00 16.58 ? 58  ALA A O   1 
ATOM   2549 C  CB  . ALA B 1 58  ? -35.372 -19.362 21.614  1.00 14.23 ? 58  ALA A CB  1 
ATOM   2550 N  N   . LYS B 1 59  ? -38.212 -19.842 19.956  1.00 15.27 ? 59  LYS A N   1 
ATOM   2551 C  CA  . LYS B 1 59  ? -39.579 -19.354 19.711  1.00 16.05 ? 59  LYS A CA  1 
ATOM   2552 C  C   . LYS B 1 59  ? -40.548 -19.412 20.900  1.00 15.67 ? 59  LYS A C   1 
ATOM   2553 O  O   . LYS B 1 59  ? -41.224 -18.428 21.187  1.00 14.40 ? 59  LYS A O   1 
ATOM   2554 C  CB  . LYS B 1 59  ? -40.178 -20.117 18.497  1.00 18.89 ? 59  LYS A CB  1 
ATOM   2555 C  CG  . LYS B 1 59  ? -39.330 -19.863 17.193  1.00 23.24 ? 59  LYS A CG  1 
ATOM   2556 C  CD  . LYS B 1 59  ? -39.124 -18.344 16.950  1.00 27.94 ? 59  LYS A CD  1 
ATOM   2557 C  CE  . LYS B 1 59  ? -38.065 -18.111 15.861  1.00 32.51 ? 59  LYS A CE  1 
ATOM   2558 N  NZ  . LYS B 1 59  ? -37.640 -16.704 15.695  1.00 31.64 ? 59  LYS A NZ  1 
ATOM   2559 N  N   . ILE B 1 60  ? -40.681 -20.599 21.465  1.00 14.74 ? 60  ILE A N   1 
ATOM   2560 C  CA  . ILE B 1 60  ? -41.731 -20.853 22.465  1.00 14.77 ? 60  ILE A CA  1 
ATOM   2561 C  C   . ILE B 1 60  ? -41.156 -21.741 23.554  1.00 14.72 ? 60  ILE A C   1 
ATOM   2562 O  O   . ILE B 1 60  ? -40.279 -22.537 23.287  1.00 13.90 ? 60  ILE A O   1 
ATOM   2563 C  CB  . ILE B 1 60  ? -43.070 -21.423 21.936  1.00 18.66 ? 60  ILE A CB  1 
ATOM   2564 C  CG1 . ILE B 1 60  ? -42.872 -22.722 21.218  1.00 19.52 ? 60  ILE A CG1 1 
ATOM   2565 C  CG2 . ILE B 1 60  ? -43.706 -20.372 20.989  1.00 18.46 ? 60  ILE A CG2 1 
ATOM   2566 C  CD1 . ILE B 1 60  ? -44.144 -23.479 20.896  1.00 24.67 ? 60  ILE A CD1 1 
ATOM   2567 N  N   . ILE B 1 61  ? -41.745 -21.649 24.740  1.00 12.46 ? 61  ILE A N   1 
ATOM   2568 C  CA  . ILE B 1 61  ? -41.540 -22.745 25.722  1.00 13.42 ? 61  ILE A CA  1 
ATOM   2569 C  C   . ILE B 1 61  ? -42.912 -23.301 26.091  1.00 13.03 ? 61  ILE A C   1 
ATOM   2570 O  O   . ILE B 1 61  ? -43.912 -22.547 26.210  1.00 12.84 ? 61  ILE A O   1 
ATOM   2571 C  CB  . ILE B 1 61  ? -40.857 -22.230 26.987  1.00 14.13 ? 61  ILE A CB  1 
ATOM   2572 C  CG1 . ILE B 1 61  ? -40.443 -23.409 27.908  1.00 14.00 ? 61  ILE A CG1 1 
ATOM   2573 C  CG2 . ILE B 1 61  ? -41.675 -21.157 27.755  1.00 13.23 ? 61  ILE A CG2 1 
ATOM   2574 C  CD1 . ILE B 1 61  ? -39.443 -22.939 28.983  1.00 16.28 ? 61  ILE A CD1 1 
ATOM   2575 N  N   . SER B 1 62  ? -42.971 -24.626 26.299  1.00 12.40 ? 62  SER A N   1 
ATOM   2576 C  CA  . SER B 1 62  ? -44.231 -25.271 26.615  1.00 13.97 ? 62  SER A CA  1 
ATOM   2577 C  C   . SER B 1 62  ? -44.024 -26.411 27.576  1.00 14.37 ? 62  SER A C   1 
ATOM   2578 O  O   . SER B 1 62  ? -42.900 -26.862 27.818  1.00 13.64 ? 62  SER A O   1 
ATOM   2579 C  CB  . SER B 1 62  ? -44.950 -25.767 25.345  1.00 18.16 ? 62  SER A CB  1 
ATOM   2580 O  OG  . SER B 1 62  ? -44.112 -26.709 24.747  1.00 23.20 ? 62  SER A OG  1 
ATOM   2581 N  N   . ASN B 1 63  ? -45.149 -26.745 28.206  1.00 12.84 ? 63  ASN A N   1 
ATOM   2582 C  CA  . ASN B 1 63  ? -45.139 -27.971 29.065  1.00 13.98 ? 63  ASN A CA  1 
ATOM   2583 C  C   . ASN B 1 63  ? -45.789 -29.046 28.218  1.00 14.47 ? 63  ASN A C   1 
ATOM   2584 O  O   . ASN B 1 63  ? -46.993 -29.041 27.907  1.00 14.48 ? 63  ASN A O   1 
ATOM   2585 C  CB  . ASN B 1 63  ? -45.984 -27.680 30.313  1.00 13.51 ? 63  ASN A CB  1 
ATOM   2586 C  CG  . ASN B 1 63  ? -46.083 -28.896 31.247  1.00 14.05 ? 63  ASN A CG  1 
ATOM   2587 O  OD1 . ASN B 1 63  ? -45.692 -29.989 30.921  1.00 16.63 ? 63  ASN A OD1 1 
ATOM   2588 N  ND2 . ASN B 1 63  ? -46.616 -28.688 32.456  1.00 14.42 ? 63  ASN A ND2 1 
ATOM   2589 N  N   . SER B 1 64  ? -44.965 -30.039 27.881  1.00 13.70 ? 64  SER A N   1 
ATOM   2590 C  CA  . SER B 1 64  ? -45.426 -31.176 27.092  1.00 14.78 ? 64  SER A CA  1 
ATOM   2591 C  C   . SER B 1 64  ? -46.085 -32.246 27.937  1.00 14.73 ? 64  SER A C   1 
ATOM   2592 O  O   . SER B 1 64  ? -46.619 -33.203 27.379  1.00 17.58 ? 64  SER A O   1 
ATOM   2593 C  CB  . SER B 1 64  ? -44.238 -31.838 26.441  1.00 14.37 ? 64  SER A CB  1 
ATOM   2594 O  OG  . SER B 1 64  ? -43.405 -32.466 27.469  1.00 14.93 ? 64  SER A OG  1 
ATOM   2595 N  N   . GLY B 1 65  ? -46.107 -32.041 29.262  1.00 15.56 ? 65  GLY A N   1 
ATOM   2596 C  CA  . GLY B 1 65  ? -46.535 -33.121 30.212  1.00 15.39 ? 65  GLY A CA  1 
ATOM   2597 C  C   . GLY B 1 65  ? -45.399 -34.004 30.714  1.00 14.96 ? 65  GLY A C   1 
ATOM   2598 O  O   . GLY B 1 65  ? -45.556 -34.697 31.723  1.00 15.09 ? 65  GLY A O   1 
ATOM   2599 N  N   . HIS B 1 66  ? -44.263 -33.995 29.994  1.00 14.19 ? 66  HIS A N   1 
ATOM   2600 C  CA  . HIS B 1 66  ? -43.105 -34.827 30.230  1.00 14.12 ? 66  HIS A CA  1 
ATOM   2601 C  C   . HIS B 1 66  ? -41.856 -34.054 30.579  1.00 11.66 ? 66  HIS A C   1 
ATOM   2602 O  O   . HIS B 1 66  ? -40.933 -34.635 31.075  1.00 12.92 ? 66  HIS A O   1 
ATOM   2603 C  CB  . HIS B 1 66  ? -42.825 -35.638 28.916  1.00 16.69 ? 66  HIS A CB  1 
ATOM   2604 C  CG  . HIS B 1 66  ? -44.034 -36.293 28.383  1.00 20.65 ? 66  HIS A CG  1 
ATOM   2605 N  ND1 . HIS B 1 66  ? -44.502 -36.061 27.112  1.00 23.49 ? 66  HIS A ND1 1 
ATOM   2606 C  CD2 . HIS B 1 66  ? -44.941 -37.150 29.005  1.00 20.53 ? 66  HIS A CD2 1 
ATOM   2607 C  CE1 . HIS B 1 66  ? -45.661 -36.790 26.953  1.00 21.16 ? 66  HIS A CE1 1 
ATOM   2608 N  NE2 . HIS B 1 66  ? -45.937 -37.426 28.111  1.00 24.81 ? 66  HIS A NE2 1 
ATOM   2609 N  N   . SER B 1 67  ? -41.850 -32.718 30.322  1.00 10.38 ? 67  SER A N   1 
ATOM   2610 C  CA  . SER B 1 67  ? -40.767 -31.832 30.633  1.00 11.71 ? 67  SER A CA  1 
ATOM   2611 C  C   . SER B 1 67  ? -41.262 -30.413 30.159  1.00 10.70 ? 67  SER A C   1 
ATOM   2612 O  O   . SER B 1 67  ? -42.415 -30.309 29.643  1.00 12.50 ? 67  SER A O   1 
ATOM   2613 C  CB  . SER B 1 67  ? -39.446 -32.209 29.962  1.00 12.12 ? 67  SER A CB  1 
ATOM   2614 O  OG  . SER B 1 67  ? -38.388 -31.378 30.424  1.00 12.07 ? 67  SER A OG  1 
ATOM   2615 N  N   . PHE B 1 68  ? -40.405 -29.418 30.326  1.00 10.46 ? 68  PHE A N   1 
ATOM   2616 C  CA  . PHE B 1 68  ? -40.679 -28.225 29.483  1.00 11.23 ? 68  PHE A CA  1 
ATOM   2617 C  C   . PHE B 1 68  ? -39.961 -28.514 28.203  1.00 12.23 ? 68  PHE A C   1 
ATOM   2618 O  O   . PHE B 1 68  ? -38.950 -29.175 28.150  1.00 11.86 ? 68  PHE A O   1 
ATOM   2619 C  CB  . PHE B 1 68  ? -40.199 -26.955 30.165  1.00 13.15 ? 68  PHE A CB  1 
ATOM   2620 C  CG  . PHE B 1 68  ? -38.706 -26.879 30.277  1.00 11.78 ? 68  PHE A CG  1 
ATOM   2621 C  CD1 . PHE B 1 68  ? -38.003 -27.321 31.450  1.00 12.23 ? 68  PHE A CD1 1 
ATOM   2622 C  CD2 . PHE B 1 68  ? -37.906 -26.407 29.184  1.00 12.44 ? 68  PHE A CD2 1 
ATOM   2623 C  CE1 . PHE B 1 68  ? -36.614 -27.265 31.509  1.00 12.10 ? 68  PHE A CE1 1 
ATOM   2624 C  CE2 . PHE B 1 68  ? -36.517 -26.356 29.266  1.00 12.72 ? 68  PHE A CE2 1 
ATOM   2625 C  CZ  . PHE B 1 68  ? -35.840 -26.808 30.436  1.00 13.38 ? 68  PHE A CZ  1 
ATOM   2626 N  N   . ASN B 1 69  ? -40.373 -27.789 27.172  1.00 12.59 ? 69  ASN A N   1 
ATOM   2627 C  CA  . ASN B 1 69  ? -39.667 -27.856 25.847  1.00 14.62 ? 69  ASN A CA  1 
ATOM   2628 C  C   . ASN B 1 69  ? -39.478 -26.461 25.336  1.00 12.47 ? 69  ASN A C   1 
ATOM   2629 O  O   . ASN B 1 69  ? -40.520 -25.712 25.178  1.00 12.98 ? 69  ASN A O   1 
ATOM   2630 C  CB  . ASN B 1 69  ? -40.508 -28.534 24.733  1.00 16.11 ? 69  ASN A CB  1 
ATOM   2631 C  CG  . ASN B 1 69  ? -40.752 -29.993 24.960  1.00 21.18 ? 69  ASN A CG  1 
ATOM   2632 O  OD1 . ASN B 1 69  ? -41.733 -30.565 24.416  1.00 23.53 ? 69  ASN A OD1 1 
ATOM   2633 N  ND2 . ASN B 1 69  ? -39.797 -30.652 25.562  1.00 22.15 ? 69  ASN A ND2 1 
ATOM   2634 N  N   . VAL B 1 70  ? -38.229 -26.074 25.048  1.00 12.37 ? 70  VAL A N   1 
ATOM   2635 C  CA  . VAL B 1 70  ? -38.029 -24.762 24.330  1.00 11.96 ? 70  VAL A CA  1 
ATOM   2636 C  C   . VAL B 1 70  ? -37.884 -25.200 22.855  1.00 12.77 ? 70  VAL A C   1 
ATOM   2637 O  O   . VAL B 1 70  ? -36.985 -26.034 22.535  1.00 13.15 ? 70  VAL A O   1 
ATOM   2638 C  CB  . VAL B 1 70  ? -36.711 -24.103 24.729  1.00 11.20 ? 70  VAL A CB  1 
ATOM   2639 C  CG1 . VAL B 1 70  ? -36.564 -22.769 23.960  1.00 13.93 ? 70  VAL A CG1 1 
ATOM   2640 C  CG2 . VAL B 1 70  ? -36.741 -23.699 26.212  1.00 13.11 ? 70  VAL A CG2 1 
ATOM   2641 N  N   . ASP B 1 71  ? -38.743 -24.610 22.002  1.00 13.44 ? 71  ASP A N   1 
ATOM   2642 C  CA  . ASP B 1 71  ? -38.676 -25.026 20.559  1.00 13.04 ? 71  ASP A CA  1 
ATOM   2643 C  C   . ASP B 1 71  ? -38.100 -23.874 19.775  1.00 12.73 ? 71  ASP A C   1 
ATOM   2644 O  O   . ASP B 1 71  ? -38.288 -22.694 20.149  1.00 14.14 ? 71  ASP A O   1 
ATOM   2645 C  CB  . ASP B 1 71  ? -40.079 -25.309 20.045  1.00 16.98 ? 71  ASP A CB  1 
ATOM   2646 C  CG  . ASP B 1 71  ? -40.668 -26.601 20.667  1.00 22.28 ? 71  ASP A CG  1 
ATOM   2647 O  OD1 . ASP B 1 71  ? -39.915 -27.535 21.009  1.00 25.02 ? 71  ASP A OD1 1 
ATOM   2648 O  OD2 . ASP B 1 71  ? -41.886 -26.626 20.927  1.00 25.62 ? 71  ASP A OD2 1 
ATOM   2649 N  N   . PHE B 1 72  ? -37.342 -24.288 18.742  1.00 13.50 ? 72  PHE A N   1 
ATOM   2650 C  CA  . PHE B 1 72  ? -36.584 -23.343 17.892  1.00 12.78 ? 72  PHE A CA  1 
ATOM   2651 C  C   . PHE B 1 72  ? -37.009 -23.450 16.483  1.00 14.55 ? 72  PHE A C   1 
ATOM   2652 O  O   . PHE B 1 72  ? -37.544 -24.431 16.049  1.00 16.39 ? 72  PHE A O   1 
ATOM   2653 C  CB  . PHE B 1 72  ? -35.096 -23.712 17.993  1.00 11.79 ? 72  PHE A CB  1 
ATOM   2654 C  CG  . PHE B 1 72  ? -34.506 -23.550 19.386  1.00 12.90 ? 72  PHE A CG  1 
ATOM   2655 C  CD1 . PHE B 1 72  ? -34.655 -24.546 20.348  1.00 13.94 ? 72  PHE A CD1 1 
ATOM   2656 C  CD2 . PHE B 1 72  ? -33.792 -22.407 19.732  1.00 14.42 ? 72  PHE A CD2 1 
ATOM   2657 C  CE1 . PHE B 1 72  ? -34.113 -24.405 21.619  1.00 13.44 ? 72  PHE A CE1 1 
ATOM   2658 C  CE2 . PHE B 1 72  ? -33.251 -22.263 21.006  1.00 13.78 ? 72  PHE A CE2 1 
ATOM   2659 C  CZ  . PHE B 1 72  ? -33.411 -23.263 21.949  1.00 13.66 ? 72  PHE A CZ  1 
ATOM   2660 N  N   A ASP B 1 73  ? -36.761 -22.375 15.763  0.50 15.20 ? 73  ASP A N   1 
ATOM   2661 N  N   B ASP B 1 73  ? -36.664 -22.430 15.717  0.50 16.41 ? 73  ASP A N   1 
ATOM   2662 C  CA  A ASP B 1 73  ? -37.001 -22.399 14.313  0.50 14.95 ? 73  ASP A CA  1 
ATOM   2663 C  CA  B ASP B 1 73  ? -36.865 -22.479 14.249  0.50 16.65 ? 73  ASP A CA  1 
ATOM   2664 C  C   A ASP B 1 73  ? -36.593 -23.709 13.498  0.50 14.20 ? 73  ASP A C   1 
ATOM   2665 C  C   B ASP B 1 73  ? -36.580 -23.780 13.504  0.50 14.90 ? 73  ASP A C   1 
ATOM   2666 O  O   A ASP B 1 73  ? -35.497 -24.265 13.534  0.50 15.75 ? 73  ASP A O   1 
ATOM   2667 O  O   B ASP B 1 73  ? -35.505 -24.357 13.527  0.50 16.05 ? 73  ASP A O   1 
ATOM   2668 C  CB  A ASP B 1 73  ? -36.433 -21.121 13.717  0.50 15.43 ? 73  ASP A CB  1 
ATOM   2669 C  CB  B ASP B 1 73  ? -36.000 -21.458 13.590  0.50 19.29 ? 73  ASP A CB  1 
ATOM   2670 C  CG  A ASP B 1 73  ? -36.906 -20.891 12.340  0.50 15.04 ? 73  ASP A CG  1 
ATOM   2671 C  CG  B ASP B 1 73  ? -36.326 -20.106 14.025  0.50 20.19 ? 73  ASP A CG  1 
ATOM   2672 O  OD1 A ASP B 1 73  ? -36.395 -21.571 11.458  0.50 16.03 ? 73  ASP A OD1 1 
ATOM   2673 O  OD1 B ASP B 1 73  ? -37.473 -19.872 14.462  0.50 23.54 ? 73  ASP A OD1 1 
ATOM   2674 O  OD2 A ASP B 1 73  ? -37.801 -20.064 12.195  0.50 18.59 ? 73  ASP A OD2 1 
ATOM   2675 O  OD2 B ASP B 1 73  ? -35.415 -19.261 13.862  0.50 23.40 ? 73  ASP A OD2 1 
ATOM   2676 N  N   . ASP B 1 74  ? -37.543 -24.181 12.695  1.00 15.35 ? 74  ASP A N   1 
ATOM   2677 C  CA  . ASP B 1 74  ? -37.413 -25.467 11.993  1.00 17.33 ? 74  ASP A CA  1 
ATOM   2678 C  C   . ASP B 1 74  ? -36.705 -25.449 10.619  1.00 16.68 ? 74  ASP A C   1 
ATOM   2679 O  O   . ASP B 1 74  ? -36.449 -26.491 10.093  1.00 18.94 ? 74  ASP A O   1 
ATOM   2680 C  CB  . ASP B 1 74  ? -38.770 -26.121 11.832  1.00 20.88 ? 74  ASP A CB  1 
ATOM   2681 C  CG  . ASP B 1 74  ? -39.259 -26.709 13.118  1.00 30.68 ? 74  ASP A CG  1 
ATOM   2682 O  OD1 . ASP B 1 74  ? -38.447 -27.240 13.939  1.00 36.61 ? 74  ASP A OD1 1 
ATOM   2683 O  OD2 . ASP B 1 74  ? -40.440 -26.537 13.363  1.00 29.18 ? 74  ASP A OD2 1 
ATOM   2684 N  N   . THR B 1 75  ? -36.619 -24.262 10.015  1.00 16.44 ? 75  THR A N   1 
ATOM   2685 C  CA  . THR B 1 75  ? -36.212 -24.167 8.593   1.00 16.77 ? 75  THR A CA  1 
ATOM   2686 C  C   . THR B 1 75  ? -35.015 -23.222 8.335   1.00 16.08 ? 75  THR A C   1 
ATOM   2687 O  O   . THR B 1 75  ? -34.668 -22.991 7.128   1.00 16.60 ? 75  THR A O   1 
ATOM   2688 C  CB  . THR B 1 75  ? -37.457 -23.818 7.708   1.00 16.65 ? 75  THR A CB  1 
ATOM   2689 O  OG1 . THR B 1 75  ? -37.922 -22.505 8.121   1.00 19.45 ? 75  THR A OG1 1 
ATOM   2690 C  CG2 . THR B 1 75  ? -38.518 -24.964 7.816   1.00 19.50 ? 75  THR A CG2 1 
ATOM   2691 N  N   . GLU B 1 76  ? -34.252 -22.748 9.310   1.00 15.05 ? 76  GLU A N   1 
ATOM   2692 C  CA  . GLU B 1 76  ? -33.111 -21.957 9.105   1.00 13.90 ? 76  GLU A CA  1 
ATOM   2693 C  C   . GLU B 1 76  ? -31.840 -22.588 9.665   1.00 14.32 ? 76  GLU A C   1 
ATOM   2694 O  O   . GLU B 1 76  ? -31.980 -23.413 10.615  1.00 14.61 ? 76  GLU A O   1 
ATOM   2695 C  CB  . GLU B 1 76  ? -33.336 -20.573 9.841   1.00 14.71 ? 76  GLU A CB  1 
ATOM   2696 C  CG  . GLU B 1 76  ? -34.592 -19.800 9.396   1.00 19.07 ? 76  GLU A CG  1 
ATOM   2697 C  CD  . GLU B 1 76  ? -34.957 -18.654 10.269  1.00 24.14 ? 76  GLU A CD  1 
ATOM   2698 O  OE1 . GLU B 1 76  ? -34.381 -18.554 11.423  1.00 27.11 ? 76  GLU A OE1 1 
ATOM   2699 O  OE2 . GLU B 1 76  ? -35.820 -17.842 9.825   1.00 25.36 ? 76  GLU A OE2 1 
ATOM   2700 N  N   . ASN B 1 77  ? -30.669 -22.267 9.151   1.00 14.18 ? 77  ASN A N   1 
ATOM   2701 C  CA  . ASN B 1 77  ? -29.367 -22.683 9.695   1.00 16.01 ? 77  ASN A CA  1 
ATOM   2702 C  C   . ASN B 1 77  ? -28.629 -21.689 10.529  1.00 13.09 ? 77  ASN A C   1 
ATOM   2703 O  O   . ASN B 1 77  ? -27.453 -21.695 10.588  1.00 13.18 ? 77  ASN A O   1 
ATOM   2704 C  CB  . ASN B 1 77  ? -28.362 -23.335 8.638   1.00 17.59 ? 77  ASN A CB  1 
ATOM   2705 C  CG  . ASN B 1 77  ? -28.796 -24.758 8.216   1.00 15.21 ? 77  ASN A CG  1 
ATOM   2706 O  OD1 . ASN B 1 77  ? -29.647 -25.393 8.882   1.00 13.68 ? 77  ASN A OD1 1 
ATOM   2707 N  ND2 . ASN B 1 77  ? -28.216 -25.286 7.098   1.00 16.60 ? 77  ASN A ND2 1 
ATOM   2708 N  N   . LYS B 1 78  ? -29.385 -20.867 11.313  1.00 15.24 ? 78  LYS A N   1 
ATOM   2709 C  CA  . LYS B 1 78  ? -28.769 -19.884 12.238  1.00 13.68 ? 78  LYS A CA  1 
ATOM   2710 C  C   . LYS B 1 78  ? -28.222 -20.563 13.490  1.00 14.55 ? 78  LYS A C   1 
ATOM   2711 O  O   . LYS B 1 78  ? -27.200 -20.161 14.086  1.00 13.79 ? 78  LYS A O   1 
ATOM   2712 C  CB  . LYS B 1 78  ? -29.774 -18.800 12.612  1.00 16.36 ? 78  LYS A CB  1 
ATOM   2713 C  CG  . LYS B 1 78  ? -30.039 -17.879 11.389  1.00 17.82 ? 78  LYS A CG  1 
ATOM   2714 C  CD  . LYS B 1 78  ? -31.196 -16.971 11.699  1.00 25.24 ? 78  LYS A CD  1 
ATOM   2715 C  CE  . LYS B 1 78  ? -31.380 -15.760 10.718  1.00 26.01 ? 78  LYS A CE  1 
ATOM   2716 N  NZ  . LYS B 1 78  ? -32.659 -15.186 11.204  1.00 34.48 ? 78  LYS A NZ  1 
ATOM   2717 N  N   . SER B 1 79  ? -28.914 -21.683 13.827  1.00 13.05 ? 79  SER A N   1 
ATOM   2718 C  CA  . SER B 1 79  ? -28.465 -22.448 15.058  1.00 11.69 ? 79  SER A CA  1 
ATOM   2719 C  C   . SER B 1 79  ? -28.238 -23.896 14.687  1.00 11.15 ? 79  SER A C   1 
ATOM   2720 O  O   . SER B 1 79  ? -29.203 -24.664 14.453  1.00 12.43 ? 79  SER A O   1 
ATOM   2721 C  CB  . SER B 1 79  ? -29.493 -22.324 16.193  1.00 10.82 ? 79  SER A CB  1 
ATOM   2722 O  OG  . SER B 1 79  ? -29.627 -20.959 16.621  1.00 11.21 ? 79  SER A OG  1 
ATOM   2723 N  N   . VAL B 1 80  ? -26.968 -24.208 14.592  1.00 12.32 ? 80  VAL A N   1 
ATOM   2724 C  CA  . VAL B 1 80  ? -26.533 -25.574 14.057  1.00 11.82 ? 80  VAL A CA  1 
ATOM   2725 C  C   . VAL B 1 80  ? -25.359 -26.136 14.895  1.00 12.56 ? 80  VAL A C   1 
ATOM   2726 O  O   . VAL B 1 80  ? -24.561 -25.374 15.453  1.00 11.81 ? 80  VAL A O   1 
ATOM   2727 C  CB  . VAL B 1 80  ? -26.147 -25.465 12.561  1.00 13.12 ? 80  VAL A CB  1 
ATOM   2728 C  CG1 . VAL B 1 80  ? -27.419 -25.125 11.744  1.00 14.39 ? 80  VAL A CG1 1 
ATOM   2729 C  CG2 . VAL B 1 80  ? -24.974 -24.435 12.392  1.00 15.39 ? 80  VAL A CG2 1 
ATOM   2730 N  N   . LEU B 1 81  ? -25.335 -27.487 14.930  1.00 12.94 ? 81  LEU A N   1 
ATOM   2731 C  CA  . LEU B 1 81  ? -24.287 -28.247 15.562  1.00 12.88 ? 81  LEU A CA  1 
ATOM   2732 C  C   . LEU B 1 81  ? -23.581 -29.018 14.428  1.00 11.65 ? 81  LEU A C   1 
ATOM   2733 O  O   . LEU B 1 81  ? -24.208 -29.683 13.621  1.00 13.58 ? 81  LEU A O   1 
ATOM   2734 C  CB  . LEU B 1 81  ? -24.918 -29.232 16.594  1.00 13.76 ? 81  LEU A CB  1 
ATOM   2735 C  CG  . LEU B 1 81  ? -23.924 -30.166 17.264  1.00 13.52 ? 81  LEU A CG  1 
ATOM   2736 C  CD1 . LEU B 1 81  ? -22.980 -29.363 18.171  1.00 14.86 ? 81  LEU A CD1 1 
ATOM   2737 C  CD2 . LEU B 1 81  ? -24.718 -31.240 18.061  1.00 12.97 ? 81  LEU A CD2 1 
ATOM   2738 N  N   . ARG B 1 82  ? -22.249 -28.887 14.474  1.00 13.14 ? 82  ARG A N   1 
ATOM   2739 C  CA  . ARG B 1 82  ? -21.385 -29.535 13.462  1.00 14.64 ? 82  ARG A CA  1 
ATOM   2740 C  C   . ARG B 1 82  ? -20.171 -30.090 14.166  1.00 15.26 ? 82  ARG A C   1 
ATOM   2741 O  O   . ARG B 1 82  ? -19.891 -29.752 15.350  1.00 14.32 ? 82  ARG A O   1 
ATOM   2742 C  CB  . ARG B 1 82  ? -20.965 -28.519 12.348  1.00 16.21 ? 82  ARG A CB  1 
ATOM   2743 C  CG  . ARG B 1 82  ? -22.142 -28.120 11.452  1.00 14.83 ? 82  ARG A CG  1 
ATOM   2744 C  CD  . ARG B 1 82  ? -21.796 -26.883 10.544  1.00 16.41 ? 82  ARG A CD  1 
ATOM   2745 N  NE  . ARG B 1 82  ? -21.663 -25.665 11.329  1.00 15.90 ? 82  ARG A NE  1 
ATOM   2746 C  CZ  . ARG B 1 82  ? -21.441 -24.433 10.827  1.00 16.97 ? 82  ARG A CZ  1 
ATOM   2747 N  NH1 . ARG B 1 82  ? -21.314 -24.243 9.489   1.00 19.71 ? 82  ARG A NH1 1 
ATOM   2748 N  NH2 . ARG B 1 82  ? -21.402 -23.414 11.648  1.00 17.96 ? 82  ARG A NH2 1 
ATOM   2749 N  N   . GLY B 1 83  ? -19.368 -30.878 13.446  1.00 14.59 ? 83  GLY A N   1 
ATOM   2750 C  CA  . GLY B 1 83  ? -18.062 -31.358 13.973  1.00 15.66 ? 83  GLY A CA  1 
ATOM   2751 C  C   . GLY B 1 83  ? -18.288 -32.522 14.942  1.00 15.39 ? 83  GLY A C   1 
ATOM   2752 O  O   . GLY B 1 83  ? -19.322 -33.225 14.907  1.00 14.54 ? 83  GLY A O   1 
ATOM   2753 N  N   . GLY B 1 84  ? -17.314 -32.717 15.829  1.00 17.69 ? 84  GLY A N   1 
ATOM   2754 C  CA  . GLY B 1 84  ? -17.343 -33.934 16.630  1.00 17.05 ? 84  GLY A CA  1 
ATOM   2755 C  C   . GLY B 1 84  ? -17.426 -35.199 15.806  1.00 16.45 ? 84  GLY A C   1 
ATOM   2756 O  O   . GLY B 1 84  ? -16.684 -35.318 14.829  1.00 19.35 ? 84  GLY A O   1 
ATOM   2757 N  N   . PRO B 1 85  ? -18.407 -36.030 16.136  1.00 14.74 ? 85  PRO A N   1 
ATOM   2758 C  CA  . PRO B 1 85  ? -18.698 -37.308 15.481  1.00 14.86 ? 85  PRO A CA  1 
ATOM   2759 C  C   . PRO B 1 85  ? -19.600 -37.115 14.241  1.00 16.32 ? 85  PRO A C   1 
ATOM   2760 O  O   . PRO B 1 85  ? -19.818 -38.086 13.504  1.00 16.42 ? 85  PRO A O   1 
ATOM   2761 C  CB  . PRO B 1 85  ? -19.415 -38.106 16.576  1.00 16.83 ? 85  PRO A CB  1 
ATOM   2762 C  CG  . PRO B 1 85  ? -20.182 -37.016 17.329  1.00 15.60 ? 85  PRO A CG  1 
ATOM   2763 C  CD  . PRO B 1 85  ? -19.219 -35.841 17.361  1.00 15.80 ? 85  PRO A CD  1 
ATOM   2764 N  N   . LEU B 1 86  ? -20.055 -35.879 13.986  1.00 14.62 ? 86  LEU A N   1 
ATOM   2765 C  CA  . LEU B 1 86  ? -21.162 -35.698 12.996  1.00 14.71 ? 86  LEU A CA  1 
ATOM   2766 C  C   . LEU B 1 86  ? -20.659 -35.487 11.574  1.00 16.30 ? 86  LEU A C   1 
ATOM   2767 O  O   . LEU B 1 86  ? -19.690 -34.793 11.384  1.00 16.57 ? 86  LEU A O   1 
ATOM   2768 C  CB  . LEU B 1 86  ? -21.957 -34.422 13.395  1.00 13.60 ? 86  LEU A CB  1 
ATOM   2769 C  CG  . LEU B 1 86  ? -22.547 -34.546 14.815  1.00 14.14 ? 86  LEU A CG  1 
ATOM   2770 C  CD1 . LEU B 1 86  ? -23.204 -33.228 15.256  1.00 14.91 ? 86  LEU A CD1 1 
ATOM   2771 C  CD2 . LEU B 1 86  ? -23.527 -35.736 14.935  1.00 15.84 ? 86  LEU A CD2 1 
ATOM   2772 N  N   . THR B 1 87  ? -21.427 -36.025 10.632  1.00 16.75 ? 87  THR A N   1 
ATOM   2773 C  CA  . THR B 1 87  ? -21.247 -35.640 9.192   1.00 17.87 ? 87  THR A CA  1 
ATOM   2774 C  C   . THR B 1 87  ? -22.348 -34.648 8.797   1.00 15.09 ? 87  THR A C   1 
ATOM   2775 O  O   . THR B 1 87  ? -23.525 -34.992 8.914   1.00 16.41 ? 87  THR A O   1 
ATOM   2776 C  CB  . THR B 1 87  ? -21.341 -36.907 8.333   1.00 15.79 ? 87  THR A CB  1 
ATOM   2777 O  OG1 . THR B 1 87  ? -20.212 -37.702 8.643   1.00 22.01 ? 87  THR A OG1 1 
ATOM   2778 C  CG2 . THR B 1 87  ? -21.162 -36.552 6.810   1.00 18.28 ? 87  THR A CG2 1 
ATOM   2779 N  N   . GLY B 1 88  ? -21.985 -33.451 8.342   1.00 14.74 ? 88  GLY A N   1 
ATOM   2780 C  CA  . GLY B 1 88  ? -22.964 -32.404 7.936   1.00 15.78 ? 88  GLY A CA  1 
ATOM   2781 C  C   . GLY B 1 88  ? -23.512 -31.587 9.095   1.00 15.63 ? 88  GLY A C   1 
ATOM   2782 O  O   . GLY B 1 88  ? -22.938 -31.613 10.214  1.00 15.87 ? 88  GLY A O   1 
ATOM   2783 N  N   . SER B 1 89  ? -24.590 -30.910 8.850   1.00 13.60 ? 89  SER A N   1 
ATOM   2784 C  CA  . SER B 1 89  ? -25.072 -29.834 9.739   1.00 13.70 ? 89  SER A CA  1 
ATOM   2785 C  C   . SER B 1 89  ? -26.376 -30.347 10.369  1.00 12.98 ? 89  SER A C   1 
ATOM   2786 O  O   . SER B 1 89  ? -27.318 -30.810 9.694   1.00 14.42 ? 89  SER A O   1 
ATOM   2787 C  CB  . SER B 1 89  ? -25.368 -28.617 8.853   1.00 13.41 ? 89  SER A CB  1 
ATOM   2788 O  OG  . SER B 1 89  ? -25.639 -27.489 9.727   1.00 14.15 ? 89  SER A OG  1 
ATOM   2789 N  N   . TYR B 1 90  ? -26.413 -30.243 11.722  1.00 12.14 ? 90  TYR A N   1 
ATOM   2790 C  CA  . TYR B 1 90  ? -27.617 -30.681 12.489  1.00 10.57 ? 90  TYR A CA  1 
ATOM   2791 C  C   . TYR B 1 90  ? -28.276 -29.436 13.097  1.00 10.72 ? 90  TYR A C   1 
ATOM   2792 O  O   . TYR B 1 90  ? -27.659 -28.665 13.903  1.00 12.96 ? 90  TYR A O   1 
ATOM   2793 C  CB  . TYR B 1 90  ? -27.162 -31.690 13.557  1.00 10.91 ? 90  TYR A CB  1 
ATOM   2794 C  CG  . TYR B 1 90  ? -26.885 -33.064 13.019  1.00 10.17 ? 90  TYR A CG  1 
ATOM   2795 C  CD1 . TYR B 1 90  ? -25.777 -33.305 12.217  1.00 10.96 ? 90  TYR A CD1 1 
ATOM   2796 C  CD2 . TYR B 1 90  ? -27.726 -34.130 13.310  1.00 10.75 ? 90  TYR A CD2 1 
ATOM   2797 C  CE1 . TYR B 1 90  ? -25.515 -34.567 11.720  1.00 10.47 ? 90  TYR A CE1 1 
ATOM   2798 C  CE2 . TYR B 1 90  ? -27.469 -35.398 12.814  1.00 11.31 ? 90  TYR A CE2 1 
ATOM   2799 C  CZ  . TYR B 1 90  ? -26.364 -35.610 12.023  1.00 11.53 ? 90  TYR A CZ  1 
ATOM   2800 O  OH  . TYR B 1 90  ? -26.105 -36.869 11.532  1.00 12.84 ? 90  TYR A OH  1 
ATOM   2801 N  N   . ARG B 1 91  ? -29.495 -29.179 12.724  1.00 10.15 ? 91  ARG A N   1 
ATOM   2802 C  CA  . ARG B 1 91  ? -30.214 -27.953 13.109  1.00 10.46 ? 91  ARG A CA  1 
ATOM   2803 C  C   . ARG B 1 91  ? -30.835 -28.098 14.486  1.00 10.08 ? 91  ARG A C   1 
ATOM   2804 O  O   . ARG B 1 91  ? -31.456 -29.104 14.792  1.00 11.78 ? 91  ARG A O   1 
ATOM   2805 C  CB  . ARG B 1 91  ? -31.318 -27.785 12.029  1.00 12.64 ? 91  ARG A CB  1 
ATOM   2806 C  CG  . ARG B 1 91  ? -32.104 -26.451 12.144  1.00 13.19 ? 91  ARG A CG  1 
ATOM   2807 C  CD  . ARG B 1 91  ? -33.104 -26.296 11.030  1.00 14.47 ? 91  ARG A CD  1 
ATOM   2808 N  NE  . ARG B 1 91  ? -32.349 -26.197 9.791   1.00 14.05 ? 91  ARG A NE  1 
ATOM   2809 C  CZ  . ARG B 1 91  ? -32.817 -26.522 8.597   1.00 12.55 ? 91  ARG A CZ  1 
ATOM   2810 N  NH1 . ARG B 1 91  ? -34.065 -26.955 8.474   1.00 11.18 ? 91  ARG A NH1 1 
ATOM   2811 N  NH2 . ARG B 1 91  ? -32.042 -26.406 7.524   1.00 13.86 ? 91  ARG A NH2 1 
ATOM   2812 N  N   . LEU B 1 92  ? -30.604 -27.047 15.264  1.00 9.90  ? 92  LEU A N   1 
ATOM   2813 C  CA  . LEU B 1 92  ? -31.174 -27.053 16.633  1.00 10.34 ? 92  LEU A CA  1 
ATOM   2814 C  C   . LEU B 1 92  ? -32.705 -27.072 16.565  1.00 10.78 ? 92  LEU A C   1 
ATOM   2815 O  O   . LEU B 1 92  ? -33.337 -26.324 15.844  1.00 12.52 ? 92  LEU A O   1 
ATOM   2816 C  CB  . LEU B 1 92  ? -30.709 -25.780 17.309  1.00 11.11 ? 92  LEU A CB  1 
ATOM   2817 C  CG  . LEU B 1 92  ? -31.329 -25.534 18.706  1.00 11.15 ? 92  LEU A CG  1 
ATOM   2818 C  CD1 . LEU B 1 92  ? -30.907 -26.719 19.657  1.00 11.84 ? 92  LEU A CD1 1 
ATOM   2819 C  CD2 . LEU B 1 92  ? -30.851 -24.188 19.250  1.00 12.71 ? 92  LEU A CD2 1 
ATOM   2820 N  N   . ARG B 1 93  ? -33.361 -27.968 17.321  1.00 11.31 ? 93  ARG A N   1 
ATOM   2821 C  CA  . ARG B 1 93  ? -34.777 -28.143 17.339  1.00 10.69 ? 93  ARG A CA  1 
ATOM   2822 C  C   . ARG B 1 93  ? -35.447 -27.822 18.715  1.00 11.09 ? 93  ARG A C   1 
ATOM   2823 O  O   . ARG B 1 93  ? -36.461 -27.128 18.750  1.00 12.54 ? 93  ARG A O   1 
ATOM   2824 C  CB  . ARG B 1 93  ? -35.047 -29.629 16.936  1.00 14.75 ? 93  ARG A CB  1 
ATOM   2825 C  CG  . ARG B 1 93  ? -36.472 -30.120 17.236  1.00 19.91 ? 93  ARG A CG  1 
ATOM   2826 C  CD  . ARG B 1 93  ? -37.376 -29.556 16.211  1.00 21.86 ? 93  ARG A CD  1 
ATOM   2827 N  NE  . ARG B 1 93  ? -38.681 -30.275 16.300  1.00 30.60 ? 93  ARG A NE  1 
ATOM   2828 C  CZ  . ARG B 1 93  ? -39.657 -30.190 15.395  1.00 34.21 ? 93  ARG A CZ  1 
ATOM   2829 N  NH1 . ARG B 1 93  ? -39.465 -29.429 14.314  1.00 32.05 ? 93  ARG A NH1 1 
ATOM   2830 N  NH2 . ARG B 1 93  ? -40.806 -30.874 15.557  1.00 38.28 ? 93  ARG A NH2 1 
ATOM   2831 N  N   A GLN B 1 94  ? -34.863 -28.379 19.806  0.50 10.61 ? 94  GLN A N   1 
ATOM   2832 N  N   B GLN B 1 94  ? -34.896 -28.349 19.831  0.50 10.69 ? 94  GLN A N   1 
ATOM   2833 C  CA  A GLN B 1 94  ? -35.517 -28.461 21.084  0.50 11.78 ? 94  GLN A CA  1 
ATOM   2834 C  CA  B GLN B 1 94  ? -35.528 -28.154 21.119  0.50 11.74 ? 94  GLN A CA  1 
ATOM   2835 C  C   A GLN B 1 94  ? -34.469 -28.494 22.227  0.50 11.04 ? 94  GLN A C   1 
ATOM   2836 C  C   B GLN B 1 94  ? -34.569 -28.505 22.224  0.50 11.88 ? 94  GLN A C   1 
