data_4WW8
# 
_entry.id   4WW8 
# 
_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   4WW8         pdb_00004ww8 10.2210/pdb4ww8/pdb 
WWPDB D_1000204620 ?            ?                   
# 
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 2015-07-01 
2 'Structure model' 1 1 2018-03-07 
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' 'Data collection'        
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' diffrn_source                 
2 3 'Structure model' chem_comp_atom                
3 3 'Structure model' chem_comp_bond                
4 3 'Structure model' database_2                    
5 3 'Structure model' pdbx_initial_refinement_model 
6 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  2 'Structure model' '_diffrn_source.pdbx_synchrotron_site' 
2  3 'Structure model' '_database_2.pdbx_DOI'                 
3  3 'Structure model' '_database_2.pdbx_database_accession'  
4  3 'Structure model' '_struct_conn.pdbx_dist_value'         
5  3 'Structure model' '_struct_conn.ptnr1_auth_asym_id'      
6  3 'Structure model' '_struct_conn.ptnr1_auth_comp_id'      
7  3 'Structure model' '_struct_conn.ptnr1_auth_seq_id'       
8  3 'Structure model' '_struct_conn.ptnr1_label_asym_id'     
9  3 'Structure model' '_struct_conn.ptnr1_label_atom_id'     
10 3 'Structure model' '_struct_conn.ptnr1_label_comp_id'     
11 3 'Structure model' '_struct_conn.ptnr1_label_seq_id'      
12 3 'Structure model' '_struct_conn.ptnr2_auth_asym_id'      
13 3 'Structure model' '_struct_conn.ptnr2_auth_comp_id'      
14 3 'Structure model' '_struct_conn.ptnr2_auth_seq_id'       
15 3 'Structure model' '_struct_conn.ptnr2_label_asym_id'     
16 3 'Structure model' '_struct_conn.ptnr2_label_atom_id'     
17 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                        4WW8 
_pdbx_database_status.recvd_initial_deposition_date   2014-11-10 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_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 . 4WR7 unspecified 
PDB . 4WUP unspecified 
PDB . 4WUQ unspecified 
PDB . 4WW6 unspecified 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'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                   NE 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Biophys.Chem. 
_citation.journal_id_ASTM           BICIAZ 
_citation.journal_id_CSD            0829 
_citation.journal_id_ISSN           0301-4622 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            205 
_citation.language                  ? 
_citation.page_first                51 
_citation.page_last                 65 
_citation.title                     
;Intrinsic thermodynamics of 4-substituted-2,3,5,6-tetrafluorobenzenesulfonamide binding to carbonic anhydrases by isothermal titration calorimetry.
;
_citation.year                      2015 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.bpc.2015.05.009 
_citation.pdbx_database_id_PubMed   26079542 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Zubriene, A.'      1  ? 
primary 'Smirnoviene, J.'   2  ? 
primary 'Smirnov, A.'       3  ? 
primary 'Morkunaite, V.'    4  ? 
primary 'Michailoviene, V.' 5  ? 
primary 'Jachno, J.'        6  ? 
primary 'Juozapaitiene, V.' 7  ? 
primary 'Norvaisas, P.'     8  ? 
primary 'Manakova, E.'      9  ? 
primary 'Grazulis, S.'      10 ? 
primary 'Matulis, D.'       11 ? 
# 
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 12'                29917.318 4   4.2.1.1 ?                              
'UNP residues 30-291' ? 
2 non-polymer syn 'ZINC ION'                             65.409    4   ?       4-Propylthiobenzenesulfonamide ? ? 
3 non-polymer syn 1,2-ETHANEDIOL                         62.068    13  ?       ?                              Zn ? 
4 non-polymer syn '4-(propylsulfanyl)benzenesulfonamide' 231.335   4   ?       ?                              ? ? 
5 water       nat water                                  18.015    912 ?       ?                              ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Carbonate dehydratase XII,Carbonic anhydrase XII,CA-XII,Tumor antigen HOM-RCC-3.1.3' 
# 
_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       
;MSKWTYFGPDGENSWSKKYPSCGGLLQSPIDLHSDILQYDASLTPLEFQGYNLSANKQFLLTNNGHSVKLNLPSDMHIQG
LQSRYSATQLHLHWGNPNDPHGSEHTVSGQHFAAELHIVHYNSDLYPDASTASNKSEGLAVLAVLIEMGSFNPSYDKIFS
HLQHVKYKGQEAFVPGFNIEELLPERTAEYYRYRGSLTTPPCNPTVLWTVFRNPVQISQEQLLALETALYCTHMDDPSPR
EMINNFRQVQKFDERLVYTSFSQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MSKWTYFGPDGENSWSKKYPSCGGLLQSPIDLHSDILQYDASLTPLEFQGYNLSANKQFLLTNNGHSVKLNLPSDMHIQG
LQSRYSATQLHLHWGNPNDPHGSEHTVSGQHFAAELHIVHYNSDLYPDASTASNKSEGLAVLAVLIEMGSFNPSYDKIFS
HLQHVKYKGQEAFVPGFNIEELLPERTAEYYRYRGSLTTPPCNPTVLWTVFRNPVQISQEQLLALETALYCTHMDDPSPR
EMINNFRQVQKFDERLVYTSFSQ
;
_entity_poly.pdbx_strand_id                 A,B,C,D 
_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 1,2-ETHANEDIOL                         EDO 
4 '4-(propylsulfanyl)benzenesulfonamide' VD9 
5 water                                  HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   SER n 
1 3   LYS n 
1 4   TRP n 
1 5   THR n 
1 6   TYR n 
1 7   PHE n 
1 8   GLY n 
1 9   PRO n 
1 10  ASP n 
1 11  GLY n 
1 12  GLU n 
1 13  ASN n 
1 14  SER n 
1 15  TRP n 
1 16  SER n 
1 17  LYS n 
1 18  LYS n 
1 19  TYR n 
1 20  PRO n 
1 21  SER n 
1 22  CYS n 
1 23  GLY n 
1 24  GLY n 
1 25  LEU n 
1 26  LEU n 
1 27  GLN n 
1 28  SER n 
1 29  PRO n 
1 30  ILE n 
1 31  ASP n 
1 32  LEU n 
1 33  HIS n 
1 34  SER n 
1 35  ASP n 
1 36  ILE n 
1 37  LEU n 
1 38  GLN n 
1 39  TYR n 
1 40  ASP n 
1 41  ALA n 
1 42  SER n 
1 43  LEU n 
1 44  THR n 
1 45  PRO n 
1 46  LEU n 
1 47  GLU n 
1 48  PHE n 
1 49  GLN n 
1 50  GLY n 
1 51  TYR n 
1 52  ASN n 
1 53  LEU n 
1 54  SER n 
1 55  ALA n 
1 56  ASN n 
1 57  LYS n 
1 58  GLN n 
1 59  PHE n 
1 60  LEU n 
1 61  LEU n 
1 62  THR n 
1 63  ASN n 
1 64  ASN n 
1 65  GLY n 
1 66  HIS n 
1 67  SER n 
1 68  VAL n 
1 69  LYS n 
1 70  LEU n 
1 71  ASN n 
1 72  LEU n 
1 73  PRO n 
1 74  SER n 
1 75  ASP n 
1 76  MET n 
1 77  HIS n 
1 78  ILE n 
1 79  GLN n 
1 80  GLY n 
1 81  LEU n 
1 82  GLN n 
1 83  SER n 
1 84  ARG n 
1 85  TYR n 
1 86  SER n 
1 87  ALA n 
1 88  THR n 
1 89  GLN n 
1 90  LEU n 
1 91  HIS n 
1 92  LEU n 
1 93  HIS n 
1 94  TRP n 
1 95  GLY n 
1 96  ASN n 
1 97  PRO n 
1 98  ASN n 
1 99  ASP n 
1 100 PRO n 
1 101 HIS n 
1 102 GLY n 
1 103 SER n 
1 104 GLU n 
1 105 HIS n 
1 106 THR n 
1 107 VAL n 
1 108 SER n 
1 109 GLY n 
1 110 GLN n 
1 111 HIS n 
1 112 PHE n 
1 113 ALA n 
1 114 ALA n 
1 115 GLU n 
1 116 LEU n 
1 117 HIS n 
1 118 ILE n 
1 119 VAL n 
1 120 HIS n 
1 121 TYR n 
1 122 ASN n 
1 123 SER n 
1 124 ASP n 
1 125 LEU n 
1 126 TYR n 
1 127 PRO n 
1 128 ASP n 
1 129 ALA n 
1 130 SER n 
1 131 THR n 
1 132 ALA n 
1 133 SER n 
1 134 ASN n 
1 135 LYS n 
1 136 SER n 
1 137 GLU n 
1 138 GLY n 
1 139 LEU n 
1 140 ALA n 
1 141 VAL n 
1 142 LEU n 
1 143 ALA n 
1 144 VAL n 
1 145 LEU n 
1 146 ILE n 
1 147 GLU n 
1 148 MET n 
1 149 GLY n 
1 150 SER n 
1 151 PHE n 
1 152 ASN n 
1 153 PRO n 
1 154 SER n 
1 155 TYR n 
1 156 ASP n 
1 157 LYS n 
1 158 ILE n 
1 159 PHE n 
1 160 SER n 
1 161 HIS n 
1 162 LEU n 
1 163 GLN n 
1 164 HIS n 
1 165 VAL n 
1 166 LYS n 
1 167 TYR n 
1 168 LYS n 
1 169 GLY n 
1 170 GLN n 
1 171 GLU n 
1 172 ALA n 
1 173 PHE n 
1 174 VAL n 
1 175 PRO n 
1 176 GLY n 
1 177 PHE n 
1 178 ASN n 
1 179 ILE n 
1 180 GLU n 
1 181 GLU n 
1 182 LEU n 
1 183 LEU n 
1 184 PRO n 
1 185 GLU n 
1 186 ARG n 
1 187 THR n 
1 188 ALA n 
1 189 GLU n 
1 190 TYR n 
1 191 TYR n 
1 192 ARG n 
1 193 TYR n 
1 194 ARG n 
1 195 GLY n 
1 196 SER n 
1 197 LEU n 
1 198 THR n 
1 199 THR n 
1 200 PRO n 
1 201 PRO n 
1 202 CYS n 
1 203 ASN n 
1 204 PRO n 
1 205 THR n 
1 206 VAL n 
1 207 LEU n 
1 208 TRP n 
1 209 THR n 
1 210 VAL n 
1 211 PHE n 
1 212 ARG n 
1 213 ASN n 
1 214 PRO n 
1 215 VAL n 
1 216 GLN n 
1 217 ILE n 
1 218 SER n 
1 219 GLN n 
1 220 GLU n 
1 221 GLN n 
1 222 LEU n 
1 223 LEU n 
1 224 ALA n 
1 225 LEU n 
1 226 GLU n 
1 227 THR n 
1 228 ALA n 
1 229 LEU n 
1 230 TYR n 
1 231 CYS n 
1 232 THR n 
1 233 HIS n 
1 234 MET n 
1 235 ASP n 
1 236 ASP n 
1 237 PRO n 
1 238 SER n 
1 239 PRO n 
1 240 ARG n 
1 241 GLU n 
1 242 MET n 
1 243 ILE n 
1 244 ASN n 
1 245 ASN n 
1 246 PHE n 
1 247 ARG n 
1 248 GLN n 
1 249 VAL n 
1 250 GLN n 
1 251 LYS n 
1 252 PHE n 
1 253 ASP n 
1 254 GLU n 
1 255 ARG n 
1 256 LEU n 
1 257 VAL n 
1 258 TYR n 
1 259 THR n 
1 260 SER n 
1 261 PHE n 
1 262 SER n 
1 263 GLN 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                 CA12 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              Rosetta 
_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                       pET21a 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                ?                 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE                               ?                 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE                             ?                 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                        ?                 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE                               ?                 'C3 H7 N O2 S'   121.158 
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 
VD9 non-polymer         . '4-(propylsulfanyl)benzenesulfonamide' ?                 'C9 H13 N O2 S2' 231.335 
ZN  non-polymer         . 'ZINC ION'                             ?                 'Zn 2'           65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   SER 2   2   ?   ?   ?   A . n 
A 1 3   LYS 3   3   3   LYS LYS A . n 
A 1 4   TRP 4   4   4   TRP TRP A . n 
A 1 5   THR 5   5   5   THR THR A . n 
A 1 6   TYR 6   6   6   TYR TYR A . n 
A 1 7   PHE 7   7   7   PHE PHE A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   PRO 9   9   9   PRO PRO A . n 
A 1 10  ASP 10  10  10  ASP ASP A . n 
A 1 11  GLY 11  11  11  GLY GLY A . n 
A 1 12  GLU 12  12  12  GLU GLU A . n 
A 1 13  ASN 13  13  13  ASN ASN A . n 
A 1 14  SER 14  14  14  SER SER A . n 
A 1 15  TRP 15  15  15  TRP TRP A . n 
A 1 16  SER 16  16  16  SER SER A . n 
A 1 17  LYS 17  17  17  LYS LYS A . n 
A 1 18  LYS 18  18  18  LYS LYS A . n 
A 1 19  TYR 19  19  19  TYR TYR A . n 
A 1 20  PRO 20  20  20  PRO PRO A . n 
A 1 21  SER 21  21  21  SER SER A . n 
A 1 22  CYS 22  22  22  CYS CYS A . n 
A 1 23  GLY 23  23  23  GLY GLY A . n 
A 1 24  GLY 24  24  24  GLY GLY A . n 
A 1 25  LEU 25  25  25  LEU LEU A . n 
A 1 26  LEU 26  26  26  LEU LEU A . n 
A 1 27  GLN 27  27  27  GLN GLN A . n 
A 1 28  SER 28  28  28  SER SER A . n 
A 1 29  PRO 29  29  29  PRO PRO A . n 
A 1 30  ILE 30  30  30  ILE ILE A . n 
A 1 31  ASP 31  31  31  ASP ASP A . n 
A 1 32  LEU 32  32  32  LEU LEU A . n 
A 1 33  HIS 33  33  33  HIS HIS A . n 
A 1 34  SER 34  34  34  SER SER A . n 
A 1 35  ASP 35  35  35  ASP ASP A . n 
A 1 36  ILE 36  36  36  ILE ILE A . n 
A 1 37  LEU 37  37  37  LEU LEU A . n 
A 1 38  GLN 38  38  38  GLN GLN A . n 
A 1 39  TYR 39  39  39  TYR TYR A . n 
A 1 40  ASP 40  40  40  ASP ASP A . n 
A 1 41  ALA 41  41  41  ALA ALA A . n 
A 1 42  SER 42  42  42  SER SER A . n 
A 1 43  LEU 43  43  43  LEU LEU A . n 
A 1 44  THR 44  44  44  THR THR A . n 
A 1 45  PRO 45  45  45  PRO PRO A . n 
A 1 46  LEU 46  46  46  LEU LEU A . n 
A 1 47  GLU 47  47  47  GLU GLU A . n 
A 1 48  PHE 48  48  48  PHE PHE A . n 
A 1 49  GLN 49  49  49  GLN GLN A . n 
A 1 50  GLY 50  50  50  GLY GLY A . n 
A 1 51  TYR 51  51  51  TYR TYR A . n 
A 1 52  ASN 52  52  52  ASN ASN A . n 
A 1 53  LEU 53  53  53  LEU LEU A . n 
A 1 54  SER 54  54  54  SER SER A . n 
A 1 55  ALA 55  55  55  ALA ALA A . n 
A 1 56  ASN 56  56  56  ASN ASN A . n 
A 1 57  LYS 57  57  57  LYS LYS A . n 
A 1 58  GLN 58  58  58  GLN GLN A . n 
A 1 59  PHE 59  59  59  PHE PHE A . n 
A 1 60  LEU 60  60  60  LEU LEU A . n 
A 1 61  LEU 61  61  61  LEU LEU A . n 
A 1 62  THR 62  62  62  THR THR A . n 
A 1 63  ASN 63  63  63  ASN ASN A . n 
A 1 64  ASN 64  64  64  ASN ASN A . n 
A 1 65  GLY 65  65  65  GLY GLY A . n 
A 1 66  HIS 66  66  66  HIS HIS A . n 
A 1 67  SER 67  67  67  SER SER A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  LYS 69  69  69  LYS LYS A . n 
A 1 70  LEU 70  70  70  LEU LEU A . n 
A 1 71  ASN 71  71  71  ASN ASN A . n 
A 1 72  LEU 72  72  72  LEU LEU A . n 
A 1 73  PRO 73  73  73  PRO PRO A . n 
A 1 74  SER 74  74  74  SER SER A . n 
A 1 75  ASP 75  75  75  ASP ASP A . n 
A 1 76  MET 76  76  76  MET MET A . n 
A 1 77  HIS 77  77  77  HIS HIS A . n 
A 1 78  ILE 78  78  78  ILE ILE A . n 
A 1 79  GLN 79  79  79  GLN GLN A . n 
A 1 80  GLY 80  80  80  GLY GLY A . n 
A 1 81  LEU 81  81  81  LEU LEU A . n 
A 1 82  GLN 82  82  82  GLN GLN A . n 
A 1 83  SER 83  83  83  SER SER A . n 
A 1 84  ARG 84  84  84  ARG ARG A . n 
A 1 85  TYR 85  85  85  TYR TYR A . n 
A 1 86  SER 86  86  86  SER SER A . n 
A 1 87  ALA 87  87  87  ALA ALA A . n 
A 1 88  THR 88  88  88  THR THR A . n 
A 1 89  GLN 89  89  89  GLN GLN A . n 
A 1 90  LEU 90  90  90  LEU LEU A . n 
A 1 91  HIS 91  91  91  HIS HIS A . n 
A 1 92  LEU 92  92  92  LEU LEU A . n 
A 1 93  HIS 93  93  93  HIS HIS A . n 
A 1 94  TRP 94  94  94  TRP TRP A . n 
A 1 95  GLY 95  95  95  GLY GLY A . n 
A 1 96  ASN 96  96  96  ASN ASN A . n 
A 1 97  PRO 97  97  97  PRO PRO A . n 
A 1 98  ASN 98  98  98  ASN ASN A . n 
A 1 99  ASP 99  99  99  ASP ASP A . n 
A 1 100 PRO 100 100 100 PRO PRO A . n 
A 1 101 HIS 101 101 101 HIS HIS A . n 
A 1 102 GLY 102 102 102 GLY GLY A . n 
A 1 103 SER 103 103 103 SER SER A . n 
A 1 104 GLU 104 104 104 GLU GLU A . n 
A 1 105 HIS 105 105 105 HIS HIS A . n 
A 1 106 THR 106 106 106 THR THR A . n 
A 1 107 VAL 107 107 107 VAL VAL A . n 
A 1 108 SER 108 108 108 SER SER A . n 
A 1 109 GLY 109 109 109 GLY GLY A . n 
A 1 110 GLN 110 110 110 GLN GLN A . n 
A 1 111 HIS 111 111 111 HIS HIS A . n 
A 1 112 PHE 112 112 112 PHE PHE A . n 
A 1 113 ALA 113 113 113 ALA ALA A . n 
A 1 114 ALA 114 114 114 ALA ALA A . n 
A 1 115 GLU 115 115 115 GLU GLU A . n 
A 1 116 LEU 116 116 116 LEU LEU A . n 
A 1 117 HIS 117 117 117 HIS HIS A . n 
A 1 118 ILE 118 118 118 ILE ILE A . n 
A 1 119 VAL 119 119 119 VAL VAL A . n 
A 1 120 HIS 120 120 120 HIS HIS A . n 
A 1 121 TYR 121 121 121 TYR TYR A . n 
A 1 122 ASN 122 122 122 ASN ASN A . n 
A 1 123 SER 123 123 123 SER SER A . n 
A 1 124 ASP 124 124 124 ASP ASP A . n 
A 1 125 LEU 125 125 125 LEU LEU A . n 
A 1 126 TYR 126 126 126 TYR TYR A . n 
A 1 127 PRO 127 127 127 PRO PRO A . n 
A 1 128 ASP 128 128 128 ASP ASP A . n 
A 1 129 ALA 129 129 129 ALA ALA A . n 
A 1 130 SER 130 130 130 SER SER A . n 
A 1 131 THR 131 131 131 THR THR A . n 
A 1 132 ALA 132 132 132 ALA ALA A . n 
A 1 133 SER 133 133 133 SER SER A . n 
A 1 134 ASN 134 134 134 ASN ASN A . n 
A 1 135 LYS 135 135 135 LYS LYS A . n 
A 1 136 SER 136 136 136 SER SER A . n 
A 1 137 GLU 137 137 137 GLU GLU A . n 
A 1 138 GLY 138 138 138 GLY GLY A . n 
A 1 139 LEU 139 139 139 LEU LEU A . n 
A 1 140 ALA 140 140 140 ALA ALA A . n 
A 1 141 VAL 141 141 141 VAL VAL A . n 
A 1 142 LEU 142 142 142 LEU LEU A . n 
A 1 143 ALA 143 143 143 ALA ALA A . n 
A 1 144 VAL 144 144 144 VAL VAL A . n 
A 1 145 LEU 145 145 145 LEU LEU A . n 
A 1 146 ILE 146 146 146 ILE ILE A . n 
A 1 147 GLU 147 147 147 GLU GLU A . n 
A 1 148 MET 148 148 148 MET MET A . n 
A 1 149 GLY 149 149 149 GLY GLY A . n 
A 1 150 SER 150 150 150 SER SER A . n 
A 1 151 PHE 151 151 151 PHE PHE A . n 
A 1 152 ASN 152 152 152 ASN ASN A . n 
A 1 153 PRO 153 153 153 PRO PRO A . n 
A 1 154 SER 154 154 154 SER SER A . n 
A 1 155 TYR 155 155 155 TYR TYR A . n 
A 1 156 ASP 156 156 156 ASP ASP A . n 
A 1 157 LYS 157 157 157 LYS LYS A . n 
A 1 158 ILE 158 158 158 ILE ILE A . n 
A 1 159 PHE 159 159 159 PHE PHE A . n 
A 1 160 SER 160 160 160 SER SER A . n 
A 1 161 HIS 161 161 161 HIS HIS A . n 
A 1 162 LEU 162 162 162 LEU LEU A . n 
A 1 163 GLN 163 163 163 GLN GLN A . n 
A 1 164 HIS 164 164 164 HIS HIS A . n 
A 1 165 VAL 165 165 165 VAL VAL A . n 
A 1 166 LYS 166 166 166 LYS LYS A . n 
A 1 167 TYR 167 167 167 TYR TYR A . n 
A 1 168 LYS 168 168 168 LYS LYS A . n 
A 1 169 GLY 169 169 169 GLY GLY A . n 
A 1 170 GLN 170 170 170 GLN GLN A . n 
A 1 171 GLU 171 171 171 GLU GLU A . n 
A 1 172 ALA 172 172 172 ALA ALA A . n 
A 1 173 PHE 173 173 173 PHE PHE A . n 
A 1 174 VAL 174 174 174 VAL VAL A . n 
A 1 175 PRO 175 175 175 PRO PRO A . n 
A 1 176 GLY 176 176 176 GLY GLY A . n 
A 1 177 PHE 177 177 177 PHE PHE A . n 
A 1 178 ASN 178 178 178 ASN ASN A . n 
A 1 179 ILE 179 179 179 ILE ILE A . n 
A 1 180 GLU 180 180 180 GLU GLU A . n 
A 1 181 GLU 181 181 181 GLU GLU A . n 
A 1 182 LEU 182 182 182 LEU LEU A . n 
A 1 183 LEU 183 183 183 LEU LEU A . n 
A 1 184 PRO 184 184 184 PRO PRO A . n 
A 1 185 GLU 185 185 185 GLU GLU A . n 
A 1 186 ARG 186 186 186 ARG ARG A . n 
A 1 187 THR 187 187 187 THR THR A . n 
A 1 188 ALA 188 188 188 ALA ALA A . n 
A 1 189 GLU 189 189 189 GLU GLU A . n 
A 1 190 TYR 190 190 190 TYR TYR A . n 
A 1 191 TYR 191 191 191 TYR TYR A . n 
A 1 192 ARG 192 192 192 ARG ARG A . n 
A 1 193 TYR 193 193 193 TYR TYR A . n 
A 1 194 ARG 194 194 194 ARG ARG A . n 
A 1 195 GLY 195 195 195 GLY GLY A . n 
A 1 196 SER 196 196 196 SER SER A . n 
A 1 197 LEU 197 197 197 LEU LEU A . n 
A 1 198 THR 198 198 198 THR THR A . n 
A 1 199 THR 199 199 199 THR THR A . n 
A 1 200 PRO 200 200 200 PRO PRO A . n 
A 1 201 PRO 201 201 201 PRO PRO A . n 
A 1 202 CYS 202 202 202 CYS CYS A . n 
A 1 203 ASN 203 203 203 ASN ASN A . n 
A 1 204 PRO 204 204 204 PRO PRO A . n 
A 1 205 THR 205 205 205 THR THR A . n 
A 1 206 VAL 206 206 206 VAL VAL A . n 
A 1 207 LEU 207 207 207 LEU LEU A . n 
A 1 208 TRP 208 208 208 TRP TRP A . n 
A 1 209 THR 209 209 209 THR THR A . n 
A 1 210 VAL 210 210 210 VAL VAL A . n 
A 1 211 PHE 211 211 211 PHE PHE A . n 
A 1 212 ARG 212 212 212 ARG ARG A . n 
A 1 213 ASN 213 213 213 ASN ASN A . n 
A 1 214 PRO 214 214 214 PRO PRO A . n 
A 1 215 VAL 215 215 215 VAL VAL A . n 
A 1 216 GLN 216 216 216 GLN GLN A . n 
A 1 217 ILE 217 217 217 ILE ILE A . n 
A 1 218 SER 218 218 218 SER SER A . n 
A 1 219 GLN 219 219 219 GLN GLN A . n 
A 1 220 GLU 220 220 220 GLU GLU A . n 
A 1 221 GLN 221 221 221 GLN GLN A . n 
A 1 222 LEU 222 222 222 LEU LEU A . n 
A 1 223 LEU 223 223 223 LEU LEU A . n 
A 1 224 ALA 224 224 224 ALA ALA A . n 
A 1 225 LEU 225 225 225 LEU LEU A . n 
A 1 226 GLU 226 226 226 GLU GLU A . n 
A 1 227 THR 227 227 227 THR THR A . n 
A 1 228 ALA 228 228 228 ALA ALA A . n 
A 1 229 LEU 229 229 229 LEU LEU A . n 
A 1 230 TYR 230 230 230 TYR TYR A . n 
A 1 231 CYS 231 231 231 CYS CYS A . n 
A 1 232 THR 232 232 232 THR THR A . n 
A 1 233 HIS 233 233 233 HIS HIS A . n 
A 1 234 MET 234 234 234 MET MET A . n 
A 1 235 ASP 235 235 235 ASP ASP A . n 
A 1 236 ASP 236 236 236 ASP ASP A . n 
A 1 237 PRO 237 237 237 PRO PRO A . n 
A 1 238 SER 238 238 238 SER SER A . n 
A 1 239 PRO 239 239 239 PRO PRO A . n 
A 1 240 ARG 240 240 240 ARG ARG A . n 
A 1 241 GLU 241 241 241 GLU GLU A . n 
A 1 242 MET 242 242 242 MET MET A . n 
A 1 243 ILE 243 243 243 ILE ILE A . n 
A 1 244 ASN 244 244 244 ASN ASN A . n 
A 1 245 ASN 245 245 245 ASN ASN A . n 
A 1 246 PHE 246 246 246 PHE PHE A . n 
A 1 247 ARG 247 247 247 ARG ARG A . n 
A 1 248 GLN 248 248 248 GLN GLN A . n 
A 1 249 VAL 249 249 249 VAL VAL A . n 
A 1 250 GLN 250 250 250 GLN GLN A . n 
A 1 251 LYS 251 251 251 LYS LYS A . n 
A 1 252 PHE 252 252 252 PHE PHE A . n 
A 1 253 ASP 253 253 253 ASP ASP A . n 
A 1 254 GLU 254 254 254 GLU GLU A . n 
A 1 255 ARG 255 255 255 ARG ARG A . n 
A 1 256 LEU 256 256 256 LEU LEU A . n 
A 1 257 VAL 257 257 257 VAL VAL A . n 
A 1 258 TYR 258 258 258 TYR TYR A . n 
A 1 259 THR 259 259 259 THR THR A . n 
A 1 260 SER 260 260 260 SER SER A . n 
A 1 261 PHE 261 261 261 PHE PHE A . n 
A 1 262 SER 262 262 262 SER SER A . n 
A 1 263 GLN 263 263 263 GLN GLN A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   SER 2   2   ?   ?   ?   B . n 
B 1 3   LYS 3   3   3   LYS LYS B . n 
B 1 4   TRP 4   4   4   TRP TRP B . n 
B 1 5   THR 5   5   5   THR THR B . n 
B 1 6   TYR 6   6   6   TYR TYR B . n 
B 1 7   PHE 7   7   7   PHE PHE B . n 
B 1 8   GLY 8   8   8   GLY GLY B . n 
B 1 9   PRO 9   9   9   PRO PRO B . n 
B 1 10  ASP 10  10  10  ASP ASP B . n 
B 1 11  GLY 11  11  11  GLY GLY B . n 
B 1 12  GLU 12  12  12  GLU GLU B . n 
B 1 13  ASN 13  13  13  ASN ASN B . n 
B 1 14  SER 14  14  14  SER SER B . n 
B 1 15  TRP 15  15  15  TRP TRP B . n 
B 1 16  SER 16  16  16  SER SER B . n 
B 1 17  LYS 17  17  17  LYS LYS B . n 
B 1 18  LYS 18  18  18  LYS LYS B . n 
B 1 19  TYR 19  19  19  TYR TYR B . n 
B 1 20  PRO 20  20  20  PRO PRO B . n 
B 1 21  SER 21  21  21  SER SER B . n 
B 1 22  CYS 22  22  22  CYS CYS B . n 
B 1 23  GLY 23  23  23  GLY GLY B . n 
B 1 24  GLY 24  24  24  GLY GLY B . n 
B 1 25  LEU 25  25  25  LEU LEU B . n 
B 1 26  LEU 26  26  26  LEU LEU B . n 
B 1 27  GLN 27  27  27  GLN GLN B . n 
B 1 28  SER 28  28  28  SER SER B . n 
B 1 29  PRO 29  29  29  PRO PRO B . n 
B 1 30  ILE 30  30  30  ILE ILE B . n 
B 1 31  ASP 31  31  31  ASP ASP B . n 
B 1 32  LEU 32  32  32  LEU LEU B . n 
B 1 33  HIS 33  33  33  HIS HIS B . n 
B 1 34  SER 34  34  34  SER SER B . n 
B 1 35  ASP 35  35  35  ASP ASP B . n 
B 1 36  ILE 36  36  36  ILE ILE B . n 
B 1 37  LEU 37  37  37  LEU LEU B . n 
B 1 38  GLN 38  38  38  GLN GLN B . n 
B 1 39  TYR 39  39  39  TYR TYR B . n 
B 1 40  ASP 40  40  40  ASP ASP B . n 
B 1 41  ALA 41  41  41  ALA ALA B . n 
B 1 42  SER 42  42  42  SER SER B . n 
B 1 43  LEU 43  43  43  LEU LEU B . n 
B 1 44  THR 44  44  44  THR THR B . n 
B 1 45  PRO 45  45  45  PRO PRO B . n 
B 1 46  LEU 46  46  46  LEU LEU B . n 
B 1 47  GLU 47  47  47  GLU GLU B . n 
B 1 48  PHE 48  48  48  PHE PHE B . n 
B 1 49  GLN 49  49  49  GLN GLN B . n 
B 1 50  GLY 50  50  50  GLY GLY B . n 
B 1 51  TYR 51  51  51  TYR TYR B . n 
B 1 52  ASN 52  52  52  ASN ASN B . n 
B 1 53  LEU 53  53  53  LEU LEU B . n 
B 1 54  SER 54  54  54  SER SER B . n 
B 1 55  ALA 55  55  55  ALA ALA B . n 
B 1 56  ASN 56  56  56  ASN ASN B . n 
B 1 57  LYS 57  57  57  LYS LYS B . n 
B 1 58  GLN 58  58  58  GLN GLN B . n 
B 1 59  PHE 59  59  59  PHE PHE B . n 
B 1 60  LEU 60  60  60  LEU LEU B . n 
B 1 61  LEU 61  61  61  LEU LEU B . n 
B 1 62  THR 62  62  62  THR THR B . n 
B 1 63  ASN 63  63  63  ASN ASN B . n 
B 1 64  ASN 64  64  64  ASN ASN B . n 
B 1 65  GLY 65  65  65  GLY GLY B . n 
B 1 66  HIS 66  66  66  HIS HIS B . n 
B 1 67  SER 67  67  67  SER SER B . n 
B 1 68  VAL 68  68  68  VAL VAL B . n 
B 1 69  LYS 69  69  69  LYS LYS B . n 
B 1 70  LEU 70  70  70  LEU LEU B . n 
B 1 71  ASN 71  71  71  ASN ASN B . n 
B 1 72  LEU 72  72  72  LEU LEU B . n 
B 1 73  PRO 73  73  73  PRO PRO B . n 
B 1 74  SER 74  74  74  SER SER B . n 
B 1 75  ASP 75  75  75  ASP ASP B . n 
B 1 76  MET 76  76  76  MET MET B . n 
B 1 77  HIS 77  77  77  HIS HIS B . n 
B 1 78  ILE 78  78  78  ILE ILE B . n 
B 1 79  GLN 79  79  79  GLN GLN B . n 
B 1 80  GLY 80  80  80  GLY GLY B . n 
B 1 81  LEU 81  81  81  LEU LEU B . n 
B 1 82  GLN 82  82  82  GLN GLN B . n 
B 1 83  SER 83  83  83  SER SER B . n 
B 1 84  ARG 84  84  84  ARG ARG B . n 
B 1 85  TYR 85  85  85  TYR TYR B . n 
B 1 86  SER 86  86  86  SER SER B . n 
B 1 87  ALA 87  87  87  ALA ALA B . n 
B 1 88  THR 88  88  88  THR THR B . n 
B 1 89  GLN 89  89  89  GLN GLN B . n 
B 1 90  LEU 90  90  90  LEU LEU B . n 
B 1 91  HIS 91  91  91  HIS HIS B . n 
B 1 92  LEU 92  92  92  LEU LEU B . n 
B 1 93  HIS 93  93  93  HIS HIS B . n 
B 1 94  TRP 94  94  94  TRP TRP B . n 
B 1 95  GLY 95  95  95  GLY GLY B . n 
B 1 96  ASN 96  96  96  ASN ASN B . n 
B 1 97  PRO 97  97  97  PRO PRO B . n 
B 1 98  ASN 98  98  98  ASN ASN B . n 
B 1 99  ASP 99  99  99  ASP ASP B . n 
B 1 100 PRO 100 100 100 PRO PRO B . n 
B 1 101 HIS 101 101 101 HIS HIS B . n 
B 1 102 GLY 102 102 102 GLY GLY B . n 
B 1 103 SER 103 103 103 SER SER B . n 
B 1 104 GLU 104 104 104 GLU GLU B . n 
B 1 105 HIS 105 105 105 HIS HIS B . n 
B 1 106 THR 106 106 106 THR THR B . n 
B 1 107 VAL 107 107 107 VAL VAL B . n 
B 1 108 SER 108 108 108 SER SER B . n 
B 1 109 GLY 109 109 109 GLY GLY B . n 
B 1 110 GLN 110 110 110 GLN GLN B . n 
B 1 111 HIS 111 111 111 HIS HIS B . n 
B 1 112 PHE 112 112 112 PHE PHE B . n 
B 1 113 ALA 113 113 113 ALA ALA B . n 
B 1 114 ALA 114 114 114 ALA ALA B . n 
B 1 115 GLU 115 115 115 GLU GLU B . n 
B 1 116 LEU 116 116 116 LEU LEU B . n 
B 1 117 HIS 117 117 117 HIS HIS B . n 
B 1 118 ILE 118 118 118 ILE ILE B . n 
B 1 119 VAL 119 119 119 VAL VAL B . n 
B 1 120 HIS 120 120 120 HIS HIS B . n 
B 1 121 TYR 121 121 121 TYR TYR B . n 
B 1 122 ASN 122 122 122 ASN ASN B . n 
B 1 123 SER 123 123 123 SER SER B . n 
B 1 124 ASP 124 124 124 ASP ASP B . n 
B 1 125 LEU 125 125 125 LEU LEU B . n 
B 1 126 TYR 126 126 126 TYR TYR B . n 
B 1 127 PRO 127 127 127 PRO PRO B . n 
B 1 128 ASP 128 128 128 ASP ASP B . n 
B 1 129 ALA 129 129 129 ALA ALA B . n 
B 1 130 SER 130 130 130 SER SER B . n 
B 1 131 THR 131 131 131 THR THR B . n 
B 1 132 ALA 132 132 132 ALA ALA B . n 
B 1 133 SER 133 133 133 SER SER B . n 
B 1 134 ASN 134 134 134 ASN ASN B . n 
B 1 135 LYS 135 135 135 LYS LYS B . n 
B 1 136 SER 136 136 136 SER SER B . n 
B 1 137 GLU 137 137 137 GLU GLU B . n 
B 1 138 GLY 138 138 138 GLY GLY B . n 
B 1 139 LEU 139 139 139 LEU LEU B . n 
B 1 140 ALA 140 140 140 ALA ALA B . n 
B 1 141 VAL 141 141 141 VAL VAL B . n 
B 1 142 LEU 142 142 142 LEU LEU B . n 
B 1 143 ALA 143 143 143 ALA ALA B . n 
B 1 144 VAL 144 144 144 VAL VAL B . n 
B 1 145 LEU 145 145 145 LEU LEU B . n 
B 1 146 ILE 146 146 146 ILE ILE B . n 
B 1 147 GLU 147 147 147 GLU GLU B . n 
B 1 148 MET 148 148 148 MET MET B . n 
B 1 149 GLY 149 149 149 GLY GLY B . n 
B 1 150 SER 150 150 150 SER SER B . n 
B 1 151 PHE 151 151 151 PHE PHE B . n 
B 1 152 ASN 152 152 152 ASN ASN B . n 
B 1 153 PRO 153 153 153 PRO PRO B . n 
B 1 154 SER 154 154 154 SER SER B . n 
B 1 155 TYR 155 155 155 TYR TYR B . n 
B 1 156 ASP 156 156 156 ASP ASP B . n 
B 1 157 LYS 157 157 157 LYS LYS B . n 
B 1 158 ILE 158 158 158 ILE ILE B . n 
B 1 159 PHE 159 159 159 PHE PHE B . n 
B 1 160 SER 160 160 160 SER SER B . n 
B 1 161 HIS 161 161 161 HIS HIS B . n 
B 1 162 LEU 162 162 162 LEU LEU B . n 
B 1 163 GLN 163 163 163 GLN GLN B . n 
B 1 164 HIS 164 164 164 HIS HIS B . n 
B 1 165 VAL 165 165 165 VAL VAL B . n 
B 1 166 LYS 166 166 166 LYS LYS B . n 
B 1 167 TYR 167 167 167 TYR TYR B . n 
B 1 168 LYS 168 168 168 LYS LYS B . n 
B 1 169 GLY 169 169 169 GLY GLY B . n 
B 1 170 GLN 170 170 170 GLN GLN B . n 
B 1 171 GLU 171 171 171 GLU GLU B . n 
B 1 172 ALA 172 172 172 ALA ALA B . n 
B 1 173 PHE 173 173 173 PHE PHE B . n 
B 1 174 VAL 174 174 174 VAL VAL B . n 
B 1 175 PRO 175 175 175 PRO PRO B . n 
B 1 176 GLY 176 176 176 GLY GLY B . n 
B 1 177 PHE 177 177 177 PHE PHE B . n 
B 1 178 ASN 178 178 178 ASN ASN B . n 
B 1 179 ILE 179 179 179 ILE ILE B . n 
B 1 180 GLU 180 180 180 GLU GLU B . n 
B 1 181 GLU 181 181 181 GLU GLU B . n 
B 1 182 LEU 182 182 182 LEU LEU B . n 
B 1 183 LEU 183 183 183 LEU LEU B . n 
B 1 184 PRO 184 184 184 PRO PRO B . n 
B 1 185 GLU 185 185 185 GLU GLU B . n 
B 1 186 ARG 186 186 186 ARG ARG B . n 
B 1 187 THR 187 187 187 THR THR B . n 
B 1 188 ALA 188 188 188 ALA ALA B . n 
B 1 189 GLU 189 189 189 GLU GLU B . n 
B 1 190 TYR 190 190 190 TYR TYR B . n 
B 1 191 TYR 191 191 191 TYR TYR B . n 
B 1 192 ARG 192 192 192 ARG ARG B . n 
B 1 193 TYR 193 193 193 TYR TYR B . n 
B 1 194 ARG 194 194 194 ARG ARG B . n 
B 1 195 GLY 195 195 195 GLY GLY B . n 
B 1 196 SER 196 196 196 SER SER B . n 
B 1 197 LEU 197 197 197 LEU LEU B . n 
B 1 198 THR 198 198 198 THR THR B . n 
B 1 199 THR 199 199 199 THR THR B . n 
B 1 200 PRO 200 200 200 PRO PRO B . n 
B 1 201 PRO 201 201 201 PRO PRO B . n 
B 1 202 CYS 202 202 202 CYS CYS B . n 
B 1 203 ASN 203 203 203 ASN ASN B . n 
B 1 204 PRO 204 204 204 PRO PRO B . n 
B 1 205 THR 205 205 205 THR THR B . n 
B 1 206 VAL 206 206 206 VAL VAL B . n 
B 1 207 LEU 207 207 207 LEU LEU B . n 
B 1 208 TRP 208 208 208 TRP TRP B . n 
B 1 209 THR 209 209 209 THR THR B . n 
B 1 210 VAL 210 210 210 VAL VAL B . n 
B 1 211 PHE 211 211 211 PHE PHE B . n 
B 1 212 ARG 212 212 212 ARG ARG B . n 
B 1 213 ASN 213 213 213 ASN ASN B . n 
B 1 214 PRO 214 214 214 PRO PRO B . n 
B 1 215 VAL 215 215 215 VAL VAL B . n 
B 1 216 GLN 216 216 216 GLN GLN B . n 
B 1 217 ILE 217 217 217 ILE ILE B . n 
B 1 218 SER 218 218 218 SER SER B . n 
B 1 219 GLN 219 219 219 GLN GLN B . n 
B 1 220 GLU 220 220 220 GLU GLU B . n 
B 1 221 GLN 221 221 221 GLN GLN B . n 
B 1 222 LEU 222 222 222 LEU LEU B . n 
B 1 223 LEU 223 223 223 LEU LEU B . n 
B 1 224 ALA 224 224 224 ALA ALA B . n 
B 1 225 LEU 225 225 225 LEU LEU B . n 
B 1 226 GLU 226 226 226 GLU GLU B . n 
B 1 227 THR 227 227 227 THR THR B . n 
B 1 228 ALA 228 228 228 ALA ALA B . n 
B 1 229 LEU 229 229 229 LEU LEU B . n 
B 1 230 TYR 230 230 230 TYR TYR B . n 
B 1 231 CYS 231 231 231 CYS CYS B . n 
B 1 232 THR 232 232 232 THR THR B . n 
B 1 233 HIS 233 233 233 HIS HIS B . n 
B 1 234 MET 234 234 234 MET MET B . n 
B 1 235 ASP 235 235 235 ASP ASP B . n 
B 1 236 ASP 236 236 236 ASP ASP B . n 
B 1 237 PRO 237 237 237 PRO PRO B . n 
B 1 238 SER 238 238 238 SER SER B . n 
B 1 239 PRO 239 239 239 PRO PRO B . n 
B 1 240 ARG 240 240 240 ARG ARG B . n 
B 1 241 GLU 241 241 241 GLU GLU B . n 
B 1 242 MET 242 242 242 MET MET B . n 
B 1 243 ILE 243 243 243 ILE ILE B . n 
B 1 244 ASN 244 244 244 ASN ASN B . n 
B 1 245 ASN 245 245 245 ASN ASN B . n 
B 1 246 PHE 246 246 246 PHE PHE B . n 
B 1 247 ARG 247 247 247 ARG ARG B . n 
B 1 248 GLN 248 248 248 GLN GLN B . n 
B 1 249 VAL 249 249 249 VAL VAL B . n 
B 1 250 GLN 250 250 250 GLN GLN B . n 
B 1 251 LYS 251 251 251 LYS LYS B . n 
B 1 252 PHE 252 252 252 PHE PHE B . n 
B 1 253 ASP 253 253 253 ASP ASP B . n 
B 1 254 GLU 254 254 254 GLU GLU B . n 
B 1 255 ARG 255 255 255 ARG ARG B . n 
B 1 256 LEU 256 256 256 LEU LEU B . n 
B 1 257 VAL 257 257 257 VAL VAL B . n 
B 1 258 TYR 258 258 258 TYR TYR B . n 
B 1 259 THR 259 259 259 THR THR B . n 
B 1 260 SER 260 260 260 SER SER B . n 
B 1 261 PHE 261 261 261 PHE PHE B . n 
B 1 262 SER 262 262 262 SER SER B . n 
B 1 263 GLN 263 263 263 GLN GLN B . n 
C 1 1   MET 1   1   ?   ?   ?   C . n 
C 1 2   SER 2   2   ?   ?   ?   C . n 
C 1 3   LYS 3   3   3   LYS LYS C . n 
C 1 4   TRP 4   4   4   TRP TRP C . n 
C 1 5   THR 5   5   5   THR THR C . n 
C 1 6   TYR 6   6   6   TYR TYR C . n 
C 1 7   PHE 7   7   7   PHE PHE C . n 
C 1 8   GLY 8   8   8   GLY GLY C . n 
C 1 9   PRO 9   9   9   PRO PRO C . n 
C 1 10  ASP 10  10  10  ASP ASP C . n 
C 1 11  GLY 11  11  11  GLY GLY C . n 
C 1 12  GLU 12  12  12  GLU GLU C . n 
C 1 13  ASN 13  13  13  ASN ASN C . n 
C 1 14  SER 14  14  14  SER SER C . n 
C 1 15  TRP 15  15  15  TRP TRP C . n 
C 1 16  SER 16  16  16  SER SER C . n 
C 1 17  LYS 17  17  17  LYS LYS C . n 