ATOM   2837 O  O   A GLN B 1 94  ? -33.363 -29.007 22.073  0.50 9.47  ? 94  GLN A O   1 
ATOM   2838 O  O   B GLN B 1 94  ? -33.647 -29.266 22.062  0.50 11.32 ? 94  GLN A O   1 
ATOM   2839 C  CB  A GLN B 1 94  ? -36.443 -29.703 21.108  0.50 11.65 ? 94  GLN A CB  1 
ATOM   2840 C  CB  B GLN B 1 94  ? -36.858 -28.976 21.185  0.50 11.99 ? 94  GLN A CB  1 
ATOM   2841 C  CG  A GLN B 1 94  ? -37.165 -29.742 22.406  0.50 16.03 ? 94  GLN A CG  1 
ATOM   2842 C  CG  B GLN B 1 94  ? -37.550 -29.280 22.523  0.50 15.52 ? 94  GLN A CG  1 
ATOM   2843 C  CD  A GLN B 1 94  ? -37.936 -30.972 22.440  0.50 15.22 ? 94  GLN A CD  1 
ATOM   2844 C  CD  B GLN B 1 94  ? -37.177 -30.672 23.018  0.50 15.90 ? 94  GLN A CD  1 
ATOM   2845 O  OE1 A GLN B 1 94  ? -37.344 -32.033 22.636  0.50 16.55 ? 94  GLN A OE1 1 
ATOM   2846 O  OE1 B GLN B 1 94  ? -36.039 -30.871 23.310  0.50 14.63 ? 94  GLN A OE1 1 
ATOM   2847 N  NE2 A GLN B 1 94  ? -39.212 -30.897 22.054  0.50 16.41 ? 94  GLN A NE2 1 
ATOM   2848 N  NE2 B GLN B 1 94  ? -38.146 -31.583 23.210  0.50 14.55 ? 94  GLN A NE2 1 
ATOM   2849 N  N   . VAL B 1 95  ? -34.862 -27.884 23.350  1.00 11.03 ? 95  VAL A N   1 
ATOM   2850 C  CA  . VAL B 1 95  ? -34.104 -28.093 24.618  1.00 11.05 ? 95  VAL A CA  1 
ATOM   2851 C  C   . VAL B 1 95  ? -35.176 -28.510 25.642  1.00 10.37 ? 95  VAL A C   1 
ATOM   2852 O  O   . VAL B 1 95  ? -36.266 -27.948 25.734  1.00 11.79 ? 95  VAL A O   1 
ATOM   2853 C  CB  . VAL B 1 95  ? -33.458 -26.789 25.008  1.00 11.45 ? 95  VAL A CB  1 
ATOM   2854 C  CG1 . VAL B 1 95  ? -32.927 -26.966 26.473  1.00 12.54 ? 95  VAL A CG1 1 
ATOM   2855 C  CG2 . VAL B 1 95  ? -32.300 -26.483 24.112  1.00 13.09 ? 95  VAL A CG2 1 
ATOM   2856 N  N   . HIS B 1 96  ? -34.781 -29.522 26.479  1.00 10.14 ? 96  HIS A N   1 
ATOM   2857 C  CA  . HIS B 1 96  ? -35.659 -29.917 27.668  1.00 9.96  ? 96  HIS A CA  1 
ATOM   2858 C  C   . HIS B 1 96  ? -34.656 -30.453 28.673  1.00 8.54  ? 96  HIS A C   1 
ATOM   2859 O  O   . HIS B 1 96  ? -33.440 -30.503 28.567  1.00 9.90  ? 96  HIS A O   1 
ATOM   2860 C  CB  . HIS B 1 96  ? -36.730 -30.885 27.242  1.00 9.49  ? 96  HIS A CB  1 
ATOM   2861 C  CG  . HIS B 1 96  ? -36.104 -32.166 26.699  1.00 10.56 ? 96  HIS A CG  1 
ATOM   2862 N  ND1 . HIS B 1 96  ? -36.024 -32.440 25.324  1.00 11.62 ? 96  HIS A ND1 1 
ATOM   2863 C  CD2 . HIS B 1 96  ? -35.559 -33.278 27.336  1.00 11.00 ? 96  HIS A CD2 1 
ATOM   2864 C  CE1 . HIS B 1 96  ? -35.398 -33.606 25.154  1.00 10.81 ? 96  HIS A CE1 1 
ATOM   2865 N  NE2 . HIS B 1 96  ? -35.093 -34.129 26.375  1.00 10.53 ? 96  HIS A NE2 1 
ATOM   2866 N  N   . LEU B 1 97  ? -35.372 -30.817 29.821  1.00 9.47  ? 97  LEU A N   1 
ATOM   2867 C  CA  . LEU B 1 97  ? -34.606 -31.199 31.042  1.00 10.29 ? 97  LEU A CA  1 
ATOM   2868 C  C   . LEU B 1 97  ? -35.284 -32.452 31.718  1.00 8.70  ? 97  LEU A C   1 
ATOM   2869 O  O   . LEU B 1 97  ? -36.469 -32.649 31.692  1.00 10.36 ? 97  LEU A O   1 
ATOM   2870 C  CB  . LEU B 1 97  ? -34.649 -29.995 32.035  1.00 9.58  ? 97  LEU A CB  1 
ATOM   2871 C  CG  . LEU B 1 97  ? -33.769 -30.215 33.310  1.00 9.63  ? 97  LEU A CG  1 
ATOM   2872 C  CD1 . LEU B 1 97  ? -32.278 -30.076 32.973  1.00 12.14 ? 97  LEU A CD1 1 
ATOM   2873 C  CD2 . LEU B 1 97  ? -34.215 -29.097 34.225  1.00 11.82 ? 97  LEU A CD2 1 
ATOM   2874 N  N   . HIS B 1 98  ? -34.353 -33.249 32.302  1.00 9.59  ? 98  HIS A N   1 
ATOM   2875 C  CA  . HIS B 1 98  ? -34.787 -34.407 33.091  1.00 10.56 ? 98  HIS A CA  1 
ATOM   2876 C  C   . HIS B 1 98  ? -34.254 -34.208 34.530  1.00 8.84  ? 98  HIS A C   1 
ATOM   2877 O  O   . HIS B 1 98  ? -33.163 -33.754 34.719  1.00 10.74 ? 98  HIS A O   1 
ATOM   2878 C  CB  . HIS B 1 98  ? -34.228 -35.698 32.496  1.00 10.77 ? 98  HIS A CB  1 
ATOM   2879 C  CG  . HIS B 1 98  ? -34.621 -35.969 31.050  1.00 11.79 ? 98  HIS A CG  1 
ATOM   2880 N  ND1 . HIS B 1 98  ? -35.748 -36.596 30.701  1.00 10.63 ? 98  HIS A ND1 1 
ATOM   2881 C  CD2 . HIS B 1 98  ? -33.946 -35.619 29.957  1.00 10.92 ? 98  HIS A CD2 1 
ATOM   2882 C  CE1 . HIS B 1 98  ? -35.793 -36.667 29.257  1.00 10.25 ? 98  HIS A CE1 1 
ATOM   2883 N  NE2 . HIS B 1 98  ? -34.662 -36.110 28.856  1.00 7.84  ? 98  HIS A NE2 1 
ATOM   2884 N  N   . TRP B 1 99  ? -35.108 -34.676 35.460  1.00 11.31 ? 99  TRP A N   1 
ATOM   2885 C  CA  . TRP B 1 99  ? -34.766 -34.585 36.896  1.00 11.74 ? 99  TRP A CA  1 
ATOM   2886 C  C   . TRP B 1 99  ? -35.404 -35.750 37.568  1.00 11.59 ? 99  TRP A C   1 
ATOM   2887 O  O   . TRP B 1 99  ? -36.187 -36.556 37.045  1.00 12.07 ? 99  TRP A O   1 
ATOM   2888 C  CB  . TRP B 1 99  ? -35.169 -33.235 37.514  1.00 11.77 ? 99  TRP A CB  1 
ATOM   2889 C  CG  . TRP B 1 99  ? -36.614 -33.002 37.325  1.00 12.08 ? 99  TRP A CG  1 
ATOM   2890 C  CD1 . TRP B 1 99  ? -37.643 -33.480 38.126  1.00 11.76 ? 99  TRP A CD1 1 
ATOM   2891 C  CD2 . TRP B 1 99  ? -37.282 -32.302 36.225  1.00 11.86 ? 99  TRP A CD2 1 
ATOM   2892 N  NE1 . TRP B 1 99  ? -38.881 -33.063 37.689  1.00 10.95 ? 99  TRP A NE1 1 
ATOM   2893 C  CE2 . TRP B 1 99  ? -38.716 -32.326 36.492  1.00 11.75 ? 99  TRP A CE2 1 
ATOM   2894 C  CE3 . TRP B 1 99  ? -36.820 -31.532 35.122  1.00 11.33 ? 99  TRP A CE3 1 
ATOM   2895 C  CZ2 . TRP B 1 99  ? -39.654 -31.733 35.710  1.00 12.84 ? 99  TRP A CZ2 1 
ATOM   2896 C  CZ3 . TRP B 1 99  ? -37.789 -30.930 34.317  1.00 12.38 ? 99  TRP A CZ3 1 
ATOM   2897 C  CH2 . TRP B 1 99  ? -39.151 -31.045 34.552  1.00 12.16 ? 99  TRP A CH2 1 
ATOM   2898 N  N   . GLY B 1 100 ? -35.064 -35.872 38.875  1.00 12.85 ? 100 GLY A N   1 
ATOM   2899 C  CA  . GLY B 1 100 ? -35.637 -36.928 39.695  1.00 15.62 ? 100 GLY A CA  1 
ATOM   2900 C  C   . GLY B 1 100 ? -36.357 -36.296 40.856  1.00 13.92 ? 100 GLY A C   1 
ATOM   2901 O  O   . GLY B 1 100 ? -36.435 -35.101 40.956  1.00 13.62 ? 100 GLY A O   1 
ATOM   2902 N  N   . SER B 1 101 ? -36.948 -37.139 41.725  1.00 16.16 ? 101 SER A N   1 
ATOM   2903 C  CA  . SER B 1 101 ? -37.837 -36.524 42.790  1.00 16.49 ? 101 SER A CA  1 
ATOM   2904 C  C   . SER B 1 101 ? -36.989 -36.081 43.927  1.00 15.63 ? 101 SER A C   1 
ATOM   2905 O  O   . SER B 1 101 ? -37.517 -35.360 44.781  1.00 17.81 ? 101 SER A O   1 
ATOM   2906 C  CB  . SER B 1 101 ? -38.840 -37.537 43.346  1.00 17.75 ? 101 SER A CB  1 
ATOM   2907 O  OG  . SER B 1 101 ? -38.167 -38.634 43.924  1.00 18.59 ? 101 SER A OG  1 
ATOM   2908 N  N   . ALA B 1 102 ? -35.717 -36.423 43.952  1.00 14.43 ? 102 ALA A N   1 
ATOM   2909 C  CA  . ALA B 1 102 ? -34.860 -35.789 44.934  1.00 15.28 ? 102 ALA A CA  1 
ATOM   2910 C  C   . ALA B 1 102 ? -33.529 -35.440 44.306  1.00 14.49 ? 102 ALA A C   1 
ATOM   2911 O  O   . ALA B 1 102 ? -33.120 -36.022 43.238  1.00 15.50 ? 102 ALA A O   1 
ATOM   2912 C  CB  . ALA B 1 102 ? -34.652 -36.758 46.061  1.00 15.98 ? 102 ALA A CB  1 
ATOM   2913 N  N   . ASP B 1 103 ? -32.787 -34.584 44.974  1.00 15.08 ? 103 ASP A N   1 
ATOM   2914 C  CA  . ASP B 1 103 ? -31.555 -34.042 44.326  1.00 13.89 ? 103 ASP A CA  1 
ATOM   2915 C  C   . ASP B 1 103 ? -30.471 -35.038 44.101  1.00 16.37 ? 103 ASP A C   1 
ATOM   2916 O  O   . ASP B 1 103 ? -29.514 -34.770 43.357  1.00 18.79 ? 103 ASP A O   1 
ATOM   2917 C  CB  . ASP B 1 103 ? -30.952 -32.854 45.140  1.00 16.44 ? 103 ASP A CB  1 
ATOM   2918 C  CG  . ASP B 1 103 ? -31.906 -31.727 45.265  1.00 17.61 ? 103 ASP A CG  1 
ATOM   2919 O  OD1 . ASP B 1 103 ? -32.857 -31.570 44.456  1.00 20.07 ? 103 ASP A OD1 1 
ATOM   2920 O  OD2 . ASP B 1 103 ? -31.659 -30.891 46.207  1.00 19.10 ? 103 ASP A OD2 1 
ATOM   2921 N  N   . ASP B 1 104 ? -30.481 -36.194 44.819  1.00 16.62 ? 104 ASP A N   1 
ATOM   2922 C  CA  . ASP B 1 104 ? -29.402 -37.147 44.722  1.00 16.11 ? 104 ASP A CA  1 
ATOM   2923 C  C   . ASP B 1 104 ? -29.278 -37.931 43.468  1.00 17.87 ? 104 ASP A C   1 
ATOM   2924 O  O   . ASP B 1 104 ? -28.185 -38.507 43.233  1.00 20.09 ? 104 ASP A O   1 
ATOM   2925 C  CB  . ASP B 1 104 ? -29.367 -38.170 45.917  1.00 20.65 ? 104 ASP A CB  1 
ATOM   2926 C  CG  . ASP B 1 104 ? -30.537 -38.996 45.937  1.00 19.82 ? 104 ASP A CG  1 
ATOM   2927 O  OD1 . ASP B 1 104 ? -31.553 -38.472 46.359  1.00 24.79 ? 104 ASP A OD1 1 
ATOM   2928 O  OD2 . ASP B 1 104 ? -30.484 -40.175 45.485  1.00 25.20 ? 104 ASP A OD2 1 
ATOM   2929 N  N   . HIS B 1 105 ? -30.336 -37.965 42.662  1.00 16.13 ? 105 HIS A N   1 
ATOM   2930 C  CA  . HIS B 1 105 ? -30.199 -38.641 41.357  1.00 18.59 ? 105 HIS A CA  1 
ATOM   2931 C  C   . HIS B 1 105 ? -31.278 -38.110 40.457  1.00 20.05 ? 105 HIS A C   1 
ATOM   2932 O  O   . HIS B 1 105 ? -32.231 -37.474 40.889  1.00 23.40 ? 105 HIS A O   1 
ATOM   2933 C  CB  . HIS B 1 105 ? -30.170 -40.188 41.443  1.00 21.11 ? 105 HIS A CB  1 
ATOM   2934 C  CG  . HIS B 1 105 ? -31.417 -40.846 41.950  1.00 24.61 ? 105 HIS A CG  1 
ATOM   2935 N  ND1 . HIS B 1 105 ? -31.625 -41.081 43.290  1.00 27.98 ? 105 HIS A ND1 1 
ATOM   2936 C  CD2 . HIS B 1 105 ? -32.460 -41.505 41.280  1.00 27.33 ? 105 HIS A CD2 1 
ATOM   2937 C  CE1 . HIS B 1 105 ? -32.776 -41.775 43.460  1.00 30.59 ? 105 HIS A CE1 1 
ATOM   2938 N  NE2 . HIS B 1 105 ? -33.296 -42.022 42.228  1.00 31.96 ? 105 HIS A NE2 1 
ATOM   2939 N  N   . GLY B 1 106 ? -31.158 -38.308 39.139  1.00 17.24 ? 106 GLY A N   1 
ATOM   2940 C  CA  . GLY B 1 106 ? -32.097 -37.560 38.350  1.00 16.18 ? 106 GLY A CA  1 
ATOM   2941 C  C   . GLY B 1 106 ? -31.503 -37.477 36.953  1.00 13.72 ? 106 GLY A C   1 
ATOM   2942 O  O   . GLY B 1 106 ? -32.298 -37.389 35.995  1.00 16.90 ? 106 GLY A O   1 
ATOM   2943 N  N   . SER B 1 107 ? -30.180 -37.480 36.817  1.00 12.67 ? 107 SER A N   1 
ATOM   2944 C  CA  . SER B 1 107 ? -29.675 -37.559 35.442  1.00 12.40 ? 107 SER A CA  1 
ATOM   2945 C  C   . SER B 1 107 ? -30.082 -38.889 34.761  1.00 11.81 ? 107 SER A C   1 
ATOM   2946 O  O   . SER B 1 107 ? -30.332 -39.942 35.386  1.00 14.88 ? 107 SER A O   1 
ATOM   2947 C  CB  . SER B 1 107 ? -28.190 -37.364 35.376  1.00 11.15 ? 107 SER A CB  1 
ATOM   2948 O  OG  . SER B 1 107 ? -27.497 -38.442 36.104  1.00 12.38 ? 107 SER A OG  1 
ATOM   2949 N  N   . GLU B 1 108 ? -30.073 -38.860 33.412  1.00 12.31 ? 108 GLU A N   1 
ATOM   2950 C  CA  . GLU B 1 108 ? -30.328 -40.057 32.647  1.00 11.39 ? 108 GLU A CA  1 
ATOM   2951 C  C   . GLU B 1 108 ? -29.059 -40.827 32.421  1.00 12.50 ? 108 GLU A C   1 
ATOM   2952 O  O   . GLU B 1 108 ? -29.015 -42.055 32.745  1.00 12.41 ? 108 GLU A O   1 
ATOM   2953 C  CB  . GLU B 1 108 ? -30.995 -39.649 31.293  1.00 11.02 ? 108 GLU A CB  1 
ATOM   2954 C  CG  . GLU B 1 108 ? -32.328 -39.055 31.616  1.00 13.17 ? 108 GLU A CG  1 
ATOM   2955 C  CD  . GLU B 1 108 ? -33.378 -39.263 30.556  1.00 11.07 ? 108 GLU A CD  1 
ATOM   2956 O  OE1 . GLU B 1 108 ? -33.031 -39.022 29.334  1.00 12.96 ? 108 GLU A OE1 1 
ATOM   2957 O  OE2 . GLU B 1 108 ? -34.502 -39.570 30.833  1.00 11.88 ? 108 GLU A OE2 1 
ATOM   2958 N  N   . HIS B 1 109 ? -28.036 -40.249 31.848  1.00 11.50 ? 109 HIS A N   1 
ATOM   2959 C  CA  . HIS B 1 109 ? -26.672 -40.882 31.800  1.00 11.46 ? 109 HIS A CA  1 
ATOM   2960 C  C   . HIS B 1 109 ? -26.068 -40.932 33.207  1.00 13.19 ? 109 HIS A C   1 
ATOM   2961 O  O   . HIS B 1 109 ? -26.323 -40.022 34.028  1.00 12.73 ? 109 HIS A O   1 
ATOM   2962 C  CB  . HIS B 1 109 ? -25.742 -40.183 30.811  1.00 11.84 ? 109 HIS A CB  1 
ATOM   2963 C  CG  . HIS B 1 109 ? -26.278 -40.350 29.379  1.00 12.76 ? 109 HIS A CG  1 
ATOM   2964 N  ND1 . HIS B 1 109 ? -27.195 -39.476 28.836  1.00 10.83 ? 109 HIS A ND1 1 
ATOM   2965 C  CD2 . HIS B 1 109 ? -26.039 -41.356 28.444  1.00 12.64 ? 109 HIS A CD2 1 
ATOM   2966 C  CE1 . HIS B 1 109 ? -27.452 -39.874 27.525  1.00 11.64 ? 109 HIS A CE1 1 
ATOM   2967 N  NE2 . HIS B 1 109 ? -26.797 -41.032 27.325  1.00 12.38 ? 109 HIS A NE2 1 
ATOM   2968 N  N   . ILE B 1 110 ? -25.282 -41.979 33.460  1.00 13.64 ? 110 ILE A N   1 
ATOM   2969 C  CA  . ILE B 1 110 ? -24.640 -42.154 34.781  1.00 14.00 ? 110 ILE A CA  1 
ATOM   2970 C  C   . ILE B 1 110 ? -23.186 -42.498 34.487  1.00 14.63 ? 110 ILE A C   1 
ATOM   2971 O  O   . ILE B 1 110 ? -22.980 -43.500 33.726  1.00 16.32 ? 110 ILE A O   1 
ATOM   2972 C  CB  . ILE B 1 110 ? -25.376 -43.227 35.580  1.00 13.10 ? 110 ILE A CB  1 
ATOM   2973 C  CG1 . ILE B 1 110 ? -26.826 -42.879 35.818  1.00 14.64 ? 110 ILE A CG1 1 
ATOM   2974 C  CG2 . ILE B 1 110 ? -24.580 -43.492 36.927  1.00 14.89 ? 110 ILE A CG2 1 
ATOM   2975 C  CD1 . ILE B 1 110 ? -27.634 -43.909 36.669  1.00 17.29 ? 110 ILE A CD1 1 
ATOM   2976 N  N   . VAL B 1 111 ? -22.218 -41.843 35.123  1.00 17.85 ? 111 VAL A N   1 
ATOM   2977 C  CA  . VAL B 1 111 ? -20.830 -41.949 34.695  1.00 18.27 ? 111 VAL A CA  1 
ATOM   2978 C  C   . VAL B 1 111 ? -20.051 -42.599 35.850  1.00 20.24 ? 111 VAL A C   1 
ATOM   2979 O  O   . VAL B 1 111 ? -19.989 -42.002 36.887  1.00 21.44 ? 111 VAL A O   1 
ATOM   2980 C  CB  . VAL B 1 111 ? -20.201 -40.566 34.341  1.00 18.04 ? 111 VAL A CB  1 
ATOM   2981 C  CG1 . VAL B 1 111 ? -18.755 -40.814 33.920  1.00 21.49 ? 111 VAL A CG1 1 
ATOM   2982 C  CG2 . VAL B 1 111 ? -20.984 -39.898 33.180  1.00 21.41 ? 111 VAL A CG2 1 
ATOM   2983 N  N   . ASP B 1 112 ? -19.541 -43.800 35.606  1.00 17.46 ? 112 ASP A N   1 
ATOM   2984 C  CA  . ASP B 1 112 ? -18.783 -44.571 36.692  1.00 18.49 ? 112 ASP A CA  1 
ATOM   2985 C  C   . ASP B 1 112 ? -19.620 -44.554 37.992  1.00 22.65 ? 112 ASP A C   1 
ATOM   2986 O  O   . ASP B 1 112 ? -19.070 -44.347 39.113  1.00 22.19 ? 112 ASP A O   1 
ATOM   2987 C  CB  . ASP B 1 112 ? -17.414 -43.977 36.917  1.00 19.03 ? 112 ASP A CB  1 
ATOM   2988 C  CG  . ASP B 1 112 ? -16.493 -44.212 35.743  1.00 20.98 ? 112 ASP A CG  1 
ATOM   2989 O  OD1 . ASP B 1 112 ? -16.571 -45.294 35.112  1.00 23.16 ? 112 ASP A OD1 1 
ATOM   2990 O  OD2 . ASP B 1 112 ? -15.648 -43.338 35.533  1.00 21.58 ? 112 ASP A OD2 1 
ATOM   2991 N  N   . GLY B 1 113 ? -20.932 -44.772 37.838  1.00 18.54 ? 113 GLY A N   1 
ATOM   2992 C  CA  . GLY B 1 113 ? -21.834 -44.892 38.976  1.00 17.94 ? 113 GLY A CA  1 
ATOM   2993 C  C   . GLY B 1 113 ? -22.278 -43.575 39.572  1.00 19.18 ? 113 GLY A C   1 
ATOM   2994 O  O   . GLY B 1 113 ? -23.128 -43.605 40.487  1.00 20.42 ? 113 GLY A O   1 
ATOM   2995 N  N   . VAL B 1 114 ? -21.789 -42.419 39.069  1.00 18.60 ? 114 VAL A N   1 
ATOM   2996 C  CA  . VAL B 1 114 ? -22.176 -41.099 39.558  1.00 19.08 ? 114 VAL A CA  1 
ATOM   2997 C  C   . VAL B 1 114 ? -23.454 -40.561 38.828  1.00 20.67 ? 114 VAL A C   1 
ATOM   2998 O  O   . VAL B 1 114 ? -23.456 -40.432 37.543  1.00 18.30 ? 114 VAL A O   1 
ATOM   2999 C  CB  . VAL B 1 114 ? -21.020 -40.099 39.426  1.00 21.46 ? 114 VAL A CB  1 
ATOM   3000 C  CG1 . VAL B 1 114 ? -21.455 -38.699 39.887  1.00 25.79 ? 114 VAL A CG1 1 
ATOM   3001 C  CG2 . VAL B 1 114 ? -19.847 -40.568 40.303  1.00 25.04 ? 114 VAL A CG2 1 
ATOM   3002 N  N   . SER B 1 115 ? -24.514 -40.266 39.599  1.00 19.12 ? 115 SER A N   1 
ATOM   3003 C  CA  . SER B 1 115 ? -25.674 -39.568 39.060  1.00 17.47 ? 115 SER A CA  1 
ATOM   3004 C  C   . SER B 1 115 ? -25.568 -38.110 39.402  1.00 20.97 ? 115 SER A C   1 
ATOM   3005 O  O   . SER B 1 115 ? -24.967 -37.727 40.443  1.00 24.51 ? 115 SER A O   1 
ATOM   3006 C  CB  . SER B 1 115 ? -27.014 -40.080 39.640  1.00 20.85 ? 115 SER A CB  1 
ATOM   3007 O  OG  . SER B 1 115 ? -27.291 -41.405 39.175  1.00 22.96 ? 115 SER A OG  1 
ATOM   3008 N  N   . TYR B 1 116 ? -26.143 -37.303 38.518  1.00 15.71 ? 116 TYR A N   1 
ATOM   3009 C  CA  . TYR B 1 116 ? -26.261 -35.879 38.805  1.00 15.63 ? 116 TYR A CA  1 
ATOM   3010 C  C   . TYR B 1 116 ? -27.723 -35.601 39.118  1.00 13.46 ? 116 TYR A C   1 
ATOM   3011 O  O   . TYR B 1 116 ? -28.533 -36.486 39.042  1.00 14.48 ? 116 TYR A O   1 
ATOM   3012 C  CB  . TYR B 1 116 ? -25.769 -35.125 37.568  1.00 13.54 ? 116 TYR A CB  1 
ATOM   3013 C  CG  . TYR B 1 116 ? -24.292 -35.302 37.429  1.00 13.71 ? 116 TYR A CG  1 
ATOM   3014 C  CD1 . TYR B 1 116 ? -23.378 -34.488 38.153  1.00 16.76 ? 116 TYR A CD1 1 
ATOM   3015 C  CD2 . TYR B 1 116 ? -23.790 -36.262 36.564  1.00 15.90 ? 116 TYR A CD2 1 
ATOM   3016 C  CE1 . TYR B 1 116 ? -21.999 -34.697 37.987  1.00 20.44 ? 116 TYR A CE1 1 
ATOM   3017 C  CE2 . TYR B 1 116 ? -22.465 -36.462 36.398  1.00 18.03 ? 116 TYR A CE2 1 
ATOM   3018 C  CZ  . TYR B 1 116 ? -21.583 -35.695 37.108  1.00 22.45 ? 116 TYR A CZ  1 
ATOM   3019 O  OH  . TYR B 1 116 ? -20.233 -35.972 36.877  1.00 32.85 ? 116 TYR A OH  1 
ATOM   3020 N  N   . ALA B 1 117 ? -28.049 -34.392 39.570  1.00 12.90 ? 117 ALA A N   1 
ATOM   3021 C  CA  . ALA B 1 117 ? -29.379 -34.078 39.960  1.00 12.90 ? 117 ALA A CA  1 
ATOM   3022 C  C   . ALA B 1 117 ? -30.300 -34.002 38.749  1.00 11.17 ? 117 ALA A C   1 
ATOM   3023 O  O   . ALA B 1 117 ? -31.477 -34.168 38.853  1.00 12.50 ? 117 ALA A O   1 
ATOM   3024 C  CB  . ALA B 1 117 ? -29.408 -32.709 40.656  1.00 14.95 ? 117 ALA A CB  1 
ATOM   3025 N  N   . ALA B 1 118 ? -29.768 -33.538 37.591  1.00 12.27 ? 118 ALA A N   1 
ATOM   3026 C  CA  . ALA B 1 118 ? -30.651 -33.348 36.398  1.00 10.94 ? 118 ALA A CA  1 
ATOM   3027 C  C   . ALA B 1 118 ? -29.720 -33.405 35.166  1.00 10.33 ? 118 ALA A C   1 
ATOM   3028 O  O   . ALA B 1 118 ? -28.502 -33.486 35.230  1.00 10.92 ? 118 ALA A O   1 
ATOM   3029 C  CB  . ALA B 1 118 ? -31.308 -31.987 36.476  1.00 12.04 ? 118 ALA A CB  1 
ATOM   3030 N  N   . GLU B 1 119 ? -30.396 -33.386 33.992  1.00 9.63  ? 119 GLU A N   1 
ATOM   3031 C  CA  . GLU B 1 119 ? -29.605 -33.490 32.693  1.00 9.23  ? 119 GLU A CA  1 
ATOM   3032 C  C   . GLU B 1 119 ? -30.459 -32.756 31.629  1.00 9.06  ? 119 GLU A C   1 
ATOM   3033 O  O   . GLU B 1 119 ? -31.636 -33.023 31.423  1.00 9.21  ? 119 GLU A O   1 
ATOM   3034 C  CB  . GLU B 1 119 ? -29.531 -34.985 32.345  1.00 10.35 ? 119 GLU A CB  1 
ATOM   3035 C  CG  . GLU B 1 119 ? -28.689 -35.173 31.090  1.00 10.72 ? 119 GLU A CG  1 
ATOM   3036 C  CD  . GLU B 1 119 ? -28.340 -36.618 30.831  1.00 12.41 ? 119 GLU A CD  1 
ATOM   3037 O  OE1 . GLU B 1 119 ? -28.154 -37.357 31.820  1.00 11.91 ? 119 GLU A OE1 1 
ATOM   3038 O  OE2 . GLU B 1 119 ? -28.274 -37.016 29.647  1.00 11.96 ? 119 GLU A OE2 1 
ATOM   3039 N  N   . LEU B 1 120 ? -29.732 -31.814 30.987  1.00 9.81  ? 120 LEU A N   1 
ATOM   3040 C  CA  . LEU B 1 120 ? -30.285 -31.010 29.899  1.00 10.27 ? 120 LEU A CA  1 
ATOM   3041 C  C   . LEU B 1 120 ? -29.982 -31.780 28.585  1.00 9.41  ? 120 LEU A C   1 
ATOM   3042 O  O   . LEU B 1 120 ? -28.884 -32.185 28.376  1.00 10.37 ? 120 LEU A O   1 
ATOM   3043 C  CB  . LEU B 1 120 ? -29.632 -29.643 29.928  1.00 12.06 ? 120 LEU A CB  1 
ATOM   3044 C  CG  . LEU B 1 120 ? -30.263 -28.576 29.025  1.00 12.77 ? 120 LEU A CG  1 
ATOM   3045 C  CD1 . LEU B 1 120 ? -31.542 -28.012 29.614  1.00 13.98 ? 120 LEU A CD1 1 
ATOM   3046 C  CD2 . LEU B 1 120 ? -29.151 -27.555 28.719  1.00 16.12 ? 120 LEU A CD2 1 
ATOM   3047 N  N   . HIS B 1 121 ? -31.025 -31.789 27.746  1.00 10.87 ? 121 HIS A N   1 
ATOM   3048 C  CA  . HIS B 1 121 ? -30.850 -32.336 26.366  1.00 10.64 ? 121 HIS A CA  1 
ATOM   3049 C  C   . HIS B 1 121 ? -31.149 -31.250 25.315  1.00 10.25 ? 121 HIS A C   1 
ATOM   3050 O  O   . HIS B 1 121 ? -32.176 -30.570 25.391  1.00 10.24 ? 121 HIS A O   1 
ATOM   3051 C  CB  . HIS B 1 121 ? -31.758 -33.510 26.140  1.00 9.93  ? 121 HIS A CB  1 
ATOM   3052 C  CG  . HIS B 1 121 ? -31.387 -34.721 26.918  1.00 9.66  ? 121 HIS A CG  1 
ATOM   3053 N  ND1 . HIS B 1 121 ? -32.245 -35.678 27.196  1.00 12.51 ? 121 HIS A ND1 1 
ATOM   3054 C  CD2 . HIS B 1 121 ? -30.143 -35.070 27.463  1.00 9.36  ? 121 HIS A CD2 1 
ATOM   3055 C  CE1 . HIS B 1 121 ? -31.659 -36.639 27.882  1.00 9.49  ? 121 HIS A CE1 1 
ATOM   3056 N  NE2 . HIS B 1 121 ? -30.336 -36.313 28.088  1.00 9.23  ? 121 HIS A NE2 1 
ATOM   3057 N  N   . VAL B 1 122 ? -30.163 -31.171 24.378  1.00 10.84 ? 122 VAL A N   1 
ATOM   3058 C  CA  . VAL B 1 122 ? -30.189 -30.182 23.254  1.00 9.60  ? 122 VAL A CA  1 
ATOM   3059 C  C   . VAL B 1 122 ? -30.342 -31.021 21.977  1.00 9.19  ? 122 VAL A C   1 
ATOM   3060 O  O   . VAL B 1 122 ? -29.399 -31.679 21.600  1.00 10.23 ? 122 VAL A O   1 
ATOM   3061 C  CB  . VAL B 1 122 ? -28.969 -29.334 23.272  1.00 10.35 ? 122 VAL A CB  1 
ATOM   3062 C  CG1 . VAL B 1 122 ? -29.243 -28.166 22.290  1.00 9.54  ? 122 VAL A CG1 1 
ATOM   3063 C  CG2 . VAL B 1 122 ? -28.755 -28.686 24.682  1.00 11.23 ? 122 VAL A CG2 1 
ATOM   3064 N  N   . VAL B 1 123 ? -31.530 -30.974 21.425  1.00 8.90  ? 123 VAL A N   1 
ATOM   3065 C  CA  . VAL B 1 123 ? -31.881 -31.915 20.273  1.00 9.11  ? 123 VAL A CA  1 
ATOM   3066 C  C   . VAL B 1 123 ? -31.714 -31.179 18.917  1.00 9.66  ? 123 VAL A C   1 
ATOM   3067 O  O   . VAL B 1 123 ? -32.277 -30.080 18.751  1.00 10.17 ? 123 VAL A O   1 
ATOM   3068 C  CB  . VAL B 1 123 ? -33.318 -32.376 20.473  1.00 9.97  ? 123 VAL A CB  1 
ATOM   3069 C  CG1 . VAL B 1 123 ? -33.639 -33.355 19.321  1.00 10.54 ? 123 VAL A CG1 1 
ATOM   3070 C  CG2 . VAL B 1 123 ? -33.524 -33.074 21.841  1.00 11.72 ? 123 VAL A CG2 1 
ATOM   3071 N  N   . HIS B 1 124 ? -31.002 -31.889 18.034  1.00 9.33  ? 124 HIS A N   1 
ATOM   3072 C  CA  . HIS B 1 124 ? -30.682 -31.308 16.706  1.00 9.49  ? 124 HIS A CA  1 
ATOM   3073 C  C   . HIS B 1 124 ? -31.035 -32.428 15.705  1.00 10.21 ? 124 HIS A C   1 
ATOM   3074 O  O   . HIS B 1 124 ? -30.985 -33.628 15.957  1.00 10.79 ? 124 HIS A O   1 
ATOM   3075 C  CB  . HIS B 1 124 ? -29.218 -31.022 16.516  1.00 10.50 ? 124 HIS A CB  1 
ATOM   3076 C  CG  . HIS B 1 124 ? -28.638 -30.149 17.597  1.00 10.65 ? 124 HIS A CG  1 
ATOM   3077 N  ND1 . HIS B 1 124 ? -28.352 -30.668 18.835  1.00 12.16 ? 124 HIS A ND1 1 
ATOM   3078 C  CD2 . HIS B 1 124 ? -28.209 -28.853 17.593  1.00 10.54 ? 124 HIS A CD2 1 
ATOM   3079 C  CE1 . HIS B 1 124 ? -27.789 -29.731 19.587  1.00 11.16 ? 124 HIS A CE1 1 
ATOM   3080 N  NE2 . HIS B 1 124 ? -27.722 -28.582 18.877  1.00 11.61 ? 124 HIS A NE2 1 
ATOM   3081 N  N   . TRP B 1 125 ? -31.306 -31.991 14.432  1.00 9.70  ? 125 TRP A N   1 
ATOM   3082 C  CA  . TRP B 1 125 ? -31.568 -33.006 13.414  1.00 10.67 ? 125 TRP A CA  1 
ATOM   3083 C  C   . TRP B 1 125 ? -30.910 -32.681 12.039  1.00 10.63 ? 125 TRP A C   1 
ATOM   3084 O  O   . TRP B 1 125 ? -30.620 -31.506 11.707  1.00 11.77 ? 125 TRP A O   1 
ATOM   3085 C  CB  . TRP B 1 125 ? -33.059 -33.169 13.119  1.00 10.58 ? 125 TRP A CB  1 
ATOM   3086 C  CG  . TRP B 1 125 ? -33.725 -31.849 12.690  1.00 11.11 ? 125 TRP A CG  1 
ATOM   3087 C  CD1 . TRP B 1 125 ? -34.092 -30.788 13.490  1.00 11.53 ? 125 TRP A CD1 1 
ATOM   3088 C  CD2 . TRP B 1 125 ? -34.215 -31.487 11.346  1.00 12.24 ? 125 TRP A CD2 1 
ATOM   3089 N  NE1 . TRP B 1 125 ? -34.754 -29.788 12.723  1.00 12.35 ? 125 TRP A NE1 1 
ATOM   3090 C  CE2 . TRP B 1 125 ? -34.835 -30.203 11.442  1.00 13.43 ? 125 TRP A CE2 1 
ATOM   3091 C  CE3 . TRP B 1 125 ? -34.086 -32.118 10.078  1.00 15.18 ? 125 TRP A CE3 1 
ATOM   3092 C  CZ2 . TRP B 1 125 ? -35.334 -29.545 10.343  1.00 14.21 ? 125 TRP A CZ2 1 
ATOM   3093 C  CZ3 . TRP B 1 125 ? -34.658 -31.442 8.965   1.00 15.35 ? 125 TRP A CZ3 1 
ATOM   3094 C  CH2 . TRP B 1 125 ? -35.253 -30.215 9.123   1.00 16.52 ? 125 TRP A CH2 1 
ATOM   3095 N  N   . ASN B 1 126 ? -30.638 -33.766 11.303  1.00 11.58 ? 126 ASN A N   1 
ATOM   3096 C  CA  . ASN B 1 126 ? -29.832 -33.650 10.072  1.00 10.98 ? 126 ASN A CA  1 
ATOM   3097 C  C   . ASN B 1 126 ? -30.590 -33.148 8.869   1.00 12.22 ? 126 ASN A C   1 
ATOM   3098 O  O   . ASN B 1 126 ? -31.273 -33.873 8.210   1.00 12.57 ? 126 ASN A O   1 
ATOM   3099 C  CB  . ASN B 1 126 ? -29.410 -35.098 9.734   1.00 11.81 ? 126 ASN A CB  1 
ATOM   3100 C  CG  . ASN B 1 126 ? -28.392 -35.127 8.616   1.00 15.55 ? 126 ASN A CG  1 
ATOM   3101 O  OD1 . ASN B 1 126 ? -28.249 -34.119 7.830   1.00 13.64 ? 126 ASN A OD1 1 
ATOM   3102 N  ND2 . ASN B 1 126 ? -27.620 -36.209 8.550   1.00 16.38 ? 126 ASN A ND2 1 
ATOM   3103 N  N   . SER B 1 127 ? -30.531 -31.829 8.738   1.00 11.72 ? 127 SER A N   1 
ATOM   3104 C  CA  . SER B 1 127 ? -31.327 -31.125 7.703   1.00 12.91 ? 127 SER A CA  1 
ATOM   3105 C  C   . SER B 1 127 ? -30.484 -31.201 6.400   1.00 12.73 ? 127 SER A C   1 
ATOM   3106 O  O   . SER B 1 127 ? -31.071 -30.791 5.326   1.00 13.81 ? 127 SER A O   1 
ATOM   3107 C  CB  . SER B 1 127 ? -31.605 -29.659 8.134   1.00 11.57 ? 127 SER A CB  1 
ATOM   3108 O  OG  . SER B 1 127 ? -30.431 -29.035 8.468   1.00 13.45 ? 127 SER A OG  1 
ATOM   3109 N  N   . ASP B 1 128 ? -29.235 -31.651 6.439   1.00 11.49 ? 128 ASP A N   1 
ATOM   3110 C  CA  . ASP B 1 128 ? -28.511 -31.924 5.173   1.00 12.48 ? 128 ASP A CA  1 
ATOM   3111 C  C   . ASP B 1 128 ? -29.085 -33.049 4.432   1.00 13.84 ? 128 ASP A C   1 
ATOM   3112 O  O   . ASP B 1 128 ? -28.959 -33.122 3.196   1.00 16.86 ? 128 ASP A O   1 
ATOM   3113 C  CB  . ASP B 1 128 ? -27.006 -32.092 5.395   1.00 13.93 ? 128 ASP A CB  1 
ATOM   3114 C  CG  . ASP B 1 128 ? -26.261 -30.793 5.675   1.00 13.53 ? 128 ASP A CG  1 
ATOM   3115 O  OD1 . ASP B 1 128 ? -25.067 -30.950 6.032   1.00 16.72 ? 128 ASP A OD1 1 
ATOM   3116 O  OD2 . ASP B 1 128 ? -26.860 -29.658 5.555   1.00 18.08 ? 128 ASP A OD2 1 
ATOM   3117 N  N   . LYS B 1 129 ? -29.730 -33.999 5.094   1.00 14.45 ? 129 LYS A N   1 
ATOM   3118 C  CA  . LYS B 1 129 ? -30.251 -35.199 4.450   1.00 12.68 ? 129 LYS A CA  1 
ATOM   3119 C  C   . LYS B 1 129 ? -31.740 -35.398 4.508   1.00 12.77 ? 129 LYS A C   1 
ATOM   3120 O  O   . LYS B 1 129 ? -32.333 -36.079 3.666   1.00 14.32 ? 129 LYS A O   1 
ATOM   3121 C  CB  . LYS B 1 129 ? -29.606 -36.450 5.075   1.00 15.20 ? 129 LYS A CB  1 
ATOM   3122 C  CG  . LYS B 1 129 ? -28.150 -36.600 4.764   1.00 18.02 ? 129 LYS A CG  1 
ATOM   3123 C  CD  . LYS B 1 129 ? -27.633 -37.962 5.270   1.00 20.13 ? 129 LYS A CD  1 
ATOM   3124 C  CE  . LYS B 1 129 ? -28.399 -39.070 4.673   1.00 20.18 ? 129 LYS A CE  1 
ATOM   3125 N  NZ  . LYS B 1 129 ? -27.741 -40.363 5.093   1.00 21.10 ? 129 LYS A NZ  1 
ATOM   3126 N  N   . TYR B 1 130 ? -32.423 -34.889 5.535   1.00 12.06 ? 130 TYR A N   1 
ATOM   3127 C  CA  . TYR B 1 130 ? -33.826 -35.173 5.695   1.00 11.77 ? 130 TYR A CA  1 
ATOM   3128 C  C   . TYR B 1 130 ? -34.662 -33.935 5.689   1.00 12.16 ? 130 TYR A C   1 
ATOM   3129 O  O   . TYR B 1 130 ? -34.144 -32.838 6.022   1.00 14.16 ? 130 TYR A O   1 
ATOM   3130 C  CB  . TYR B 1 130 ? -33.987 -35.954 7.116   1.00 13.52 ? 130 TYR A CB  1 
ATOM   3131 C  CG  . TYR B 1 130 ? -33.124 -37.202 7.120   1.00 14.18 ? 130 TYR A CG  1 
ATOM   3132 C  CD1 . TYR B 1 130 ? -33.289 -38.181 6.123   1.00 15.05 ? 130 TYR A CD1 1 
ATOM   3133 C  CD2 . TYR B 1 130 ? -32.002 -37.332 7.978   1.00 15.32 ? 130 TYR A CD2 1 
ATOM   3134 C  CE1 . TYR B 1 130 ? -32.424 -39.267 6.033   1.00 16.72 ? 130 TYR A CE1 1 
ATOM   3135 C  CE2 . TYR B 1 130 ? -31.166 -38.464 7.977   1.00 14.94 ? 130 TYR A CE2 1 
ATOM   3136 C  CZ  . TYR B 1 130 ? -31.405 -39.443 6.979   1.00 15.19 ? 130 TYR A CZ  1 
ATOM   3137 O  OH  . TYR B 1 130 ? -30.580 -40.530 6.822   1.00 17.44 ? 130 TYR A OH  1 
ATOM   3138 N  N   . PRO B 1 131 ? -35.936 -34.112 5.357   1.00 14.48 ? 131 PRO A N   1 
ATOM   3139 C  CA  . PRO B 1 131 ? -36.763 -32.938 5.020   1.00 15.75 ? 131 PRO A CA  1 
ATOM   3140 C  C   . PRO B 1 131 ? -37.382 -32.293 6.271   1.00 15.98 ? 131 PRO A C   1 
ATOM   3141 O  O   . PRO B 1 131 ? -37.899 -31.194 6.177   1.00 19.06 ? 131 PRO A O   1 
ATOM   3142 C  CB  . PRO B 1 131 ? -37.894 -33.542 4.154   1.00 18.17 ? 131 PRO A CB  1 
ATOM   3143 C  CG  . PRO B 1 131 ? -37.998 -34.993 4.620   1.00 17.52 ? 131 PRO A CG  1 
ATOM   3144 C  CD  . PRO B 1 131 ? -36.533 -35.376 4.899   1.00 14.81 ? 131 PRO A CD  1 
ATOM   3145 N  N   . SER B 1 132 ? -37.391 -33.038 7.417   1.00 14.66 ? 132 SER A N   1 
ATOM   3146 C  CA  . SER B 1 132 ? -38.082 -32.521 8.591   1.00 16.62 ? 132 SER A CA  1 
ATOM   3147 C  C   . SER B 1 132 ? -37.505 -33.286 9.780   1.00 15.11 ? 132 SER A C   1 
ATOM   3148 O  O   . SER B 1 132 ? -36.887 -34.319 9.629   1.00 15.26 ? 132 SER A O   1 
ATOM   3149 C  CB  . SER B 1 132 ? -39.601 -32.888 8.562   1.00 17.27 ? 132 SER A CB  1 
ATOM   3150 O  OG  . SER B 1 132 ? -39.749 -34.277 8.534   1.00 19.96 ? 132 SER A OG  1 
ATOM   3151 N  N   . PHE B 1 133 ? -37.726 -32.699 10.953  1.00 17.36 ? 133 PHE A N   1 
ATOM   3152 C  CA  . PHE B 1 133 ? -37.337 -33.379 12.198  1.00 20.01 ? 133 PHE A CA  1 
ATOM   3153 C  C   . PHE B 1 133 ? -38.009 -34.739 12.330  1.00 19.92 ? 133 PHE A C   1 
ATOM   3154 O  O   . PHE B 1 133 ? -37.381 -35.768 12.652  1.00 17.00 ? 133 PHE A O   1 
ATOM   3155 C  CB  . PHE B 1 133 ? -37.731 -32.504 13.397  1.00 19.15 ? 133 PHE A CB  1 
ATOM   3156 C  CG  . PHE B 1 133 ? -37.546 -33.245 14.716  1.00 18.10 ? 133 PHE A CG  1 
ATOM   3157 C  CD1 . PHE B 1 133 ? -36.270 -33.320 15.335  1.00 20.89 ? 133 PHE A CD1 1 
ATOM   3158 C  CD2 . PHE B 1 133 ? -38.627 -33.961 15.240  1.00 21.38 ? 133 PHE A CD2 1 
ATOM   3159 C  CE1 . PHE B 1 133 ? -36.144 -34.048 16.541  1.00 22.53 ? 133 PHE A CE1 1 
ATOM   3160 C  CE2 . PHE B 1 133 ? -38.494 -34.700 16.431  1.00 24.88 ? 133 PHE A CE2 1 
ATOM   3161 C  CZ  . PHE B 1 133 ? -37.243 -34.745 17.062  1.00 26.13 ? 133 PHE A CZ  1 
ATOM   3162 N  N   . VAL B 1 134 ? -39.293 -34.802 12.026  1.00 20.31 ? 134 VAL A N   1 
ATOM   3163 C  CA  . VAL B 1 134 ? -40.028 -36.074 12.148  1.00 23.84 ? 134 VAL A CA  1 
ATOM   3164 C  C   . VAL B 1 134 ? -39.467 -37.189 11.303  1.00 20.83 ? 134 VAL A C   1 
ATOM   3165 O  O   . VAL B 1 134 ? -39.318 -38.370 11.688  1.00 22.63 ? 134 VAL A O   1 
ATOM   3166 C  CB  . VAL B 1 134 ? -41.560 -35.872 11.895  1.00 28.28 ? 134 VAL A CB  1 
ATOM   3167 C  CG1 . VAL B 1 134 ? -42.302 -37.141 12.235  1.00 35.57 ? 134 VAL A CG1 1 
ATOM   3168 C  CG2 . VAL B 1 134 ? -42.056 -34.721 12.727  1.00 31.62 ? 134 VAL A CG2 1 
ATOM   3169 N  N   . GLU B 1 135 ? -39.082 -36.827 10.073  1.00 19.39 ? 135 GLU A N   1 
ATOM   3170 C  CA  . GLU B 1 135 ? -38.419 -37.813 9.245   1.00 18.33 ? 135 GLU A CA  1 
ATOM   3171 C  C   . GLU B 1 135 ? -37.004 -38.229 9.725   1.00 18.81 ? 135 GLU A C   1 
ATOM   3172 O  O   . GLU B 1 135 ? -36.672 -39.419 9.746   1.00 20.18 ? 135 GLU A O   1 
ATOM   3173 C  CB  . GLU B 1 135 ? -38.367 -37.364 7.736   1.00 22.94 ? 135 GLU A CB  1 
ATOM   3174 C  CG  . GLU B 1 135 ? -37.395 -38.232 6.928   1.00 31.39 ? 135 GLU A CG  1 
ATOM   3175 C  CD  . GLU B 1 135 ? -37.879 -39.660 6.750   1.00 35.94 ? 135 GLU A CD  1 
ATOM   3176 O  OE1 . GLU B 1 135 ? -37.041 -40.563 6.921   1.00 31.58 ? 135 GLU A OE1 1 
ATOM   3177 O  OE2 . GLU B 1 135 ? -39.116 -39.877 6.519   1.00 35.50 ? 135 GLU A OE2 1 
ATOM   3178 N  N   . ALA B 1 136 ? -36.204 -37.262 10.151  1.00 15.23 ? 136 ALA A N   1 
ATOM   3179 C  CA  . ALA B 1 136 ? -34.872 -37.501 10.650  1.00 13.94 ? 136 ALA A CA  1 
ATOM   3180 C  C   . ALA B 1 136 ? -34.933 -38.438 11.922  1.00 14.05 ? 136 ALA A C   1 
ATOM   3181 O  O   . ALA B 1 136 ? -34.047 -39.238 12.105  1.00 14.28 ? 136 ALA A O   1 
ATOM   3182 C  CB  . ALA B 1 136 ? -34.221 -36.149 11.012  1.00 14.82 ? 136 ALA A CB  1 
ATOM   3183 N  N   . ALA B 1 137 ? -35.977 -38.267 12.712  1.00 15.97 ? 137 ALA A N   1 
ATOM   3184 C  CA  . ALA B 1 137 ? -36.101 -39.069 13.965  1.00 14.76 ? 137 ALA A CA  1 
ATOM   3185 C  C   . ALA B 1 137 ? -36.223 -40.549 13.656  1.00 16.06 ? 137 ALA A C   1 
ATOM   3186 O  O   . ALA B 1 137 ? -35.993 -41.345 14.588  1.00 14.85 ? 137 ALA A O   1 
ATOM   3187 C  CB  . ALA B 1 137 ? -37.289 -38.626 14.745  1.00 16.19 ? 137 ALA A CB  1 
ATOM   3188 N  N   . HIS B 1 138 ? -36.488 -40.970 12.421  1.00 15.55 ? 138 HIS A N   1 
ATOM   3189 C  CA  . HIS B 1 138 ? -36.560 -42.376 12.041  1.00 15.87 ? 138 HIS A CA  1 
ATOM   3190 C  C   . HIS B 1 138 ? -35.345 -42.912 11.281  1.00 17.92 ? 138 HIS A C   1 
ATOM   3191 O  O   . HIS B 1 138 ? -35.398 -43.988 10.614  1.00 20.95 ? 138 HIS A O   1 
ATOM   3192 C  CB  . HIS B 1 138 ? -37.826 -42.605 11.209  1.00 19.46 ? 138 HIS A CB  1 
ATOM   3193 C  CG  . HIS B 1 138 ? -39.085 -42.358 11.989  1.00 18.53 ? 138 HIS A CG  1 
ATOM   3194 N  ND1 . HIS B 1 138 ? -39.787 -43.360 12.587  1.00 23.31 ? 138 HIS A ND1 1 
ATOM   3195 C  CD2 . HIS B 1 138 ? -39.707 -41.175 12.346  1.00 20.47 ? 138 HIS A CD2 1 
ATOM   3196 C  CE1 . HIS B 1 138 ? -40.844 -42.848 13.221  1.00 20.04 ? 138 HIS A CE1 1 
ATOM   3197 N  NE2 . HIS B 1 138 ? -40.791 -41.502 13.112  1.00 23.93 ? 138 HIS A NE2 1 
ATOM   3198 N  N   . GLU B 1 139 ? -34.223 -42.206 11.306  1.00 17.00 ? 139 GLU A N   1 
ATOM   3199 C  CA  . GLU B 1 139 ? -33.056 -42.644 10.558  1.00 18.53 ? 139 GLU A CA  1 
ATOM   3200 C  C   . GLU B 1 139 ? -31.858 -42.731 11.478  1.00 17.76 ? 139 GLU A C   1 
ATOM   3201 O  O   . GLU B 1 139 ? -31.691 -41.879 12.372  1.00 14.64 ? 139 GLU A O   1 
ATOM   3202 C  CB  . GLU B 1 139 ? -32.723 -41.524 9.502   1.00 21.36 ? 139 GLU A CB  1 
ATOM   3203 C  CG  . GLU B 1 139 ? -33.903 -41.008 8.657   1.00 27.99 ? 139 GLU A CG  1 
ATOM   3204 C  CD  . GLU B 1 139 ? -34.134 -41.925 7.480   1.00 32.80 ? 139 GLU A CD  1 
ATOM   3205 O  OE1 . GLU B 1 139 ? -33.426 -42.950 7.465   1.00 32.85 ? 139 GLU A OE1 1 
ATOM   3206 O  OE2 . GLU B 1 139 ? -34.977 -41.611 6.560   1.00 33.51 ? 139 GLU A OE2 1 
ATOM   3207 N  N   . PRO B 1 140 ? -30.952 -43.670 11.297  1.00 19.37 ? 140 PRO A N   1 
ATOM   3208 C  CA  . PRO B 1 140 ? -29.846 -43.792 12.216  1.00 18.34 ? 140 PRO A CA  1 
ATOM   3209 C  C   . PRO B 1 140 ? -28.986 -42.606 12.421  1.00 18.20 ? 140 PRO A C   1 
ATOM   3210 O  O   . PRO B 1 140 ? -28.476 -42.391 13.529  1.00 16.55 ? 140 PRO A O   1 
ATOM   3211 C  CB  . PRO B 1 140 ? -29.029 -44.999 11.666  1.00 20.93 ? 140 PRO A CB  1 
ATOM   3212 C  CG  . PRO B 1 140 ? -30.148 -45.841 11.106  1.00 28.17 ? 140 PRO A CG  1 
ATOM   3213 C  CD  . PRO B 1 140 ? -30.987 -44.826 10.361  1.00 22.94 ? 140 PRO A CD  1 
ATOM   3214 N  N   . ASP B 1 141 ? -28.794 -41.828 11.369  1.00 14.21 ? 141 ASP A N   1 
ATOM   3215 C  CA  . ASP B 1 141 ? -27.910 -40.658 11.384  1.00 15.66 ? 141 ASP A CA  1 
ATOM   3216 C  C   . ASP B 1 141 ? -28.850 -39.401 11.443  1.00 13.07 ? 141 ASP A C   1 
ATOM   3217 O  O   . ASP B 1 141 ? -28.407 -38.271 11.103  1.00 13.19 ? 141 ASP A O   1 
ATOM   3218 C  CB  . ASP B 1 141 ? -26.994 -40.618 10.097  1.00 17.02 ? 141 ASP A CB  1 
ATOM   3219 C  CG  . ASP B 1 141 ? -27.786 -40.537 8.820   1.00 16.85 ? 141 ASP A CG  1 
ATOM   3220 O  OD1 . ASP B 1 141 ? -28.977 -40.885 8.811   1.00 15.91 ? 141 ASP A OD1 1 
ATOM   3221 O  OD2 . ASP B 1 141 ? -27.192 -40.170 7.791   1.00 19.80 ? 141 ASP A OD2 1 
ATOM   3222 N  N   . GLY B 1 142 ? -30.116 -39.571 11.885  1.00 13.18 ? 142 GLY A N   1 
ATOM   3223 C  CA  . GLY B 1 142 ? -31.069 -38.460 11.842  1.00 11.90 ? 142 GLY A CA  1 
ATOM   3224 C  C   . GLY B 1 142 ? -30.813 -37.354 12.883  1.00 10.98 ? 142 GLY A C   1 
ATOM   3225 O  O   . GLY B 1 142 ? -31.061 -36.175 12.653  1.00 11.63 ? 142 GLY A O   1 
ATOM   3226 N  N   . LEU B 1 143 ? -30.593 -37.783 14.128  1.00 11.25 ? 143 LEU A N   1 
ATOM   3227 C  CA  . LEU B 1 143 ? -30.563 -36.858 15.277  1.00 10.61 ? 143 LEU A CA  1 
ATOM   3228 C  C   . LEU B 1 143 ? -29.220 -36.784 15.962  1.00 11.54 ? 143 LEU A C   1 
ATOM   3229 O  O   . LEU B 1 143 ? -28.487 -37.759 15.978  1.00 12.17 ? 143 LEU A O   1 
ATOM   3230 C  CB  . LEU B 1 143 ? -31.612 -37.214 16.332  1.00 11.81 ? 143 LEU A CB  1 
ATOM   3231 C  CG  . LEU B 1 143 ? -33.023 -37.423 15.847  1.00 10.12 ? 143 LEU A CG  1 
ATOM   3232 C  CD1 . LEU B 1 143 ? -33.992 -37.776 17.010  1.00 11.76 ? 143 LEU A CD1 1 
ATOM   3233 C  CD2 . LEU B 1 143 ? -33.536 -36.149 15.079  1.00 13.15 ? 143 LEU A CD2 1 
ATOM   3234 N  N   . ALA B 1 144 ? -28.959 -35.645 16.608  1.00 10.61 ? 144 ALA A N   1 
ATOM   3235 C  CA  . ALA B 1 144 ? -27.712 -35.460 17.407  1.00 12.07 ? 144 ALA A CA  1 
ATOM   3236 C  C   . ALA B 1 144 ? -28.167 -34.762 18.669  1.00 11.49 ? 144 ALA A C   1 
ATOM   3237 O  O   . ALA B 1 144 ? -28.806 -33.697 18.567  1.00 12.13 ? 144 ALA A O   1 
ATOM   3238 C  CB  . ALA B 1 144 ? -26.607 -34.653 16.685  1.00 12.14 ? 144 ALA A CB  1 
ATOM   3239 N  N   . VAL B 1 145 ? -27.821 -35.319 19.843  1.00 12.14 ? 145 VAL A N   1 
ATOM   3240 C  CA  . VAL B 1 145 ? -28.306 -34.707 21.104  1.00 11.85 ? 145 VAL A CA  1 
ATOM   3241 C  C   . VAL B 1 145 ? -27.117 -34.403 21.949  1.00 10.65 ? 145 VAL A C   1 
ATOM   3242 O  O   . VAL B 1 145 ? -26.334 -35.335 22.206  1.00 11.43 ? 145 VAL A O   1 
ATOM   3243 C  CB  . VAL B 1 145 ? -29.328 -35.554 21.847  1.00 11.40 ? 145 VAL A CB  1 
ATOM   3244 C  CG1 . VAL B 1 145 ? -29.800 -34.759 23.102  1.00 11.84 ? 145 VAL A CG1 1 
ATOM   3245 C  CG2 . VAL B 1 145 ? -30.496 -35.857 20.894  1.00 11.60 ? 145 VAL A CG2 1 
ATOM   3246 N  N   . LEU B 1 146 ? -27.021 -33.166 22.449  1.00 11.75 ? 146 LEU A N   1 
ATOM   3247 C  CA  . LEU B 1 146 ? -26.017 -32.805 23.466  1.00 11.40 ? 146 LEU A CA  1 
ATOM   3248 C  C   . LEU B 1 146 ? -26.668 -33.015 24.818  1.00 12.63 ? 146 LEU A C   1 
ATOM   3249 O  O   . LEU B 1 146 ? -27.843 -32.628 25.028  1.00 14.65 ? 146 LEU A O   1 
ATOM   3250 C  CB  . LEU B 1 146 ? -25.645 -31.301 23.381  1.00 13.36 ? 146 LEU A CB  1 
ATOM   3251 C  CG  . LEU B 1 146 ? -25.006 -30.836 22.159  1.00 16.79 ? 146 LEU A CG  1 
ATOM   3252 C  CD1 . LEU B 1 146 ? -24.796 -29.325 22.442  1.00 17.26 ? 146 LEU A CD1 1 
ATOM   3253 C  CD2 . LEU B 1 146 ? -23.654 -31.437 21.887  1.00 17.55 ? 146 LEU A CD2 1 
ATOM   3254 N  N   . GLY B 1 147 ? -25.928 -33.748 25.653  1.00 11.47 ? 147 GLY A N   1 
ATOM   3255 C  CA  . GLY B 1 147 ? -26.358 -33.956 27.091  1.00 12.28 ? 147 GLY A CA  1 
ATOM   3256 C  C   . GLY B 1 147 ? -25.451 -33.178 28.051  1.00 12.16 ? 147 GLY A C   1 
ATOM   3257 O  O   . GLY B 1 147 ? -24.261 -33.228 27.878  1.00 13.09 ? 147 GLY A O   1 
ATOM   3258 N  N   . VAL B 1 148 ? -26.093 -32.427 28.967  1.00 10.95 ? 148 VAL A N   1 
ATOM   3259 C  CA  . VAL B 1 148 ? -25.370 -31.607 29.941  1.00 11.79 ? 148 VAL A CA  1 
ATOM   3260 C  C   . VAL B 1 148 ? -25.893 -32.001 31.310  1.00 10.22 ? 148 VAL A C   1 
ATOM   3261 O  O   . VAL B 1 148 ? -27.116 -31.935 31.600  1.00 11.15 ? 148 VAL A O   1 
ATOM   3262 C  CB  . VAL B 1 148 ? -25.543 -30.117 29.683  1.00 12.12 ? 148 VAL A CB  1 
ATOM   3263 C  CG1 . VAL B 1 148 ? -24.717 -29.317 30.740  1.00 13.19 ? 148 VAL A CG1 1 
ATOM   3264 C  CG2 . VAL B 1 148 ? -25.043 -29.780 28.245  1.00 17.12 ? 148 VAL A CG2 1 
ATOM   3265 N  N   . PHE B 1 149 ? -24.884 -32.405 32.123  1.00 10.37 ? 149 PHE A N   1 
ATOM   3266 C  CA  . PHE B 1 149 ? -25.291 -32.753 33.544  1.00 11.39 ? 149 PHE A CA  1 
ATOM   3267 C  C   . PHE B 1 149 ? -25.423 -31.519 34.380  1.00 10.92 ? 149 PHE A C   1 
ATOM   3268 O  O   . PHE B 1 149 ? -24.690 -30.551 34.193  1.00 11.80 ? 149 PHE A O   1 
ATOM   3269 C  CB  . PHE B 1 149 ? -24.177 -33.617 34.143  1.00 11.30 ? 149 PHE A CB  1 
ATOM   3270 C  CG  . PHE B 1 149 ? -24.009 -34.927 33.490  1.00 10.32 ? 149 PHE A CG  1 
ATOM   3271 C  CD1 . PHE B 1 149 ? -25.075 -35.820 33.461  1.00 10.67 ? 149 PHE A CD1 1 
ATOM   3272 C  CD2 . PHE B 1 149 ? -22.752 -35.258 32.960  1.00 10.83 ? 149 PHE A CD2 1 
ATOM   3273 C  CE1 . PHE B 1 149 ? -24.944 -37.115 32.892  1.00 12.40 ? 149 PHE A CE1 1 
ATOM   3274 C  CE2 . PHE B 1 149 ? -22.588 -36.517 32.368  1.00 10.78 ? 149 PHE A CE2 1 
ATOM   3275 C  CZ  . PHE B 1 149 ? -23.671 -37.399 32.332  1.00 11.17 ? 149 PHE A CZ  1 
ATOM   3276 N  N   . LEU B 1 150 ? -26.381 -31.567 35.284  1.00 11.96 ? 150 LEU A N   1 
ATOM   3277 C  CA  . LEU B 1 150 ? -26.573 -30.455 36.265  1.00 11.99 ? 150 LEU A CA  1 
ATOM   3278 C  C   . LEU B 1 150 ? -26.265 -31.107 37.644  1.00 13.17 ? 150 LEU A C   1 
ATOM   3279 O  O   . LEU B 1 150 ? -26.883 -32.059 38.051  1.00 14.99 ? 150 LEU A O   1 
ATOM   3280 C  CB  . LEU B 1 150 ? -28.016 -29.859 36.258  1.00 14.25 ? 150 LEU A CB  1 
ATOM   3281 C  CG  . LEU B 1 150 ? -28.298 -28.916 35.077  1.00 13.26 ? 150 LEU A CG  1 
ATOM   3282 C  CD1 . LEU B 1 150 ? -28.561 -29.831 33.845  1.00 16.76 ? 150 LEU A CD1 1 
ATOM   3283 C  CD2 . LEU B 1 150 ? -29.590 -28.169 35.313  1.00 17.60 ? 150 LEU A CD2 1 
ATOM   3284 N  N   . GLN B 1 151 ? -25.348 -30.441 38.354  1.00 14.38 ? 151 GLN A N   1 
ATOM   3285 C  CA  . GLN B 1 151 ? -25.009 -30.847 39.729  1.00 13.16 ? 151 GLN A CA  1 
ATOM   3286 C  C   . GLN B 1 151 ? -25.497 -29.836 40.722  1.00 14.45 ? 151 GLN A C   1 
ATOM   3287 O  O   . GLN B 1 151 ? -25.566 -28.639 40.429  1.00 16.21 ? 151 GLN A O   1 
ATOM   3288 C  CB  . GLN B 1 151 ? -23.513 -30.943 39.811  1.00 14.43 ? 151 GLN A CB  1 
ATOM   3289 C  CG  . GLN B 1 151 ? -22.659 -29.685 39.680  1.00 17.50 ? 151 GLN A CG  1 
ATOM   3290 C  CD  . GLN B 1 151 ? -21.138 -29.929 39.789  1.00 20.28 ? 151 GLN A CD  1 
ATOM   3291 O  OE1 . GLN B 1 151 ? -20.609 -31.083 39.963  1.00 22.25 ? 151 GLN A OE1 1 
ATOM   3292 N  NE2 . GLN B 1 151 ? -20.401 -28.807 39.702  1.00 28.62 ? 151 GLN A NE2 1 
ATOM   3293 N  N   . ILE B 1 152 ? -25.970 -30.277 41.902  1.00 14.84 ? 152 ILE A N   1 
ATOM   3294 C  CA  . ILE B 1 152 ? -26.338 -29.282 42.902  1.00 16.67 ? 152 ILE A CA  1 
ATOM   3295 C  C   . ILE B 1 152 ? -25.130 -28.435 43.272  1.00 18.34 ? 152 ILE A C   1 
ATOM   3296 O  O   . ILE B 1 152 ? -24.054 -28.947 43.518  1.00 18.98 ? 152 ILE A O   1 
ATOM   3297 C  CB  . ILE B 1 152 ? -26.829 -29.973 44.186  1.00 16.22 ? 152 ILE A CB  1 
ATOM   3298 C  CG1 . ILE B 1 152 ? -28.111 -30.720 43.889  1.00 16.68 ? 152 ILE A CG1 1 
ATOM   3299 C  CG2 . ILE B 1 152 ? -27.222 -28.927 45.223  1.00 17.73 ? 152 ILE A CG2 1 
ATOM   3300 C  CD1 . ILE B 1 152 ? -29.286 -29.944 43.260  1.00 16.45 ? 152 ILE A CD1 1 
ATOM   3301 N  N   . GLY B 1 153 ? -25.350 -27.108 43.282  1.00 17.99 ? 153 GLY A N   1 
ATOM   3302 C  CA  . GLY B 1 153 ? -24.244 -26.150 43.514  1.00 20.06 ? 153 GLY A CA  1 
ATOM   3303 C  C   . GLY B 1 153 ? -24.861 -24.763 43.709  1.00 17.69 ? 153 GLY A C   1 
ATOM   3304 O  O   . GLY B 1 153 ? -26.072 -24.622 43.958  1.00 21.15 ? 153 GLY A O   1 
ATOM   3305 N  N   . GLU B 1 154 ? -24.036 -23.759 43.485  1.00 23.23 ? 154 GLU A N   1 
ATOM   3306 C  CA  . GLU B 1 154 ? -24.619 -22.407 43.649  1.00 24.72 ? 154 GLU A CA  1 
ATOM   3307 C  C   . GLU B 1 154 ? -25.588 -22.121 42.503  1.00 20.43 ? 154 GLU A C   1 
ATOM   3308 O  O   . GLU B 1 154 ? -25.495 -22.766 41.446  1.00 20.63 ? 154 GLU A O   1 
ATOM   3309 C  CB  . GLU B 1 154 ? -23.500 -21.426 43.915  1.00 28.00 ? 154 GLU A CB  1 
ATOM   3310 C  CG  . GLU B 1 154 ? -22.944 -21.738 45.356  1.00 29.89 ? 154 GLU A CG  1 
ATOM   3311 C  CD  . GLU B 1 154 ? -21.499 -21.319 45.503  1.00 33.73 ? 154 GLU A CD  1 
ATOM   3312 O  OE1 . GLU B 1 154 ? -20.822 -21.277 44.463  1.00 35.65 ? 154 GLU A OE1 1 
ATOM   3313 O  OE2 . GLU B 1 154 ? -21.049 -20.972 46.634  1.00 30.31 ? 154 GLU A OE2 1 
ATOM   3314 N  N   . PRO B 1 155 ? -26.619 -21.270 42.717  1.00 19.30 ? 155 PRO A N   1 
ATOM   3315 C  CA  . PRO B 1 155 ? -27.679 -21.156 41.735  1.00 17.26 ? 155 PRO A CA  1 
ATOM   3316 C  C   . PRO B 1 155 ? -27.042 -20.668 40.414  1.00 17.54 ? 155 PRO A C   1 
ATOM   3317 O  O   . PRO B 1 155 ? -26.033 -19.970 40.415  1.00 18.69 ? 155 PRO A O   1 
ATOM   3318 C  CB  . PRO B 1 155 ? -28.605 -20.044 42.297  1.00 18.81 ? 155 PRO A CB  1 
ATOM   3319 C  CG  . PRO B 1 155 ? -27.952 -19.555 43.581  1.00 16.84 ? 155 PRO A CG  1 
ATOM   3320 C  CD  . PRO B 1 155 ? -26.961 -20.598 44.006  1.00 16.13 ? 155 PRO A CD  1 
ATOM   3321 N  N   . ASN B 1 156 ? -27.697 -21.036 39.322  1.00 17.92 ? 156 ASN A N   1 
ATOM   3322 C  CA  . ASN B 1 156 ? -27.236 -20.716 37.987  1.00 19.53 ? 156 ASN A CA  1 
ATOM   3323 C  C   . ASN B 1 156 ? -28.100 -19.628 37.381  1.00 16.42 ? 156 ASN A C   1 
ATOM   3324 O  O   . ASN B 1 156 ? -29.291 -19.858 37.062  1.00 17.28 ? 156 ASN A O   1 
ATOM   3325 C  CB  . ASN B 1 156 ? -27.328 -21.985 37.189  1.00 17.33 ? 156 ASN A CB  1 
ATOM   3326 C  CG  . ASN B 1 156 ? -26.610 -21.887 35.869  1.00 18.98 ? 156 ASN A CG  1 
ATOM   3327 O  OD1 . ASN B 1 156 ? -26.450 -20.811 35.292  1.00 21.42 ? 156 ASN A OD1 1 
ATOM   3328 N  ND2 . ASN B 1 156 ? -26.185 -23.011 35.381  1.00 17.48 ? 156 ASN A ND2 1 
ATOM   3329 N  N   . SER B 1 157 ? -27.499 -18.429 37.244  1.00 19.26 ? 157 SER A N   1 
ATOM   3330 C  CA  . SER B 1 157 ? -28.216 -17.235 36.715  1.00 20.56 ? 157 SER A CA  1 
ATOM   3331 C  C   . SER B 1 157 ? -28.682 -17.509 35.292  1.00 20.50 ? 157 SER A C   1 
ATOM   3332 O  O   . SER B 1 157 ? -29.689 -16.938 34.843  1.00 21.30 ? 157 SER A O   1 
ATOM   3333 C  CB  . SER B 1 157 ? -27.254 -15.999 36.761  1.00 23.28 ? 157 SER A CB  1 
ATOM   3334 O  OG  . SER B 1 157 ? -26.049 -16.293 36.090  1.00 26.93 ? 157 SER A OG  1 
ATOM   3335 N  N   . GLN B 1 158 ? -28.032 -18.479 34.613  1.00 20.24 ? 158 GLN A N   1 
ATOM   3336 C  CA  . GLN B 1 158 ? -28.444 -18.769 33.225  1.00 21.51 ? 158 GLN A CA  1 
ATOM   3337 C  C   . GLN B 1 158 ? -29.745 -19.555 33.105  1.00 21.08 ? 158 GLN A C   1 
ATOM   3338 O  O   . GLN B 1 158 ? -30.240 -19.779 32.009  1.00 21.30 ? 158 GLN A O   1 
ATOM   3339 C  CB  . GLN B 1 158 ? -27.319 -19.476 32.457  1.00 24.10 ? 158 GLN A CB  1 
ATOM   3340 C  CG  . GLN B 1 158 ? -26.034 -18.658 32.378  1.00 24.81 ? 158 GLN A CG  1 
ATOM   3341 C  CD  . GLN B 1 158 ? -26.245 -17.252 31.875  1.00 34.38 ? 158 GLN A CD  1 
ATOM   3342 O  OE1 . GLN B 1 158 ? -25.726 -16.296 32.457  1.00 43.68 ? 158 GLN A OE1 1 
ATOM   3343 N  NE2 . GLN B 1 158 ? -27.005 -17.108 30.785  1.00 28.87 ? 158 GLN A NE2 1 
ATOM   3344 N  N   . LEU B 1 159 ? -30.270 -20.117 34.221  1.00 19.40 ? 159 LEU A N   1 
ATOM   3345 C  CA  . LEU B 1 159 ? -31.579 -20.717 34.187  1.00 19.07 ? 159 LEU A CA  1 
ATOM   3346 C  C   . LEU B 1 159 ? -32.718 -19.743 34.432  1.00 16.20 ? 159 LEU A C   1 
ATOM   3347 O  O   . LEU B 1 159 ? -33.873 -20.213 34.309  1.00 17.57 ? 159 LEU A O   1 
ATOM   3348 C  CB  . LEU B 1 159 ? -31.682 -21.865 35.248  1.00 17.86 ? 159 LEU A CB  1 
ATOM   3349 C  CG  . LEU B 1 159 ? -30.719 -22.999 34.997  1.00 18.43 ? 159 LEU A CG  1 
ATOM   3350 C  CD1 . LEU B 1 159 ? -30.587 -23.808 36.284  1.00 20.83 ? 159 LEU A CD1 1 
ATOM   3351 C  CD2 . LEU B 1 159 ? -31.183 -23.883 33.808  1.00 17.51 ? 159 LEU A CD2 1 
ATOM   3352 N  N   . GLN B 1 160 ? -32.446 -18.446 34.790  1.00 17.28 ? 160 GLN A N   1 
ATOM   3353 C  CA  . GLN B 1 160 ? -33.587 -17.536 35.096  1.00 19.28 ? 160 GLN A CA  1 
ATOM   3354 C  C   . GLN B 1 160 ? -34.612 -17.413 33.990  1.00 15.52 ? 160 GLN A C   1 
ATOM   3355 O  O   . GLN B 1 160 ? -35.815 -17.344 34.262  1.00 16.52 ? 160 GLN A O   1 
ATOM   3356 C  CB  . GLN B 1 160 ? -33.115 -16.120 35.533  1.00 22.14 ? 160 GLN A CB  1 
ATOM   3357 C  CG  . GLN B 1 160 ? -34.257 -15.213 35.970  1.00 22.61 ? 160 GLN A CG  1 
ATOM   3358 C  CD  . GLN B 1 160 ? -33.921 -13.730 35.978  1.00 24.08 ? 160 GLN A CD  1 
ATOM   3359 O  OE1 . GLN B 1 160 ? -34.821 -12.901 36.033  1.00 32.60 ? 160 GLN A OE1 1 
ATOM   3360 N  NE2 . GLN B 1 160 ? -32.674 -13.395 35.946  1.00 25.64 ? 160 GLN A NE2 1 
ATOM   3361 N  N   . LYS B 1 161 ? -34.170 -17.311 32.717  1.00 16.76 ? 161 LYS A N   1 
ATOM   3362 C  CA  . LYS B 1 161 ? -35.211 -17.071 31.735  1.00 19.22 ? 161 LYS A CA  1 
ATOM   3363 C  C   . LYS B 1 161 ? -36.171 -18.229 31.701  1.00 17.46 ? 161 LYS A C   1 
ATOM   3364 O  O   . LYS B 1 161 ? -37.369 -18.037 31.609  1.00 20.76 ? 161 LYS A O   1 
ATOM   3365 C  CB  . LYS B 1 161 ? -34.619 -16.920 30.344  1.00 19.58 ? 161 LYS A CB  1 
ATOM   3366 C  CG  . LYS B 1 161 ? -35.609 -16.323 29.289  1.00 20.63 ? 161 LYS A CG  1 
ATOM   3367 C  CD  . LYS B 1 161 ? -35.045 -16.264 27.855  1.00 22.28 ? 161 LYS A CD  1 
ATOM   3368 C  CE  . LYS B 1 161 ? -36.146 -16.116 26.822  1.00 20.89 ? 161 LYS A CE  1 
ATOM   3369 N  NZ  . LYS B 1 161 ? -36.627 -14.642 26.851  1.00 21.90 ? 161 LYS A NZ  1 
ATOM   3370 N  N   . ILE B 1 162 ? -35.653 -19.454 31.825  1.00 16.11 ? 162 ILE A N   1 
ATOM   3371 C  CA  . ILE B 1 162 ? -36.543 -20.596 31.983  1.00 15.60 ? 162 ILE A CA  1 
ATOM   3372 C  C   . ILE B 1 162 ? -37.459 -20.641 33.245  1.00 14.94 ? 162 ILE A C   1 
ATOM   3373 O  O   . ILE B 1 162 ? -38.691 -20.833 33.175  1.00 16.81 ? 162 ILE A O   1 
ATOM   3374 C  CB  . ILE B 1 162 ? -35.738 -21.946 31.875  1.00 13.32 ? 162 ILE A CB  1 
ATOM   3375 C  CG1 . ILE B 1 162 ? -35.013 -22.028 30.482  1.00 15.67 ? 162 ILE A CG1 1 
ATOM   3376 C  CG2 . ILE B 1 162 ? -36.640 -23.130 32.111  1.00 14.86 ? 162 ILE A CG2 1 
ATOM   3377 C  CD1 . ILE B 1 162 ? -33.942 -23.154 30.434  1.00 13.40 ? 162 ILE A CD1 1 
ATOM   3378 N  N   . THR B 1 163 ? -36.794 -20.524 34.358  1.00 17.38 ? 163 THR A N   1 
ATOM   3379 C  CA  . THR B 1 163 ? -37.569 -20.658 35.601  1.00 16.46 ? 163 THR A CA  1 
ATOM   3380 C  C   . THR B 1 163 ? -38.615 -19.602 35.785  1.00 14.37 ? 163 THR A C   1 
ATOM   3381 O  O   . THR B 1 163 ? -39.666 -19.883 36.372  1.00 16.31 ? 163 THR A O   1 
ATOM   3382 C  CB  . THR B 1 163 ? -36.653 -20.678 36.846  1.00 18.75 ? 163 THR A CB  1 
ATOM   3383 O  OG1 . THR B 1 163 ? -35.916 -19.465 36.996  1.00 18.79 ? 163 THR A OG1 1 
ATOM   3384 C  CG2 . THR B 1 163 ? -35.768 -21.875 36.808  1.00 17.86 ? 163 THR A CG2 1 
ATOM   3385 N  N   . ASP B 1 164 ? -38.347 -18.385 35.258  1.00 17.48 ? 164 ASP A N   1 
ATOM   3386 C  CA  . ASP B 1 164 ? -39.387 -17.306 35.318  1.00 17.43 ? 164 ASP A CA  1 
ATOM   3387 C  C   . ASP B 1 164 ? -40.683 -17.666 34.557  1.00 19.69 ? 164 ASP A C   1 
ATOM   3388 O  O   . ASP B 1 164 ? -41.768 -17.073 34.804  1.00 21.88 ? 164 ASP A O   1 
ATOM   3389 C  CB  . ASP B 1 164 ? -38.845 -16.054 34.647  1.00 21.67 ? 164 ASP A CB  1 
ATOM   3390 C  CG  . ASP B 1 164 ? -38.006 -15.182 35.582  1.00 24.65 ? 164 ASP A CG  1 
ATOM   3391 O  OD1 . ASP B 1 164 ? -37.872 -15.513 36.785  1.00 25.80 ? 164 ASP A OD1 1 
ATOM   3392 O  OD2 . ASP B 1 164 ? -37.481 -14.163 35.097  1.00 22.99 ? 164 ASP A OD2 1 
ATOM   3393 N  N   . THR B 1 165 ? -40.605 -18.642 33.633  1.00 16.30 ? 165 THR A N   1 
ATOM   3394 C  CA  . THR B 1 165 ? -41.783 -18.955 32.843  1.00 17.16 ? 165 THR A CA  1 
ATOM   3395 C  C   . THR B 1 165 ? -42.597 -20.122 33.399  1.00 17.15 ? 165 THR A C   1 
ATOM   3396 O  O   . THR B 1 165 ? -43.700 -20.412 32.905  1.00 19.30 ? 165 THR A O   1 
ATOM   3397 C  CB  . THR B 1 165 ? -41.434 -19.404 31.384  1.00 18.93 ? 165 THR A CB  1 
ATOM   3398 O  OG1 . THR B 1 165 ? -40.813 -20.722 31.417  1.00 18.16 ? 165 THR A OG1 1 
ATOM   3399 C  CG2 . THR B 1 165 ? -40.564 -18.370 30.694  1.00 22.75 ? 165 THR A CG2 1 
ATOM   3400 N  N   . LEU B 1 166 ? -42.130 -20.808 34.484  1.00 15.69 ? 166 LEU A N   1 
ATOM   3401 C  CA  . LEU B 1 166 ? -42.738 -22.077 34.786  1.00 15.79 ? 166 LEU A CA  1 
ATOM   3402 C  C   . LEU B 1 166 ? -44.119 -21.978 35.358  1.00 17.30 ? 166 LEU A C   1 
ATOM   3403 O  O   . LEU B 1 166 ? -44.948 -22.819 35.039  1.00 17.95 ? 166 LEU A O   1 
ATOM   3404 C  CB  . LEU B 1 166 ? -41.877 -22.939 35.758  1.00 16.28 ? 166 LEU A CB  1 
ATOM   3405 C  CG  . LEU B 1 166 ? -40.430 -23.293 35.295  1.00 15.20 ? 166 LEU A CG  1 
ATOM   3406 C  CD1 . LEU B 1 166 ? -39.525 -23.826 36.459  1.00 16.74 ? 166 LEU A CD1 1 
ATOM   3407 C  CD2 . LEU B 1 166 ? -40.538 -24.275 34.107  1.00 18.52 ? 166 LEU A CD2 1 
ATOM   3408 N  N   . ASP B 1 167 ? -44.384 -20.917 36.139  1.00 18.98 ? 167 ASP A N   1 
ATOM   3409 C  CA  . ASP B 1 167 ? -45.788 -20.748 36.604  1.00 20.63 ? 167 ASP A CA  1 
ATOM   3410 C  C   . ASP B 1 167 ? -46.726 -20.570 35.413  1.00 21.14 ? 167 ASP A C   1 
ATOM   3411 O  O   . ASP B 1 167 ? -47.807 -21.128 35.436  1.00 23.60 ? 167 ASP A O   1 
ATOM   3412 C  CB  . ASP B 1 167 ? -45.873 -19.511 37.501  1.00 23.13 ? 167 ASP A CB  1 