C 1 18  LYS 18  18  18  LYS LYS C . n 
C 1 19  TYR 19  19  19  TYR TYR C . n 
C 1 20  PRO 20  20  20  PRO PRO C . n 
C 1 21  SER 21  21  21  SER SER C . n 
C 1 22  CYS 22  22  22  CYS CYS C . n 
C 1 23  GLY 23  23  23  GLY GLY C . n 
C 1 24  GLY 24  24  24  GLY GLY C . n 
C 1 25  LEU 25  25  25  LEU LEU C . n 
C 1 26  LEU 26  26  26  LEU LEU C . n 
C 1 27  GLN 27  27  27  GLN GLN C . n 
C 1 28  SER 28  28  28  SER SER C . n 
C 1 29  PRO 29  29  29  PRO PRO C . n 
C 1 30  ILE 30  30  30  ILE ILE C . n 
C 1 31  ASP 31  31  31  ASP ASP C . n 
C 1 32  LEU 32  32  32  LEU LEU C . n 
C 1 33  HIS 33  33  33  HIS HIS C . n 
C 1 34  SER 34  34  34  SER SER C . n 
C 1 35  ASP 35  35  35  ASP ASP C . n 
C 1 36  ILE 36  36  36  ILE ILE C . n 
C 1 37  LEU 37  37  37  LEU LEU C . n 
C 1 38  GLN 38  38  38  GLN GLN C . n 
C 1 39  TYR 39  39  39  TYR TYR C . n 
C 1 40  ASP 40  40  40  ASP ASP C . n 
C 1 41  ALA 41  41  41  ALA ALA C . n 
C 1 42  SER 42  42  42  SER SER C . n 
C 1 43  LEU 43  43  43  LEU LEU C . n 
C 1 44  THR 44  44  44  THR THR C . n 
C 1 45  PRO 45  45  45  PRO PRO C . n 
C 1 46  LEU 46  46  46  LEU LEU C . n 
C 1 47  GLU 47  47  47  GLU GLU C . n 
C 1 48  PHE 48  48  48  PHE PHE C . n 
C 1 49  GLN 49  49  49  GLN GLN C . n 
C 1 50  GLY 50  50  50  GLY GLY C . n 
C 1 51  TYR 51  51  51  TYR TYR C . n 
C 1 52  ASN 52  52  52  ASN ASN C . n 
C 1 53  LEU 53  53  53  LEU LEU C . n 
C 1 54  SER 54  54  54  SER SER C . n 
C 1 55  ALA 55  55  55  ALA ALA C . n 
C 1 56  ASN 56  56  56  ASN ASN C . n 
C 1 57  LYS 57  57  57  LYS LYS C . n 
C 1 58  GLN 58  58  58  GLN GLN C . n 
C 1 59  PHE 59  59  59  PHE PHE C . n 
C 1 60  LEU 60  60  60  LEU LEU C . n 
C 1 61  LEU 61  61  61  LEU LEU C . n 
C 1 62  THR 62  62  62  THR THR C . n 
C 1 63  ASN 63  63  63  ASN ASN C . n 
C 1 64  ASN 64  64  64  ASN ASN C . n 
C 1 65  GLY 65  65  65  GLY GLY C . n 
C 1 66  HIS 66  66  66  HIS HIS C . n 
C 1 67  SER 67  67  67  SER SER C . n 
C 1 68  VAL 68  68  68  VAL VAL C . n 
C 1 69  LYS 69  69  69  LYS LYS C . n 
C 1 70  LEU 70  70  70  LEU LEU C . n 
C 1 71  ASN 71  71  71  ASN ASN C . n 
C 1 72  LEU 72  72  72  LEU LEU C . n 
C 1 73  PRO 73  73  73  PRO PRO C . n 
C 1 74  SER 74  74  74  SER SER C . n 
C 1 75  ASP 75  75  75  ASP ASP C . n 
C 1 76  MET 76  76  76  MET MET C . n 
C 1 77  HIS 77  77  77  HIS HIS C . n 
C 1 78  ILE 78  78  78  ILE ILE C . n 
C 1 79  GLN 79  79  79  GLN GLN C . n 
C 1 80  GLY 80  80  80  GLY GLY C . n 
C 1 81  LEU 81  81  81  LEU LEU C . n 
C 1 82  GLN 82  82  82  GLN GLN C . n 
C 1 83  SER 83  83  83  SER SER C . n 
C 1 84  ARG 84  84  84  ARG ARG C . n 
C 1 85  TYR 85  85  85  TYR TYR C . n 
C 1 86  SER 86  86  86  SER SER C . n 
C 1 87  ALA 87  87  87  ALA ALA C . n 
C 1 88  THR 88  88  88  THR THR C . n 
C 1 89  GLN 89  89  89  GLN GLN C . n 
C 1 90  LEU 90  90  90  LEU LEU C . n 
C 1 91  HIS 91  91  91  HIS HIS C . n 
C 1 92  LEU 92  92  92  LEU LEU C . n 
C 1 93  HIS 93  93  93  HIS HIS C . n 
C 1 94  TRP 94  94  94  TRP TRP C . n 
C 1 95  GLY 95  95  95  GLY GLY C . n 
C 1 96  ASN 96  96  96  ASN ASN C . n 
C 1 97  PRO 97  97  97  PRO PRO C . n 
C 1 98  ASN 98  98  98  ASN ASN C . n 
C 1 99  ASP 99  99  99  ASP ASP C . n 
C 1 100 PRO 100 100 100 PRO PRO C . n 
C 1 101 HIS 101 101 101 HIS HIS C . n 
C 1 102 GLY 102 102 102 GLY GLY C . n 
C 1 103 SER 103 103 103 SER SER C . n 
C 1 104 GLU 104 104 104 GLU GLU C . n 
C 1 105 HIS 105 105 105 HIS HIS C . n 
C 1 106 THR 106 106 106 THR THR C . n 
C 1 107 VAL 107 107 107 VAL VAL C . n 
C 1 108 SER 108 108 108 SER SER C . n 
C 1 109 GLY 109 109 109 GLY GLY C . n 
C 1 110 GLN 110 110 110 GLN GLN C . n 
C 1 111 HIS 111 111 111 HIS HIS C . n 
C 1 112 PHE 112 112 112 PHE PHE C . n 
C 1 113 ALA 113 113 113 ALA ALA C . n 
C 1 114 ALA 114 114 114 ALA ALA C . n 
C 1 115 GLU 115 115 115 GLU GLU C . n 
C 1 116 LEU 116 116 116 LEU LEU C . n 
C 1 117 HIS 117 117 117 HIS HIS C . n 
C 1 118 ILE 118 118 118 ILE ILE C . n 
C 1 119 VAL 119 119 119 VAL VAL C . n 
C 1 120 HIS 120 120 120 HIS HIS C . n 
C 1 121 TYR 121 121 121 TYR TYR C . n 
C 1 122 ASN 122 122 122 ASN ASN C . n 
C 1 123 SER 123 123 123 SER SER C . n 
C 1 124 ASP 124 124 124 ASP ASP C . n 
C 1 125 LEU 125 125 125 LEU LEU C . n 
C 1 126 TYR 126 126 126 TYR TYR C . n 
C 1 127 PRO 127 127 127 PRO PRO C . n 
C 1 128 ASP 128 128 128 ASP ASP C . n 
C 1 129 ALA 129 129 129 ALA ALA C . n 
C 1 130 SER 130 130 130 SER SER C . n 
C 1 131 THR 131 131 131 THR THR C . n 
C 1 132 ALA 132 132 132 ALA ALA C . n 
C 1 133 SER 133 133 133 SER SER C . n 
C 1 134 ASN 134 134 134 ASN ASN C . n 
C 1 135 LYS 135 135 135 LYS LYS C . n 
C 1 136 SER 136 136 136 SER SER C . n 
C 1 137 GLU 137 137 137 GLU GLU C . n 
C 1 138 GLY 138 138 138 GLY GLY C . n 
C 1 139 LEU 139 139 139 LEU LEU C . n 
C 1 140 ALA 140 140 140 ALA ALA C . n 
C 1 141 VAL 141 141 141 VAL VAL C . n 
C 1 142 LEU 142 142 142 LEU LEU C . n 
C 1 143 ALA 143 143 143 ALA ALA C . n 
C 1 144 VAL 144 144 144 VAL VAL C . n 
C 1 145 LEU 145 145 145 LEU LEU C . n 
C 1 146 ILE 146 146 146 ILE ILE C . n 
C 1 147 GLU 147 147 147 GLU GLU C . n 
C 1 148 MET 148 148 148 MET MET C . n 
C 1 149 GLY 149 149 149 GLY GLY C . n 
C 1 150 SER 150 150 150 SER SER C . n 
C 1 151 PHE 151 151 151 PHE PHE C . n 
C 1 152 ASN 152 152 152 ASN ASN C . n 
C 1 153 PRO 153 153 153 PRO PRO C . n 
C 1 154 SER 154 154 154 SER SER C . n 
C 1 155 TYR 155 155 155 TYR TYR C . n 
C 1 156 ASP 156 156 156 ASP ASP C . n 
C 1 157 LYS 157 157 157 LYS LYS C . n 
C 1 158 ILE 158 158 158 ILE ILE C . n 
C 1 159 PHE 159 159 159 PHE PHE C . n 
C 1 160 SER 160 160 160 SER SER C . n 
C 1 161 HIS 161 161 161 HIS HIS C . n 
C 1 162 LEU 162 162 162 LEU LEU C . n 
C 1 163 GLN 163 163 163 GLN GLN C . n 
C 1 164 HIS 164 164 164 HIS HIS C . n 
C 1 165 VAL 165 165 165 VAL VAL C . n 
C 1 166 LYS 166 166 166 LYS LYS C . n 
C 1 167 TYR 167 167 167 TYR TYR C . n 
C 1 168 LYS 168 168 168 LYS LYS C . n 
C 1 169 GLY 169 169 169 GLY GLY C . n 
C 1 170 GLN 170 170 170 GLN GLN C . n 
C 1 171 GLU 171 171 171 GLU GLU C . n 
C 1 172 ALA 172 172 172 ALA ALA C . n 
C 1 173 PHE 173 173 173 PHE PHE C . n 
C 1 174 VAL 174 174 174 VAL VAL C . n 
C 1 175 PRO 175 175 175 PRO PRO C . n 
C 1 176 GLY 176 176 176 GLY GLY C . n 
C 1 177 PHE 177 177 177 PHE PHE C . n 
C 1 178 ASN 178 178 178 ASN ASN C . n 
C 1 179 ILE 179 179 179 ILE ILE C . n 
C 1 180 GLU 180 180 180 GLU GLU C . n 
C 1 181 GLU 181 181 181 GLU GLU C . n 
C 1 182 LEU 182 182 182 LEU LEU C . n 
C 1 183 LEU 183 183 183 LEU LEU C . n 
C 1 184 PRO 184 184 184 PRO PRO C . n 
C 1 185 GLU 185 185 185 GLU GLU C . n 
C 1 186 ARG 186 186 186 ARG ARG C . n 
C 1 187 THR 187 187 187 THR THR C . n 
C 1 188 ALA 188 188 188 ALA ALA C . n 
C 1 189 GLU 189 189 189 GLU GLU C . n 
C 1 190 TYR 190 190 190 TYR TYR C . n 
C 1 191 TYR 191 191 191 TYR TYR C . n 
C 1 192 ARG 192 192 192 ARG ARG C . n 
C 1 193 TYR 193 193 193 TYR TYR C . n 
C 1 194 ARG 194 194 194 ARG ARG C . n 
C 1 195 GLY 195 195 195 GLY GLY C . n 
C 1 196 SER 196 196 196 SER SER C . n 
C 1 197 LEU 197 197 197 LEU LEU C . n 
C 1 198 THR 198 198 198 THR THR C . n 
C 1 199 THR 199 199 199 THR THR C . n 
C 1 200 PRO 200 200 200 PRO PRO C . n 
C 1 201 PRO 201 201 201 PRO PRO C . n 
C 1 202 CYS 202 202 202 CYS CYS C . n 
C 1 203 ASN 203 203 203 ASN ASN C . n 
C 1 204 PRO 204 204 204 PRO PRO C . n 
C 1 205 THR 205 205 205 THR THR C . n 
C 1 206 VAL 206 206 206 VAL VAL C . n 
C 1 207 LEU 207 207 207 LEU LEU C . n 
C 1 208 TRP 208 208 208 TRP TRP C . n 
C 1 209 THR 209 209 209 THR THR C . n 
C 1 210 VAL 210 210 210 VAL VAL C . n 
C 1 211 PHE 211 211 211 PHE PHE C . n 
C 1 212 ARG 212 212 212 ARG ARG C . n 
C 1 213 ASN 213 213 213 ASN ASN C . n 
C 1 214 PRO 214 214 214 PRO PRO C . n 
C 1 215 VAL 215 215 215 VAL VAL C . n 
C 1 216 GLN 216 216 216 GLN GLN C . n 
C 1 217 ILE 217 217 217 ILE ILE C . n 
C 1 218 SER 218 218 218 SER SER C . n 
C 1 219 GLN 219 219 219 GLN GLN C . n 
C 1 220 GLU 220 220 220 GLU GLU C . n 
C 1 221 GLN 221 221 221 GLN GLN C . n 
C 1 222 LEU 222 222 222 LEU LEU C . n 
C 1 223 LEU 223 223 223 LEU LEU C . n 
C 1 224 ALA 224 224 224 ALA ALA C . n 
C 1 225 LEU 225 225 225 LEU LEU C . n 
C 1 226 GLU 226 226 226 GLU GLU C . n 
C 1 227 THR 227 227 227 THR THR C . n 
C 1 228 ALA 228 228 228 ALA ALA C . n 
C 1 229 LEU 229 229 229 LEU LEU C . n 
C 1 230 TYR 230 230 230 TYR TYR C . n 
C 1 231 CYS 231 231 231 CYS CYS C . n 
C 1 232 THR 232 232 232 THR THR C . n 
C 1 233 HIS 233 233 233 HIS HIS C . n 
C 1 234 MET 234 234 234 MET MET C . n 
C 1 235 ASP 235 235 235 ASP ASP C . n 
C 1 236 ASP 236 236 236 ASP ASP C . n 
C 1 237 PRO 237 237 237 PRO PRO C . n 
C 1 238 SER 238 238 238 SER SER C . n 
C 1 239 PRO 239 239 239 PRO PRO C . n 
C 1 240 ARG 240 240 240 ARG ARG C . n 
C 1 241 GLU 241 241 241 GLU GLU C . n 
C 1 242 MET 242 242 242 MET MET C . n 
C 1 243 ILE 243 243 243 ILE ILE C . n 
C 1 244 ASN 244 244 244 ASN ASN C . n 
C 1 245 ASN 245 245 245 ASN ASN C . n 
C 1 246 PHE 246 246 246 PHE PHE C . n 
C 1 247 ARG 247 247 247 ARG ARG C . n 
C 1 248 GLN 248 248 248 GLN GLN C . n 
C 1 249 VAL 249 249 249 VAL VAL C . n 
C 1 250 GLN 250 250 250 GLN GLN C . n 
C 1 251 LYS 251 251 251 LYS LYS C . n 
C 1 252 PHE 252 252 252 PHE PHE C . n 
C 1 253 ASP 253 253 253 ASP ASP C . n 
C 1 254 GLU 254 254 254 GLU GLU C . n 
C 1 255 ARG 255 255 255 ARG ARG C . n 
C 1 256 LEU 256 256 256 LEU LEU C . n 
C 1 257 VAL 257 257 257 VAL VAL C . n 
C 1 258 TYR 258 258 258 TYR TYR C . n 
C 1 259 THR 259 259 259 THR THR C . n 
C 1 260 SER 260 260 260 SER SER C . n 
C 1 261 PHE 261 261 261 PHE PHE C . n 
C 1 262 SER 262 262 262 SER SER C . n 
C 1 263 GLN 263 263 263 GLN GLN C . n 
D 1 1   MET 1   1   ?   ?   ?   D . n 
D 1 2   SER 2   2   ?   ?   ?   D . n 
D 1 3   LYS 3   3   3   LYS LYS D . n 
D 1 4   TRP 4   4   4   TRP TRP D . n 
D 1 5   THR 5   5   5   THR THR D . n 
D 1 6   TYR 6   6   6   TYR TYR D . n 
D 1 7   PHE 7   7   7   PHE PHE D . n 
D 1 8   GLY 8   8   8   GLY GLY D . n 
D 1 9   PRO 9   9   9   PRO PRO D . n 
D 1 10  ASP 10  10  10  ASP ASP D . n 
D 1 11  GLY 11  11  11  GLY GLY D . n 
D 1 12  GLU 12  12  12  GLU GLU D . n 
D 1 13  ASN 13  13  13  ASN ASN D . n 
D 1 14  SER 14  14  14  SER SER D . n 
D 1 15  TRP 15  15  15  TRP TRP D . n 
D 1 16  SER 16  16  16  SER SER D . n 
D 1 17  LYS 17  17  17  LYS LYS D . n 
D 1 18  LYS 18  18  18  LYS LYS D . n 
D 1 19  TYR 19  19  19  TYR TYR D . n 
D 1 20  PRO 20  20  20  PRO PRO D . n 
D 1 21  SER 21  21  21  SER SER D . n 
D 1 22  CYS 22  22  22  CYS CYS D . n 
D 1 23  GLY 23  23  23  GLY GLY D . n 
D 1 24  GLY 24  24  24  GLY GLY D . n 
D 1 25  LEU 25  25  25  LEU LEU D . n 
D 1 26  LEU 26  26  26  LEU LEU D . n 
D 1 27  GLN 27  27  27  GLN GLN D . n 
D 1 28  SER 28  28  28  SER SER D . n 
D 1 29  PRO 29  29  29  PRO PRO D . n 
D 1 30  ILE 30  30  30  ILE ILE D . n 
D 1 31  ASP 31  31  31  ASP ASP D . n 
D 1 32  LEU 32  32  32  LEU LEU D . n 
D 1 33  HIS 33  33  33  HIS HIS D . n 
D 1 34  SER 34  34  34  SER SER D . n 
D 1 35  ASP 35  35  35  ASP ASP D . n 
D 1 36  ILE 36  36  36  ILE ILE D . n 
D 1 37  LEU 37  37  37  LEU LEU D . n 
D 1 38  GLN 38  38  38  GLN GLN D . n 
D 1 39  TYR 39  39  39  TYR TYR D . n 
D 1 40  ASP 40  40  40  ASP ASP D . n 
D 1 41  ALA 41  41  41  ALA ALA D . n 
D 1 42  SER 42  42  42  SER SER D . n 
D 1 43  LEU 43  43  43  LEU LEU D . n 
D 1 44  THR 44  44  44  THR THR D . n 
D 1 45  PRO 45  45  45  PRO PRO D . n 
D 1 46  LEU 46  46  46  LEU LEU D . n 
D 1 47  GLU 47  47  47  GLU GLU D . n 
D 1 48  PHE 48  48  48  PHE PHE D . n 
D 1 49  GLN 49  49  49  GLN GLN D . n 
D 1 50  GLY 50  50  50  GLY GLY D . n 
D 1 51  TYR 51  51  51  TYR TYR D . n 
D 1 52  ASN 52  52  52  ASN ASN D . n 
D 1 53  LEU 53  53  53  LEU LEU D . n 
D 1 54  SER 54  54  54  SER SER D . n 
D 1 55  ALA 55  55  55  ALA ALA D . n 
D 1 56  ASN 56  56  56  ASN ASN D . n 
D 1 57  LYS 57  57  57  LYS LYS D . n 
D 1 58  GLN 58  58  58  GLN GLN D . n 
D 1 59  PHE 59  59  59  PHE PHE D . n 
D 1 60  LEU 60  60  60  LEU LEU D . n 
D 1 61  LEU 61  61  61  LEU LEU D . n 
D 1 62  THR 62  62  62  THR THR D . n 
D 1 63  ASN 63  63  63  ASN ASN D . n 
D 1 64  ASN 64  64  64  ASN ASN D . n 
D 1 65  GLY 65  65  65  GLY GLY D . n 
D 1 66  HIS 66  66  66  HIS HIS D . n 
D 1 67  SER 67  67  67  SER SER D . n 
D 1 68  VAL 68  68  68  VAL VAL D . n 
D 1 69  LYS 69  69  69  LYS LYS D . n 
D 1 70  LEU 70  70  70  LEU LEU D . n 
D 1 71  ASN 71  71  71  ASN ASN D . n 
D 1 72  LEU 72  72  72  LEU LEU D . n 
D 1 73  PRO 73  73  73  PRO PRO D . n 
D 1 74  SER 74  74  74  SER SER D . n 
D 1 75  ASP 75  75  75  ASP ASP D . n 
D 1 76  MET 76  76  76  MET MET D . n 
D 1 77  HIS 77  77  77  HIS HIS D . n 
D 1 78  ILE 78  78  78  ILE ILE D . n 
D 1 79  GLN 79  79  79  GLN GLN D . n 
D 1 80  GLY 80  80  80  GLY GLY D . n 
D 1 81  LEU 81  81  81  LEU LEU D . n 
D 1 82  GLN 82  82  82  GLN GLN D . n 
D 1 83  SER 83  83  83  SER SER D . n 
D 1 84  ARG 84  84  84  ARG ARG D . n 
D 1 85  TYR 85  85  85  TYR TYR D . n 
D 1 86  SER 86  86  86  SER SER D . n 
D 1 87  ALA 87  87  87  ALA ALA D . n 
D 1 88  THR 88  88  88  THR THR D . n 
D 1 89  GLN 89  89  89  GLN GLN D . n 
D 1 90  LEU 90  90  90  LEU LEU D . n 
D 1 91  HIS 91  91  91  HIS HIS D . n 
D 1 92  LEU 92  92  92  LEU LEU D . n 
D 1 93  HIS 93  93  93  HIS HIS D . n 
D 1 94  TRP 94  94  94  TRP TRP D . n 
D 1 95  GLY 95  95  95  GLY GLY D . n 
D 1 96  ASN 96  96  96  ASN ASN D . n 
D 1 97  PRO 97  97  97  PRO PRO D . n 
D 1 98  ASN 98  98  98  ASN ASN D . n 
D 1 99  ASP 99  99  99  ASP ASP D . n 
D 1 100 PRO 100 100 100 PRO PRO D . n 
D 1 101 HIS 101 101 101 HIS HIS D . n 
D 1 102 GLY 102 102 102 GLY GLY D . n 
D 1 103 SER 103 103 103 SER SER D . n 
D 1 104 GLU 104 104 104 GLU GLU D . n 
D 1 105 HIS 105 105 105 HIS HIS D . n 
D 1 106 THR 106 106 106 THR THR D . n 
D 1 107 VAL 107 107 107 VAL VAL D . n 
D 1 108 SER 108 108 108 SER SER D . n 
D 1 109 GLY 109 109 109 GLY GLY D . n 
D 1 110 GLN 110 110 110 GLN GLN D . n 
D 1 111 HIS 111 111 111 HIS HIS D . n 
D 1 112 PHE 112 112 112 PHE PHE D . n 
D 1 113 ALA 113 113 113 ALA ALA D . n 
D 1 114 ALA 114 114 114 ALA ALA D . n 
D 1 115 GLU 115 115 115 GLU GLU D . n 
D 1 116 LEU 116 116 116 LEU LEU D . n 
D 1 117 HIS 117 117 117 HIS HIS D . n 
D 1 118 ILE 118 118 118 ILE ILE D . n 
D 1 119 VAL 119 119 119 VAL VAL D . n 
D 1 120 HIS 120 120 120 HIS HIS D . n 
D 1 121 TYR 121 121 121 TYR TYR D . n 
D 1 122 ASN 122 122 122 ASN ASN D . n 
D 1 123 SER 123 123 123 SER SER D . n 
D 1 124 ASP 124 124 124 ASP ASP D . n 
D 1 125 LEU 125 125 125 LEU LEU D . n 
D 1 126 TYR 126 126 126 TYR TYR D . n 
D 1 127 PRO 127 127 127 PRO PRO D . n 
D 1 128 ASP 128 128 128 ASP ASP D . n 
D 1 129 ALA 129 129 129 ALA ALA D . n 
D 1 130 SER 130 130 130 SER SER D . n 
D 1 131 THR 131 131 131 THR THR D . n 
D 1 132 ALA 132 132 132 ALA ALA D . n 
D 1 133 SER 133 133 133 SER SER D . n 
D 1 134 ASN 134 134 134 ASN ASN D . n 
D 1 135 LYS 135 135 135 LYS LYS D . n 
D 1 136 SER 136 136 136 SER SER D . n 
D 1 137 GLU 137 137 137 GLU GLU D . n 
D 1 138 GLY 138 138 138 GLY GLY D . n 
D 1 139 LEU 139 139 139 LEU LEU D . n 
D 1 140 ALA 140 140 140 ALA ALA D . n 
D 1 141 VAL 141 141 141 VAL VAL D . n 
D 1 142 LEU 142 142 142 LEU LEU D . n 
D 1 143 ALA 143 143 143 ALA ALA D . n 
D 1 144 VAL 144 144 144 VAL VAL D . n 
D 1 145 LEU 145 145 145 LEU LEU D . n 
D 1 146 ILE 146 146 146 ILE ILE D . n 
D 1 147 GLU 147 147 147 GLU GLU D . n 
D 1 148 MET 148 148 148 MET MET D . n 
D 1 149 GLY 149 149 149 GLY GLY D . n 
D 1 150 SER 150 150 150 SER SER D . n 
D 1 151 PHE 151 151 151 PHE PHE D . n 
D 1 152 ASN 152 152 152 ASN ASN D . n 
D 1 153 PRO 153 153 153 PRO PRO D . n 
D 1 154 SER 154 154 154 SER SER D . n 
D 1 155 TYR 155 155 155 TYR TYR D . n 
D 1 156 ASP 156 156 156 ASP ASP D . n 
D 1 157 LYS 157 157 157 LYS LYS D . n 
D 1 158 ILE 158 158 158 ILE ILE D . n 
D 1 159 PHE 159 159 159 PHE PHE D . n 
D 1 160 SER 160 160 160 SER SER D . n 
D 1 161 HIS 161 161 161 HIS HIS D . n 
D 1 162 LEU 162 162 162 LEU LEU D . n 
D 1 163 GLN 163 163 163 GLN GLN D . n 
D 1 164 HIS 164 164 164 HIS HIS D . n 
D 1 165 VAL 165 165 165 VAL VAL D . n 
D 1 166 LYS 166 166 166 LYS LYS D . n 
D 1 167 TYR 167 167 167 TYR TYR D . n 
D 1 168 LYS 168 168 168 LYS LYS D . n 
D 1 169 GLY 169 169 169 GLY GLY D . n 
D 1 170 GLN 170 170 170 GLN GLN D . n 
D 1 171 GLU 171 171 171 GLU GLU D . n 
D 1 172 ALA 172 172 172 ALA ALA D . n 
D 1 173 PHE 173 173 173 PHE PHE D . n 
D 1 174 VAL 174 174 174 VAL VAL D . n 
D 1 175 PRO 175 175 175 PRO PRO D . n 
D 1 176 GLY 176 176 176 GLY GLY D . n 
D 1 177 PHE 177 177 177 PHE PHE D . n 
D 1 178 ASN 178 178 178 ASN ASN D . n 
D 1 179 ILE 179 179 179 ILE ILE D . n 
D 1 180 GLU 180 180 180 GLU GLU D . n 
D 1 181 GLU 181 181 181 GLU GLU D . n 
D 1 182 LEU 182 182 182 LEU LEU D . n 
D 1 183 LEU 183 183 183 LEU LEU D . n 
D 1 184 PRO 184 184 184 PRO PRO D . n 
D 1 185 GLU 185 185 185 GLU GLU D . n 
D 1 186 ARG 186 186 186 ARG ARG D . n 
D 1 187 THR 187 187 187 THR THR D . n 
D 1 188 ALA 188 188 188 ALA ALA D . n 
D 1 189 GLU 189 189 189 GLU GLU D . n 
D 1 190 TYR 190 190 190 TYR TYR D . n 
D 1 191 TYR 191 191 191 TYR TYR D . n 
D 1 192 ARG 192 192 192 ARG ARG D . n 
D 1 193 TYR 193 193 193 TYR TYR D . n 
D 1 194 ARG 194 194 194 ARG ARG D . n 
D 1 195 GLY 195 195 195 GLY GLY D . n 
D 1 196 SER 196 196 196 SER SER D . n 
D 1 197 LEU 197 197 197 LEU LEU D . n 
D 1 198 THR 198 198 198 THR THR D . n 
D 1 199 THR 199 199 199 THR THR D . n 
D 1 200 PRO 200 200 200 PRO PRO D . n 
D 1 201 PRO 201 201 201 PRO PRO D . n 
D 1 202 CYS 202 202 202 CYS CYS D . n 
D 1 203 ASN 203 203 203 ASN ASN D . n 
D 1 204 PRO 204 204 204 PRO PRO D . n 
D 1 205 THR 205 205 205 THR THR D . n 
D 1 206 VAL 206 206 206 VAL VAL D . n 
D 1 207 LEU 207 207 207 LEU LEU D . n 
D 1 208 TRP 208 208 208 TRP TRP D . n 
D 1 209 THR 209 209 209 THR THR D . n 
D 1 210 VAL 210 210 210 VAL VAL D . n 
D 1 211 PHE 211 211 211 PHE PHE D . n 
D 1 212 ARG 212 212 212 ARG ARG D . n 
D 1 213 ASN 213 213 213 ASN ASN D . n 
D 1 214 PRO 214 214 214 PRO PRO D . n 
D 1 215 VAL 215 215 215 VAL VAL D . n 
D 1 216 GLN 216 216 216 GLN GLN D . n 
D 1 217 ILE 217 217 217 ILE ILE D . n 
D 1 218 SER 218 218 218 SER SER D . n 
D 1 219 GLN 219 219 219 GLN GLN D . n 
D 1 220 GLU 220 220 220 GLU GLU D . n 
D 1 221 GLN 221 221 221 GLN GLN D . n 
D 1 222 LEU 222 222 222 LEU LEU D . n 
D 1 223 LEU 223 223 223 LEU LEU D . n 
D 1 224 ALA 224 224 224 ALA ALA D . n 
D 1 225 LEU 225 225 225 LEU LEU D . n 
D 1 226 GLU 226 226 226 GLU GLU D . n 
D 1 227 THR 227 227 227 THR THR D . n 
D 1 228 ALA 228 228 228 ALA ALA D . n 
D 1 229 LEU 229 229 229 LEU LEU D . n 
D 1 230 TYR 230 230 230 TYR TYR D . n 
D 1 231 CYS 231 231 231 CYS CYS D . n 
D 1 232 THR 232 232 232 THR THR D . n 
D 1 233 HIS 233 233 233 HIS HIS D . n 
D 1 234 MET 234 234 234 MET MET D . n 
D 1 235 ASP 235 235 235 ASP ASP D . n 
D 1 236 ASP 236 236 236 ASP ASP D . n 
D 1 237 PRO 237 237 237 PRO PRO D . n 
D 1 238 SER 238 238 238 SER SER D . n 
D 1 239 PRO 239 239 239 PRO PRO D . n 
D 1 240 ARG 240 240 240 ARG ARG D . n 
D 1 241 GLU 241 241 241 GLU GLU D . n 
D 1 242 MET 242 242 242 MET MET D . n 
D 1 243 ILE 243 243 243 ILE ILE D . n 
D 1 244 ASN 244 244 244 ASN ASN D . n 
D 1 245 ASN 245 245 245 ASN ASN D . n 
D 1 246 PHE 246 246 246 PHE PHE D . n 
D 1 247 ARG 247 247 247 ARG ARG D . n 
D 1 248 GLN 248 248 248 GLN GLN D . n 
D 1 249 VAL 249 249 249 VAL VAL D . n 
D 1 250 GLN 250 250 250 GLN GLN D . n 
D 1 251 LYS 251 251 251 LYS LYS D . n 
D 1 252 PHE 252 252 252 PHE PHE D . n 
D 1 253 ASP 253 253 253 ASP ASP D . n 
D 1 254 GLU 254 254 254 GLU GLU D . n 
D 1 255 ARG 255 255 255 ARG ARG D . n 
D 1 256 LEU 256 256 256 LEU LEU D . n 
D 1 257 VAL 257 257 257 VAL VAL D . n 
D 1 258 TYR 258 258 258 TYR TYR D . n 
D 1 259 THR 259 259 259 THR THR D . n 
D 1 260 SER 260 260 260 SER SER D . n 
D 1 261 PHE 261 261 261 PHE PHE D . n 
D 1 262 SER 262 262 262 SER SER D . n 
D 1 263 GLN 263 263 ?   ?   ?   D . 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 
E  2 ZN  1   301 1   ZN  ZN  A . 
F  3 EDO 1   302 1   EDO EDO A . 
G  3 EDO 1   303 7   EDO EDO A . 
H  3 EDO 1   304 9   EDO EDO A . 
I  4 VD9 1   305 1   VD9 VD9 A . 
J  2 ZN  1   301 2   ZN  ZN  B . 
K  3 EDO 1   302 2   EDO EDO B . 
L  3 EDO 1   303 5   EDO EDO B . 
M  3 EDO 1   304 6   EDO EDO B . 
N  3 EDO 1   305 8   EDO EDO B . 
O  3 EDO 1   306 10  EDO EDO B . 
P  3 EDO 1   307 11  EDO EDO B . 
Q  4 VD9 1   308 2   VD9 VD9 B . 
R  2 ZN  1   301 3   ZN  ZN  C . 
S  3 EDO 1   302 3   EDO EDO C . 
T  3 EDO 1   303 12  EDO EDO C . 
U  4 VD9 1   304 3   VD9 VD9 C . 
V  2 ZN  1   301 4   ZN  ZN  D . 
W  3 EDO 1   302 4   EDO EDO D . 
X  3 EDO 1   303 13  EDO EDO D . 
Y  4 VD9 1   304 4   VD9 VD9 D . 
Z  5 HOH 1   401 440 HOH HOH A . 
Z  5 HOH 2   402 758 HOH HOH A . 
Z  5 HOH 3   403 364 HOH HOH A . 
Z  5 HOH 4   404 335 HOH HOH A . 
Z  5 HOH 5   405 455 HOH HOH A . 
Z  5 HOH 6   406 666 HOH HOH A . 
Z  5 HOH 7   407 757 HOH HOH A . 
Z  5 HOH 8   408 420 HOH HOH A . 
Z  5 HOH 9   409 23  HOH HOH A . 
Z  5 HOH 10  410 398 HOH HOH A . 
Z  5 HOH 11  411 170 HOH HOH A . 
Z  5 HOH 12  412 247 HOH HOH A . 
Z  5 HOH 13  413 803 HOH HOH A . 
Z  5 HOH 14  414 237 HOH HOH A . 
Z  5 HOH 15  415 732 HOH HOH A . 
Z  5 HOH 16  416 904 HOH HOH A . 
Z  5 HOH 17  417 468 HOH HOH A . 
Z  5 HOH 18  418 671 HOH HOH A . 
Z  5 HOH 19  419 435 HOH HOH A . 
Z  5 HOH 20  420 731 HOH HOH A . 
Z  5 HOH 21  421 664 HOH HOH A . 
Z  5 HOH 22  422 846 HOH HOH A . 
Z  5 HOH 23  423 839 HOH HOH A . 
Z  5 HOH 24  424 367 HOH HOH A . 
Z  5 HOH 25  425 505 HOH HOH A . 
Z  5 HOH 26  426 423 HOH HOH A . 
Z  5 HOH 27  427 786 HOH HOH A . 
Z  5 HOH 28  428 432 HOH HOH A . 
Z  5 HOH 29  429 305 HOH HOH A . 
Z  5 HOH 30  430 752 HOH HOH A . 
Z  5 HOH 31  431 402 HOH HOH A . 
Z  5 HOH 32  432 653 HOH HOH A . 
Z  5 HOH 33  433 429 HOH HOH A . 
Z  5 HOH 34  434 570 HOH HOH A . 
Z  5 HOH 35  435 842 HOH HOH A . 
Z  5 HOH 36  436 10  HOH HOH A . 
Z  5 HOH 37  437 12  HOH HOH A . 
Z  5 HOH 38  438 14  HOH HOH A . 
Z  5 HOH 39  439 15  HOH HOH A . 
Z  5 HOH 40  440 21  HOH HOH A . 
Z  5 HOH 41  441 25  HOH HOH A . 
Z  5 HOH 42  442 32  HOH HOH A . 
Z  5 HOH 43  443 34  HOH HOH A . 
Z  5 HOH 44  444 35  HOH HOH A . 
Z  5 HOH 45  445 38  HOH HOH A . 
Z  5 HOH 46  446 43  HOH HOH A . 
Z  5 HOH 47  447 48  HOH HOH A . 
Z  5 HOH 48  448 49  HOH HOH A . 
Z  5 HOH 49  449 58  HOH HOH A . 
Z  5 HOH 50  450 61  HOH HOH A . 
Z  5 HOH 51  451 66  HOH HOH A . 
Z  5 HOH 52  452 69  HOH HOH A . 
Z  5 HOH 53  453 73  HOH HOH A . 
Z  5 HOH 54  454 74  HOH HOH A . 
Z  5 HOH 55  455 80  HOH HOH A . 
Z  5 HOH 56  456 96  HOH HOH A . 
Z  5 HOH 57  457 98  HOH HOH A . 
Z  5 HOH 58  458 101 HOH HOH A . 
Z  5 HOH 59  459 104 HOH HOH A . 
Z  5 HOH 60  460 106 HOH HOH A . 
Z  5 HOH 61  461 108 HOH HOH A . 
Z  5 HOH 62  462 113 HOH HOH A . 
Z  5 HOH 63  463 114 HOH HOH A . 
Z  5 HOH 64  464 115 HOH HOH A . 
Z  5 HOH 65  465 119 HOH HOH A . 
Z  5 HOH 66  466 122 HOH HOH A . 
Z  5 HOH 67  467 126 HOH HOH A . 
Z  5 HOH 68  468 130 HOH HOH A . 
Z  5 HOH 69  469 139 HOH HOH A . 
Z  5 HOH 70  470 141 HOH HOH A . 
Z  5 HOH 71  471 150 HOH HOH A . 
Z  5 HOH 72  472 152 HOH HOH A . 
Z  5 HOH 73  473 158 HOH HOH A . 
Z  5 HOH 74  474 167 HOH HOH A . 
Z  5 HOH 75  475 174 HOH HOH A . 
Z  5 HOH 76  476 177 HOH HOH A . 
Z  5 HOH 77  477 183 HOH HOH A . 
Z  5 HOH 78  478 185 HOH HOH A . 
Z  5 HOH 79  479 195 HOH HOH A . 
Z  5 HOH 80  480 197 HOH HOH A . 
Z  5 HOH 81  481 200 HOH HOH A . 
Z  5 HOH 82  482 201 HOH HOH A . 
Z  5 HOH 83  483 207 HOH HOH A . 
Z  5 HOH 84  484 213 HOH HOH A . 
Z  5 HOH 85  485 214 HOH HOH A . 
Z  5 HOH 86  486 215 HOH HOH A . 
Z  5 HOH 87  487 223 HOH HOH A . 
Z  5 HOH 88  488 227 HOH HOH A . 
Z  5 HOH 89  489 228 HOH HOH A . 
Z  5 HOH 90  490 229 HOH HOH A . 
Z  5 HOH 91  491 239 HOH HOH A . 
Z  5 HOH 92  492 261 HOH HOH A . 
Z  5 HOH 93  493 264 HOH HOH A . 
Z  5 HOH 94  494 265 HOH HOH A . 
Z  5 HOH 95  495 269 HOH HOH A . 
Z  5 HOH 96  496 270 HOH HOH A . 
Z  5 HOH 97  497 272 HOH HOH A . 
Z  5 HOH 98  498 274 HOH HOH A . 
Z  5 HOH 99  499 281 HOH HOH A . 
Z  5 HOH 100 500 287 HOH HOH A . 
Z  5 HOH 101 501 293 HOH HOH A . 
Z  5 HOH 102 502 294 HOH HOH A . 
Z  5 HOH 103 503 296 HOH HOH A . 
Z  5 HOH 104 504 300 HOH HOH A . 
Z  5 HOH 105 505 303 HOH HOH A . 
Z  5 HOH 106 506 309 HOH HOH A . 
Z  5 HOH 107 507 324 HOH HOH A . 
Z  5 HOH 108 508 329 HOH HOH A . 
Z  5 HOH 109 509 330 HOH HOH A . 
Z  5 HOH 110 510 331 HOH HOH A . 
Z  5 HOH 111 511 338 HOH HOH A . 
Z  5 HOH 112 512 339 HOH HOH A . 
Z  5 HOH 113 513 341 HOH HOH A . 
Z  5 HOH 114 514 345 HOH HOH A . 
Z  5 HOH 115 515 356 HOH HOH A . 
Z  5 HOH 116 516 357 HOH HOH A . 
Z  5 HOH 117 517 369 HOH HOH A . 
Z  5 HOH 118 518 374 HOH HOH A . 
Z  5 HOH 119 519 377 HOH HOH A . 
Z  5 HOH 120 520 380 HOH HOH A . 
Z  5 HOH 121 521 381 HOH HOH A . 
Z  5 HOH 122 522 382 HOH HOH A . 
Z  5 HOH 123 523 386 HOH HOH A . 
Z  5 HOH 124 524 390 HOH HOH A . 
Z  5 HOH 125 525 391 HOH HOH A . 
Z  5 HOH 126 526 395 HOH HOH A . 
Z  5 HOH 127 527 405 HOH HOH A . 
Z  5 HOH 128 528 406 HOH HOH A . 
Z  5 HOH 129 529 407 HOH HOH A . 
Z  5 HOH 130 530 431 HOH HOH A . 
Z  5 HOH 131 531 442 HOH HOH A . 
Z  5 HOH 132 532 443 HOH HOH A . 
Z  5 HOH 133 533 445 HOH HOH A . 
Z  5 HOH 134 534 451 HOH HOH A . 
Z  5 HOH 135 535 452 HOH HOH A . 
Z  5 HOH 136 536 461 HOH HOH A . 
Z  5 HOH 137 537 465 HOH HOH A . 
Z  5 HOH 138 538 475 HOH HOH A . 
Z  5 HOH 139 539 484 HOH HOH A . 
Z  5 HOH 140 540 485 HOH HOH A . 
Z  5 HOH 141 541 489 HOH HOH A . 
Z  5 HOH 142 542 494 HOH HOH A . 
Z  5 HOH 143 543 529 HOH HOH A . 
Z  5 HOH 144 544 532 HOH HOH A . 
Z  5 HOH 145 545 535 HOH HOH A . 
Z  5 HOH 146 546 544 HOH HOH A . 
Z  5 HOH 147 547 550 HOH HOH A . 
Z  5 HOH 148 548 555 HOH HOH A . 
Z  5 HOH 149 549 557 HOH HOH A . 
Z  5 HOH 150 550 558 HOH HOH A . 
Z  5 HOH 151 551 559 HOH HOH A . 
Z  5 HOH 152 552 562 HOH HOH A . 
Z  5 HOH 153 553 566 HOH HOH A . 
Z  5 HOH 154 554 579 HOH HOH A . 
Z  5 HOH 155 555 587 HOH HOH A . 
Z  5 HOH 156 556 588 HOH HOH A . 
Z  5 HOH 157 557 596 HOH HOH A . 
Z  5 HOH 158 558 602 HOH HOH A . 
Z  5 HOH 159 559 616 HOH HOH A . 
Z  5 HOH 160 560 623 HOH HOH A . 
Z  5 HOH 161 561 628 HOH HOH A . 
Z  5 HOH 162 562 630 HOH HOH A . 
Z  5 HOH 163 563 633 HOH HOH A . 
Z  5 HOH 164 564 636 HOH HOH A . 
Z  5 HOH 165 565 638 HOH HOH A . 
Z  5 HOH 166 566 641 HOH HOH A . 
Z  5 HOH 167 567 645 HOH HOH A . 
Z  5 HOH 168 568 650 HOH HOH A . 
Z  5 HOH 169 569 656 HOH HOH A . 
Z  5 HOH 170 570 665 HOH HOH A . 
Z  5 HOH 171 571 669 HOH HOH A . 
Z  5 HOH 172 572 670 HOH HOH A . 
Z  5 HOH 173 573 673 HOH HOH A . 
Z  5 HOH 174 574 684 HOH HOH A . 
Z  5 HOH 175 575 685 HOH HOH A . 
Z  5 HOH 176 576 689 HOH HOH A . 
Z  5 HOH 177 577 691 HOH HOH A . 
Z  5 HOH 178 578 697 HOH HOH A . 
Z  5 HOH 179 579 699 HOH HOH A . 
Z  5 HOH 180 580 701 HOH HOH A . 
Z  5 HOH 181 581 706 HOH HOH A . 
Z  5 HOH 182 582 707 HOH HOH A . 
Z  5 HOH 183 583 708 HOH HOH A . 
Z  5 HOH 184 584 725 HOH HOH A . 
Z  5 HOH 185 585 744 HOH HOH A . 
Z  5 HOH 186 586 749 HOH HOH A . 
Z  5 HOH 187 587 753 HOH HOH A . 
Z  5 HOH 188 588 765 HOH HOH A . 
Z  5 HOH 189 589 770 HOH HOH A . 
Z  5 HOH 190 590 779 HOH HOH A . 
Z  5 HOH 191 591 782 HOH HOH A . 
Z  5 HOH 192 592 784 HOH HOH A . 
Z  5 HOH 193 593 787 HOH HOH A . 
Z  5 HOH 194 594 795 HOH HOH A . 
Z  5 HOH 195 595 797 HOH HOH A . 
Z  5 HOH 196 596 798 HOH HOH A . 
Z  5 HOH 197 597 811 HOH HOH A . 
Z  5 HOH 198 598 816 HOH HOH A . 
Z  5 HOH 199 599 818 HOH HOH A . 
Z  5 HOH 200 600 819 HOH HOH A . 
Z  5 HOH 201 601 834 HOH HOH A . 
Z  5 HOH 202 602 836 HOH HOH A . 
Z  5 HOH 203 603 837 HOH HOH A . 
Z  5 HOH 204 604 838 HOH HOH A . 
Z  5 HOH 205 605 840 HOH HOH A . 
Z  5 HOH 206 606 841 HOH HOH A . 
Z  5 HOH 207 607 848 HOH HOH A . 
Z  5 HOH 208 608 849 HOH HOH A . 
Z  5 HOH 209 609 852 HOH HOH A . 
Z  5 HOH 210 610 853 HOH HOH A . 
Z  5 HOH 211 611 856 HOH HOH A . 
Z  5 HOH 212 612 857 HOH HOH A . 
Z  5 HOH 213 613 858 HOH HOH A . 
Z  5 HOH 214 614 896 HOH HOH A . 
Z  5 HOH 215 615 897 HOH HOH A . 
Z  5 HOH 216 616 901 HOH HOH A . 
Z  5 HOH 217 617 903 HOH HOH A . 
Z  5 HOH 218 618 905 HOH HOH A . 
Z  5 HOH 219 619 906 HOH HOH A . 
AA 5 HOH 1   401 762 HOH HOH B . 
AA 5 HOH 2   402 523 HOH HOH B . 
AA 5 HOH 3   403 756 HOH HOH B . 
AA 5 HOH 4   404 773 HOH HOH B . 
AA 5 HOH 5   405 308 HOH HOH B . 
AA 5 HOH 6   406 624 HOH HOH B . 
AA 5 HOH 7   407 680 HOH HOH B . 
AA 5 HOH 8   408 617 HOH HOH B . 
AA 5 HOH 9   409 326 HOH HOH B . 
AA 5 HOH 10  410 541 HOH HOH B . 
AA 5 HOH 11  411 844 HOH HOH B . 
AA 5 HOH 12  412 569 HOH HOH B . 
AA 5 HOH 13  413 151 HOH HOH B . 
AA 5 HOH 14  414 730 HOH HOH B . 
AA 5 HOH 15  415 291 HOH HOH B . 
AA 5 HOH 16  416 248 HOH HOH B . 
AA 5 HOH 17  417 655 HOH HOH B . 
AA 5 HOH 18  418 909 HOH HOH B . 
AA 5 HOH 19  419 19  HOH HOH B . 
AA 5 HOH 20  420 528 HOH HOH B . 
AA 5 HOH 21  421 411 HOH HOH B . 
AA 5 HOH 22  422 543 HOH HOH B . 
AA 5 HOH 23  423 190 HOH HOH B . 
AA 5 HOH 24  424 625 HOH HOH B . 
AA 5 HOH 25  425 393 HOH HOH B . 
AA 5 HOH 26  426 37  HOH HOH B . 
AA 5 HOH 27  427 908 HOH HOH B . 
AA 5 HOH 28  428 370 HOH HOH B . 
AA 5 HOH 29  429 698 HOH HOH B . 
AA 5 HOH 30  430 346 HOH HOH B . 
AA 5 HOH 31  431 304 HOH HOH B . 
AA 5 HOH 32  432 715 HOH HOH B . 
AA 5 HOH 33  433 536 HOH HOH B . 
AA 5 HOH 34  434 257 HOH HOH B . 
AA 5 HOH 35  435 537 HOH HOH B . 
AA 5 HOH 36  436 647 HOH HOH B . 
AA 5 HOH 37  437 530 HOH HOH B . 
AA 5 HOH 38  438 516 HOH HOH B . 
AA 5 HOH 39  439 315 HOH HOH B . 
AA 5 HOH 40  440 129 HOH HOH B . 
AA 5 HOH 41  441 383 HOH HOH B . 
AA 5 HOH 42  442 720 HOH HOH B . 
AA 5 HOH 43  443 696 HOH HOH B . 
AA 5 HOH 44  444 716 HOH HOH B . 
AA 5 HOH 45  445 806 HOH HOH B . 
AA 5 HOH 46  446 576 HOH HOH B . 
AA 5 HOH 47  447 582 HOH HOH B . 
AA 5 HOH 48  448 441 HOH HOH B . 
AA 5 HOH 49  449 678 HOH HOH B . 
AA 5 HOH 50  450 859 HOH HOH B . 
AA 5 HOH 51  451 668 HOH HOH B . 
AA 5 HOH 52  452 606 HOH HOH B . 
AA 5 HOH 53  453 517 HOH HOH B . 
AA 5 HOH 54  454 907 HOH HOH B . 
AA 5 HOH 55  455 99  HOH HOH B . 
AA 5 HOH 56  456 378 HOH HOH B . 
AA 5 HOH 57  457 462 HOH HOH B . 
AA 5 HOH 58  458 212 HOH HOH B . 
AA 5 HOH 59  459 164 HOH HOH B . 
AA 5 HOH 60  460 512 HOH HOH B . 
AA 5 HOH 61  461 674 HOH HOH B . 
AA 5 HOH 62  462 821 HOH HOH B . 
AA 5 HOH 63  463 511 HOH HOH B . 
AA 5 HOH 64  464 845 HOH HOH B . 
AA 5 HOH 65  465 458 HOH HOH B . 
AA 5 HOH 66  466 768 HOH HOH B . 
AA 5 HOH 67  467 815 HOH HOH B . 
AA 5 HOH 68  468 593 HOH HOH B . 
AA 5 HOH 69  469 610 HOH HOH B . 
AA 5 HOH 70  470 412 HOH HOH B . 
AA 5 HOH 71  471 739 HOH HOH B . 
AA 5 HOH 72  472 843 HOH HOH B . 
AA 5 HOH 73  473 491 HOH HOH B . 
AA 5 HOH 74  474 820 HOH HOH B . 
AA 5 HOH 75  475 482 HOH HOH B . 
AA 5 HOH 76  476 424 HOH HOH B . 