ATOM   3413 C  CG  . ASP B 1 167 ? -45.261 -19.722 38.883  1.00 29.16 ? 167 ASP A CG  1 
ATOM   3414 O  OD1 . ASP B 1 167 ? -45.165 -20.863 39.423  1.00 33.22 ? 167 ASP A OD1 1 
ATOM   3415 O  OD2 . ASP B 1 167 ? -44.894 -18.674 39.470  1.00 39.05 ? 167 ASP A OD2 1 
ATOM   3416 N  N   . SER B 1 168 ? -46.261 -19.896 34.335  1.00 19.60 ? 168 SER A N   1 
ATOM   3417 C  CA  . SER B 1 168 ? -47.061 -19.667 33.121  1.00 20.86 ? 168 SER A CA  1 
ATOM   3418 C  C   . SER B 1 168 ? -47.322 -20.927 32.348  1.00 19.22 ? 168 SER A C   1 
ATOM   3419 O  O   . SER B 1 168 ? -48.362 -21.018 31.618  1.00 22.01 ? 168 SER A O   1 
ATOM   3420 C  CB  . SER B 1 168 ? -46.472 -18.563 32.268  1.00 24.25 ? 168 SER A CB  1 
ATOM   3421 O  OG  . SER B 1 168 ? -45.405 -19.069 31.494  1.00 23.31 ? 168 SER A OG  1 
ATOM   3422 N  N   . ILE B 1 169 ? -46.502 -21.966 32.560  1.00 17.09 ? 169 ILE A N   1 
ATOM   3423 C  CA  . ILE B 1 169 ? -46.738 -23.231 31.851  1.00 16.70 ? 169 ILE A CA  1 
ATOM   3424 C  C   . ILE B 1 169 ? -46.975 -24.374 32.817  1.00 16.84 ? 169 ILE A C   1 
ATOM   3425 O  O   . ILE B 1 169 ? -46.648 -25.494 32.546  1.00 16.30 ? 169 ILE A O   1 
ATOM   3426 C  CB  . ILE B 1 169 ? -45.615 -23.620 30.816  1.00 17.51 ? 169 ILE A CB  1 
ATOM   3427 C  CG1 . ILE B 1 169 ? -44.260 -23.624 31.503  1.00 16.35 ? 169 ILE A CG1 1 
ATOM   3428 C  CG2 . ILE B 1 169 ? -45.487 -22.550 29.700  1.00 16.31 ? 169 ILE A CG2 1 
ATOM   3429 C  CD1 . ILE B 1 169 ? -43.277 -24.436 30.649  1.00 18.04 ? 169 ILE A CD1 1 
ATOM   3430 N  N   . LYS B 1 170 ? -47.629 -24.068 33.952  1.00 17.00 ? 170 LYS A N   1 
ATOM   3431 C  CA  . LYS B 1 170 ? -47.818 -25.138 34.935  1.00 18.74 ? 170 LYS A CA  1 
ATOM   3432 C  C   . LYS B 1 170 ? -48.573 -26.369 34.434  1.00 17.23 ? 170 LYS A C   1 
ATOM   3433 O  O   . LYS B 1 170 ? -48.158 -27.530 34.670  1.00 16.77 ? 170 LYS A O   1 
ATOM   3434 C  CB  . LYS B 1 170 ? -48.474 -24.537 36.181  1.00 23.41 ? 170 LYS A CB  1 
ATOM   3435 C  CG  . LYS B 1 170 ? -48.852 -25.544 37.231  1.00 25.18 ? 170 LYS A CG  1 
ATOM   3436 C  CD  . LYS B 1 170 ? -49.275 -24.767 38.490  1.00 29.72 ? 170 LYS A CD  1 
ATOM   3437 C  CE  . LYS B 1 170 ? -49.303 -25.662 39.766  1.00 34.45 ? 170 LYS A CE  1 
ATOM   3438 N  NZ  . LYS B 1 170 ? -47.953 -26.066 40.371  1.00 30.52 ? 170 LYS A NZ  1 
ATOM   3439 N  N   . GLU B 1 171 ? -49.621 -26.178 33.629  1.00 17.81 ? 171 GLU A N   1 
ATOM   3440 C  CA  . GLU B 1 171 ? -50.448 -27.271 33.141  1.00 18.00 ? 171 GLU A CA  1 
ATOM   3441 C  C   . GLU B 1 171 ? -49.941 -27.811 31.823  1.00 16.95 ? 171 GLU A C   1 
ATOM   3442 O  O   . GLU B 1 171 ? -49.413 -27.044 30.991  1.00 17.91 ? 171 GLU A O   1 
ATOM   3443 C  CB  . GLU B 1 171 ? -51.914 -26.819 32.946  1.00 19.26 ? 171 GLU A CB  1 
ATOM   3444 C  CG  . GLU B 1 171 ? -52.592 -26.353 34.246  1.00 23.04 ? 171 GLU A CG  1 
ATOM   3445 C  CD  . GLU B 1 171 ? -52.133 -24.966 34.731  1.00 29.17 ? 171 GLU A CD  1 
ATOM   3446 O  OE1 . GLU B 1 171 ? -52.195 -24.755 35.956  1.00 45.30 ? 171 GLU A OE1 1 
ATOM   3447 O  OE2 . GLU B 1 171 ? -51.694 -24.053 33.969  1.00 29.84 ? 171 GLU A OE2 1 
ATOM   3448 N  N   . LYS B 1 172 ? -50.094 -29.105 31.649  1.00 16.87 ? 172 LYS A N   1 
ATOM   3449 C  CA  . LYS B 1 172 ? -49.794 -29.750 30.344  1.00 16.02 ? 172 LYS A CA  1 
ATOM   3450 C  C   . LYS B 1 172 ? -50.530 -28.981 29.198  1.00 19.06 ? 172 LYS A C   1 
ATOM   3451 O  O   . LYS B 1 172 ? -51.747 -28.677 29.299  1.00 17.83 ? 172 LYS A O   1 
ATOM   3452 C  CB  . LYS B 1 172 ? -50.195 -31.193 30.350  1.00 15.63 ? 172 LYS A CB  1 
ATOM   3453 C  CG  . LYS B 1 172 ? -49.924 -31.890 29.085  1.00 17.16 ? 172 LYS A CG  1 
ATOM   3454 C  CD  . LYS B 1 172 ? -50.248 -33.404 29.171  1.00 20.07 ? 172 LYS A CD  1 
ATOM   3455 C  CE  . LYS B 1 172 ? -50.014 -34.109 27.830  1.00 21.29 ? 172 LYS A CE  1 
ATOM   3456 N  NZ  . LYS B 1 172 ? -50.270 -35.557 28.065  1.00 25.84 ? 172 LYS A NZ  1 
ATOM   3457 N  N   . GLY B 1 173 ? -49.764 -28.702 28.156  1.00 15.93 ? 173 GLY A N   1 
ATOM   3458 C  CA  . GLY B 1 173 ? -50.257 -28.018 26.953  1.00 17.40 ? 173 GLY A CA  1 
ATOM   3459 C  C   . GLY B 1 173 ? -50.087 -26.518 26.927  1.00 18.06 ? 173 GLY A C   1 
ATOM   3460 O  O   . GLY B 1 173 ? -50.206 -25.902 25.836  1.00 19.20 ? 173 GLY A O   1 
ATOM   3461 N  N   . LYS B 1 174 ? -49.804 -25.853 28.060  1.00 14.65 ? 174 LYS A N   1 
ATOM   3462 C  CA  . LYS B 1 174 ? -49.605 -24.424 28.065  1.00 15.95 ? 174 LYS A CA  1 
ATOM   3463 C  C   . LYS B 1 174 ? -48.307 -24.119 27.370  1.00 16.28 ? 174 LYS A C   1 
ATOM   3464 O  O   . LYS B 1 174 ? -47.287 -24.881 27.473  1.00 16.53 ? 174 LYS A O   1 
ATOM   3465 C  CB  . LYS B 1 174 ? -49.525 -23.847 29.458  1.00 16.91 ? 174 LYS A CB  1 
ATOM   3466 C  CG  . LYS B 1 174 ? -50.865 -24.026 30.284  1.00 23.58 ? 174 LYS A CG  1 
ATOM   3467 C  CD  . LYS B 1 174 ? -51.479 -22.666 30.579  1.00 33.93 ? 174 LYS A CD  1 
ATOM   3468 C  CE  . LYS B 1 174 ? -52.862 -22.772 31.208  1.00 37.01 ? 174 LYS A CE  1 
ATOM   3469 N  NZ  . LYS B 1 174 ? -53.678 -23.775 30.485  1.00 42.05 ? 174 LYS A NZ  1 
ATOM   3470 N  N   . GLN B 1 175 ? -48.297 -22.972 26.698  1.00 14.23 ? 175 GLN A N   1 
ATOM   3471 C  CA  . GLN B 1 175 ? -47.080 -22.423 26.088  1.00 16.33 ? 175 GLN A CA  1 
ATOM   3472 C  C   . GLN B 1 175 ? -46.999 -20.919 26.270  1.00 16.79 ? 175 GLN A C   1 
ATOM   3473 O  O   . GLN B 1 175 ? -48.026 -20.221 26.526  1.00 20.08 ? 175 GLN A O   1 
ATOM   3474 C  CB  . GLN B 1 175 ? -46.969 -22.743 24.573  1.00 16.99 ? 175 GLN A CB  1 
ATOM   3475 C  CG  . GLN B 1 175 ? -47.916 -21.981 23.632  1.00 19.62 ? 175 GLN A CG  1 
ATOM   3476 C  CD  . GLN B 1 175 ? -47.931 -22.558 22.230  1.00 20.84 ? 175 GLN A CD  1 
ATOM   3477 O  OE1 . GLN B 1 175 ? -47.775 -21.805 21.254  1.00 22.64 ? 175 GLN A OE1 1 
ATOM   3478 N  NE2 . GLN B 1 175 ? -48.135 -23.826 22.094  1.00 19.30 ? 175 GLN A NE2 1 
ATOM   3479 N  N   . THR B 1 176 ? -45.793 -20.403 26.123  1.00 15.02 ? 176 THR A N   1 
ATOM   3480 C  CA  . THR B 1 176 ? -45.526 -18.983 26.358  1.00 15.93 ? 176 THR A CA  1 
ATOM   3481 C  C   . THR B 1 176 ? -44.430 -18.613 25.326  1.00 18.95 ? 176 THR A C   1 
ATOM   3482 O  O   . THR B 1 176 ? -43.518 -19.432 24.992  1.00 17.27 ? 176 THR A O   1 
ATOM   3483 C  CB  . THR B 1 176 ? -44.934 -18.884 27.795  1.00 22.16 ? 176 THR A CB  1 
ATOM   3484 O  OG1 . THR B 1 176 ? -46.043 -19.021 28.697  1.00 25.73 ? 176 THR A OG1 1 
ATOM   3485 C  CG2 . THR B 1 176 ? -44.211 -17.637 28.071  1.00 23.96 ? 176 THR A CG2 1 
ATOM   3486 N  N   A ARG B 1 177 ? -44.499 -17.389 24.847  0.50 15.69 ? 177 ARG A N   1 
ATOM   3487 N  N   B ARG B 1 177 ? -44.501 -17.387 24.796  0.50 15.69 ? 177 ARG A N   1 
ATOM   3488 C  CA  A ARG B 1 177 ? -43.475 -16.866 23.966  0.50 15.93 ? 177 ARG A CA  1 
ATOM   3489 C  CA  B ARG B 1 177 ? -43.440 -16.895 23.885  0.50 15.92 ? 177 ARG A CA  1 
ATOM   3490 C  C   A ARG B 1 177 ? -42.074 -16.871 24.601  0.50 15.88 ? 177 ARG A C   1 
ATOM   3491 C  C   B ARG B 1 177 ? -42.121 -17.049 24.606  0.50 15.84 ? 177 ARG A C   1 
ATOM   3492 O  O   A ARG B 1 177 ? -41.895 -16.430 25.779  0.50 14.36 ? 177 ARG A O   1 
ATOM   3493 O  O   B ARG B 1 177 ? -42.040 -16.907 25.851  0.50 14.44 ? 177 ARG A O   1 
ATOM   3494 C  CB  A ARG B 1 177 ? -43.844 -15.419 23.636  0.50 16.12 ? 177 ARG A CB  1 
ATOM   3495 C  CB  B ARG B 1 177 ? -43.581 -15.385 23.478  0.50 16.28 ? 177 ARG A CB  1 
ATOM   3496 C  CG  A ARG B 1 177 ? -42.686 -14.645 23.081  0.50 16.78 ? 177 ARG A CG  1 
ATOM   3497 C  CG  B ARG B 1 177 ? -42.431 -14.888 22.563  0.50 16.82 ? 177 ARG A CG  1 
ATOM   3498 C  CD  A ARG B 1 177 ? -43.217 -13.262 22.797  0.50 18.39 ? 177 ARG A CD  1 
ATOM   3499 C  CD  B ARG B 1 177 ? -42.755 -13.605 21.779  0.50 20.67 ? 177 ARG A CD  1 
ATOM   3500 N  NE  A ARG B 1 177 ? -42.412 -12.616 21.789  0.50 18.08 ? 177 ARG A NE  1 
ATOM   3501 N  NE  B ARG B 1 177 ? -41.677 -12.971 20.999  0.50 18.87 ? 177 ARG A NE  1 
ATOM   3502 C  CZ  A ARG B 1 177 ? -41.590 -11.602 22.036  0.50 21.84 ? 177 ARG A CZ  1 
ATOM   3503 C  CZ  B ARG B 1 177 ? -41.268 -13.294 19.764  0.50 21.29 ? 177 ARG A CZ  1 
ATOM   3504 N  NH1 A ARG B 1 177 ? -41.451 -11.161 23.277  0.50 25.07 ? 177 ARG A NH1 1 
ATOM   3505 N  NH1 B ARG B 1 177 ? -41.784 -14.282 19.109  0.50 17.21 ? 177 ARG A NH1 1 
ATOM   3506 N  NH2 A ARG B 1 177 ? -40.922 -11.036 21.043  0.50 24.63 ? 177 ARG A NH2 1 
ATOM   3507 N  NH2 B ARG B 1 177 ? -40.332 -12.554 19.138  0.50 25.65 ? 177 ARG A NH2 1 
ATOM   3508 N  N   . PHE B 1 178 ? -41.053 -17.359 23.853  1.00 15.05 ? 178 PHE A N   1 
ATOM   3509 C  CA  . PHE B 1 178 ? -39.751 -17.537 24.503  1.00 15.05 ? 178 PHE A CA  1 
ATOM   3510 C  C   . PHE B 1 178 ? -38.669 -17.349 23.473  1.00 14.71 ? 178 PHE A C   1 
ATOM   3511 O  O   . PHE B 1 178 ? -38.448 -18.252 22.660  1.00 13.79 ? 178 PHE A O   1 
ATOM   3512 C  CB  . PHE B 1 178 ? -39.672 -18.952 25.054  1.00 14.99 ? 178 PHE A CB  1 
ATOM   3513 C  CG  . PHE B 1 178 ? -38.565 -19.182 26.059  1.00 14.71 ? 178 PHE A CG  1 
ATOM   3514 C  CD1 . PHE B 1 178 ? -38.707 -18.858 27.385  1.00 15.66 ? 178 PHE A CD1 1 
ATOM   3515 C  CD2 . PHE B 1 178 ? -37.361 -19.726 25.654  1.00 14.56 ? 178 PHE A CD2 1 
ATOM   3516 C  CE1 . PHE B 1 178 ? -37.687 -19.099 28.273  1.00 15.99 ? 178 PHE A CE1 1 
ATOM   3517 C  CE2 . PHE B 1 178 ? -36.305 -19.946 26.557  1.00 15.33 ? 178 PHE A CE2 1 
ATOM   3518 C  CZ  . PHE B 1 178 ? -36.494 -19.637 27.900  1.00 16.24 ? 178 PHE A CZ  1 
ATOM   3519 N  N   . THR B 1 179 ? -38.154 -16.130 23.379  1.00 16.08 ? 179 THR A N   1 
ATOM   3520 C  CA  . THR B 1 179 ? -37.093 -15.869 22.378  1.00 16.29 ? 179 THR A CA  1 
ATOM   3521 C  C   . THR B 1 179 ? -35.943 -15.100 23.017  1.00 17.05 ? 179 THR A C   1 
ATOM   3522 O  O   . THR B 1 179 ? -36.024 -14.713 24.171  1.00 17.84 ? 179 THR A O   1 
ATOM   3523 C  CB  . THR B 1 179 ? -37.635 -15.205 21.074  1.00 19.64 ? 179 THR A CB  1 
ATOM   3524 O  OG1 . THR B 1 179 ? -36.664 -15.270 20.010  1.00 18.20 ? 179 THR A OG1 1 
ATOM   3525 C  CG2 . THR B 1 179 ? -37.943 -13.712 21.353  1.00 19.53 ? 179 THR A CG2 1 
ATOM   3526 N  N   A ASN B 1 180 ? -34.904 -14.882 22.226  0.50 16.66 ? 180 ASN A N   1 
ATOM   3527 N  N   B ASN B 1 180 ? -34.854 -14.840 22.287  0.50 16.85 ? 180 ASN A N   1 
ATOM   3528 C  CA  A ASN B 1 180 ? -33.715 -14.211 22.714  0.50 15.60 ? 180 ASN A CA  1 
ATOM   3529 C  CA  B ASN B 1 180 ? -33.628 -14.157 22.834  0.50 15.97 ? 180 ASN A CA  1 
ATOM   3530 C  C   A ASN B 1 180 ? -33.273 -14.997 23.945  0.50 15.67 ? 180 ASN A C   1 
ATOM   3531 C  C   B ASN B 1 180 ? -32.994 -14.996 23.945  0.50 15.58 ? 180 ASN A C   1 
ATOM   3532 O  O   A ASN B 1 180 ? -33.205 -14.455 25.074  0.50 15.39 ? 180 ASN A O   1 
ATOM   3533 O  O   B ASN B 1 180 ? -32.486 -14.500 24.996  0.50 14.04 ? 180 ASN A O   1 
ATOM   3534 C  CB  A ASN B 1 180 ? -33.963 -12.707 22.956  0.50 18.95 ? 180 ASN A CB  1 
ATOM   3535 C  CB  B ASN B 1 180 ? -33.865 -12.711 23.322  0.50 19.23 ? 180 ASN A CB  1 
ATOM   3536 C  CG  A ASN B 1 180 ? -34.357 -11.994 21.670  0.50 19.26 ? 180 ASN A CG  1 
ATOM   3537 C  CG  B ASN B 1 180 ? -32.577 -11.967 23.640  0.50 23.11 ? 180 ASN A CG  1 
ATOM   3538 O  OD1 A ASN B 1 180 ? -33.737 -12.207 20.620  0.50 23.89 ? 180 ASN A OD1 1 
ATOM   3539 O  OD1 B ASN B 1 180 ? -31.479 -12.263 23.124  0.50 24.07 ? 180 ASN A OD1 1 
ATOM   3540 N  ND2 A ASN B 1 180 ? -35.435 -11.206 21.727  0.50 21.10 ? 180 ASN A ND2 1 
ATOM   3541 N  ND2 B ASN B 1 180 ? -32.703 -10.984 24.519  0.50 25.55 ? 180 ASN A ND2 1 
ATOM   3542 N  N   . PHE B 1 181 ? -33.042 -16.300 23.706  1.00 14.21 ? 181 PHE A N   1 
ATOM   3543 C  CA  . PHE B 1 181 ? -32.604 -17.252 24.753  1.00 15.98 ? 181 PHE A CA  1 
ATOM   3544 C  C   . PHE B 1 181 ? -31.110 -17.562 24.556  1.00 14.14 ? 181 PHE A C   1 
ATOM   3545 O  O   . PHE B 1 181 ? -30.755 -18.098 23.504  1.00 15.79 ? 181 PHE A O   1 
ATOM   3546 C  CB  . PHE B 1 181 ? -33.401 -18.552 24.615  1.00 16.61 ? 181 PHE A CB  1 
ATOM   3547 C  CG  . PHE B 1 181 ? -32.951 -19.701 25.502  1.00 15.97 ? 181 PHE A CG  1 
ATOM   3548 C  CD1 . PHE B 1 181 ? -32.560 -19.512 26.802  1.00 15.16 ? 181 PHE A CD1 1 
ATOM   3549 C  CD2 . PHE B 1 181 ? -32.970 -20.973 24.965  1.00 15.81 ? 181 PHE A CD2 1 
ATOM   3550 C  CE1 . PHE B 1 181 ? -32.137 -20.625 27.568  1.00 14.85 ? 181 PHE A CE1 1 
ATOM   3551 C  CE2 . PHE B 1 181 ? -32.609 -22.080 25.724  1.00 19.15 ? 181 PHE A CE2 1 
ATOM   3552 C  CZ  . PHE B 1 181 ? -32.179 -21.901 27.036  1.00 15.21 ? 181 PHE A CZ  1 
ATOM   3553 N  N   . ASP B 1 182 ? -30.304 -17.348 25.572  1.00 15.01 ? 182 ASP A N   1 
ATOM   3554 C  CA  . ASP B 1 182 ? -28.853 -17.581 25.471  1.00 14.81 ? 182 ASP A CA  1 
ATOM   3555 C  C   . ASP B 1 182 ? -28.548 -19.011 25.908  1.00 15.74 ? 182 ASP A C   1 
ATOM   3556 O  O   . ASP B 1 182 ? -28.212 -19.252 27.072  1.00 17.62 ? 182 ASP A O   1 
ATOM   3557 C  CB  . ASP B 1 182 ? -28.141 -16.622 26.414  1.00 17.61 ? 182 ASP A CB  1 
ATOM   3558 C  CG  . ASP B 1 182 ? -26.591 -16.754 26.399  1.00 17.86 ? 182 ASP A CG  1 
ATOM   3559 O  OD1 . ASP B 1 182 ? -26.069 -17.578 25.606  1.00 18.44 ? 182 ASP A OD1 1 
ATOM   3560 O  OD2 . ASP B 1 182 ? -25.990 -15.942 27.135  1.00 20.22 ? 182 ASP A OD2 1 
ATOM   3561 N  N   . LEU B 1 183 ? -28.656 -19.924 24.964  1.00 14.52 ? 183 LEU A N   1 
ATOM   3562 C  CA  . LEU B 1 183 ? -28.452 -21.348 25.238  1.00 13.68 ? 183 LEU A CA  1 
ATOM   3563 C  C   . LEU B 1 183 ? -26.950 -21.615 25.425  1.00 16.55 ? 183 LEU A C   1 
ATOM   3564 O  O   . LEU B 1 183 ? -26.489 -22.483 26.242  1.00 14.69 ? 183 LEU A O   1 
ATOM   3565 C  CB  . LEU B 1 183 ? -28.992 -22.188 24.080  1.00 14.78 ? 183 LEU A CB  1 
ATOM   3566 C  CG  . LEU B 1 183 ? -28.806 -23.730 24.144  1.00 13.24 ? 183 LEU A CG  1 
ATOM   3567 C  CD1 . LEU B 1 183 ? -29.391 -24.294 25.443  1.00 15.99 ? 183 LEU A CD1 1 
ATOM   3568 C  CD2 . LEU B 1 183 ? -29.552 -24.388 22.969  1.00 15.81 ? 183 LEU A CD2 1 
ATOM   3569 N  N   . LEU B 1 184 ? -26.118 -20.946 24.656  1.00 16.11 ? 184 LEU A N   1 
ATOM   3570 C  CA  . LEU B 1 184 ? -24.729 -21.189 24.694  1.00 16.45 ? 184 LEU A CA  1 
ATOM   3571 C  C   . LEU B 1 184 ? -24.161 -21.038 26.101  1.00 16.83 ? 184 LEU A C   1 
ATOM   3572 O  O   . LEU B 1 184 ? -23.270 -21.874 26.486  1.00 21.22 ? 184 LEU A O   1 
ATOM   3573 C  CB  . LEU B 1 184 ? -23.965 -20.294 23.646  1.00 19.30 ? 184 LEU A CB  1 
ATOM   3574 C  CG  . LEU B 1 184 ? -22.521 -20.624 23.350  1.00 27.00 ? 184 LEU A CG  1 
ATOM   3575 C  CD1 . LEU B 1 184 ? -22.523 -21.872 22.466  1.00 27.60 ? 184 LEU A CD1 1 
ATOM   3576 C  CD2 . LEU B 1 184 ? -21.914 -19.451 22.586  1.00 23.60 ? 184 LEU A CD2 1 
ATOM   3577 N  N   A SER B 1 185 ? -24.674 -20.072 26.892  0.50 17.71 ? 185 SER A N   1 
ATOM   3578 N  N   B SER B 1 185 ? -24.651 -20.060 26.895  0.50 18.78 ? 185 SER A N   1 
ATOM   3579 C  CA  A SER B 1 185 ? -24.205 -19.839 28.242  0.50 18.72 ? 185 SER A CA  1 
ATOM   3580 C  CA  B SER B 1 185 ? -24.175 -19.842 28.251  0.50 20.50 ? 185 SER A CA  1 
ATOM   3581 C  C   A SER B 1 185 ? -24.719 -20.849 29.259  0.50 18.18 ? 185 SER A C   1 
ATOM   3582 C  C   B SER B 1 185 ? -24.635 -20.912 29.229  0.50 19.42 ? 185 SER A C   1 
ATOM   3583 O  O   A SER B 1 185 ? -24.332 -20.773 30.444  0.50 19.18 ? 185 SER A O   1 
ATOM   3584 O  O   B SER B 1 185 ? -24.162 -20.903 30.387  0.50 20.59 ? 185 SER A O   1 
ATOM   3585 C  CB  A SER B 1 185 ? -24.533 -18.424 28.712  0.50 17.75 ? 185 SER A CB  1 
ATOM   3586 C  CB  B SER B 1 185 ? -24.678 -18.530 28.826  0.50 20.17 ? 185 SER A CB  1 
ATOM   3587 O  OG  A SER B 1 185 ? -23.928 -17.507 27.800  0.50 16.12 ? 185 SER A OG  1 
ATOM   3588 O  OG  B SER B 1 185 ? -26.067 -18.633 29.008  0.50 24.70 ? 185 SER A OG  1 
ATOM   3589 N  N   . LEU B 1 186 ? -25.566 -21.780 28.815  1.00 17.25 ? 186 LEU A N   1 
ATOM   3590 C  CA  . LEU B 1 186 ? -25.965 -22.946 29.665  1.00 18.51 ? 186 LEU A CA  1 
ATOM   3591 C  C   . LEU B 1 186 ? -25.066 -24.168 29.440  1.00 23.22 ? 186 LEU A C   1 
ATOM   3592 O  O   . LEU B 1 186 ? -25.252 -25.273 30.023  1.00 28.83 ? 186 LEU A O   1 
ATOM   3593 C  CB  . LEU B 1 186 ? -27.422 -23.346 29.468  1.00 21.01 ? 186 LEU A CB  1 
ATOM   3594 C  CG  . LEU B 1 186 ? -28.558 -22.632 30.149  1.00 22.90 ? 186 LEU A CG  1 
ATOM   3595 C  CD1 . LEU B 1 186 ? -29.797 -23.245 29.510  1.00 22.53 ? 186 LEU A CD1 1 
ATOM   3596 C  CD2 . LEU B 1 186 ? -28.383 -23.021 31.667  1.00 20.18 ? 186 LEU A CD2 1 
ATOM   3597 N  N   . LEU B 1 187 ? -24.079 -24.047 28.581  1.00 16.84 ? 187 LEU A N   1 
ATOM   3598 C  CA  . LEU B 1 187 ? -23.138 -25.069 28.406  1.00 16.32 ? 187 LEU A CA  1 
ATOM   3599 C  C   . LEU B 1 187 ? -21.911 -24.793 29.331  1.00 14.77 ? 187 LEU A C   1 
ATOM   3600 O  O   . LEU B 1 187 ? -21.575 -23.617 29.625  1.00 16.24 ? 187 LEU A O   1 
ATOM   3601 C  CB  . LEU B 1 187 ? -22.666 -25.164 26.976  1.00 17.46 ? 187 LEU A CB  1 
ATOM   3602 C  CG  . LEU B 1 187 ? -23.729 -25.325 25.908  1.00 22.89 ? 187 LEU A CG  1 
ATOM   3603 C  CD1 . LEU B 1 187 ? -22.942 -25.365 24.616  1.00 22.41 ? 187 LEU A CD1 1 
ATOM   3604 C  CD2 . LEU B 1 187 ? -24.482 -26.631 26.100  1.00 20.96 ? 187 LEU A CD2 1 
ATOM   3605 N  N   . PRO B 1 188 ? -21.277 -25.864 29.845  1.00 15.60 ? 188 PRO A N   1 
ATOM   3606 C  CA  . PRO B 1 188 ? -20.116 -25.712 30.700  1.00 14.34 ? 188 PRO A CA  1 
ATOM   3607 C  C   . PRO B 1 188 ? -18.905 -25.105 29.947  1.00 16.85 ? 188 PRO A C   1 
ATOM   3608 O  O   . PRO B 1 188 ? -18.933 -25.097 28.695  1.00 15.43 ? 188 PRO A O   1 
ATOM   3609 C  CB  . PRO B 1 188 ? -19.821 -27.146 31.176  1.00 14.95 ? 188 PRO A CB  1 
ATOM   3610 C  CG  . PRO B 1 188 ? -20.236 -27.986 30.019  1.00 16.14 ? 188 PRO A CG  1 
ATOM   3611 C  CD  . PRO B 1 188 ? -21.497 -27.309 29.556  1.00 14.86 ? 188 PRO A CD  1 
ATOM   3612 N  N   . PRO B 1 189 ? -17.888 -24.622 30.627  1.00 17.06 ? 189 PRO A N   1 
ATOM   3613 C  CA  . PRO B 1 189 ? -16.759 -24.021 29.867  1.00 15.93 ? 189 PRO A CA  1 
ATOM   3614 C  C   . PRO B 1 189 ? -16.030 -25.089 29.022  1.00 15.91 ? 189 PRO A C   1 
ATOM   3615 O  O   . PRO B 1 189 ? -15.673 -24.829 27.849  1.00 16.46 ? 189 PRO A O   1 
ATOM   3616 C  CB  . PRO B 1 189 ? -15.819 -23.518 31.001  1.00 19.33 ? 189 PRO A CB  1 
ATOM   3617 C  CG  . PRO B 1 189 ? -16.765 -23.230 32.129  1.00 21.44 ? 189 PRO A CG  1 
ATOM   3618 C  CD  . PRO B 1 189 ? -17.835 -24.278 32.086  1.00 17.45 ? 189 PRO A CD  1 
ATOM   3619 N  N   . SER B 1 190 ? -15.859 -26.325 29.504  1.00 13.62 ? 190 SER A N   1 
ATOM   3620 C  CA  . SER B 1 190 ? -15.250 -27.367 28.704  1.00 13.48 ? 190 SER A CA  1 
ATOM   3621 C  C   . SER B 1 190 ? -16.319 -28.149 28.011  1.00 13.66 ? 190 SER A C   1 
ATOM   3622 O  O   . SER B 1 190 ? -17.328 -28.515 28.603  1.00 15.39 ? 190 SER A O   1 
ATOM   3623 C  CB  . SER B 1 190 ? -14.511 -28.374 29.608  1.00 14.62 ? 190 SER A CB  1 
ATOM   3624 O  OG  . SER B 1 190 ? -13.993 -29.458 28.813  1.00 16.12 ? 190 SER A OG  1 
ATOM   3625 N  N   . TRP B 1 191 ? -16.097 -28.392 26.717  1.00 13.15 ? 191 TRP A N   1 
ATOM   3626 C  CA  . TRP B 1 191 ? -16.964 -29.189 25.947  1.00 14.34 ? 191 TRP A CA  1 
ATOM   3627 C  C   . TRP B 1 191 ? -16.407 -30.527 25.629  1.00 14.47 ? 191 TRP A C   1 
ATOM   3628 O  O   . TRP B 1 191 ? -16.879 -31.207 24.696  1.00 16.58 ? 191 TRP A O   1 
ATOM   3629 C  CB  . TRP B 1 191 ? -17.348 -28.506 24.598  1.00 16.48 ? 191 TRP A CB  1 
ATOM   3630 C  CG  . TRP B 1 191 ? -18.031 -27.211 24.751  1.00 15.32 ? 191 TRP A CG  1 
ATOM   3631 C  CD1 . TRP B 1 191 ? -18.554 -26.669 25.907  1.00 14.03 ? 191 TRP A CD1 1 
ATOM   3632 C  CD2 . TRP B 1 191 ? -18.267 -26.174 23.718  1.00 13.60 ? 191 TRP A CD2 1 
ATOM   3633 N  NE1 . TRP B 1 191 ? -19.047 -25.424 25.698  1.00 14.58 ? 191 TRP A NE1 1 
ATOM   3634 C  CE2 . TRP B 1 191 ? -18.958 -25.105 24.363  1.00 14.48 ? 191 TRP A CE2 1 
ATOM   3635 C  CE3 . TRP B 1 191 ? -18.074 -26.120 22.344  1.00 16.44 ? 191 TRP A CE3 1 
ATOM   3636 C  CZ2 . TRP B 1 191 ? -19.317 -23.899 23.712  1.00 13.30 ? 191 TRP A CZ2 1 
ATOM   3637 C  CZ3 . TRP B 1 191 ? -18.447 -24.893 21.684  1.00 14.51 ? 191 TRP A CZ3 1 
ATOM   3638 C  CH2 . TRP B 1 191 ? -19.089 -23.853 22.355  1.00 14.57 ? 191 TRP A CH2 1 
ATOM   3639 N  N   . ASP B 1 192 ? -15.452 -31.021 26.438  1.00 14.16 ? 192 ASP A N   1 
ATOM   3640 C  CA  . ASP B 1 192 ? -15.050 -32.399 26.290  1.00 15.05 ? 192 ASP A CA  1 
ATOM   3641 C  C   . ASP B 1 192 ? -16.287 -33.352 26.464  1.00 14.92 ? 192 ASP A C   1 
ATOM   3642 O  O   . ASP B 1 192 ? -17.172 -33.094 27.291  1.00 13.85 ? 192 ASP A O   1 
ATOM   3643 C  CB  . ASP B 1 192 ? -14.113 -32.771 27.439  1.00 15.66 ? 192 ASP A CB  1 
ATOM   3644 C  CG  . ASP B 1 192 ? -12.679 -32.161 27.293  1.00 19.68 ? 192 ASP A CG  1 
ATOM   3645 O  OD1 . ASP B 1 192 ? -12.393 -31.674 26.183  1.00 19.67 ? 192 ASP A OD1 1 
ATOM   3646 O  OD2 . ASP B 1 192 ? -11.846 -32.227 28.252  1.00 21.86 ? 192 ASP A OD2 1 
ATOM   3647 N  N   . TYR B 1 193 ? -16.343 -34.426 25.678  1.00 12.11 ? 193 TYR A N   1 
ATOM   3648 C  CA  . TYR B 1 193 ? -17.535 -35.265 25.629  1.00 12.37 ? 193 TYR A CA  1 
ATOM   3649 C  C   . TYR B 1 193 ? -17.276 -36.722 25.356  1.00 12.72 ? 193 TYR A C   1 
ATOM   3650 O  O   . TYR B 1 193 ? -16.154 -37.076 24.880  1.00 12.58 ? 193 TYR A O   1 
ATOM   3651 C  CB  . TYR B 1 193 ? -18.562 -34.740 24.496  1.00 12.45 ? 193 TYR A CB  1 
ATOM   3652 C  CG  . TYR B 1 193 ? -18.007 -34.850 23.130  1.00 14.05 ? 193 TYR A CG  1 
ATOM   3653 C  CD1 . TYR B 1 193 ? -18.121 -36.022 22.396  1.00 12.89 ? 193 TYR A CD1 1 
ATOM   3654 C  CD2 . TYR B 1 193 ? -17.337 -33.785 22.582  1.00 12.56 ? 193 TYR A CD2 1 
ATOM   3655 C  CE1 . TYR B 1 193 ? -17.570 -36.109 21.136  1.00 16.48 ? 193 TYR A CE1 1 
ATOM   3656 C  CE2 . TYR B 1 193 ? -16.788 -33.862 21.334  1.00 14.20 ? 193 TYR A CE2 1 
ATOM   3657 C  CZ  . TYR B 1 193 ? -16.899 -35.023 20.617  1.00 14.66 ? 193 TYR A CZ  1 
ATOM   3658 O  OH  . TYR B 1 193 ? -16.342 -35.077 19.371  1.00 15.26 ? 193 TYR A OH  1 
ATOM   3659 N  N   . TRP B 1 194 ? -18.306 -37.537 25.640  1.00 11.85 ? 194 TRP A N   1 
ATOM   3660 C  CA  . TRP B 1 194 ? -18.401 -38.886 25.219  1.00 12.49 ? 194 TRP A CA  1 
ATOM   3661 C  C   . TRP B 1 194 ? -19.480 -38.998 24.154  1.00 13.17 ? 194 TRP A C   1 
ATOM   3662 O  O   . TRP B 1 194 ? -20.434 -38.285 24.171  1.00 14.50 ? 194 TRP A O   1 
ATOM   3663 C  CB  . TRP B 1 194 ? -18.798 -39.836 26.392  1.00 13.23 ? 194 TRP A CB  1 
ATOM   3664 C  CG  . TRP B 1 194 ? -17.811 -39.864 27.541  1.00 14.03 ? 194 TRP A CG  1 
ATOM   3665 C  CD1 . TRP B 1 194 ? -16.583 -40.471 27.588  1.00 16.25 ? 194 TRP A CD1 1 
ATOM   3666 C  CD2 . TRP B 1 194 ? -17.996 -39.222 28.840  1.00 13.61 ? 194 TRP A CD2 1 
ATOM   3667 N  NE1 . TRP B 1 194 ? -15.995 -40.265 28.846  1.00 16.98 ? 194 TRP A NE1 1 
ATOM   3668 C  CE2 . TRP B 1 194 ? -16.797 -39.488 29.609  1.00 16.78 ? 194 TRP A CE2 1 
ATOM   3669 C  CE3 . TRP B 1 194 ? -19.014 -38.446 29.403  1.00 14.70 ? 194 TRP A CE3 1 
ATOM   3670 C  CZ2 . TRP B 1 194 ? -16.651 -39.041 30.923  1.00 16.73 ? 194 TRP A CZ2 1 
ATOM   3671 C  CZ3 . TRP B 1 194 ? -18.850 -37.950 30.702  1.00 16.45 ? 194 TRP A CZ3 1 
ATOM   3672 C  CH2 . TRP B 1 194 ? -17.654 -38.249 31.458  1.00 17.01 ? 194 TRP A CH2 1 
ATOM   3673 N  N   . THR B 1 195 ? -19.276 -39.956 23.234  1.00 14.17 ? 195 THR A N   1 
ATOM   3674 C  CA  . THR B 1 195 ? -20.260 -40.138 22.152  1.00 13.14 ? 195 THR A CA  1 
ATOM   3675 C  C   . THR B 1 195 ? -20.467 -41.589 21.880  1.00 12.13 ? 195 THR A C   1 
ATOM   3676 O  O   . THR B 1 195 ? -19.567 -42.399 21.986  1.00 13.88 ? 195 THR A O   1 
ATOM   3677 C  CB  . THR B 1 195 ? -19.843 -39.298 20.899  1.00 13.84 ? 195 THR A CB  1 
ATOM   3678 O  OG1 . THR B 1 195 ? -20.844 -39.438 19.930  1.00 13.62 ? 195 THR A OG1 1 
ATOM   3679 C  CG2 . THR B 1 195 ? -18.468 -39.812 20.235  1.00 14.90 ? 195 THR A CG2 1 
ATOM   3680 N  N   . TYR B 1 196 ? -21.700 -41.932 21.528  1.00 11.24 ? 196 TYR A N   1 
ATOM   3681 C  CA  . TYR B 1 196 ? -22.126 -43.260 21.247  1.00 11.09 ? 196 TYR A CA  1 
ATOM   3682 C  C   . TYR B 1 196 ? -23.469 -43.227 20.481  1.00 12.93 ? 196 TYR A C   1 
ATOM   3683 O  O   . TYR B 1 196 ? -24.206 -42.219 20.524  1.00 12.67 ? 196 TYR A O   1 
ATOM   3684 C  CB  . TYR B 1 196 ? -22.266 -44.178 22.556  1.00 12.03 ? 196 TYR A CB  1 
ATOM   3685 C  CG  . TYR B 1 196 ? -23.508 -43.819 23.339  1.00 11.55 ? 196 TYR A CG  1 
ATOM   3686 C  CD1 . TYR B 1 196 ? -23.528 -42.718 24.191  1.00 10.67 ? 196 TYR A CD1 1 
ATOM   3687 C  CD2 . TYR B 1 196 ? -24.674 -44.553 23.192  1.00 11.04 ? 196 TYR A CD2 1 
ATOM   3688 C  CE1 . TYR B 1 196 ? -24.671 -42.380 24.893  1.00 11.23 ? 196 TYR A CE1 1 
ATOM   3689 C  CE2 . TYR B 1 196 ? -25.819 -44.223 23.889  1.00 11.96 ? 196 TYR A CE2 1 
ATOM   3690 C  CZ  . TYR B 1 196 ? -25.814 -43.138 24.736  1.00 9.62  ? 196 TYR A CZ  1 
ATOM   3691 O  OH  . TYR B 1 196 ? -26.964 -42.823 25.424  1.00 11.17 ? 196 TYR A OH  1 
ATOM   3692 N  N   . PRO B 1 197 ? -23.812 -44.299 19.773  1.00 14.25 ? 197 PRO A N   1 
ATOM   3693 C  CA  . PRO B 1 197 ? -25.088 -44.414 19.050  1.00 12.50 ? 197 PRO A CA  1 
ATOM   3694 C  C   . PRO B 1 197 ? -26.158 -44.888 19.957  1.00 12.33 ? 197 PRO A C   1 
ATOM   3695 O  O   . PRO B 1 197 ? -25.982 -45.962 20.648  1.00 14.27 ? 197 PRO A O   1 
ATOM   3696 C  CB  . PRO B 1 197 ? -24.774 -45.475 17.946  1.00 14.12 ? 197 PRO A CB  1 
ATOM   3697 C  CG  . PRO B 1 197 ? -23.747 -46.349 18.605  1.00 13.75 ? 197 PRO A CG  1 
ATOM   3698 C  CD  . PRO B 1 197 ? -22.906 -45.443 19.496  1.00 15.41 ? 197 PRO A CD  1 
ATOM   3699 N  N   . GLY B 1 198 ? -27.257 -44.144 19.988  1.00 12.53 ? 198 GLY A N   1 
ATOM   3700 C  CA  . GLY B 1 198 ? -28.374 -44.518 20.819  1.00 11.37 ? 198 GLY A CA  1 
ATOM   3701 C  C   . GLY B 1 198 ? -29.715 -44.047 20.348  1.00 11.42 ? 198 GLY A C   1 
ATOM   3702 O  O   . GLY B 1 198 ? -30.045 -44.051 19.148  1.00 13.36 ? 198 GLY A O   1 
ATOM   3703 N  N   . SER B 1 199 ? -30.551 -43.680 21.307  1.00 12.00 ? 199 SER A N   1 
ATOM   3704 C  CA  . SER B 1 199 ? -31.936 -43.512 21.000  1.00 11.85 ? 199 SER A CA  1 
ATOM   3705 C  C   . SER B 1 199 ? -32.577 -42.317 21.719  1.00 10.26 ? 199 SER A C   1 
ATOM   3706 O  O   . SER B 1 199 ? -31.935 -41.697 22.609  1.00 11.49 ? 199 SER A O   1 
ATOM   3707 C  CB  . SER B 1 199 ? -32.784 -44.769 21.455  1.00 11.37 ? 199 SER A CB  1 
ATOM   3708 O  OG  . SER B 1 199 ? -32.885 -44.762 22.871  1.00 10.85 ? 199 SER A OG  1 
ATOM   3709 N  N   . LEU B 1 200 ? -33.780 -41.994 21.354  1.00 10.50 ? 200 LEU A N   1 
ATOM   3710 C  CA  . LEU B 1 200 ? -34.538 -41.077 22.230  1.00 10.50 ? 200 LEU A CA  1 
ATOM   3711 C  C   . LEU B 1 200 ? -34.716 -41.760 23.569  1.00 10.99 ? 200 LEU A C   1 
ATOM   3712 O  O   . LEU B 1 200 ? -34.911 -42.948 23.624  1.00 11.23 ? 200 LEU A O   1 
ATOM   3713 C  CB  . LEU B 1 200 ? -35.982 -40.966 21.721  1.00 12.39 ? 200 LEU A CB  1 
ATOM   3714 C  CG  . LEU B 1 200 ? -36.262 -39.919 20.664  1.00 18.97 ? 200 LEU A CG  1 
ATOM   3715 C  CD1 . LEU B 1 200 ? -35.372 -39.994 19.553  1.00 19.14 ? 200 LEU A CD1 1 
ATOM   3716 C  CD2 . LEU B 1 200 ? -37.681 -40.025 20.103  1.00 15.49 ? 200 LEU A CD2 1 
ATOM   3717 N  N   . THR B 1 201 ? -34.781 -40.927 24.613  1.00 9.92  ? 201 THR A N   1 
ATOM   3718 C  CA  . THR B 1 201 ? -34.947 -41.565 25.987  1.00 11.81 ? 201 THR A CA  1 
ATOM   3719 C  C   . THR B 1 201 ? -36.396 -41.504 26.411  1.00 13.39 ? 201 THR A C   1 
ATOM   3720 O  O   . THR B 1 201 ? -36.727 -41.866 27.582  1.00 13.34 ? 201 THR A O   1 
ATOM   3721 C  CB  . THR B 1 201 ? -34.052 -40.948 27.038  1.00 10.41 ? 201 THR A CB  1 
ATOM   3722 O  OG1 . THR B 1 201 ? -34.494 -39.619 27.293  1.00 10.55 ? 201 THR A OG1 1 
ATOM   3723 C  CG2 . THR B 1 201 ? -32.589 -40.950 26.572  1.00 9.95  ? 201 THR A CG2 1 
ATOM   3724 N  N   . VAL B 1 202 ? -37.301 -41.105 25.525  1.00 11.07 ? 202 VAL A N   1 
ATOM   3725 C  CA  . VAL B 1 202 ? -38.749 -41.164 25.726  1.00 12.08 ? 202 VAL A CA  1 
ATOM   3726 C  C   . VAL B 1 202 ? -39.383 -41.868 24.599  1.00 14.07 ? 202 VAL A C   1 
ATOM   3727 O  O   . VAL B 1 202 ? -38.840 -41.807 23.493  1.00 12.69 ? 202 VAL A O   1 
ATOM   3728 C  CB  . VAL B 1 202 ? -39.347 -39.735 25.854  1.00 13.50 ? 202 VAL A CB  1 
ATOM   3729 C  CG1 . VAL B 1 202 ? -38.813 -38.998 27.090  1.00 14.32 ? 202 VAL A CG1 1 
ATOM   3730 C  CG2 . VAL B 1 202 ? -39.052 -38.796 24.685  1.00 12.80 ? 202 VAL A CG2 1 
ATOM   3731 N  N   . PRO B 1 203 ? -40.531 -42.474 24.792  1.00 13.21 ? 203 PRO A N   1 
ATOM   3732 C  CA  . PRO B 1 203 ? -41.344 -42.978 23.649  1.00 14.61 ? 203 PRO A CA  1 
ATOM   3733 C  C   . PRO B 1 203 ? -41.425 -41.904 22.615  1.00 13.78 ? 203 PRO A C   1 
ATOM   3734 O  O   . PRO B 1 203 ? -41.687 -40.740 22.910  1.00 15.15 ? 203 PRO A O   1 
ATOM   3735 C  CB  . PRO B 1 203 ? -42.680 -43.284 24.276  1.00 13.72 ? 203 PRO A CB  1 
ATOM   3736 C  CG  . PRO B 1 203 ? -42.266 -43.738 25.709  1.00 13.58 ? 203 PRO A CG  1 
ATOM   3737 C  CD  . PRO B 1 203 ? -41.216 -42.694 26.099  1.00 14.32 ? 203 PRO A CD  1 
ATOM   3738 N  N   . PRO B 1 204 ? -41.181 -42.256 21.318  1.00 13.89 ? 204 PRO A N   1 
ATOM   3739 C  CA  . PRO B 1 204 ? -41.189 -43.592 20.745  1.00 14.93 ? 204 PRO A CA  1 
ATOM   3740 C  C   . PRO B 1 204 ? -39.833 -44.301 20.822  1.00 15.42 ? 204 PRO A C   1 
ATOM   3741 O  O   . PRO B 1 204 ? -39.695 -45.417 20.256  1.00 17.04 ? 204 PRO A O   1 
ATOM   3742 C  CB  . PRO B 1 204 ? -41.633 -43.292 19.259  1.00 14.55 ? 204 PRO A CB  1 
ATOM   3743 C  CG  . PRO B 1 204 ? -41.064 -41.925 18.996  1.00 17.45 ? 204 PRO A CG  1 
ATOM   3744 C  CD  . PRO B 1 204 ? -41.344 -41.193 20.332  1.00 15.42 ? 204 PRO A CD  1 
ATOM   3745 N  N   . LEU B 1 205 ? -38.825 -43.709 21.510  1.00 12.89 ? 205 LEU A N   1 
ATOM   3746 C  CA  . LEU B 1 205 ? -37.587 -44.504 21.791  1.00 12.74 ? 205 LEU A CA  1 
ATOM   3747 C  C   . LEU B 1 205 ? -36.785 -44.896 20.518  1.00 13.55 ? 205 LEU A C   1 
ATOM   3748 O  O   . LEU B 1 205 ? -35.935 -45.823 20.536  1.00 12.80 ? 205 LEU A O   1 
ATOM   3749 C  CB  . LEU B 1 205 ? -37.865 -45.760 22.663  1.00 12.81 ? 205 LEU A CB  1 
ATOM   3750 C  CG  . LEU B 1 205 ? -38.500 -45.394 24.050  1.00 13.17 ? 205 LEU A CG  1 
ATOM   3751 C  CD1 . LEU B 1 205 ? -39.014 -46.713 24.695  1.00 17.02 ? 205 LEU A CD1 1 
ATOM   3752 C  CD2 . LEU B 1 205 ? -37.492 -44.679 24.942  1.00 14.60 ? 205 LEU A CD2 1 
ATOM   3753 N  N   . LEU B 1 206 ? -36.963 -44.061 19.513  1.00 12.79 ? 206 LEU A N   1 
ATOM   3754 C  CA  . LEU B 1 206 ? -36.296 -44.451 18.223  1.00 12.79 ? 206 LEU A CA  1 
ATOM   3755 C  C   . LEU B 1 206 ? -34.806 -44.417 18.281  1.00 12.61 ? 206 LEU A C   1 
ATOM   3756 O  O   . LEU B 1 206 ? -34.242 -43.507 18.865  1.00 11.79 ? 206 LEU A O   1 
ATOM   3757 C  CB  . LEU B 1 206 ? -36.806 -43.450 17.127  1.00 11.91 ? 206 LEU A CB  1 
ATOM   3758 C  CG  . LEU B 1 206 ? -38.314 -43.477 16.974  1.00 13.41 ? 206 LEU A CG  1 
ATOM   3759 C  CD1 . LEU B 1 206 ? -38.809 -42.171 16.231  1.00 17.15 ? 206 LEU A CD1 1 
ATOM   3760 C  CD2 . LEU B 1 206 ? -38.683 -44.728 16.201  1.00 17.59 ? 206 LEU A CD2 1 
ATOM   3761 N  N   . GLU B 1 207 ? -34.182 -45.368 17.570  1.00 13.12 ? 207 GLU A N   1 
ATOM   3762 C  CA  . GLU B 1 207 ? -32.706 -45.493 17.588  1.00 12.00 ? 207 GLU A CA  1 
ATOM   3763 C  C   . GLU B 1 207 ? -32.139 -44.666 16.445  1.00 14.29 ? 207 GLU A C   1 
ATOM   3764 O  O   . GLU B 1 207 ? -31.556 -45.198 15.458  1.00 16.27 ? 207 GLU A O   1 
ATOM   3765 C  CB  . GLU B 1 207 ? -32.324 -47.006 17.561  1.00 12.62 ? 207 GLU A CB  1 
ATOM   3766 C  CG  . GLU B 1 207 ? -32.892 -47.645 18.852  1.00 13.51 ? 207 GLU A CG  1 
ATOM   3767 C  CD  . GLU B 1 207 ? -32.650 -49.101 18.937  1.00 15.51 ? 207 GLU A CD  1 
ATOM   3768 O  OE1 . GLU B 1 207 ? -32.571 -49.768 17.881  1.00 16.95 ? 207 GLU A OE1 1 
ATOM   3769 O  OE2 . GLU B 1 207 ? -32.533 -49.645 20.049  1.00 14.30 ? 207 GLU A OE2 1 
ATOM   3770 N  N   . SER B 1 208 ? -32.170 -43.359 16.617  1.00 13.31 ? 208 SER A N   1 
ATOM   3771 C  CA  . SER B 1 208 ? -31.680 -42.395 15.611  1.00 12.22 ? 208 SER A CA  1 
ATOM   3772 C  C   . SER B 1 208 ? -30.805 -41.312 16.168  1.00 12.35 ? 208 SER A C   1 
ATOM   3773 O  O   . SER B 1 208 ? -30.526 -40.307 15.460  1.00 11.29 ? 208 SER A O   1 
ATOM   3774 C  CB  . SER B 1 208 ? -32.943 -41.704 15.082  1.00 14.67 ? 208 SER A CB  1 
ATOM   3775 O  OG  . SER B 1 208 ? -33.718 -41.190 16.164  1.00 15.66 ? 208 SER A OG  1 
ATOM   3776 N  N   . VAL B 1 209 ? -30.227 -41.520 17.390  1.00 11.76 ? 209 VAL A N   1 
ATOM   3777 C  CA  . VAL B 1 209 ? -29.456 -40.437 17.978  1.00 12.58 ? 209 VAL A CA  1 
ATOM   3778 C  C   . VAL B 1 209 ? -27.987 -40.712 18.063  1.00 12.60 ? 209 VAL A C   1 
ATOM   3779 O  O   . VAL B 1 209 ? -27.593 -41.756 18.657  1.00 13.93 ? 209 VAL A O   1 
ATOM   3780 C  CB  . VAL B 1 209 ? -29.969 -40.226 19.415  1.00 12.16 ? 209 VAL A CB  1 
ATOM   3781 C  CG1 . VAL B 1 209 ? -29.247 -39.064 20.141  1.00 11.61 ? 209 VAL A CG1 1 
ATOM   3782 C  CG2 . VAL B 1 209 ? -31.484 -39.895 19.368  1.00 12.68 ? 209 VAL A CG2 1 
ATOM   3783 N  N   . THR B 1 210 ? -27.200 -39.749 17.654  1.00 11.14 ? 210 THR A N   1 
ATOM   3784 C  CA  . THR B 1 210 ? -25.798 -39.724 18.045  1.00 11.00 ? 210 THR A CA  1 
ATOM   3785 C  C   . THR B 1 210 ? -25.715 -38.886 19.271  1.00 11.06 ? 210 THR A C   1 
ATOM   3786 O  O   . THR B 1 210 ? -25.935 -37.673 19.231  1.00 12.82 ? 210 THR A O   1 
ATOM   3787 C  CB  . THR B 1 210 ? -24.978 -39.041 16.874  1.00 12.00 ? 210 THR A CB  1 
ATOM   3788 O  OG1 . THR B 1 210 ? -25.093 -39.848 15.673  1.00 13.88 ? 210 THR A OG1 1 
ATOM   3789 C  CG2 . THR B 1 210 ? -23.510 -38.912 17.218  1.00 12.45 ? 210 THR A CG2 1 
ATOM   3790 N  N   . TRP B 1 211 ? -25.436 -39.529 20.414  1.00 11.71 ? 211 TRP A N   1 
ATOM   3791 C  CA  . TRP B 1 211 ? -25.283 -38.813 21.682  1.00 10.62 ? 211 TRP A CA  1 
ATOM   3792 C  C   . TRP B 1 211 ? -23.921 -38.241 21.840  1.00 10.84 ? 211 TRP A C   1 
ATOM   3793 O  O   . TRP B 1 211 ? -22.902 -38.802 21.521  1.00 12.80 ? 211 TRP A O   1 
ATOM   3794 C  CB  . TRP B 1 211 ? -25.510 -39.864 22.785  1.00 10.78 ? 211 TRP A CB  1 
ATOM   3795 C  CG  . TRP B 1 211 ? -26.969 -40.067 23.045  1.00 11.02 ? 211 TRP A CG  1 
ATOM   3796 C  CD1 . TRP B 1 211 ? -27.877 -40.980 22.533  1.00 9.38  ? 211 TRP A CD1 1 
ATOM   3797 C  CD2 . TRP B 1 211 ? -27.815 -39.129 23.834  1.00 9.36  ? 211 TRP A CD2 1 
ATOM   3798 N  NE1 . TRP B 1 211 ? -29.175 -40.735 22.963  1.00 12.19 ? 211 TRP A NE1 1 
ATOM   3799 C  CE2 . TRP B 1 211 ? -29.190 -39.600 23.720  1.00 9.88  ? 211 TRP A CE2 1 
ATOM   3800 C  CE3 . TRP B 1 211 ? -27.573 -37.942 24.505  1.00 10.61 ? 211 TRP A CE3 1 
ATOM   3801 C  CZ2 . TRP B 1 211 ? -30.270 -38.968 24.315  1.00 11.41 ? 211 TRP A CZ2 1 
ATOM   3802 C  CZ3 . TRP B 1 211 ? -28.649 -37.309 25.102  1.00 8.88  ? 211 TRP A CZ3 1 
ATOM   3803 C  CH2 . TRP B 1 211 ? -29.956 -37.770 25.037  1.00 9.15  ? 211 TRP A CH2 1 
ATOM   3804 N  N   . ILE B 1 212 ? -23.934 -37.003 22.316  1.00 10.33 ? 212 ILE A N   1 
ATOM   3805 C  CA  . ILE B 1 212 ? -22.760 -36.247 22.669  1.00 11.45 ? 212 ILE A CA  1 
ATOM   3806 C  C   . ILE B 1 212 ? -22.979 -35.781 24.095  1.00 11.49 ? 212 ILE A C   1 
ATOM   3807 O  O   . ILE B 1 212 ? -23.694 -34.788 24.376  1.00 12.78 ? 212 ILE A O   1 
ATOM   3808 C  CB  . ILE B 1 212 ? -22.525 -35.042 21.697  1.00 11.31 ? 212 ILE A CB  1 
ATOM   3809 C  CG1 . ILE B 1 212 ? -22.364 -35.645 20.317  1.00 12.15 ? 212 ILE A CG1 1 
ATOM   3810 C  CG2 . ILE B 1 212 ? -21.353 -34.214 22.121  1.00 13.65 ? 212 ILE A CG2 1 
ATOM   3811 C  CD1 . ILE B 1 212 ? -22.561 -34.591 19.200  1.00 13.94 ? 212 ILE A CD1 1 
ATOM   3812 N  N   . VAL B 1 213 ? -22.335 -36.543 25.036  1.00 12.21 ? 213 VAL A N   1 
ATOM   3813 C  CA  . VAL B 1 213 ? -22.617 -36.253 26.476  1.00 11.51 ? 213 VAL A CA  1 
ATOM   3814 C  C   . VAL B 1 213 ? -21.412 -35.540 27.039  1.00 11.66 ? 213 VAL A C   1 
ATOM   3815 O  O   . VAL B 1 213 ? -20.287 -36.083 27.041  1.00 11.64 ? 213 VAL A O   1 
ATOM   3816 C  CB  . VAL B 1 213 ? -22.820 -37.611 27.174  1.00 11.56 ? 213 VAL A CB  1 
ATOM   3817 C  CG1 . VAL B 1 213 ? -23.004 -37.454 28.661  1.00 13.43 ? 213 VAL A CG1 1 
ATOM   3818 C  CG2 . VAL B 1 213 ? -24.098 -38.262 26.609  1.00 13.05 ? 213 VAL A CG2 1 
ATOM   3819 N  N   . LEU B 1 214 ? -21.613 -34.283 27.476  1.00 11.81 ? 214 LEU A N   1 
ATOM   3820 C  CA  . LEU B 1 214 ? -20.465 -33.478 27.973  1.00 12.63 ? 214 LEU A CA  1 
ATOM   3821 C  C   . LEU B 1 214 ? -20.028 -33.929 29.413  1.00 11.54 ? 214 LEU A C   1 
ATOM   3822 O  O   . LEU B 1 214 ? -20.872 -34.293 30.238  1.00 13.05 ? 214 LEU A O   1 
ATOM   3823 C  CB  . LEU B 1 214 ? -20.859 -32.022 28.015  1.00 14.77 ? 214 LEU A CB  1 
ATOM   3824 C  CG  . LEU B 1 214 ? -20.665 -31.275 26.661  1.00 16.93 ? 214 LEU A CG  1 
ATOM   3825 C  CD1 . LEU B 1 214 ? -21.405 -31.975 25.542  1.00 20.21 ? 214 LEU A CD1 1 
ATOM   3826 C  CD2 . LEU B 1 214 ? -20.972 -29.741 26.830  1.00 16.32 ? 214 LEU A CD2 1 
ATOM   3827 N  N   . LYS B 1 215 ? -18.722 -33.961 29.593  1.00 11.53 ? 215 LYS A N   1 
ATOM   3828 C  CA  . LYS B 1 215 ? -18.169 -34.434 30.898  1.00 13.08 ? 215 LYS A CA  1 
ATOM   3829 C  C   . LYS B 1 215 ? -18.387 -33.462 32.035  1.00 14.26 ? 215 LYS A C   1 
ATOM   3830 O  O   . LYS B 1 215 ? -18.742 -33.873 33.182  1.00 15.04 ? 215 LYS A O   1 
ATOM   3831 C  CB  . LYS B 1 215 ? -16.682 -34.749 30.675  1.00 13.42 ? 215 LYS A CB  1 
ATOM   3832 C  CG  . LYS B 1 215 ? -15.970 -35.047 32.066  1.00 15.87 ? 215 LYS A CG  1 
ATOM   3833 C  CD  . LYS B 1 215 ? -14.504 -35.508 31.804  1.00 19.58 ? 215 LYS A CD  1 
ATOM   3834 C  CE  . LYS B 1 215 ? -13.656 -35.494 33.065  1.00 28.50 ? 215 LYS A CE  1 
ATOM   3835 N  NZ  . LYS B 1 215 ? -12.311 -35.989 32.676  1.00 33.07 ? 215 LYS A NZ  1 
ATOM   3836 N  N   . GLN B 1 216 ? -18.252 -32.173 31.786  1.00 14.11 ? 216 GLN A N   1 
ATOM   3837 C  CA  . GLN B 1 216 ? -18.284 -31.207 32.876  1.00 13.00 ? 216 GLN A CA  1 
ATOM   3838 C  C   . GLN B 1 216 ? -19.686 -30.794 33.180  1.00 14.77 ? 216 GLN A C   1 
ATOM   3839 O  O   . GLN B 1 216 ? -20.405 -30.317 32.304  1.00 13.60 ? 216 GLN A O   1 
ATOM   3840 C  CB  . GLN B 1 216 ? -17.551 -29.895 32.496  1.00 13.44 ? 216 GLN A CB  1 
ATOM   3841 C  CG  . GLN B 1 216 ? -17.564 -28.843 33.649  1.00 13.83 ? 216 GLN A CG  1 
ATOM   3842 C  CD  . GLN B 1 216 ? -16.615 -27.698 33.436  1.00 18.42 ? 216 GLN A CD  1 
ATOM   3843 O  OE1 . GLN B 1 216 ? -16.154 -27.427 32.308  1.00 18.73 ? 216 GLN A OE1 1 
ATOM   3844 N  NE2 . GLN B 1 216 ? -16.385 -26.937 34.510  1.00 20.34 ? 216 GLN A NE2 1 
ATOM   3845 N  N   . PRO B 1 217 ? -20.193 -30.907 34.396  1.00 13.47 ? 217 PRO A N   1 
ATOM   3846 C  CA  . PRO B 1 217 ? -21.568 -30.485 34.752  1.00 12.87 ? 217 PRO A CA  1 
ATOM   3847 C  C   . PRO B 1 217 ? -21.658 -28.983 34.872  1.00 12.53 ? 217 PRO A C   1 
ATOM   3848 O  O   . PRO B 1 217 ? -20.605 -28.330 35.070  1.00 14.92 ? 217 PRO A O   1 
ATOM   3849 C  CB  . PRO B 1 217 ? -21.810 -31.117 36.174  1.00 13.41 ? 217 PRO A CB  1 
ATOM   3850 C  CG  . PRO B 1 217 ? -20.439 -31.415 36.590  1.00 16.34 ? 217 PRO A CG  1 
ATOM   3851 C  CD  . PRO B 1 217 ? -19.461 -31.629 35.472  1.00 14.07 ? 217 PRO A CD  1 
ATOM   3852 N  N   . ILE B 1 218 ? -22.883 -28.467 34.833  1.00 11.47 ? 218 ILE A N   1 
ATOM   3853 C  CA  . ILE B 1 218 ? -23.127 -27.102 35.199  1.00 13.35 ? 218 ILE A CA  1 
ATOM   3854 C  C   . ILE B 1 218 ? -23.835 -27.141 36.556  1.00 13.45 ? 218 ILE A C   1 
ATOM   3855 O  O   . ILE B 1 218 ? -24.270 -28.243 37.015  1.00 13.95 ? 218 ILE A O   1 
ATOM   3856 C  CB  . ILE B 1 218 ? -23.989 -26.391 34.132  1.00 14.31 ? 218 ILE A CB  1 
ATOM   3857 C  CG1 . ILE B 1 218 ? -25.376 -26.993 34.002  1.00 14.75 ? 218 ILE A CG1 1 
ATOM   3858 C  CG2 . ILE B 1 218 ? -23.268 -26.297 32.800  1.00 15.15 ? 218 ILE A CG2 1 
ATOM   3859 C  CD1 . ILE B 1 218 ? -26.352 -26.182 33.071  1.00 13.09 ? 218 ILE A CD1 1 
ATOM   3860 N  N   . ASN B 1 219 ? -23.974 -26.007 37.218  1.00 14.94 ? 219 ASN A N   1 
ATOM   3861 C  CA  . ASN B 1 219 ? -24.653 -26.018 38.524  1.00 13.91 ? 219 ASN A CA  1 
ATOM   3862 C  C   . ASN B 1 219 ? -26.106 -25.695 38.452  1.00 13.59 ? 219 ASN A C   1 
ATOM   3863 O  O   . ASN B 1 219 ? -26.595 -25.016 37.529  1.00 14.53 ? 219 ASN A O   1 
ATOM   3864 C  CB  . ASN B 1 219 ? -24.006 -24.968 39.443  1.00 17.08 ? 219 ASN A CB  1 
ATOM   3865 C  CG  . ASN B 1 219 ? -22.603 -25.333 39.871  1.00 23.59 ? 219 ASN A CG  1 
ATOM   3866 O  OD1 . ASN B 1 219 ? -21.762 -24.440 39.989  1.00 43.90 ? 219 ASN A OD1 1 
ATOM   3867 N  ND2 . ASN B 1 219 ? -22.343 -26.557 40.149  1.00 23.06 ? 219 ASN A ND2 1 
ATOM   3868 N  N   . ILE B 1 220 ? -26.854 -26.072 39.501  1.00 12.39 ? 220 ILE A N   1 
ATOM   3869 C  CA  . ILE B 1 220 ? -28.226 -25.716 39.712  1.00 12.61 ? 220 ILE A CA  1 
ATOM   3870 C  C   . ILE B 1 220 ? -28.392 -25.716 41.243  1.00 11.82 ? 220 ILE A C   1 
ATOM   3871 O  O   . ILE B 1 220 ? -27.856 -26.628 41.864  1.00 14.39 ? 220 ILE A O   1 
ATOM   3872 C  CB  . ILE B 1 220 ? -29.284 -26.611 38.967  1.00 12.69 ? 220 ILE A CB  1 
ATOM   3873 C  CG1 . ILE B 1 220 ? -30.710 -26.038 39.110  1.00 13.14 ? 220 ILE A CG1 1 
ATOM   3874 C  CG2 . ILE B 1 220 ? -29.143 -28.105 39.423  1.00 13.15 ? 220 ILE A CG2 1 
ATOM   3875 C  CD1 . ILE B 1 220 ? -31.794 -26.764 38.264  1.00 14.26 ? 220 ILE A CD1 1 
ATOM   3876 N  N   . SER B 1 221 ? -29.207 -24.805 41.786  1.00 11.98 ? 221 SER A N   1 
ATOM   3877 C  CA  . SER B 1 221 ? -29.394 -24.971 43.239  1.00 12.10 ? 221 SER A CA  1 
ATOM   3878 C  C   . SER B 1 221 ? -30.600 -25.882 43.464  1.00 14.36 ? 221 SER A C   1 
ATOM   3879 O  O   . SER B 1 221 ? -31.523 -26.112 42.605  1.00 13.45 ? 221 SER A O   1 
ATOM   3880 C  CB  . SER B 1 221 ? -29.728 -23.573 43.821  1.00 12.34 ? 221 SER A CB  1 
ATOM   3881 O  OG  . SER B 1 221 ? -30.959 -23.085 43.498  1.00 13.56 ? 221 SER A OG  1 
ATOM   3882 N  N   A SER B 1 222 ? -30.724 -26.356 44.705  0.50 13.71 ? 222 SER A N   1 
ATOM   3883 N  N   B SER B 1 222 ? -30.694 -26.346 44.703  0.50 14.05 ? 222 SER A N   1 
ATOM   3884 C  CA  A SER B 1 222 ? -31.900 -27.119 45.077  0.50 12.78 ? 222 SER A CA  1 
ATOM   3885 C  CA  B SER B 1 222 ? -31.842 -27.111 45.065  0.50 13.32 ? 222 SER A CA  1 
ATOM   3886 C  C   A SER B 1 222 ? -33.189 -26.349 44.906  0.50 12.70 ? 222 SER A C   1 
ATOM   3887 C  C   B SER B 1 222 ? -33.147 -26.352 44.908  0.50 12.94 ? 222 SER A C   1 
ATOM   3888 O  O   A SER B 1 222 ? -34.218 -26.901 44.485  0.50 14.02 ? 222 SER A O   1 
ATOM   3889 O  O   B SER B 1 222 ? -34.142 -26.921 44.477  0.50 14.49 ? 222 SER A O   1 
ATOM   3890 C  CB  A SER B 1 222 ? -31.734 -27.603 46.559  0.50 12.42 ? 222 SER A CB  1 
ATOM   3891 C  CB  B SER B 1 222 ? -31.649 -27.625 46.519  0.50 13.31 ? 222 SER A CB  1 
ATOM   3892 O  OG  A SER B 1 222 ? -30.662 -28.525 46.706  0.50 12.59 ? 222 SER A OG  1 
ATOM   3893 O  OG  B SER B 1 222 ? -32.833 -28.261 46.928  0.50 15.04 ? 222 SER A OG  1 
ATOM   3894 N  N   . GLN B 1 223 ? -33.186 -25.042 45.258  1.00 12.10 ? 223 GLN A N   1 
ATOM   3895 C  CA  . GLN B 1 223 ? -34.374 -24.287 45.145  1.00 12.29 ? 223 GLN A CA  1 
ATOM   3896 C  C   . GLN B 1 223 ? -34.815 -24.102 43.632  1.00 11.57 ? 223 GLN A C   1 
ATOM   3897 O  O   . GLN B 1 223 ? -36.016 -24.132 43.305  1.00 14.67 ? 223 GLN A O   1 
ATOM   3898 C  CB  . GLN B 1 223 ? -34.190 -22.862 45.722  1.00 13.92 ? 223 GLN A CB  1 
ATOM   3899 C  CG  . GLN B 1 223 ? -34.240 -22.863 47.267  1.00 16.19 ? 223 GLN A CG  1 
ATOM   3900 C  CD  . GLN B 1 223 ? -34.291 -21.461 47.808  1.00 19.06 ? 223 GLN A CD  1 
ATOM   3901 O  OE1 . GLN B 1 223 ? -35.025 -20.621 47.316  1.00 19.23 ? 223 GLN A OE1 1 
ATOM   3902 N  NE2 . GLN B 1 223 ? -33.470 -21.223 48.859  1.00 21.18 ? 223 GLN A NE2 1 
ATOM   3903 N  N   . GLN B 1 224 ? -33.765 -23.915 42.829  1.00 12.66 ? 224 GLN A N   1 
ATOM   3904 C  CA  . GLN B 1 224 ? -34.099 -23.871 41.382  1.00 13.21 ? 224 GLN A CA  1 
ATOM   3905 C  C   . GLN B 1 224 ? -34.665 -25.163 40.862  1.00 13.73 ? 224 GLN A C   1 
ATOM   3906 O  O   . GLN B 1 224 ? -35.695 -25.168 40.141  1.00 12.71 ? 224 GLN A O   1 
ATOM   3907 C  CB  . GLN B 1 224 ? -32.850 -23.517 40.581  1.00 12.14 ? 224 GLN A CB  1 
ATOM   3908 C  CG  . GLN B 1 224 ? -32.393 -22.092 40.666  1.00 12.84 ? 224 GLN A CG  1 
ATOM   3909 C  CD  . GLN B 1 224 ? -31.131 -21.901 39.821  1.00 12.94 ? 224 GLN A CD  1 
ATOM   3910 O  OE1 . GLN B 1 224 ? -30.106 -22.542 39.984  1.00 14.13 ? 224 GLN A OE1 1 
ATOM   3911 N  NE2 . GLN B 1 224 ? -31.236 -20.864 38.910  1.00 14.32 ? 224 GLN A NE2 1 
ATOM   3912 N  N   . LEU B 1 225 ? -33.974 -26.249 41.220  1.00 13.34 ? 225 LEU A N   1 
ATOM   3913 C  CA  . LEU B 1 225 ? -34.448 -27.582 40.731  1.00 13.47 ? 225 LEU A CA  1 
ATOM   3914 C  C   . LEU B 1 225 ? -35.852 -27.901 41.149  1.00 14.34 ? 225 LEU A C   1 
ATOM   3915 O  O   . LEU B 1 225 ? -36.691 -28.430 40.420  1.00 16.29 ? 225 LEU A O   1 
ATOM   3916 C  CB  . LEU B 1 225 ? -33.496 -28.701 41.155  1.00 15.29 ? 225 LEU A CB  1 
ATOM   3917 C  CG  . LEU B 1 225 ? -33.725 -30.063 40.491  1.00 15.85 ? 225 LEU A CG  1 
ATOM   3918 C  CD1 . LEU B 1 225 ? -33.979 -29.904 38.999  1.00 16.64 ? 225 LEU A CD1 1 
ATOM   3919 C  CD2 . LEU B 1 225 ? -32.523 -30.959 40.742  1.00 15.61 ? 225 LEU A CD2 1 
ATOM   3920 N  N   . ALA B 1 226 ? -36.169 -27.572 42.410  1.00 14.33 ? 226 ALA A N   1 
ATOM   3921 C  CA  . ALA B 1 226 ? -37.460 -27.842 42.920  1.00 15.18 ? 226 ALA A CA  1 
ATOM   3922 C  C   . ALA B 1 226 ? -38.618 -27.208 42.155  1.00 13.28 ? 226 ALA A C   1 
ATOM   3923 O  O   . ALA B 1 226 ? -39.748 -27.696 42.150  1.00 15.29 ? 226 ALA A O   1 
ATOM   3924 C  CB  . ALA B 1 226 ? -37.497 -27.433 44.408  1.00 18.21 ? 226 ALA A CB  1 
ATOM   3925 N  N   . LYS B 1 227 ? -38.292 -26.089 41.467  1.00 13.49 ? 227 LYS A N   1 
ATOM   3926 C  CA  . LYS B 1 227 ? -39.339 -25.418 40.686  1.00 14.72 ? 227 LYS A CA  1 
ATOM   3927 C  C   . LYS B 1 227 ? -39.848 -26.263 39.512  1.00 11.48 ? 227 LYS A C   1 
ATOM   3928 O  O   . LYS B 1 227 ? -41.027 -26.160 39.199  1.00 13.81 ? 227 LYS A O   1 
ATOM   3929 C  CB  . LYS B 1 227 ? -38.829 -24.052 40.176  1.00 15.77 ? 227 LYS A CB  1 
ATOM   3930 C  CG  . LYS B 1 227 ? -38.525 -23.101 41.405  1.00 18.27 ? 227 LYS A CG  1 
ATOM   3931 C  CD  . LYS B 1 227 ? -37.718 -21.846 41.062  1.00 27.01 ? 227 LYS A CD  1 
ATOM   3932 C  CE  . LYS B 1 227 ? -38.564 -20.826 40.311  1.00 32.32 ? 227 LYS A CE  1 
ATOM   3933 N  NZ  . LYS B 1 227 ? -38.230 -19.459 40.875  1.00 36.66 ? 227 LYS A NZ  1 
ATOM   3934 N  N   . PHE B 1 228 ? -38.923 -27.046 38.967  1.00 13.87 ? 228 PHE A N   1 
ATOM   3935 C  CA  . PHE B 1 228 ? -39.331 -27.867 37.813  1.00 12.96 ? 228 PHE A CA  1 
ATOM   3936 C  C   . PHE B 1 228 ? -40.305 -28.903 38.235  1.00 13.38 ? 228 PHE A C   1 
ATOM   3937 O  O   . PHE B 1 228 ? -41.203 -29.343 37.494  1.00 13.43 ? 228 PHE A O   1 
ATOM   3938 C  CB  . PHE B 1 228 ? -38.061 -28.520 37.164  1.00 12.34 ? 228 PHE A CB  1 
ATOM   3939 C  CG  . PHE B 1 228 ? -37.238 -27.476 36.486  1.00 13.41 ? 228 PHE A CG  1 
ATOM   3940 C  CD1 . PHE B 1 228 ? -36.116 -26.924 37.090  1.00 13.28 ? 228 PHE A CD1 1 
ATOM   3941 C  CD2 . PHE B 1 228 ? -37.657 -27.013 35.189  1.00 14.69 ? 228 PHE A CD2 1 
ATOM   3942 C  CE1 . PHE B 1 228 ? -35.357 -25.909 36.493  1.00 14.47 ? 228 PHE A CE1 1 
ATOM   3943 C  CE2 . PHE B 1 228 ? -36.905 -25.994 34.631  1.00 15.43 ? 228 PHE A CE2 1 
ATOM   3944 C  CZ  . PHE B 1 228 ? -35.806 -25.441 35.228  1.00 14.97 ? 228 PHE A CZ  1 
ATOM   3945 N  N   . ARG B 1 229 ? -40.145 -29.347 39.504  1.00 14.38 ? 229 ARG A N   1 
ATOM   3946 C  CA  . ARG B 1 229 ? -41.064 -30.409 40.018  1.00 14.16 ? 229 ARG A CA  1 
ATOM   3947 C  C   . ARG B 1 229 ? -42.485 -29.984 40.296  1.00 14.45 ? 229 ARG A C   1 
ATOM   3948 O  O   . ARG B 1 229 ? -43.348 -30.805 40.465  1.00 15.49 ? 229 ARG A O   1 
ATOM   3949 C  CB  . ARG B 1 229 ? -40.468 -31.053 41.289  1.00 13.08 ? 229 ARG A CB  1 
ATOM   3950 C  CG  . ARG B 1 229 ? -39.088 -31.598 41.117  1.00 11.32 ? 229 ARG A CG  1 
ATOM   3951 C  CD  . ARG B 1 229 ? -38.768 -32.488 42.422  1.00 12.60 ? 229 ARG A CD  1 
ATOM   3952 N  NE  . ARG B 1 229 ? -37.380 -32.930 42.392  1.00 12.88 ? 229 ARG A NE  1 
ATOM   3953 C  CZ  . ARG B 1 229 ? -36.387 -32.284 42.992  1.00 11.75 ? 229 ARG A CZ  1 
ATOM   3954 N  NH1 . ARG B 1 229 ? -36.639 -31.177 43.676  1.00 13.32 ? 229 ARG A NH1 1 
ATOM   3955 N  NH2 . ARG B 1 229 ? -35.145 -32.742 42.911  1.00 12.41 ? 229 ARG A NH2 1 
ATOM   3956 N  N   A SER B 1 230 ? -42.773 -28.666 40.294  0.50 14.33 ? 230 SER A N   1 
ATOM   3957 N  N   B SER B 1 230 ? -42.687 -28.661 40.271  0.50 14.75 ? 230 SER A N   1 
ATOM   3958 C  CA  A SER B 1 230 ? -44.177 -28.181 40.370  0.50 16.48 ? 230 SER A CA  1 
ATOM   3959 C  CA  B SER B 1 230 ? -44.008 -28.059 40.346  0.50 16.87 ? 230 SER A CA  1 
ATOM   3960 C  C   A SER B 1 230 ? -44.925 -28.108 39.035  0.50 15.84 ? 230 SER A C   1 
ATOM   3961 C  C   B SER B 1 230 ? -44.827 -27.995 39.062  0.50 16.44 ? 230 SER A C   1 
ATOM   3962 O  O   A SER B 1 230 ? -46.159 -27.807 39.012  0.50 16.23 ? 230 SER A O   1 
ATOM   3963 O  O   B SER B 1 230 ? -46.016 -27.620 39.123  0.50 18.32 ? 230 SER A O   1 
ATOM   3964 C  CB  A SER B 1 230 ? -44.337 -26.806 41.024  0.50 17.09 ? 230 SER A CB  1 
ATOM   3965 C  CB  B SER B 1 230 ? -43.965 -26.665 40.938  0.50 18.79 ? 230 SER A CB  1 
ATOM   3966 O  OG  A SER B 1 230 ? -43.691 -25.821 40.288  0.50 20.68 ? 230 SER A OG  1 
ATOM   3967 O  OG  B SER B 1 230 ? -43.943 -26.827 42.336  0.50 23.23 ? 230 SER A OG  1 
ATOM   3968 N  N   . LEU B 1 231 ? -44.205 -28.366 37.922  1.00 15.41 ? 231 LEU A N   1 
ATOM   3969 C  CA  . LEU B 1 231 ? -44.881 -28.496 36.668  1.00 16.05 ? 231 LEU A CA  1 
ATOM   3970 C  C   . LEU B 1 231 ? -45.825 -29.692 36.806  1.00 14.68 ? 231 LEU A C   1 
ATOM   3971 O  O   . LEU B 1 231 ? -45.532 -30.690 37.510  1.00 16.38 ? 231 LEU A O   1 
ATOM   3972 C  CB  . LEU B 1 231 ? -43.850 -28.836 35.563  1.00 15.31 ? 231 LEU A CB  1 
ATOM   3973 C  CG  . LEU B 1 231 ? -43.077 -27.624 35.100  1.00 14.13 ? 231 LEU A CG  1 
ATOM   3974 C  CD1 . LEU B 1 231 ? -42.060 -28.198 34.138  1.00 16.76 ? 231 LEU A CD1 1 
ATOM   3975 C  CD2 . LEU B 1 231 ? -43.911 -26.535 34.371  1.00 15.59 ? 231 LEU A CD2 1 
ATOM   3976 N  N   . LEU B 1 232 ? -46.992 -29.653 36.157  1.00 15.88 ? 232 LEU A N   1 
ATOM   3977 C  CA  . LEU B 1 232 ? -47.937 -30.795 36.162  1.00 17.35 ? 232 LEU A CA  1 
ATOM   3978 C  C   . LEU B 1 232 ? -47.793 -31.665 34.936  1.00 19.50 ? 232 LEU A C   1 
ATOM   3979 O  O   . LEU B 1 232 ? -47.451 -31.154 33.833  1.00 17.51 ? 232 LEU A O   1 
ATOM   3980 C  CB  . LEU B 1 232 ? -49.399 -30.333 36.229  1.00 18.86 ? 232 LEU A CB  1 
ATOM   3981 C  CG  . LEU B 1 232 ? -49.612 -29.310 37.333  1.00 17.48 ? 232 LEU A CG  1 
ATOM   3982 C  CD1 . LEU B 1 232 ? -51.101 -28.964 37.250  1.00 20.30 ? 232 LEU A CD1 1 
ATOM   3983 C  CD2 . LEU B 1 232 ? -49.347 -29.968 38.685  1.00 19.84 ? 232 LEU A CD2 1 
ATOM   3984 N  N   . CYS B 1 233 ? -48.047 -32.942 35.064  1.00 16.44 ? 233 CYS A N   1 
ATOM   3985 C  CA  . CYS B 1 233 ? -48.156 -33.825 33.880  1.00 16.67 ? 233 CYS A CA  1 
ATOM   3986 C  C   . CYS B 1 233 ? -49.608 -33.934 33.426  1.00 17.93 ? 233 CYS A C   1 
ATOM   3987 O  O   . CYS B 1 233 ? -49.922 -34.702 32.483  1.00 20.32 ? 233 CYS A O   1 
ATOM   3988 C  CB  . CYS B 1 233 ? -47.546 -35.194 34.101  1.00 15.77 ? 233 CYS A CB  1 
ATOM   3989 S  SG  . CYS B 1 233 ? -48.315 -36.146 35.483  1.00 21.53 ? 233 CYS A SG  1 