AA 5 HOH 77  477 497 HOH HOH B . 
AA 5 HOH 78  478 711 HOH HOH B . 
AA 5 HOH 79  479 368 HOH HOH B . 
AA 5 HOH 80  480 703 HOH HOH B . 
AA 5 HOH 81  481 553 HOH HOH B . 
AA 5 HOH 82  482 590 HOH HOH B . 
AA 5 HOH 83  483 1   HOH HOH B . 
AA 5 HOH 84  484 7   HOH HOH B . 
AA 5 HOH 85  485 13  HOH HOH B . 
AA 5 HOH 86  486 22  HOH HOH B . 
AA 5 HOH 87  487 24  HOH HOH B . 
AA 5 HOH 88  488 29  HOH HOH B . 
AA 5 HOH 89  489 31  HOH HOH B . 
AA 5 HOH 90  490 36  HOH HOH B . 
AA 5 HOH 91  491 42  HOH HOH B . 
AA 5 HOH 92  492 55  HOH HOH B . 
AA 5 HOH 93  493 56  HOH HOH B . 
AA 5 HOH 94  494 57  HOH HOH B . 
AA 5 HOH 95  495 59  HOH HOH B . 
AA 5 HOH 96  496 60  HOH HOH B . 
AA 5 HOH 97  497 63  HOH HOH B . 
AA 5 HOH 98  498 64  HOH HOH B . 
AA 5 HOH 99  499 67  HOH HOH B . 
AA 5 HOH 100 500 71  HOH HOH B . 
AA 5 HOH 101 501 75  HOH HOH B . 
AA 5 HOH 102 502 76  HOH HOH B . 
AA 5 HOH 103 503 84  HOH HOH B . 
AA 5 HOH 104 504 85  HOH HOH B . 
AA 5 HOH 105 505 88  HOH HOH B . 
AA 5 HOH 106 506 91  HOH HOH B . 
AA 5 HOH 107 507 92  HOH HOH B . 
AA 5 HOH 108 508 97  HOH HOH B . 
AA 5 HOH 109 509 105 HOH HOH B . 
AA 5 HOH 110 510 110 HOH HOH B . 
AA 5 HOH 111 511 111 HOH HOH B . 
AA 5 HOH 112 512 116 HOH HOH B . 
AA 5 HOH 113 513 120 HOH HOH B . 
AA 5 HOH 114 514 125 HOH HOH B . 
AA 5 HOH 115 515 133 HOH HOH B . 
AA 5 HOH 116 516 134 HOH HOH B . 
AA 5 HOH 117 517 135 HOH HOH B . 
AA 5 HOH 118 518 143 HOH HOH B . 
AA 5 HOH 119 519 146 HOH HOH B . 
AA 5 HOH 120 520 149 HOH HOH B . 
AA 5 HOH 121 521 168 HOH HOH B . 
AA 5 HOH 122 522 173 HOH HOH B . 
AA 5 HOH 123 523 175 HOH HOH B . 
AA 5 HOH 124 524 176 HOH HOH B . 
AA 5 HOH 125 525 179 HOH HOH B . 
AA 5 HOH 126 526 180 HOH HOH B . 
AA 5 HOH 127 527 181 HOH HOH B . 
AA 5 HOH 128 528 187 HOH HOH B . 
AA 5 HOH 129 529 191 HOH HOH B . 
AA 5 HOH 130 530 199 HOH HOH B . 
AA 5 HOH 131 531 202 HOH HOH B . 
AA 5 HOH 132 532 203 HOH HOH B . 
AA 5 HOH 133 533 204 HOH HOH B . 
AA 5 HOH 134 534 220 HOH HOH B . 
AA 5 HOH 135 535 226 HOH HOH B . 
AA 5 HOH 136 536 236 HOH HOH B . 
AA 5 HOH 137 537 242 HOH HOH B . 
AA 5 HOH 138 538 249 HOH HOH B . 
AA 5 HOH 139 539 251 HOH HOH B . 
AA 5 HOH 140 540 252 HOH HOH B . 
AA 5 HOH 141 541 259 HOH HOH B . 
AA 5 HOH 142 542 262 HOH HOH B . 
AA 5 HOH 143 543 263 HOH HOH B . 
AA 5 HOH 144 544 266 HOH HOH B . 
AA 5 HOH 145 545 268 HOH HOH B . 
AA 5 HOH 146 546 275 HOH HOH B . 
AA 5 HOH 147 547 277 HOH HOH B . 
AA 5 HOH 148 548 279 HOH HOH B . 
AA 5 HOH 149 549 285 HOH HOH B . 
AA 5 HOH 150 550 286 HOH HOH B . 
AA 5 HOH 151 551 292 HOH HOH B . 
AA 5 HOH 152 552 299 HOH HOH B . 
AA 5 HOH 153 553 306 HOH HOH B . 
AA 5 HOH 154 554 307 HOH HOH B . 
AA 5 HOH 155 555 310 HOH HOH B . 
AA 5 HOH 156 556 311 HOH HOH B . 
AA 5 HOH 157 557 314 HOH HOH B . 
AA 5 HOH 158 558 316 HOH HOH B . 
AA 5 HOH 159 559 317 HOH HOH B . 
AA 5 HOH 160 560 323 HOH HOH B . 
AA 5 HOH 161 561 325 HOH HOH B . 
AA 5 HOH 162 562 333 HOH HOH B . 
AA 5 HOH 163 563 334 HOH HOH B . 
AA 5 HOH 164 564 342 HOH HOH B . 
AA 5 HOH 165 565 347 HOH HOH B . 
AA 5 HOH 166 566 352 HOH HOH B . 
AA 5 HOH 167 567 354 HOH HOH B . 
AA 5 HOH 168 568 355 HOH HOH B . 
AA 5 HOH 169 569 372 HOH HOH B . 
AA 5 HOH 170 570 376 HOH HOH B . 
AA 5 HOH 171 571 384 HOH HOH B . 
AA 5 HOH 172 572 421 HOH HOH B . 
AA 5 HOH 173 573 427 HOH HOH B . 
AA 5 HOH 174 574 428 HOH HOH B . 
AA 5 HOH 175 575 430 HOH HOH B . 
AA 5 HOH 176 576 438 HOH HOH B . 
AA 5 HOH 177 577 444 HOH HOH B . 
AA 5 HOH 178 578 449 HOH HOH B . 
AA 5 HOH 179 579 459 HOH HOH B . 
AA 5 HOH 180 580 464 HOH HOH B . 
AA 5 HOH 181 581 472 HOH HOH B . 
AA 5 HOH 182 582 473 HOH HOH B . 
AA 5 HOH 183 583 480 HOH HOH B . 
AA 5 HOH 184 584 487 HOH HOH B . 
AA 5 HOH 185 585 493 HOH HOH B . 
AA 5 HOH 186 586 498 HOH HOH B . 
AA 5 HOH 187 587 501 HOH HOH B . 
AA 5 HOH 188 588 507 HOH HOH B . 
AA 5 HOH 189 589 508 HOH HOH B . 
AA 5 HOH 190 590 509 HOH HOH B . 
AA 5 HOH 191 591 514 HOH HOH B . 
AA 5 HOH 192 592 518 HOH HOH B . 
AA 5 HOH 193 593 521 HOH HOH B . 
AA 5 HOH 194 594 534 HOH HOH B . 
AA 5 HOH 195 595 539 HOH HOH B . 
AA 5 HOH 196 596 542 HOH HOH B . 
AA 5 HOH 197 597 552 HOH HOH B . 
AA 5 HOH 198 598 563 HOH HOH B . 
AA 5 HOH 199 599 564 HOH HOH B . 
AA 5 HOH 200 600 567 HOH HOH B . 
AA 5 HOH 201 601 574 HOH HOH B . 
AA 5 HOH 202 602 589 HOH HOH B . 
AA 5 HOH 203 603 609 HOH HOH B . 
AA 5 HOH 204 604 611 HOH HOH B . 
AA 5 HOH 205 605 613 HOH HOH B . 
AA 5 HOH 206 606 615 HOH HOH B . 
AA 5 HOH 207 607 618 HOH HOH B . 
AA 5 HOH 208 608 620 HOH HOH B . 
AA 5 HOH 209 609 621 HOH HOH B . 
AA 5 HOH 210 610 626 HOH HOH B . 
AA 5 HOH 211 611 632 HOH HOH B . 
AA 5 HOH 212 612 644 HOH HOH B . 
AA 5 HOH 213 613 654 HOH HOH B . 
AA 5 HOH 214 614 657 HOH HOH B . 
AA 5 HOH 215 615 659 HOH HOH B . 
AA 5 HOH 216 616 675 HOH HOH B . 
AA 5 HOH 217 617 681 HOH HOH B . 
AA 5 HOH 218 618 686 HOH HOH B . 
AA 5 HOH 219 619 693 HOH HOH B . 
AA 5 HOH 220 620 695 HOH HOH B . 
AA 5 HOH 221 621 704 HOH HOH B . 
AA 5 HOH 222 622 709 HOH HOH B . 
AA 5 HOH 223 623 710 HOH HOH B . 
AA 5 HOH 224 624 714 HOH HOH B . 
AA 5 HOH 225 625 717 HOH HOH B . 
AA 5 HOH 226 626 722 HOH HOH B . 
AA 5 HOH 227 627 727 HOH HOH B . 
AA 5 HOH 228 628 733 HOH HOH B . 
AA 5 HOH 229 629 735 HOH HOH B . 
AA 5 HOH 230 630 743 HOH HOH B . 
AA 5 HOH 231 631 748 HOH HOH B . 
AA 5 HOH 232 632 754 HOH HOH B . 
AA 5 HOH 233 633 755 HOH HOH B . 
AA 5 HOH 234 634 759 HOH HOH B . 
AA 5 HOH 235 635 763 HOH HOH B . 
AA 5 HOH 236 636 764 HOH HOH B . 
AA 5 HOH 237 637 792 HOH HOH B . 
AA 5 HOH 238 638 801 HOH HOH B . 
AA 5 HOH 239 639 807 HOH HOH B . 
AA 5 HOH 240 640 809 HOH HOH B . 
AA 5 HOH 241 641 822 HOH HOH B . 
AA 5 HOH 242 642 833 HOH HOH B . 
AA 5 HOH 243 643 835 HOH HOH B . 
AA 5 HOH 244 644 847 HOH HOH B . 
AA 5 HOH 245 645 860 HOH HOH B . 
AA 5 HOH 246 646 861 HOH HOH B . 
AA 5 HOH 247 647 862 HOH HOH B . 
AA 5 HOH 248 648 863 HOH HOH B . 
AA 5 HOH 249 649 864 HOH HOH B . 
AA 5 HOH 250 650 865 HOH HOH B . 
AA 5 HOH 251 651 866 HOH HOH B . 
AA 5 HOH 252 652 867 HOH HOH B . 
AA 5 HOH 253 653 868 HOH HOH B . 
AA 5 HOH 254 654 869 HOH HOH B . 
AA 5 HOH 255 655 870 HOH HOH B . 
AA 5 HOH 256 656 872 HOH HOH B . 
AA 5 HOH 257 657 895 HOH HOH B . 
AA 5 HOH 258 658 899 HOH HOH B . 
AA 5 HOH 259 659 910 HOH HOH B . 
AA 5 HOH 260 660 911 HOH HOH B . 
BA 5 HOH 1   401 648 HOH HOH C . 
BA 5 HOH 2   402 688 HOH HOH C . 
BA 5 HOH 3   403 800 HOH HOH C . 
BA 5 HOH 4   404 50  HOH HOH C . 
BA 5 HOH 5   405 375 HOH HOH C . 
BA 5 HOH 6   406 793 HOH HOH C . 
BA 5 HOH 7   407 336 HOH HOH C . 
BA 5 HOH 8   408 598 HOH HOH C . 
BA 5 HOH 9   409 640 HOH HOH C . 
BA 5 HOH 10  410 253 HOH HOH C . 
BA 5 HOH 11  411 224 HOH HOH C . 
BA 5 HOH 12  412 231 HOH HOH C . 
BA 5 HOH 13  413 871 HOH HOH C . 
BA 5 HOH 14  414 267 HOH HOH C . 
BA 5 HOH 15  415 676 HOH HOH C . 
BA 5 HOH 16  416 453 HOH HOH C . 
BA 5 HOH 17  417 538 HOH HOH C . 
BA 5 HOH 18  418 851 HOH HOH C . 
BA 5 HOH 19  419 439 HOH HOH C . 
BA 5 HOH 20  420 527 HOH HOH C . 
BA 5 HOH 21  421 878 HOH HOH C . 
BA 5 HOH 22  422 486 HOH HOH C . 
BA 5 HOH 23  423 322 HOH HOH C . 
BA 5 HOH 24  424 747 HOH HOH C . 
BA 5 HOH 25  425 446 HOH HOH C . 
BA 5 HOH 26  426 912 HOH HOH C . 
BA 5 HOH 27  427 415 HOH HOH C . 
BA 5 HOH 28  428 312 HOH HOH C . 
BA 5 HOH 29  429 643 HOH HOH C . 
BA 5 HOH 30  430 522 HOH HOH C . 
BA 5 HOH 31  431 813 HOH HOH C . 
BA 5 HOH 32  432 850 HOH HOH C . 
BA 5 HOH 33  433 891 HOH HOH C . 
BA 5 HOH 34  434 777 HOH HOH C . 
BA 5 HOH 35  435 580 HOH HOH C . 
BA 5 HOH 36  436 584 HOH HOH C . 
BA 5 HOH 37  437 729 HOH HOH C . 
BA 5 HOH 38  438 594 HOH HOH C . 
BA 5 HOH 39  439 881 HOH HOH C . 
BA 5 HOH 40  440 2   HOH HOH C . 
BA 5 HOH 41  441 4   HOH HOH C . 
BA 5 HOH 42  442 9   HOH HOH C . 
BA 5 HOH 43  443 11  HOH HOH C . 
BA 5 HOH 44  444 28  HOH HOH C . 
BA 5 HOH 45  445 30  HOH HOH C . 
BA 5 HOH 46  446 39  HOH HOH C . 
BA 5 HOH 47  447 41  HOH HOH C . 
BA 5 HOH 48  448 47  HOH HOH C . 
BA 5 HOH 49  449 51  HOH HOH C . 
BA 5 HOH 50  450 65  HOH HOH C . 
BA 5 HOH 51  451 70  HOH HOH C . 
BA 5 HOH 52  452 77  HOH HOH C . 
BA 5 HOH 53  453 78  HOH HOH C . 
BA 5 HOH 54  454 81  HOH HOH C . 
BA 5 HOH 55  455 83  HOH HOH C . 
BA 5 HOH 56  456 86  HOH HOH C . 
BA 5 HOH 57  457 93  HOH HOH C . 
BA 5 HOH 58  458 100 HOH HOH C . 
BA 5 HOH 59  459 103 HOH HOH C . 
BA 5 HOH 60  460 109 HOH HOH C . 
BA 5 HOH 61  461 121 HOH HOH C . 
BA 5 HOH 62  462 123 HOH HOH C . 
BA 5 HOH 63  463 127 HOH HOH C . 
BA 5 HOH 64  464 128 HOH HOH C . 
BA 5 HOH 65  465 137 HOH HOH C . 
BA 5 HOH 66  466 145 HOH HOH C . 
BA 5 HOH 67  467 155 HOH HOH C . 
BA 5 HOH 68  468 157 HOH HOH C . 
BA 5 HOH 69  469 159 HOH HOH C . 
BA 5 HOH 70  470 162 HOH HOH C . 
BA 5 HOH 71  471 165 HOH HOH C . 
BA 5 HOH 72  472 166 HOH HOH C . 
BA 5 HOH 73  473 186 HOH HOH C . 
BA 5 HOH 74  474 192 HOH HOH C . 
BA 5 HOH 75  475 194 HOH HOH C . 
BA 5 HOH 76  476 198 HOH HOH C . 
BA 5 HOH 77  477 205 HOH HOH C . 
BA 5 HOH 78  478 208 HOH HOH C . 
BA 5 HOH 79  479 217 HOH HOH C . 
BA 5 HOH 80  480 219 HOH HOH C . 
BA 5 HOH 81  481 221 HOH HOH C . 
BA 5 HOH 82  482 225 HOH HOH C . 
BA 5 HOH 83  483 232 HOH HOH C . 
BA 5 HOH 84  484 235 HOH HOH C . 
BA 5 HOH 85  485 240 HOH HOH C . 
BA 5 HOH 86  486 255 HOH HOH C . 
BA 5 HOH 87  487 273 HOH HOH C . 
BA 5 HOH 88  488 276 HOH HOH C . 
BA 5 HOH 89  489 278 HOH HOH C . 
BA 5 HOH 90  490 290 HOH HOH C . 
BA 5 HOH 91  491 298 HOH HOH C . 
BA 5 HOH 92  492 301 HOH HOH C . 
BA 5 HOH 93  493 318 HOH HOH C . 
BA 5 HOH 94  494 320 HOH HOH C . 
BA 5 HOH 95  495 328 HOH HOH C . 
BA 5 HOH 96  496 337 HOH HOH C . 
BA 5 HOH 97  497 340 HOH HOH C . 
BA 5 HOH 98  498 343 HOH HOH C . 
BA 5 HOH 99  499 344 HOH HOH C . 
BA 5 HOH 100 500 348 HOH HOH C . 
BA 5 HOH 101 501 351 HOH HOH C . 
BA 5 HOH 102 502 358 HOH HOH C . 
BA 5 HOH 103 503 359 HOH HOH C . 
BA 5 HOH 104 504 361 HOH HOH C . 
BA 5 HOH 105 505 363 HOH HOH C . 
BA 5 HOH 106 506 365 HOH HOH C . 
BA 5 HOH 107 507 371 HOH HOH C . 
BA 5 HOH 108 508 385 HOH HOH C . 
BA 5 HOH 109 509 400 HOH HOH C . 
BA 5 HOH 110 510 401 HOH HOH C . 
BA 5 HOH 111 511 417 HOH HOH C . 
BA 5 HOH 112 512 418 HOH HOH C . 
BA 5 HOH 113 513 419 HOH HOH C . 
BA 5 HOH 114 514 425 HOH HOH C . 
BA 5 HOH 115 515 433 HOH HOH C . 
BA 5 HOH 116 516 434 HOH HOH C . 
BA 5 HOH 117 517 436 HOH HOH C . 
BA 5 HOH 118 518 450 HOH HOH C . 
BA 5 HOH 119 519 463 HOH HOH C . 
BA 5 HOH 120 520 466 HOH HOH C . 
BA 5 HOH 121 521 470 HOH HOH C . 
BA 5 HOH 122 522 478 HOH HOH C . 
BA 5 HOH 123 523 479 HOH HOH C . 
BA 5 HOH 124 524 483 HOH HOH C . 
BA 5 HOH 125 525 488 HOH HOH C . 
BA 5 HOH 126 526 495 HOH HOH C . 
BA 5 HOH 127 527 500 HOH HOH C . 
BA 5 HOH 128 528 510 HOH HOH C . 
BA 5 HOH 129 529 515 HOH HOH C . 
BA 5 HOH 130 530 519 HOH HOH C . 
BA 5 HOH 131 531 525 HOH HOH C . 
BA 5 HOH 132 532 526 HOH HOH C . 
BA 5 HOH 133 533 540 HOH HOH C . 
BA 5 HOH 134 534 549 HOH HOH C . 
BA 5 HOH 135 535 551 HOH HOH C . 
BA 5 HOH 136 536 561 HOH HOH C . 
BA 5 HOH 137 537 568 HOH HOH C . 
BA 5 HOH 138 538 571 HOH HOH C . 
BA 5 HOH 139 539 578 HOH HOH C . 
BA 5 HOH 140 540 591 HOH HOH C . 
BA 5 HOH 141 541 600 HOH HOH C . 
BA 5 HOH 142 542 604 HOH HOH C . 
BA 5 HOH 143 543 605 HOH HOH C . 
BA 5 HOH 144 544 612 HOH HOH C . 
BA 5 HOH 145 545 614 HOH HOH C . 
BA 5 HOH 146 546 627 HOH HOH C . 
BA 5 HOH 147 547 631 HOH HOH C . 
BA 5 HOH 148 548 635 HOH HOH C . 
BA 5 HOH 149 549 637 HOH HOH C . 
BA 5 HOH 150 550 651 HOH HOH C . 
BA 5 HOH 151 551 658 HOH HOH C . 
BA 5 HOH 152 552 661 HOH HOH C . 
BA 5 HOH 153 553 663 HOH HOH C . 
BA 5 HOH 154 554 667 HOH HOH C . 
BA 5 HOH 155 555 683 HOH HOH C . 
BA 5 HOH 156 556 687 HOH HOH C . 
BA 5 HOH 157 557 690 HOH HOH C . 
BA 5 HOH 158 558 705 HOH HOH C . 
BA 5 HOH 159 559 719 HOH HOH C . 
BA 5 HOH 160 560 728 HOH HOH C . 
BA 5 HOH 161 561 736 HOH HOH C . 
BA 5 HOH 162 562 737 HOH HOH C . 
BA 5 HOH 163 563 760 HOH HOH C . 
BA 5 HOH 164 564 766 HOH HOH C . 
BA 5 HOH 165 565 774 HOH HOH C . 
BA 5 HOH 166 566 783 HOH HOH C . 
BA 5 HOH 167 567 785 HOH HOH C . 
BA 5 HOH 168 568 790 HOH HOH C . 
BA 5 HOH 169 569 791 HOH HOH C . 
BA 5 HOH 170 570 799 HOH HOH C . 
BA 5 HOH 171 571 804 HOH HOH C . 
BA 5 HOH 172 572 808 HOH HOH C . 
BA 5 HOH 173 573 810 HOH HOH C . 
BA 5 HOH 174 574 812 HOH HOH C . 
BA 5 HOH 175 575 823 HOH HOH C . 
BA 5 HOH 176 576 824 HOH HOH C . 
BA 5 HOH 177 577 825 HOH HOH C . 
BA 5 HOH 178 578 826 HOH HOH C . 
BA 5 HOH 179 579 827 HOH HOH C . 
BA 5 HOH 180 580 875 HOH HOH C . 
BA 5 HOH 181 581 876 HOH HOH C . 
BA 5 HOH 182 582 877 HOH HOH C . 
BA 5 HOH 183 583 879 HOH HOH C . 
BA 5 HOH 184 584 880 HOH HOH C . 
BA 5 HOH 185 585 884 HOH HOH C . 
BA 5 HOH 186 586 885 HOH HOH C . 
BA 5 HOH 187 587 902 HOH HOH C . 
CA 5 HOH 1   401 234 HOH HOH D . 
CA 5 HOH 2   402 802 HOH HOH D . 
CA 5 HOH 3   403 608 HOH HOH D . 
CA 5 HOH 4   404 890 HOH HOH D . 
CA 5 HOH 5   405 132 HOH HOH D . 
CA 5 HOH 6   406 189 HOH HOH D . 
CA 5 HOH 7   407 416 HOH HOH D . 
CA 5 HOH 8   408 426 HOH HOH D . 
CA 5 HOH 9   409 750 HOH HOH D . 
CA 5 HOH 10  410 646 HOH HOH D . 
CA 5 HOH 11  411 607 HOH HOH D . 
CA 5 HOH 12  412 788 HOH HOH D . 
CA 5 HOH 13  413 3   HOH HOH D . 
CA 5 HOH 14  414 883 HOH HOH D . 
CA 5 HOH 15  415 649 HOH HOH D . 
CA 5 HOH 16  416 408 HOH HOH D . 
CA 5 HOH 17  417 218 HOH HOH D . 
CA 5 HOH 18  418 182 HOH HOH D . 
CA 5 HOH 19  419 118 HOH HOH D . 
CA 5 HOH 20  420 206 HOH HOH D . 
CA 5 HOH 21  421 742 HOH HOH D . 
CA 5 HOH 22  422 297 HOH HOH D . 
CA 5 HOH 23  423 250 HOH HOH D . 
CA 5 HOH 24  424 560 HOH HOH D . 
CA 5 HOH 25  425 603 HOH HOH D . 
CA 5 HOH 26  426 410 HOH HOH D . 
CA 5 HOH 27  427 319 HOH HOH D . 
CA 5 HOH 28  428 321 HOH HOH D . 
CA 5 HOH 29  429 233 HOH HOH D . 
CA 5 HOH 30  430 160 HOH HOH D . 
CA 5 HOH 31  431 601 HOH HOH D . 
CA 5 HOH 32  432 887 HOH HOH D . 
CA 5 HOH 33  433 892 HOH HOH D . 
CA 5 HOH 34  434 327 HOH HOH D . 
CA 5 HOH 35  435 238 HOH HOH D . 
CA 5 HOH 36  436 499 HOH HOH D . 
CA 5 HOH 37  437 854 HOH HOH D . 
CA 5 HOH 38  438 740 HOH HOH D . 
CA 5 HOH 39  439 874 HOH HOH D . 
CA 5 HOH 40  440 178 HOH HOH D . 
CA 5 HOH 41  441 548 HOH HOH D . 
CA 5 HOH 42  442 289 HOH HOH D . 
CA 5 HOH 43  443 403 HOH HOH D . 
CA 5 HOH 44  444 520 HOH HOH D . 
CA 5 HOH 45  445 448 HOH HOH D . 
CA 5 HOH 46  446 469 HOH HOH D . 
CA 5 HOH 47  447 33  HOH HOH D . 
CA 5 HOH 48  448 502 HOH HOH D . 
CA 5 HOH 49  449 662 HOH HOH D . 
CA 5 HOH 50  450 886 HOH HOH D . 
CA 5 HOH 51  451 193 HOH HOH D . 
CA 5 HOH 52  452 172 HOH HOH D . 
CA 5 HOH 53  453 694 HOH HOH D . 
CA 5 HOH 54  454 889 HOH HOH D . 
CA 5 HOH 55  455 639 HOH HOH D . 
CA 5 HOH 56  456 751 HOH HOH D . 
CA 5 HOH 57  457 660 HOH HOH D . 
CA 5 HOH 58  458 360 HOH HOH D . 
CA 5 HOH 59  459 506 HOH HOH D . 
CA 5 HOH 60  460 577 HOH HOH D . 
CA 5 HOH 61  461 723 HOH HOH D . 
CA 5 HOH 62  462 196 HOH HOH D . 
CA 5 HOH 63  463 898 HOH HOH D . 
CA 5 HOH 64  464 726 HOH HOH D . 
CA 5 HOH 65  465 855 HOH HOH D . 
CA 5 HOH 66  466 702 HOH HOH D . 
CA 5 HOH 67  467 244 HOH HOH D . 
CA 5 HOH 68  468 775 HOH HOH D . 
CA 5 HOH 69  469 700 HOH HOH D . 
CA 5 HOH 70  470 581 HOH HOH D . 
CA 5 HOH 71  471 169 HOH HOH D . 
CA 5 HOH 72  472 597 HOH HOH D . 
CA 5 HOH 73  473 583 HOH HOH D . 
CA 5 HOH 74  474 642 HOH HOH D . 
CA 5 HOH 75  475 5   HOH HOH D . 
CA 5 HOH 76  476 6   HOH HOH D . 
CA 5 HOH 77  477 8   HOH HOH D . 
CA 5 HOH 78  478 16  HOH HOH D . 
CA 5 HOH 79  479 17  HOH HOH D . 
CA 5 HOH 80  480 18  HOH HOH D . 
CA 5 HOH 81  481 20  HOH HOH D . 
CA 5 HOH 82  482 26  HOH HOH D . 
CA 5 HOH 83  483 27  HOH HOH D . 
CA 5 HOH 84  484 40  HOH HOH D . 
CA 5 HOH 85  485 44  HOH HOH D . 
CA 5 HOH 86  486 45  HOH HOH D . 
CA 5 HOH 87  487 46  HOH HOH D . 
CA 5 HOH 88  488 52  HOH HOH D . 
CA 5 HOH 89  489 53  HOH HOH D . 
CA 5 HOH 90  490 54  HOH HOH D . 
CA 5 HOH 91  491 62  HOH HOH D . 
CA 5 HOH 92  492 68  HOH HOH D . 
CA 5 HOH 93  493 72  HOH HOH D . 
CA 5 HOH 94  494 79  HOH HOH D . 
CA 5 HOH 95  495 82  HOH HOH D . 
CA 5 HOH 96  496 87  HOH HOH D . 
CA 5 HOH 97  497 89  HOH HOH D . 
CA 5 HOH 98  498 90  HOH HOH D . 
CA 5 HOH 99  499 94  HOH HOH D . 
CA 5 HOH 100 500 95  HOH HOH D . 
CA 5 HOH 101 501 102 HOH HOH D . 
CA 5 HOH 102 502 107 HOH HOH D . 
CA 5 HOH 103 503 112 HOH HOH D . 
CA 5 HOH 104 504 117 HOH HOH D . 
CA 5 HOH 105 505 124 HOH HOH D . 
CA 5 HOH 106 506 131 HOH HOH D . 
CA 5 HOH 107 507 136 HOH HOH D . 
CA 5 HOH 108 508 138 HOH HOH D . 
CA 5 HOH 109 509 140 HOH HOH D . 
CA 5 HOH 110 510 142 HOH HOH D . 
CA 5 HOH 111 511 144 HOH HOH D . 
CA 5 HOH 112 512 147 HOH HOH D . 
CA 5 HOH 113 513 148 HOH HOH D . 
CA 5 HOH 114 514 153 HOH HOH D . 
CA 5 HOH 115 515 154 HOH HOH D . 
CA 5 HOH 116 516 156 HOH HOH D . 
CA 5 HOH 117 517 161 HOH HOH D . 
CA 5 HOH 118 518 163 HOH HOH D . 
CA 5 HOH 119 519 171 HOH HOH D . 
CA 5 HOH 120 520 184 HOH HOH D . 
CA 5 HOH 121 521 188 HOH HOH D . 
CA 5 HOH 122 522 209 HOH HOH D . 
CA 5 HOH 123 523 210 HOH HOH D . 
CA 5 HOH 124 524 211 HOH HOH D . 
CA 5 HOH 125 525 216 HOH HOH D . 
CA 5 HOH 126 526 222 HOH HOH D . 
CA 5 HOH 127 527 230 HOH HOH D . 
CA 5 HOH 128 528 241 HOH HOH D . 
CA 5 HOH 129 529 243 HOH HOH D . 
CA 5 HOH 130 530 245 HOH HOH D . 
CA 5 HOH 131 531 246 HOH HOH D . 
CA 5 HOH 132 532 254 HOH HOH D . 
CA 5 HOH 133 533 256 HOH HOH D . 
CA 5 HOH 134 534 258 HOH HOH D . 
CA 5 HOH 135 535 260 HOH HOH D . 
CA 5 HOH 136 536 271 HOH HOH D . 
CA 5 HOH 137 537 280 HOH HOH D . 
CA 5 HOH 138 538 282 HOH HOH D . 
CA 5 HOH 139 539 283 HOH HOH D . 
CA 5 HOH 140 540 284 HOH HOH D . 
CA 5 HOH 141 541 288 HOH HOH D . 
CA 5 HOH 142 542 295 HOH HOH D . 
CA 5 HOH 143 543 302 HOH HOH D . 
CA 5 HOH 144 544 313 HOH HOH D . 
CA 5 HOH 145 545 332 HOH HOH D . 
CA 5 HOH 146 546 349 HOH HOH D . 
CA 5 HOH 147 547 350 HOH HOH D . 
CA 5 HOH 148 548 353 HOH HOH D . 
CA 5 HOH 149 549 362 HOH HOH D . 
CA 5 HOH 150 550 366 HOH HOH D . 
CA 5 HOH 151 551 373 HOH HOH D . 
CA 5 HOH 152 552 379 HOH HOH D . 
CA 5 HOH 153 553 387 HOH HOH D . 
CA 5 HOH 154 554 388 HOH HOH D . 
CA 5 HOH 155 555 389 HOH HOH D . 
CA 5 HOH 156 556 392 HOH HOH D . 
CA 5 HOH 157 557 394 HOH HOH D . 
CA 5 HOH 158 558 396 HOH HOH D . 
CA 5 HOH 159 559 397 HOH HOH D . 
CA 5 HOH 160 560 399 HOH HOH D . 
CA 5 HOH 161 561 404 HOH HOH D . 
CA 5 HOH 162 562 409 HOH HOH D . 
CA 5 HOH 163 563 413 HOH HOH D . 
CA 5 HOH 164 564 414 HOH HOH D . 
CA 5 HOH 165 565 422 HOH HOH D . 
CA 5 HOH 166 566 437 HOH HOH D . 
CA 5 HOH 167 567 447 HOH HOH D . 
CA 5 HOH 168 568 454 HOH HOH D . 
CA 5 HOH 169 569 456 HOH HOH D . 
CA 5 HOH 170 570 457 HOH HOH D . 
CA 5 HOH 171 571 460 HOH HOH D . 
CA 5 HOH 172 572 467 HOH HOH D . 
CA 5 HOH 173 573 471 HOH HOH D . 
CA 5 HOH 174 574 474 HOH HOH D . 
CA 5 HOH 175 575 476 HOH HOH D . 
CA 5 HOH 176 576 477 HOH HOH D . 
CA 5 HOH 177 577 481 HOH HOH D . 
CA 5 HOH 178 578 490 HOH HOH D . 
CA 5 HOH 179 579 492 HOH HOH D . 
CA 5 HOH 180 580 496 HOH HOH D . 
CA 5 HOH 181 581 503 HOH HOH D . 
CA 5 HOH 182 582 504 HOH HOH D . 
CA 5 HOH 183 583 513 HOH HOH D . 
CA 5 HOH 184 584 524 HOH HOH D . 
CA 5 HOH 185 585 531 HOH HOH D . 
CA 5 HOH 186 586 533 HOH HOH D . 
CA 5 HOH 187 587 545 HOH HOH D . 
CA 5 HOH 188 588 546 HOH HOH D . 
CA 5 HOH 189 589 547 HOH HOH D . 
CA 5 HOH 190 590 554 HOH HOH D . 
CA 5 HOH 191 591 556 HOH HOH D . 
CA 5 HOH 192 592 565 HOH HOH D . 
CA 5 HOH 193 593 572 HOH HOH D . 
CA 5 HOH 194 594 573 HOH HOH D . 
CA 5 HOH 195 595 575 HOH HOH D . 
CA 5 HOH 196 596 585 HOH HOH D . 
CA 5 HOH 197 597 586 HOH HOH D . 
CA 5 HOH 198 598 592 HOH HOH D . 
CA 5 HOH 199 599 595 HOH HOH D . 
CA 5 HOH 200 600 599 HOH HOH D . 
CA 5 HOH 201 601 619 HOH HOH D . 
CA 5 HOH 202 602 622 HOH HOH D . 
CA 5 HOH 203 603 629 HOH HOH D . 
CA 5 HOH 204 604 634 HOH HOH D . 
CA 5 HOH 205 605 652 HOH HOH D . 
CA 5 HOH 206 606 672 HOH HOH D . 
CA 5 HOH 207 607 677 HOH HOH D . 
CA 5 HOH 208 608 679 HOH HOH D . 
CA 5 HOH 209 609 682 HOH HOH D . 
CA 5 HOH 210 610 692 HOH HOH D . 
CA 5 HOH 211 611 712 HOH HOH D . 
CA 5 HOH 212 612 713 HOH HOH D . 
CA 5 HOH 213 613 718 HOH HOH D . 
CA 5 HOH 214 614 721 HOH HOH D . 
CA 5 HOH 215 615 724 HOH HOH D . 
CA 5 HOH 216 616 734 HOH HOH D . 
CA 5 HOH 217 617 738 HOH HOH D . 
CA 5 HOH 218 618 741 HOH HOH D . 
CA 5 HOH 219 619 745 HOH HOH D . 
CA 5 HOH 220 620 746 HOH HOH D . 
CA 5 HOH 221 621 761 HOH HOH D . 
CA 5 HOH 222 622 767 HOH HOH D . 
CA 5 HOH 223 623 769 HOH HOH D . 
CA 5 HOH 224 624 771 HOH HOH D . 
CA 5 HOH 225 625 772 HOH HOH D . 
CA 5 HOH 226 626 776 HOH HOH D . 
CA 5 HOH 227 627 778 HOH HOH D . 
CA 5 HOH 228 628 780 HOH HOH D . 
CA 5 HOH 229 629 781 HOH HOH D . 
CA 5 HOH 230 630 789 HOH HOH D . 
CA 5 HOH 231 631 794 HOH HOH D . 
CA 5 HOH 232 632 796 HOH HOH D . 
CA 5 HOH 233 633 805 HOH HOH D . 
CA 5 HOH 234 634 814 HOH HOH D . 
CA 5 HOH 235 635 817 HOH HOH D . 
CA 5 HOH 236 636 828 HOH HOH D . 
CA 5 HOH 237 637 829 HOH HOH D . 
CA 5 HOH 238 638 830 HOH HOH D . 
CA 5 HOH 239 639 831 HOH HOH D . 
CA 5 HOH 240 640 832 HOH HOH D . 
CA 5 HOH 241 641 873 HOH HOH D . 
CA 5 HOH 242 642 882 HOH HOH D . 
CA 5 HOH 243 643 888 HOH HOH D . 
CA 5 HOH 244 644 893 HOH HOH D . 
CA 5 HOH 245 645 894 HOH HOH D . 
CA 5 HOH 246 646 900 HOH HOH D . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 3   ? CD  ? A LYS 3   CD  
2  1 Y 1 A LYS 3   ? CE  ? A LYS 3   CE  
3  1 Y 1 A LYS 3   ? NZ  ? A LYS 3   NZ  
4  1 Y 1 A ASP 35  ? CG  ? A ASP 35  CG  
5  1 Y 1 A ASP 35  ? OD1 ? A ASP 35  OD1 
6  1 Y 1 A ASP 35  ? OD2 ? A ASP 35  OD2 
7  1 Y 1 A GLU 47  ? CD  ? A GLU 47  CD  
8  1 Y 1 A GLU 47  ? OE1 ? A GLU 47  OE1 
9  1 Y 1 A GLU 47  ? OE2 ? A GLU 47  OE2 
10 1 Y 1 A GLN 79  ? CD  ? A GLN 79  CD  
11 1 Y 1 A GLN 79  ? OE1 ? A GLN 79  OE1 
12 1 Y 1 A GLN 79  ? NE2 ? A GLN 79  NE2 
13 1 Y 1 A GLU 137 ? OE2 ? A GLU 137 OE2 
14 1 Y 1 A GLN 163 ? CG  ? A GLN 163 CG  
15 1 Y 1 A GLN 163 ? CD  ? A GLN 163 CD  
16 1 Y 1 A GLN 163 ? OE1 ? A GLN 163 OE1 
17 1 Y 1 A GLN 163 ? NE2 ? A GLN 163 NE2 
18 1 Y 1 A ARG 194 ? NE  ? A ARG 194 NE  
19 1 Y 1 A ARG 194 ? CZ  ? A ARG 194 CZ  
20 1 Y 1 A ARG 194 ? NH1 ? A ARG 194 NH1 
21 1 Y 1 A ARG 194 ? NH2 ? A ARG 194 NH2 
22 1 Y 1 A ARG 240 ? CG  ? A ARG 240 CG  
23 1 Y 1 A ARG 240 ? CD  ? A ARG 240 CD  
24 1 Y 1 A ARG 240 ? NE  ? A ARG 240 NE  
25 1 Y 1 A ARG 240 ? CZ  ? A ARG 240 CZ  
26 1 Y 1 A ARG 240 ? NH1 ? A ARG 240 NH1 
27 1 Y 1 A ARG 240 ? NH2 ? A ARG 240 NH2 
28 1 Y 1 B GLU 137 ? CG  ? B GLU 137 CG  
29 1 Y 1 B GLU 137 ? CD  ? B GLU 137 CD  
30 1 Y 1 B GLU 137 ? OE1 ? B GLU 137 OE1 
31 1 Y 1 B GLU 137 ? OE2 ? B GLU 137 OE2 
32 1 Y 1 B ARG 194 ? NE  ? B ARG 194 NE  
33 1 Y 1 B ARG 194 ? CZ  ? B ARG 194 CZ  
34 1 Y 1 B ARG 194 ? NH1 ? B ARG 194 NH1 
35 1 Y 1 B ARG 194 ? NH2 ? B ARG 194 NH2 
36 1 Y 1 C LYS 3   ? CE  ? C LYS 3   CE  
37 1 Y 1 C LYS 3   ? NZ  ? C LYS 3   NZ  
38 1 Y 1 C GLU 47  ? CD  ? C GLU 47  CD  
39 1 Y 1 C GLU 47  ? OE1 ? C GLU 47  OE1 
40 1 Y 1 C GLU 47  ? OE2 ? C GLU 47  OE2 
41 1 Y 1 C GLN 49  ? OE1 ? C GLN 49  OE1 
42 1 Y 1 C GLN 49  ? NE2 ? C GLN 49  NE2 
43 1 Y 1 C ASN 56  ? CB  ? C ASN 56  CB  
44 1 Y 1 C ASN 56  ? CG  ? C ASN 56  CG  
45 1 Y 1 C ASN 56  ? OD1 ? C ASN 56  OD1 
46 1 Y 1 C ASN 56  ? ND2 ? C ASN 56  ND2 
47 1 Y 1 C LYS 57  ? CD  ? C LYS 57  CD  
48 1 Y 1 C LYS 57  ? CE  ? C LYS 57  CE  
49 1 Y 1 C LYS 57  ? NZ  ? C LYS 57  NZ  
50 1 Y 1 C GLN 79  ? CD  ? C GLN 79  CD  
51 1 Y 1 C GLN 79  ? OE1 ? C GLN 79  OE1 
52 1 Y 1 C GLN 79  ? NE2 ? C GLN 79  NE2 
53 1 Y 1 C GLN 82  ? CG  ? C GLN 82  CG  
54 1 Y 1 C GLN 82  ? CD  ? C GLN 82  CD  
55 1 Y 1 C GLN 82  ? OE1 ? C GLN 82  OE1 
56 1 Y 1 C GLN 82  ? NE2 ? C GLN 82  NE2 
57 1 Y 1 C ARG 194 ? CD  ? C ARG 194 CD  
58 1 Y 1 C ARG 194 ? NE  ? C ARG 194 NE  
59 1 Y 1 C ARG 194 ? CZ  ? C ARG 194 CZ  
60 1 Y 1 C ARG 194 ? NH1 ? C ARG 194 NH1 
61 1 Y 1 C ARG 194 ? NH2 ? C ARG 194 NH2 
62 1 Y 1 C GLN 219 ? CG  ? C GLN 219 CG  
63 1 Y 1 C GLN 219 ? CD  ? C GLN 219 CD  
64 1 Y 1 C GLN 219 ? OE1 ? C GLN 219 OE1 
65 1 Y 1 C GLN 219 ? NE2 ? C GLN 219 NE2 
66 1 Y 1 C ASP 235 ? CB  ? C ASP 235 CB  
67 1 Y 1 C ASP 235 ? CG  ? C ASP 235 CG  
68 1 Y 1 C ASP 235 ? OD1 ? C ASP 235 OD1 
69 1 Y 1 C ASP 235 ? OD2 ? C ASP 235 OD2 
70 1 Y 1 C ARG 240 ? CD  ? C ARG 240 CD  
71 1 Y 1 C ARG 240 ? NE  ? C ARG 240 NE  
72 1 Y 1 C ARG 240 ? CZ  ? C ARG 240 CZ  
73 1 Y 1 C ARG 240 ? NH1 ? C ARG 240 NH1 
74 1 Y 1 C ARG 240 ? NH2 ? C ARG 240 NH2 
75 1 Y 1 C ASP 253 ? CG  ? C ASP 253 CG  
76 1 Y 1 C ASP 253 ? OD1 ? C ASP 253 OD1 
77 1 Y 1 C ASP 253 ? OD2 ? C ASP 253 OD2 
78 1 Y 1 D ARG 194 ? NE  ? D ARG 194 NE  
79 1 Y 1 D ARG 194 ? CZ  ? D ARG 194 CZ  
80 1 Y 1 D ARG 194 ? NH1 ? D ARG 194 NH1 
81 1 Y 1 D ARG 194 ? NH2 ? D ARG 194 NH2 
82 1 Y 1 D ARG 240 ? CG  ? D ARG 240 CG  
83 1 Y 1 D ARG 240 ? CD  ? D ARG 240 CD  
84 1 Y 1 D ARG 240 ? NE  ? D ARG 240 NE  
85 1 Y 1 D ARG 240 ? CZ  ? D ARG 240 CZ  
86 1 Y 1 D ARG 240 ? NH1 ? D ARG 240 NH1 
87 1 Y 1 D ARG 240 ? NH2 ? D ARG 240 NH2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? XDS         ? ? ? .        1 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.006    2 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? SCALA       ? ? ? .        3 
? refinement        ? ? ? ? ? ? ? ? ? ? ? REFMAC      ? ? ? 5.6.0117 4 
? 'model building'  ? ? ? ? ? ? ? ? ? ? ? Coot        ? ? ? .        5 
? phasing           ? ? ? ? ? ? ? ? ? ? ? MOLREP      ? ? ? .        6 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   108.660 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     4WW8 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     77.313 
_cell.length_a_esd                 ? 
_cell.length_b                     74.260 
_cell.length_b_esd                 ? 
_cell.length_c                     91.570 
_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                         4WW8 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   4WW8 
_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            2.08 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         40.5 
_exptl_crystal.description                 ? 
_exptl_crystal.F_000                       ? 
_exptl_crystal.id                          1 
_exptl_crystal.preparation                 ? 
_exptl_crystal.size_max                    ? 
_exptl_crystal.size_mid                    ? 
_exptl_crystal.size_min                    ? 
_exptl_crystal.size_rad                    ? 
_exptl_crystal.colour_lustre               ? 
_exptl_crystal.colour_modifier             ? 
_exptl_crystal.colour_primary              ? 
_exptl_crystal.density_meas                ? 
_exptl_crystal.density_meas_esd            ? 
_exptl_crystal.density_meas_gt             ? 
_exptl_crystal.density_meas_lt             ? 
_exptl_crystal.density_meas_temp           ? 
_exptl_crystal.density_meas_temp_esd       ? 
_exptl_crystal.density_meas_temp_gt        ? 
_exptl_crystal.density_meas_temp_lt        ? 
_exptl_crystal.pdbx_crystal_image_url      ? 
_exptl_crystal.pdbx_crystal_image_format   ? 
_exptl_crystal.pdbx_mosaicity              ? 
_exptl_crystal.pdbx_mosaicity_esd          ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.0 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp            291 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
'Crystallization buffer: 0.1M ammonium citrate (pH 7.0), 0.2M ammonium sulfate and 30% PEG4000.' 
_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         2014-01-08 
# 
_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 P14 (MX2)' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.826606 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'P14 (MX2)' 
_diffrn_source.pdbx_synchrotron_site       'PETRA III, EMBL c/o DESY' 
# 
_reflns.B_iso_Wilson_estimate            ? 
_reflns.entry_id                         4WW8 
_reflns.data_reduction_details           ? 
_reflns.data_reduction_method            ? 
_reflns.d_resolution_high                1.420 
_reflns.d_resolution_low                 74.260 
_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                       176873 
_reflns.number_obs                       176873 
_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             95.800 
_reflns.R_free_details                   ? 
_reflns.Rmerge_F_all                     ? 
_reflns.Rmerge_F_obs                     ? 
_reflns.Friedel_coverage                 ? 
_reflns.number_gt                        ? 
_reflns.threshold_expression             ? 
_reflns.pdbx_redundancy                  6.700 
_reflns.pdbx_Rmerge_I_obs                ? 
_reflns.pdbx_Rmerge_I_all                ? 
_reflns.pdbx_Rsym_value                  0.054 
_reflns.pdbx_netI_over_av_sigmaI         5.314 
_reflns.pdbx_netI_over_sigmaI            16.700 
_reflns.pdbx_res_netI_over_av_sigmaI_2   ? 
_reflns.pdbx_res_netI_over_sigmaI_2      ? 
_reflns.pdbx_chi_squared                 ? 
_reflns.pdbx_scaling_rejects             ? 
_reflns.pdbx_d_res_high_opt              ? 
_reflns.pdbx_d_res_low_opt               ? 
_reflns.pdbx_d_res_opt_method            ? 
_reflns.phase_calculation_details        ? 
_reflns.pdbx_Rrim_I_all                  0.064 
_reflns.pdbx_Rpim_I_all                  0.024 
_reflns.pdbx_d_opt                       ? 
_reflns.pdbx_number_measured_all         1192219 
_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 
1.42 1.50  ? 2.0  118275 ? ? 21090 ? 79.00 ? ? ? 0.453 0.370 ? ? ? ? ? ? ? ? 5.60 0.370 ? ? 3.90  0.45 0.19 ? 1  1 ? ? 
1.50 1.59  ? 2.7  171340 ? ? 25006 ? 98.20 ? ? ? 0.319 0.270 ? ? ? ? ? ? ? ? 6.90 0.270 ? ? 6.00  0.32 0.12 ? 2  ? ? ? 
1.59 1.70  ? 4.2  161966 ? ? 23616 ? 98.60 ? ? ? 0.209 0.176 ? ? ? ? ? ? ? ? 6.90 0.176 ? ? 8.30  0.21 0.08 ? 3  ? ? ? 
1.70 1.83  ? 6.4  151777 ? ? 21970 ? 98.80 ? ? ? 0.135 0.112 ? ? ? ? ? ? ? ? 6.90 0.112 ? ? 11.80 0.14 0.05 ? 4  ? ? ? 
1.83 2.01  ? 9.4  138563 ? ? 20242 ? 98.80 ? ? ? 0.088 0.072 ? ? ? ? ? ? ? ? 6.80 0.072 ? ? 16.90 0.09 0.03 ? 5  ? ? ? 
2.01 2.25  ? 11.8 124324 ? ? 18323 ? 98.80 ? ? ? 0.065 0.053 ? ? ? ? ? ? ? ? 6.80 0.053 ? ? 22.50 0.06 0.03 ? 6  ? ? ? 
2.25 2.59  ? 12.9 113745 ? ? 16283 ? 99.20 ? ? ? 0.055 0.045 ? ? ? ? ? ? ? ? 7.00 0.045 ? ? 26.90 0.05 0.02 ? 7  ? ? ? 
2.59 3.18  ? 12.7 97329  ? ? 13729 ? 98.70 ? ? ? 0.048 0.040 ? ? ? ? ? ? ? ? 7.10 0.040 ? ? 32.20 0.05 0.02 ? 8  ? ? ? 
3.18 4.49  ? 11.8 74699  ? ? 10681 ? 99.00 ? ? ? 0.046 0.040 ? ? ? ? ? ? ? ? 7.00 0.040 ? ? 38.20 0.05 0.02 ? 9  ? ? ? 
4.49 74.26 ? 7.7  40201  ? ? 5933  ? 98.90 ? ? ? 0.058 0.050 ? ? ? ? ? ? ? ? 6.80 0.050 ? ? 37.40 0.06 0.02 ? 10 ? ? ? 
# 
_refine.aniso_B[1][1]                            -0.400 
_refine.aniso_B[1][2]                            0.000 
_refine.aniso_B[1][3]                            0.240 
_refine.aniso_B[2][2]                            0.310 
_refine.aniso_B[2][3]                            0.000 
_refine.aniso_B[3][3]                            0.240 
_refine.B_iso_max                                78.64 
_refine.B_iso_mean                               18.976 
_refine.B_iso_min                                6.06 
_refine.correlation_coeff_Fo_to_Fc               0.971 
_refine.correlation_coeff_Fo_to_Fc_free          0.959 
_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                                 4WW8 
_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                            1.420 
_refine.ls_d_res_low                             56.420 
_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                     176847 
_refine.ls_number_reflns_R_free                  17544 
_refine.ls_number_reflns_R_work                  159303 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    95.700 
_refine.ls_percent_reflns_R_free                 9.900 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.175 
_refine.ls_R_factor_R_free                       0.205 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.172 
_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                      0.212 
_refine.ls_wR_factor_R_work                      0.178 
_refine.occupancy_max                            1.00 
_refine.occupancy_min                            0.00 
_refine.solvent_model_details                    MASK 
_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                          0.00 
_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                      1JD0 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.072 
_refine.pdbx_overall_ESU_R_Free                  0.075 
_refine.pdbx_solvent_vdw_probe_radii             1.400 
_refine.pdbx_solvent_ion_probe_radii             0.800 
_refine.pdbx_solvent_shrinkage_radii             0.800 
_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             0.072 
_refine.overall_SU_R_free                        0.075 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   0.854 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        8380 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         112 
_refine_hist.number_atoms_solvent             912 
_refine_hist.number_atoms_total               9404 
_refine_hist.d_res_high                       1.420 
_refine_hist.d_res_low                        56.420 
# 
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' ? 0.024  0.020  8951  ? r_bond_refined_d       ? ? 
'X-RAY DIFFRACTION' ? 2.270  1.950  12216 ? r_angle_refined_deg    ? ? 
'X-RAY DIFFRACTION' ? 7.030  5.000  1103  ? r_dihedral_angle_1_deg ? ? 
'X-RAY DIFFRACTION' ? 36.784 24.700 434   ? r_dihedral_angle_2_deg ? ? 
'X-RAY DIFFRACTION' ? 12.229 15.000 1377  ? r_dihedral_angle_3_deg ? ? 
'X-RAY DIFFRACTION' ? 16.090 15.000 28    ? r_dihedral_angle_4_deg ? ? 
'X-RAY DIFFRACTION' ? 0.173  0.200  1276  ? r_chiral_restr         ? ? 
'X-RAY DIFFRACTION' ? 0.014  0.021  7077  ? r_gen_planes_refined   ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.420 
_refine_ls_shell.d_res_low                        1.457 
_refine_ls_shell.number_reflns_all                8790 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             852 
_refine_ls_shell.number_reflns_R_work             7938 
_refine_ls_shell.percent_reflns_obs               64.390 
_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                  0.270 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.237 
_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                     4WW8 
_struct.title                        
'Crystal structure of human carbonic anhydrase isozyme XII with 4-Propylthiobenzenesulfonamide' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               ? 
# 
_struct_keywords.entry_id        4WW8 
_struct_keywords.text            
'drug design, carbonic anhydrase, benzenesulfonamide, metal-binding, lyase-lyase inhibitor comple, 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 1 ? 
D  N N 1 ? 
E  N N 2 ? 
F  N N 3 ? 
G  N N 3 ? 
H  N N 3 ? 
I  N N 4 ? 
J  N N 2 ? 
K  N N 3 ? 
L  N N 3 ? 
M  N N 3 ? 
N  N N 3 ? 
O  N N 3 ? 
P  N N 3 ? 
Q  N N 4 ? 
R  N N 2 ? 
S  N N 3 ? 
T  N N 3 ? 
U  N N 4 ? 
V  N N 2 ? 
W  N N 3 ? 
X  N N 3 ? 
Y  N N 4 ? 
Z  N N 5 ? 
AA N N 5 ? 
BA N N 5 ? 
CA N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CAH12_HUMAN 
_struct_ref.pdbx_db_accession          O43570 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SKWTYFGPDGENSWSKKYPSCGGLLQSPIDLHSDILQYDASLTPLEFQGYNLSANKQFLLTNNGHSVKLNLPSDMHIQGL
QSRYSATQLHLHWGNPNDPHGSEHTVSGQHFAAELHIVHYNSDLYPDASTASNKSEGLAVLAVLIEMGSFNPSYDKIFSH
LQHVKYKGQEAFVPGFNIEELLPERTAEYYRYRGSLTTPPCNPTVLWTVFRNPVQISQEQLLALETALYCTHMDDPSPRE
MINNFRQVQKFDERLVYTSFSQ
;
_struct_ref.pdbx_align_begin           30 
# 
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 4WW8 A 2 ? 263 ? O43570 30 ? 291 ? 2 263 
2 1 4WW8 B 2 ? 263 ? O43570 30 ? 291 ? 2 263 
3 1 4WW8 C 2 ? 263 ? O43570 30 ? 291 ? 2 263 
4 1 4WW8 D 2 ? 263 ? O43570 30 ? 291 ? 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 4WW8 MET A 1 ? UNP O43570 ? ? 'initiating methionine' 1 1 
2 4WW8 MET B 1 ? UNP O43570 ? ? 'initiating methionine' 1 2 
3 4WW8 MET C 1 ? UNP O43570 ? ? 'initiating methionine' 1 3 
4 4WW8 MET D 1 ? UNP O43570 ? ? 'initiating methionine' 1 4 
# 
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 ? dimeric 2 
2 author_defined_assembly ? dimeric 2 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,B,E,F,G,H,I,J,K,L,M,N,O,P,Q,Z,AA 
2 1 C,D,R,S,T,U,V,W,X,Y,BA,CA          
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
_struct_biol.details                      'The asymmetric unit contains two dimers:' 
_struct_biol.id                           1 
_struct_biol.pdbx_parent_biol_id          ? 
_struct_biol.pdbx_formula_weight          ? 
_struct_biol.pdbx_formula_weight_method   ? 
_struct_biol.pdbx_aggregation_state       ? 
_struct_biol.pdbx_assembly_method         ? 
# 
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 PHE A 7   ? TRP A 15  ? PHE A 7   TRP A 15  5 ? 9  
HELX_P HELX_P2  AA2 TYR A 19  ? GLY A 24  ? TYR A 19  GLY A 24  5 ? 6  
HELX_P HELX_P3  AA3 HIS A 33  ? ASP A 35  ? HIS A 33  ASP A 35  5 ? 3  
HELX_P HELX_P4  AA4 ASP A 128 ? SER A 133 ? ASP A 128 SER A 133 1 ? 6  
HELX_P HELX_P5  AA5 ASN A 152 ? SER A 160 ? ASN A 152 SER A 160 1 ? 9  
HELX_P HELX_P6  AA6 HIS A 161 ? LYS A 166 ? HIS A 161 LYS A 166 5 ? 6  
HELX_P HELX_P7  AA7 ASN A 178 ? LEU A 183 ? ASN A 178 LEU A 183 5 ? 6  
HELX_P HELX_P8  AA8 SER A 218 ? ALA A 228 ? SER A 218 ALA A 228 1 ? 11 
HELX_P HELX_P9  AA9 GLY B 11  ? ASN B 13  ? GLY B 11  ASN B 13  5 ? 3  
HELX_P HELX_P10 AB1 SER B 14  ? TYR B 19  ? SER B 14  TYR B 19  1 ? 6  
HELX_P HELX_P11 AB2 PRO B 20  ? GLY B 24  ? PRO B 20  GLY B 24  5 ? 5  
HELX_P HELX_P12 AB3 HIS B 33  ? ASP B 35  ? HIS B 33  ASP B 35  5 ? 3  
HELX_P HELX_P13 AB4 ASP B 128 ? SER B 133 ? ASP B 128 SER B 133 1 ? 6  
HELX_P HELX_P14 AB5 ASN B 152 ? SER B 160 ? ASN B 152 SER B 160 1 ? 9  
HELX_P HELX_P15 AB6 HIS B 161 ? VAL B 165 ? HIS B 161 VAL B 165 5 ? 5  
HELX_P HELX_P16 AB7 ASN B 178 ? LEU B 183 ? ASN B 178 LEU B 183 5 ? 6  
HELX_P HELX_P17 AB8 SER B 218 ? LEU B 229 ? SER B 218 LEU B 229 1 ? 12 
HELX_P HELX_P18 AB9 PHE C 7   ? GLY C 11  ? PHE C 7   GLY C 11  5 ? 5  
HELX_P HELX_P19 AC1 SER C 14  ? LYS C 18  ? SER C 14  LYS C 18  5 ? 5  
HELX_P HELX_P20 AC2 TYR C 19  ? GLY C 24  ? TYR C 19  GLY C 24  5 ? 6  
HELX_P HELX_P21 AC3 HIS C 33  ? ASP C 35  ? HIS C 33  ASP C 35  5 ? 3  
HELX_P HELX_P22 AC4 ASP C 128 ? SER C 133 ? ASP C 128 SER C 133 1 ? 6  
HELX_P HELX_P23 AC5 TYR C 155 ? SER C 160 ? TYR C 155 SER C 160 1 ? 6  
HELX_P HELX_P24 AC6 HIS C 161 ? VAL C 165 ? HIS C 161 VAL C 165 5 ? 5  
HELX_P HELX_P25 AC7 ASN C 178 ? LEU C 183 ? ASN C 178 LEU C 183 5 ? 6  
HELX_P HELX_P26 AC8 SER C 218 ? ALA C 228 ? SER C 218 ALA C 228 1 ? 11 
HELX_P HELX_P27 AC9 GLY D 11  ? LYS D 18  ? GLY D 11  LYS D 18  5 ? 8  
HELX_P HELX_P28 AD1 TYR D 19  ? GLY D 24  ? TYR D 19  GLY D 24  5 ? 6  
HELX_P HELX_P29 AD2 HIS D 33  ? ASP D 35  ? HIS D 33  ASP D 35  5 ? 3  
HELX_P HELX_P30 AD3 ASP D 128 ? SER D 133 ? ASP D 128 SER D 133 1 ? 6  
HELX_P HELX_P31 AD4 SER D 154 ? SER D 160 ? SER D 154 SER D 160 1 ? 7  
HELX_P HELX_P32 AD5 HIS D 161 ? VAL D 165 ? HIS D 161 VAL D 165 5 ? 5  
HELX_P HELX_P33 AD6 ASN D 178 ? LEU D 183 ? ASN D 178 LEU D 183 5 ? 6  
HELX_P HELX_P34 AD7 SER D 218 ? LEU D 229 ? SER D 218 LEU D 229 1 ? 12 
# 
_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 
disulf1  disulf ? ? A CYS 22  SG  ? ? ? 1_555 A CYS 202 SG ? ? A CYS 22  A CYS 202 1_555 ? ? ? ? ? ? ? 2.087 ? ? 
disulf2  disulf ? ? B CYS 22  SG  ? ? ? 1_555 B CYS 202 SG ? ? B CYS 22  B CYS 202 1_555 ? ? ? ? ? ? ? 2.052 ? ? 
disulf3  disulf ? ? C CYS 22  SG  ? ? ? 1_555 C CYS 202 SG ? ? C CYS 22  C CYS 202 1_555 ? ? ? ? ? ? ? 2.093 ? ? 
disulf4  disulf ? ? D CYS 22  SG  ? ? ? 1_555 D CYS 202 SG ? ? D CYS 22  D CYS 202 1_555 ? ? ? ? ? ? ? 2.063 ? ? 
metalc1  metalc ? ? A HIS 91  NE2 ? ? ? 1_555 E ZN  .   ZN ? ? A HIS 91  A ZN  301 1_555 ? ? ? ? ? ? ? 2.030 ? ? 
metalc2  metalc ? ? A HIS 93  NE2 ? ? ? 1_555 E ZN  .   ZN ? ? A HIS 93  A ZN  301 1_555 ? ? ? ? ? ? ? 2.041 ? ? 
metalc3  metalc ? ? A HIS 117 ND1 ? ? ? 1_555 E ZN  .   ZN ? ? A HIS 117 A ZN  301 1_555 ? ? ? ? ? ? ? 2.015 ? ? 
metalc4  metalc ? ? E ZN  .   ZN  ? ? ? 1_555 I VD9 .   S2 ? ? A ZN  301 A VD9 305 1_555 ? ? ? ? ? ? ? 2.996 ? ? 
metalc5  metalc ? ? E ZN  .   ZN  ? ? ? 1_555 I VD9 .   N3 ? ? A ZN  301 A VD9 305 1_555 ? ? ? ? ? ? ? 1.936 ? ? 
metalc6  metalc ? ? B HIS 91  NE2 ? ? ? 1_555 J ZN  .   ZN ? ? B HIS 91  B ZN  301 1_555 ? ? ? ? ? ? ? 2.007 ? ? 
metalc7  metalc ? ? B HIS 93  NE2 ? ? ? 1_555 J ZN  .   ZN ? ? B HIS 93  B ZN  301 1_555 ? ? ? ? ? ? ? 2.029 ? ? 
metalc8  metalc ? ? B HIS 117 ND1 ? ? ? 1_555 J ZN  .   ZN ? ? B HIS 117 B ZN  301 1_555 ? ? ? ? ? ? ? 2.006 ? ? 
metalc9  metalc ? ? J ZN  .   ZN  ? ? ? 1_555 Q VD9 .   N3 ? ? B ZN  301 B VD9 308 1_555 ? ? ? ? ? ? ? 1.870 ? ? 
metalc10 metalc ? ? C HIS 91  NE2 ? ? ? 1_555 R ZN  .   ZN ? ? C HIS 91  C ZN  301 1_555 ? ? ? ? ? ? ? 2.017 ? ? 
metalc11 metalc ? ? C HIS 93  NE2 ? ? ? 1_555 R ZN  .   ZN ? ? C HIS 93  C ZN  301 1_555 ? ? ? ? ? ? ? 2.060 ? ? 
metalc12 metalc ? ? C HIS 117 ND1 ? ? ? 1_555 R ZN  .   ZN ? ? C HIS 117 C ZN  301 1_555 ? ? ? ? ? ? ? 1.981 ? ? 
metalc13 metalc ? ? R ZN  .   ZN  ? ? ? 1_555 U VD9 .   S2 ? ? C ZN  301 C VD9 304 1_555 ? ? ? ? ? ? ? 2.986 ? ? 
metalc14 metalc ? ? R ZN  .   ZN  ? ? ? 1_555 U VD9 .   N3 ? ? C ZN  301 C VD9 304 1_555 ? ? ? ? ? ? ? 1.964 ? ? 
metalc15 metalc ? ? D HIS 91  NE2 ? ? ? 1_555 V ZN  .   ZN ? ? D HIS 91  D ZN  301 1_555 ? ? ? ? ? ? ? 2.001 ? ? 
metalc16 metalc ? ? D HIS 93  NE2 ? ? ? 1_555 V ZN  .   ZN ? ? D HIS 93  D ZN  301 1_555 ? ? ? ? ? ? ? 2.009 ? ? 
metalc17 metalc ? ? D HIS 117 ND1 ? ? ? 1_555 V ZN  .   ZN ? ? D HIS 117 D ZN  301 1_555 ? ? ? ? ? ? ? 2.043 ? ? 
metalc18 metalc ? ? V ZN  .   ZN  ? ? ? 1_555 Y VD9 .   N3 ? ? D ZN  301 D VD9 304 1_555 ? ? ? ? ? ? ? 1.963 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
metalc ? ? 
# 
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 91  ? A HIS 91  ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 NE2 ? A HIS 93  ? A HIS 93  ? 1_555 103.4 ? 
2  NE2 ? A HIS 91  ? A HIS 91  ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 117 ? A HIS 117 ? 1_555 111.4 ? 
3  NE2 ? A HIS 93  ? A HIS 93  ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 ND1 ? A HIS 117 ? A HIS 117 ? 1_555 99.3  ? 
4  NE2 ? A HIS 91  ? A HIS 91  ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 S2  ? I VD9 .   ? A VD9 305 ? 1_555 97.9  ? 
5  NE2 ? A HIS 93  ? A HIS 93  ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 S2  ? I VD9 .   ? A VD9 305 ? 1_555 142.6 ? 
6  ND1 ? A HIS 117 ? A HIS 117 ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 S2  ? I VD9 .   ? A VD9 305 ? 1_555 101.0 ? 
7  NE2 ? A HIS 91  ? A HIS 91  ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 N3  ? I VD9 .   ? A VD9 305 ? 1_555 110.5 ? 
8  NE2 ? A HIS 93  ? A HIS 93  ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 N3  ? I VD9 .   ? A VD9 305 ? 1_555 114.0 ? 
9  ND1 ? A HIS 117 ? A HIS 117 ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 N3  ? I VD9 .   ? A VD9 305 ? 1_555 117.0 ? 
10 S2  ? I VD9 .   ? A VD9 305 ? 1_555 ZN ? E ZN . ? A ZN 301 ? 1_555 N3  ? I VD9 .   ? A VD9 305 ? 1_555 28.7  ? 
11 NE2 ? B HIS 91  ? B HIS 91  ? 1_555 ZN ? J ZN . ? B ZN 301 ? 1_555 NE2 ? B HIS 93  ? B HIS 93  ? 1_555 103.1 ? 
12 NE2 ? B HIS 91  ? B HIS 91  ? 1_555 ZN ? J ZN . ? B ZN 301 ? 1_555 ND1 ? B HIS 117 ? B HIS 117 ? 1_555 111.6 ? 
13 NE2 ? B HIS 93  ? B HIS 93  ? 1_555 ZN ? J ZN . ? B ZN 301 ? 1_555 ND1 ? B HIS 117 ? B HIS 117 ? 1_555 99.3  ? 
14 NE2 ? B HIS 91  ? B HIS 91  ? 1_555 ZN ? J ZN . ? B ZN 301 ? 1_555 N3  ? Q VD9 .   ? B VD9 308 ? 1_555 111.1 ? 
15 NE2 ? B HIS 93  ? B HIS 93  ? 1_555 ZN ? J ZN . ? B ZN 301 ? 1_555 N3  ? Q VD9 .   ? B VD9 308 ? 1_555 115.1 ? 
16 ND1 ? B HIS 117 ? B HIS 117 ? 1_555 ZN ? J ZN . ? B ZN 301 ? 1_555 N3  ? Q VD9 .   ? B VD9 308 ? 1_555 115.5 ? 
17 NE2 ? C HIS 91  ? C HIS 91  ? 1_555 ZN ? R ZN . ? C ZN 301 ? 1_555 NE2 ? C HIS 93  ? C HIS 93  ? 1_555 101.1 ? 
18 NE2 ? C HIS 91  ? C HIS 91  ? 1_555 ZN ? R ZN . ? C ZN 301 ? 1_555 ND1 ? C HIS 117 ? C HIS 117 ? 1_555 114.2 ? 
19 NE2 ? C HIS 93  ? C HIS 93  ? 1_555 ZN ? R ZN . ? C ZN 301 ? 1_555 ND1 ? C HIS 117 ? C HIS 117 ? 1_555 99.1  ? 
20 NE2 ? C HIS 91  ? C HIS 91  ? 1_555 ZN ? R ZN . ? C ZN 301 ? 1_555 S2  ? U VD9 .   ? C VD9 304 ? 1_555 98.8  ? 
21 NE2 ? C HIS 93  ? C HIS 93  ? 1_555 ZN ? R ZN . ? C ZN 301 ? 1_555 S2  ? U VD9 .   ? C VD9 304 ? 1_555 142.9 ? 
22 ND1 ? C HIS 117 ? C HIS 117 ? 1_555 ZN ? R ZN . ? C ZN 301 ? 1_555 S2  ? U VD9 .   ? C VD9 304 ? 1_555 100.8 ? 
23 NE2 ? C HIS 91  ? C HIS 91  ? 1_555 ZN ? R ZN . ? C ZN 301 ? 1_555 N3  ? U VD9 .   ? C VD9 304 ? 1_555 111.9 ? 
24 NE2 ? C HIS 93  ? C HIS 93  ? 1_555 ZN ? R ZN . ? C ZN 301 ? 1_555 N3  ? U VD9 .   ? C VD9 304 ? 1_555 113.2 ? 
25 ND1 ? C HIS 117 ? C HIS 117 ? 1_555 ZN ? R ZN . ? C ZN 301 ? 1_555 N3  ? U VD9 .   ? C VD9 304 ? 1_555 115.7 ? 
26 S2  ? U VD9 .   ? C VD9 304 ? 1_555 ZN ? R ZN . ? C ZN 301 ? 1_555 N3  ? U VD9 .   ? C VD9 304 ? 1_555 29.8  ? 
27 NE2 ? D HIS 91  ? D HIS 91  ? 1_555 ZN ? V ZN . ? D ZN 301 ? 1_555 NE2 ? D HIS 93  ? D HIS 93  ? 1_555 103.6 ? 
28 NE2 ? D HIS 91  ? D HIS 91  ? 1_555 ZN ? V ZN . ? D ZN 301 ? 1_555 ND1 ? D HIS 117 ? D HIS 117 ? 1_555 111.6 ? 
29 NE2 ? D HIS 93  ? D HIS 93  ? 1_555 ZN ? V ZN . ? D ZN 301 ? 1_555 ND1 ? D HIS 117 ? D HIS 117 ? 1_555 99.2  ? 
30 NE2 ? D HIS 91  ? D HIS 91  ? 1_555 ZN ? V ZN . ? D ZN 301 ? 1_555 N3  ? Y VD9 .   ? D VD9 304 ? 1_555 110.2 ? 
31 NE2 ? D HIS 93  ? D HIS 93  ? 1_555 ZN ? V ZN . ? D ZN 301 ? 1_555 N3  ? Y VD9 .   ? D VD9 304 ? 1_555 114.1 ? 
32 ND1 ? D HIS 117 ? D HIS 117 ? 1_555 ZN ? V ZN . ? D ZN 301 ? 1_555 N3  ? Y VD9 .   ? D VD9 304 ? 1_555 116.8 ? 
# 
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 28  A . ? SER 28  A PRO 29  A ? PRO 29  A 1 5.23  
2 PRO 200 A . ? PRO 200 A PRO 201 A ? PRO 201 A 1 12.20 
3 SER 28  B . ? SER 28  B PRO 29  B ? PRO 29  B 1 -2.28 
4 PRO 200 B . ? PRO 200 B PRO 201 B ? PRO 201 B 1 12.77 
5 PRO 200 B . ? PRO 200 B PRO 201 B ? PRO 201 B 1 5.72  
6 SER 28  C . ? SER 28  C PRO 29  C ? PRO 29  C 1 1.04  
7 PRO 200 C . ? PRO 200 C PRO 201 C ? PRO 201 C 1 6.42  
8 SER 28  D . ? SER 28  D PRO 29  D ? PRO 29  D 1 2.25  
9 PRO 200 D . ? PRO 200 D PRO 201 D ? PRO 201 D 1 3.82  
# 
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  ? 
AA7 ? 2  ? 
AA8 ? 10 ? 
AA9 ? 6  ? 
AB1 ? 2  ? 
AB2 ? 10 ? 
AB3 ? 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      
AA7 1 2  ? parallel      
AA8 1 2  ? parallel      
AA8 2 3  ? anti-parallel 
AA8 3 4  ? anti-parallel 
AA8 4 5  ? parallel      
AA8 5 6  ? anti-parallel 
AA8 6 7  ? anti-parallel 
AA8 7 8  ? anti-parallel 
AA8 8 9  ? anti-parallel 
AA8 9 10 ? anti-parallel 
AA9 1 2  ? anti-parallel 
AA9 2 3  ? anti-parallel 
AA9 3 4  ? anti-parallel 
AA9 4 5  ? anti-parallel 
AA9 5 6  ? parallel      
AB1 1 2  ? parallel      
AB2 1 2  ? parallel      
AB2 2 3  ? anti-parallel 
AB2 3 4  ? anti-parallel 
AB2 4 5  ? parallel      
AB2 5 6  ? anti-parallel 
AB2 6 7  ? anti-parallel 
AB2 7 8  ? anti-parallel 
AB2 8 9  ? anti-parallel 
AB2 9 10 ? anti-parallel 
AB3 1 2  ? anti-parallel 
AB3 2 3  ? anti-parallel 
AB3 3 4  ? anti-parallel 
AB3 4 5  ? anti-parallel 
AB3 5 6  ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1  ASP A 31  ? LEU A 32  ? ASP A 31  LEU A 32  
AA1 2  THR A 106 ? VAL A 107 ? THR A 106 VAL A 107 
AA2 1  LEU A 37  ? TYR A 39  ? LEU A 37  TYR A 39  
AA2 2  VAL A 257 ? THR A 259 ? VAL A 257 THR A 259 
AA2 3  TYR A 190 ? GLY A 195 ? TYR A 190 GLY A 195 
AA2 4  VAL A 206 ? PHE A 211 ? VAL A 206 PHE A 211 
AA2 5  LEU A 139 ? MET A 148 ? LEU A 139 MET A 148 
AA2 6  ALA A 114 ? ASN A 122 ? ALA A 114 ASN A 122 
AA2 7  TYR A 85  ? TRP A 94  ? TYR A 85  TRP A 94  
AA2 8  VAL A 68  ? ASN A 71  ? VAL A 68  ASN A 71  
AA2 9  GLN A 58  ? ASN A 63  ? GLN A 58  ASN A 63  
AA2 10 GLU A 171 ? PRO A 175 ? GLU A 171 PRO A 175 
AA3 1  GLU A 47  ? GLN A 49  ? GLU A 47  GLN A 49  
AA3 2  HIS A 77  ? GLN A 79  ? HIS A 77  GLN A 79  
AA3 3  TYR A 85  ? TRP A 94  ? TYR A 85  TRP A 94  
AA3 4  ALA A 114 ? ASN A 122 ? ALA A 114 ASN A 122 
AA3 5  LEU A 139 ? MET A 148 ? LEU A 139 MET A 148 
AA3 6  VAL A 215 ? ILE A 217 ? VAL A 215 ILE A 217 
AA4 1  ASP B 31  ? LEU B 32  ? ASP B 31  LEU B 32  
AA4 2  THR B 106 ? VAL B 107 ? THR B 106 VAL B 107 
AA5 1  LEU B 37  ? TYR B 39  ? LEU B 37  TYR B 39  
AA5 2  VAL B 257 ? THR B 259 ? VAL B 257 THR B 259 
AA5 3  TYR B 190 ? GLY B 195 ? TYR B 190 GLY B 195 
AA5 4  VAL B 206 ? PHE B 211 ? VAL B 206 PHE B 211 
AA5 5  LEU B 139 ? MET B 148 ? LEU B 139 MET B 148 
AA5 6  ALA B 114 ? ASN B 122 ? ALA B 114 ASN B 122 
AA5 7  TYR B 85  ? TRP B 94  ? TYR B 85  TRP B 94  
AA5 8  VAL B 68  ? ASN B 71  ? VAL B 68  ASN B 71  
AA5 9  GLN B 58  ? ASN B 63  ? GLN B 58  ASN B 63  
AA5 10 GLU B 171 ? PRO B 175 ? GLU B 171 PRO B 175 
AA6 1  GLU B 47  ? GLN B 49  ? GLU B 47  GLN B 49  
AA6 2  HIS B 77  ? GLN B 79  ? HIS B 77  GLN B 79  
AA6 3  TYR B 85  ? TRP B 94  ? TYR B 85  TRP B 94  
AA6 4  ALA B 114 ? ASN B 122 ? ALA B 114 ASN B 122 
AA6 5  LEU B 139 ? MET B 148 ? LEU B 139 MET B 148 
AA6 6  VAL B 215 ? ILE B 217 ? VAL B 215 ILE B 217 
AA7 1  ASP C 31  ? LEU C 32  ? ASP C 31  LEU C 32  
AA7 2  THR C 106 ? VAL C 107 ? THR C 106 VAL C 107 
AA8 1  LEU C 37  ? TYR C 39  ? LEU C 37  TYR C 39  
AA8 2  VAL C 257 ? THR C 259 ? VAL C 257 THR C 259 
AA8 3  TYR C 190 ? GLY C 195 ? TYR C 190 GLY C 195 
AA8 4  VAL C 206 ? PHE C 211 ? VAL C 206 PHE C 211 
AA8 5  LEU C 139 ? MET C 148 ? LEU C 139 MET C 148 
AA8 6  ALA C 114 ? ASN C 122 ? ALA C 114 ASN C 122 
AA8 7  TYR C 85  ? TRP C 94  ? TYR C 85  TRP C 94  
AA8 8  VAL C 68  ? ASN C 71  ? VAL C 68  ASN C 71  
AA8 9  GLN C 58  ? ASN C 63  ? GLN C 58  ASN C 63  
AA8 10 GLU C 171 ? PRO C 175 ? GLU C 171 PRO C 175 
AA9 1  GLU C 47  ? GLN C 49  ? GLU C 47  GLN C 49  
AA9 2  HIS C 77  ? GLN C 79  ? HIS C 77  GLN C 79  
AA9 3  TYR C 85  ? TRP C 94  ? TYR C 85  TRP C 94  
AA9 4  ALA C 114 ? ASN C 122 ? ALA C 114 ASN C 122 
AA9 5  LEU C 139 ? MET C 148 ? LEU C 139 MET C 148 
AA9 6  VAL C 215 ? ILE C 217 ? VAL C 215 ILE C 217 
AB1 1  ASP D 31  ? LEU D 32  ? ASP D 31  LEU D 32  
AB1 2  THR D 106 ? VAL D 107 ? THR D 106 VAL D 107 
AB2 1  LEU D 37  ? TYR D 39  ? LEU D 37  TYR D 39  
AB2 2  VAL D 257 ? THR D 259 ? VAL D 257 THR D 259 
AB2 3  TYR D 190 ? GLY D 195 ? TYR D 190 GLY D 195 
AB2 4  VAL D 206 ? PHE D 211 ? VAL D 206 PHE D 211 
AB2 5  LEU D 139 ? MET D 148 ? LEU D 139 MET D 148 
AB2 6  ALA D 114 ? ASN D 122 ? ALA D 114 ASN D 122 
AB2 7  TYR D 85  ? TRP D 94  ? TYR D 85  TRP D 94  
AB2 8  VAL D 68  ? ASN D 71  ? VAL D 68  ASN D 71  
AB2 9  GLN D 58  ? ASN D 63  ? GLN D 58  ASN D 63  
AB2 10 GLU D 171 ? PRO D 175 ? GLU D 171 PRO D 175 
AB3 1  GLU D 47  ? GLN D 49  ? GLU D 47  GLN D 49  
AB3 2  HIS D 77  ? GLN D 79  ? HIS D 77  GLN D 79  
AB3 3  TYR D 85  ? TRP D 94  ? TYR D 85  TRP D 94  
AB3 4  ALA D 114 ? ASN D 122 ? ALA D 114 ASN D 122 
AB3 5  LEU D 139 ? MET D 148 ? LEU D 139 MET D 148 
AB3 6  VAL D 215 ? ILE D 217 ? VAL D 215 ILE D 217 
# 
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 LEU A 32  ? N LEU A 32  O THR A 106 ? O THR A 106 
AA2 1 2  N GLN A 38  ? N GLN A 38  O THR A 259 ? O THR A 259 
AA2 2 3  O TYR A 258 ? O TYR A 258 N ARG A 192 ? N ARG A 192 
AA2 3 4  N GLY A 195 ? N GLY A 195 O VAL A 206 ? O VAL A 206 
AA2 4 5  O THR A 209 ? O THR A 209 N ALA A 143 ? N ALA A 143 
AA2 5 6  O ILE A 146 ? O ILE A 146 N ALA A 114 ? N ALA A 114 
AA2 6 7  O VAL A 119 ? O VAL A 119 N GLN A 89  ? N GLN A 89  
AA2 7 8  O LEU A 90  ? O LEU A 90  N LEU A 70  ? N LEU A 70  
AA2 8 9  O LYS A 69  ? O LYS A 69  N THR A 62  ? N THR A 62  
AA2 9 10 N LEU A 61  ? N LEU A 61  O ALA A 172 ? O ALA A 172 
AA3 1 2  N GLN A 49  ? N GLN A 49  O HIS A 77  ? O HIS A 77  
AA3 2 3  N ILE A 78  ? N ILE A 78  O TYR A 85  ? O TYR A 85  
AA3 3 4  N GLN A 89  ? N GLN A 89  O VAL A 119 ? O VAL A 119 
AA3 4 5  N ALA A 114 ? N ALA A 114 O ILE A 146 ? O ILE A 146 
AA3 5 6  N GLU A 147 ? N GLU A 147 O VAL A 215 ? O VAL A 215 
AA4 1 2  N LEU B 32  ? N LEU B 32  O THR B 106 ? O THR B 106 
AA5 1 2  N GLN B 38  ? N GLN B 38  O VAL B 257 ? O VAL B 257 
AA5 2 3  O TYR B 258 ? O TYR B 258 N ARG B 192 ? N ARG B 192 
AA5 3 4  N GLY B 195 ? N GLY B 195 O VAL B 206 ? O VAL B 206 
AA5 4 5  O THR B 209 ? O THR B 209 N ALA B 143 ? N ALA B 143 
AA5 5 6  O LEU B 142 ? O LEU B 142 N ILE B 118 ? N ILE B 118 
AA5 6 7  O VAL B 119 ? O VAL B 119 N GLN B 89  ? N GLN B 89  
AA5 7 8  O LEU B 90  ? O LEU B 90  N LEU B 70  ? N LEU B 70  
AA5 8 9  O ASN B 71  ? O ASN B 71  N LEU B 60  ? N LEU B 60  
AA5 9 10 N LEU B 61  ? N LEU B 61  O ALA B 172 ? O ALA B 172 
AA6 1 2  N GLU B 47  ? N GLU B 47  O GLN B 79  ? O GLN B 79  
AA6 2 3  N ILE B 78  ? N ILE B 78  O TYR B 85  ? O TYR B 85  
AA6 3 4  N GLN B 89  ? N GLN B 89  O VAL B 119 ? O VAL B 119 
AA6 4 5  N ILE B 118 ? N ILE B 118 O LEU B 142 ? O LEU B 142 
AA6 5 6  N GLU B 147 ? N GLU B 147 O VAL B 215 ? O VAL B 215 
AA7 1 2  N LEU C 32  ? N LEU C 32  O THR C 106 ? O THR C 106 
AA8 1 2  N GLN C 38  ? N GLN C 38  O THR C 259 ? O THR C 259 
AA8 2 3  O TYR C 258 ? O TYR C 258 N ARG C 192 ? N ARG C 192 
AA8 3 4  N GLY C 195 ? N GLY C 195 O VAL C 206 ? O VAL C 206 
AA8 4 5  O THR C 209 ? O THR C 209 N ALA C 143 ? N ALA C 143 
AA8 5 6  O VAL C 144 ? O VAL C 144 N LEU C 116 ? N LEU C 116 
AA8 6 7  O VAL C 119 ? O VAL C 119 N GLN C 89  ? N GLN C 89  
AA8 7 8  O LEU C 90  ? O LEU C 90  N LEU C 70  ? N LEU C 70  
AA8 8 9  O ASN C 71  ? O ASN C 71  N LEU C 60  ? N LEU C 60  
AA8 9 10 N LEU C 61  ? N LEU C 61  O ALA C 172 ? O ALA C 172 
AA9 1 2  N GLU C 47  ? N GLU C 47  O GLN C 79  ? O GLN C 79  
AA9 2 3  N ILE C 78  ? N ILE C 78  O TYR C 85  ? O TYR C 85  
AA9 3 4  N GLN C 89  ? N GLN C 89  O VAL C 119 ? O VAL C 119 
AA9 4 5  N LEU C 116 ? N LEU C 116 O VAL C 144 ? O VAL C 144 
AA9 5 6  N GLU C 147 ? N GLU C 147 O VAL C 215 ? O VAL C 215 
AB1 1 2  N LEU D 32  ? N LEU D 32  O THR D 106 ? O THR D 106 
AB2 1 2  N GLN D 38  ? N GLN D 38  O VAL D 257 ? O VAL D 257 
AB2 2 3  O TYR D 258 ? O TYR D 258 N ARG D 192 ? N ARG D 192 
AB2 3 4  N GLY D 195 ? N GLY D 195 O VAL D 206 ? O VAL D 206 
AB2 4 5  O THR D 209 ? O THR D 209 N ALA D 143 ? N ALA D 143 
AB2 5 6  O LEU D 142 ? O LEU D 142 N ILE D 118 ? N ILE D 118 
AB2 6 7  O VAL D 119 ? O VAL D 119 N GLN D 89  ? N GLN D 89  
AB2 7 8  O LEU D 90  ? O LEU D 90  N LEU D 70  ? N LEU D 70  
AB2 8 9  O LYS D 69  ? O LYS D 69  N THR D 62  ? N THR D 62  
AB2 9 10 N LEU D 61  ? N LEU D 61  O ALA D 172 ? O ALA D 172 
AB3 1 2  N GLN D 49  ? N GLN D 49  O HIS D 77  ? O HIS D 77  
AB3 2 3  N ILE D 78  ? N ILE D 78  O TYR D 85  ? O TYR D 85  
AB3 3 4  N GLN D 89  ? N GLN D 89  O VAL D 119 ? O VAL D 119 
AB3 4 5  N ILE D 118 ? N ILE D 118 O LEU D 142 ? O LEU D 142 
AB3 5 6  N GLU D 147 ? N GLU D 147 O VAL D 215 ? O VAL D 215 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software A ZN  301 ? 4  'binding site for residue ZN A 301'  
AC2 Software A EDO 302 ? 6  'binding site for residue EDO A 302' 
AC3 Software A EDO 303 ? 3  'binding site for residue EDO A 303' 
AC4 Software A EDO 304 ? 5  'binding site for residue EDO A 304' 
AC5 Software A VD9 305 ? 9  'binding site for residue VD9 A 305' 
AC6 Software B ZN  301 ? 4  'binding site for residue ZN B 301'  
AC7 Software B EDO 302 ? 6  'binding site for residue EDO B 302' 
AC8 Software B EDO 303 ? 6  'binding site for residue EDO B 303' 
AC9 Software B EDO 304 ? 5  'binding site for residue EDO B 304' 
AD1 Software B EDO 305 ? 6  'binding site for residue EDO B 305' 
AD2 Software B EDO 306 ? 5  'binding site for residue EDO B 306' 
AD3 Software B EDO 307 ? 4  'binding site for residue EDO B 307' 
AD4 Software B VD9 308 ? 9  'binding site for residue VD9 B 308' 
AD5 Software C ZN  301 ? 4  'binding site for residue ZN C 301'  
AD6 Software C EDO 302 ? 4  'binding site for residue EDO C 302' 
AD7 Software C EDO 303 ? 6  'binding site for residue EDO C 303' 
AD8 Software C VD9 304 ? 9  'binding site for residue VD9 C 304' 
AD9 Software D ZN  301 ? 4  'binding site for residue ZN D 301'  
AE1 Software D EDO 302 ? 8  'binding site for residue EDO D 302' 
AE2 Software D EDO 303 ? 6  'binding site for residue EDO D 303' 
AE3 Software D VD9 304 ? 10 'binding site for residue VD9 D 304' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1   AC1 4  HIS A  91  ? HIS A 91  . ? 1_555 ? 