ATOM   3990 N  N   . THR B 1 234 ? -50.480 -33.161 34.069  1.00 18.92 ? 234 THR A N   1 
ATOM   3991 C  CA  . THR B 1 234 ? -51.910 -33.101 33.740  1.00 19.66 ? 234 THR A CA  1 
ATOM   3992 C  C   . THR B 1 234 ? -52.298 -31.735 33.148  1.00 22.32 ? 234 THR A C   1 
ATOM   3993 O  O   . THR B 1 234 ? -51.694 -30.719 33.447  1.00 18.68 ? 234 THR A O   1 
ATOM   3994 C  CB  . THR B 1 234 ? -52.746 -33.366 35.014  1.00 21.14 ? 234 THR A CB  1 
ATOM   3995 O  OG1 . THR B 1 234 ? -52.235 -32.571 36.078  1.00 20.16 ? 234 THR A OG1 1 
ATOM   3996 C  CG2 . THR B 1 234 ? -52.656 -34.862 35.348  1.00 22.48 ? 234 THR A CG2 1 
ATOM   3997 N  N   . ALA B 1 235 ? -53.363 -31.755 32.313  1.00 22.77 ? 235 ALA A N   1 
ATOM   3998 C  CA  . ALA B 1 235 ? -53.916 -30.543 31.735  1.00 27.52 ? 235 ALA A CA  1 
ATOM   3999 C  C   . ALA B 1 235 ? -54.858 -29.768 32.686  1.00 27.93 ? 235 ALA A C   1 
ATOM   4000 O  O   . ALA B 1 235 ? -55.345 -30.315 33.689  1.00 28.45 ? 235 ALA A O   1 
ATOM   4001 C  CB  . ALA B 1 235 ? -54.604 -30.878 30.378  1.00 26.39 ? 235 ALA A CB  1 
ATOM   4002 N  N   . GLU B 1 236 ? -55.113 -28.505 32.363  1.00 32.78 ? 236 GLU A N   1 
ATOM   4003 C  CA  . GLU B 1 236 ? -56.141 -27.707 33.040  1.00 34.65 ? 236 GLU A CA  1 
ATOM   4004 C  C   . GLU B 1 236 ? -57.448 -28.504 33.216  1.00 35.56 ? 236 GLU A C   1 
ATOM   4005 O  O   . GLU B 1 236 ? -57.860 -29.284 32.307  1.00 36.21 ? 236 GLU A O   1 
ATOM   4006 C  CB  . GLU B 1 236 ? -56.409 -26.428 32.238  1.00 34.38 ? 236 GLU A CB  1 
ATOM   4007 C  CG  . GLU B 1 236 ? -56.642 -25.208 33.116  1.00 42.25 ? 236 GLU A CG  1 
ATOM   4008 C  CD  . GLU B 1 236 ? -56.479 -23.921 32.327  1.00 53.18 ? 236 GLU A CD  1 
ATOM   4009 O  OE1 . GLU B 1 236 ? -55.879 -22.958 32.882  1.00 58.69 ? 236 GLU A OE1 1 
ATOM   4010 O  OE2 . GLU B 1 236 ? -56.936 -23.883 31.151  1.00 49.20 ? 236 GLU A OE2 1 
ATOM   4011 N  N   . GLY B 1 237 ? -58.027 -28.372 34.418  1.00 36.81 ? 237 GLY A N   1 
ATOM   4012 C  CA  . GLY B 1 237 ? -59.329 -28.970 34.740  1.00 43.88 ? 237 GLY A CA  1 
ATOM   4013 C  C   . GLY B 1 237 ? -59.321 -30.479 34.974  1.00 45.96 ? 237 GLY A C   1 
ATOM   4014 O  O   . GLY B 1 237 ? -60.378 -31.115 35.062  1.00 46.27 ? 237 GLY A O   1 
ATOM   4015 N  N   . GLU B 1 238 ? -58.128 -31.053 35.044  1.00 39.76 ? 238 GLU A N   1 
ATOM   4016 C  CA  . GLU B 1 238 ? -57.943 -32.452 35.378  1.00 41.20 ? 238 GLU A CA  1 
ATOM   4017 C  C   . GLU B 1 238 ? -57.445 -32.417 36.813  1.00 37.80 ? 238 GLU A C   1 
ATOM   4018 O  O   . GLU B 1 238 ? -56.803 -31.438 37.226  1.00 33.43 ? 238 GLU A O   1 
ATOM   4019 C  CB  . GLU B 1 238 ? -56.811 -33.067 34.582  1.00 42.99 ? 238 GLU A CB  1 
ATOM   4020 C  CG  . GLU B 1 238 ? -57.035 -33.526 33.165  1.00 50.28 ? 238 GLU A CG  1 
ATOM   4021 C  CD  . GLU B 1 238 ? -55.851 -34.417 32.772  1.00 56.13 ? 238 GLU A CD  1 
ATOM   4022 O  OE1 . GLU B 1 238 ? -55.038 -34.049 31.880  1.00 50.51 ? 238 GLU A OE1 1 
ATOM   4023 O  OE2 . GLU B 1 238 ? -55.683 -35.484 33.420  1.00 59.42 ? 238 GLU A OE2 1 
ATOM   4024 N  N   . ALA B 1 239 ? -57.753 -33.473 37.567  1.00 40.82 ? 239 ALA A N   1 
ATOM   4025 C  CA  . ALA B 1 239 ? -57.101 -33.739 38.871  1.00 33.39 ? 239 ALA A CA  1 
ATOM   4026 C  C   . ALA B 1 239 ? -55.560 -33.618 38.719  1.00 28.11 ? 239 ALA A C   1 
ATOM   4027 O  O   . ALA B 1 239 ? -54.997 -34.273 37.871  1.00 28.00 ? 239 ALA A O   1 
ATOM   4028 C  CB  . ALA B 1 239 ? -57.491 -35.143 39.345  1.00 31.30 ? 239 ALA A CB  1 
ATOM   4029 N  N   . ALA B 1 240 ? -54.939 -32.777 39.542  1.00 28.31 ? 240 ALA A N   1 
ATOM   4030 C  CA  . ALA B 1 240 ? -53.510 -32.451 39.368  1.00 24.49 ? 240 ALA A CA  1 
ATOM   4031 C  C   . ALA B 1 240 ? -52.580 -33.634 39.717  1.00 24.87 ? 240 ALA A C   1 
ATOM   4032 O  O   . ALA B 1 240 ? -52.798 -34.392 40.693  1.00 21.84 ? 240 ALA A O   1 
ATOM   4033 C  CB  . ALA B 1 240 ? -53.130 -31.185 40.125  1.00 23.63 ? 240 ALA A CB  1 
ATOM   4034 N  N   . ALA B 1 241 ? -51.526 -33.788 38.929  1.00 17.67 ? 241 ALA A N   1 
ATOM   4035 C  CA  . ALA B 1 241 ? -50.453 -34.730 39.228  1.00 16.24 ? 241 ALA A CA  1 
ATOM   4036 C  C   . ALA B 1 241 ? -49.209 -34.044 38.830  1.00 17.28 ? 241 ALA A C   1 
ATOM   4037 O  O   . ALA B 1 241 ? -49.234 -33.317 37.783  1.00 16.82 ? 241 ALA A O   1 
ATOM   4038 C  CB  . ALA B 1 241 ? -50.560 -36.054 38.492  1.00 18.87 ? 241 ALA A CB  1 
ATOM   4039 N  N   . PHE B 1 242 ? -48.167 -34.149 39.663  1.00 14.38 ? 242 PHE A N   1 
ATOM   4040 C  CA  . PHE B 1 242 ? -46.966 -33.336 39.506  1.00 14.25 ? 242 PHE A CA  1 
ATOM   4041 C  C   . PHE B 1 242 ? -45.857 -34.122 38.809  1.00 13.32 ? 242 PHE A C   1 
ATOM   4042 O  O   . PHE B 1 242 ? -45.668 -35.373 39.064  1.00 15.31 ? 242 PHE A O   1 
ATOM   4043 C  CB  . PHE B 1 242 ? -46.445 -32.971 40.911  1.00 13.86 ? 242 PHE A CB  1 
ATOM   4044 C  CG  . PHE B 1 242 ? -47.314 -31.971 41.609  1.00 19.05 ? 242 PHE A CG  1 
ATOM   4045 C  CD1 . PHE B 1 242 ? -48.427 -32.436 42.364  1.00 18.35 ? 242 PHE A CD1 1 
ATOM   4046 C  CD2 . PHE B 1 242 ? -47.121 -30.598 41.400  1.00 20.87 ? 242 PHE A CD2 1 
ATOM   4047 C  CE1 . PHE B 1 242 ? -49.268 -31.497 43.014  1.00 20.85 ? 242 PHE A CE1 1 
ATOM   4048 C  CE2 . PHE B 1 242 ? -47.947 -29.673 42.032  1.00 24.55 ? 242 PHE A CE2 1 
ATOM   4049 C  CZ  . PHE B 1 242 ? -49.030 -30.133 42.794  1.00 18.10 ? 242 PHE A CZ  1 
ATOM   4050 N  N   . LEU B 1 243 ? -45.062 -33.416 37.972  1.00 14.64 ? 243 LEU A N   1 
ATOM   4051 C  CA  . LEU B 1 243 ? -43.965 -34.052 37.252  1.00 13.99 ? 243 LEU A CA  1 
ATOM   4052 C  C   . LEU B 1 243 ? -42.744 -33.995 38.179  1.00 12.41 ? 243 LEU A C   1 
ATOM   4053 O  O   . LEU B 1 243 ? -41.778 -33.269 37.984  1.00 12.89 ? 243 LEU A O   1 
ATOM   4054 C  CB  . LEU B 1 243 ? -43.794 -33.264 35.913  1.00 14.30 ? 243 LEU A CB  1 
ATOM   4055 C  CG  . LEU B 1 243 ? -42.727 -33.881 34.997  1.00 13.11 ? 243 LEU A CG  1 
ATOM   4056 C  CD1 . LEU B 1 243 ? -43.128 -35.272 34.542  1.00 13.49 ? 243 LEU A CD1 1 
ATOM   4057 C  CD2 . LEU B 1 243 ? -42.637 -32.923 33.777  1.00 16.64 ? 243 LEU A CD2 1 
ATOM   4058 N  N   . VAL B 1 244 ? -42.829 -34.792 39.252  1.00 13.60 ? 244 VAL A N   1 
ATOM   4059 C  CA  . VAL B 1 244 ? -41.706 -34.737 40.190  1.00 13.10 ? 244 VAL A CA  1 
ATOM   4060 C  C   . VAL B 1 244 ? -40.427 -35.465 39.767  1.00 11.38 ? 244 VAL A C   1 
ATOM   4061 O  O   . VAL B 1 244 ? -39.336 -35.265 40.280  1.00 13.60 ? 244 VAL A O   1 
ATOM   4062 C  CB  . VAL B 1 244 ? -42.121 -35.296 41.626  1.00 15.17 ? 244 VAL A CB  1 
ATOM   4063 C  CG1 . VAL B 1 244 ? -43.147 -34.387 42.269  1.00 16.23 ? 244 VAL A CG1 1 
ATOM   4064 C  CG2 . VAL B 1 244 ? -42.656 -36.699 41.572  1.00 17.67 ? 244 VAL A CG2 1 
ATOM   4065 N  N   . SER B 1 245 ? -40.573 -36.374 38.758  1.00 11.79 ? 245 SER A N   1 
ATOM   4066 C  CA  . SER B 1 245 ? -39.480 -37.126 38.263  1.00 11.40 ? 245 SER A CA  1 
ATOM   4067 C  C   . SER B 1 245 ? -39.828 -37.491 36.768  1.00 11.03 ? 245 SER A C   1 
ATOM   4068 O  O   . SER B 1 245 ? -40.942 -37.832 36.456  1.00 13.09 ? 245 SER A O   1 
ATOM   4069 C  CB  . SER B 1 245 ? -39.276 -38.495 39.054  1.00 12.45 ? 245 SER A CB  1 
ATOM   4070 O  OG  . SER B 1 245 ? -38.090 -39.173 38.693  1.00 14.40 ? 245 SER A OG  1 
ATOM   4071 N  N   . ASN B 1 246 ? -38.769 -37.388 35.949  1.00 9.93  ? 246 ASN A N   1 
ATOM   4072 C  CA  . ASN B 1 246 ? -39.028 -37.646 34.495  1.00 12.03 ? 246 ASN A CA  1 
ATOM   4073 C  C   . ASN B 1 246 ? -37.752 -38.186 33.867  1.00 11.74 ? 246 ASN A C   1 
ATOM   4074 O  O   . ASN B 1 246 ? -37.414 -37.731 32.702  1.00 12.17 ? 246 ASN A O   1 
ATOM   4075 C  CB  . ASN B 1 246 ? -39.521 -36.343 33.765  1.00 12.42 ? 246 ASN A CB  1 
ATOM   4076 C  CG  . ASN B 1 246 ? -38.534 -35.190 33.846  1.00 11.04 ? 246 ASN A CG  1 
ATOM   4077 O  OD1 . ASN B 1 246 ? -37.549 -35.255 34.539  1.00 11.61 ? 246 ASN A OD1 1 
ATOM   4078 N  ND2 . ASN B 1 246 ? -38.724 -34.177 32.983  1.00 10.60 ? 246 ASN A ND2 1 
ATOM   4079 N  N   . HIS B 1 247 ? -36.979 -39.080 34.489  1.00 10.71 ? 247 HIS A N   1 
ATOM   4080 C  CA  . HIS B 1 247 ? -35.806 -39.629 33.912  1.00 11.75 ? 247 HIS A CA  1 
ATOM   4081 C  C   . HIS B 1 247 ? -35.948 -41.111 33.699  1.00 13.52 ? 247 HIS A C   1 
ATOM   4082 O  O   . HIS B 1 247 ? -36.521 -41.908 34.517  1.00 15.31 ? 247 HIS A O   1 
ATOM   4083 C  CB  . HIS B 1 247 ? -34.582 -39.285 34.759  1.00 12.42 ? 247 HIS A CB  1 
ATOM   4084 C  CG  . HIS B 1 247 ? -34.650 -39.857 36.170  1.00 13.59 ? 247 HIS A CG  1 
ATOM   4085 N  ND1 . HIS B 1 247 ? -34.011 -41.005 36.501  1.00 17.77 ? 247 HIS A ND1 1 
ATOM   4086 C  CD2 . HIS B 1 247 ? -35.405 -39.468 37.271  1.00 11.55 ? 247 HIS A CD2 1 
ATOM   4087 C  CE1 . HIS B 1 247 ? -34.298 -41.292 37.841  1.00 16.85 ? 247 HIS A CE1 1 
ATOM   4088 N  NE2 . HIS B 1 247 ? -35.136 -40.404 38.286  1.00 16.96 ? 247 HIS A NE2 1 
ATOM   4089 N  N   . ARG B 1 248 ? -35.369 -41.559 32.600  1.00 11.48 ? 248 ARG A N   1 
ATOM   4090 C  CA  . ARG B 1 248 ? -35.335 -43.008 32.299  1.00 10.72 ? 248 ARG A CA  1 
ATOM   4091 C  C   . ARG B 1 248 ? -33.999 -43.559 32.805  1.00 10.66 ? 248 ARG A C   1 
ATOM   4092 O  O   . ARG B 1 248 ? -32.926 -42.979 32.604  1.00 12.05 ? 248 ARG A O   1 
ATOM   4093 C  CB  . ARG B 1 248 ? -35.386 -43.205 30.749  1.00 11.24 ? 248 ARG A CB  1 
ATOM   4094 C  CG  . ARG B 1 248 ? -35.478 -44.706 30.400  1.00 11.62 ? 248 ARG A CG  1 
ATOM   4095 C  CD  . ARG B 1 248 ? -35.199 -44.934 28.870  1.00 13.63 ? 248 ARG A CD  1 
ATOM   4096 N  NE  . ARG B 1 248 ? -35.741 -46.286 28.595  1.00 13.13 ? 248 ARG A NE  1 
ATOM   4097 C  CZ  . ARG B 1 248 ? -35.619 -46.953 27.423  1.00 16.37 ? 248 ARG A CZ  1 
ATOM   4098 N  NH1 . ARG B 1 248 ? -34.801 -46.547 26.487  1.00 14.23 ? 248 ARG A NH1 1 
ATOM   4099 N  NH2 . ARG B 1 248 ? -36.189 -48.150 27.254  1.00 15.59 ? 248 ARG A NH2 1 
ATOM   4100 N  N   . PRO B 1 249 ? -34.033 -44.777 33.420  1.00 13.11 ? 249 PRO A N   1 
ATOM   4101 C  CA  . PRO B 1 249 ? -32.791 -45.403 33.856  1.00 12.74 ? 249 PRO A CA  1 
ATOM   4102 C  C   . PRO B 1 249 ? -31.908 -45.806 32.654  1.00 11.91 ? 249 PRO A C   1 
ATOM   4103 O  O   . PRO B 1 249 ? -32.491 -46.133 31.534  1.00 12.65 ? 249 PRO A O   1 
ATOM   4104 C  CB  . PRO B 1 249 ? -33.263 -46.708 34.537  1.00 16.16 ? 249 PRO A CB  1 
ATOM   4105 C  CG  . PRO B 1 249 ? -34.694 -46.399 34.905  1.00 17.39 ? 249 PRO A CG  1 
ATOM   4106 C  CD  . PRO B 1 249 ? -35.221 -45.533 33.750  1.00 14.56 ? 249 PRO A CD  1 
ATOM   4107 N  N   . PRO B 1 250 ? -30.621 -45.884 32.869  1.00 12.99 ? 250 PRO A N   1 
ATOM   4108 C  CA  . PRO B 1 250 ? -29.722 -46.448 31.841  1.00 14.26 ? 250 PRO A CA  1 
ATOM   4109 C  C   . PRO B 1 250 ? -30.150 -47.820 31.389  1.00 13.40 ? 250 PRO A C   1 
ATOM   4110 O  O   . PRO B 1 250 ? -30.610 -48.690 32.213  1.00 13.69 ? 250 PRO A O   1 
ATOM   4111 C  CB  . PRO B 1 250 ? -28.344 -46.527 32.578  1.00 14.53 ? 250 PRO A CB  1 
ATOM   4112 C  CG  . PRO B 1 250 ? -28.417 -45.315 33.569  1.00 14.01 ? 250 PRO A CG  1 
ATOM   4113 C  CD  . PRO B 1 250 ? -29.820 -45.375 34.044  1.00 14.04 ? 250 PRO A CD  1 
ATOM   4114 N  N   . GLN B 1 251 ? -29.937 -48.061 30.104  1.00 12.55 ? 251 GLN A N   1 
ATOM   4115 C  CA  . GLN B 1 251 ? -30.197 -49.356 29.497  1.00 13.24 ? 251 GLN A CA  1 
ATOM   4116 C  C   . GLN B 1 251 ? -28.854 -49.958 29.092  1.00 11.40 ? 251 GLN A C   1 
ATOM   4117 O  O   . GLN B 1 251 ? -27.799 -49.300 28.963  1.00 14.40 ? 251 GLN A O   1 
ATOM   4118 C  CB  . GLN B 1 251 ? -31.049 -49.056 28.216  1.00 14.32 ? 251 GLN A CB  1 
ATOM   4119 C  CG  . GLN B 1 251 ? -32.386 -48.378 28.553  1.00 15.51 ? 251 GLN A CG  1 
ATOM   4120 C  CD  . GLN B 1 251 ? -33.203 -49.105 29.590  1.00 18.26 ? 251 GLN A CD  1 
ATOM   4121 O  OE1 . GLN B 1 251 ? -33.561 -48.548 30.640  1.00 19.63 ? 251 GLN A OE1 1 
ATOM   4122 N  NE2 . GLN B 1 251 ? -33.477 -50.361 29.345  1.00 17.75 ? 251 GLN A NE2 1 
ATOM   4123 N  N   . PRO B 1 252 ? -28.867 -51.295 28.892  1.00 13.73 ? 252 PRO A N   1 
ATOM   4124 C  CA  . PRO B 1 252 ? -27.588 -51.923 28.632  1.00 15.39 ? 252 PRO A CA  1 
ATOM   4125 C  C   . PRO B 1 252 ? -26.924 -51.554 27.309  1.00 14.23 ? 252 PRO A C   1 
ATOM   4126 O  O   . PRO B 1 252 ? -27.659 -51.335 26.314  1.00 15.22 ? 252 PRO A O   1 
ATOM   4127 C  CB  . PRO B 1 252 ? -27.952 -53.428 28.606  1.00 17.79 ? 252 PRO A CB  1 
ATOM   4128 C  CG  . PRO B 1 252 ? -29.244 -53.545 29.290  1.00 18.21 ? 252 PRO A CG  1 
ATOM   4129 C  CD  . PRO B 1 252 ? -29.958 -52.239 29.027  1.00 14.32 ? 252 PRO A CD  1 
ATOM   4130 N  N   . LEU B 1 253 ? -25.591 -51.591 27.312  1.00 15.49 ? 253 LEU A N   1 
ATOM   4131 C  CA  . LEU B 1 253 ? -24.828 -51.190 26.130  1.00 16.56 ? 253 LEU A CA  1 
ATOM   4132 C  C   . LEU B 1 253 ? -25.001 -52.148 24.984  1.00 18.02 ? 253 LEU A C   1 
ATOM   4133 O  O   . LEU B 1 253 ? -24.924 -51.695 23.838  1.00 16.01 ? 253 LEU A O   1 
ATOM   4134 C  CB  . LEU B 1 253 ? -23.354 -50.997 26.426  1.00 21.28 ? 253 LEU A CB  1 
ATOM   4135 C  CG  . LEU B 1 253 ? -22.883 -49.631 26.816  1.00 27.95 ? 253 LEU A CG  1 
ATOM   4136 C  CD1 . LEU B 1 253 ? -21.405 -49.850 27.106  1.00 29.58 ? 253 LEU A CD1 1 
ATOM   4137 C  CD2 . LEU B 1 253 ? -23.108 -48.619 25.703  1.00 25.97 ? 253 LEU A CD2 1 
ATOM   4138 N  N   . LYS B 1 254 ? -25.167 -53.451 25.269  1.00 17.59 ? 254 LYS A N   1 
ATOM   4139 C  CA  . LYS B 1 254 ? -25.357 -54.473 24.241  1.00 19.32 ? 254 LYS A CA  1 
ATOM   4140 C  C   . LYS B 1 254 ? -24.260 -54.400 23.165  1.00 16.71 ? 254 LYS A C   1 
ATOM   4141 O  O   . LYS B 1 254 ? -24.562 -54.403 21.936  1.00 22.93 ? 254 LYS A O   1 
ATOM   4142 C  CB  . LYS B 1 254 ? -26.781 -54.326 23.714  1.00 23.08 ? 254 LYS A CB  1 
ATOM   4143 C  CG  . LYS B 1 254 ? -27.784 -54.813 24.740  1.00 25.91 ? 254 LYS A CG  1 
ATOM   4144 C  CD  . LYS B 1 254 ? -29.187 -54.733 24.214  1.00 30.99 ? 254 LYS A CD  1 
ATOM   4145 C  CE  . LYS B 1 254 ? -30.053 -55.589 25.137  1.00 38.97 ? 254 LYS A CE  1 
ATOM   4146 N  NZ  . LYS B 1 254 ? -31.484 -55.419 24.797  1.00 42.27 ? 254 LYS A NZ  1 
ATOM   4147 N  N   . GLY B 1 255 ? -23.018 -54.232 23.557  1.00 19.22 ? 255 GLY A N   1 
ATOM   4148 C  CA  . GLY B 1 255 ? -21.952 -54.371 22.574  1.00 19.78 ? 255 GLY A CA  1 
ATOM   4149 C  C   . GLY B 1 255 ? -21.521 -53.071 21.918  1.00 18.67 ? 255 GLY A C   1 
ATOM   4150 O  O   . GLY B 1 255 ? -20.415 -53.042 21.324  1.00 18.21 ? 255 GLY A O   1 
ATOM   4151 N  N   . ARG B 1 256 ? -22.244 -51.946 22.197  1.00 16.28 ? 256 ARG A N   1 
ATOM   4152 C  CA  . ARG B 1 256 ? -21.712 -50.668 21.724  1.00 17.43 ? 256 ARG A CA  1 
ATOM   4153 C  C   . ARG B 1 256 ? -20.511 -50.198 22.530  1.00 18.80 ? 256 ARG A C   1 
ATOM   4154 O  O   . ARG B 1 256 ? -20.374 -50.612 23.715  1.00 21.79 ? 256 ARG A O   1 
ATOM   4155 C  CB  . ARG B 1 256 ? -22.846 -49.616 21.860  1.00 17.83 ? 256 ARG A CB  1 
ATOM   4156 C  CG  . ARG B 1 256 ? -24.075 -49.846 20.981  1.00 17.67 ? 256 ARG A CG  1 
ATOM   4157 C  CD  . ARG B 1 256 ? -25.233 -48.875 21.407  1.00 17.29 ? 256 ARG A CD  1 
ATOM   4158 N  NE  . ARG B 1 256 ? -25.795 -49.282 22.698  1.00 16.93 ? 256 ARG A NE  1 
ATOM   4159 C  CZ  . ARG B 1 256 ? -26.742 -48.585 23.308  1.00 16.48 ? 256 ARG A CZ  1 
ATOM   4160 N  NH1 . ARG B 1 256 ? -27.168 -47.386 22.772  1.00 13.50 ? 256 ARG A NH1 1 
ATOM   4161 N  NH2 . ARG B 1 256 ? -27.292 -49.062 24.428  1.00 15.09 ? 256 ARG A NH2 1 
ATOM   4162 N  N   . LYS B 1 257 ? -19.685 -49.354 21.958  1.00 21.49 ? 257 LYS A N   1 
ATOM   4163 C  CA  . LYS B 1 257 ? -18.580 -48.789 22.699  1.00 22.82 ? 257 LYS A CA  1 
ATOM   4164 C  C   . LYS B 1 257 ? -18.830 -47.273 22.676  1.00 21.96 ? 257 LYS A C   1 
ATOM   4165 O  O   . LYS B 1 257 ? -19.373 -46.688 21.745  1.00 24.02 ? 257 LYS A O   1 
ATOM   4166 C  CB  . LYS B 1 257 ? -17.263 -49.155 22.008  1.00 27.53 ? 257 LYS A CB  1 
ATOM   4167 C  CG  . LYS B 1 257 ? -16.886 -50.649 22.251  1.00 29.49 ? 257 LYS A CG  1 
ATOM   4168 C  CD  . LYS B 1 257 ? -15.913 -51.153 21.206  1.00 32.32 ? 257 LYS A CD  1 
ATOM   4169 C  CE  . LYS B 1 257 ? -15.482 -52.562 21.528  1.00 32.91 ? 257 LYS A CE  1 
ATOM   4170 N  NZ  . LYS B 1 257 ? -15.670 -53.362 20.320  1.00 44.15 ? 257 LYS A NZ  1 
ATOM   4171 N  N   . VAL B 1 258 ? -18.372 -46.669 23.735  1.00 19.67 ? 258 VAL A N   1 
ATOM   4172 C  CA  . VAL B 1 258 ? -18.429 -45.254 23.889  1.00 18.38 ? 258 VAL A CA  1 
ATOM   4173 C  C   . VAL B 1 258 ? -17.050 -44.683 23.560  1.00 20.16 ? 258 VAL A C   1 
ATOM   4174 O  O   . VAL B 1 258 ? -16.017 -45.226 24.010  1.00 21.07 ? 258 VAL A O   1 
ATOM   4175 C  CB  . VAL B 1 258 ? -18.765 -44.967 25.347  1.00 17.09 ? 258 VAL A CB  1 
ATOM   4176 C  CG1 . VAL B 1 258 ? -18.866 -43.467 25.561  1.00 19.85 ? 258 VAL A CG1 1 
ATOM   4177 C  CG2 . VAL B 1 258 ? -20.060 -45.672 25.774  1.00 17.12 ? 258 VAL A CG2 1 
ATOM   4178 N  N   . ARG B 1 259 ? -16.974 -43.594 22.787  1.00 17.56 ? 259 ARG A N   1 
ATOM   4179 C  CA  . ARG B 1 259 ? -15.686 -42.949 22.463  1.00 17.67 ? 259 ARG A CA  1 
ATOM   4180 C  C   . ARG B 1 259 ? -15.574 -41.600 23.241  1.00 18.04 ? 259 ARG A C   1 
ATOM   4181 O  O   . ARG B 1 259 ? -16.615 -40.975 23.545  1.00 17.54 ? 259 ARG A O   1 
ATOM   4182 C  CB  . ARG B 1 259 ? -15.636 -42.594 20.999  1.00 20.86 ? 259 ARG A CB  1 
ATOM   4183 C  CG  . ARG B 1 259 ? -15.732 -43.836 20.142  1.00 23.39 ? 259 ARG A CG  1 
ATOM   4184 C  CD  . ARG B 1 259 ? -15.550 -43.416 18.681  1.00 29.01 ? 259 ARG A CD  1 
ATOM   4185 N  NE  . ARG B 1 259 ? -16.804 -42.847 18.167  1.00 25.51 ? 259 ARG A NE  1 
ATOM   4186 C  CZ  . ARG B 1 259 ? -16.932 -42.034 17.118  1.00 25.37 ? 259 ARG A CZ  1 
ATOM   4187 N  NH1 . ARG B 1 259 ? -15.883 -41.655 16.399  1.00 26.76 ? 259 ARG A NH1 1 
ATOM   4188 N  NH2 . ARG B 1 259 ? -18.140 -41.597 16.783  1.00 24.67 ? 259 ARG A NH2 1 
ATOM   4189 N  N   . ALA B 1 260 ? -14.366 -41.156 23.522  1.00 16.60 ? 260 ALA A N   1 
ATOM   4190 C  CA  . ALA B 1 260 ? -14.124 -39.885 24.186  1.00 17.29 ? 260 ALA A CA  1 
ATOM   4191 C  C   . ALA B 1 260 ? -13.495 -38.874 23.242  1.00 20.15 ? 260 ALA A C   1 
ATOM   4192 O  O   . ALA B 1 260 ? -12.605 -39.234 22.443  1.00 19.88 ? 260 ALA A O   1 
ATOM   4193 C  CB  . ALA B 1 260 ? -13.206 -40.119 25.380  1.00 18.77 ? 260 ALA A CB  1 
ATOM   4194 N  N   . SER B 1 261 ? -13.815 -37.601 23.403  1.00 16.21 ? 261 SER A N   1 
ATOM   4195 C  CA  . SER B 1 261 ? -13.206 -36.553 22.615  1.00 18.16 ? 261 SER A CA  1 
ATOM   4196 C  C   . SER B 1 261 ? -11.828 -36.071 23.185  1.00 19.70 ? 261 SER A C   1 
ATOM   4197 O  O   . SER B 1 261 ? -11.172 -35.134 22.592  1.00 19.99 ? 261 SER A O   1 
ATOM   4198 C  CB  . SER B 1 261 ? -14.117 -35.358 22.556  1.00 17.03 ? 261 SER A CB  1 
ATOM   4199 O  OG  . SER B 1 261 ? -14.093 -34.642 23.807  1.00 14.12 ? 261 SER A OG  1 
ATOM   4200 N  N   . PHE B 1 262 ? -11.443 -36.639 24.351  1.00 17.71 ? 262 PHE A N   1 
ATOM   4201 C  CA  . PHE B 1 262 ? -10.369 -36.069 25.158  1.00 21.27 ? 262 PHE A CA  1 
ATOM   4202 C  C   . PHE B 1 262 ? -9.504  -37.225 25.705  1.00 24.41 ? 262 PHE A C   1 
ATOM   4203 O  O   . PHE B 1 262 ? -9.945  -38.388 25.782  1.00 23.87 ? 262 PHE A O   1 
ATOM   4204 C  CB  . PHE B 1 262 ? -10.965 -35.206 26.327  1.00 20.30 ? 262 PHE A CB  1 
ATOM   4205 C  CG  . PHE B 1 262 ? -11.841 -36.005 27.245  1.00 19.07 ? 262 PHE A CG  1 
ATOM   4206 C  CD1 . PHE B 1 262 ? -11.338 -36.562 28.422  1.00 22.27 ? 262 PHE A CD1 1 
ATOM   4207 C  CD2 . PHE B 1 262 ? -13.212 -36.214 26.955  1.00 18.54 ? 262 PHE A CD2 1 
ATOM   4208 C  CE1 . PHE B 1 262 ? -12.181 -37.381 29.204  1.00 20.30 ? 262 PHE A CE1 1 
ATOM   4209 C  CE2 . PHE B 1 262 ? -14.035 -37.010 27.739  1.00 17.86 ? 262 PHE A CE2 1 
ATOM   4210 C  CZ  . PHE B 1 262 ? -13.534 -37.606 28.885  1.00 19.45 ? 262 PHE A CZ  1 
ATOM   4211 N  N   . HIS B 1 263 ? -8.263  -36.843 26.052  1.00 31.52 ? 263 HIS A N   1 
ATOM   4212 C  CA  . HIS B 1 263 ? -7.176  -37.762 26.433  1.00 43.27 ? 263 HIS A CA  1 
ATOM   4213 C  C   . HIS B 1 263 ? -7.262  -38.114 27.888  1.00 51.10 ? 263 HIS A C   1 
ATOM   4214 O  O   . HIS B 1 263 ? -6.284  -38.573 28.506  1.00 57.72 ? 263 HIS A O   1 
ATOM   4215 C  CB  . HIS B 1 263 ? -5.819  -37.094 26.178  1.00 45.94 ? 263 HIS A CB  1 
ATOM   4216 C  CG  . HIS B 1 263 ? -5.244  -37.357 24.814  1.00 51.64 ? 263 HIS A CG  1 
ATOM   4217 N  ND1 . HIS B 1 263 ? -5.002  -38.603 24.358  1.00 53.93 ? 263 HIS A ND1 1 
ATOM   4218 C  CD2 . HIS B 1 263 ? -4.801  -36.470 23.808  1.00 59.35 ? 263 HIS A CD2 1 
ATOM   4219 C  CE1 . HIS B 1 263 ? -4.453  -38.528 23.114  1.00 59.79 ? 263 HIS A CE1 1 
ATOM   4220 N  NE2 . HIS B 1 263 ? -4.335  -37.223 22.781  1.00 59.01 ? 263 HIS A NE2 1 
ATOM   4221 O  OXT . HIS B 1 263 ? -8.311  -37.941 28.509  1.00 57.08 ? 263 HIS A OXT 1 
HETATM 4222 ZN ZN  . ZN  C 2 .   ? -6.650  -4.608  13.186  1.00 12.19 ? 301 ZN  B ZN  1 
HETATM 4223 CL CL1 . 6YQ D 3 .   ? -6.674  -5.057  19.204  1.00 27.94 ? 302 6YQ B CL1 1 
HETATM 4224 C  C6  . 6YQ D 3 .   ? -6.747  -3.466  18.461  1.00 25.08 ? 302 6YQ B C6  1 
HETATM 4225 C  C1  . 6YQ D 3 .   ? -6.334  -3.308  17.116  1.00 25.01 ? 302 6YQ B C1  1 
HETATM 4226 S  S7  . 6YQ D 3 .   ? -5.667  -4.594  16.078  1.00 22.66 ? 302 6YQ B S7  1 
HETATM 4227 O  O9  . 6YQ D 3 .   ? -4.472  -5.325  16.568  1.00 25.72 ? 302 6YQ B O9  1 
HETATM 4228 N  N10 . 6YQ D 3 .   ? -5.441  -3.827  14.421  1.00 21.48 ? 302 6YQ B N10 1 
HETATM 4229 O  O8  . 6YQ D 3 .   ? -6.826  -5.358  15.609  1.00 21.07 ? 302 6YQ B O8  1 
HETATM 4230 C  C5  . 6YQ D 3 .   ? -7.237  -2.381  19.216  1.00 28.67 ? 302 6YQ B C5  1 
HETATM 4231 C  C4  . 6YQ D 3 .   ? -7.302  -1.108  18.666  1.00 29.99 ? 302 6YQ B C4  1 
HETATM 4232 C  C3  . 6YQ D 3 .   ? -6.879  -1.002  17.335  1.00 27.91 ? 302 6YQ B C3  1 
HETATM 4233 C  C2  . 6YQ D 3 .   ? -6.414  -2.047  16.564  1.00 27.04 ? 302 6YQ B C2  1 
HETATM 4234 C  C11 . 6YQ D 3 .   ? -7.772  0.064   19.439  1.00 41.51 ? 302 6YQ B C11 1 
HETATM 4235 O  O12 . 6YQ D 3 .   ? -8.711  -0.073  20.226  1.00 40.91 ? 302 6YQ B O12 1 
HETATM 4236 C  C13 . 6YQ D 3 .   ? -7.074  1.427   19.307  1.00 49.03 ? 302 6YQ B C13 1 
HETATM 4237 N  N14 . 6YQ D 3 .   ? -7.390  2.329   20.456  1.00 60.98 ? 302 6YQ B N14 1 
HETATM 4238 C  C18 . 6YQ D 3 .   ? -6.905  2.220   21.737  1.00 58.34 ? 302 6YQ B C18 1 
HETATM 4239 C  C20 . 6YQ D 3 .   ? -5.984  1.300   22.283  1.00 52.02 ? 302 6YQ B C20 1 
HETATM 4240 C  C21 . 6YQ D 3 .   ? -5.678  1.437   23.668  1.00 52.82 ? 302 6YQ B C21 1 
HETATM 4241 C  C22 . 6YQ D 3 .   ? -6.249  2.488   24.465  1.00 53.66 ? 302 6YQ B C22 1 
HETATM 4242 C  C23 . 6YQ D 3 .   ? -7.158  3.404   23.877  1.00 60.03 ? 302 6YQ B C23 1 
HETATM 4243 C  C19 . 6YQ D 3 .   ? -7.460  3.230   22.508  1.00 61.60 ? 302 6YQ B C19 1 
HETATM 4244 N  N17 . 6YQ D 3 .   ? -8.299  3.979   21.735  1.00 60.91 ? 302 6YQ B N17 1 
HETATM 4245 C  C16 . 6YQ D 3 .   ? -8.250  3.404   20.492  1.00 60.40 ? 302 6YQ B C16 1 
HETATM 4246 C  C1  . CIT E 4 .   ? 3.096   -5.011  -2.213  1.00 47.77 ? 303 CIT B C1  1 
HETATM 4247 O  O1  . CIT E 4 .   ? 3.200   -5.116  -3.463  1.00 55.04 ? 303 CIT B O1  1 
HETATM 4248 O  O2  . CIT E 4 .   ? 3.139   -5.992  -1.470  1.00 44.62 ? 303 CIT B O2  1 
HETATM 4249 C  C2  . CIT E 4 .   ? 2.952   -3.635  -1.599  1.00 41.81 ? 303 CIT B C2  1 
HETATM 4250 C  C3  . CIT E 4 .   ? 1.786   -3.494  -0.624  1.00 35.11 ? 303 CIT B C3  1 
HETATM 4251 O  O7  . CIT E 4 .   ? 0.967   -4.621  -0.251  1.00 29.23 ? 303 CIT B O7  1 
HETATM 4252 C  C4  . CIT E 4 .   ? 1.358   -2.125  -0.135  1.00 31.76 ? 303 CIT B C4  1 
HETATM 4253 C  C5  . CIT E 4 .   ? 0.148   -2.015  -1.062  1.00 29.74 ? 303 CIT B C5  1 
HETATM 4254 O  O3  . CIT E 4 .   ? 0.303   -1.848  -2.314  1.00 33.31 ? 303 CIT B O3  1 
HETATM 4255 O  O4  . CIT E 4 .   ? -0.943  -2.302  -0.642  1.00 23.15 ? 303 CIT B O4  1 
HETATM 4256 C  C6  . CIT E 4 .   ? 2.755   -3.785  0.525   1.00 37.50 ? 303 CIT B C6  1 
HETATM 4257 O  O5  . CIT E 4 .   ? 3.909   -3.249  0.567   1.00 36.06 ? 303 CIT B O5  1 
HETATM 4258 O  O6  . CIT E 4 .   ? 2.432   -4.597  1.432   1.00 32.86 ? 303 CIT B O6  1 
HETATM 4259 C  C1  . EDO F 5 .   ? -17.734 -26.855 11.362  1.00 32.14 ? 304 EDO B C1  1 
HETATM 4260 O  O1  . EDO F 5 .   ? -17.449 -28.291 11.539  1.00 29.31 ? 304 EDO B O1  1 
HETATM 4261 C  C2  . EDO F 5 .   ? -18.017 -26.561 9.893   1.00 31.35 ? 304 EDO B C2  1 
HETATM 4262 O  O2  . EDO F 5 .   ? -16.863 -26.761 9.048   1.00 37.83 ? 304 EDO B O2  1 
HETATM 4263 ZN ZN  . ZN  G 2 .   ? -34.260 -35.910 26.894  1.00 11.41 ? 301 ZN  A ZN  1 
HETATM 4264 CL CL1 . 6YQ H 3 .   ? -33.997 -36.824 21.006  1.00 23.91 ? 302 6YQ A CL1 1 
HETATM 4265 C  C6  . 6YQ H 3 .   ? -35.533 -36.521 21.783  1.00 25.30 ? 302 6YQ A C6  1 
HETATM 4266 C  C1  . 6YQ H 3 .   ? -35.643 -36.628 23.169  1.00 21.09 ? 302 6YQ A C1  1 
HETATM 4267 S  S7  . 6YQ H 3 .   ? -34.301 -37.182 24.231  1.00 19.81 ? 302 6YQ A S7  1 
HETATM 4268 O  O9  . 6YQ H 3 .   ? -33.795 -38.468 23.834  1.00 18.51 ? 302 6YQ A O9  1 
HETATM 4269 N  N10 . 6YQ H 3 .   ? -34.893 -37.305 25.955  1.00 19.35 ? 302 6YQ A N10 1 
HETATM 4270 O  O8  . 6YQ H 3 .   ? -33.409 -36.106 24.355  1.00 18.12 ? 302 6YQ A O8  1 
HETATM 4271 C  C5  . 6YQ H 3 .   ? -36.619 -36.132 21.010  1.00 28.54 ? 302 6YQ A C5  1 
HETATM 4272 C  C4  . 6YQ H 3 .   ? -37.837 -35.904 21.635  1.00 35.14 ? 302 6YQ A C4  1 
HETATM 4273 C  C3  . 6YQ H 3 .   ? -37.938 -36.059 23.008  1.00 27.09 ? 302 6YQ A C3  1 
HETATM 4274 C  C2  . 6YQ H 3 .   ? -36.872 -36.438 23.805  1.00 23.90 ? 302 6YQ A C2  1 
HETATM 4275 C  C11 . 6YQ H 3 .   ? -39.013 -35.482 20.836  1.00 43.80 ? 302 6YQ A C11 1 
HETATM 4276 O  O12 . 6YQ H 3 .   ? -38.863 -34.506 20.105  1.00 52.75 ? 302 6YQ A O12 1 
HETATM 4277 C  C13 . 6YQ H 3 .   ? -40.341 -36.221 20.886  1.00 56.31 ? 302 6YQ A C13 1 