2   AC1 4  HIS A  93  ? HIS A 93  . ? 1_555 ? 
3   AC1 4  HIS A  117 ? HIS A 117 . ? 1_555 ? 
4   AC1 4  VD9 I  .   ? VD9 A 305 . ? 1_555 ? 
5   AC2 6  ASN A  64  ? ASN A 64  . ? 1_555 ? 
6   AC2 6  GLN A  89  ? GLN A 89  . ? 1_555 ? 
7   AC2 6  HIS A  91  ? HIS A 91  . ? 1_555 ? 
8   AC2 6  HOH Z  .   ? HOH A 547 . ? 1_555 ? 
9   AC2 6  HOH Z  .   ? HOH A 583 . ? 1_555 ? 
10  AC2 6  HOH Z  .   ? HOH A 600 . ? 1_555 ? 
11  AC3 3  ASP A  156 ? ASP A 156 . ? 1_555 ? 
12  AC3 3  SER A  160 ? SER A 160 . ? 1_555 ? 
13  AC3 3  HOH Z  .   ? HOH A 556 . ? 1_555 ? 
14  AC4 5  ASN A  71  ? ASN A 71  . ? 1_555 ? 
15  AC4 5  LEU A  72  ? LEU A 72  . ? 1_555 ? 
16  AC4 5  THR A  88  ? THR A 88  . ? 1_555 ? 
17  AC4 5  HOH Z  .   ? HOH A 486 . ? 1_555 ? 
18  AC4 5  HOH Z  .   ? HOH A 509 . ? 1_555 ? 
19  AC5 9  HIS A  91  ? HIS A 91  . ? 1_555 ? 
20  AC5 9  HIS A  93  ? HIS A 93  . ? 1_555 ? 
21  AC5 9  HIS A  117 ? HIS A 117 . ? 1_555 ? 
22  AC5 9  VAL A  119 ? VAL A 119 . ? 1_555 ? 
23  AC5 9  LEU A  197 ? LEU A 197 . ? 1_555 ? 
24  AC5 9  THR A  198 ? THR A 198 . ? 1_555 ? 
25  AC5 9  THR A  199 ? THR A 199 . ? 1_555 ? 
26  AC5 9  TRP A  208 ? TRP A 208 . ? 1_555 ? 
27  AC5 9  ZN  E  .   ? ZN  A 301 . ? 1_555 ? 
28  AC6 4  HIS B  91  ? HIS B 91  . ? 1_555 ? 
29  AC6 4  HIS B  93  ? HIS B 93  . ? 1_555 ? 
30  AC6 4  HIS B  117 ? HIS B 117 . ? 1_555 ? 
31  AC6 4  VD9 Q  .   ? VD9 B 308 . ? 1_555 ? 
32  AC7 6  ASN B  64  ? ASN B 64  . ? 1_555 ? 
33  AC7 6  GLN B  89  ? GLN B 89  . ? 1_555 ? 
34  AC7 6  HIS B  91  ? HIS B 91  . ? 1_555 ? 
35  AC7 6  EDO N  .   ? EDO B 305 . ? 1_555 ? 
36  AC7 6  HOH AA .   ? HOH B 501 . ? 1_555 ? 
37  AC7 6  HOH AA .   ? HOH B 576 . ? 1_555 ? 
38  AC8 6  SER B  42  ? SER B 42  . ? 1_555 ? 
39  AC8 6  THR B  44  ? THR B 44  . ? 1_555 ? 
40  AC8 6  LEU B  46  ? LEU B 46  . ? 1_555 ? 
41  AC8 6  GLY B  80  ? GLY B 80  . ? 1_555 ? 
42  AC8 6  TYR B  190 ? TYR B 190 . ? 1_555 ? 
43  AC8 6  ARG B  192 ? ARG B 192 . ? 1_555 ? 
44  AC9 5  ASP B  156 ? ASP B 156 . ? 1_555 ? 
45  AC9 5  SER B  160 ? SER B 160 . ? 1_555 ? 
46  AC9 5  GLN B  221 ? GLN B 221 . ? 1_555 ? 
47  AC9 5  ALA B  224 ? ALA B 224 . ? 1_555 ? 
48  AC9 5  HOH AA .   ? HOH B 657 . ? 1_555 ? 
49  AD1 6  ASN B  64  ? ASN B 64  . ? 1_555 ? 
50  AD1 6  LYS B  69  ? LYS B 69  . ? 1_555 ? 
51  AD1 6  GLN B  89  ? GLN B 89  . ? 1_555 ? 
52  AD1 6  EDO K  .   ? EDO B 302 . ? 1_555 ? 
53  AD1 6  VD9 Q  .   ? VD9 B 308 . ? 1_555 ? 
54  AD1 6  HOH AA .   ? HOH B 404 . ? 1_555 ? 
55  AD2 5  LEU B  183 ? LEU B 183 . ? 1_555 ? 
56  AD2 5  VAL B  215 ? VAL B 215 . ? 1_555 ? 
57  AD2 5  HOH AA .   ? HOH B 493 . ? 1_555 ? 
58  AD2 5  HOH AA .   ? HOH B 508 . ? 1_555 ? 
59  AD2 5  HOH AA .   ? HOH B 622 . ? 1_555 ? 
60  AD3 4  LEU B  256 ? LEU B 256 . ? 1_555 ? 
61  AD3 4  TYR B  258 ? TYR B 258 . ? 1_555 ? 
62  AD3 4  HOH AA .   ? HOH B 522 . ? 1_555 ? 
63  AD3 4  HOH AA .   ? HOH B 595 . ? 1_555 ? 
64  AD4 9  HIS B  91  ? HIS B 91  . ? 1_555 ? 
65  AD4 9  HIS B  93  ? HIS B 93  . ? 1_555 ? 
66  AD4 9  HIS B  117 ? HIS B 117 . ? 1_555 ? 
67  AD4 9  LEU B  197 ? LEU B 197 . ? 1_555 ? 
68  AD4 9  THR B  198 ? THR B 198 . ? 1_555 ? 
69  AD4 9  THR B  199 ? THR B 199 . ? 1_555 ? 
70  AD4 9  TRP B  208 ? TRP B 208 . ? 1_555 ? 
71  AD4 9  ZN  J  .   ? ZN  B 301 . ? 1_555 ? 
72  AD4 9  EDO N  .   ? EDO B 305 . ? 1_555 ? 
73  AD5 4  HIS C  91  ? HIS C 91  . ? 1_555 ? 
74  AD5 4  HIS C  93  ? HIS C 93  . ? 1_555 ? 
75  AD5 4  HIS C  117 ? HIS C 117 . ? 1_555 ? 
76  AD5 4  VD9 U  .   ? VD9 C 304 . ? 1_555 ? 
77  AD6 4  ASN C  64  ? ASN C 64  . ? 1_555 ? 
78  AD6 4  GLN C  89  ? GLN C 89  . ? 1_555 ? 
79  AD6 4  HIS C  91  ? HIS C 91  . ? 1_555 ? 
80  AD6 4  HOH BA .   ? HOH C 562 . ? 1_555 ? 
81  AD7 6  ASN C  71  ? ASN C 71  . ? 1_555 ? 
82  AD7 6  LEU C  72  ? LEU C 72  . ? 1_555 ? 
83  AD7 6  THR C  88  ? THR C 88  . ? 1_555 ? 
84  AD7 6  HOH BA .   ? HOH C 489 . ? 1_555 ? 
85  AD7 6  HOH BA .   ? HOH C 512 . ? 1_555 ? 
86  AD7 6  HOH BA .   ? HOH C 518 . ? 1_555 ? 
87  AD8 9  HIS C  91  ? HIS C 91  . ? 1_555 ? 
88  AD8 9  HIS C  93  ? HIS C 93  . ? 1_555 ? 
89  AD8 9  HIS C  117 ? HIS C 117 . ? 1_555 ? 
90  AD8 9  VAL C  119 ? VAL C 119 . ? 1_555 ? 
91  AD8 9  LEU C  197 ? LEU C 197 . ? 1_555 ? 
92  AD8 9  THR C  198 ? THR C 198 . ? 1_555 ? 
93  AD8 9  THR C  199 ? THR C 199 . ? 1_555 ? 
94  AD8 9  TRP C  208 ? TRP C 208 . ? 1_555 ? 
95  AD8 9  ZN  R  .   ? ZN  C 301 . ? 1_555 ? 
96  AD9 4  HIS D  91  ? HIS D 91  . ? 1_555 ? 
97  AD9 4  HIS D  93  ? HIS D 93  . ? 1_555 ? 
98  AD9 4  HIS D  117 ? HIS D 117 . ? 1_555 ? 
99  AD9 4  VD9 Y  .   ? VD9 D 304 . ? 1_555 ? 
100 AE1 8  ASN D  64  ? ASN D 64  . ? 1_555 ? 
101 AE1 8  HIS D  66  ? HIS D 66  . ? 1_555 ? 
102 AE1 8  GLN D  89  ? GLN D 89  . ? 1_555 ? 
103 AE1 8  HIS D  91  ? HIS D 91  . ? 1_555 ? 
104 AE1 8  VD9 Y  .   ? VD9 D 304 . ? 1_555 ? 
105 AE1 8  HOH CA .   ? HOH D 478 . ? 1_555 ? 
106 AE1 8  HOH CA .   ? HOH D 612 . ? 1_555 ? 
107 AE1 8  HOH CA .   ? HOH D 637 . ? 1_555 ? 
108 AE2 6  SER D  42  ? SER D 42  . ? 1_555 ? 
109 AE2 6  THR D  44  ? THR D 44  . ? 1_555 ? 
110 AE2 6  LEU D  46  ? LEU D 46  . ? 1_555 ? 
111 AE2 6  GLY D  80  ? GLY D 80  . ? 1_555 ? 
112 AE2 6  TYR D  190 ? TYR D 190 . ? 1_555 ? 
113 AE2 6  ARG D  192 ? ARG D 192 . ? 1_555 ? 
114 AE3 10 HIS D  91  ? HIS D 91  . ? 1_555 ? 
115 AE3 10 HIS D  93  ? HIS D 93  . ? 1_555 ? 
116 AE3 10 HIS D  117 ? HIS D 117 . ? 1_555 ? 
117 AE3 10 ALA D  129 ? ALA D 129 . ? 1_555 ? 
118 AE3 10 LEU D  197 ? LEU D 197 . ? 1_555 ? 
119 AE3 10 THR D  198 ? THR D 198 . ? 1_555 ? 
120 AE3 10 THR D  199 ? THR D 199 . ? 1_555 ? 
121 AE3 10 TRP D  208 ? TRP D 208 . ? 1_555 ? 
122 AE3 10 ZN  V  .   ? ZN  D 301 . ? 1_555 ? 
123 AE3 10 EDO W  .   ? EDO D 302 . ? 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   A HOH 601 ? ? O B HOH 642 ? ? 2.17 
2 1 OD2 B ASP 75  ? ? O B HOH 623 ? ? 2.17 
# 
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 CA B ARG 84  ? B C   B ARG 84  ? B 1.686 1.525 0.161 0.026 N 
2 1 CG B HIS 91  ? ? CD2 B HIS 91  ? ? 1.419 1.354 0.065 0.009 N 
3 1 CG B HIS 111 ? ? CD2 B HIS 111 ? ? 1.414 1.354 0.060 0.009 N 
4 1 CG C HIS 101 ? ? CD2 C HIS 101 ? ? 1.421 1.354 0.067 0.009 N 
5 1 CG D HIS 33  ? ? CD2 D HIS 33  ? ? 1.428 1.354 0.074 0.009 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ASN A 245 ? ? -97.59  56.25  
2  1 ASP B 99  ? ? -150.91 81.81  
3  1 ASN B 245 ? ? -91.48  57.96  
4  1 PHE B 252 ? A -105.58 63.31  
5  1 ASP B 253 ? ? -2.45   41.76  
6  1 THR C 88  ? ? -132.91 -43.04 
7  1 ASP C 99  ? ? -151.23 82.89  
8  1 ASN C 245 ? ? -96.93  58.15  
9  1 PRO D 204 ? ? -91.08  59.42  
10 1 ASN D 245 ? ? -93.99  54.66  
11 1 GLU D 254 ? ? 77.02   -11.74 
# 
_phasing.method   MR 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A MET 1   ? A MET 1   
2 1 Y 1 A SER 2   ? A SER 2   
3 1 Y 1 B MET 1   ? B MET 1   
4 1 Y 1 B SER 2   ? B SER 2   
5 1 Y 1 C MET 1   ? C MET 1   
6 1 Y 1 C SER 2   ? C SER 2   
7 1 Y 1 D MET 1   ? D MET 1   
8 1 Y 1 D SER 2   ? D SER 2   
9 1 Y 1 D GLN 263 ? D GLN 263 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CYS N    N  N N 74  
CYS CA   C  N R 75  
CYS C    C  N N 76  
CYS O    O  N N 77  
CYS CB   C  N N 78  
CYS SG   S  N N 79  
CYS OXT  O  N N 80  
CYS H    H  N N 81  
CYS H2   H  N N 82  
CYS HA   H  N N 83  
CYS HB2  H  N N 84  
CYS HB3  H  N N 85  
CYS HG   H  N N 86  
CYS HXT  H  N N 87  
EDO C1   C  N N 88  
EDO O1   O  N N 89  
EDO C2   C  N N 90  
EDO O2   O  N N 91  
EDO H11  H  N N 92  
EDO H12  H  N N 93  
EDO HO1  H  N N 94  
EDO H21  H  N N 95  
EDO H22  H  N N 96  
EDO HO2  H  N N 97  
GLN N    N  N N 98  
GLN CA   C  N S 99  
GLN C    C  N N 100 
GLN O    O  N N 101 
GLN CB   C  N N 102 
GLN CG   C  N N 103 
GLN CD   C  N N 104 
GLN OE1  O  N N 105 
GLN NE2  N  N N 106 
GLN OXT  O  N N 107 
GLN H    H  N N 108 
GLN H2   H  N N 109 
GLN HA   H  N N 110 
GLN HB2  H  N N 111 
GLN HB3  H  N N 112 
GLN HG2  H  N N 113 
GLN HG3  H  N N 114 
GLN HE21 H  N N 115 
GLN HE22 H  N N 116 
GLN HXT  H  N N 117 
GLU N    N  N N 118 
GLU CA   C  N S 119 
GLU C    C  N N 120 
GLU O    O  N N 121 
GLU CB   C  N N 122 
GLU CG   C  N N 123 
GLU CD   C  N N 124 
GLU OE1  O  N N 125 
GLU OE2  O  N N 126 
GLU OXT  O  N N 127 
GLU H    H  N N 128 
GLU H2   H  N N 129 
GLU HA   H  N N 130 
GLU HB2  H  N N 131 
GLU HB3  H  N N 132 
GLU HG2  H  N N 133 
GLU HG3  H  N N 134 
GLU HE2  H  N N 135 
GLU HXT  H  N N 136 
GLY N    N  N N 137 
GLY CA   C  N N 138 
GLY C    C  N N 139 
GLY O    O  N N 140 
GLY OXT  O  N N 141 
GLY H    H  N N 142 
GLY H2   H  N N 143 
GLY HA2  H  N N 144 
GLY HA3  H  N N 145 
GLY HXT  H  N N 146 
HIS N    N  N N 147 
HIS CA   C  N S 148 
HIS C    C  N N 149 
HIS O    O  N N 150 
HIS CB   C  N N 151 
HIS CG   C  Y N 152 
HIS ND1  N  Y N 153 
HIS CD2  C  Y N 154 
HIS CE1  C  Y N 155 
HIS NE2  N  Y N 156 
HIS OXT  O  N N 157 
HIS H    H  N N 158 
HIS H2   H  N N 159 
HIS HA   H  N N 160 
HIS HB2  H  N N 161 
HIS HB3  H  N N 162 
HIS HD1  H  N N 163 
HIS HD2  H  N N 164 
HIS HE1  H  N N 165 
HIS HE2  H  N N 166 
HIS HXT  H  N N 167 
HOH O    O  N N 168 
HOH H1   H  N N 169 
HOH H2   H  N N 170 
ILE N    N  N N 171 
ILE CA   C  N S 172 
ILE C    C  N N 173 
ILE O    O  N N 174 
ILE CB   C  N S 175 
ILE CG1  C  N N 176 
ILE CG2  C  N N 177 
ILE CD1  C  N N 178 
ILE OXT  O  N N 179 
ILE H    H  N N 180 
ILE H2   H  N N 181 
ILE HA   H  N N 182 
ILE HB   H  N N 183 
ILE HG12 H  N N 184 
ILE HG13 H  N N 185 
ILE HG21 H  N N 186 
ILE HG22 H  N N 187 
ILE HG23 H  N N 188 
ILE HD11 H  N N 189 
ILE HD12 H  N N 190 
ILE HD13 H  N N 191 
ILE HXT  H  N N 192 
LEU N    N  N N 193 
LEU CA   C  N S 194 
LEU C    C  N N 195 
LEU O    O  N N 196 
LEU CB   C  N N 197 
LEU CG   C  N N 198 
LEU CD1  C  N N 199 
LEU CD2  C  N N 200 
LEU OXT  O  N N 201 
LEU H    H  N N 202 
LEU H2   H  N N 203 
LEU HA   H  N N 204 
LEU HB2  H  N N 205 
LEU HB3  H  N N 206 
LEU HG   H  N N 207 
LEU HD11 H  N N 208 
LEU HD12 H  N N 209 
LEU HD13 H  N N 210 
LEU HD21 H  N N 211 
LEU HD22 H  N N 212 
LEU HD23 H  N N 213 
LEU HXT  H  N N 214 
LYS N    N  N N 215 
LYS CA   C  N S 216 
LYS C    C  N N 217 
LYS O    O  N N 218 
LYS CB   C  N N 219 
LYS CG   C  N N 220 
LYS CD   C  N N 221 
LYS CE   C  N N 222 
LYS NZ   N  N N 223 
LYS OXT  O  N N 224 
LYS H    H  N N 225 
LYS H2   H  N N 226 
LYS HA   H  N N 227 
LYS HB2  H  N N 228 
LYS HB3  H  N N 229 
LYS HG2  H  N N 230 
LYS HG3  H  N N 231 
LYS HD2  H  N N 232 
LYS HD3  H  N N 233 
LYS HE2  H  N N 234 
LYS HE3  H  N N 235 
LYS HZ1  H  N N 236 
LYS HZ2  H  N N 237 
LYS HZ3  H  N N 238 
LYS HXT  H  N N 239 
MET N    N  N N 240 
MET CA   C  N S 241 
MET C    C  N N 242 
MET O    O  N N 243 
MET CB   C  N N 244 
MET CG   C  N N 245 
MET SD   S  N N 246 
MET CE   C  N N 247 
MET OXT  O  N N 248 
MET H    H  N N 249 
MET H2   H  N N 250 
MET HA   H  N N 251 
MET HB2  H  N N 252 
MET HB3  H  N N 253 
MET HG2  H  N N 254 
MET HG3  H  N N 255 
MET HE1  H  N N 256 
MET HE2  H  N N 257 
MET HE3  H  N N 258 
MET HXT  H  N N 259 
PHE N    N  N N 260 
PHE CA   C  N S 261 
PHE C    C  N N 262 
PHE O    O  N N 263 
PHE CB   C  N N 264 
PHE CG   C  Y N 265 
PHE CD1  C  Y N 266 
PHE CD2  C  Y N 267 
PHE CE1  C  Y N 268 
PHE CE2  C  Y N 269 
PHE CZ   C  Y N 270 
PHE OXT  O  N N 271 
PHE H    H  N N 272 
PHE H2   H  N N 273 
PHE HA   H  N N 274 
PHE HB2  H  N N 275 
PHE HB3  H  N N 276 
PHE HD1  H  N N 277 
PHE HD2  H  N N 278 
PHE HE1  H  N N 279 
PHE HE2  H  N N 280 
PHE HZ   H  N N 281 
PHE HXT  H  N N 282 
PRO N    N  N N 283 
PRO CA   C  N S 284 
PRO C    C  N N 285 
PRO O    O  N N 286 
PRO CB   C  N N 287 
PRO CG   C  N N 288 
PRO CD   C  N N 289 
PRO OXT  O  N N 290 
PRO H    H  N N 291 
PRO HA   H  N N 292 
PRO HB2  H  N N 293 
PRO HB3  H  N N 294 
PRO HG2  H  N N 295 
PRO HG3  H  N N 296 
PRO HD2  H  N N 297 
PRO HD3  H  N N 298 
PRO HXT  H  N N 299 
SER N    N  N N 300 
SER CA   C  N S 301 
SER C    C  N N 302 
SER O    O  N N 303 
SER CB   C  N N 304 
SER OG   O  N N 305 
SER OXT  O  N N 306 
SER H    H  N N 307 
SER H2   H  N N 308 
SER HA   H  N N 309 
SER HB2  H  N N 310 
SER HB3  H  N N 311 
SER HG   H  N N 312 
SER HXT  H  N N 313 
THR N    N  N N 314 
THR CA   C  N S 315 
THR C    C  N N 316 
THR O    O  N N 317 
THR CB   C  N R 318 
THR OG1  O  N N 319 
THR CG2  C  N N 320 
THR OXT  O  N N 321 
THR H    H  N N 322 
THR H2   H  N N 323 
THR HA   H  N N 324 
THR HB   H  N N 325 
THR HG1  H  N N 326 
THR HG21 H  N N 327 
THR HG22 H  N N 328 
THR HG23 H  N N 329 
THR HXT  H  N N 330 
TRP N    N  N N 331 
TRP CA   C  N S 332 
TRP C    C  N N 333 
TRP O    O  N N 334 
TRP CB   C  N N 335 
TRP CG   C  Y N 336 
TRP CD1  C  Y N 337 
TRP CD2  C  Y N 338 
TRP NE1  N  Y N 339 
TRP CE2  C  Y N 340 
TRP CE3  C  Y N 341 
TRP CZ2  C  Y N 342 
TRP CZ3  C  Y N 343 
TRP CH2  C  Y N 344 
TRP OXT  O  N N 345 
TRP H    H  N N 346 
TRP H2   H  N N 347 
TRP HA   H  N N 348 
TRP HB2  H  N N 349 
TRP HB3  H  N N 350 
TRP HD1  H  N N 351 
TRP HE1  H  N N 352 
TRP HE3  H  N N 353 
TRP HZ2  H  N N 354 
TRP HZ3  H  N N 355 
TRP HH2  H  N N 356 
TRP HXT  H  N N 357 
TYR N    N  N N 358 
TYR CA   C  N S 359 
TYR C    C  N N 360 
TYR O    O  N N 361 
TYR CB   C  N N 362 
TYR CG   C  Y N 363 
TYR CD1  C  Y N 364 
TYR CD2  C  Y N 365 
TYR CE1  C  Y N 366 
TYR CE2  C  Y N 367 
TYR CZ   C  Y N 368 
TYR OH   O  N N 369 
TYR OXT  O  N N 370 
TYR H    H  N N 371 
TYR H2   H  N N 372 
TYR HA   H  N N 373 
TYR HB2  H  N N 374 
TYR HB3  H  N N 375 
TYR HD1  H  N N 376 
TYR HD2  H  N N 377 
TYR HE1  H  N N 378 
TYR HE2  H  N N 379 
TYR HH   H  N N 380 
TYR HXT  H  N N 381 
VAL N    N  N N 382 
VAL CA   C  N S 383 
VAL C    C  N N 384 
VAL O    O  N N 385 
VAL CB   C  N N 386 
VAL CG1  C  N N 387 
VAL CG2  C  N N 388 
VAL OXT  O  N N 389 
VAL H    H  N N 390 
VAL H2   H  N N 391 
VAL HA   H  N N 392 
VAL HB   H  N N 393 
VAL HG11 H  N N 394 
VAL HG12 H  N N 395 
VAL HG13 H  N N 396 
VAL HG21 H  N N 397 
VAL HG22 H  N N 398 
VAL HG23 H  N N 399 
VAL HXT  H  N N 400 
VD9 O4   O  N N 401 
VD9 S2   S  N N 402 
VD9 O1   O  N N 403 
VD9 N3   N  N N 404 
VD9 C5   C  Y N 405 
VD9 C10  C  Y N 406 
VD9 C9   C  Y N 407 
VD9 C8   C  Y N 408 
VD9 C7   C  Y N 409 
VD9 C6   C  Y N 410 
VD9 S11  S  N N 411 
VD9 C12  C  N N 412 
VD9 C13  C  N N 413 
VD9 C14  C  N N 414 
VD9 H1   H  N N 415 
VD9 H2   H  N N 416 
VD9 H3   H  N N 417 
VD9 H4   H  N N 418 
VD9 H5   H  N N 419 
VD9 H6   H  N N 420 
VD9 H7   H  N N 421 
VD9 H8   H  N N 422 
VD9 H9   H  N N 423 
VD9 H10  H  N N 424 
VD9 H11  H  N N 425 
VD9 H12  H  N N 426 
VD9 H13  H  N N 427 
ZN  ZN   ZN N N 428 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
EDO C1  O1   sing N N 83  
EDO C1  C2   sing N N 84  
EDO C1  H11  sing N N 85  
EDO C1  H12  sing N N 86  
EDO O1  HO1  sing N N 87  
EDO C2  O2   sing N N 88  
EDO C2  H21  sing N N 89  
EDO C2  H22  sing N N 90  
EDO O2  HO2  sing N N 91  
GLN N   CA   sing N N 92  
GLN N   H    sing N N 93  
GLN N   H2   sing N N 94  
GLN CA  C    sing N N 95  
GLN CA  CB   sing N N 96  
GLN CA  HA   sing N N 97  
GLN C   O    doub N N 98  
GLN C   OXT  sing N N 99  
GLN CB  CG   sing N N 100 
GLN CB  HB2  sing N N 101 
GLN CB  HB3  sing N N 102 
GLN CG  CD   sing N N 103 
GLN CG  HG2  sing N N 104 
GLN CG  HG3  sing N N 105 
GLN CD  OE1  doub N N 106 
GLN CD  NE2  sing N N 107 
GLN NE2 HE21 sing N N 108 
GLN NE2 HE22 sing N N 109 
GLN OXT HXT  sing N N 110 
GLU N   CA   sing N N 111 
GLU N   H    sing N N 112 
GLU N   H2   sing N N 113 
GLU CA  C    sing N N 114 
GLU CA  CB   sing N N 115 
GLU CA  HA   sing N N 116 
GLU C   O    doub N N 117 
GLU C   OXT  sing N N 118 
GLU CB  CG   sing N N 119 
GLU CB  HB2  sing N N 120 
GLU CB  HB3  sing N N 121 
GLU CG  CD   sing N N 122 
GLU CG  HG2  sing N N 123 
GLU CG  HG3  sing N N 124 
GLU CD  OE1  doub N N 125 
GLU CD  OE2  sing N N 126 
GLU OE2 HE2  sing N N 127 
GLU OXT HXT  sing N N 128 
GLY N   CA   sing N N 129 
GLY N   H    sing N N 130 
GLY N   H2   sing N N 131 
GLY CA  C    sing N N 132 
GLY CA  HA2  sing N N 133 
GLY CA  HA3  sing N N 134 
GLY C   O    doub N N 135 
GLY C   OXT  sing N N 136 
GLY OXT HXT  sing N N 137 
HIS N   CA   sing N N 138 
HIS N   H    sing N N 139 
HIS N   H2   sing N N 140 
HIS CA  C    sing N N 141 
HIS CA  CB   sing N N 142 
HIS CA  HA   sing N N 143 
HIS C   O    doub N N 144 
HIS C   OXT  sing N N 145 
HIS CB  CG   sing N N 146 
HIS CB  HB2  sing N N 147 
HIS CB  HB3  sing N N 148 
HIS CG  ND1  sing Y N 149 
HIS CG  CD2  doub Y N 150 
HIS ND1 CE1  doub Y N 151 
HIS ND1 HD1  sing N N 152 
HIS CD2 NE2  sing Y N 153 
HIS CD2 HD2  sing N N 154 
HIS CE1 NE2  sing Y N 155 
HIS CE1 HE1  sing N N 156 
HIS NE2 HE2  sing N N 157 
HIS OXT HXT  sing N N 158 
HOH O   H1   sing N N 159 
HOH O   H2   sing N N 160 
ILE N   CA   sing N N 161 
ILE N   H    sing N N 162 
ILE N   H2   sing N N 163 
ILE CA  C    sing N N 164 
ILE CA  CB   sing N N 165 
ILE CA  HA   sing N N 166 
ILE C   O    doub N N 167 
ILE C   OXT  sing N N 168 
ILE CB  CG1  sing N N 169 
ILE CB  CG2  sing N N 170 
ILE CB  HB   sing N N 171 
ILE CG1 CD1  sing N N 172 
ILE CG1 HG12 sing N N 173 
ILE CG1 HG13 sing N N 174 
ILE CG2 HG21 sing N N 175 
ILE CG2 HG22 sing N N 176 
ILE CG2 HG23 sing N N 177 
ILE CD1 HD11 sing N N 178 
ILE CD1 HD12 sing N N 179 
ILE CD1 HD13 sing N N 180 
ILE OXT HXT  sing N N 181 
LEU N   CA   sing N N 182 
LEU N   H    sing N N 183 
LEU N   H2   sing N N 184 
LEU CA  C    sing N N 185 
LEU CA  CB   sing N N 186 
LEU CA  HA   sing N N 187 
LEU C   O    doub N N 188 
LEU C   OXT  sing N N 189 
LEU CB  CG   sing N N 190 
LEU CB  HB2  sing N N 191 
LEU CB  HB3  sing N N 192 
LEU CG  CD1  sing N N 193 
LEU CG  CD2  sing N N 194 
LEU CG  HG   sing N N 195 
LEU CD1 HD11 sing N N 196 
LEU CD1 HD12 sing N N 197 
LEU CD1 HD13 sing N N 198 
LEU CD2 HD21 sing N N 199 
LEU CD2 HD22 sing N N 200 
LEU CD2 HD23 sing N N 201 
LEU OXT HXT  sing N N 202 
LYS N   CA   sing N N 203 
LYS N   H    sing N N 204 
LYS N   H2   sing N N 205 
LYS CA  C    sing N N 206 
LYS CA  CB   sing N N 207 
LYS CA  HA   sing N N 208 
LYS C   O    doub N N 209 
LYS C   OXT  sing N N 210 
LYS CB  CG   sing N N 211 
LYS CB  HB2  sing N N 212 
LYS CB  HB3  sing N N 213 
LYS CG  CD   sing N N 214 
LYS CG  HG2  sing N N 215 
LYS CG  HG3  sing N N 216 
LYS CD  CE   sing N N 217 
LYS CD  HD2  sing N N 218 
LYS CD  HD3  sing N N 219 
LYS CE  NZ   sing N N 220 
LYS CE  HE2  sing N N 221 
LYS CE  HE3  sing N N 222 
LYS NZ  HZ1  sing N N 223 
LYS NZ  HZ2  sing N N 224 
LYS NZ  HZ3  sing N N 225 
LYS OXT HXT  sing N N 226 
MET N   CA   sing N N 227 
MET N   H    sing N N 228 
MET N   H2   sing N N 229 
MET CA  C    sing N N 230 
MET CA  CB   sing N N 231 
MET CA  HA   sing N N 232 
MET C   O    doub N N 233 
MET C   OXT  sing N N 234 
MET CB  CG   sing N N 235 
MET CB  HB2  sing N N 236 
MET CB  HB3  sing N N 237 
MET CG  SD   sing N N 238 
MET CG  HG2  sing N N 239 
MET CG  HG3  sing N N 240 
MET SD  CE   sing N N 241 
MET CE  HE1  sing N N 242 
MET CE  HE2  sing N N 243 
MET CE  HE3  sing N N 244 
MET OXT HXT  sing N N 245 
PHE N   CA   sing N N 246 
PHE N   H    sing N N 247 
PHE N   H2   sing N N 248 
PHE CA  C    sing N N 249 
PHE CA  CB   sing N N 250 
PHE CA  HA   sing N N 251 
PHE C   O    doub N N 252 
PHE C   OXT  sing N N 253 
PHE CB  CG   sing N N 254 
PHE CB  HB2  sing N N 255 
PHE CB  HB3  sing N N 256 
PHE CG  CD1  doub Y N 257 
PHE CG  CD2  sing Y N 258 
PHE CD1 CE1  sing Y N 259 
PHE CD1 HD1  sing N N 260 
PHE CD2 CE2  doub Y N 261 
PHE CD2 HD2  sing N N 262 
PHE CE1 CZ   doub Y N 263 
PHE CE1 HE1  sing N N 264 
PHE CE2 CZ   sing Y N 265 
PHE CE2 HE2  sing N N 266 
PHE CZ  HZ   sing N N 267 
PHE OXT HXT  sing N N 268 
PRO N   CA   sing N N 269 
PRO N   CD   sing N N 270 
PRO N   H    sing N N 271 
PRO CA  C    sing N N 272 
PRO CA  CB   sing N N 273 
PRO CA  HA   sing N N 274 
PRO C   O    doub N N 275 
PRO C   OXT  sing N N 276 
PRO CB  CG   sing N N 277 
PRO CB  HB2  sing N N 278 
PRO CB  HB3  sing N N 279 
PRO CG  CD   sing N N 280 
PRO CG  HG2  sing N N 281 
PRO CG  HG3  sing N N 282 
PRO CD  HD2  sing N N 283 
PRO CD  HD3  sing N N 284 
PRO OXT HXT  sing N N 285 
SER N   CA   sing N N 286 
SER N   H    sing N N 287 
SER N   H2   sing N N 288 
SER CA  C    sing N N 289 
SER CA  CB   sing N N 290 
SER CA  HA   sing N N 291 
SER C   O    doub N N 292 
SER C   OXT  sing N N 293 
SER CB  OG   sing N N 294 
SER CB  HB2  sing N N 295 
SER CB  HB3  sing N N 296 
SER OG  HG   sing N N 297 
SER OXT HXT  sing N N 298 
THR N   CA   sing N N 299 
THR N   H    sing N N 300 
THR N   H2   sing N N 301 
THR CA  C    sing N N 302 
THR CA  CB   sing N N 303 
THR CA  HA   sing N N 304 
THR C   O    doub N N 305 
THR C   OXT  sing N N 306 
THR CB  OG1  sing N N 307 
THR CB  CG2  sing N N 308 
THR CB  HB   sing N N 309 
THR OG1 HG1  sing N N 310 
THR CG2 HG21 sing N N 311 
THR CG2 HG22 sing N N 312 
THR CG2 HG23 sing N N 313 
THR OXT HXT  sing N N 314 
TRP N   CA   sing N N 315 
TRP N   H    sing N N 316 
TRP N   H2   sing N N 317 
TRP CA  C    sing N N 318 
TRP CA  CB   sing N N 319 
TRP CA  HA   sing N N 320 
TRP C   O    doub N N 321 
TRP C   OXT  sing N N 322 
TRP CB  CG   sing N N 323 
TRP CB  HB2  sing N N 324 
TRP CB  HB3  sing N N 325 
TRP CG  CD1  doub Y N 326 
TRP CG  CD2  sing Y N 327 
TRP CD1 NE1  sing Y N 328 
TRP CD1 HD1  sing N N 329 
TRP CD2 CE2  doub Y N 330 
TRP CD2 CE3  sing Y N 331 
TRP NE1 CE2  sing Y N 332 
TRP NE1 HE1  sing N N 333 
TRP CE2 CZ2  sing Y N 334 
TRP CE3 CZ3  doub Y N 335 
TRP CE3 HE3  sing N N 336 
TRP CZ2 CH2  doub Y N 337 
TRP CZ2 HZ2  sing N N 338 
TRP CZ3 CH2  sing Y N 339 
TRP CZ3 HZ3  sing N N 340 
TRP CH2 HH2  sing N N 341 
TRP OXT HXT  sing N N 342 
TYR N   CA   sing N N 343 
TYR N   H    sing N N 344 
TYR N   H2   sing N N 345 
TYR CA  C    sing N N 346 
TYR CA  CB   sing N N 347 
TYR CA  HA   sing N N 348 
TYR C   O    doub N N 349 
TYR C   OXT  sing N N 350 
TYR CB  CG   sing N N 351 
TYR CB  HB2  sing N N 352 
TYR CB  HB3  sing N N 353 
TYR CG  CD1  doub Y N 354 
TYR CG  CD2  sing Y N 355 
TYR CD1 CE1  sing Y N 356 
TYR CD1 HD1  sing N N 357 
TYR CD2 CE2  doub Y N 358 
TYR CD2 HD2  sing N N 359 
TYR CE1 CZ   doub Y N 360 
TYR CE1 HE1  sing N N 361 
TYR CE2 CZ   sing Y N 362 
TYR CE2 HE2  sing N N 363 
TYR CZ  OH   sing N N 364 
TYR OH  HH   sing N N 365 
TYR OXT HXT  sing N N 366 
VAL N   CA   sing N N 367 
VAL N   H    sing N N 368 
VAL N   H2   sing N N 369 
VAL CA  C    sing N N 370 
VAL CA  CB   sing N N 371 
VAL CA  HA   sing N N 372 
VAL C   O    doub N N 373 
VAL C   OXT  sing N N 374 
VAL CB  CG1  sing N N 375 
VAL CB  CG2  sing N N 376 
VAL CB  HB   sing N N 377 
VAL CG1 HG11 sing N N 378 
VAL CG1 HG12 sing N N 379 
VAL CG1 HG13 sing N N 380 
VAL CG2 HG21 sing N N 381 
VAL CG2 HG22 sing N N 382 
VAL CG2 HG23 sing N N 383 
VAL OXT HXT  sing N N 384 
VD9 C14 C13  sing N N 385 
VD9 O4  S2   doub N N 386 
VD9 C13 C12  sing N N 387 
VD9 S2  O1   doub N N 388 
VD9 S2  C5   sing N N 389 
VD9 S2  N3   sing N N 390 
VD9 C10 C5   doub Y N 391 
VD9 C10 C9   sing Y N 392 
VD9 C5  C6   sing Y N 393 
VD9 C12 S11  sing N N 394 
VD9 C9  C8   doub Y N 395 
VD9 C6  C7   doub Y N 396 
VD9 C8  C7   sing Y N 397 
VD9 C8  S11  sing N N 398 
VD9 N3  H1   sing N N 399 
VD9 N3  H2   sing N N 400 
VD9 C10 H3   sing N N 401 
VD9 C9  H4   sing N N 402 
VD9 C7  H5   sing N N 403 
VD9 C6  H6   sing N N 404 
VD9 C12 H7   sing N N 405 
VD9 C12 H8   sing N N 406 
VD9 C13 H9   sing N N 407 
VD9 C13 H10  sing N N 408 
VD9 C14 H11  sing N N 409 
VD9 C14 H12  sing N N 410 
VD9 C14 H13  sing N N 411 
# 
_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   1JD0 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    4WW8 
_atom_sites.fract_transf_matrix[1][1]   0.012934 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.004367 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.013466 
_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]   0.011526 
_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  
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   A LYS A  1 3   ? 17.862  16.238  19.935  0.50 34.10 ? 3   LYS A N   1 
ATOM   2    N  N   B LYS A  1 3   ? 16.922  16.286  19.297  0.50 33.09 ? 3   LYS A N   1 
ATOM   3    C  CA  A LYS A  1 3   ? 17.544  16.195  18.480  0.50 30.10 ? 3   LYS A CA  1 
ATOM   4    C  CA  B LYS A  1 3   ? 17.473  16.484  17.914  0.50 30.93 ? 3   LYS A CA  1 
ATOM   5    C  C   A LYS A  1 3   ? 16.717  14.939  18.151  0.50 26.20 ? 3   LYS A C   1 
ATOM   6    C  C   B LYS A  1 3   ? 16.902  15.505  16.883  0.50 26.31 ? 3   LYS A C   1 
ATOM   7    O  O   A LYS A  1 3   ? 15.667  14.688  18.778  0.50 24.53 ? 3   LYS A O   1 
ATOM   8    O  O   B LYS A  1 3   ? 16.501  15.918  15.793  0.50 23.80 ? 3   LYS A O   1 
ATOM   9    C  CB  A LYS A  1 3   ? 18.840  16.279  17.656  0.50 31.97 ? 3   LYS A CB  1 
ATOM   10   C  CB  B LYS A  1 3   ? 18.995  16.341  17.926  0.50 33.70 ? 3   LYS A CB  1 
ATOM   11   C  CG  B LYS A  1 3   ? 19.610  16.461  16.534  0.50 36.92 ? 3   LYS A CG  1 
ATOM   12   N  N   A TRP A  1 4   ? 17.193  14.148  17.184  0.50 20.09 ? 4   TRP A N   1 
ATOM   13   N  N   B TRP A  1 4   ? 17.029  14.213  17.214  0.50 20.49 ? 4   TRP A N   1 
ATOM   14   C  CA  A TRP A  1 4   ? 16.340  13.077  16.651  0.50 17.16 ? 4   TRP A CA  1 
ATOM   15   C  CA  B TRP A  1 4   ? 16.251  13.119  16.610  0.50 17.14 ? 4   TRP A CA  1 
ATOM   16   C  C   A TRP A  1 4   ? 16.289  11.915  17.596  0.50 16.92 ? 4   TRP A C   1 
ATOM   17   C  C   B TRP A  1 4   ? 16.277  11.946  17.552  0.50 16.93 ? 4   TRP A C   1 
ATOM   18   O  O   A TRP A  1 4   ? 17.242  11.681  18.352  0.50 17.18 ? 4   TRP A O   1 
ATOM   19   O  O   B TRP A  1 4   ? 17.287  11.738  18.250  0.50 17.12 ? 4   TRP A O   1 
ATOM   20   C  CB  A TRP A  1 4   ? 16.812  12.651  15.278  0.50 16.41 ? 4   TRP A CB  1 
ATOM   21   C  CB  B TRP A  1 4   ? 16.812  12.732  15.256  0.50 16.68 ? 4   TRP A CB  1 
ATOM   22   C  CG  A TRP A  1 4   ? 18.160  12.004  15.202  0.50 15.98 ? 4   TRP A CG  1 
ATOM   23   C  CG  B TRP A  1 4   ? 18.154  12.048  15.205  0.50 16.13 ? 4   TRP A CG  1 
ATOM   24   C  CD1 A TRP A  1 4   ? 19.363  12.609  14.920  0.50 15.78 ? 4   TRP A CD1 1 
ATOM   25   C  CD1 B TRP A  1 4   ? 19.371  12.629  14.923  0.50 16.06 ? 4   TRP A CD1 1 
ATOM   26   C  CD2 A TRP A  1 4   ? 18.444  10.600  15.315  0.50 14.58 ? 4   TRP A CD2 1 
ATOM   27   C  CD2 B TRP A  1 4   ? 18.418  10.631  15.324  0.50 14.72 ? 4   TRP A CD2 1 
ATOM   28   N  NE1 A TRP A  1 4   ? 20.391  11.714  14.891  0.50 15.34 ? 4   TRP A NE1 1 
ATOM   29   N  NE1 B TRP A  1 4   ? 20.385  11.716  14.904  0.50 15.46 ? 4   TRP A NE1 1 
ATOM   30   C  CE2 A TRP A  1 4   ? 19.870  10.443  15.127  0.50 13.65 ? 4   TRP A CE2 1 
ATOM   31   C  CE2 B TRP A  1 4   ? 19.846  10.455  15.142  0.50 13.69 ? 4   TRP A CE2 1 
ATOM   32   C  CE3 A TRP A  1 4   ? 17.660  9.474   15.555  0.50 13.44 ? 4   TRP A CE3 1 
ATOM   33   C  CE3 B TRP A  1 4   ? 17.620  9.511   15.568  0.50 13.52 ? 4   TRP A CE3 1 
ATOM   34   C  CZ2 A TRP A  1 4   ? 20.478  9.200   15.180  0.50 14.95 ? 4   TRP A CZ2 1 
ATOM   35   C  CZ2 B TRP A  1 4   ? 20.440  9.204   15.205  0.50 14.93 ? 4   TRP A CZ2 1 
ATOM   36   C  CZ3 A TRP A  1 4   ? 18.275  8.228   15.600  0.50 13.62 ? 4   TRP A CZ3 1 
ATOM   37   C  CZ3 B TRP A  1 4   ? 18.224  8.256   15.616  0.50 13.65 ? 4   TRP A CZ3 1 
ATOM   38   C  CH2 A TRP A  1 4   ? 19.648  8.096   15.412  0.50 14.01 ? 4   TRP A CH2 1 
ATOM   39   C  CH2 B TRP A  1 4   ? 19.597  8.109   15.436  0.50 13.96 ? 4   TRP A CH2 1 
ATOM   40   N  N   . THR A  1 5   ? 15.178  11.181  17.568  1.00 16.33 ? 5   THR A N   1 
ATOM   41   C  CA  . THR A  1 5   ? 15.010  10.037  18.465  1.00 16.56 ? 5   THR A CA  1 
ATOM   42   C  C   . THR A  1 5   ? 14.269  8.953   17.688  1.00 14.81 ? 5   THR A C   1 
ATOM   43   O  O   . THR A  1 5   ? 13.943  9.082   16.495  1.00 15.00 ? 5   THR A O   1 
ATOM   44   C  CB  . THR A  1 5   ? 14.049  10.418  19.618  1.00 18.18 ? 5   THR A CB  1 
ATOM   45   O  OG1 . THR A  1 5   ? 12.766  10.740  19.038  1.00 19.94 ? 5   THR A OG1 1 
ATOM   46   C  CG2 . THR A  1 5   ? 14.596  11.648  20.373  1.00 20.48 ? 5   THR A CG2 1 
ATOM   47   N  N   . TYR A  1 6   ? 13.949  7.866   18.368  1.00 16.47 ? 6   TYR A N   1 
ATOM   48   C  CA  . TYR A  1 6   ? 13.124  6.819   17.818  1.00 14.69 ? 6   TYR A CA  1 
ATOM   49   C  C   . TYR A  1 6   ? 11.679  6.787   18.349  1.00 17.82 ? 6   TYR A C   1 
ATOM   50   O  O   . TYR A  1 6   ? 10.960  5.840   18.217  1.00 18.58 ? 6   TYR A O   1 
ATOM   51   C  CB  . TYR A  1 6   ? 13.669  5.372   17.989  1.00 15.47 ? 6   TYR A CB  1 
ATOM   52   C  CG  . TYR A  1 6   ? 14.965  5.075   17.253  1.00 13.67 ? 6   TYR A CG  1 
ATOM   53   C  CD1 . TYR A  1 6   ? 16.211  5.320   17.832  1.00 13.78 ? 6   TYR A CD1 1 
ATOM   54   C  CD2 . TYR A  1 6   ? 14.938  4.524   15.985  1.00 13.60 ? 6   TYR A CD2 1 
ATOM   55   C  CE1 . TYR A  1 6   ? 17.387  5.035   17.147  1.00 12.85 ? 6   TYR A CE1 1 
ATOM   56   C  CE2 . TYR A  1 6   ? 16.100  4.236   15.297  1.00 12.46 ? 6   TYR A CE2 1 
ATOM   57   C  CZ  . TYR A  1 6   ? 17.320  4.487   15.877  1.00 12.86 ? 6   TYR A CZ  1 
ATOM   58   O  OH  . TYR A  1 6   ? 18.459  4.191   15.162  1.00 13.86 ? 6   TYR A OH  1 
ATOM   59   N  N   . PHE A  1 7   ? 11.246  7.868   19.014  1.00 24.93 ? 7   PHE A N   1 
ATOM   60   C  CA  . PHE A  1 7   ? 9.953   7.826   19.669  1.00 30.84 ? 7   PHE A CA  1 
ATOM   61   C  C   . PHE A  1 7   ? 9.517   9.260   19.757  1.00 34.40 ? 7   PHE A C   1 
ATOM   62   O  O   . PHE A  1 7   ? 10.343  10.174  19.603  1.00 34.71 ? 7   PHE A O   1 
ATOM   63   C  CB  . PHE A  1 7   ? 10.115  7.297   21.095  1.00 35.37 ? 7   PHE A CB  1 
ATOM   64   C  CG  . PHE A  1 7   ? 10.639  8.354   22.025  1.00 41.66 ? 7   PHE A CG  1 
ATOM   65   C  CD1 . PHE A  1 7   ? 12.010  8.612   22.118  1.00 43.87 ? 7   PHE A CD1 1 
ATOM   66   C  CD2 . PHE A  1 7   ? 9.753   9.166   22.751  1.00 49.10 ? 7   PHE A CD2 1 
ATOM   67   C  CE1 . PHE A  1 7   ? 12.495  9.624   22.938  1.00 49.64 ? 7   PHE A CE1 1 
ATOM   68   C  CE2 . PHE A  1 7   ? 10.236  10.191  23.566  1.00 54.46 ? 7   PHE A CE2 1 
ATOM   69   C  CZ  . PHE A  1 7   ? 11.608  10.421  23.657  1.00 50.24 ? 7   PHE A CZ  1 
ATOM   70   N  N   . GLY A  1 8   ? 8.233   9.443   20.045  1.00 35.08 ? 8   GLY A N   1 
ATOM   71   C  CA  . GLY A  1 8   ? 7.626   10.776  20.353  1.00 33.16 ? 8   GLY A CA  1 
ATOM   72   C  C   . GLY A  1 8   ? 7.641   11.659  19.092  1.00 36.99 ? 8   GLY A C   1 
ATOM   73   O  O   . GLY A  1 8   ? 7.578   11.176  17.948  1.00 37.10 ? 8   GLY A O   1 
ATOM   74   N  N   . PRO A  1 9   ? 7.741   12.952  19.294  1.00 27.54 ? 9   PRO A N   1 
ATOM   75   C  CA  . PRO A  1 9   ? 7.637   14.012  18.283  1.00 26.53 ? 9   PRO A CA  1 
ATOM   76   C  C   . PRO A  1 9   ? 8.831   14.084  17.384  1.00 22.18 ? 9   PRO A C   1 
ATOM   77   O  O   . PRO A  1 9   ? 8.734   14.576  16.265  1.00 19.33 ? 9   PRO A O   1 
ATOM   78   C  CB  . PRO A  1 9   ? 7.503   15.328  19.124  1.00 28.85 ? 9   PRO A CB  1 
ATOM   79   C  CG  . PRO A  1 9   ? 7.682   14.914  20.521  1.00 28.97 ? 9   PRO A CG  1 
ATOM   80   C  CD  . PRO A  1 9   ? 7.442   13.448  20.653  1.00 30.61 ? 9   PRO A CD  1 
ATOM   81   N  N   . ASP A  1 10  ? 9.975   13.558  17.867  1.00 23.57 ? 10  ASP A N   1 
ATOM   82   C  CA  . ASP A  1 10  ? 11.178  13.653  17.108  1.00 21.55 ? 10  ASP A CA  1 
ATOM   83   C  C   . ASP A  1 10  ? 11.656  12.330  16.503  1.00 19.40 ? 10  ASP A C   1 
ATOM   84   O  O   . ASP A  1 10  ? 12.820  12.233  16.025  1.00 18.05 ? 10  ASP A O   1 
ATOM   85   C  CB  . ASP A  1 10  ? 12.300  14.256  17.977  1.00 24.11 ? 10  ASP A CB  1 
ATOM   86   C  CG  . ASP A  1 10  ? 11.965  15.674  18.441  1.00 32.42 ? 10  ASP A CG  1 
ATOM   87   O  OD1 . ASP A  1 10  ? 11.555  16.488  17.557  1.00 33.63 ? 10  ASP A OD1 1 
ATOM   88   O  OD2 . ASP A  1 10  ? 12.044  15.907  19.688  1.00 37.10 ? 10  ASP A OD2 1 
ATOM   89   N  N   . GLY A  1 11  ? 10.716  11.371  16.518  1.00 18.09 ? 11  GLY A N   1 
ATOM   90   C  CA  . GLY A  1 11  ? 10.875  10.002  15.963  1.00 13.89 ? 11  GLY A CA  1 
ATOM   91   C  C   . GLY A  1 11  ? 10.900  10.012  14.447  1.00 13.77 ? 11  GLY A C   1 
ATOM   92   O  O   . GLY A  1 11  ? 10.966  11.047  13.709  1.00 12.18 ? 11  GLY A O   1 
ATOM   93   N  N   . GLU A  1 12  ? 10.971  8.800   13.907  1.00 10.77 ? 12  GLU A N   1 
ATOM   94   C  CA  . GLU A  1 12  ? 11.316  8.564   12.539  1.00 10.25 ? 12  GLU A CA  1 
ATOM   95   C  C   . GLU A  1 12  ? 10.478  9.220   11.459  1.00 9.87  ? 12  GLU A C   1 
ATOM   96   O  O   . GLU A  1 12  ? 11.010  9.526   10.411  1.00 9.42  ? 12  GLU A O   1 
ATOM   97   C  CB  . GLU A  1 12  ? 11.574  7.025   12.281  1.00 10.53 ? 12  GLU A CB  1 
ATOM   98   C  CG  . GLU A  1 12  ? 10.268  6.238   12.300  1.00 9.87  ? 12  GLU A CG  1 
ATOM   99   C  CD  . GLU A  1 12  ? 10.570  4.781   12.387  1.00 9.38  ? 12  GLU A CD  1 
ATOM   100  O  OE1 . GLU A  1 12  ? 10.831  4.134   11.338  1.00 10.21 ? 12  GLU A OE1 1 
ATOM   101  O  OE2 . GLU A  1 12  ? 10.575  4.311   13.543  1.00 11.92 ? 12  GLU A OE2 1 
ATOM   102  N  N   . ASN A  1 13  ? 9.157   9.433   11.729  1.00 9.93  ? 13  ASN A N   1 
ATOM   103  C  CA  . ASN A  1 13  ? 8.372   10.039  10.688  1.00 11.00 ? 13  ASN A CA  1 
ATOM   104  C  C   . ASN A  1 13  ? 8.715   11.522  10.541  1.00 12.18 ? 13  ASN A C   1 
ATOM   105  O  O   . ASN A  1 13  ? 8.341   12.089  9.526   1.00 11.48 ? 13  ASN A O   1 
ATOM   106  C  CB  . ASN A  1 13  ? 6.891   9.905   10.955  1.00 10.22 ? 13  ASN A CB  1 
ATOM   107  C  CG  . ASN A  1 13  ? 6.421   8.472   10.898  1.00 10.30 ? 13  ASN A CG  1 
ATOM   108  O  OD1 . ASN A  1 13  ? 7.114   7.603   10.380  1.00 11.75 ? 13  ASN A OD1 1 
ATOM   109  N  ND2 . ASN A  1 13  ? 5.191   8.265   11.359  1.00 10.06 ? 13  ASN A ND2 1 
ATOM   110  N  N   A SER A  1 14  ? 9.406   12.065  11.568  0.50 10.86 ? 14  SER A N   1 
ATOM   111  N  N   B SER A  1 14  ? 9.412   12.117  11.507  0.50 12.35 ? 14  SER A N   1 
ATOM   112  C  CA  A SER A  1 14  ? 9.805   13.511  11.633  0.50 9.86  ? 14  SER A CA  1 
ATOM   113  C  CA  B SER A  1 14  ? 9.750   13.557  11.327  0.50 11.89 ? 14  SER A CA  1 
ATOM   114  C  C   A SER A  1 14  ? 11.257  13.738  11.244  0.50 10.56 ? 14  SER A C   1 
ATOM   115  C  C   B SER A  1 14  ? 11.235  13.733  10.985  0.50 12.11 ? 14  SER A C   1 
ATOM   116  O  O   A SER A  1 14  ? 11.648  14.907  11.130  0.50 10.58 ? 14  SER A O   1 
ATOM   117  O  O   B SER A  1 14  ? 11.680  14.849  10.744  0.50 11.61 ? 14  SER A O   1 
ATOM   118  C  CB  A SER A  1 14  ? 9.510   14.074  13.018  0.50 11.31 ? 14  SER A CB  1 
ATOM   119  C  CB  B SER A  1 14  ? 9.460   14.315  12.586  0.50 15.65 ? 14  SER A CB  1 
ATOM   120  O  OG  A SER A  1 14  ? 8.102   14.124  13.093  0.50 12.68 ? 14  SER A OG  1 
ATOM   121  O  OG  B SER A  1 14  ? 10.299  13.780  13.574  0.50 20.49 ? 14  SER A OG  1 
ATOM   122  N  N   . TRP A  1 15  ? 12.048  12.687  10.973  1.00 10.41 ? 15  TRP A N   1 
ATOM   123  C  CA  . TRP A  1 15  ? 13.464  12.917  10.598  1.00 10.59 ? 15  TRP A CA  1 
ATOM   124  C  C   . TRP A  1 15  ? 13.632  13.703  9.314   1.00 11.83 ? 15  TRP A C   1 
ATOM   125  O  O   . TRP A  1 15  ? 14.588  14.515  9.219   1.00 11.49 ? 15  TRP A O   1 
ATOM   126  C  CB  . TRP A  1 15  ? 14.180  11.549  10.367  1.00 9.38  ? 15  TRP A CB  1 
ATOM   127  C  CG  . TRP A  1 15  ? 14.293  10.704  11.615  1.00 9.95  ? 15  TRP A CG  1 
ATOM   128  C  CD1 . TRP A  1 15  ? 14.082  11.024  12.912  1.00 10.43 ? 15  TRP A CD1 1 
ATOM   129  C  CD2 . TRP A  1 15  ? 14.752  9.343   11.604  1.00 8.87  ? 15  TRP A CD2 1 
ATOM   130  N  NE1 . TRP A  1 15  ? 14.363  9.976   13.748  1.00 10.18 ? 15  TRP A NE1 1 
ATOM   131  C  CE2 . TRP A  1 15  ? 14.815  8.933   12.982  1.00 8.58  ? 15  TRP A CE2 1 
ATOM   132  C  CE3 . TRP A  1 15  ? 15.185  8.494   10.614  1.00 8.29  ? 15  TRP A CE3 1 
ATOM   133  C  CZ2 . TRP A  1 15  ? 15.217  7.610   13.342  1.00 9.03  ? 15  TRP A CZ2 1 
ATOM   134  C  CZ3 . TRP A  1 15  ? 15.608  7.166   10.971  1.00 8.22  ? 15  TRP A CZ3 1 
ATOM   135  C  CH2 . TRP A  1 15  ? 15.600  6.779   12.306  1.00 8.54  ? 15  TRP A CH2 1 
ATOM   136  N  N   . SER A  1 16  ? 12.743  13.590  8.341   1.00 9.75  ? 16  SER A N   1 
ATOM   137  C  CA  . SER A  1 16  ? 12.950  14.247  7.046   1.00 11.14 ? 16  SER A CA  1 
ATOM   138  C  C   . SER A  1 16  ? 12.794  15.785  7.160   1.00 11.12 ? 16  SER A C   1 
ATOM   139  O  O   . SER A  1 16  ? 13.222  16.412  6.185   1.00 10.93 ? 16  SER A O   1 
ATOM   140  C  CB  . SER A  1 16  ? 11.887  13.743  6.041   1.00 10.86 ? 16  SER A CB  1 
ATOM   141  O  OG  . SER A  1 16  ? 10.612  14.111  6.533   1.00 12.30 ? 16  SER A OG  1 
ATOM   142  N  N   A LYS A  1 17  ? 12.286  16.291  8.268   0.50 11.46 ? 17  LYS A N   1 
ATOM   143  N  N   B LYS A  1 17  ? 12.297  16.287  8.269   0.50 11.41 ? 17  LYS A N   1 
ATOM   144  C  CA  A LYS A  1 17  ? 12.211  17.779  8.379   0.50 12.31 ? 17  LYS A CA  1 
ATOM   145  C  CA  B LYS A  1 17  ? 12.233  17.767  8.322   0.50 12.24 ? 17  LYS A CA  1 
ATOM   146  C  C   A LYS A  1 17  ? 13.636  18.369  8.411   0.50 13.45 ? 17  LYS A C   1 
ATOM   147  C  C   B LYS A  1 17  ? 13.644  18.367  8.402   0.50 13.43 ? 17  LYS A C   1 
ATOM   148  O  O   A LYS A  1 17  ? 14.011  19.232  7.624   0.50 14.08 ? 17  LYS A O   1 
ATOM   149  O  O   B LYS A  1 17  ? 14.017  19.238  7.630   0.50 14.09 ? 17  LYS A O   1 
ATOM   150  C  CB  A LYS A  1 17  ? 11.520  18.150  9.665   0.50 12.95 ? 17  LYS A CB  1 
ATOM   151  C  CB  B LYS A  1 17  ? 11.454  18.213  9.511   0.50 12.63 ? 17  LYS A CB  1 
ATOM   152  C  CG  A LYS A  1 17  ? 10.009  17.984  9.671   0.50 15.95 ? 17  LYS A CG  1 
ATOM   153  C  CG  B LYS A  1 17  ? 11.451  19.738  9.604   0.50 15.18 ? 17  LYS A CG  1 
ATOM   154  C  CD  A LYS A  1 17  ? 9.503   17.985  11.110  0.50 17.26 ? 17  LYS A CD  1 
ATOM   155  C  CD  B LYS A  1 17  ? 10.626  20.181  10.786  0.50 15.70 ? 17  LYS A CD  1 
ATOM   156  C  CE  A LYS A  1 17  ? 8.123   17.301  11.202  0.50 18.96 ? 17  LYS A CE  1 
ATOM   157  C  CE  B LYS A  1 17  ? 9.118   20.198  10.436  0.50 16.50 ? 17  LYS A CE  1 
ATOM   158  N  NZ  A LYS A  1 17  ? 7.493   17.535  12.544  0.50 21.01 ? 17  LYS A NZ  1 
ATOM   159  N  NZ  B LYS A  1 17  ? 8.183   20.425  11.596  0.50 18.64 ? 17  LYS A NZ  1 
ATOM   160  N  N   . LYS A  1 18  ? 14.486  17.832  9.279   1.00 11.44 ? 18  LYS A N   1 
ATOM   161  C  CA  . LYS A  1 18  ? 15.835  18.362  9.369   1.00 13.03 ? 18  LYS A CA  1 
ATOM   162  C  C   . LYS A  1 18  ? 16.834  17.576  8.511   1.00 13.63 ? 18  LYS A C   1 
ATOM   163  O  O   . LYS A  1 18  ? 17.941  18.111  8.171   1.00 16.68 ? 18  LYS A O   1 
ATOM   164  C  CB  . LYS A  1 18  ? 16.303  18.304  10.808  1.00 15.98 ? 18  LYS A CB  1 
ATOM   165  C  CG  . LYS A  1 18  ? 17.784  18.627  11.034  1.00 23.64 ? 18  LYS A CG  1 
ATOM   166  C  CD  . LYS A  1 18  ? 18.070  18.586  12.540  1.00 29.61 ? 18  LYS A CD  1 
ATOM   167  C  CE  . LYS A  1 18  ? 19.576  18.739  12.738  1.00 31.95 ? 18  LYS A CE  1 
ATOM   168  N  NZ  . LYS A  1 18  ? 19.843  20.149  13.162  1.00 44.09 ? 18  LYS A NZ  1 
ATOM   169  N  N   . TYR A  1 19  ? 16.528  16.328  8.128   1.00 11.19 ? 19  TYR A N   1 
ATOM   170  C  CA  . TYR A  1 19  ? 17.404  15.480  7.310   1.00 11.91 ? 19  TYR A CA  1 
ATOM   171  C  C   . TYR A  1 19  ? 16.742  15.039  6.057   1.00 12.70 ? 19  TYR A C   1 
ATOM   172  O  O   . TYR A  1 19  ? 16.154  13.924  6.003   1.00 10.53 ? 19  TYR A O   1 
ATOM   173  C  CB  . TYR A  1 19  ? 17.866  14.265  8.120   1.00 11.80 ? 19  TYR A CB  1 
ATOM   174  C  CG  . TYR A  1 19  ? 18.524  14.627  9.434   1.00 12.34 ? 19  TYR A CG  1 
ATOM   175  C  CD1 . TYR A  1 19  ? 19.877  14.929  9.493   1.00 12.58 ? 19  TYR A CD1 1 
ATOM   176  C  CD2 . TYR A  1 19  ? 17.791  14.670  10.613  1.00 11.95 ? 19  TYR A CD2 1 
ATOM   177  C  CE1 . TYR A  1 19  ? 20.484  15.262  10.689  1.00 13.65 ? 19  TYR A CE1 1 
ATOM   178  C  CE2 . TYR A  1 19  ? 18.390  15.002  11.814  1.00 12.47 ? 19  TYR A CE2 1 
ATOM   179  C  CZ  . TYR A  1 19  ? 19.736  15.297  11.846  1.00 15.03 ? 19  TYR A CZ  1 
ATOM   180  O  OH  . TYR A  1 19  ? 20.337  15.628  13.040  1.00 20.30 ? 19  TYR A OH  1 
ATOM   181  N  N   . PRO A  1 20  ? 16.740  15.834  4.999   1.00 11.22 ? 20  PRO A N   1 
ATOM   182  C  CA  . PRO A  1 20  ? 15.831  15.617  3.902   1.00 11.45 ? 20  PRO A CA  1 
ATOM   183  C  C   . PRO A  1 20  ? 16.101  14.287  3.256   1.00 11.40 ? 20  PRO A C   1 
ATOM   184  O  O   . PRO A  1 20  ? 15.182  13.704  2.591   1.00 11.24 ? 20  PRO A O   1 
ATOM   185  C  CB  . PRO A  1 20  ? 16.171  16.725  2.872   1.00 12.89 ? 20  PRO A CB  1 
ATOM   186  C  CG  . PRO A  1 20  ? 16.748  17.798  3.761   1.00 13.79 ? 20  PRO A CG  1 
ATOM   187  C  CD  . PRO A  1 20  ? 17.446  17.161  4.947   1.00 11.52 ? 20  PRO A CD  1 
ATOM   188  N  N   . SER A  1 21  ? 17.310  13.693  3.351   1.00 10.00 ? 21  SER A N   1 
ATOM   189  C  CA  . SER A  1 21  ? 17.503  12.402  2.690   1.00 10.95 ? 21  SER A CA  1 
ATOM   190  C  C   . SER A  1 21  ? 16.636  11.299  3.324   1.00 10.04 ? 21  SER A C   1 
ATOM   191  O  O   . SER A  1 21  ? 16.432  10.266  2.646   1.00 9.00  ? 21  SER A O   1 
ATOM   192  C  CB  . SER A  1 21  ? 19.031  12.002  2.741   1.00 11.46 ? 21  SER A CB  1 
ATOM   193  O  OG  . SER A  1 21  ? 19.740  12.866  1.802   1.00 14.13 ? 21  SER A OG  1 
ATOM   194  N  N   . CYS A  1 22  ? 16.175  11.505  4.574   1.00 10.47 ? 22  CYS A N   1 
ATOM   195  C  CA  . CYS A  1 22  ? 15.314  10.500  5.208   1.00 10.68 ? 22  CYS A CA  1 
ATOM   196  C  C   . CYS A  1 22  ? 14.030  10.307  4.454   1.00 10.63 ? 22  CYS A C   1 
ATOM   197  O  O   . CYS A  1 22  ? 13.328  9.328   4.719   1.00 11.23 ? 22  CYS A O   1 
ATOM   198  C  CB  . CYS A  1 22  ? 15.109  10.799  6.673   1.00 11.68 ? 22  CYS A CB  1 
ATOM   199  S  SG  . CYS A  1 22  ? 16.697  10.879  7.615   1.00 12.45 ? 22  CYS A SG  1 
ATOM   200  N  N   . GLY A  1 23  ? 13.647  11.280  3.653   1.00 11.89 ? 23  GLY A N   1 
ATOM   201  C  CA  . GLY A  1 23  ? 12.459  11.164  2.757   1.00 11.21 ? 23  GLY A CA  1 
ATOM   202  C  C   . GLY A  1 23  ? 12.763  10.984  1.354   1.00 11.52 ? 23  GLY A C   1 
ATOM   203  O  O   . GLY A  1 23  ? 11.854  11.053  0.530   1.00 12.24 ? 23  GLY A O   1 
ATOM   204  N  N   . GLY A  1 24  ? 14.009  10.677  1.040   1.00 11.01 ? 24  GLY A N   1 
ATOM   205  C  CA  . GLY A  1 24  ? 14.455  10.460  -0.348  1.00 11.40 ? 24  GLY A CA  1 
ATOM   206  C  C   . GLY A  1 24  ? 14.534  9.054   -0.820  1.00 12.84 ? 24  GLY A C   1 
ATOM   207  O  O   . GLY A  1 24  ? 13.808  8.211   -0.226  1.00 13.69 ? 24  GLY A O   1 
ATOM   208  N  N   . LEU A  1 25  ? 15.315  8.803   -1.845  1.00 14.18 ? 25  LEU A N   1 
ATOM   209  C  CA  . LEU A  1 25  ? 15.420  7.491   -2.472  1.00 14.69 ? 25  LEU A CA  1 
ATOM   210  C  C   . LEU A  1 25  ? 16.384  6.595   -1.656  1.00 14.68 ? 25  LEU A C   1 
ATOM   211  O  O   . LEU A  1 25  ? 17.148  7.021   -0.769  1.00 13.17 ? 25  LEU A O   1 
ATOM   212  C  CB  . LEU A  1 25  ? 16.012  7.646   -3.884  1.00 18.60 ? 25  LEU A CB  1 
ATOM   213  C  CG  . LEU A  1 25  ? 15.088  8.513   -4.789  1.00 22.31 ? 25  LEU A CG  1 
ATOM   214  C  CD1 . LEU A  1 25  ? 15.762  8.657   -6.126  1.00 28.91 ? 25  LEU A CD1 1 
ATOM   215  C  CD2 . LEU A  1 25  ? 13.676  7.995   -4.984  1.00 26.58 ? 25  LEU A CD2 1 
ATOM   216  N  N   . LEU A  1 26  ? 16.235  5.320   -1.987  1.00 14.95 ? 26  LEU A N   1 
ATOM   217  C  CA  . LEU A  1 26  ? 17.141  4.247   -1.586  1.00 16.25 ? 26  LEU A CA  1 
ATOM   218  C  C   . LEU A  1 26  ? 17.139  4.053   -0.060  1.00 12.47 ? 26  LEU A C   1 
ATOM   219  O  O   . LEU A  1 26  ? 18.208  3.716   0.491   1.00 14.05 ? 26  LEU A O   1 
ATOM   220  C  CB  . LEU A  1 26  ? 18.572  4.441   -2.137  1.00 15.71 ? 26  LEU A CB  1 
ATOM   221  C  CG  . LEU A  1 26  ? 18.711  4.547   -3.681  1.00 22.04 ? 26  LEU A CG  1 
ATOM   222  C  CD1 . LEU A  1 26  ? 20.214  4.723   -3.976  1.00 26.95 ? 26  LEU A CD1 1 
ATOM   223  C  CD2 . LEU A  1 26  ? 18.248  3.266   -4.314  1.00 23.11 ? 26  LEU A CD2 1 
ATOM   224  N  N   . GLN A  1 27  ? 16.055  4.241   0.639   1.00 11.13 ? 27  GLN A N   1 
ATOM   225  C  CA  . GLN A  1 27  ? 16.089  4.165   2.136   1.00 9.51  ? 27  GLN A CA  1 
ATOM   226  C  C   . GLN A  1 27  ? 16.109  2.706   2.588   1.00 9.57  ? 27  GLN A C   1 
ATOM   227  O  O   . GLN A  1 27  ? 15.492  1.788   2.026   1.00 11.45 ? 27  GLN A O   1 
ATOM   228  C  CB  . GLN A  1 27  ? 14.921  4.888   2.702   1.00 10.03 ? 27  GLN A CB  1 
ATOM   229  C  CG  . GLN A  1 27  ? 15.028  6.394   2.444   1.00 9.62  ? 27  GLN A CG  1 
ATOM   230  C  CD  . GLN A  1 27  ? 16.187  6.995   3.138   1.00 9.44  ? 27  GLN A CD  1 
ATOM   231  O  OE1 . GLN A  1 27  ? 16.183  7.209   4.340   1.00 8.76  ? 27  GLN A OE1 1 
ATOM   232  N  NE2 . GLN A  1 27  ? 17.206  7.250   2.333   1.00 9.18  ? 27  GLN A NE2 1 
ATOM   233  N  N   . SER A  1 28  ? 16.829  2.524   3.686   1.00 9.01  ? 28  SER A N   1 
ATOM   234  C  CA  . SER A  1 28  ? 16.944  1.271   4.431   1.00 8.23  ? 28  SER A CA  1 
ATOM   235  C  C   . SER A  1 28  ? 16.424  1.498   5.813   1.00 9.01  ? 28  SER A C   1 
ATOM   236  O  O   . SER A  1 28  ? 16.343  2.622   6.322   1.00 9.35  ? 28  SER A O   1 
ATOM   237  C  CB  . SER A  1 28  ? 18.460  0.984   4.553   1.00 8.78  ? 28  SER A CB  1 
ATOM   238  O  OG  . SER A  1 28  ? 19.004  0.693   3.268   1.00 8.92  ? 28  SER A OG  1 
ATOM   239  N  N   . PRO A  1 29  ? 16.034  0.410   6.540   1.00 8.72  ? 29  PRO A N   1 
ATOM   240  C  CA  . PRO A  1 29  ? 16.168  -0.980  6.149   1.00 7.70  ? 29  PRO A CA  1 
ATOM   241  C  C   . PRO A  1 29  ? 14.937  -1.432  5.359   1.00 7.52  ? 29  PRO A C   1 
ATOM   242  O  O   . PRO A  1 29  ? 14.003  -0.626  5.164   1.00 9.44  ? 29  PRO A O   1 
ATOM   243  C  CB  . PRO A  1 29  ? 16.157  -1.726  7.506   1.00 8.11  ? 29  PRO A CB  1 
ATOM   244  C  CG  . PRO A  1 29  ? 15.186  -0.900  8.349   1.00 8.33  ? 29  PRO A CG  1 
ATOM   245  C  CD  . PRO A  1 29  ? 15.508  0.584   7.913   1.00 7.20  ? 29  PRO A CD  1 
ATOM   246  N  N   . ILE A  1 30  ? 14.935  -2.677  4.924   1.00 9.11  ? 30  ILE A N   1 
ATOM   247  C  CA  . ILE A  1 30  ? 13.897  -3.259  4.066   1.00 9.71  ? 30  ILE A CA  1 
ATOM   248  C  C   . ILE A  1 30  ? 13.610  -4.660  4.518   1.00 10.55 ? 30  ILE A C   1 
ATOM   249  O  O   . ILE A  1 30  ? 14.408  -5.304  5.247   1.00 11.40 ? 30  ILE A O   1 
ATOM   250  C  CB  . ILE A  1 30  ? 14.349  -3.281  2.593   1.00 11.17 ? 30  ILE A CB  1 
ATOM   251  C  CG1 . ILE A  1 30  ? 15.597  -4.153  2.372   1.00 10.30 ? 30  ILE A CG1 1 
ATOM   252  C  CG2 . ILE A  1 30  ? 14.530  -1.816  2.136   1.00 12.23 ? 30  ILE A CG2 1 
ATOM   253  C  CD1 . ILE A  1 30  ? 15.804  -4.201  0.873   1.00 13.36 ? 30  ILE A CD1 1 
ATOM   254  N  N   . ASP A  1 31  ? 12.476  -5.171  4.063   1.00 10.00 ? 31  ASP A N   1 
ATOM   255  C  CA  . ASP A  1 31  ? 12.103  -6.566  4.279   1.00 10.33 ? 31  ASP A CA  1 
ATOM   256  C  C   . ASP A  1 31  ? 12.726  -7.371  3.145   1.00 10.61 ? 31  ASP A C   1 
ATOM   257  O  O   . ASP A  1 31  ? 12.541  -7.114  1.924   1.00 13.53 ? 31  ASP A O   1 
ATOM   258  C  CB  . ASP A  1 31  ? 10.587  -6.719  4.229   1.00 11.34 ? 31  ASP A CB  1 
ATOM   259  C  CG  . ASP A  1 31  ? 10.132  -8.134  4.469   1.00 14.55 ? 31  ASP A CG  1 
ATOM   260  O  OD1 . ASP A  1 31  ? 10.718  -8.812  5.348   1.00 12.23 ? 31  ASP A OD1 1 
ATOM   261  O  OD2 . ASP A  1 31  ? 9.184   -8.564  3.792   1.00 16.73 ? 31  ASP A OD2 1 
ATOM   262  N  N   . LEU A  1 32  ? 13.494  -8.371  3.500   1.00 11.76 ? 32  LEU A N   1 
ATOM   263  C  CA  . LEU A  1 32  ? 14.101  -9.280  2.576   1.00 12.80 ? 32  LEU A CA  1 
ATOM   264  C  C   . LEU A  1 32  ? 13.180  -10.512 2.349   1.00 14.82 ? 32  LEU A C   1 
ATOM   265  O  O   . LEU A  1 32  ? 13.039  -11.370 3.226   1.00 15.04 ? 32  LEU A O   1 
ATOM   266  C  CB  . LEU A  1 32  ? 15.447  -9.774  3.187   1.00 13.95 ? 32  LEU A CB  1 
ATOM   267  C  CG  . LEU A  1 32  ? 16.397  -8.601  3.585   1.00 11.27 ? 32  LEU A CG  1 
ATOM   268  C  CD1 . LEU A  1 32  ? 17.594  -9.081  4.381   1.00 14.37 ? 32  LEU A CD1 1 
ATOM   269  C  CD2 . LEU A  1 32  ? 16.908  -7.917  2.341   1.00 15.08 ? 32  LEU A CD2 1 
ATOM   270  N  N   . HIS A  1 33  ? 12.474  -10.501 1.226   1.00 20.30 ? 33  HIS A N   1 
ATOM   271  C  CA  . HIS A  1 33  ? 11.477  -11.560 1.063   1.00 21.05 ? 33  HIS A CA  1 
ATOM   272  C  C   . HIS A  1 33  ? 11.611  -12.092 -0.269  1.00 23.53 ? 33  HIS A C   1 
ATOM   273  O  O   . HIS A  1 33  ? 12.153  -11.435 -1.137  1.00 18.67 ? 33  HIS A O   1 
ATOM   274  C  CB  . HIS A  1 33  ? 10.076  -11.048 1.380   1.00 22.19 ? 33  HIS A CB  1 
ATOM   275  C  CG  . HIS A  1 33  ? 9.648   -9.921  0.508   1.00 22.50 ? 33  HIS A CG  1 
ATOM   276  N  ND1 . HIS A  1 33  ? 8.908   -10.110 -0.594  1.00 23.73 ? 33  HIS A ND1 1 
ATOM   277  C  CD2 . HIS A  1 33  ? 9.919   -8.554  0.577   1.00 26.44 ? 33  HIS A CD2 1 
ATOM   278  C  CE1 . HIS A  1 33  ? 8.701   -8.930  -1.198  1.00 26.37 ? 33  HIS A CE1 1 
ATOM   279  N  NE2 . HIS A  1 33  ? 9.320   -7.976  -0.479  1.00 27.44 ? 33  HIS A NE2 1 
ATOM   280  N  N   . SER A  1 34  ? 11.112  -13.323 -0.430  1.00 25.46 ? 34  SER A N   1 
ATOM   281  C  CA  . SER A  1 34  ? 11.442  -14.186 -1.548  1.00 27.95 ? 34  SER A CA  1 
ATOM   282  C  C   . SER A  1 34  ? 11.169  -13.587 -2.944  1.00 28.28 ? 34  SER A C   1 
ATOM   283  O  O   . SER A  1 34  ? 12.038  -13.725 -3.820  1.00 30.09 ? 34  SER A O   1 
ATOM   284  C  CB  . SER A  1 34  ? 10.766  -15.556 -1.385  1.00 33.10 ? 34  SER A CB  1 
ATOM   285  O  OG  . SER A  1 34  ? 9.389   -15.365 -1.605  1.00 42.14 ? 34  SER A OG  1 
ATOM   286  N  N   . ASP A  1 35  ? 10.053  -12.838 -3.099  1.00 27.47 ? 35  ASP A N   1 
ATOM   287  C  CA  . ASP A  1 35  ? 9.662   -12.288 -4.377  1.00 33.53 ? 35  ASP A CA  1 
ATOM   288  C  C   . ASP A  1 35  ? 10.729  -11.359 -4.932  1.00 31.56 ? 35  ASP A C   1 
ATOM   289  O  O   . ASP A  1 35  ? 10.813  -11.152 -6.155  1.00 30.17 ? 35  ASP A O   1 
ATOM   290  C  CB  . ASP A  1 35  ? 8.362   -11.473 -4.208  1.00 37.16 ? 35  ASP A CB  1 
ATOM   291  N  N   . ILE A  1 36  ? 11.527  -10.733 -4.050  1.00 25.93 ? 36  ILE A N   1 
ATOM   292  C  CA  . ILE A  1 36  ? 12.432  -9.699  -4.566  1.00 22.74 ? 36  ILE A CA  1 
ATOM   293  C  C   . ILE A  1 36  ? 13.859  -10.192 -4.511  1.00 23.08 ? 36  ILE A C   1 
ATOM   294  O  O   . ILE A  1 36  ? 14.785  -9.389  -4.745  1.00 22.40 ? 36  ILE A O   1 
ATOM   295  C  CB  . ILE A  1 36  ? 12.349  -8.372  -3.810  1.00 20.84 ? 36  ILE A CB  1 
ATOM   296  C  CG1 . ILE A  1 36  ? 12.737  -8.668  -2.301  1.00 23.51 ? 36  ILE A CG1 1 
ATOM   297  C  CG2 . ILE A  1 36  ? 10.995  -7.707  -4.030  1.00 25.45 ? 36  ILE A CG2 1 
ATOM   298  C  CD1 . ILE A  1 36  ? 12.879  -7.413  -1.508  1.00 24.90 ? 36  ILE A CD1 1 
ATOM   299  N  N   . LEU A  1 37  ? 14.055  -11.444 -4.171  1.00 20.03 ? 37  LEU A N   1 
ATOM   300  C  CA  . LEU A  1 37  ? 15.449  -12.003 -4.130  1.00 21.48 ? 37  LEU A CA  1 
ATOM   301  C  C   . LEU A  1 37  ? 15.899  -12.543 -5.478  1.00 25.51 ? 37  LEU A C   1 
ATOM   302  O  O   . LEU A  1 37  ? 15.108  -13.208 -6.224  1.00 26.46 ? 37  LEU A O   1 
ATOM   303  C  CB  . LEU A  1 37  ? 15.534  -13.099 -3.071  1.00 20.54 ? 37  LEU A CB  1 
ATOM   304  C  CG  . LEU A  1 37  ? 15.158  -12.707 -1.615  1.00 20.94 ? 37  LEU A CG  1 
ATOM   305  C  CD1 . LEU A  1 37  ? 15.362  -13.954 -0.783  1.00 23.98 ? 37  LEU A CD1 1 
ATOM   306  C  CD2 . LEU A  1 37  ? 16.052  -11.579 -1.088  1.00 19.78 ? 37  LEU A CD2 1 
ATOM   307  N  N   . GLN A  1 38  ? 17.147  -12.324 -5.816  1.00 21.31 ? 38  GLN A N   1 
ATOM   308  C  CA  . GLN A  1 38  ? 17.681  -12.775 -7.114  1.00 22.25 ? 38  GLN A CA  1 
ATOM   309  C  C   . GLN A  1 38  ? 19.108  -13.231 -6.916  1.00 22.59 ? 38  GLN A C   1 
ATOM   310  O  O   . GLN A  1 38  ? 19.967  -12.452 -6.483  1.00 17.95 ? 38  GLN A O   1 
ATOM   311  C  CB  . GLN A  1 38  ? 17.619  -11.679 -8.172  1.00 25.45 ? 38  GLN A CB  1 
ATOM   312  C  CG  . GLN A  1 38  ? 18.408  -12.086 -9.400  1.00 32.76 ? 38  GLN A CG  1 
ATOM   313  C  CD  . GLN A  1 38  ? 17.882  -11.516 -10.696 1.00 40.97 ? 38  GLN A CD  1 
ATOM   314  O  OE1 . GLN A  1 38  ? 16.721  -11.763 -11.084 1.00 42.09 ? 38  GLN A OE1 1 
ATOM   315  N  NE2 . GLN A  1 38  ? 18.744  -10.747 -11.390 1.00 39.73 ? 38  GLN A NE2 1 
ATOM   316  N  N   . TYR A  1 39  ? 19.390  -14.503 -7.144  1.00 20.85 ? 39  TYR A N   1 
ATOM   317  C  CA  . TYR A  1 39  ? 20.719  -15.004 -7.075  1.00 19.48 ? 39  TYR A CA  1 
ATOM   318  C  C   . TYR A  1 39  ? 21.606  -14.286 -8.113  1.00 20.69 ? 39  TYR A C   1 
ATOM   319  O  O   . TYR A  1 39  ? 21.208  -14.077 -9.281  1.00 22.84 ? 39  TYR A O   1 
ATOM   320  C  CB  . TYR A  1 39  ? 20.671  -16.512 -7.446  1.00 19.09 ? 39  TYR A CB  1 
ATOM   321  C  CG  . TYR A  1 39  ? 21.991  -17.161 -7.568  1.00 23.89 ? 39  TYR A CG  1 
ATOM   322  C  CD1 . TYR A  1 39  ? 22.850  -17.210 -6.467  1.00 20.34 ? 39  TYR A CD1 1 
ATOM   323  C  CD2 . TYR A  1 39  ? 22.419  -17.741 -8.782  1.00 25.04 ? 39  TYR A CD2 1 
ATOM   324  C  CE1 . TYR A  1 39  ? 24.077  -17.841 -6.509  1.00 23.38 ? 39  TYR A CE1 1 
ATOM   325  C  CE2 . TYR A  1 39  ? 23.692  -18.304 -8.876  1.00 26.96 ? 39  TYR A CE2 1 
ATOM   326  C  CZ  . TYR A  1 39  ? 24.516  -18.412 -7.739  1.00 23.01 ? 39  TYR A CZ  1 
ATOM   327  O  OH  . TYR A  1 39  ? 25.785  -18.968 -7.737  1.00 29.95 ? 39  TYR A OH  1 
ATOM   328  N  N   . ASP A  1 40  ? 22.808  -13.941 -7.698  1.00 19.42 ? 40  ASP A N   1 
ATOM   329  C  CA  . ASP A  1 40  ? 23.762  -13.319 -8.547  1.00 20.46 ? 40  ASP A CA  1 
ATOM   330  C  C   . ASP A  1 40  ? 25.084  -14.046 -8.275  1.00 24.29 ? 40  ASP A C   1 
ATOM   331  O  O   . ASP A  1 40  ? 25.712  -13.904 -7.231  1.00 20.12 ? 40  ASP A O   1 
ATOM   332  C  CB  . ASP A  1 40  ? 23.819  -11.835 -8.245  1.00 24.50 ? 40  ASP A CB  1 
ATOM   333  C  CG  . ASP A  1 40  ? 24.820  -11.070 -9.160  1.00 31.21 ? 40  ASP A CG  1 
ATOM   334  O  OD1 . ASP A  1 40  ? 25.674  -11.697 -9.802  1.00 28.54 ? 40  ASP A OD1 1 
ATOM   335  O  OD2 . ASP A  1 40  ? 24.706  -9.827  -9.201  1.00 35.81 ? 40  ASP A OD2 1 
ATOM   336  N  N   . ALA A  1 41  ? 25.483  -14.923 -9.225  1.00 25.89 ? 41  ALA A N   1 
ATOM   337  C  CA  . ALA A  1 41  ? 26.781  -15.649 -9.147  1.00 28.71 ? 41  ALA A CA  1 
ATOM   338  C  C   . ALA A  1 41  ? 28.025  -14.725 -9.074  1.00 25.00 ? 41  ALA A C   1 
ATOM   339  O  O   . ALA A  1 41  ? 29.092  -15.162 -8.700  1.00 32.19 ? 41  ALA A O   1 
ATOM   340  C  CB  . ALA A  1 41  ? 26.912  -16.606 -10.342 1.00 30.35 ? 41  ALA A CB  1 
ATOM   341  N  N   . SER A  1 42  ? 27.888  -13.433 -9.400  1.00 27.18 ? 42  SER A N   1 
ATOM   342  C  CA  . SER A  1 42  ? 28.961  -12.452 -9.217  1.00 27.16 ? 42  SER A CA  1 
ATOM   343  C  C   . SER A  1 42  ? 29.283  -12.134 -7.762  1.00 31.54 ? 42  SER A C   1 
ATOM   344  O  O   . SER A  1 42  ? 30.299  -11.539 -7.453  1.00 31.97 ? 42  SER A O   1 
ATOM   345  C  CB  . SER A  1 42  ? 28.621  -11.180 -10.016 1.00 31.87 ? 42  SER A CB  1 
ATOM   346  O  OG  . SER A  1 42  ? 28.363  -10.040 -9.207  1.00 40.59 ? 42  SER A OG  1 
ATOM   347  N  N   . LEU A  1 43  ? 28.416  -12.523 -6.844  1.00 23.29 ? 43  LEU A N   1 
ATOM   348  C  CA  . LEU A  1 43  ? 28.637  -12.201 -5.414  1.00 22.66 ? 43  LEU A CA  1 
ATOM   349  C  C   . LEU A  1 43  ? 29.547  -13.194 -4.698  1.00 21.33 ? 43  LEU A C   1 
ATOM   350  O  O   . LEU A  1 43  ? 29.104  -14.159 -4.060  1.00 25.54 ? 43  LEU A O   1 
ATOM   351  C  CB  . LEU A  1 43  ? 27.269  -12.089 -4.702  1.00 18.18 ? 43  LEU A CB  1 
ATOM   352  C  CG  . LEU A  1 43  ? 26.417  -10.940 -5.234  1.00 18.84 ? 43  LEU A CG  1 
ATOM   353  C  CD1 . LEU A  1 43  ? 25.062  -10.975 -4.557  1.00 16.12 ? 43  LEU A CD1 1 
ATOM   354  C  CD2 . LEU A  1 43  ? 27.056  -9.559  -5.078  1.00 17.81 ? 43  LEU A CD2 1 
ATOM   355  N  N   . THR A  1 44  ? 30.835  -12.937 -4.745  1.00 22.08 ? 44  THR A N   1 
ATOM   356  C  CA  . THR A  1 44  ? 31.833  -13.855 -4.197  1.00 21.81 ? 44  THR A CA  1 
ATOM   357  C  C   . THR A  1 44  ? 32.102  -13.521 -2.711  1.00 20.71 ? 44  THR A C   1 
ATOM   358  O  O   . THR A  1 44  ? 31.615  -12.460 -2.222  1.00 19.24 ? 44  THR A O   1 
ATOM   359  C  CB  . THR A  1 44  ? 33.142  -13.698 -4.983  1.00 23.88 ? 44  THR A CB  1 
ATOM   360  O  OG1 . THR A  1 44  ? 33.488  -12.328 -4.916  1.00 27.68 ? 44  THR A OG1 1 
ATOM   361  C  CG2 . THR A  1 44  ? 32.961  -14.078 -6.450  1.00 30.15 ? 44  THR A CG2 1 
ATOM   362  N  N   . PRO A  1 45  ? 32.831  -14.378 -2.000  1.00 20.37 ? 45  PRO A N   1 
ATOM   363  C  CA  . PRO A  1 45  ? 33.005  -14.152 -0.576  1.00 19.15 ? 45  PRO A CA  1 
ATOM   364  C  C   . PRO A  1 45  ? 33.856  -12.952 -0.273  1.00 20.88 ? 45  PRO A C   1 
ATOM   365  O  O   . PRO A  1 45  ? 34.802  -12.671 -1.006  1.00 24.45 ? 45  PRO A O   1 
ATOM   366  C  CB  . PRO A  1 45  ? 33.728  -15.406 -0.130  1.00 21.42 ? 45  PRO A CB  1 
ATOM   367  C  CG  . PRO A  1 45  ? 33.309  -16.478 -1.124  1.00 20.53 ? 45  PRO A CG  1 
ATOM   368  C  CD  . PRO A  1 45  ? 33.311  -15.736 -2.413  1.00 22.36 ? 45  PRO A CD  1 
ATOM   369  N  N   . LEU A  1 46  ? 33.471  -12.151 0.710   1.00 16.42 ? 46  LEU A N   1 
ATOM   370  C  CA  . LEU A  1 46  ? 34.292  -11.040 1.178   1.00 17.49 ? 46  LEU A CA  1 
ATOM   371  C  C   . LEU A  1 46  ? 35.404  -11.638 2.053   1.00 17.13 ? 46  LEU A C   1 
ATOM   372  O  O   . LEU A  1 46  ? 35.216  -12.720 2.621   1.00 19.73 ? 46  LEU A O   1 
ATOM   373  C  CB  . LEU A  1 46  ? 33.480  -10.137 2.107   1.00 15.91 ? 46  LEU A CB  1 
ATOM   374  C  CG  . LEU A  1 46  ? 32.325  -9.405  1.372   1.00 17.62 ? 46  LEU A CG  1 
ATOM   375  C  CD1 . LEU A  1 46  ? 31.556  -8.563  2.381   1.00 17.96 ? 46  LEU A CD1 1 
ATOM   376  C  CD2 . LEU A  1 46  ? 32.890  -8.537  0.247   1.00 21.60 ? 46  LEU A CD2 1 
ATOM   377  N  N   . GLU A  1 47  ? 36.471  -10.867 2.156   1.00 16.52 ? 47  GLU A N   1 
ATOM   378  C  CA  . GLU A  1 47  ? 37.612  -11.178 3.033   1.00 18.93 ? 47  GLU A CA  1 
ATOM   379  C  C   . GLU A  1 47  ? 37.720  -10.126 4.108   1.00 17.40 ? 47  GLU A C   1 
ATOM   380  O  O   . GLU A  1 47  ? 37.673  -8.910  3.809   1.00 18.88 ? 47  GLU A O   1 
ATOM   381  C  CB  . GLU A  1 47  ? 38.929  -11.256 2.268   1.00 25.06 ? 47  GLU A CB  1 
ATOM   382  C  CG  . GLU A  1 47  ? 38.857  -12.254 1.124   1.00 36.56 ? 47  GLU A CG  1 
ATOM   383  N  N   . PHE A  1 48  ? 37.859  -10.534 5.377   1.00 15.98 ? 48  PHE A N   1 
ATOM   384  C  CA  . PHE A  1 48  ? 37.820  -9.602  6.458   1.00 16.77 ? 48  PHE A CA  1 
ATOM   385  C  C   . PHE A  1 48  ? 39.251  -9.479  6.903   1.00 18.28 ? 48  PHE A C   1 
ATOM   386  O  O   . PHE A  1 48  ? 39.782  -10.470 7.453   1.00 21.81 ? 48  PHE A O   1 
ATOM   387  C  CB  . PHE A  1 48  ? 36.891  -10.191 7.533   1.00 20.22 ? 48  PHE A CB  1 
ATOM   388  C  CG  . PHE A  1 48  ? 35.543  -10.565 6.977   1.00 18.03 ? 48  PHE A CG  1 
ATOM   389  C  CD1 . PHE A  1 48  ? 34.613  -9.580  6.590   1.00 17.01 ? 48  PHE A CD1 1 
ATOM   390  C  CD2 . PHE A  1 48  ? 35.193  -11.929 6.758   1.00 18.46 ? 48  PHE A CD2 1 
ATOM   391  C  CE1 . PHE A  1 48  ? 33.371  -9.938  6.027   1.00 16.51 ? 48  PHE A CE1 1 
ATOM   392  C  CE2 . PHE A  1 48  ? 34.004  -12.262 6.167   1.00 17.30 ? 48  PHE A CE2 1 
ATOM   393  C  CZ  . PHE A  1 48  ? 33.082  -11.235 5.795   1.00 16.37 ? 48  PHE A CZ  1 
ATOM   394  N  N   . GLN A  1 49  ? 39.882  -8.359  6.657   1.00 16.52 ? 49  GLN A N   1 
ATOM   395  C  CA  . GLN A  1 49  ? 41.323  -8.203  6.884   1.00 15.70 ? 49  GLN A CA  1 
ATOM   396  C  C   . GLN A  1 49  ? 41.597  -7.248  7.956   1.00 14.11 ? 49  GLN A C   1 
ATOM   397  O  O   . GLN A  1 49  ? 40.961  -6.201  8.130   1.00 13.78 ? 49  GLN A O   1 
ATOM   398  C  CB  . GLN A  1 49  ? 41.905  -7.604  5.571   1.00 16.67 ? 49  GLN A CB  1 
ATOM   399  C  CG  . GLN A  1 49  ? 41.719  -8.402  4.274   1.00 22.75 ? 49  GLN A CG  1 
ATOM   400  C  CD  . GLN A  1 49  ? 42.969  -9.016  3.701   1.00 35.22 ? 49  GLN A CD  1 
ATOM   401  O  OE1 . GLN A  1 49  ? 44.060  -8.776  4.185   1.00 34.99 ? 49  GLN A OE1 1 
ATOM   402  N  NE2 . GLN A  1 49  ? 42.814  -9.809  2.662   1.00 41.42 ? 49  GLN A NE2 1 
ATOM   403  N  N   . GLY A  1 50  ? 42.529  -7.551  8.877   1.00 16.08 ? 50  GLY A N   1 
ATOM   404  C  CA  . GLY A  1 50  ? 42.732  -6.711  9.988   1.00 16.37 ? 50  GLY A CA  1 
ATOM   405  C  C   . GLY A  1 50  ? 41.596  -6.670  11.039  1.00 13.76 ? 50  GLY A C   1 
ATOM   406  O  O   . GLY A  1 50  ? 41.592  -5.810  11.875  1.00 17.33 ? 50  GLY A O   1 
ATOM   407  N  N   . TYR A  1 51  ? 40.752  -7.701  10.983  1.00 15.46 ? 51  TYR A N   1 
ATOM   408  C  CA  . TYR A  1 51  ? 39.671  -7.879  12.009  1.00 15.16 ? 51  TYR A CA  1 
ATOM   409  C  C   . TYR A  1 51  ? 40.222  -8.331  13.357  1.00 17.57 ? 51  TYR A C   1 
ATOM   410  O  O   . TYR A  1 51  ? 39.561  -8.141  14.364  1.00 15.27 ? 51  TYR A O   1 
ATOM   411  C  CB  . TYR A  1 51  ? 38.591  -8.838  11.430  1.00 14.14 ? 51  TYR A CB  1 
ATOM   412  C  CG  . TYR A  1 51  ? 37.501  -8.090  10.612  1.00 13.51 ? 51  TYR A CG  1 
ATOM   413  C  CD1 . TYR A  1 51  ? 37.841  -7.225  9.547   1.00 13.81 ? 51  TYR A CD1 1 
ATOM   414  C  CD2 . TYR A  1 51  ? 36.143  -8.354  10.892  1.00 12.99 ? 51  TYR A CD2 1 
ATOM   415  C  CE1 . TYR A  1 51  ? 36.851  -6.578  8.778   1.00 13.67 ? 51  TYR A CE1 1 
ATOM   416  C  CE2 . TYR A  1 51  ? 35.141  -7.721  10.128  1.00 13.71 ? 51  TYR A CE2 1 
ATOM   417  C  CZ  . TYR A  1 51  ? 35.531  -6.824  9.144   1.00 14.26 ? 51  TYR A CZ  1 
ATOM   418  O  OH  . TYR A  1 51  ? 34.507  -6.189  8.418   1.00 14.47 ? 51  TYR A OH  1 
ATOM   419  N  N   . ASN A  1 52  ? 41.373  -9.029  13.343  1.00 18.54 ? 52  ASN A N   1 
ATOM   420  C  CA  . ASN A  1 52  ? 41.930  -9.568  14.609  1.00 20.83 ? 52  ASN A CA  1 
ATOM   421  C  C   . ASN A  1 52  ? 42.669  -8.432  15.340  1.00 21.10 ? 52  ASN A C   1 
ATOM   422  O  O   . ASN A  1 52  ? 43.874  -8.192  15.102  1.00 24.88 ? 52  ASN A O   1 
ATOM   423  C  CB  . ASN A  1 52  ? 42.797  -10.777 14.344  1.00 20.59 ? 52  ASN A CB  1 
ATOM   424  C  CG  . ASN A  1 52  ? 43.182  -11.516 15.632  1.00 25.07 ? 52  ASN A CG  1 
ATOM   425  O  OD1 . ASN A  1 52  ? 42.524  -11.427 16.640  1.00 22.29 ? 52  ASN A OD1 1 
ATOM   426  N  ND2 . ASN A  1 52  ? 44.341  -12.179 15.597  1.00 31.51 ? 52  ASN A ND2 1 
ATOM   427  N  N   . LEU A  1 53  ? 41.950  -7.623  16.099  1.00 20.13 ? 53  LEU A N   1 
ATOM   428  C  CA  . LEU A  1 53  ? 42.469  -6.422  16.660  1.00 19.23 ? 53  LEU A CA  1 
ATOM   429  C  C   . LEU A  1 53  ? 43.484  -6.809  17.728  1.00 23.78 ? 53  LEU A C   1 
ATOM   430  O  O   . LEU A  1 53  ? 43.247  -7.742  18.513  1.00 24.48 ? 53  LEU A O   1 
ATOM   431  C  CB  . LEU A  1 53  ? 41.391  -5.492  17.260  1.00 17.37 ? 53  LEU A CB  1 
ATOM   432  C  CG  . LEU A  1 53  ? 40.271  -5.138  16.219  1.00 15.61 ? 53  LEU A CG  1 
ATOM   433  C  CD1 . LEU A  1 53  ? 39.308  -4.259  16.941  1.00 16.49 ? 53  LEU A CD1 1 
ATOM   434  C  CD2 . LEU A  1 53  ? 40.827  -4.455  14.961  1.00 19.33 ? 53  LEU A CD2 1 