HETATM 4278 N  N14 . 6YQ H 3 .   ? -41.064 -36.021 19.610  1.00 67.91 ? 302 6YQ A N14 1 
HETATM 4279 C  C18 . 6YQ H 3 .   ? -41.055 -36.853 18.534  1.00 72.53 ? 302 6YQ A C18 1 
HETATM 4280 C  C20 . 6YQ H 3 .   ? -40.443 -38.107 18.349  1.00 65.93 ? 302 6YQ A C20 1 
HETATM 4281 C  C21 . 6YQ H 3 .   ? -40.623 -38.757 17.101  1.00 60.13 ? 302 6YQ A C21 1 
HETATM 4282 C  C22 . 6YQ H 3 .   ? -41.409 -38.178 16.070  1.00 63.77 ? 302 6YQ A C22 1 
HETATM 4283 C  C23 . 6YQ H 3 .   ? -42.017 -36.921 16.289  1.00 69.10 ? 302 6YQ A C23 1 
HETATM 4284 C  C19 . 6YQ H 3 .   ? -41.814 -36.286 17.533  1.00 78.46 ? 302 6YQ A C19 1 
HETATM 4285 N  N17 . 6YQ H 3 .   ? -42.291 -35.081 17.955  1.00 81.28 ? 302 6YQ A N17 1 
HETATM 4286 C  C16 . 6YQ H 3 .   ? -41.814 -34.936 19.229  1.00 73.10 ? 302 6YQ A C16 1 
HETATM 4287 C  C1  . CIT I 4 .   ? -36.489 -44.066 42.943  1.00 55.94 ? 303 CIT A C1  1 
HETATM 4288 O  O1  . CIT I 4 .   ? -35.606 -43.181 42.980  1.00 49.27 ? 303 CIT A O1  1 
HETATM 4289 O  O2  . CIT I 4 .   ? -36.665 -44.963 43.827  1.00 63.10 ? 303 CIT A O2  1 
HETATM 4290 C  C2  . CIT I 4 .   ? -37.360 -43.999 41.727  1.00 44.74 ? 303 CIT A C2  1 
HETATM 4291 C  C3  . CIT I 4 .   ? -36.637 -43.062 40.745  1.00 37.68 ? 303 CIT A C3  1 
HETATM 4292 O  O7  . CIT I 4 .   ? -35.253 -43.224 40.265  1.00 31.57 ? 303 CIT A O7  1 
HETATM 4293 C  C4  . CIT I 4 .   ? -37.415 -41.791 40.250  1.00 32.37 ? 303 CIT A C4  1 
HETATM 4294 C  C5  . CIT I 4 .   ? -36.950 -40.619 41.098  1.00 26.57 ? 303 CIT A C5  1 
HETATM 4295 O  O3  . CIT I 4 .   ? -35.873 -40.085 40.789  1.00 25.47 ? 303 CIT A O3  1 
HETATM 4296 O  O4  . CIT I 4 .   ? -37.606 -40.341 42.125  1.00 34.26 ? 303 CIT A O4  1 
HETATM 4297 C  C6  . CIT I 4 .   ? -37.192 -44.058 39.711  1.00 46.24 ? 303 CIT A C6  1 
HETATM 4298 O  O5  . CIT I 4 .   ? -37.892 -43.628 38.754  1.00 58.94 ? 303 CIT A O5  1 
HETATM 4299 O  O6  . CIT I 4 .   ? -36.989 -45.310 39.855  1.00 56.76 ? 303 CIT A O6  1 
HETATM 4300 C  C1  . EDO J 5 .   ? -14.894 -32.106 34.097  1.00 39.97 ? 304 EDO A C1  1 
HETATM 4301 O  O1  . EDO J 5 .   ? -15.511 -31.575 35.296  1.00 37.70 ? 304 EDO A O1  1 
HETATM 4302 C  C2  . EDO J 5 .   ? -13.734 -31.251 33.606  1.00 47.32 ? 304 EDO A C2  1 
HETATM 4303 O  O2  . EDO J 5 .   ? -12.641 -32.165 33.372  1.00 64.04 ? 304 EDO A O2  1 
HETATM 4304 O  O   . HOH K 6 .   ? -30.729 -6.281  15.150  1.00 41.39 ? 401 HOH B O   1 
HETATM 4305 O  O   . HOH K 6 .   ? -0.504  -8.594  2.843   1.00 22.77 ? 402 HOH B O   1 
HETATM 4306 O  O   . HOH K 6 .   ? -21.451 4.142   0.235   1.00 24.60 ? 403 HOH B O   1 
HETATM 4307 O  O   . HOH K 6 .   ? -9.478  2.418   12.927  1.00 26.94 ? 404 HOH B O   1 
HETATM 4308 O  O   . HOH K 6 .   ? -17.346 3.952   15.109  1.00 30.91 ? 405 HOH B O   1 
HETATM 4309 O  O   . HOH K 6 .   ? -27.441 -10.896 4.587   1.00 44.29 ? 406 HOH B O   1 
HETATM 4310 O  O   . HOH K 6 .   ? 3.529   -17.124 5.854   1.00 17.79 ? 407 HOH B O   1 
HETATM 4311 O  O   . HOH K 6 .   ? -13.753 15.249  8.876   1.00 39.10 ? 408 HOH B O   1 
HETATM 4312 O  O   . HOH K 6 .   ? -13.019 -28.876 11.774  1.00 31.99 ? 409 HOH B O   1 
HETATM 4313 O  O   . HOH K 6 .   ? -30.877 -8.792  19.368  1.00 41.03 ? 410 HOH B O   1 
HETATM 4314 O  O   . HOH K 6 .   ? 8.858   -5.882  15.310  1.00 26.14 ? 411 HOH B O   1 
HETATM 4315 O  O   . HOH K 6 .   ? -27.496 -1.369  3.194   1.00 40.50 ? 412 HOH B O   1 
HETATM 4316 O  O   . HOH K 6 .   ? -8.899  8.991   14.371  1.00 40.39 ? 413 HOH B O   1 
HETATM 4317 O  O   . HOH K 6 .   ? -30.555 -7.625  22.814  1.00 37.16 ? 414 HOH B O   1 
HETATM 4318 O  O   . HOH K 6 .   ? -25.979 0.307   -2.345  1.00 35.90 ? 415 HOH B O   1 
HETATM 4319 O  O   . HOH K 6 .   ? -28.551 -9.906  9.003   1.00 41.19 ? 416 HOH B O   1 
HETATM 4320 O  O   . HOH K 6 .   ? -28.232 -6.303  33.124  1.00 33.06 ? 417 HOH B O   1 
HETATM 4321 O  O   . HOH K 6 .   ? -10.314 -26.742 9.601   1.00 28.71 ? 418 HOH B O   1 
HETATM 4322 O  O   . HOH K 6 .   ? -18.424 9.667   -1.448  1.00 36.20 ? 419 HOH B O   1 
HETATM 4323 O  O   . HOH K 6 .   ? 9.048   -13.261 22.067  1.00 32.53 ? 420 HOH B O   1 
HETATM 4324 O  O   . HOH K 6 .   ? -13.652 8.898   -1.626  1.00 22.73 ? 421 HOH B O   1 
HETATM 4325 O  O   . HOH K 6 .   ? -10.720 2.822   32.655  1.00 34.74 ? 422 HOH B O   1 
HETATM 4326 O  O   . HOH K 6 .   ? -32.388 4.761   18.311  1.00 19.73 ? 423 HOH B O   1 
HETATM 4327 O  O   . HOH K 6 .   ? 4.555   -24.452 6.806   1.00 18.55 ? 424 HOH B O   1 
HETATM 4328 O  O   . HOH K 6 .   ? -10.823 -4.811  -4.632  1.00 17.50 ? 425 HOH B O   1 
HETATM 4329 O  O   . HOH K 6 .   ? -4.872  3.060   17.561  1.00 38.23 ? 426 HOH B O   1 
HETATM 4330 O  O   . HOH K 6 .   ? 8.327   -6.976  24.334  1.00 23.95 ? 427 HOH B O   1 
HETATM 4331 O  O   . HOH K 6 .   ? -1.962  -2.145  10.887  1.00 14.88 ? 428 HOH B O   1 
HETATM 4332 O  O   . HOH K 6 .   ? -1.083  -23.571 4.165   1.00 33.85 ? 429 HOH B O   1 
HETATM 4333 O  O   . HOH K 6 .   ? 5.278   -8.944  25.624  1.00 25.76 ? 430 HOH B O   1 
HETATM 4334 O  O   . HOH K 6 .   ? -18.410 0.865   27.984  1.00 31.78 ? 431 HOH B O   1 
HETATM 4335 O  O   . HOH K 6 .   ? 10.152  -7.355  16.983  1.00 35.50 ? 432 HOH B O   1 
HETATM 4336 O  O   . HOH K 6 .   ? -11.737 -28.179 27.832  1.00 32.30 ? 433 HOH B O   1 
HETATM 4337 O  O   . HOH K 6 .   ? -21.876 10.796  8.498   1.00 31.76 ? 434 HOH B O   1 
HETATM 4338 O  O   . HOH K 6 .   ? 1.401   -8.287  6.758   1.00 23.64 ? 435 HOH B O   1 
HETATM 4339 O  O   . HOH K 6 .   ? 8.720   -19.966 17.554  1.00 32.03 ? 436 HOH B O   1 
HETATM 4340 O  O   . HOH K 6 .   ? -24.477 -4.782  23.309  1.00 20.80 ? 437 HOH B O   1 
HETATM 4341 O  O   . HOH K 6 .   ? -13.455 2.233   17.663  1.00 38.80 ? 438 HOH B O   1 
HETATM 4342 O  O   . HOH K 6 .   ? 1.930   -28.372 12.231  1.00 36.17 ? 439 HOH B O   1 
HETATM 4343 O  O   . HOH K 6 .   ? -19.856 1.208   24.612  1.00 26.81 ? 440 HOH B O   1 
HETATM 4344 O  O   . HOH K 6 .   ? 6.459   -13.574 11.384  1.00 22.47 ? 441 HOH B O   1 
HETATM 4345 O  O   . HOH K 6 .   ? -4.910  -11.451 26.001  1.00 14.04 ? 442 HOH B O   1 
HETATM 4346 O  O   . HOH K 6 .   ? -20.256 -6.471  -5.640  1.00 17.03 ? 443 HOH B O   1 
HETATM 4347 O  O   . HOH K 6 .   ? -6.379  -14.261 32.674  1.00 26.25 ? 444 HOH B O   1 
HETATM 4348 O  O   . HOH K 6 .   ? -17.526 -9.992  32.733  1.00 19.97 ? 445 HOH B O   1 
HETATM 4349 O  O   . HOH K 6 .   ? -16.263 -0.412  -5.956  1.00 21.23 ? 446 HOH B O   1 
HETATM 4350 O  O   . HOH K 6 .   ? -6.775  -0.404  -6.032  1.00 12.79 ? 447 HOH B O   1 
HETATM 4351 O  O   . HOH K 6 .   ? -13.145 5.143   14.180  1.00 34.38 ? 448 HOH B O   1 
HETATM 4352 O  O   . HOH K 6 .   ? -21.835 -6.821  25.001  1.00 18.25 ? 449 HOH B O   1 
HETATM 4353 O  O   . HOH K 6 .   ? -7.591  -7.445  37.785  1.00 21.31 ? 450 HOH B O   1 
HETATM 4354 O  O   . HOH K 6 .   ? 0.386   -10.043 -8.499  1.00 32.30 ? 451 HOH B O   1 
HETATM 4355 O  O   . HOH K 6 .   ? 8.277   -7.568  7.784   1.00 34.83 ? 452 HOH B O   1 
HETATM 4356 O  O   . HOH K 6 .   ? -18.265 -11.573 -7.203  1.00 31.77 ? 453 HOH B O   1 
HETATM 4357 O  O   . HOH K 6 .   ? -4.538  -1.931  33.422  1.00 26.55 ? 454 HOH B O   1 
HETATM 4358 O  O   . HOH K 6 .   ? -15.866 -23.771 23.914  1.00 20.48 ? 455 HOH B O   1 
HETATM 4359 O  O   . HOH K 6 .   ? 1.523   -23.875 25.413  1.00 29.99 ? 456 HOH B O   1 
HETATM 4360 O  O   . HOH K 6 .   ? -26.212 -0.044  5.350   1.00 29.97 ? 457 HOH B O   1 
HETATM 4361 O  O   . HOH K 6 .   ? -19.833 -13.861 30.061  1.00 23.84 ? 458 HOH B O   1 
HETATM 4362 O  O   . HOH K 6 .   ? -1.448  -20.985 2.549   1.00 34.75 ? 459 HOH B O   1 
HETATM 4363 O  O   . HOH K 6 .   ? -21.266 2.428   -4.421  1.00 37.96 ? 460 HOH B O   1 
HETATM 4364 O  O   . HOH K 6 .   ? -20.810 -0.968  32.089  1.00 22.89 ? 461 HOH B O   1 
HETATM 4365 O  O   . HOH K 6 .   ? -17.430 0.436   21.567  1.00 27.55 ? 462 HOH B O   1 
HETATM 4366 O  O   . HOH K 6 .   ? -24.865 2.322   27.981  1.00 24.43 ? 463 HOH B O   1 
HETATM 4367 O  O   . HOH K 6 .   ? 2.520   -2.936  4.703   1.00 29.81 ? 464 HOH B O   1 
HETATM 4368 O  O   . HOH K 6 .   ? -19.429 -14.243 5.426   1.00 20.50 ? 465 HOH B O   1 
HETATM 4369 O  O   . HOH K 6 .   ? -17.167 -10.548 28.725  1.00 15.73 ? 466 HOH B O   1 
HETATM 4370 O  O   . HOH K 6 .   ? -24.370 -11.721 15.339  1.00 16.33 ? 467 HOH B O   1 
HETATM 4371 O  O   . HOH K 6 .   ? -6.501  -5.661  -0.734  1.00 12.25 ? 468 HOH B O   1 
HETATM 4372 O  O   . HOH K 6 .   ? -20.654 -5.639  22.839  1.00 14.94 ? 469 HOH B O   1 
HETATM 4373 O  O   . HOH K 6 .   ? -28.654 -10.611 23.848  1.00 31.80 ? 470 HOH B O   1 
HETATM 4374 O  O   . HOH K 6 .   ? -2.603  3.934   2.321   1.00 20.96 ? 471 HOH B O   1 
HETATM 4375 O  O   . HOH K 6 .   ? -16.737 -15.915 32.929  1.00 35.59 ? 472 HOH B O   1 
HETATM 4376 O  O   . HOH K 6 .   ? -21.952 -0.644  -1.215  1.00 26.48 ? 473 HOH B O   1 
HETATM 4377 O  O   . HOH K 6 .   ? -21.810 -4.543  32.682  1.00 23.86 ? 474 HOH B O   1 
HETATM 4378 O  O   . HOH K 6 .   ? -18.420 -15.218 2.687   1.00 31.16 ? 475 HOH B O   1 
HETATM 4379 O  O   . HOH K 6 .   ? -1.018  -0.558  -6.267  1.00 13.41 ? 476 HOH B O   1 
HETATM 4380 O  O   . HOH K 6 .   ? 3.376   1.645   23.197  1.00 27.53 ? 477 HOH B O   1 
HETATM 4381 O  O   . HOH K 6 .   ? -4.575  -23.993 26.064  1.00 26.13 ? 478 HOH B O   1 
HETATM 4382 O  O   . HOH K 6 .   ? -21.126 -18.138 10.827  1.00 16.32 ? 479 HOH B O   1 
HETATM 4383 O  O   . HOH K 6 .   ? -11.025 -29.111 22.957  1.00 35.95 ? 480 HOH B O   1 
HETATM 4384 O  O   . HOH K 6 .   ? -23.756 -13.045 1.117   1.00 20.19 ? 481 HOH B O   1 
HETATM 4385 O  O   . HOH K 6 .   ? -5.709  -19.898 5.924   1.00 18.01 ? 482 HOH B O   1 
HETATM 4386 O  O   . HOH K 6 .   ? -14.149 -27.455 10.147  1.00 28.47 ? 483 HOH B O   1 
HETATM 4387 O  O   . HOH K 6 .   ? -24.598 -13.744 3.225   1.00 36.09 ? 484 HOH B O   1 
HETATM 4388 O  O   . HOH K 6 .   ? -9.588  15.626  3.211   1.00 33.30 ? 485 HOH B O   1 
HETATM 4389 O  O   . HOH K 6 .   ? -5.350  9.520   9.713   1.00 21.13 ? 486 HOH B O   1 
HETATM 4390 O  O   . HOH K 6 .   ? -13.250 -15.608 34.498  1.00 32.03 ? 487 HOH B O   1 
HETATM 4391 O  O   . HOH K 6 .   ? -28.552 -12.789 9.297   1.00 30.01 ? 488 HOH B O   1 
HETATM 4392 O  O   . HOH K 6 .   ? 8.530   0.364   12.917  1.00 31.04 ? 489 HOH B O   1 
HETATM 4393 O  O   . HOH K 6 .   ? -4.980  -12.348 -2.081  1.00 20.80 ? 490 HOH B O   1 
HETATM 4394 O  O   . HOH K 6 .   ? -14.710 -11.770 37.732  1.00 28.82 ? 491 HOH B O   1 
HETATM 4395 O  O   . HOH K 6 .   ? -7.909  -28.504 20.599  1.00 26.09 ? 492 HOH B O   1 
HETATM 4396 O  O   . HOH K 6 .   ? -10.240 -16.562 8.220   1.00 11.01 ? 493 HOH B O   1 
HETATM 4397 O  O   . HOH K 6 .   ? -23.911 -4.693  26.399  1.00 25.68 ? 494 HOH B O   1 
HETATM 4398 O  O   . HOH K 6 .   ? -23.457 6.231   2.593   1.00 30.95 ? 495 HOH B O   1 
HETATM 4399 O  O   . HOH K 6 .   ? -11.504 -21.679 10.183  1.00 14.98 ? 496 HOH B O   1 
HETATM 4400 O  O   . HOH K 6 .   ? 6.336   2.117   6.225   1.00 36.68 ? 497 HOH B O   1 
HETATM 4401 O  O   . HOH K 6 .   ? -5.851  -18.787 28.983  1.00 22.89 ? 498 HOH B O   1 
HETATM 4402 O  O   . HOH K 6 .   ? -0.741  -25.617 26.377  1.00 31.51 ? 499 HOH B O   1 
HETATM 4403 O  O   . HOH K 6 .   ? 0.147   -19.957 21.716  1.00 16.89 ? 500 HOH B O   1 
HETATM 4404 O  O   . HOH K 6 .   ? -16.929 -2.923  34.066  1.00 19.87 ? 501 HOH B O   1 
HETATM 4405 O  O   . HOH K 6 .   ? -26.386 -12.932 20.868  1.00 17.61 ? 502 HOH B O   1 
HETATM 4406 O  O   . HOH K 6 .   ? -27.359 -6.805  2.196   1.00 28.06 ? 503 HOH B O   1 
HETATM 4407 O  O   . HOH K 6 .   ? -10.070 -15.399 -4.571  1.00 34.55 ? 504 HOH B O   1 
HETATM 4408 O  O   . HOH K 6 .   ? -16.352 -18.980 4.039   1.00 24.73 ? 505 HOH B O   1 
HETATM 4409 O  O   . HOH K 6 .   ? 1.245   -10.455 24.115  1.00 14.83 ? 506 HOH B O   1 
HETATM 4410 O  O   . HOH K 6 .   ? -26.733 -3.126  9.139   1.00 46.23 ? 507 HOH B O   1 
HETATM 4411 O  O   . HOH K 6 .   ? -10.550 -21.808 26.796  1.00 18.81 ? 508 HOH B O   1 
HETATM 4412 O  O   . HOH K 6 .   ? -0.317  -0.780  4.151   1.00 17.84 ? 509 HOH B O   1 
HETATM 4413 O  O   . HOH K 6 .   ? -8.276  -25.674 28.355  1.00 39.42 ? 510 HOH B O   1 
HETATM 4414 O  O   . HOH K 6 .   ? -13.111 -18.688 28.122  1.00 16.08 ? 511 HOH B O   1 
HETATM 4415 O  O   . HOH K 6 .   ? 12.001  -14.190 15.174  1.00 30.30 ? 512 HOH B O   1 
HETATM 4416 O  O   . HOH K 6 .   ? 5.553   -22.313 4.077   1.00 20.67 ? 513 HOH B O   1 
HETATM 4417 O  O   . HOH K 6 .   ? -1.730  -4.805  -2.271  1.00 17.95 ? 514 HOH B O   1 
HETATM 4418 O  O   . HOH K 6 .   ? -12.652 2.727   -4.779  1.00 28.10 ? 515 HOH B O   1 
HETATM 4419 O  O   . HOH K 6 .   ? -5.708  0.401   10.756  1.00 16.62 ? 516 HOH B O   1 
HETATM 4420 O  O   . HOH K 6 .   ? -8.792  -13.526 -3.386  1.00 20.74 ? 517 HOH B O   1 
HETATM 4421 O  O   . HOH K 6 .   ? -18.588 -21.090 26.756  1.00 21.29 ? 518 HOH B O   1 
HETATM 4422 O  O   . HOH K 6 .   ? 7.807   -9.483  17.706  1.00 19.59 ? 519 HOH B O   1 
HETATM 4423 O  O   . HOH K 6 .   ? -4.012  5.989   8.290   1.00 21.98 ? 520 HOH B O   1 
HETATM 4424 O  O   . HOH K 6 .   ? 5.905   -1.805  11.893  1.00 20.31 ? 521 HOH B O   1 
HETATM 4425 O  O   . HOH K 6 .   ? 6.310   -16.138 12.326  1.00 29.51 ? 522 HOH B O   1 
HETATM 4426 O  O   . HOH K 6 .   ? -11.430 -25.567 16.607  1.00 18.28 ? 523 HOH B O   1 
HETATM 4427 O  O   . HOH K 6 .   ? -9.012  -14.163 32.638  1.00 19.44 ? 524 HOH B O   1 
HETATM 4428 O  O   . HOH K 6 .   ? -4.186  -20.663 26.336  1.00 20.36 ? 525 HOH B O   1 
HETATM 4429 O  O   . HOH K 6 .   ? -17.371 -16.904 -3.371  1.00 25.86 ? 526 HOH B O   1 
HETATM 4430 O  O   . HOH K 6 .   ? -19.656 -16.912 24.320  1.00 23.03 ? 527 HOH B O   1 
HETATM 4431 O  O   . HOH K 6 .   ? -15.626 -25.387 6.400   1.00 32.45 ? 528 HOH B O   1 
HETATM 4432 O  O   . HOH K 6 .   ? -23.298 -18.093 8.068   1.00 23.45 ? 529 HOH B O   1 
HETATM 4433 O  O   . HOH K 6 .   ? -15.596 -9.946  -7.416  1.00 22.19 ? 530 HOH B O   1 
HETATM 4434 O  O   . HOH K 6 .   ? -17.793 -23.741 18.238  1.00 15.24 ? 531 HOH B O   1 
HETATM 4435 O  O   . HOH K 6 .   ? 2.833   -9.179  26.826  1.00 23.52 ? 532 HOH B O   1 
HETATM 4436 O  O   . HOH K 6 .   ? -1.900  -14.148 24.682  1.00 15.73 ? 533 HOH B O   1 
HETATM 4437 O  O   . HOH K 6 .   ? -0.479  -12.011 25.575  1.00 16.18 ? 534 HOH B O   1 
HETATM 4438 O  O   . HOH K 6 .   ? -19.673 -13.956 0.018   1.00 28.12 ? 535 HOH B O   1 
HETATM 4439 O  O   . HOH K 6 .   ? -14.753 -0.293  28.261  1.00 22.18 ? 536 HOH B O   1 
HETATM 4440 O  O   . HOH K 6 .   ? -20.810 -19.271 7.438   1.00 23.89 ? 537 HOH B O   1 
HETATM 4441 O  O   . HOH K 6 .   ? -7.136  -15.579 28.588  1.00 16.75 ? 538 HOH B O   1 
HETATM 4442 O  O   . HOH K 6 .   ? -22.487 -19.601 18.551  1.00 14.86 ? 539 HOH B O   1 
HETATM 4443 O  O   . HOH K 6 .   ? -12.740 -19.675 31.735  1.00 31.46 ? 540 HOH B O   1 
HETATM 4444 O  O   . HOH K 6 .   ? 1.170   -21.704 0.556   1.00 24.77 ? 541 HOH B O   1 
HETATM 4445 O  O   . HOH K 6 .   ? 4.229   -18.261 22.966  1.00 22.31 ? 542 HOH B O   1 
HETATM 4446 O  O   . HOH K 6 .   ? -18.765 11.533  3.879   1.00 34.32 ? 543 HOH B O   1 
HETATM 4447 O  O   . HOH K 6 .   ? -22.063 -14.981 0.528   1.00 31.29 ? 544 HOH B O   1 
HETATM 4448 O  O   . HOH K 6 .   ? -26.312 -3.142  26.561  1.00 41.94 ? 545 HOH B O   1 
HETATM 4449 O  O   . HOH K 6 .   ? -26.737 2.072   8.795   1.00 42.46 ? 546 HOH B O   1 
HETATM 4450 O  O   . HOH K 6 .   ? -13.388 -23.423 17.190  1.00 14.81 ? 547 HOH B O   1 
HETATM 4451 O  O   . HOH K 6 .   ? -12.141 0.733   20.842  1.00 32.81 ? 548 HOH B O   1 
HETATM 4452 O  O   . HOH K 6 .   ? -15.782 -5.521  34.595  1.00 17.58 ? 549 HOH B O   1 
HETATM 4453 O  O   . HOH K 6 .   ? 5.320   -21.925 16.704  1.00 35.27 ? 550 HOH B O   1 
HETATM 4454 O  O   . HOH K 6 .   ? -2.175  -18.484 22.247  1.00 14.25 ? 551 HOH B O   1 
HETATM 4455 O  O   . HOH K 6 .   ? -3.007  6.512   2.818   1.00 36.19 ? 552 HOH B O   1 
HETATM 4456 O  O   . HOH K 6 .   ? -27.872 -1.403  23.523  1.00 34.57 ? 553 HOH B O   1 
HETATM 4457 O  O   . HOH K 6 .   ? -25.111 -14.883 19.230  1.00 16.45 ? 554 HOH B O   1 
HETATM 4458 O  O   . HOH K 6 .   ? -15.500 -19.722 0.433   1.00 38.99 ? 555 HOH B O   1 
HETATM 4459 O  O   . HOH K 6 .   ? -8.280  -27.905 8.340   1.00 27.94 ? 556 HOH B O   1 
HETATM 4460 O  O   . HOH K 6 .   ? -12.061 -22.135 31.662  1.00 35.26 ? 557 HOH B O   1 
HETATM 4461 O  O   . HOH K 6 .   ? -5.457  -15.934 26.532  1.00 17.99 ? 558 HOH B O   1 
HETATM 4462 O  O   . HOH K 6 .   ? -20.174 -20.791 11.061  1.00 16.44 ? 559 HOH B O   1 
HETATM 4463 O  O   . HOH K 6 .   ? -23.131 -12.662 4.431   1.00 30.79 ? 560 HOH B O   1 
HETATM 4464 O  O   . HOH K 6 .   ? -1.749  -31.629 22.171  1.00 32.46 ? 561 HOH B O   1 
HETATM 4465 O  O   . HOH K 6 .   ? -23.884 -6.422  16.276  1.00 20.01 ? 562 HOH B O   1 
HETATM 4466 O  O   . HOH K 6 .   ? -28.204 0.585   10.692  1.00 30.63 ? 563 HOH B O   1 
HETATM 4467 O  O   . HOH K 6 .   ? -2.400  6.747   6.249   1.00 27.10 ? 564 HOH B O   1 
HETATM 4468 O  O   . HOH K 6 .   ? -1.627  9.592   7.280   1.00 33.60 ? 565 HOH B O   1 
HETATM 4469 O  O   . HOH K 6 .   ? -19.943 12.574  11.596  1.00 30.91 ? 566 HOH B O   1 
HETATM 4470 O  O   . HOH K 6 .   ? -26.511 4.418   17.357  1.00 24.92 ? 567 HOH B O   1 
HETATM 4471 O  O   . HOH K 6 .   ? 4.093   -19.700 12.285  1.00 24.68 ? 568 HOH B O   1 
HETATM 4472 O  O   . HOH K 6 .   ? 3.473   -5.594  3.954   1.00 26.92 ? 569 HOH B O   1 
HETATM 4473 O  O   . HOH K 6 .   ? 6.161   2.038   22.474  1.00 23.41 ? 570 HOH B O   1 
HETATM 4474 O  O   . HOH K 6 .   ? -10.568 -27.066 18.869  1.00 25.04 ? 571 HOH B O   1 
HETATM 4475 O  O   . HOH K 6 .   ? -6.960  -20.512 1.703   1.00 42.96 ? 572 HOH B O   1 
HETATM 4476 O  O   . HOH K 6 .   ? 1.317   -31.388 18.893  1.00 39.51 ? 573 HOH B O   1 
HETATM 4477 O  O   . HOH K 6 .   ? 7.796   -18.242 23.980  1.00 32.73 ? 574 HOH B O   1 
HETATM 4478 O  O   . HOH K 6 .   ? 2.337   -12.695 0.787   1.00 27.43 ? 575 HOH B O   1 
HETATM 4479 O  O   . HOH K 6 .   ? 2.886   -3.416  25.657  1.00 20.49 ? 576 HOH B O   1 
HETATM 4480 O  O   . HOH K 6 .   ? -23.819 -19.029 -3.290  1.00 36.03 ? 577 HOH B O   1 
HETATM 4481 O  O   . HOH K 6 .   ? -18.415 -2.129  31.666  1.00 26.00 ? 578 HOH B O   1 
HETATM 4482 O  O   . HOH K 6 .   ? 9.910   -14.948 12.565  1.00 27.17 ? 579 HOH B O   1 
HETATM 4483 O  O   . HOH K 6 .   ? -9.182  -0.022  15.006  1.00 29.24 ? 580 HOH B O   1 
HETATM 4484 O  O   . HOH K 6 .   ? -0.603  -13.848 -1.648  1.00 26.33 ? 581 HOH B O   1 
HETATM 4485 O  O   . HOH K 6 .   ? -2.605  -28.008 12.333  1.00 26.52 ? 582 HOH B O   1 
HETATM 4486 O  O   . HOH K 6 .   ? -14.888 -25.408 13.856  1.00 22.50 ? 583 HOH B O   1 
HETATM 4487 O  O   . HOH K 6 .   ? -2.415  7.768   0.110   1.00 40.04 ? 584 HOH B O   1 
HETATM 4488 O  O   . HOH K 6 .   ? -17.041 -24.627 4.217   1.00 28.69 ? 585 HOH B O   1 
HETATM 4489 O  O   . HOH K 6 .   ? -21.835 -15.360 5.592   1.00 33.84 ? 586 HOH B O   1 
HETATM 4490 O  O   . HOH K 6 .   ? -13.691 -20.436 2.307   1.00 25.67 ? 587 HOH B O   1 
HETATM 4491 O  O   . HOH K 6 .   ? 0.453   -5.863  28.254  1.00 24.59 ? 588 HOH B O   1 
HETATM 4492 O  O   . HOH K 6 .   ? 1.672   -30.526 16.225  1.00 34.82 ? 589 HOH B O   1 
HETATM 4493 O  O   . HOH K 6 .   ? -2.026  -25.824 10.809  1.00 21.89 ? 590 HOH B O   1 
HETATM 4494 O  O   . HOH K 6 .   ? 11.976  0.783   18.743  1.00 41.31 ? 591 HOH B O   1 
HETATM 4495 O  O   . HOH K 6 .   ? 1.249   -26.562 23.096  1.00 32.99 ? 592 HOH B O   1 
HETATM 4496 O  O   . HOH K 6 .   ? -13.616 -4.579  -9.568  1.00 33.35 ? 593 HOH B O   1 
HETATM 4497 O  O   . HOH K 6 .   ? -9.677  -20.659 0.271   1.00 37.29 ? 594 HOH B O   1 
HETATM 4498 O  O   . HOH K 6 .   ? 0.260   3.284   26.550  1.00 46.97 ? 595 HOH B O   1 
HETATM 4499 O  O   . HOH K 6 .   ? 4.899   -5.117  26.494  1.00 24.27 ? 596 HOH B O   1 
HETATM 4500 O  O   . HOH K 6 .   ? -3.563  -25.888 8.078   1.00 21.95 ? 597 HOH B O   1 
HETATM 4501 O  O   . HOH K 6 .   ? -8.737  -31.701 14.333  1.00 30.07 ? 598 HOH B O   1 
HETATM 4502 O  O   . HOH K 6 .   ? -12.547 1.909   28.014  1.00 28.34 ? 599 HOH B O   1 
HETATM 4503 O  O   . HOH K 6 .   ? -10.836 -11.345 38.533  1.00 38.02 ? 600 HOH B O   1 
HETATM 4504 O  O   . HOH K 6 .   ? -23.932 8.656   15.134  1.00 30.48 ? 601 HOH B O   1 
HETATM 4505 O  O   . HOH K 6 .   ? -4.438  -10.885 -8.213  1.00 36.75 ? 602 HOH B O   1 
HETATM 4506 O  O   . HOH K 6 .   ? -3.692  11.972  -2.701  1.00 33.49 ? 603 HOH B O   1 
HETATM 4507 O  O   . HOH K 6 .   ? 7.609   -3.393  10.077  1.00 25.81 ? 604 HOH B O   1 
HETATM 4508 O  O   . HOH K 6 .   ? 2.783   -3.056  -5.721  1.00 45.81 ? 605 HOH B O   1 
HETATM 4509 O  O   . HOH K 6 .   ? -26.433 8.878   12.042  1.00 28.91 ? 606 HOH B O   1 
HETATM 4510 O  O   . HOH K 6 .   ? -26.622 -14.381 17.041  1.00 16.35 ? 607 HOH B O   1 
HETATM 4511 O  O   . HOH K 6 .   ? -4.168  -37.496 17.246  1.00 43.73 ? 608 HOH B O   1 
HETATM 4512 O  O   . HOH K 6 .   ? -9.306  -21.611 30.988  1.00 40.32 ? 609 HOH B O   1 
HETATM 4513 O  O   . HOH K 6 .   ? -7.238  -13.680 -1.268  1.00 21.72 ? 610 HOH B O   1 
HETATM 4514 O  O   . HOH K 6 .   ? -14.396 -21.692 27.999  1.00 25.71 ? 611 HOH B O   1 
HETATM 4515 O  O   . HOH K 6 .   ? 1.910   -13.102 26.838  1.00 35.06 ? 612 HOH B O   1 
HETATM 4516 O  O   . HOH K 6 .   ? -10.707 -24.147 8.616   1.00 20.99 ? 613 HOH B O   1 
HETATM 4517 O  O   . HOH K 6 .   ? -0.193  3.697   1.219   1.00 28.48 ? 614 HOH B O   1 
HETATM 4518 O  O   . HOH K 6 .   ? 1.924   -7.756  -7.016  1.00 36.82 ? 615 HOH B O   1 
HETATM 4519 O  O   . HOH K 6 .   ? -4.382  2.408   32.222  1.00 54.42 ? 616 HOH B O   1 
HETATM 4520 O  O   . HOH K 6 .   ? -2.701  9.431   13.707  1.00 34.99 ? 617 HOH B O   1 
HETATM 4521 O  O   . HOH K 6 .   ? -13.317 8.643   14.271  1.00 44.30 ? 618 HOH B O   1 
HETATM 4522 O  O   . HOH K 6 .   ? -12.600 -23.764 32.699  1.00 36.48 ? 619 HOH B O   1 
HETATM 4523 O  O   . HOH K 6 .   ? -5.159  -31.791 27.014  1.00 36.43 ? 620 HOH B O   1 
HETATM 4524 O  O   . HOH K 6 .   ? -19.762 5.276   -4.505  1.00 44.74 ? 621 HOH B O   1 
HETATM 4525 O  O   . HOH K 6 .   ? -7.152  -16.504 -1.284  1.00 33.17 ? 622 HOH B O   1 
HETATM 4526 O  O   . HOH K 6 .   ? -30.765 -2.476  21.734  1.00 39.65 ? 623 HOH B O   1 
HETATM 4527 O  O   . HOH K 6 .   ? -3.671  -17.937 26.049  1.00 20.48 ? 624 HOH B O   1 
HETATM 4528 O  O   . HOH K 6 .   ? 7.331   -24.285 7.447   1.00 20.90 ? 625 HOH B O   1 
HETATM 4529 O  O   . HOH K 6 .   ? -29.733 -1.108  25.457  1.00 37.85 ? 626 HOH B O   1 
HETATM 4530 O  O   . HOH K 6 .   ? -1.143  12.890  -1.556  1.00 36.95 ? 627 HOH B O   1 
HETATM 4531 O  O   . HOH K 6 .   ? -19.466 -18.299 -1.761  1.00 37.85 ? 628 HOH B O   1 
HETATM 4532 O  O   . HOH K 6 .   ? -31.090 -4.024  15.268  1.00 41.60 ? 629 HOH B O   1 
HETATM 4533 O  O   . HOH K 6 .   ? -0.168  -6.068  -4.023  1.00 32.56 ? 630 HOH B O   1 
HETATM 4534 O  O   . HOH K 6 .   ? 8.689   10.848  3.649   1.00 52.02 ? 631 HOH B O   1 
HETATM 4535 O  O   . HOH K 6 .   ? -15.470 -24.410 1.450   1.00 41.33 ? 632 HOH B O   1 
HETATM 4536 O  O   . HOH K 6 .   ? -0.211  -28.721 8.459   1.00 39.88 ? 633 HOH B O   1 
HETATM 4537 O  O   . HOH K 6 .   ? -22.667 -13.834 28.995  1.00 40.80 ? 634 HOH B O   1 
HETATM 4538 O  O   . HOH K 6 .   ? -26.835 -3.424  22.765  1.00 31.34 ? 635 HOH B O   1 
HETATM 4539 O  O   . HOH K 6 .   ? 0.784   -3.327  27.416  1.00 24.43 ? 636 HOH B O   1 
HETATM 4540 O  O   . HOH K 6 .   ? -25.465 5.403   6.025   1.00 45.39 ? 637 HOH B O   1 
HETATM 4541 O  O   . HOH K 6 .   ? -12.824 -18.272 34.216  1.00 29.59 ? 638 HOH B O   1 
HETATM 4542 O  O   . HOH K 6 .   ? -12.736 -27.511 7.912   1.00 32.52 ? 639 HOH B O   1 
HETATM 4543 O  O   . HOH K 6 .   ? -16.412 -17.230 30.981  1.00 36.51 ? 640 HOH B O   1 
HETATM 4544 O  O   . HOH K 6 .   ? -17.366 -0.549  29.967  1.00 41.39 ? 641 HOH B O   1 
HETATM 4545 O  O   . HOH K 6 .   ? -7.612  -22.484 3.880   1.00 36.47 ? 642 HOH B O   1 
HETATM 4546 O  O   . HOH K 6 .   ? -9.002  2.612   17.112  1.00 50.20 ? 643 HOH B O   1 
HETATM 4547 O  O   . HOH K 6 .   ? 2.226   -7.967  4.225   1.00 20.28 ? 644 HOH B O   1 
HETATM 4548 O  O   . HOH K 6 .   ? 10.036  -10.971 10.085  1.00 40.88 ? 645 HOH B O   1 
HETATM 4549 O  O   . HOH K 6 .   ? -28.766 -12.062 19.776  1.00 17.41 ? 646 HOH B O   1 
HETATM 4550 O  O   . HOH K 6 .   ? 13.060  -18.392 17.006  1.00 25.71 ? 647 HOH B O   1 
HETATM 4551 O  O   . HOH K 6 .   ? 1.937   -19.479 23.809  1.00 20.01 ? 648 HOH B O   1 
HETATM 4552 O  O   . HOH K 6 .   ? 5.635   -21.199 14.106  1.00 39.30 ? 649 HOH B O   1 
HETATM 4553 O  O   . HOH K 6 .   ? -32.652 -4.324  19.647  1.00 47.46 ? 650 HOH B O   1 
HETATM 4554 O  O   . HOH K 6 .   ? -8.854  -23.090 28.702  1.00 34.95 ? 651 HOH B O   1 
HETATM 4555 O  O   . HOH K 6 .   ? -3.294  -29.733 10.004  1.00 36.68 ? 652 HOH B O   1 
HETATM 4556 O  O   . HOH K 6 .   ? -20.622 -2.756  -4.080  1.00 32.59 ? 653 HOH B O   1 
HETATM 4557 O  O   . HOH K 6 .   ? 1.205   -1.036  28.859  1.00 31.59 ? 654 HOH B O   1 
HETATM 4558 O  O   . HOH K 6 .   ? -3.312  -24.201 5.751   1.00 31.03 ? 655 HOH B O   1 
HETATM 4559 O  O   . HOH K 6 .   ? -18.833 -13.239 -8.290  1.00 33.20 ? 656 HOH B O   1 
HETATM 4560 O  O   . HOH K 6 .   ? -1.601  -16.803 24.433  1.00 17.78 ? 657 HOH B O   1 
HETATM 4561 O  O   . HOH K 6 .   ? -1.882  -21.218 27.778  1.00 32.22 ? 658 HOH B O   1 
HETATM 4562 O  O   . HOH K 6 .   ? -27.076 -2.545  28.831  1.00 29.94 ? 659 HOH B O   1 
HETATM 4563 O  O   . HOH K 6 .   ? -5.236  -15.865 30.616  1.00 24.37 ? 660 HOH B O   1 
HETATM 4564 O  O   . HOH K 6 .   ? -11.802 -22.042 2.077   1.00 36.95 ? 661 HOH B O   1 
HETATM 4565 O  O   . HOH K 6 .   ? -5.015  -22.378 4.957   1.00 27.69 ? 662 HOH B O   1 