ATOM   435  N  N   . SER A  1 54  ? 44.569  -6.056  17.700  1.00 25.35 ? 54  SER A N   1 
ATOM   436  C  CA  . SER A  1 54  ? 45.625  -6.225  18.722  1.00 26.00 ? 54  SER A CA  1 
ATOM   437  C  C   . SER A  1 54  ? 45.024  -6.260  20.125  1.00 26.87 ? 54  SER A C   1 
ATOM   438  O  O   . SER A  1 54  ? 44.435  -5.275  20.515  1.00 24.11 ? 54  SER A O   1 
ATOM   439  C  CB  . SER A  1 54  ? 46.504  -4.968  18.640  1.00 24.30 ? 54  SER A CB  1 
ATOM   440  O  OG  . SER A  1 54  ? 47.643  -5.186  19.469  1.00 31.17 ? 54  SER A OG  1 
ATOM   441  N  N   . ALA A  1 55  ? 45.263  -7.320  20.907  1.00 29.18 ? 55  ALA A N   1 
ATOM   442  C  CA  . ALA A  1 55  ? 44.853  -7.341  22.325  1.00 29.66 ? 55  ALA A CA  1 
ATOM   443  C  C   . ALA A  1 55  ? 45.663  -6.341  23.121  1.00 31.86 ? 55  ALA A C   1 
ATOM   444  O  O   . ALA A  1 55  ? 45.388  -6.162  24.286  1.00 32.66 ? 55  ALA A O   1 
ATOM   445  C  CB  . ALA A  1 55  ? 45.041  -8.729  22.933  1.00 37.78 ? 55  ALA A CB  1 
ATOM   446  N  N   . ASN A  1 56  ? 46.678  -5.723  22.485  1.00 30.83 ? 56  ASN A N   1 
ATOM   447  C  CA  . ASN A  1 56  ? 47.525  -4.671  23.134  1.00 28.53 ? 56  ASN A CA  1 
ATOM   448  C  C   . ASN A  1 56  ? 47.096  -3.254  22.825  1.00 29.64 ? 56  ASN A C   1 
ATOM   449  O  O   . ASN A  1 56  ? 47.697  -2.316  23.286  1.00 33.74 ? 56  ASN A O   1 
ATOM   450  C  CB  . ASN A  1 56  ? 48.993  -4.823  22.688  1.00 30.71 ? 56  ASN A CB  1 
ATOM   451  C  CG  . ASN A  1 56  ? 49.592  -6.130  23.109  1.00 33.12 ? 56  ASN A CG  1 
ATOM   452  O  OD1 . ASN A  1 56  ? 49.441  -6.548  24.272  1.00 37.61 ? 56  ASN A OD1 1 
ATOM   453  N  ND2 . ASN A  1 56  ? 50.247  -6.811  22.172  1.00 33.14 ? 56  ASN A ND2 1 
ATOM   454  N  N   . LYS A  1 57  ? 46.061  -3.103  21.973  1.00 23.52 ? 57  LYS A N   1 
ATOM   455  C  CA  . LYS A  1 57  ? 45.440  -1.806  21.746  1.00 22.55 ? 57  LYS A CA  1 
ATOM   456  C  C   . LYS A  1 57  ? 44.054  -1.743  22.440  1.00 19.51 ? 57  LYS A C   1 
ATOM   457  O  O   . LYS A  1 57  ? 43.490  -2.741  22.732  1.00 22.02 ? 57  LYS A O   1 
ATOM   458  C  CB  . LYS A  1 57  ? 45.237  -1.642  20.218  1.00 23.34 ? 57  LYS A CB  1 
ATOM   459  C  CG  . LYS A  1 57  ? 46.513  -1.349  19.414  1.00 28.41 ? 57  LYS A CG  1 
ATOM   460  C  CD  . LYS A  1 57  ? 46.096  -0.959  17.989  1.00 31.03 ? 57  LYS A CD  1 
ATOM   461  C  CE  . LYS A  1 57  ? 45.229  0.328   17.912  1.00 30.28 ? 57  LYS A CE  1 
ATOM   462  N  NZ  . LYS A  1 57  ? 45.253  0.875   16.507  1.00 38.29 ? 57  LYS A NZ  1 
ATOM   463  N  N   . GLN A  1 58  ? 43.607  -0.551  22.736  1.00 21.69 ? 58  GLN A N   1 
ATOM   464  C  CA  . GLN A  1 58  ? 42.241  -0.323  23.298  1.00 22.09 ? 58  GLN A CA  1 
ATOM   465  C  C   . GLN A  1 58  ? 41.411  0.465   22.337  1.00 21.35 ? 58  GLN A C   1 
ATOM   466  O  O   . GLN A  1 58  ? 41.889  1.346   21.659  1.00 23.10 ? 58  GLN A O   1 
ATOM   467  C  CB  . GLN A  1 58  ? 42.309  0.417   24.606  1.00 22.81 ? 58  GLN A CB  1 
ATOM   468  C  CG  . GLN A  1 58  ? 42.824  -0.546  25.633  1.00 23.15 ? 58  GLN A CG  1 
ATOM   469  C  CD  . GLN A  1 58  ? 43.093  0.135   26.931  1.00 24.71 ? 58  GLN A CD  1 
ATOM   470  O  OE1 . GLN A  1 58  ? 42.797  1.331   27.081  1.00 29.56 ? 58  GLN A OE1 1 
ATOM   471  N  NE2 . GLN A  1 58  ? 43.780  -0.594  27.843  1.00 24.83 ? 58  GLN A NE2 1 
ATOM   472  N  N   . PHE A  1 59  ? 40.116  0.105   22.247  1.00 20.23 ? 59  PHE A N   1 
ATOM   473  C  CA  . PHE A  1 59  ? 39.183  0.777   21.321  1.00 19.90 ? 59  PHE A CA  1 
ATOM   474  C  C   . PHE A  1 59  ? 38.047  1.420   22.057  1.00 18.20 ? 59  PHE A C   1 
ATOM   475  O  O   . PHE A  1 59  ? 37.568  0.810   23.038  1.00 19.19 ? 59  PHE A O   1 
ATOM   476  C  CB  . PHE A  1 59  ? 38.712  -0.319  20.356  1.00 18.25 ? 59  PHE A CB  1 
ATOM   477  C  CG  . PHE A  1 59  ? 39.875  -0.890  19.591  1.00 18.81 ? 59  PHE A CG  1 
ATOM   478  C  CD1 . PHE A  1 59  ? 40.287  -0.278  18.453  1.00 18.19 ? 59  PHE A CD1 1 
ATOM   479  C  CD2 . PHE A  1 59  ? 40.611  -1.965  20.092  1.00 18.51 ? 59  PHE A CD2 1 
ATOM   480  C  CE1 . PHE A  1 59  ? 41.374  -0.711  17.731  1.00 20.55 ? 59  PHE A CE1 1 
ATOM   481  C  CE2 . PHE A  1 59  ? 41.775  -2.420  19.352  1.00 17.37 ? 59  PHE A CE2 1 
ATOM   482  C  CZ  . PHE A  1 59  ? 42.133  -1.775  18.153  1.00 17.35 ? 59  PHE A CZ  1 
ATOM   483  N  N   . LEU A  1 60  ? 37.668  2.613   21.636  1.00 18.24 ? 60  LEU A N   1 
ATOM   484  C  CA  . LEU A  1 60  ? 36.774  3.477   22.359  1.00 18.00 ? 60  LEU A CA  1 
ATOM   485  C  C   . LEU A  1 60  ? 35.292  3.015   22.168  1.00 20.85 ? 60  LEU A C   1 
ATOM   486  O  O   . LEU A  1 60  ? 34.828  2.920   21.040  1.00 16.90 ? 60  LEU A O   1 
ATOM   487  C  CB  . LEU A  1 60  ? 36.934  4.912   21.898  1.00 20.32 ? 60  LEU A CB  1 
ATOM   488  C  CG  . LEU A  1 60  ? 36.119  5.901   22.641  1.00 21.20 ? 60  LEU A CG  1 
ATOM   489  C  CD1 . LEU A  1 60  ? 36.706  5.993   24.089  1.00 25.03 ? 60  LEU A CD1 1 
ATOM   490  C  CD2 . LEU A  1 60  ? 36.126  7.248   21.950  1.00 24.36 ? 60  LEU A CD2 1 
ATOM   491  N  N   . LEU A  1 61  ? 34.633  2.650   23.239  1.00 17.87 ? 61  LEU A N   1 
ATOM   492  C  CA  . LEU A  1 61  ? 33.186  2.394   23.275  1.00 16.66 ? 61  LEU A CA  1 
ATOM   493  C  C   . LEU A  1 61  ? 32.460  3.585   23.768  1.00 18.62 ? 61  LEU A C   1 
ATOM   494  O  O   . LEU A  1 61  ? 32.797  4.135   24.806  1.00 18.51 ? 61  LEU A O   1 
ATOM   495  C  CB  . LEU A  1 61  ? 32.921  1.231   24.229  1.00 18.19 ? 61  LEU A CB  1 
ATOM   496  C  CG  . LEU A  1 61  ? 31.536  0.496   24.153  1.00 19.46 ? 61  LEU A CG  1 
ATOM   497  C  CD1 . LEU A  1 61  ? 31.344  -0.289  22.852  1.00 19.77 ? 61  LEU A CD1 1 
ATOM   498  C  CD2 . LEU A  1 61  ? 31.389  -0.516  25.282  1.00 19.87 ? 61  LEU A CD2 1 
ATOM   499  N  N   A THR A  1 62  ? 31.409  3.996   23.071  0.50 17.26 ? 62  THR A N   1 
ATOM   500  N  N   B THR A  1 62  ? 31.415  4.024   23.071  0.50 17.48 ? 62  THR A N   1 
ATOM   501  C  CA  A THR A  1 62  ? 30.678  5.176   23.454  0.50 17.71 ? 62  THR A CA  1 
ATOM   502  C  CA  B THR A  1 62  ? 30.671  5.189   23.514  0.50 18.06 ? 62  THR A CA  1 
ATOM   503  C  C   A THR A  1 62  ? 29.193  4.811   23.496  0.50 17.88 ? 62  THR A C   1 
ATOM   504  C  C   B THR A  1 62  ? 29.170  5.035   23.336  0.50 18.90 ? 62  THR A C   1 
ATOM   505  O  O   A THR A  1 62  ? 28.745  3.932   22.765  0.50 17.02 ? 62  THR A O   1 
ATOM   506  O  O   B THR A  1 62  ? 28.672  4.538   22.306  0.50 18.40 ? 62  THR A O   1 
ATOM   507  C  CB  A THR A  1 62  ? 30.877  6.391   22.475  0.50 21.86 ? 62  THR A CB  1 
ATOM   508  C  CB  B THR A  1 62  ? 31.067  6.531   22.822  0.50 21.67 ? 62  THR A CB  1 
ATOM   509  O  OG1 A THR A  1 62  ? 32.270  6.627   22.185  0.50 22.96 ? 62  THR A OG1 1 
ATOM   510  O  OG1 B THR A  1 62  ? 30.650  6.503   21.450  0.50 19.47 ? 62  THR A OG1 1 
ATOM   511  C  CG2 A THR A  1 62  ? 30.273  7.654   23.067  0.50 20.97 ? 62  THR A CG2 1 
ATOM   512  C  CG2 B THR A  1 62  ? 32.563  6.839   22.898  0.50 23.99 ? 62  THR A CG2 1 
ATOM   513  N  N   . ASN A  1 63  ? 28.444  5.513   24.331  1.00 18.35 ? 63  ASN A N   1 
ATOM   514  C  CA  . ASN A  1 63  ? 26.964  5.590   24.202  1.00 16.52 ? 63  ASN A CA  1 
ATOM   515  C  C   . ASN A  1 63  ? 26.731  6.945   23.571  1.00 18.48 ? 63  ASN A C   1 
ATOM   516  O  O   . ASN A  1 63  ? 26.977  8.031   24.112  1.00 18.36 ? 63  ASN A O   1 
ATOM   517  C  CB  . ASN A  1 63  ? 26.363  5.537   25.588  1.00 15.94 ? 63  ASN A CB  1 
ATOM   518  C  CG  . ASN A  1 63  ? 24.857  5.788   25.625  1.00 15.81 ? 63  ASN A CG  1 
ATOM   519  O  OD1 . ASN A  1 63  ? 24.271  6.499   24.758  1.00 17.61 ? 63  ASN A OD1 1 
ATOM   520  N  ND2 . ASN A  1 63  ? 24.226  5.230   26.706  1.00 16.23 ? 63  ASN A ND2 1 
ATOM   521  N  N   . ASN A  1 64  ? 26.265  6.949   22.332  1.00 20.17 ? 64  ASN A N   1 
ATOM   522  C  CA  . ASN A  1 64  ? 26.045  8.221   21.646  1.00 19.79 ? 64  ASN A CA  1 
ATOM   523  C  C   . ASN A  1 64  ? 24.598  8.721   21.708  1.00 18.86 ? 64  ASN A C   1 
ATOM   524  O  O   . ASN A  1 64  ? 24.248  9.662   20.977  1.00 21.79 ? 64  ASN A O   1 
ATOM   525  C  CB  . ASN A  1 64  ? 26.470  8.154   20.168  1.00 20.88 ? 64  ASN A CB  1 
ATOM   526  C  CG  . ASN A  1 64  ? 25.651  7.118   19.363  1.00 21.71 ? 64  ASN A CG  1 
ATOM   527  O  OD1 . ASN A  1 64  ? 24.579  6.684   19.808  1.00 19.64 ? 64  ASN A OD1 1 
ATOM   528  N  ND2 . ASN A  1 64  ? 26.146  6.723   18.172  1.00 24.63 ? 64  ASN A ND2 1 
ATOM   529  N  N   . GLY A  1 65  ? 23.795  8.152   22.608  1.00 17.96 ? 65  GLY A N   1 
ATOM   530  C  CA  . GLY A  1 65  ? 22.412  8.519   22.812  1.00 20.93 ? 65  GLY A CA  1 
ATOM   531  C  C   . GLY A  1 65  ? 21.470  7.809   21.825  1.00 21.06 ? 65  GLY A C   1 
ATOM   532  O  O   . GLY A  1 65  ? 20.263  7.933   21.974  1.00 22.99 ? 65  GLY A O   1 
ATOM   533  N  N   . HIS A  1 66  ? 22.000  7.048   20.864  1.00 17.04 ? 66  HIS A N   1 
ATOM   534  C  CA  . HIS A  1 66  ? 21.202  6.335   19.886  1.00 16.15 ? 66  HIS A CA  1 
ATOM   535  C  C   . HIS A  1 66  ? 21.541  4.874   19.854  1.00 15.06 ? 66  HIS A C   1 
ATOM   536  O  O   . HIS A  1 66  ? 20.653  4.121   19.415  1.00 16.81 ? 66  HIS A O   1 
ATOM   537  C  CB  . HIS A  1 66  ? 21.354  6.930   18.485  1.00 16.30 ? 66  HIS A CB  1 
ATOM   538  C  CG  . HIS A  1 66  ? 21.151  8.446   18.422  1.00 19.26 ? 66  HIS A CG  1 
ATOM   539  N  ND1 . HIS A  1 66  ? 19.927  9.059   18.537  1.00 22.56 ? 66  HIS A ND1 1 
ATOM   540  C  CD2 . HIS A  1 66  ? 22.090  9.451   18.224  1.00 20.44 ? 66  HIS A CD2 1 
ATOM   541  C  CE1 . HIS A  1 66  ? 20.110  10.415  18.435  1.00 20.28 ? 66  HIS A CE1 1 
ATOM   542  N  NE2 . HIS A  1 66  ? 21.423  10.642  18.236  1.00 21.38 ? 66  HIS A NE2 1 
ATOM   543  N  N   . SER A  1 67  ? 22.749  4.447   20.246  1.00 14.93 ? 67  SER A N   1 
ATOM   544  C  CA  . SER A  1 67  ? 23.188  3.070   20.261  1.00 14.51 ? 67  SER A CA  1 
ATOM   545  C  C   . SER A  1 67  ? 24.451  3.053   21.117  1.00 15.94 ? 67  SER A C   1 
ATOM   546  O  O   . SER A  1 67  ? 24.829  4.078   21.675  1.00 16.01 ? 67  SER A O   1 
ATOM   547  C  CB  . SER A  1 67  ? 23.522  2.692   18.804  1.00 14.45 ? 67  SER A CB  1 
ATOM   548  O  OG  . SER A  1 67  ? 23.924  1.287   18.791  1.00 15.48 ? 67  SER A OG  1 
ATOM   549  N  N   . VAL A  1 68  ? 25.040  1.880   21.208  1.00 14.48 ? 68  VAL A N   1 
ATOM   550  C  CA  . VAL A  1 68  ? 26.379  1.772   21.746  1.00 13.98 ? 68  VAL A CA  1 
ATOM   551  C  C   . VAL A  1 68  ? 27.273  1.544   20.507  1.00 14.34 ? 68  VAL A C   1 
ATOM   552  O  O   . VAL A  1 68  ? 26.971  0.656   19.695  1.00 14.60 ? 68  VAL A O   1 
ATOM   553  C  CB  . VAL A  1 68  ? 26.432  0.682   22.866  1.00 17.61 ? 68  VAL A CB  1 
ATOM   554  C  CG1 . VAL A  1 68  ? 25.945  -0.697  22.469  1.00 18.16 ? 68  VAL A CG1 1 
ATOM   555  C  CG2 . VAL A  1 68  ? 27.857  0.556   23.323  1.00 21.99 ? 68  VAL A CG2 1 
ATOM   556  N  N   . LYS A  1 69  ? 28.362  2.321   20.437  1.00 14.19 ? 69  LYS A N   1 
ATOM   557  C  CA  . LYS A  1 69  ? 29.265  2.185   19.307  1.00 13.97 ? 69  LYS A CA  1 
ATOM   558  C  C   . LYS A  1 69  ? 30.693  1.935   19.734  1.00 13.69 ? 69  LYS A C   1 
ATOM   559  O  O   . LYS A  1 69  ? 31.126  2.505   20.742  1.00 16.40 ? 69  LYS A O   1 
ATOM   560  C  CB  . LYS A  1 69  ? 29.193  3.345   18.351  1.00 18.36 ? 69  LYS A CB  1 
ATOM   561  C  CG  . LYS A  1 69  ? 29.740  4.647   18.674  1.00 21.71 ? 69  LYS A CG  1 
ATOM   562  C  CD  . LYS A  1 69  ? 29.963  5.461   17.376  1.00 20.98 ? 69  LYS A CD  1 
ATOM   563  C  CE  . LYS A  1 69  ? 30.510  6.763   17.968  1.00 27.75 ? 69  LYS A CE  1 
ATOM   564  N  NZ  . LYS A  1 69  ? 30.741  7.837   16.966  1.00 27.33 ? 69  LYS A NZ  1 
ATOM   565  N  N   . LEU A  1 70  ? 31.338  1.038   19.002  1.00 13.12 ? 70  LEU A N   1 
ATOM   566  C  CA  . LEU A  1 70  ? 32.798  0.744   19.211  1.00 14.07 ? 70  LEU A CA  1 
ATOM   567  C  C   . LEU A  1 70  ? 33.540  1.353   18.053  1.00 13.49 ? 70  LEU A C   1 
ATOM   568  O  O   . LEU A  1 70  ? 33.284  0.983   16.899  1.00 13.56 ? 70  LEU A O   1 
ATOM   569  C  CB  . LEU A  1 70  ? 32.973  -0.744  19.308  1.00 13.75 ? 70  LEU A CB  1 
ATOM   570  C  CG  . LEU A  1 70  ? 34.484  -1.172  19.582  1.00 14.72 ? 70  LEU A CG  1 
ATOM   571  C  CD1 . LEU A  1 70  ? 35.077  -0.696  20.931  1.00 16.12 ? 70  LEU A CD1 1 
ATOM   572  C  CD2 . LEU A  1 70  ? 34.531  -2.657  19.461  1.00 14.80 ? 70  LEU A CD2 1 
ATOM   573  N  N   . ASN A  1 71  ? 34.536  2.245   18.304  1.00 14.36 ? 71  ASN A N   1 
ATOM   574  C  CA  . ASN A  1 71  ? 35.361  2.758   17.239  1.00 13.98 ? 71  ASN A CA  1 
ATOM   575  C  C   . ASN A  1 71  ? 36.357  1.693   16.764  1.00 16.34 ? 71  ASN A C   1 
ATOM   576  O  O   . ASN A  1 71  ? 36.854  0.851   17.524  1.00 16.96 ? 71  ASN A O   1 
ATOM   577  C  CB  . ASN A  1 71  ? 36.194  3.921   17.747  1.00 17.03 ? 71  ASN A CB  1 
ATOM   578  C  CG  . ASN A  1 71  ? 35.398  5.205   17.768  1.00 20.67 ? 71  ASN A CG  1 
ATOM   579  O  OD1 . ASN A  1 71  ? 34.208  5.264   17.393  1.00 29.14 ? 71  ASN A OD1 1 
ATOM   580  N  ND2 . ASN A  1 71  ? 36.063  6.290   18.200  1.00 25.45 ? 71  ASN A ND2 1 
ATOM   581  N  N   . LEU A  1 72  ? 36.538  1.616   15.462  1.00 13.21 ? 72  LEU A N   1 
ATOM   582  C  CA  . LEU A  1 72  ? 37.393  0.610   14.856  1.00 14.45 ? 72  LEU A CA  1 
ATOM   583  C  C   . LEU A  1 72  ? 38.540  1.323   14.102  1.00 15.32 ? 72  LEU A C   1 
ATOM   584  O  O   . LEU A  1 72  ? 38.350  2.429   13.564  1.00 15.88 ? 72  LEU A O   1 
ATOM   585  C  CB  . LEU A  1 72  ? 36.544  -0.290  13.891  1.00 12.49 ? 72  LEU A CB  1 
ATOM   586  C  CG  . LEU A  1 72  ? 35.461  -1.105  14.546  1.00 13.58 ? 72  LEU A CG  1 
ATOM   587  C  CD1 . LEU A  1 72  ? 34.520  -1.769  13.514  1.00 12.92 ? 72  LEU A CD1 1 
ATOM   588  C  CD2 . LEU A  1 72  ? 35.951  -2.129  15.562  1.00 14.64 ? 72  LEU A CD2 1 
ATOM   589  N  N   . PRO A  1 73  ? 39.673  0.601   13.890  1.00 14.75 ? 73  PRO A N   1 
ATOM   590  C  CA  . PRO A  1 73  ? 40.811  1.262   13.231  1.00 16.50 ? 73  PRO A CA  1 
ATOM   591  C  C   . PRO A  1 73  ? 40.729  1.106   11.718  1.00 15.39 ? 73  PRO A C   1 
ATOM   592  O  O   . PRO A  1 73  ? 40.246  0.085   11.203  1.00 16.52 ? 73  PRO A O   1 
ATOM   593  C  CB  . PRO A  1 73  ? 42.005  0.482   13.875  1.00 16.55 ? 73  PRO A CB  1 
ATOM   594  C  CG  . PRO A  1 73  ? 41.486  -0.931  14.080  1.00 16.32 ? 73  PRO A CG  1 
ATOM   595  C  CD  . PRO A  1 73  ? 39.960  -0.762  14.399  1.00 14.94 ? 73  PRO A CD  1 
ATOM   596  N  N   . SER A  1 74  ? 41.289  2.105   11.054  1.00 18.03 ? 74  SER A N   1 
ATOM   597  C  CA  . SER A  1 74  ? 41.188  2.099   9.598   1.00 17.89 ? 74  SER A CA  1 
ATOM   598  C  C   . SER A  1 74  ? 42.066  1.085   8.881   1.00 17.26 ? 74  SER A C   1 
ATOM   599  O  O   . SER A  1 74  ? 41.948  0.903   7.675   1.00 19.12 ? 74  SER A O   1 
ATOM   600  C  CB  . SER A  1 74  ? 41.472  3.462   9.010   1.00 22.95 ? 74  SER A CB  1 
ATOM   601  O  OG  . SER A  1 74  ? 42.751  3.882   9.413   1.00 26.68 ? 74  SER A OG  1 
ATOM   602  N  N   . ASP A  1 75  ? 42.978  0.376   9.558   1.00 16.22 ? 75  ASP A N   1 
ATOM   603  C  CA  . ASP A  1 75  ? 43.629  -0.754  8.898   1.00 18.17 ? 75  ASP A CA  1 
ATOM   604  C  C   . ASP A  1 75  ? 42.778  -2.019  8.798   1.00 15.51 ? 75  ASP A C   1 
ATOM   605  O  O   . ASP A  1 75  ? 43.095  -2.977  8.126   1.00 19.38 ? 75  ASP A O   1 
ATOM   606  C  CB  . ASP A  1 75  ? 44.975  -1.048  9.661   1.00 19.65 ? 75  ASP A CB  1 
ATOM   607  C  CG  . ASP A  1 75  ? 44.746  -1.475  11.102  1.00 21.31 ? 75  ASP A CG  1 
ATOM   608  O  OD1 . ASP A  1 75  ? 44.359  -0.643  11.930  1.00 25.86 ? 75  ASP A OD1 1 
ATOM   609  O  OD2 . ASP A  1 75  ? 45.018  -2.659  11.387  1.00 29.05 ? 75  ASP A OD2 1 
ATOM   610  N  N   . MET A  1 76  ? 41.637  -2.043  9.533   1.00 15.35 ? 76  MET A N   1 
ATOM   611  C  CA  . MET A  1 76  ? 40.653  -3.133  9.398   1.00 14.98 ? 76  MET A CA  1 
ATOM   612  C  C   . MET A  1 76  ? 39.833  -2.769  8.163   1.00 13.00 ? 76  MET A C   1 
ATOM   613  O  O   . MET A  1 76  ? 39.444  -1.640  8.007   1.00 13.99 ? 76  MET A O   1 
ATOM   614  C  CB  . MET A  1 76  ? 39.765  -3.088  10.642  1.00 15.72 ? 76  MET A CB  1 
ATOM   615  C  CG  . MET A  1 76  ? 38.593  -4.002  10.611  1.00 15.19 ? 76  MET A CG  1 
ATOM   616  S  SD  . MET A  1 76  ? 37.843  -3.925  12.279  1.00 15.33 ? 76  MET A SD  1 
ATOM   617  C  CE  . MET A  1 76  ? 36.229  -4.648  11.882  1.00 14.60 ? 76  MET A CE  1 
ATOM   618  N  N   . HIS A  1 77  ? 39.701  -3.728  7.311   1.00 11.49 ? 77  HIS A N   1 
ATOM   619  C  CA  . HIS A  1 77  ? 38.956  -3.510  6.035   1.00 12.53 ? 77  HIS A CA  1 
ATOM   620  C  C   . HIS A  1 77  ? 38.391  -4.734  5.457   1.00 13.19 ? 77  HIS A C   1 
ATOM   621  O  O   . HIS A  1 77  ? 38.720  -5.897  5.771   1.00 14.02 ? 77  HIS A O   1 
ATOM   622  C  CB  . HIS A  1 77  ? 39.888  -2.776  4.995   1.00 14.90 ? 77  HIS A CB  1 
ATOM   623  C  CG  . HIS A  1 77  ? 41.077  -3.596  4.552   1.00 18.03 ? 77  HIS A CG  1 
ATOM   624  N  ND1 . HIS A  1 77  ? 42.262  -3.507  5.199   1.00 18.99 ? 77  HIS A ND1 1 
ATOM   625  C  CD2 . HIS A  1 77  ? 41.244  -4.481  3.525   1.00 19.44 ? 77  HIS A CD2 1 
ATOM   626  C  CE1 . HIS A  1 77  ? 43.156  -4.318  4.615   1.00 19.09 ? 77  HIS A CE1 1 
ATOM   627  N  NE2 . HIS A  1 77  ? 42.575  -4.927  3.595   1.00 17.31 ? 77  HIS A NE2 1 
ATOM   628  N  N   . ILE A  1 78  ? 37.453  -4.511  4.542   1.00 13.38 ? 78  ILE A N   1 
ATOM   629  C  CA  . ILE A  1 78  ? 36.861  -5.526  3.633   1.00 16.18 ? 78  ILE A CA  1 
ATOM   630  C  C   . ILE A  1 78  ? 37.604  -5.592  2.323   1.00 15.01 ? 78  ILE A C   1 
ATOM   631  O  O   . ILE A  1 78  ? 37.823  -4.502  1.738   1.00 15.55 ? 78  ILE A O   1 
ATOM   632  C  CB  . ILE A  1 78  ? 35.325  -5.227  3.350   1.00 15.95 ? 78  ILE A CB  1 
ATOM   633  C  CG1 . ILE A  1 78  ? 34.474  -5.256  4.613   1.00 19.75 ? 78  ILE A CG1 1 
ATOM   634  C  CG2 . ILE A  1 78  ? 34.782  -6.180  2.267   1.00 21.53 ? 78  ILE A CG2 1 
ATOM   635  C  CD1 . ILE A  1 78  ? 33.156  -4.497  4.333   1.00 16.90 ? 78  ILE A CD1 1 
ATOM   636  N  N   . GLN A  1 79  ? 38.009  -6.786  1.909   1.00 14.81 ? 79  GLN A N   1 
ATOM   637  C  CA  . GLN A  1 79  ? 38.525  -6.968  0.580   1.00 18.11 ? 79  GLN A CA  1 
ATOM   638  C  C   . GLN A  1 79  ? 37.476  -7.743  -0.201  1.00 18.82 ? 79  GLN A C   1 
ATOM   639  O  O   . GLN A  1 79  ? 36.809  -8.686  0.330   1.00 20.01 ? 79  GLN A O   1 
ATOM   640  C  CB  . GLN A  1 79  ? 39.832  -7.830  0.697   1.00 23.33 ? 79  GLN A CB  1 
ATOM   641  C  CG  . GLN A  1 79  ? 40.421  -8.275  -0.653  1.00 29.29 ? 79  GLN A CG  1 
ATOM   642  N  N   . GLY A  1 80  ? 37.373  -7.463  -1.479  1.00 21.56 ? 80  GLY A N   1 
ATOM   643  C  CA  . GLY A  1 80  ? 36.447  -8.237  -2.335  1.00 20.32 ? 80  GLY A CA  1 
ATOM   644  C  C   . GLY A  1 80  ? 35.434  -7.348  -3.037  1.00 19.58 ? 80  GLY A C   1 
ATOM   645  O  O   . GLY A  1 80  ? 34.826  -7.771  -4.011  1.00 22.91 ? 80  GLY A O   1 
ATOM   646  N  N   . LEU A  1 81  ? 35.271  -6.096  -2.604  1.00 17.64 ? 81  LEU A N   1 
ATOM   647  C  CA  . LEU A  1 81  ? 34.448  -5.111  -3.292  1.00 21.16 ? 81  LEU A CA  1 
ATOM   648  C  C   . LEU A  1 81  ? 35.367  -4.402  -4.304  1.00 24.36 ? 81  LEU A C   1 
ATOM   649  O  O   . LEU A  1 81  ? 36.573  -4.693  -4.365  1.00 23.69 ? 81  LEU A O   1 
ATOM   650  C  CB  . LEU A  1 81  ? 33.820  -4.116  -2.342  1.00 19.13 ? 81  LEU A CB  1 
ATOM   651  C  CG  . LEU A  1 81  ? 32.827  -4.796  -1.350  1.00 17.05 ? 81  LEU A CG  1 
ATOM   652  C  CD1 . LEU A  1 81  ? 32.423  -3.823  -0.247  1.00 17.41 ? 81  LEU A CD1 1 
ATOM   653  C  CD2 . LEU A  1 81  ? 31.592  -5.404  -2.045  1.00 19.32 ? 81  LEU A CD2 1 
ATOM   654  N  N   . GLN A  1 82  ? 34.796  -3.510  -5.083  1.00 26.89 ? 82  GLN A N   1 
ATOM   655  C  CA  . GLN A  1 82  ? 35.633  -2.846  -6.087  1.00 26.28 ? 82  GLN A CA  1 
ATOM   656  C  C   . GLN A  1 82  ? 36.760  -2.038  -5.540  1.00 25.34 ? 82  GLN A C   1 
ATOM   657  O  O   . GLN A  1 82  ? 37.962  -2.061  -6.020  1.00 24.11 ? 82  GLN A O   1 
ATOM   658  C  CB  . GLN A  1 82  ? 34.754  -2.031  -7.033  1.00 31.13 ? 82  GLN A CB  1 
ATOM   659  C  CG  . GLN A  1 82  ? 35.648  -1.459  -8.125  1.00 37.58 ? 82  GLN A CG  1 
ATOM   660  C  CD  . GLN A  1 82  ? 34.921  -0.966  -9.353  1.00 44.96 ? 82  GLN A CD  1 
ATOM   661  O  OE1 . GLN A  1 82  ? 34.647  -1.729  -10.282 1.00 43.42 ? 82  GLN A OE1 1 
ATOM   662  N  NE2 . GLN A  1 82  ? 34.645  0.332   -9.387  1.00 41.38 ? 82  GLN A NE2 1 
ATOM   663  N  N   . SER A  1 83  ? 36.360  -1.303  -4.503  1.00 19.63 ? 83  SER A N   1 
ATOM   664  C  CA  . SER A  1 83  ? 37.269  -0.465  -3.757  1.00 14.70 ? 83  SER A CA  1 
ATOM   665  C  C   . SER A  1 83  ? 37.476  -1.122  -2.420  1.00 14.36 ? 83  SER A C   1 
ATOM   666  O  O   . SER A  1 83  ? 36.630  -1.938  -1.982  1.00 14.57 ? 83  SER A O   1 
ATOM   667  C  CB  . SER A  1 83  ? 36.716  0.885   -3.480  1.00 16.61 ? 83  SER A CB  1 
ATOM   668  O  OG  . SER A  1 83  ? 36.515  1.664   -4.669  1.00 17.48 ? 83  SER A OG  1 
ATOM   669  N  N   . ARG A  1 84  ? 38.566  -0.748  -1.743  1.00 13.91 ? 84  ARG A N   1 
ATOM   670  C  CA  . ARG A  1 84  ? 38.693  -1.145  -0.347  1.00 13.51 ? 84  ARG A CA  1 
ATOM   671  C  C   . ARG A  1 84  ? 37.799  -0.294  0.487   1.00 12.08 ? 84  ARG A C   1 
ATOM   672  O  O   . ARG A  1 84  ? 37.772  0.922   0.379   1.00 12.59 ? 84  ARG A O   1 
ATOM   673  C  CB  . ARG A  1 84  ? 40.169  -0.903  0.095   1.00 13.36 ? 84  ARG A CB  1 
ATOM   674  C  CG  . ARG A  1 84  ? 40.384  -1.276  1.606   1.00 13.99 ? 84  ARG A CG  1 
ATOM   675  C  CD  . ARG A  1 84  ? 41.835  -1.006  2.079   1.00 14.60 ? 84  ARG A CD  1 
ATOM   676  N  NE  . ARG A  1 84  ? 42.603  -2.095  1.545   1.00 14.33 ? 84  ARG A NE  1 
ATOM   677  C  CZ  . ARG A  1 84  ? 43.908  -2.221  1.844   1.00 14.49 ? 84  ARG A CZ  1 
ATOM   678  N  NH1 . ARG A  1 84  ? 44.503  -1.292  2.566   1.00 16.33 ? 84  ARG A NH1 1 
ATOM   679  N  NH2 . ARG A  1 84  ? 44.578  -3.233  1.357   1.00 17.62 ? 84  ARG A NH2 1 
ATOM   680  N  N   . TYR A  1 85  ? 37.072  -0.984  1.432   1.00 11.97 ? 85  TYR A N   1 
ATOM   681  C  CA  . TYR A  1 85  ? 36.327  -0.289  2.440   1.00 11.38 ? 85  TYR A CA  1 
ATOM   682  C  C   . TYR A  1 85  ? 36.884  -0.539  3.849   1.00 10.80 ? 85  TYR A C   1 
ATOM   683  O  O   . TYR A  1 85  ? 36.996  -1.687  4.298   1.00 12.37 ? 85  TYR A O   1 
ATOM   684  C  CB  . TYR A  1 85  ? 34.822  -0.791  2.406   1.00 12.39 ? 85  TYR A CB  1 
ATOM   685  C  CG  . TYR A  1 85  ? 34.073  -0.249  1.176   1.00 10.42 ? 85  TYR A CG  1 
ATOM   686  C  CD1 . TYR A  1 85  ? 34.192  -0.861  -0.059  1.00 12.25 ? 85  TYR A CD1 1 
ATOM   687  C  CD2 . TYR A  1 85  ? 33.269  0.882   1.328   1.00 10.71 ? 85  TYR A CD2 1 
ATOM   688  C  CE1 . TYR A  1 85  ? 33.526  -0.296  -1.188  1.00 11.99 ? 85  TYR A CE1 1 
ATOM   689  C  CE2 . TYR A  1 85  ? 32.585  1.408   0.201   1.00 11.76 ? 85  TYR A CE2 1 
ATOM   690  C  CZ  . TYR A  1 85  ? 32.751  0.834   -1.011  1.00 13.28 ? 85  TYR A CZ  1 
ATOM   691  O  OH  . TYR A  1 85  ? 32.035  1.385   -2.102  1.00 18.39 ? 85  TYR A OH  1 
ATOM   692  N  N   . SER A  1 86  ? 37.279  0.547   4.482   1.00 11.42 ? 86  SER A N   1 
ATOM   693  C  CA  . SER A  1 86  ? 37.974  0.443   5.813   1.00 12.08 ? 86  SER A CA  1 
ATOM   694  C  C   . SER A  1 86  ? 36.986  0.684   6.910   1.00 12.96 ? 86  SER A C   1 
ATOM   695  O  O   . SER A  1 86  ? 36.069  1.457   6.763   1.00 12.43 ? 86  SER A O   1 
ATOM   696  C  CB  . SER A  1 86  ? 39.077  1.519   5.886   1.00 13.38 ? 86  SER A CB  1 
ATOM   697  O  OG  . SER A  1 86  ? 40.072  1.208   4.897   1.00 16.17 ? 86  SER A OG  1 
ATOM   698  N  N   . ALA A  1 87  ? 37.198  -0.022  8.021   1.00 12.87 ? 87  ALA A N   1 
ATOM   699  C  CA  . ALA A  1 87  ? 36.232  0.037   9.123   1.00 12.94 ? 87  ALA A CA  1 
ATOM   700  C  C   . ALA A  1 87  ? 36.286  1.379   9.796   1.00 12.09 ? 87  ALA A C   1 
ATOM   701  O  O   . ALA A  1 87  ? 37.382  2.040   9.843   1.00 13.83 ? 87  ALA A O   1 
ATOM   702  C  CB  . ALA A  1 87  ? 36.545  -1.010  10.178  1.00 13.17 ? 87  ALA A CB  1 
ATOM   703  N  N   . THR A  1 88  ? 35.159  1.813   10.354  1.00 11.63 ? 88  THR A N   1 
ATOM   704  C  CA  . THR A  1 88  ? 35.119  3.015   11.189  1.00 11.03 ? 88  THR A CA  1 
ATOM   705  C  C   . THR A  1 88  ? 34.471  2.745   12.572  1.00 12.53 ? 88  THR A C   1 
ATOM   706  O  O   . THR A  1 88  ? 34.934  3.297   13.529  1.00 13.30 ? 88  THR A O   1 
ATOM   707  C  CB  . THR A  1 88  ? 34.505  4.233   10.415  1.00 12.88 ? 88  THR A CB  1 
ATOM   708  O  OG1 . THR A  1 88  ? 34.383  5.380   11.268  1.00 15.83 ? 88  THR A OG1 1 
ATOM   709  C  CG2 . THR A  1 88  ? 33.080  3.953   9.930   1.00 14.46 ? 88  THR A CG2 1 
ATOM   710  N  N   . GLN A  1 89  ? 33.370  1.960   12.606  1.00 11.44 ? 89  GLN A N   1 
ATOM   711  C  CA  . GLN A  1 89  ? 32.725  1.703   13.907  1.00 12.11 ? 89  GLN A CA  1 
ATOM   712  C  C   . GLN A  1 89  ? 31.755  0.575   13.723  1.00 11.26 ? 89  GLN A C   1 
ATOM   713  O  O   . GLN A  1 89  ? 31.414  0.196   12.622  1.00 11.86 ? 89  GLN A O   1 
ATOM   714  C  CB  . GLN A  1 89  ? 31.963  2.914   14.466  1.00 14.44 ? 89  GLN A CB  1 
ATOM   715  C  CG  . GLN A  1 89  ? 30.958  3.509   13.454  1.00 15.16 ? 89  GLN A CG  1 
ATOM   716  C  CD  . GLN A  1 89  ? 29.569  3.327   13.936  1.00 15.56 ? 89  GLN A CD  1 
ATOM   717  O  OE1 . GLN A  1 89  ? 29.257  2.210   14.265  1.00 15.36 ? 89  GLN A OE1 1 
ATOM   718  N  NE2 . GLN A  1 89  ? 28.758  4.245   13.797  1.00 19.53 ? 89  GLN A NE2 1 
ATOM   719  N  N   . LEU A  1 90  ? 31.450  -0.063  14.848  1.00 11.46 ? 90  LEU A N   1 
ATOM   720  C  CA  . LEU A  1 90  ? 30.314  -0.961  14.938  1.00 10.10 ? 90  LEU A CA  1 
ATOM   721  C  C   . LEU A  1 90  ? 29.348  -0.547  15.971  1.00 9.88  ? 90  LEU A C   1 
ATOM   722  O  O   . LEU A  1 90  ? 29.681  0.160   16.906  1.00 10.75 ? 90  LEU A O   1 
ATOM   723  C  CB  . LEU A  1 90  ? 30.743  -2.437  14.984  1.00 10.88 ? 90  LEU A CB  1 
ATOM   724  C  CG  . LEU A  1 90  ? 31.565  -2.903  16.281  1.00 11.03 ? 90  LEU A CG  1 
ATOM   725  C  CD1 . LEU A  1 90  ? 30.675  -3.006  17.509  1.00 12.85 ? 90  LEU A CD1 1 
ATOM   726  C  CD2 . LEU A  1 90  ? 32.159  -4.284  15.911  1.00 12.47 ? 90  LEU A CD2 1 
ATOM   727  N  N   . HIS A  1 91  ? 28.099  -1.001  15.818  1.00 9.41  ? 91  HIS A N   1 
ATOM   728  C  CA  . HIS A  1 91  ? 27.057  -0.655  16.784  1.00 9.11  ? 91  HIS A CA  1 
ATOM   729  C  C   . HIS A  1 91  ? 25.857  -1.597  16.610  1.00 8.89  ? 91  HIS A C   1 
ATOM   730  O  O   . HIS A  1 91  ? 25.878  -2.488  15.718  1.00 9.69  ? 91  HIS A O   1 
ATOM   731  C  CB  . HIS A  1 91  ? 26.599  0.820   16.589  1.00 9.98  ? 91  HIS A CB  1 
ATOM   732  C  CG  . HIS A  1 91  ? 25.960  1.029   15.248  1.00 10.06 ? 91  HIS A CG  1 
ATOM   733  N  ND1 . HIS A  1 91  ? 26.671  1.441   14.201  1.00 9.73  ? 91  HIS A ND1 1 
ATOM   734  C  CD2 . HIS A  1 91  ? 24.687  0.750   14.817  1.00 10.76 ? 91  HIS A CD2 1 
ATOM   735  C  CE1 . HIS A  1 91  ? 25.847  1.434   13.070  1.00 9.59  ? 91  HIS A CE1 1 
ATOM   736  N  NE2 . HIS A  1 91  ? 24.634  1.021   13.465  1.00 8.79  ? 91  HIS A NE2 1 
ATOM   737  N  N   . LEU A  1 92  ? 24.886  -1.473  17.525  1.00 10.47 ? 92  LEU A N   1 
ATOM   738  C  CA  . LEU A  1 92  ? 23.770  -2.440  17.503  1.00 9.43  ? 92  LEU A CA  1 
ATOM   739  C  C   . LEU A  1 92  ? 22.423  -1.738  17.529  1.00 9.14  ? 92  LEU A C   1 
ATOM   740  O  O   . LEU A  1 92  ? 22.268  -0.581  17.866  1.00 10.47 ? 92  LEU A O   1 
ATOM   741  C  CB  . LEU A  1 92  ? 23.835  -3.347  18.788  1.00 13.18 ? 92  LEU A CB  1 
ATOM   742  C  CG  . LEU A  1 92  ? 25.037  -4.279  18.634  1.00 12.43 ? 92  LEU A CG  1 
ATOM   743  C  CD1 . LEU A  1 92  ? 26.049  -3.779  19.664  1.00 17.58 ? 92  LEU A CD1 1 
ATOM   744  C  CD2 . LEU A  1 92  ? 24.616  -5.685  18.830  1.00 16.23 ? 92  LEU A CD2 1 
ATOM   745  N  N   . HIS A  1 93  ? 21.413  -2.527  17.174  1.00 8.75  ? 93  HIS A N   1 
ATOM   746  C  CA  . HIS A  1 93  ? 19.945  -2.055  17.267  1.00 9.15  ? 93  HIS A CA  1 
ATOM   747  C  C   . HIS A  1 93  ? 19.184  -3.154  17.922  1.00 9.37  ? 93  HIS A C   1 
ATOM   748  O  O   . HIS A  1 93  ? 19.468  -4.357  17.654  1.00 10.13 ? 93  HIS A O   1 
ATOM   749  C  CB  . HIS A  1 93  ? 19.374  -1.881  15.808  1.00 9.18  ? 93  HIS A CB  1 
ATOM   750  C  CG  . HIS A  1 93  ? 20.127  -0.845  15.025  1.00 7.90  ? 93  HIS A CG  1 
ATOM   751  N  ND1 . HIS A  1 93  ? 19.818  0.494   15.049  1.00 8.73  ? 93  HIS A ND1 1 
ATOM   752  C  CD2 . HIS A  1 93  ? 21.203  -0.987  14.202  1.00 7.51  ? 93  HIS A CD2 1 
ATOM   753  C  CE1 . HIS A  1 93  ? 20.689  1.159   14.229  1.00 8.74  ? 93  HIS A CE1 1 
ATOM   754  N  NE2 . HIS A  1 93  ? 21.535  0.286   13.719  1.00 9.27  ? 93  HIS A NE2 1 
ATOM   755  N  N   . TRP A  1 94  ? 18.196  -2.795  18.717  1.00 9.06  ? 94  TRP A N   1 
ATOM   756  C  CA  . TRP A  1 94  ? 17.444  -3.839  19.437  1.00 9.35  ? 94  TRP A CA  1 
ATOM   757  C  C   . TRP A  1 94  ? 16.072  -3.325  19.806  1.00 10.08 ? 94  TRP A C   1 
ATOM   758  O  O   . TRP A  1 94  ? 15.743  -2.150  19.596  1.00 9.69  ? 94  TRP A O   1 
ATOM   759  C  CB  . TRP A  1 94  ? 18.150  -4.241  20.781  1.00 9.92  ? 94  TRP A CB  1 
ATOM   760  C  CG  . TRP A  1 94  ? 18.489  -3.079  21.677  1.00 11.04 ? 94  TRP A CG  1 
ATOM   761  C  CD1 . TRP A  1 94  ? 17.665  -2.547  22.679  1.00 11.99 ? 94  TRP A CD1 1 
ATOM   762  C  CD2 . TRP A  1 94  ? 19.700  -2.261  21.680  1.00 10.69 ? 94  TRP A CD2 1 
ATOM   763  N  NE1 . TRP A  1 94  ? 18.295  -1.484  23.322  1.00 12.35 ? 94  TRP A NE1 1 
ATOM   764  C  CE2 . TRP A  1 94  ? 19.565  -1.302  22.746  1.00 11.66 ? 94  TRP A CE2 1 
ATOM   765  C  CE3 . TRP A  1 94  ? 20.879  -2.237  20.886  1.00 11.34 ? 94  TRP A CE3 1 
ATOM   766  C  CZ2 . TRP A  1 94  ? 20.503  -0.336  22.987  1.00 10.87 ? 94  TRP A CZ2 1 
ATOM   767  C  CZ3 . TRP A  1 94  ? 21.861  -1.270  21.161  1.00 11.23 ? 94  TRP A CZ3 1 
ATOM   768  C  CH2 . TRP A  1 94  ? 21.679  -0.338  22.190  1.00 10.96 ? 94  TRP A CH2 1 
ATOM   769  N  N   . GLY A  1 95  ? 15.272  -4.235  20.362  1.00 9.09  ? 95  GLY A N   1 
ATOM   770  C  CA  . GLY A  1 95  ? 13.858  -3.894  20.744  1.00 10.60 ? 95  GLY A CA  1 
ATOM   771  C  C   . GLY A  1 95  ? 13.715  -3.596  22.243  1.00 9.65  ? 95  GLY A C   1 
ATOM   772  O  O   . GLY A  1 95  ? 14.385  -2.727  22.816  1.00 11.02 ? 95  GLY A O   1 
ATOM   773  N  N   . ASN A  1 96  ? 12.916  -4.453  22.921  1.00 11.06 ? 96  ASN A N   1 
ATOM   774  C  CA  . ASN A  1 96  ? 12.728  -4.208  24.400  1.00 12.25 ? 96  ASN A CA  1 
ATOM   775  C  C   . ASN A  1 96  ? 12.231  -5.519  25.001  1.00 14.38 ? 96  ASN A C   1 
ATOM   776  O  O   . ASN A  1 96  ? 11.786  -6.384  24.285  1.00 12.53 ? 96  ASN A O   1 
ATOM   777  C  CB  . ASN A  1 96  ? 11.778  -3.044  24.615  1.00 14.33 ? 96  ASN A CB  1 
ATOM   778  C  CG  . ASN A  1 96  ? 10.331  -3.406  24.302  1.00 15.98 ? 96  ASN A CG  1 
ATOM   779  O  OD1 . ASN A  1 96  ? 9.664   -3.967  25.242  1.00 20.23 ? 96  ASN A OD1 1 
ATOM   780  N  ND2 . ASN A  1 96  ? 9.828   -3.201  23.067  1.00 17.56 ? 96  ASN A ND2 1 
ATOM   781  N  N   . PRO A  1 97  ? 12.295  -5.663  26.334  1.00 13.18 ? 97  PRO A N   1 
ATOM   782  C  CA  . PRO A  1 97  ? 12.003  -6.984  26.826  1.00 15.09 ? 97  PRO A CA  1 
ATOM   783  C  C   . PRO A  1 97  ? 10.549  -7.426  26.621  1.00 14.18 ? 97  PRO A C   1 
ATOM   784  O  O   . PRO A  1 97  ? 10.325  -8.616  26.652  1.00 17.13 ? 97  PRO A O   1 