HETATM 4566 O  O   . HOH K 6 .   ? -33.195 8.107   13.187  1.00 37.19 ? 663 HOH B O   1 
HETATM 4567 O  O   . HOH K 6 .   ? -34.206 3.206   17.198  1.00 35.31 ? 664 HOH B O   1 
HETATM 4568 O  O   . HOH K 6 .   ? -11.792 -29.244 20.279  1.00 24.00 ? 665 HOH B O   1 
HETATM 4569 O  O   . HOH K 6 .   ? -0.652  -29.296 13.149  1.00 32.29 ? 666 HOH B O   1 
HETATM 4570 O  O   . HOH K 6 .   ? -2.817  -14.529 28.819  1.00 41.51 ? 667 HOH B O   1 
HETATM 4571 O  O   . HOH K 6 .   ? -10.207 -22.886 4.108   1.00 28.51 ? 668 HOH B O   1 
HETATM 4572 O  O   . HOH K 6 .   ? -7.725  -12.221 -5.694  1.00 27.41 ? 669 HOH B O   1 
HETATM 4573 O  O   . HOH K 6 .   ? -10.722 12.520  14.129  1.00 37.86 ? 670 HOH B O   1 
HETATM 4574 O  O   . HOH K 6 .   ? -13.559 8.284   -4.189  1.00 36.17 ? 671 HOH B O   1 
HETATM 4575 O  O   . HOH K 6 .   ? -17.873 -20.586 29.282  1.00 35.81 ? 672 HOH B O   1 
HETATM 4576 O  O   . HOH K 6 .   ? 15.134  2.451   16.979  1.00 38.98 ? 673 HOH B O   1 
HETATM 4577 O  O   . HOH K 6 .   ? -27.440 0.441   28.644  1.00 25.84 ? 674 HOH B O   1 
HETATM 4578 O  O   . HOH K 6 .   ? -10.541 -14.787 34.910  1.00 27.30 ? 675 HOH B O   1 
HETATM 4579 O  O   . HOH K 6 .   ? -10.746 -24.587 5.931   1.00 29.76 ? 676 HOH B O   1 
HETATM 4580 O  O   . HOH K 6 .   ? 4.455   -0.695  4.926   1.00 41.51 ? 677 HOH B O   1 
HETATM 4581 O  O   . HOH K 6 .   ? 6.208   -5.797  3.698   1.00 33.54 ? 678 HOH B O   1 
HETATM 4582 O  O   . HOH K 6 .   ? -18.396 -17.549 4.409   1.00 34.11 ? 679 HOH B O   1 
HETATM 4583 O  O   . HOH K 6 .   ? -7.054  0.703   13.366  1.00 29.13 ? 680 HOH B O   1 
HETATM 4584 O  O   . HOH K 6 .   ? -5.537  -18.550 -1.255  1.00 34.32 ? 681 HOH B O   1 
HETATM 4585 O  O   . HOH K 6 .   ? -6.525  2.723   15.061  1.00 40.82 ? 682 HOH B O   1 
HETATM 4586 O  O   . HOH K 6 .   ? -20.812 -18.831 4.658   1.00 34.47 ? 683 HOH B O   1 
HETATM 4587 O  O   . HOH K 6 .   ? 8.719   -4.607  7.634   1.00 35.51 ? 684 HOH B O   1 
HETATM 4588 O  O   . HOH K 6 .   ? 2.074   -15.836 26.860  1.00 24.36 ? 685 HOH B O   1 
HETATM 4589 O  O   . HOH K 6 .   ? 0.590   -17.871 25.609  1.00 20.94 ? 686 HOH B O   1 
HETATM 4590 O  O   . HOH K 6 .   ? 2.679   0.659   27.503  1.00 41.19 ? 687 HOH B O   1 
HETATM 4591 O  O   . HOH K 6 .   ? 5.402   8.577   -3.460  1.00 37.89 ? 688 HOH B O   1 
HETATM 4592 O  O   . HOH K 6 .   ? 7.202   -3.640  27.590  1.00 38.44 ? 689 HOH B O   1 
HETATM 4593 O  O   . HOH K 6 .   ? 4.126   -0.884  25.529  1.00 31.92 ? 690 HOH B O   1 
HETATM 4594 O  O   . HOH L 6 .   ? -43.107 -24.203 39.022  1.00 32.27 ? 401 HOH A O   1 
HETATM 4595 O  O   . HOH L 6 .   ? -20.913 -32.928 41.333  1.00 36.29 ? 402 HOH A O   1 
HETATM 4596 O  O   . HOH L 6 .   ? -31.236 -11.735 20.857  1.00 32.39 ? 403 HOH A O   1 
HETATM 4597 O  O   . HOH L 6 .   ? -32.147 -53.431 25.933  1.00 33.68 ? 404 HOH A O   1 
HETATM 4598 O  O   . HOH L 6 .   ? -35.528 -16.889 13.395  1.00 37.02 ? 405 HOH A O   1 
HETATM 4599 O  O   . HOH L 6 .   ? -37.765 -52.061 28.592  1.00 40.05 ? 406 HOH A O   1 
HETATM 4600 O  O   . HOH L 6 .   ? -18.572 -20.316 44.447  1.00 39.87 ? 407 HOH A O   1 
HETATM 4601 O  O   . HOH L 6 .   ? -18.674 -20.694 47.174  1.00 37.42 ? 408 HOH A O   1 
HETATM 4602 O  O   . HOH L 6 .   ? -42.801 -55.242 23.957  1.00 30.22 ? 409 HOH A O   1 
HETATM 4603 O  O   . HOH L 6 .   ? -13.135 -43.614 14.967  1.00 42.40 ? 410 HOH A O   1 
HETATM 4604 O  O   . HOH L 6 .   ? -26.445 -24.612 46.412  1.00 21.70 ? 411 HOH A O   1 
HETATM 4605 O  O   . HOH L 6 .   ? -15.606 -40.917 36.225  1.00 28.64 ? 412 HOH A O   1 
HETATM 4606 O  O   . HOH L 6 .   ? -41.037 -32.898 26.719  1.00 26.00 ? 413 HOH A O   1 
HETATM 4607 O  O   . HOH L 6 .   ? -30.074 -13.596 13.376  1.00 29.02 ? 414 HOH A O   1 
HETATM 4608 O  O   . HOH L 6 .   ? -32.936 -19.918 13.445  1.00 26.25 ? 415 HOH A O   1 
HETATM 4609 O  O   . HOH L 6 .   ? -29.219 -12.971 17.079  1.00 24.35 ? 416 HOH A O   1 
HETATM 4610 O  O   . HOH L 6 .   ? -37.232 -17.706 38.304  1.00 24.14 ? 417 HOH A O   1 
HETATM 4611 O  O   . HOH L 6 .   ? -17.750 -23.563 13.108  1.00 21.47 ? 418 HOH A O   1 
HETATM 4612 O  O   . HOH L 6 .   ? -41.566 -26.908 43.773  1.00 30.81 ? 419 HOH A O   1 
HETATM 4613 O  O   . HOH L 6 .   ? -14.316 -49.278 24.214  1.00 39.48 ? 420 HOH A O   1 
HETATM 4614 O  O   . HOH L 6 .   ? -14.250 -33.218 19.147  1.00 20.40 ? 421 HOH A O   1 
HETATM 4615 O  O   . HOH L 6 .   ? -14.128 -46.838 23.291  1.00 35.69 ? 422 HOH A O   1 
HETATM 4616 O  O   . HOH L 6 .   ? -26.076 -50.222 32.533  1.00 19.98 ? 423 HOH A O   1 
HETATM 4617 O  O   . HOH L 6 .   ? -31.637 -11.343 37.138  1.00 27.99 ? 424 HOH A O   1 
HETATM 4618 O  O   . HOH L 6 .   ? -36.913 -40.084 29.830  1.00 11.50 ? 425 HOH A O   1 
HETATM 4619 O  O   . HOH L 6 .   ? -42.397 -25.393 23.153  1.00 17.72 ? 426 HOH A O   1 
HETATM 4620 O  O   . HOH L 6 .   ? -16.348 -34.019 35.622  1.00 37.24 ? 427 HOH A O   1 
HETATM 4621 O  O   . HOH L 6 .   ? -36.455 -43.590 36.506  1.00 30.87 ? 428 HOH A O   1 
HETATM 4622 O  O   . HOH L 6 .   ? -19.794 -21.165 19.899  1.00 14.50 ? 429 HOH A O   1 
HETATM 4623 O  O   . HOH L 6 .   ? -34.574 -29.639 44.858  1.00 17.49 ? 430 HOH A O   1 
HETATM 4624 O  O   . HOH L 6 .   ? -23.134 -29.220 5.663   1.00 25.17 ? 431 HOH A O   1 
HETATM 4625 O  O   . HOH L 6 .   ? -25.977 -52.816 20.206  1.00 24.07 ? 432 HOH A O   1 
HETATM 4626 O  O   . HOH L 6 .   ? -42.416 -16.817 19.359  1.00 22.54 ? 433 HOH A O   1 
HETATM 4627 O  O   . HOH L 6 .   ? -25.951 -27.504 4.358   1.00 34.42 ? 434 HOH A O   1 
HETATM 4628 O  O   . HOH L 6 .   ? -53.889 -27.306 29.979  1.00 27.80 ? 435 HOH A O   1 
HETATM 4629 O  O   . HOH L 6 .   ? -24.785 -39.149 7.481   1.00 23.61 ? 436 HOH A O   1 
HETATM 4630 O  O   . HOH L 6 .   ? -31.558 -37.118 48.628  1.00 28.96 ? 437 HOH A O   1 
HETATM 4631 O  O   . HOH L 6 .   ? -29.708 -31.342 47.936  1.00 32.21 ? 438 HOH A O   1 
HETATM 4632 O  O   . HOH L 6 .   ? -40.306 -47.022 18.243  1.00 26.53 ? 439 HOH A O   1 
HETATM 4633 O  O   . HOH L 6 .   ? -24.961 -42.472 16.017  1.00 21.96 ? 440 HOH A O   1 
HETATM 4634 O  O   . HOH L 6 .   ? -32.947 -55.705 27.002  1.00 36.08 ? 441 HOH A O   1 
HETATM 4635 O  O   . HOH L 6 .   ? -36.911 -13.763 32.524  1.00 28.53 ? 442 HOH A O   1 
HETATM 4636 O  O   . HOH L 6 .   ? -12.633 -32.307 23.604  1.00 24.02 ? 443 HOH A O   1 
HETATM 4637 O  O   . HOH L 6 .   ? -23.841 -32.734 4.475   1.00 22.14 ? 444 HOH A O   1 
HETATM 4638 O  O   . HOH L 6 .   ? -24.451 -17.409 20.652  1.00 15.31 ? 445 HOH A O   1 
HETATM 4639 O  O   . HOH L 6 .   ? -20.730 -22.514 27.021  1.00 26.61 ? 446 HOH A O   1 
HETATM 4640 O  O   . HOH L 6 .   ? -45.839 -37.460 37.401  1.00 35.92 ? 447 HOH A O   1 
HETATM 4641 O  O   . HOH L 6 .   ? -27.478 -39.785 14.465  1.00 15.04 ? 448 HOH A O   1 
HETATM 4642 O  O   . HOH L 6 .   ? -43.176 -37.946 37.922  1.00 19.97 ? 449 HOH A O   1 
HETATM 4643 O  O   . HOH L 6 .   ? -27.050 -46.832 14.703  1.00 28.36 ? 450 HOH A O   1 
HETATM 4644 O  O   . HOH L 6 .   ? -27.268 -40.843 44.163  1.00 37.53 ? 451 HOH A O   1 
HETATM 4645 O  O   . HOH L 6 .   ? -30.206 -14.386 36.269  1.00 33.68 ? 452 HOH A O   1 
HETATM 4646 O  O   . HOH L 6 .   ? -37.108 -33.265 46.409  1.00 28.14 ? 453 HOH A O   1 
HETATM 4647 O  O   . HOH L 6 .   ? -24.055 -19.715 34.769  1.00 38.91 ? 454 HOH A O   1 
HETATM 4648 O  O   . HOH L 6 .   ? -33.707 -30.381 5.004   1.00 15.11 ? 455 HOH A O   1 
HETATM 4649 O  O   . HOH L 6 .   ? -25.408 -49.036 30.165  1.00 17.79 ? 456 HOH A O   1 
HETATM 4650 O  O   . HOH L 6 .   ? -14.349 -46.791 34.846  1.00 22.05 ? 457 HOH A O   1 
HETATM 4651 O  O   . HOH L 6 .   ? -28.711 -45.514 17.162  1.00 18.03 ? 458 HOH A O   1 
HETATM 4652 O  O   . HOH L 6 .   ? -33.248 -51.574 26.945  1.00 26.31 ? 459 HOH A O   1 
HETATM 4653 O  O   . HOH L 6 .   ? -21.992 -25.111 14.034  1.00 18.51 ? 460 HOH A O   1 
HETATM 4654 O  O   . HOH L 6 .   ? -48.448 -26.164 23.799  1.00 28.52 ? 461 HOH A O   1 
HETATM 4655 O  O   . HOH L 6 .   ? -34.369 -38.925 42.715  1.00 23.40 ? 462 HOH A O   1 
HETATM 4656 O  O   . HOH L 6 .   ? -34.081 -49.592 15.638  1.00 18.52 ? 463 HOH A O   1 
HETATM 4657 O  O   . HOH L 6 .   ? -37.187 -18.317 7.530   1.00 22.93 ? 464 HOH A O   1 
HETATM 4658 O  O   . HOH L 6 .   ? -22.312 -32.152 31.282  1.00 11.93 ? 465 HOH A O   1 
HETATM 4659 O  O   . HOH L 6 .   ? -33.342 -34.402 40.817  1.00 14.37 ? 466 HOH A O   1 
HETATM 4660 O  O   . HOH L 6 .   ? -16.203 -22.633 26.336  1.00 16.70 ? 467 HOH A O   1 
HETATM 4661 O  O   . HOH L 6 .   ? -25.799 -43.221 40.823  1.00 24.89 ? 468 HOH A O   1 
HETATM 4662 O  O   . HOH L 6 .   ? -38.460 -15.586 31.145  1.00 22.87 ? 469 HOH A O   1 
HETATM 4663 O  O   . HOH L 6 .   ? -41.930 -38.075 22.407  1.00 29.82 ? 470 HOH A O   1 
HETATM 4664 O  O   . HOH L 6 .   ? -19.389 -33.266 7.534   1.00 29.60 ? 471 HOH A O   1 
HETATM 4665 O  O   . HOH L 6 .   ? -23.572 -37.872 11.454  1.00 16.39 ? 472 HOH A O   1 
HETATM 4666 O  O   . HOH L 6 .   ? -34.247 -12.925 27.076  1.00 40.41 ? 473 HOH A O   1 
HETATM 4667 O  O   . HOH L 6 .   ? -24.893 -25.158 8.523   1.00 22.01 ? 474 HOH A O   1 
HETATM 4668 O  O   . HOH L 6 .   ? -48.573 -54.770 24.897  1.00 31.94 ? 475 HOH A O   1 
HETATM 4669 O  O   . HOH L 6 .   ? -44.448 -17.573 34.651  1.00 26.77 ? 476 HOH A O   1 
HETATM 4670 O  O   . HOH L 6 .   ? -38.543 -40.859 36.593  1.00 14.01 ? 477 HOH A O   1 
HETATM 4671 O  O   . HOH L 6 .   ? -19.065 -52.119 19.132  1.00 27.88 ? 478 HOH A O   1 
HETATM 4672 O  O   . HOH L 6 .   ? -31.621 -22.374 13.121  1.00 15.35 ? 479 HOH A O   1 
HETATM 4673 O  O   . HOH L 6 .   ? -20.353 -39.156 11.042  1.00 26.86 ? 480 HOH A O   1 
HETATM 4674 O  O   . HOH L 6 .   ? -27.351 -44.009 15.430  1.00 21.12 ? 481 HOH A O   1 
HETATM 4675 O  O   . HOH L 6 .   ? -31.708 -37.998 1.807   1.00 19.94 ? 482 HOH A O   1 
HETATM 4676 O  O   . HOH L 6 .   ? -54.162 -30.478 36.160  1.00 25.13 ? 483 HOH A O   1 
HETATM 4677 O  O   . HOH L 6 .   ? -29.184 -18.518 29.533  1.00 28.85 ? 484 HOH A O   1 
HETATM 4678 O  O   . HOH L 6 .   ? -16.338 -55.116 31.682  1.00 31.50 ? 485 HOH A O   1 
HETATM 4679 O  O   . HOH L 6 .   ? -17.184 -34.073 12.254  1.00 22.76 ? 486 HOH A O   1 
HETATM 4680 O  O   . HOH L 6 .   ? -23.195 -31.500 44.077  1.00 38.76 ? 487 HOH A O   1 
HETATM 4681 O  O   . HOH L 6 .   ? -21.919 -19.347 30.748  1.00 29.52 ? 488 HOH A O   1 
HETATM 4682 O  O   . HOH L 6 .   ? -29.686 -58.535 18.256  1.00 27.51 ? 489 HOH A O   1 
HETATM 4683 O  O   . HOH L 6 .   ? -18.398 -27.895 36.661  1.00 23.85 ? 490 HOH A O   1 
HETATM 4684 O  O   . HOH L 6 .   ? -26.626 -15.258 14.272  1.00 17.53 ? 491 HOH A O   1 
HETATM 4685 O  O   . HOH L 6 .   ? -26.313 -17.873 22.874  1.00 27.37 ? 492 HOH A O   1 
HETATM 4686 O  O   . HOH L 6 .   ? -33.635 -19.318 38.541  1.00 19.56 ? 493 HOH A O   1 
HETATM 4687 O  O   . HOH L 6 .   ? -10.445 -35.980 18.518  1.00 28.63 ? 494 HOH A O   1 
HETATM 4688 O  O   . HOH L 6 .   ? -39.944 -50.758 29.288  1.00 24.82 ? 495 HOH A O   1 
HETATM 4689 O  O   . HOH L 6 .   ? -28.832 -50.798 32.402  1.00 20.08 ? 496 HOH A O   1 
HETATM 4690 O  O   . HOH L 6 .   ? -32.825 -19.677 31.033  1.00 23.29 ? 497 HOH A O   1 
HETATM 4691 O  O   . HOH L 6 .   ? -17.082 -31.213 29.316  1.00 15.10 ? 498 HOH A O   1 
HETATM 4692 O  O   . HOH L 6 .   ? -11.027 -29.310 25.728  1.00 42.65 ? 499 HOH A O   1 
HETATM 4693 O  O   . HOH L 6 .   ? -38.378 -19.132 43.624  1.00 27.28 ? 500 HOH A O   1 
HETATM 4694 O  O   . HOH L 6 .   ? -46.424 -26.226 43.421  1.00 32.34 ? 501 HOH A O   1 
HETATM 4695 O  O   . HOH L 6 .   ? -28.392 -27.738 9.981   1.00 12.16 ? 502 HOH A O   1 
HETATM 4696 O  O   . HOH L 6 .   ? -27.504 -31.303 1.675   1.00 31.87 ? 503 HOH A O   1 
HETATM 4697 O  O   . HOH L 6 .   ? -40.515 -42.636 36.980  1.00 34.37 ? 504 HOH A O   1 
HETATM 4698 O  O   . HOH L 6 .   ? -31.810 -42.307 35.068  1.00 16.18 ? 505 HOH A O   1 
HETATM 4699 O  O   . HOH L 6 .   ? -29.938 -47.340 14.700  1.00 19.88 ? 506 HOH A O   1 
HETATM 4700 O  O   . HOH L 6 .   ? -37.521 -28.429 6.172   1.00 16.92 ? 507 HOH A O   1 
HETATM 4701 O  O   . HOH L 6 .   ? -7.166  -44.272 21.675  1.00 38.75 ? 508 HOH A O   1 
HETATM 4702 O  O   . HOH L 6 .   ? -24.981 -22.321 9.185   1.00 22.71 ? 509 HOH A O   1 
HETATM 4703 O  O   . HOH L 6 .   ? -36.640 -13.297 18.026  1.00 34.66 ? 510 HOH A O   1 
HETATM 4704 O  O   . HOH L 6 .   ? -20.259 -31.984 10.934  1.00 15.10 ? 511 HOH A O   1 
HETATM 4705 O  O   . HOH L 6 .   ? -15.408 -52.992 35.739  1.00 36.34 ? 512 HOH A O   1 
HETATM 4706 O  O   . HOH L 6 .   ? -45.035 -37.425 32.082  1.00 20.57 ? 513 HOH A O   1 
HETATM 4707 O  O   . HOH L 6 .   ? -19.047 -36.448 34.241  1.00 22.77 ? 514 HOH A O   1 
HETATM 4708 O  O   . HOH L 6 .   ? -33.686 -40.156 47.037  1.00 21.48 ? 515 HOH A O   1 
HETATM 4709 O  O   . HOH L 6 .   ? -16.563 -30.025 37.379  1.00 31.13 ? 516 HOH A O   1 
HETATM 4710 O  O   . HOH L 6 .   ? -29.869 -40.693 38.045  1.00 20.47 ? 517 HOH A O   1 
HETATM 4711 O  O   . HOH L 6 .   ? -48.016 -39.514 27.091  1.00 35.24 ? 518 HOH A O   1 
HETATM 4712 O  O   . HOH L 6 .   ? -40.023 -22.973 12.196  1.00 30.80 ? 519 HOH A O   1 
HETATM 4713 O  O   . HOH L 6 .   ? -42.298 -35.105 7.713   1.00 33.32 ? 520 HOH A O   1 
HETATM 4714 O  O   . HOH L 6 .   ? -15.264 -56.136 20.336  1.00 32.81 ? 521 HOH A O   1 
HETATM 4715 O  O   . HOH L 6 .   ? -43.113 -40.304 39.288  1.00 28.96 ? 522 HOH A O   1 
HETATM 4716 O  O   . HOH L 6 .   ? -21.288 -28.452 43.403  1.00 36.67 ? 523 HOH A O   1 
HETATM 4717 O  O   . HOH L 6 .   ? -48.889 -19.553 29.123  1.00 31.45 ? 524 HOH A O   1 
HETATM 4718 O  O   . HOH L 6 .   ? -24.696 -18.290 42.242  1.00 35.78 ? 525 HOH A O   1 
HETATM 4719 O  O   . HOH L 6 .   ? -24.548 -46.881 38.518  1.00 26.56 ? 526 HOH A O   1 
HETATM 4720 O  O   . HOH L 6 .   ? -18.676 -40.613 14.058  1.00 33.81 ? 527 HOH A O   1 
HETATM 4721 O  O   . HOH L 6 .   ? -37.572 -48.080 30.103  1.00 20.05 ? 528 HOH A O   1 
HETATM 4722 O  O   . HOH L 6 .   ? -13.360 -27.328 32.747  1.00 37.60 ? 529 HOH A O   1 
HETATM 4723 O  O   . HOH L 6 .   ? -28.487 -34.810 0.971   1.00 31.19 ? 530 HOH A O   1 
HETATM 4724 O  O   . HOH L 6 .   ? -45.693 -38.719 34.221  1.00 28.21 ? 531 HOH A O   1 
HETATM 4725 O  O   . HOH L 6 .   ? -8.775  -33.618 22.652  1.00 32.57 ? 532 HOH A O   1 
HETATM 4726 O  O   . HOH L 6 .   ? -37.356 -52.058 31.538  1.00 38.01 ? 533 HOH A O   1 
HETATM 4727 O  O   . HOH L 6 .   ? -19.600 -47.927 29.311  1.00 33.76 ? 534 HOH A O   1 
HETATM 4728 O  O   . HOH L 6 .   ? -25.237 -40.267 3.752   1.00 38.26 ? 535 HOH A O   1 
HETATM 4729 O  O   . HOH L 6 .   ? -17.045 -48.282 25.668  1.00 24.58 ? 536 HOH A O   1 
HETATM 4730 O  O   . HOH L 6 .   ? -54.685 -34.219 42.819  1.00 33.92 ? 537 HOH A O   1 
HETATM 4731 O  O   . HOH L 6 .   ? -39.246 -36.379 29.491  1.00 16.36 ? 538 HOH A O   1 
HETATM 4732 O  O   . HOH L 6 .   ? -21.229 -24.223 43.332  1.00 41.58 ? 539 HOH A O   1 
HETATM 4733 O  O   . HOH L 6 .   ? -38.867 -14.693 28.613  1.00 26.64 ? 540 HOH A O   1 
HETATM 4734 O  O   . HOH L 6 .   ? -21.503 -49.227 36.861  1.00 22.90 ? 541 HOH A O   1 
HETATM 4735 O  O   . HOH L 6 .   ? -11.810 -34.179 19.980  1.00 22.67 ? 542 HOH A O   1 
HETATM 4736 O  O   . HOH L 6 .   ? -33.149 -23.587 15.008  1.00 13.23 ? 543 HOH A O   1 
HETATM 4737 O  O   . HOH L 6 .   ? -28.496 -28.069 48.508  1.00 21.54 ? 544 HOH A O   1 
HETATM 4738 O  O   . HOH L 6 .   ? -42.272 -19.278 37.370  1.00 25.78 ? 545 HOH A O   1 
HETATM 4739 O  O   . HOH L 6 .   ? -33.534 -52.609 31.105  1.00 36.93 ? 546 HOH A O   1 
HETATM 4740 O  O   . HOH L 6 .   ? -21.896 -21.703 8.320   1.00 23.69 ? 547 HOH A O   1 
HETATM 4741 O  O   . HOH L 6 .   ? -31.367 -16.218 27.970  1.00 20.89 ? 548 HOH A O   1 
HETATM 4742 O  O   . HOH L 6 .   ? -20.673 -41.806 18.342  1.00 20.60 ? 549 HOH A O   1 
HETATM 4743 O  O   . HOH L 6 .   ? -19.798 -25.656 34.466  1.00 22.50 ? 550 HOH A O   1 
HETATM 4744 O  O   . HOH L 6 .   ? -7.291  -41.944 19.211  1.00 38.35 ? 551 HOH A O   1 
HETATM 4745 O  O   . HOH L 6 .   ? -29.830 -51.026 24.360  1.00 17.25 ? 552 HOH A O   1 
HETATM 4746 O  O   . HOH L 6 .   ? -41.230 -49.567 19.325  1.00 27.91 ? 553 HOH A O   1 
HETATM 4747 O  O   . HOH L 6 .   ? -26.896 -35.609 42.538  1.00 32.79 ? 554 HOH A O   1 
HETATM 4748 O  O   . HOH L 6 .   ? -47.791 -16.743 28.642  1.00 42.29 ? 555 HOH A O   1 
HETATM 4749 O  O   . HOH L 6 .   ? -14.267 -30.508 20.279  1.00 20.71 ? 556 HOH A O   1 
HETATM 4750 O  O   . HOH L 6 .   ? -24.896 -18.018 38.401  1.00 33.71 ? 557 HOH A O   1 
HETATM 4751 O  O   . HOH L 6 .   ? -25.131 -36.454 7.021   1.00 24.59 ? 558 HOH A O   1 
HETATM 4752 O  O   . HOH L 6 .   ? -24.234 -46.062 41.508  1.00 24.34 ? 559 HOH A O   1 
HETATM 4753 O  O   . HOH L 6 .   ? -28.857 -25.811 46.859  1.00 14.92 ? 560 HOH A O   1 
HETATM 4754 O  O   . HOH L 6 .   ? -51.757 -36.882 32.025  1.00 37.23 ? 561 HOH A O   1 
HETATM 4755 O  O   . HOH L 6 .   ? -20.565 -48.674 19.286  1.00 39.91 ? 562 HOH A O   1 
HETATM 4756 O  O   . HOH L 6 .   ? -14.945 -30.322 22.732  1.00 26.69 ? 563 HOH A O   1 
HETATM 4757 O  O   . HOH L 6 .   ? -26.028 -17.737 13.013  1.00 18.03 ? 564 HOH A O   1 
HETATM 4758 O  O   . HOH L 6 .   ? -35.451 -27.331 14.096  1.00 24.47 ? 565 HOH A O   1 
HETATM 4759 O  O   . HOH L 6 .   ? -50.449 -21.319 34.255  1.00 40.45 ? 566 HOH A O   1 
HETATM 4760 O  O   . HOH L 6 .   ? -13.324 -40.979 29.732  1.00 27.43 ? 567 HOH A O   1 
HETATM 4761 O  O   . HOH L 6 .   ? -22.500 -23.610 36.497  1.00 26.59 ? 568 HOH A O   1 
HETATM 4762 O  O   . HOH L 6 .   ? -42.766 -29.258 21.787  1.00 35.79 ? 569 HOH A O   1 
HETATM 4763 O  O   . HOH L 6 .   ? -28.372 -54.927 16.402  1.00 28.28 ? 570 HOH A O   1 
HETATM 4764 O  O   . HOH L 6 .   ? -22.982 -39.328 13.737  1.00 22.10 ? 571 HOH A O   1 
HETATM 4765 O  O   . HOH L 6 .   ? -18.132 -54.428 22.513  1.00 38.45 ? 572 HOH A O   1 
HETATM 4766 O  O   . HOH L 6 .   ? -39.007 -14.055 25.255  1.00 23.85 ? 573 HOH A O   1 
HETATM 4767 O  O   . HOH L 6 .   ? -25.612 -18.157 10.421  1.00 20.49 ? 574 HOH A O   1 
HETATM 4768 O  O   . HOH L 6 .   ? -14.163 -25.032 34.545  1.00 38.12 ? 575 HOH A O   1 
HETATM 4769 O  O   . HOH L 6 .   ? -35.884 -19.218 44.888  1.00 21.52 ? 576 HOH A O   1 
HETATM 4770 O  O   . HOH L 6 .   ? -38.901 -30.011 10.945  1.00 24.57 ? 577 HOH A O   1 
HETATM 4771 O  O   . HOH L 6 .   ? -14.826 -25.934 25.266  1.00 23.52 ? 578 HOH A O   1 
HETATM 4772 O  O   . HOH L 6 .   ? -22.081 -45.846 35.360  1.00 18.44 ? 579 HOH A O   1 
HETATM 4773 O  O   . HOH L 6 .   ? -22.006 -54.547 26.294  1.00 28.69 ? 580 HOH A O   1 
HETATM 4774 O  O   . HOH L 6 .   ? -48.489 -36.111 30.332  1.00 25.44 ? 581 HOH A O   1 
HETATM 4775 O  O   . HOH L 6 .   ? -17.892 -40.040 37.508  1.00 28.92 ? 582 HOH A O   1 
HETATM 4776 O  O   . HOH L 6 .   ? -10.237 -44.463 18.855  1.00 38.49 ? 583 HOH A O   1 
HETATM 4777 O  O   . HOH L 6 .   ? -45.228 -24.516 37.429  1.00 28.63 ? 584 HOH A O   1 
HETATM 4778 O  O   . HOH L 6 .   ? -41.159 -47.341 35.781  1.00 28.22 ? 585 HOH A O   1 
HETATM 4779 O  O   . HOH L 6 .   ? -31.354 -16.536 32.277  1.00 25.33 ? 586 HOH A O   1 
HETATM 4780 O  O   . HOH L 6 .   ? -39.135 -26.769 16.908  1.00 29.66 ? 587 HOH A O   1 
HETATM 4781 O  O   . HOH L 6 .   ? -35.756 -47.340 16.027  1.00 18.44 ? 588 HOH A O   1 
HETATM 4782 O  O   . HOH L 6 .   ? -35.083 -26.619 47.923  1.00 23.80 ? 589 HOH A O   1 
HETATM 4783 O  O   . HOH L 6 .   ? -50.975 -21.730 26.370  1.00 24.33 ? 590 HOH A O   1 
HETATM 4784 O  O   . HOH L 6 .   ? -29.344 -13.609 24.691  1.00 30.14 ? 591 HOH A O   1 
HETATM 4785 O  O   . HOH L 6 .   ? -4.291  -36.216 19.334  1.00 40.34 ? 592 HOH A O   1 
HETATM 4786 O  O   . HOH L 6 .   ? -48.561 -39.334 33.336  1.00 31.25 ? 593 HOH A O   1 
HETATM 4787 O  O   . HOH L 6 .   ? -46.723 -15.554 25.604  1.00 25.81 ? 594 HOH A O   1 
HETATM 4788 O  O   . HOH L 6 .   ? -40.498 -24.567 15.619  1.00 43.46 ? 595 HOH A O   1 
HETATM 4789 O  O   . HOH L 6 .   ? -33.271 -45.244 13.007  1.00 24.41 ? 596 HOH A O   1 
HETATM 4790 O  O   . HOH L 6 .   ? -18.862 -26.381 38.857  1.00 43.48 ? 597 HOH A O   1 
HETATM 4791 O  O   . HOH L 6 .   ? -14.719 -31.560 30.844  1.00 26.59 ? 598 HOH A O   1 
HETATM 4792 O  O   . HOH L 6 .   ? -15.542 -24.847 16.458  1.00 16.94 ? 599 HOH A O   1 
HETATM 4793 O  O   . HOH L 6 .   ? -47.511 -43.124 40.596  1.00 35.96 ? 600 HOH A O   1 
HETATM 4794 O  O   . HOH L 6 .   ? -24.181 -52.775 29.703  1.00 20.59 ? 601 HOH A O   1 
HETATM 4795 O  O   . HOH L 6 .   ? -48.939 -36.446 25.503  1.00 38.31 ? 602 HOH A O   1 
HETATM 4796 O  O   . HOH L 6 .   ? -24.302 -22.869 33.021  1.00 20.81 ? 603 HOH A O   1 
HETATM 4797 O  O   . HOH L 6 .   ? -20.759 -26.229 7.274   1.00 30.59 ? 604 HOH A O   1 
HETATM 4798 O  O   . HOH L 6 .   ? -36.963 -54.752 20.887  1.00 39.79 ? 605 HOH A O   1 
HETATM 4799 O  O   . HOH L 6 .   ? -10.628 -40.703 27.630  1.00 49.66 ? 606 HOH A O   1 
HETATM 4800 O  O   . HOH L 6 .   ? -25.700 -33.314 41.778  1.00 22.96 ? 607 HOH A O   1 
HETATM 4801 O  O   . HOH L 6 .   ? -35.182 -19.597 40.596  1.00 27.40 ? 608 HOH A O   1 
HETATM 4802 O  O   . HOH L 6 .   ? -18.692 -53.852 32.120  1.00 23.57 ? 609 HOH A O   1 
HETATM 4803 O  O   . HOH L 6 .   ? -7.573  -33.899 25.210  1.00 43.02 ? 610 HOH A O   1 
HETATM 4804 O  O   . HOH L 6 .   ? -56.342 -30.628 41.370  1.00 39.22 ? 611 HOH A O   1 
HETATM 4805 O  O   . HOH L 6 .   ? -30.955 -24.054 47.257  1.00 14.79 ? 612 HOH A O   1 
HETATM 4806 O  O   . HOH L 6 .   ? -41.510 -32.957 21.366  1.00 44.43 ? 613 HOH A O   1 
HETATM 4807 O  O   . HOH L 6 .   ? -42.428 -33.523 23.536  1.00 45.02 ? 614 HOH A O   1 
HETATM 4808 O  O   . HOH L 6 .   ? -26.620 -16.851 40.344  1.00 31.84 ? 615 HOH A O   1 
HETATM 4809 O  O   . HOH L 6 .   ? -38.271 -46.149 12.418  1.00 30.63 ? 616 HOH A O   1 
HETATM 4810 O  O   . HOH L 6 .   ? -13.049 -39.121 32.366  1.00 31.67 ? 617 HOH A O   1 
HETATM 4811 O  O   . HOH L 6 .   ? -21.566 -19.808 41.668  1.00 30.25 ? 618 HOH A O   1 
HETATM 4812 O  O   . HOH L 6 .   ? -13.477 -28.465 24.804  1.00 23.29 ? 619 HOH A O   1 
HETATM 4813 O  O   . HOH L 6 .   ? -40.759 -31.774 11.880  1.00 26.88 ? 620 HOH A O   1 
HETATM 4814 O  O   . HOH L 6 .   ? -38.003 -45.964 36.411  1.00 31.34 ? 621 HOH A O   1 
HETATM 4815 O  O   . HOH L 6 .   ? -38.816 -53.221 18.114  1.00 32.77 ? 622 HOH A O   1 
HETATM 4816 O  O   . HOH L 6 .   ? -41.821 -21.452 39.630  1.00 37.40 ? 623 HOH A O   1 
HETATM 4817 O  O   . HOH L 6 .   ? -29.338 -17.167 39.852  1.00 25.93 ? 624 HOH A O   1 
HETATM 4818 O  O   . HOH L 6 .   ? -21.152 -41.131 14.365  1.00 28.94 ? 625 HOH A O   1 
HETATM 4819 O  O   . HOH L 6 .   ? -23.905 -21.381 38.057  1.00 44.54 ? 626 HOH A O   1 
HETATM 4820 O  O   . HOH L 6 .   ? -51.079 -36.904 42.385  1.00 42.36 ? 627 HOH A O   1 
HETATM 4821 O  O   . HOH L 6 .   ? -46.326 -41.571 22.136  1.00 43.24 ? 628 HOH A O   1 
HETATM 4822 O  O   . HOH L 6 .   ? -35.197 -40.305 44.938  1.00 29.41 ? 629 HOH A O   1 
HETATM 4823 O  O   . HOH L 6 .   ? -47.558 -38.574 39.904  1.00 42.83 ? 630 HOH A O   1 
HETATM 4824 O  O   . HOH L 6 .   ? -35.875 -45.581 13.727  1.00 29.44 ? 631 HOH A O   1 
HETATM 4825 O  O   . HOH L 6 .   ? -38.994 -28.471 8.608   1.00 22.68 ? 632 HOH A O   1 
HETATM 4826 O  O   . HOH L 6 .   ? -41.654 -35.865 24.990  1.00 38.77 ? 633 HOH A O   1 
HETATM 4827 O  O   . HOH L 6 .   ? -47.110 -16.546 35.200  1.00 43.04 ? 634 HOH A O   1 
HETATM 4828 O  O   . HOH L 6 .   ? -18.155 -24.041 35.734  1.00 26.77 ? 635 HOH A O   1 
HETATM 4829 O  O   . HOH L 6 .   ? -11.127 -31.728 18.746  1.00 31.02 ? 636 HOH A O   1 
HETATM 4830 O  O   . HOH L 6 .   ? -41.105 -14.701 31.879  1.00 29.90 ? 637 HOH A O   1 
HETATM 4831 O  O   . HOH L 6 .   ? -12.241 -45.482 36.614  1.00 39.65 ? 638 HOH A O   1 
HETATM 4832 O  O   . HOH L 6 .   ? -21.510 -28.866 7.798   1.00 26.46 ? 639 HOH A O   1 
HETATM 4833 O  O   . HOH L 6 .   ? -48.280 -54.643 34.227  1.00 41.95 ? 640 HOH A O   1 
HETATM 4834 O  O   . HOH L 6 .   ? -32.004 -44.217 37.346  1.00 32.72 ? 641 HOH A O   1 
HETATM 4835 O  O   . HOH L 6 .   ? -30.703 -57.491 28.027  1.00 36.29 ? 642 HOH A O   1 
HETATM 4836 O  O   . HOH L 6 .   ? -34.196 -13.472 31.933  1.00 39.33 ? 643 HOH A O   1 
HETATM 4837 O  O   . HOH L 6 .   ? -24.753 -42.371 12.261  1.00 36.71 ? 644 HOH A O   1 
HETATM 4838 O  O   . HOH L 6 .   ? -23.305 -39.932 9.671   1.00 23.40 ? 645 HOH A O   1 
HETATM 4839 O  O   . HOH L 6 .   ? -54.605 -28.137 37.386  1.00 35.70 ? 646 HOH A O   1 
HETATM 4840 O  O   . HOH L 6 .   ? -16.822 -37.174 35.229  1.00 30.63 ? 647 HOH A O   1 
HETATM 4841 O  O   . HOH L 6 .   ? -2.123  -34.427 20.905  1.00 38.79 ? 648 HOH A O   1 
HETATM 4842 O  O   . HOH L 6 .   ? -14.680 -39.081 33.929  1.00 35.29 ? 649 HOH A O   1 
HETATM 4843 O  O   . HOH L 6 .   ? -22.218 -42.776 16.307  1.00 31.32 ? 650 HOH A O   1 
HETATM 4844 O  O   . HOH L 6 .   ? -29.232 -13.390 27.805  1.00 38.01 ? 651 HOH A O   1 
HETATM 4845 O  O   . HOH L 6 .   ? -21.720 -23.514 33.976  1.00 29.08 ? 652 HOH A O   1 
HETATM 4846 O  O   . HOH L 6 .   ? -8.040  -41.728 12.359  1.00 38.45 ? 653 HOH A O   1 
HETATM 4847 O  O   . HOH L 6 .   ? -24.675 -35.480 4.651   1.00 27.85 ? 654 HOH A O   1 
HETATM 4848 O  O   . HOH L 6 .   ? -39.559 -35.301 26.754  1.00 29.59 ? 655 HOH A O   1 
HETATM 4849 O  O   . HOH L 6 .   ? -39.341 -11.612 29.322  1.00 36.85 ? 656 HOH A O   1 
HETATM 4850 O  O   . HOH L 6 .   ? -38.346 -48.258 16.456  1.00 21.95 ? 657 HOH A O   1 
HETATM 4851 O  O   . HOH L 6 .   ? -38.684 -50.911 15.933  1.00 28.82 ? 658 HOH A O   1 
HETATM 4852 O  O   . HOH L 6 .   ? -36.146 -51.562 14.873  1.00 40.51 ? 659 HOH A O   1 
HETATM 4853 O  O   . HOH L 6 .   ? -25.723 -28.139 48.668  1.00 36.86 ? 660 HOH A O   1 
# 