ATOM   785  C  CB  . PRO A  1 97  ? 12.296  -6.854  28.328  1.00 14.99 ? 97  PRO A CB  1 
ATOM   786  C  CG  . PRO A  1 97  ? 13.391  -5.810  28.378  1.00 14.43 ? 97  PRO A CG  1 
ATOM   787  C  CD  . PRO A  1 97  ? 12.969  -4.801  27.336  1.00 15.63 ? 97  PRO A CD  1 
ATOM   788  N  N   . ASN A  1 98  ? 9.609   -6.525  26.474  1.00 15.25 ? 98  ASN A N   1 
ATOM   789  C  CA  . ASN A  1 98  ? 8.212   -6.916  26.165  1.00 17.67 ? 98  ASN A CA  1 
ATOM   790  C  C   . ASN A  1 98  ? 7.942   -7.284  24.719  1.00 17.23 ? 98  ASN A C   1 
ATOM   791  O  O   . ASN A  1 98  ? 6.938   -7.927  24.338  1.00 19.63 ? 98  ASN A O   1 
ATOM   792  C  CB  . ASN A  1 98  ? 7.270   -5.752  26.539  1.00 18.99 ? 98  ASN A CB  1 
ATOM   793  C  CG  . ASN A  1 98  ? 7.232   -5.507  28.027  1.00 26.16 ? 98  ASN A CG  1 
ATOM   794  O  OD1 . ASN A  1 98  ? 7.223   -6.434  28.825  1.00 28.71 ? 98  ASN A OD1 1 
ATOM   795  N  ND2 . ASN A  1 98  ? 7.095   -4.270  28.396  1.00 32.28 ? 98  ASN A ND2 1 
ATOM   796  N  N   . ASP A  1 99  ? 8.870   -6.874  23.840  1.00 14.27 ? 99  ASP A N   1 
ATOM   797  C  CA  . ASP A  1 99  ? 8.790   -7.135  22.424  1.00 14.89 ? 99  ASP A CA  1 
ATOM   798  C  C   . ASP A  1 99  ? 10.237  -7.240  21.851  1.00 12.27 ? 99  ASP A C   1 
ATOM   799  O  O   . ASP A  1 99  ? 10.764  -6.297  21.238  1.00 13.62 ? 99  ASP A O   1 
ATOM   800  C  CB  . ASP A  1 99  ? 7.997   -6.049  21.698  1.00 14.65 ? 99  ASP A CB  1 
ATOM   801  C  CG  . ASP A  1 99  ? 7.428   -6.530  20.375  1.00 17.80 ? 99  ASP A CG  1 
ATOM   802  O  OD1 . ASP A  1 99  ? 7.806   -7.635  19.929  1.00 18.38 ? 99  ASP A OD1 1 
ATOM   803  O  OD2 . ASP A  1 99  ? 6.603   -5.806  19.780  1.00 22.40 ? 99  ASP A OD2 1 
ATOM   804  N  N   . PRO A  1 100 ? 10.905  -8.370  22.064  1.00 12.08 ? 100 PRO A N   1 
ATOM   805  C  CA  . PRO A  1 100 ? 12.366  -8.455  21.921  1.00 13.26 ? 100 PRO A CA  1 
ATOM   806  C  C   . PRO A  1 100 ? 12.708  -8.823  20.490  1.00 13.36 ? 100 PRO A C   1 
ATOM   807  O  O   . PRO A  1 100 ? 13.304  -9.872  20.168  1.00 14.03 ? 100 PRO A O   1 
ATOM   808  C  CB  . PRO A  1 100 ? 12.751  -9.563  22.912  1.00 13.88 ? 100 PRO A CB  1 
ATOM   809  C  CG  . PRO A  1 100 ? 11.557  -10.472 22.918  1.00 13.96 ? 100 PRO A CG  1 
ATOM   810  C  CD  . PRO A  1 100 ? 10.392  -9.530  22.854  1.00 13.89 ? 100 PRO A CD  1 
ATOM   811  N  N   . HIS A  1 101 ? 12.258  -7.969  19.588  1.00 12.84 ? 101 HIS A N   1 
ATOM   812  C  CA  . HIS A  1 101 ? 12.403  -8.186  18.088  1.00 13.53 ? 101 HIS A CA  1 
ATOM   813  C  C   . HIS A  1 101 ? 12.711  -6.978  17.378  1.00 13.39 ? 101 HIS A C   1 
ATOM   814  O  O   . HIS A  1 101 ? 11.884  -6.443  16.603  1.00 18.56 ? 101 HIS A O   1 
ATOM   815  C  CB  . HIS A  1 101 ? 11.103  -8.767  17.523  1.00 16.27 ? 101 HIS A CB  1 
ATOM   816  C  CG  . HIS A  1 101 ? 10.531  -9.888  18.341  1.00 18.00 ? 101 HIS A CG  1 
ATOM   817  N  ND1 . HIS A  1 101 ? 10.940  -11.160 18.203  1.00 20.30 ? 101 HIS A ND1 1 
ATOM   818  C  CD2 . HIS A  1 101 ? 9.547   -9.894  19.324  1.00 16.25 ? 101 HIS A CD2 1 
ATOM   819  C  CE1 . HIS A  1 101 ? 10.259  -11.944 19.055  1.00 16.87 ? 101 HIS A CE1 1 
ATOM   820  N  NE2 . HIS A  1 101 ? 9.410   -11.166 19.746  1.00 21.89 ? 101 HIS A NE2 1 
ATOM   821  N  N   . GLY A  1 102 ? 13.898  -6.503  17.636  1.00 11.03 ? 102 GLY A N   1 
ATOM   822  C  CA  . GLY A  1 102 ? 14.336  -5.203  17.189  1.00 11.20 ? 102 GLY A CA  1 
ATOM   823  C  C   . GLY A  1 102 ? 15.456  -5.121  16.154  1.00 11.16 ? 102 GLY A C   1 
ATOM   824  O  O   . GLY A  1 102 ? 16.173  -4.128  16.074  1.00 10.32 ? 102 GLY A O   1 
ATOM   825  N  N   . SER A  1 103 ? 15.629  -6.144  15.328  1.00 10.61 ? 103 SER A N   1 
ATOM   826  C  CA  . SER A  1 103 ? 16.424  -5.969  14.137  1.00 9.85  ? 103 SER A CA  1 
ATOM   827  C  C   . SER A  1 103 ? 15.858  -4.879  13.209  1.00 10.68 ? 103 SER A C   1 
ATOM   828  O  O   . SER A  1 103 ? 14.676  -4.530  13.320  1.00 12.40 ? 103 SER A O   1 
ATOM   829  C  CB  . SER A  1 103 ? 16.614  -7.284  13.384  1.00 10.75 ? 103 SER A CB  1 
ATOM   830  O  OG  . SER A  1 103 ? 15.386  -7.697  12.750  1.00 10.50 ? 103 SER A OG  1 
ATOM   831  N  N   . GLU A  1 104 ? 16.719  -4.362  12.367  1.00 9.27  ? 104 GLU A N   1 
ATOM   832  C  CA  . GLU A  1 104 ? 16.250  -3.377  11.390  1.00 9.10  ? 104 GLU A CA  1 
ATOM   833  C  C   . GLU A  1 104 ? 15.801  -4.060  10.139  1.00 9.46  ? 104 GLU A C   1 
ATOM   834  O  O   . GLU A  1 104 ? 14.632  -3.882  9.707   1.00 9.22  ? 104 GLU A O   1 
ATOM   835  C  CB  . GLU A  1 104 ? 17.429  -2.415  11.058  1.00 9.60  ? 104 GLU A CB  1 
ATOM   836  C  CG  . GLU A  1 104 ? 17.989  -1.733  12.314  1.00 9.14  ? 104 GLU A CG  1 
ATOM   837  C  CD  . GLU A  1 104 ? 18.309  -0.293  11.999  1.00 9.82  ? 104 GLU A CD  1 
ATOM   838  O  OE1 . GLU A  1 104 ? 19.363  -0.067  11.408  1.00 10.12 ? 104 GLU A OE1 1 
ATOM   839  O  OE2 . GLU A  1 104 ? 17.430  0.587   12.251  1.00 11.74 ? 104 GLU A OE2 1 
ATOM   840  N  N   . HIS A  1 105 ? 16.635  -4.867  9.516   1.00 8.51  ? 105 HIS A N   1 
ATOM   841  C  CA  . HIS A  1 105 ? 16.125  -5.719  8.383   1.00 8.84  ? 105 HIS A CA  1 
ATOM   842  C  C   . HIS A  1 105 ? 15.236  -6.794  8.914   1.00 9.15  ? 105 HIS A C   1 
ATOM   843  O  O   . HIS A  1 105 ? 15.424  -7.269  10.080  1.00 9.72  ? 105 HIS A O   1 
ATOM   844  C  CB  . HIS A  1 105 ? 17.305  -6.321  7.629   1.00 9.29  ? 105 HIS A CB  1 
ATOM   845  C  CG  . HIS A  1 105 ? 18.093  -5.229  6.899   1.00 8.71  ? 105 HIS A CG  1 
ATOM   846  N  ND1 . HIS A  1 105 ? 19.125  -4.538  7.485   1.00 9.19  ? 105 HIS A ND1 1 
ATOM   847  C  CD2 . HIS A  1 105 ? 17.949  -4.718  5.629   1.00 9.64  ? 105 HIS A CD2 1 
ATOM   848  C  CE1 . HIS A  1 105 ? 19.560  -3.609  6.639   1.00 9.02  ? 105 HIS A CE1 1 
ATOM   849  N  NE2 . HIS A  1 105 ? 18.830  -3.717  5.493   1.00 10.32 ? 105 HIS A NE2 1 
ATOM   850  N  N   . THR A  1 106 ? 14.266  -7.197  8.096   1.00 8.98  ? 106 THR A N   1 
ATOM   851  C  CA  . THR A  1 106 ? 13.404  -8.360  8.396   1.00 9.61  ? 106 THR A CA  1 
ATOM   852  C  C   . THR A  1 106 ? 13.589  -9.326  7.274   1.00 9.93  ? 106 THR A C   1 
ATOM   853  O  O   . THR A  1 106 ? 14.003  -9.028  6.182   1.00 10.57 ? 106 THR A O   1 
ATOM   854  C  CB  . THR A  1 106 ? 11.935  -7.933  8.569   1.00 10.28 ? 106 THR A CB  1 
ATOM   855  O  OG1 . THR A  1 106 ? 11.532  -7.280  7.342   1.00 11.45 ? 106 THR A OG1 1 
ATOM   856  C  CG2 . THR A  1 106 ? 11.787  -6.926  9.677   1.00 10.88 ? 106 THR A CG2 1 
ATOM   857  N  N   . VAL A  1 107 ? 13.242  -10.612 7.569   1.00 10.06 ? 107 VAL A N   1 
ATOM   858  C  CA  . VAL A  1 107 ? 13.339  -11.670 6.537   1.00 11.03 ? 107 VAL A CA  1 
ATOM   859  C  C   . VAL A  1 107 ? 11.944  -12.352 6.452   1.00 12.20 ? 107 VAL A C   1 
ATOM   860  O  O   . VAL A  1 107 ? 11.420  -12.804 7.486   1.00 12.67 ? 107 VAL A O   1 
ATOM   861  C  CB  . VAL A  1 107 ? 14.412  -12.728 6.897   1.00 12.70 ? 107 VAL A CB  1 
ATOM   862  C  CG1 . VAL A  1 107 ? 14.395  -13.892 5.930   1.00 13.42 ? 107 VAL A CG1 1 
ATOM   863  C  CG2 . VAL A  1 107 ? 15.831  -12.109 6.962   1.00 14.22 ? 107 VAL A CG2 1 
ATOM   864  N  N   . SER A  1 108 ? 11.323  -12.229 5.285   1.00 12.58 ? 108 SER A N   1 
ATOM   865  C  CA  . SER A  1 108 ? 9.933   -12.745 5.089   1.00 13.95 ? 108 SER A CA  1 
ATOM   866  C  C   . SER A  1 108 ? 9.063   -12.161 6.152   1.00 14.11 ? 108 SER A C   1 
ATOM   867  O  O   . SER A  1 108 ? 8.186   -12.824 6.730   1.00 14.80 ? 108 SER A O   1 
ATOM   868  C  CB  . SER A  1 108 ? 9.903   -14.269 5.155   1.00 14.71 ? 108 SER A CB  1 
ATOM   869  O  OG  . SER A  1 108 ? 10.777  -14.777 4.157   1.00 19.58 ? 108 SER A OG  1 
ATOM   870  N  N   . GLY A  1 109 ? 9.283   -10.882 6.457   1.00 12.69 ? 109 GLY A N   1 
ATOM   871  C  CA  . GLY A  1 109 ? 8.361   -10.132 7.332   1.00 12.53 ? 109 GLY A CA  1 
ATOM   872  C  C   . GLY A  1 109 ? 8.699   -10.237 8.830   1.00 13.79 ? 109 GLY A C   1 
ATOM   873  O  O   . GLY A  1 109 ? 8.127   -9.545  9.659   1.00 16.36 ? 109 GLY A O   1 
ATOM   874  N  N   . GLN A  1 110 ? 9.676   -11.080 9.160   1.00 12.45 ? 110 GLN A N   1 
ATOM   875  C  CA  . GLN A  1 110 ? 10.058  -11.327 10.539  1.00 12.79 ? 110 GLN A CA  1 
ATOM   876  C  C   . GLN A  1 110 ? 11.302  -10.581 11.062  1.00 10.58 ? 110 GLN A C   1 
ATOM   877  O  O   . GLN A  1 110 ? 12.283  -10.588 10.377  1.00 10.39 ? 110 GLN A O   1 
ATOM   878  C  CB  . GLN A  1 110 ? 10.358  -12.804 10.736  1.00 12.51 ? 110 GLN A CB  1 
ATOM   879  C  CG  . GLN A  1 110 ? 9.218   -13.712 10.175  1.00 15.08 ? 110 GLN A CG  1 
ATOM   880  C  CD  . GLN A  1 110 ? 7.829   -13.302 10.632  1.00 15.43 ? 110 GLN A CD  1 
ATOM   881  O  OE1 . GLN A  1 110 ? 7.533   -13.223 11.853  1.00 17.54 ? 110 GLN A OE1 1 
ATOM   882  N  NE2 . GLN A  1 110 ? 6.976   -12.978 9.634   1.00 19.57 ? 110 GLN A NE2 1 
ATOM   883  N  N   . HIS A  1 111 ? 11.184  -9.937  12.205  1.00 12.06 ? 111 HIS A N   1 
ATOM   884  C  CA  . HIS A  1 111 ? 12.314  -9.360  12.844  1.00 12.09 ? 111 HIS A CA  1 
ATOM   885  C  C   . HIS A  1 111 ? 13.088  -10.403 13.584  1.00 13.45 ? 111 HIS A C   1 
ATOM   886  O  O   . HIS A  1 111 ? 12.535  -11.401 14.084  1.00 16.88 ? 111 HIS A O   1 
ATOM   887  C  CB  . HIS A  1 111 ? 11.941  -8.383  13.935  1.00 13.17 ? 111 HIS A CB  1 
ATOM   888  C  CG  . HIS A  1 111 ? 11.491  -7.065  13.411  1.00 12.51 ? 111 HIS A CG  1 
ATOM   889  N  ND1 . HIS A  1 111 ? 10.224  -6.733  13.001  1.00 17.63 ? 111 HIS A ND1 1 
ATOM   890  C  CD2 . HIS A  1 111 ? 12.256  -5.985  13.237  1.00 12.36 ? 111 HIS A CD2 1 
ATOM   891  C  CE1 . HIS A  1 111 ? 10.231  -5.464  12.574  1.00 16.49 ? 111 HIS A CE1 1 
ATOM   892  N  NE2 . HIS A  1 111 ? 11.504  -5.004  12.717  1.00 16.74 ? 111 HIS A NE2 1 
ATOM   893  N  N   . PHE A  1 112 ? 14.369  -10.235 13.622  1.00 11.14 ? 112 PHE A N   1 
ATOM   894  C  CA  . PHE A  1 112 ? 15.236  -10.917 14.560  1.00 11.09 ? 112 PHE A CA  1 
ATOM   895  C  C   . PHE A  1 112 ? 15.354  -10.098 15.835  1.00 10.98 ? 112 PHE A C   1 
ATOM   896  O  O   . PHE A  1 112 ? 14.795  -8.943  15.929  1.00 11.55 ? 112 PHE A O   1 
ATOM   897  C  CB  . PHE A  1 112 ? 16.626  -11.163 13.967  1.00 11.82 ? 112 PHE A CB  1 
ATOM   898  C  CG  . PHE A  1 112 ? 16.603  -12.226 12.906  1.00 13.75 ? 112 PHE A CG  1 
ATOM   899  C  CD1 . PHE A  1 112 ? 16.022  -11.986 11.605  1.00 15.40 ? 112 PHE A CD1 1 
ATOM   900  C  CD2 . PHE A  1 112 ? 17.056  -13.555 13.232  1.00 16.06 ? 112 PHE A CD2 1 
ATOM   901  C  CE1 . PHE A  1 112 ? 15.938  -13.062 10.697  1.00 18.44 ? 112 PHE A CE1 1 
ATOM   902  C  CE2 . PHE A  1 112 ? 16.983  -14.556 12.272  1.00 18.29 ? 112 PHE A CE2 1 
ATOM   903  C  CZ  . PHE A  1 112 ? 16.444  -14.310 11.041  1.00 18.66 ? 112 PHE A CZ  1 
ATOM   904  N  N   . ALA A  1 113 ? 15.948  -10.658 16.908  1.00 10.42 ? 113 ALA A N   1 
ATOM   905  C  CA  . ALA A  1 113 ? 15.979  -9.963  18.163  1.00 11.13 ? 113 ALA A CA  1 
ATOM   906  C  C   . ALA A  1 113 ? 16.730  -8.656  18.091  1.00 10.14 ? 113 ALA A C   1 
ATOM   907  O  O   . ALA A  1 113 ? 16.412  -7.699  18.761  1.00 11.32 ? 113 ALA A O   1 
ATOM   908  C  CB  . ALA A  1 113 ? 16.579  -10.897 19.259  1.00 12.32 ? 113 ALA A CB  1 
ATOM   909  N  N   . ALA A  1 114 ? 17.838  -8.680  17.358  1.00 10.04 ? 114 ALA A N   1 
ATOM   910  C  CA  . ALA A  1 114 ? 18.737  -7.513  17.310  1.00 8.82  ? 114 ALA A CA  1 
ATOM   911  C  C   . ALA A  1 114 ? 19.559  -7.565  16.050  1.00 8.67  ? 114 ALA A C   1 
ATOM   912  O  O   . ALA A  1 114 ? 19.472  -8.569  15.296  1.00 9.44  ? 114 ALA A O   1 
ATOM   913  C  CB  . ALA A  1 114 ? 19.599  -7.498  18.595  1.00 11.86 ? 114 ALA A CB  1 
ATOM   914  N  N   . GLU A  1 115 ? 20.345  -6.489  15.838  1.00 9.31  ? 115 GLU A N   1 
ATOM   915  C  CA  . GLU A  1 115 ? 21.162  -6.474  14.596  1.00 9.78  ? 115 GLU A CA  1 
ATOM   916  C  C   . GLU A  1 115 ? 22.432  -5.737  14.864  1.00 9.62  ? 115 GLU A C   1 
ATOM   917  O  O   . GLU A  1 115 ? 22.386  -4.652  15.499  1.00 10.26 ? 115 GLU A O   1 
ATOM   918  C  CB  . GLU A  1 115 ? 20.331  -5.846  13.487  1.00 9.84  ? 115 GLU A CB  1 
ATOM   919  C  CG  . GLU A  1 115 ? 20.975  -5.897  12.078  1.00 10.15 ? 115 GLU A CG  1 
ATOM   920  C  CD  . GLU A  1 115 ? 20.013  -5.487  10.994  1.00 11.10 ? 115 GLU A CD  1 
ATOM   921  O  OE1 . GLU A  1 115 ? 18.833  -5.800  11.121  1.00 9.57  ? 115 GLU A OE1 1 
ATOM   922  O  OE2 . GLU A  1 115 ? 20.479  -4.933  9.972   1.00 9.65  ? 115 GLU A OE2 1 
ATOM   923  N  N   . LEU A  1 116 ? 23.576  -6.281  14.440  1.00 8.48  ? 116 LEU A N   1 
ATOM   924  C  CA  . LEU A  1 116 ? 24.918  -5.634  14.545  1.00 8.48  ? 116 LEU A CA  1 
ATOM   925  C  C   . LEU A  1 116 ? 25.236  -5.046  13.165  1.00 8.05  ? 116 LEU A C   1 
ATOM   926  O  O   . LEU A  1 116 ? 25.060  -5.706  12.156  1.00 8.58  ? 116 LEU A O   1 
ATOM   927  C  CB  . LEU A  1 116 ? 25.970  -6.729  14.939  1.00 9.64  ? 116 LEU A CB  1 
ATOM   928  C  CG  . LEU A  1 116 ? 27.434  -6.224  14.782  1.00 10.28 ? 116 LEU A CG  1 
ATOM   929  C  CD1 . LEU A  1 116 ? 27.778  -5.303  15.904  1.00 13.41 ? 116 LEU A CD1 1 
ATOM   930  C  CD2 . LEU A  1 116 ? 28.358  -7.472  14.749  1.00 11.01 ? 116 LEU A CD2 1 
ATOM   931  N  N   . HIS A  1 117 ? 25.744  -3.827  13.161  1.00 7.60  ? 117 HIS A N   1 
ATOM   932  C  CA  . HIS A  1 117 ? 26.259  -3.125  11.956  1.00 7.98  ? 117 HIS A CA  1 
ATOM   933  C  C   . HIS A  1 117 ? 27.672  -2.800  12.059  1.00 8.97  ? 117 HIS A C   1 
ATOM   934  O  O   . HIS A  1 117 ? 28.095  -2.228  13.074  1.00 9.57  ? 117 HIS A O   1 
ATOM   935  C  CB  . HIS A  1 117 ? 25.479  -1.862  11.734  1.00 8.47  ? 117 HIS A CB  1 
ATOM   936  C  CG  . HIS A  1 117 ? 24.100  -2.130  11.339  1.00 6.97  ? 117 HIS A CG  1 
ATOM   937  N  ND1 . HIS A  1 117 ? 23.087  -1.179  11.483  1.00 7.84  ? 117 HIS A ND1 1 
ATOM   938  C  CD2 . HIS A  1 117 ? 23.531  -3.224  10.805  1.00 7.61  ? 117 HIS A CD2 1 
ATOM   939  C  CE1 . HIS A  1 117 ? 21.931  -1.715  10.971  1.00 7.72  ? 117 HIS A CE1 1 
ATOM   940  N  NE2 . HIS A  1 117 ? 22.179  -2.949  10.577  1.00 8.09  ? 117 HIS A NE2 1 
ATOM   941  N  N   . ILE A  1 118 ? 28.502  -3.312  11.151  1.00 9.60  ? 118 ILE A N   1 
ATOM   942  C  CA  . ILE A  1 118 ? 29.962  -2.959  11.123  1.00 8.92  ? 118 ILE A CA  1 
ATOM   943  C  C   . ILE A  1 118 ? 30.111  -2.004  9.935   1.00 9.12  ? 118 ILE A C   1 
ATOM   944  O  O   . ILE A  1 118 ? 29.909  -2.413  8.750   1.00 9.52  ? 118 ILE A O   1 
ATOM   945  C  CB  . ILE A  1 118 ? 30.830  -4.235  10.970  1.00 10.31 ? 118 ILE A CB  1 
ATOM   946  C  CG1 . ILE A  1 118 ? 30.473  -5.297  12.012  1.00 10.81 ? 118 ILE A CG1 1 
ATOM   947  C  CG2 . ILE A  1 118 ? 32.302  -3.787  11.182  1.00 11.31 ? 118 ILE A CG2 1 
ATOM   948  C  CD1 . ILE A  1 118 ? 31.290  -6.567  11.887  1.00 12.52 ? 118 ILE A CD1 1 
ATOM   949  N  N   . VAL A  1 119 ? 30.392  -0.784  10.238  1.00 9.41  ? 119 VAL A N   1 
ATOM   950  C  CA  . VAL A  1 119 ? 30.326  0.347   9.245   1.00 10.35 ? 119 VAL A CA  1 
ATOM   951  C  C   . VAL A  1 119 ? 31.717  0.503   8.666   1.00 11.38 ? 119 VAL A C   1 
ATOM   952  O  O   . VAL A  1 119 ? 32.703  0.668   9.439   1.00 11.45 ? 119 VAL A O   1 
ATOM   953  C  CB  . VAL A  1 119 ? 29.881  1.657   9.921   1.00 10.27 ? 119 VAL A CB  1 
ATOM   954  C  CG1 . VAL A  1 119 ? 29.737  2.774   8.868   1.00 11.21 ? 119 VAL A CG1 1 
ATOM   955  C  CG2 . VAL A  1 119 ? 28.542  1.415   10.692  1.00 10.74 ? 119 VAL A CG2 1 
ATOM   956  N  N   . HIS A  1 120 ? 31.784  0.594   7.346   1.00 11.25 ? 120 HIS A N   1 
ATOM   957  C  CA  . HIS A  1 120 ? 33.089  0.835   6.614   1.00 10.44 ? 120 HIS A CA  1 
ATOM   958  C  C   . HIS A  1 120 ? 32.883  1.956   5.626   1.00 10.50 ? 120 HIS A C   1 
ATOM   959  O  O   . HIS A  1 120 ? 31.740  2.280   5.199   1.00 11.51 ? 120 HIS A O   1 
ATOM   960  C  CB  . HIS A  1 120 ? 33.489  -0.375  5.814   1.00 10.34 ? 120 HIS A CB  1 
ATOM   961  C  CG  . HIS A  1 120 ? 33.632  -1.677  6.596   1.00 11.01 ? 120 HIS A CG  1 
ATOM   962  N  ND1 . HIS A  1 120 ? 32.559  -2.371  7.199   1.00 10.43 ? 120 HIS A ND1 1 
ATOM   963  C  CD2 . HIS A  1 120 ? 34.783  -2.422  6.903   1.00 10.86 ? 120 HIS A CD2 1 
ATOM   964  C  CE1 . HIS A  1 120 ? 33.040  -3.502  7.792   1.00 10.53 ? 120 HIS A CE1 1 
ATOM   965  N  NE2 . HIS A  1 120 ? 34.378  -3.586  7.619   1.00 11.27 ? 120 HIS A NE2 1 
ATOM   966  N  N   . TYR A  1 121 ? 33.996  2.625   5.257   1.00 10.97 ? 121 TYR A N   1 
ATOM   967  C  CA  . TYR A  1 121 ? 33.951  3.666   4.218   1.00 11.24 ? 121 TYR A CA  1 
ATOM   968  C  C   . TYR A  1 121 ? 34.968  3.374   3.119   1.00 12.58 ? 121 TYR A C   1 
ATOM   969  O  O   . TYR A  1 121 ? 35.992  2.697   3.365   1.00 11.44 ? 121 TYR A O   1 
ATOM   970  C  CB  . TYR A  1 121 ? 34.226  5.058   4.822   1.00 13.33 ? 121 TYR A CB  1 
ATOM   971  C  CG  . TYR A  1 121 ? 35.664  5.272   5.348   1.00 14.32 ? 121 TYR A CG  1 
ATOM   972  C  CD1 . TYR A  1 121 ? 36.059  4.703   6.580   1.00 15.26 ? 121 TYR A CD1 1 
ATOM   973  C  CD2 . TYR A  1 121 ? 36.598  5.972   4.563   1.00 15.81 ? 121 TYR A CD2 1 
ATOM   974  C  CE1 . TYR A  1 121 ? 37.379  4.812   7.032   1.00 17.21 ? 121 TYR A CE1 1 
ATOM   975  C  CE2 . TYR A  1 121 ? 37.975  6.053   5.042   1.00 15.78 ? 121 TYR A CE2 1 
ATOM   976  C  CZ  . TYR A  1 121 ? 38.259  5.551   6.283   1.00 17.37 ? 121 TYR A CZ  1 
ATOM   977  O  OH  . TYR A  1 121 ? 39.574  5.664   6.779   1.00 19.60 ? 121 TYR A OH  1 
ATOM   978  N  N   . ASN A  1 122 ? 34.738  3.989   1.949   1.00 12.27 ? 122 ASN A N   1 
ATOM   979  C  CA  . ASN A  1 122 ? 35.584  3.767   0.760   1.00 12.70 ? 122 ASN A CA  1 
ATOM   980  C  C   . ASN A  1 122 ? 36.841  4.630   0.974   1.00 13.49 ? 122 ASN A C   1 
ATOM   981  O  O   . ASN A  1 122 ? 36.887  5.804   0.650   1.00 12.44 ? 122 ASN A O   1 
ATOM   982  C  CB  . ASN A  1 122 ? 34.845  4.262   -0.474  1.00 12.23 ? 122 ASN A CB  1 
ATOM   983  C  CG  . ASN A  1 122 ? 35.521  3.831   -1.715  1.00 13.71 ? 122 ASN A CG  1 
ATOM   984  O  OD1 . ASN A  1 122 ? 36.782  3.714   -1.732  1.00 13.18 ? 122 ASN A OD1 1 
ATOM   985  N  ND2 . ASN A  1 122 ? 34.738  3.465   -2.785  1.00 15.11 ? 122 ASN A ND2 1 
ATOM   986  N  N   . SER A  1 123 ? 37.900  3.977   1.455   1.00 11.71 ? 123 SER A N   1 
ATOM   987  C  CA  . SER A  1 123 ? 39.124  4.665   1.745   1.00 13.42 ? 123 SER A CA  1 
ATOM   988  C  C   . SER A  1 123 ? 39.985  4.760   0.456   1.00 13.92 ? 123 SER A C   1 
ATOM   989  O  O   . SER A  1 123 ? 40.975  5.547   0.534   1.00 15.99 ? 123 SER A O   1 
ATOM   990  C  CB  . SER A  1 123 ? 39.904  3.833   2.832   1.00 12.91 ? 123 SER A CB  1 
ATOM   991  O  OG  . SER A  1 123 ? 39.920  2.463   2.501   1.00 14.22 ? 123 SER A OG  1 
ATOM   992  N  N   . ASP A  1 124 ? 39.658  4.073   -0.626  1.00 14.15 ? 124 ASP A N   1 
ATOM   993  C  CA  . ASP A  1 124 ? 40.430  4.325   -1.870  1.00 14.69 ? 124 ASP A CA  1 
ATOM   994  C  C   . ASP A  1 124 ? 39.971  5.664   -2.442  1.00 19.01 ? 124 ASP A C   1 
ATOM   995  O  O   . ASP A  1 124 ? 40.771  6.367   -3.091  1.00 20.60 ? 124 ASP A O   1 
ATOM   996  C  CB  . ASP A  1 124 ? 40.092  3.252   -2.893  1.00 14.36 ? 124 ASP A CB  1 
ATOM   997  C  CG  . ASP A  1 124 ? 40.757  1.934   -2.593  1.00 14.17 ? 124 ASP A CG  1 
ATOM   998  O  OD1 . ASP A  1 124 ? 41.753  1.924   -1.838  1.00 15.88 ? 124 ASP A OD1 1 
ATOM   999  O  OD2 . ASP A  1 124 ? 40.278  0.905   -3.114  1.00 15.05 ? 124 ASP A OD2 1 
ATOM   1000 N  N   . LEU A  1 125 ? 38.723  6.051   -2.247  1.00 15.08 ? 125 LEU A N   1 
ATOM   1001 C  CA  . LEU A  1 125 ? 38.209  7.314   -2.868  1.00 16.80 ? 125 LEU A CA  1 
ATOM   1002 C  C   . LEU A  1 125 ? 38.228  8.468   -1.896  1.00 16.68 ? 125 LEU A C   1 
ATOM   1003 O  O   . LEU A  1 125 ? 38.288  9.648   -2.345  1.00 22.22 ? 125 LEU A O   1 
ATOM   1004 C  CB  . LEU A  1 125 ? 36.789  7.107   -3.463  1.00 16.98 ? 125 LEU A CB  1 
ATOM   1005 C  CG  . LEU A  1 125 ? 36.721  5.995   -4.509  1.00 20.25 ? 125 LEU A CG  1 
ATOM   1006 C  CD1 . LEU A  1 125 ? 35.308  5.906   -5.093  1.00 19.28 ? 125 LEU A CD1 1 
ATOM   1007 C  CD2 . LEU A  1 125 ? 37.762  6.288   -5.632  1.00 25.79 ? 125 LEU A CD2 1 
ATOM   1008 N  N   . TYR A  1 126 ? 38.124  8.209   -0.558  1.00 15.50 ? 126 TYR A N   1 
ATOM   1009 C  CA  . TYR A  1 126 ? 37.851  9.265   0.416   1.00 16.89 ? 126 TYR A CA  1 
ATOM   1010 C  C   . TYR A  1 126 ? 38.739  9.137   1.635   1.00 19.94 ? 126 TYR A C   1 
ATOM   1011 O  O   . TYR A  1 126 ? 39.206  8.024   1.988   1.00 19.03 ? 126 TYR A O   1 
ATOM   1012 C  CB  . TYR A  1 126 ? 36.333  9.255   0.885   1.00 16.80 ? 126 TYR A CB  1 
ATOM   1013 C  CG  . TYR A  1 126 ? 35.426  9.284   -0.263  1.00 17.19 ? 126 TYR A CG  1 
ATOM   1014 C  CD1 . TYR A  1 126 ? 35.391  10.401  -1.140  1.00 19.62 ? 126 TYR A CD1 1 
ATOM   1015 C  CD2 . TYR A  1 126 ? 34.625  8.158   -0.557  1.00 19.20 ? 126 TYR A CD2 1 
ATOM   1016 C  CE1 . TYR A  1 126 ? 34.564  10.350  -2.235  1.00 19.61 ? 126 TYR A CE1 1 
ATOM   1017 C  CE2 . TYR A  1 126 ? 33.800  8.093   -1.696  1.00 19.29 ? 126 TYR A CE2 1 
ATOM   1018 C  CZ  . TYR A  1 126 ? 33.783  9.208   -2.541  1.00 18.77 ? 126 TYR A CZ  1 
ATOM   1019 O  OH  . TYR A  1 126 ? 32.959  9.188   -3.713  1.00 21.24 ? 126 TYR A OH  1 
ATOM   1020 N  N   . PRO A  1 127 ? 39.001  10.259  2.300   1.00 20.07 ? 127 PRO A N   1 
ATOM   1021 C  CA  . PRO A  1 127 ? 40.027  10.212  3.355   1.00 19.88 ? 127 PRO A CA  1 
ATOM   1022 C  C   . PRO A  1 127 ? 39.597  9.705   4.717   1.00 20.95 ? 127 PRO A C   1 
ATOM   1023 O  O   . PRO A  1 127 ? 40.425  9.233   5.530   1.00 24.18 ? 127 PRO A O   1 
ATOM   1024 C  CB  . PRO A  1 127 ? 40.478  11.674  3.488   1.00 22.07 ? 127 PRO A CB  1 
ATOM   1025 C  CG  . PRO A  1 127 ? 39.284  12.458  3.036   1.00 20.28 ? 127 PRO A CG  1 
ATOM   1026 C  CD  . PRO A  1 127 ? 38.738  11.651  1.879   1.00 22.38 ? 127 PRO A CD  1 
ATOM   1027 N  N   . ASP A  1 128 ? 38.287  9.774   4.975   1.00 19.67 ? 128 ASP A N   1 
ATOM   1028 C  CA  . ASP A  1 128 ? 37.732  9.375   6.249   1.00 18.66 ? 128 ASP A CA  1 
ATOM   1029 C  C   . ASP A  1 128 ? 36.206  9.163   6.094   1.00 16.95 ? 128 ASP A C   1 
ATOM   1030 O  O   . ASP A  1 128 ? 35.649  9.476   5.026   1.00 18.48 ? 128 ASP A O   1 
ATOM   1031 C  CB  . ASP A  1 128 ? 38.014  10.406  7.323   1.00 22.89 ? 128 ASP A CB  1 
ATOM   1032 C  CG  . ASP A  1 128 ? 37.656  11.805  6.875   1.00 25.08 ? 128 ASP A CG  1 
ATOM   1033 O  OD1 . ASP A  1 128 ? 38.504  12.726  7.002   1.00 32.32 ? 128 ASP A OD1 1 
ATOM   1034 O  OD2 . ASP A  1 128 ? 36.555  12.019  6.402   1.00 22.73 ? 128 ASP A OD2 1 
ATOM   1035 N  N   . ALA A  1 129 ? 35.628  8.546   7.109   1.00 17.82 ? 129 ALA A N   1 
ATOM   1036 C  CA  . ALA A  1 129 ? 34.233  8.135   7.017   1.00 17.77 ? 129 ALA A CA  1 
ATOM   1037 C  C   . ALA A  1 129 ? 33.324  9.336   6.919   1.00 19.44 ? 129 ALA A C   1 
ATOM   1038 O  O   . ALA A  1 129 ? 32.353  9.299   6.196   1.00 18.44 ? 129 ALA A O   1 
ATOM   1039 C  CB  . ALA A  1 129 ? 33.841  7.322   8.240   1.00 18.72 ? 129 ALA A CB  1 
ATOM   1040 N  N   . SER A  1 130 ? 33.651  10.414  7.633   1.00 20.36 ? 130 SER A N   1 
ATOM   1041 C  CA  . SER A  1 130 ? 32.771  11.588  7.583   1.00 20.01 ? 130 SER A CA  1 
ATOM   1042 C  C   . SER A  1 130 ? 32.723  12.133  6.132   1.00 20.60 ? 130 SER A C   1 
ATOM   1043 O  O   . SER A  1 130 ? 31.647  12.432  5.595   1.00 21.07 ? 130 SER A O   1 
ATOM   1044 C  CB  . SER A  1 130 ? 33.310  12.599  8.620   1.00 23.59 ? 130 SER A CB  1 
ATOM   1045 O  OG  . SER A  1 130 ? 32.611  13.840  8.500   1.00 29.00 ? 130 SER A OG  1 
ATOM   1046 N  N   . THR A  1 131 ? 33.860  12.265  5.480   1.00 20.68 ? 131 THR A N   1 
ATOM   1047 C  CA  . THR A  1 131 ? 33.844  12.804  4.112   1.00 21.20 ? 131 THR A CA  1 
ATOM   1048 C  C   . THR A  1 131 ? 33.123  11.804  3.197   1.00 20.59 ? 131 THR A C   1 
ATOM   1049 O  O   . THR A  1 131 ? 32.443  12.199  2.269   1.00 18.42 ? 131 THR A O   1 
ATOM   1050 C  CB  . THR A  1 131 ? 35.301  13.008  3.634   1.00 22.76 ? 131 THR A CB  1 
ATOM   1051 O  OG1 . THR A  1 131 ? 35.960  13.820  4.628   1.00 24.02 ? 131 THR A OG1 1 
ATOM   1052 C  CG2 . THR A  1 131 ? 35.426  13.649  2.181   1.00 20.44 ? 131 THR A CG2 1 
ATOM   1053 N  N   . ALA A  1 132 ? 33.360  10.474  3.383   1.00 18.37 ? 132 ALA A N   1 
ATOM   1054 C  CA  . ALA A  1 132 ? 32.720  9.496   2.458   1.00 16.05 ? 132 ALA A CA  1 
ATOM   1055 C  C   . ALA A  1 132 ? 31.192  9.418   2.619   1.00 16.24 ? 132 ALA A C   1 
ATOM   1056 O  O   . ALA A  1 132 ? 30.562  8.991   1.716   1.00 15.29 ? 132 ALA A O   1 
ATOM   1057 C  CB  . ALA A  1 132 ? 33.224  8.097   2.774   1.00 14.85 ? 132 ALA A CB  1 
ATOM   1058 N  N   . SER A  1 133 ? 30.710  9.818   3.750   1.00 16.41 ? 133 SER A N   1 
ATOM   1059 C  CA  . SER A  1 133 ? 29.342  9.426   4.151   1.00 18.63 ? 133 SER A CA  1 
ATOM   1060 C  C   . SER A  1 133 ? 28.240  9.913   3.215   1.00 18.62 ? 133 SER A C   1 
ATOM   1061 O  O   . SER A  1 133 ? 27.190  9.281   3.103   1.00 17.51 ? 133 SER A O   1 
ATOM   1062 C  CB  . SER A  1 133 ? 29.061  9.869   5.577   1.00 19.75 ? 133 SER A CB  1 
ATOM   1063 O  OG  . SER A  1 133 ? 29.021  11.300  5.699   1.00 23.94 ? 133 SER A OG  1 
ATOM   1064 N  N   . ASN A  1 134 ? 28.441  11.044  2.549   1.00 17.91 ? 134 ASN A N   1 
ATOM   1065 C  CA  . ASN A  1 134 ? 27.473  11.635  1.627   1.00 19.46 ? 134 ASN A CA  1 
ATOM   1066 C  C   . ASN A  1 134 ? 27.913  11.603  0.200   1.00 19.19 ? 134 ASN A C   1 
ATOM   1067 O  O   . ASN A  1 134 ? 27.365  12.330  -0.654  1.00 21.85 ? 134 ASN A O   1 
ATOM   1068 C  CB  . ASN A  1 134 ? 27.034  13.069  2.080   1.00 23.70 ? 134 ASN A CB  1 
ATOM   1069 C  CG  . ASN A  1 134 ? 28.192  14.090  1.972   1.00 29.41 ? 134 ASN A CG  1 
ATOM   1070 O  OD1 . ASN A  1 134 ? 29.383  13.688  1.889   1.00 31.11 ? 134 ASN A OD1 1 
ATOM   1071 N  ND2 . ASN A  1 134 ? 27.849  15.419  1.968   1.00 34.16 ? 134 ASN A ND2 1 
ATOM   1072 N  N   . LYS A  1 135 ? 28.823  10.690  -0.139  1.00 16.96 ? 135 LYS A N   1 
ATOM   1073 C  CA  . LYS A  1 135 ? 29.369  10.563  -1.461  1.00 18.42 ? 135 LYS A CA  1 
ATOM   1074 C  C   . LYS A  1 135 ? 29.146  9.270   -2.122  1.00 19.73 ? 135 LYS A C   1 
ATOM   1075 O  O   . LYS A  1 135 ? 28.881  8.265   -1.465  1.00 17.16 ? 135 LYS A O   1 
ATOM   1076 C  CB  . LYS A  1 135 ? 30.908  10.880  -1.391  1.00 19.18 ? 135 LYS A CB  1 
ATOM   1077 C  CG  . LYS A  1 135 ? 31.085  12.402  -1.063  1.00 23.97 ? 135 LYS A CG  1 
ATOM   1078 C  CD  . LYS A  1 135 ? 32.497  12.903  -1.204  1.00 28.06 ? 135 LYS A CD  1 
ATOM   1079 C  CE  . LYS A  1 135 ? 32.596  14.290  -0.625  1.00 25.49 ? 135 LYS A CE  1 
ATOM   1080 N  NZ  . LYS A  1 135 ? 31.962  14.521  0.713   1.00 27.56 ? 135 LYS A NZ  1 
ATOM   1081 N  N   . SER A  1 136 ? 29.208  9.268   -3.439  1.00 19.44 ? 136 SER A N   1 
ATOM   1082 C  CA  . SER A  1 136 ? 29.000  8.126   -4.249  1.00 20.83 ? 136 SER A CA  1 
ATOM   1083 C  C   . SER A  1 136 ? 29.908  6.967   -3.859  1.00 18.92 ? 136 SER A C   1 
ATOM   1084 O  O   . SER A  1 136 ? 31.100  7.122   -3.722  1.00 18.50 ? 136 SER A O   1 
ATOM   1085 C  CB  . SER A  1 136 ? 29.400  8.511   -5.671  1.00 22.68 ? 136 SER A CB  1 
ATOM   1086 O  OG  . SER A  1 136 ? 28.898  7.624   -6.607  1.00 33.70 ? 136 SER A OG  1 
ATOM   1087 N  N   . GLU A  1 137 ? 29.300  5.799   -3.688  1.00 20.84 ? 137 GLU A N   1 
ATOM   1088 C  CA  . GLU A  1 137 ? 30.084  4.625   -3.284  1.00 18.72 ? 137 GLU A CA  1 
ATOM   1089 C  C   . GLU A  1 137 ? 30.756  4.861   -1.951  1.00 16.67 ? 137 GLU A C   1 
ATOM   1090 O  O   . GLU A  1 137 ? 31.780  4.261   -1.664  1.00 16.85 ? 137 GLU A O   1 
ATOM   1091 C  CB  . GLU A  1 137 ? 31.091  4.177   -4.347  1.00 25.73 ? 137 GLU A CB  1 
ATOM   1092 C  CG  . GLU A  1 137 ? 30.420  3.874   -5.708  1.00 29.49 ? 137 GLU A CG  1 
ATOM   1093 C  CD  . GLU A  1 137 ? 31.409  3.703   -6.861  1.00 43.27 ? 137 GLU A CD  1 
ATOM   1094 O  OE1 . GLU A  1 137 ? 32.661  3.746   -6.666  1.00 50.56 ? 137 GLU A OE1 1 
ATOM   1095 N  N   . GLY A  1 138 ? 30.179  5.662   -1.078  1.00 13.65 ? 138 GLY A N   1 
ATOM   1096 C  CA  . GLY A  1 138 ? 30.931  6.074   0.060   1.00 13.53 ? 138 GLY A CA  1 
ATOM   1097 C  C   . GLY A  1 138 ? 31.080  5.024   1.152   1.00 13.44 ? 138 GLY A C   1 
ATOM   1098 O  O   . GLY A  1 138 ? 32.105  4.992   1.830   1.00 12.55 ? 138 GLY A O   1 
ATOM   1099 N  N   . LEU A  1 139 ? 30.011  4.240   1.405   1.00 13.00 ? 139 LEU A N   1 
ATOM   1100 C  CA  . LEU A  1 139 ? 29.929  3.421   2.646   1.00 11.35 ? 139 LEU A CA  1 
ATOM   1101 C  C   . LEU A  1 139 ? 29.567  1.993   2.303   1.00 11.18 ? 139 LEU A C   1 
ATOM   1102 O  O   . LEU A  1 139 ? 28.890  1.733   1.344   1.00 11.53 ? 139 LEU A O   1 
ATOM   1103 C  CB  . LEU A  1 139 ? 28.927  3.975   3.669   1.00 10.60 ? 139 LEU A CB  1 
ATOM   1104 C  CG  . LEU A  1 139 ? 29.159  5.391   4.103   1.00 11.08 ? 139 LEU A CG  1 
ATOM   1105 C  CD1 . LEU A  1 139 ? 27.959  5.836   4.959   1.00 13.21 ? 139 LEU A CD1 1 
ATOM   1106 C  CD2 . LEU A  1 139 ? 30.499  5.563   4.824   1.00 13.85 ? 139 LEU A CD2 1 
ATOM   1107 N  N   . ALA A  1 140 ? 29.964  1.061   3.178   1.00 10.72 ? 140 ALA A N   1 
ATOM   1108 C  CA  . ALA A  1 140 ? 29.572  -0.322  3.075   1.00 9.58  ? 140 ALA A CA  1 
ATOM   1109 C  C   . ALA A  1 140 ? 29.310  -0.758  4.520   1.00 10.28 ? 140 ALA A C   1 
ATOM   1110 O  O   . ALA A  1 140 ? 30.168  -0.575  5.397   1.00 10.83 ? 140 ALA A O   1 
ATOM   1111 C  CB  . ALA A  1 140 ? 30.614  -1.158  2.391   1.00 11.25 ? 140 ALA A CB  1 
ATOM   1112 N  N   . VAL A  1 141 ? 28.156  -1.341  4.787   1.00 9.44  ? 141 VAL A N   1 
ATOM   1113 C  CA  . VAL A  1 141 ? 27.870  -1.818  6.164   1.00 9.05  ? 141 VAL A CA  1 
ATOM   1114 C  C   . VAL A  1 141 ? 27.591  -3.304  6.057   1.00 9.70  ? 141 VAL A C   1 
ATOM   1115 O  O   . VAL A  1 141 ? 26.928  -3.793  5.147   1.00 10.19 ? 141 VAL A O   1 
ATOM   1116 C  CB  . VAL A  1 141 ? 26.619  -1.090  6.696   1.00 9.06  ? 141 VAL A CB  1 
ATOM   1117 C  CG1 . VAL A  1 141 ? 26.327  -1.535  8.152   1.00 10.79 ? 141 VAL A CG1 1 
ATOM   1118 C  CG2 . VAL A  1 141 ? 26.879  0.424   6.747   1.00 10.98 ? 141 VAL A CG2 1 
ATOM   1119 N  N   . LEU A  1 142 ? 28.162  -4.045  7.027   1.00 8.76  ? 142 LEU A N   1 
ATOM   1120 C  CA  . LEU A  1 142 ? 27.861  -5.461  7.171   1.00 9.60  ? 142 LEU A CA  1 
ATOM   1121 C  C   . LEU A  1 142 ? 26.812  -5.540  8.232   1.00 10.10 ? 142 LEU A C   1 
ATOM   1122 O  O   . LEU A  1 142 ? 27.013  -4.947  9.327   1.00 10.66 ? 142 LEU A O   1 
ATOM   1123 C  CB  . LEU A  1 142 ? 29.131  -6.249  7.672   1.00 10.56 ? 142 LEU A CB  1 
ATOM   1124 C  CG  . LEU A  1 142 ? 30.317  -6.077  6.752   1.00 11.12 ? 142 LEU A CG  1 
ATOM   1125 C  CD1 . LEU A  1 142 ? 31.447  -6.927  7.346   1.00 13.85 ? 142 LEU A CD1 1 
ATOM   1126 C  CD2 . LEU A  1 142 ? 30.111  -6.591  5.341   1.00 12.37 ? 142 LEU A CD2 1 
ATOM   1127 N  N   . ALA A  1 143 ? 25.809  -6.378  8.023   1.00 8.99  ? 143 ALA A N   1 
ATOM   1128 C  CA  . ALA A  1 143 ? 24.750  -6.576  9.076   1.00 8.45  ? 143 ALA A CA  1 
ATOM   1129 C  C   . ALA A  1 143 ? 24.699  -8.044  9.445   1.00 9.22  ? 143 ALA A C   1 
ATOM   1130 O  O   . ALA A  1 143 ? 24.616  -8.924  8.586   1.00 9.80  ? 143 ALA A O   1 
ATOM   1131 C  CB  . ALA A  1 143 ? 23.378  -6.094  8.485   1.00 10.60 ? 143 ALA A CB  1 
ATOM   1132 N  N   . VAL A  1 144 ? 24.710  -8.220  10.797  1.00 9.19  ? 144 VAL A N   1 
ATOM   1133 C  CA  . VAL A  1 144 ? 24.536  -9.565  11.346  1.00 10.19 ? 144 VAL A CA  1 
ATOM   1134 C  C   . VAL A  1 144 ? 23.210  -9.597  12.089  1.00 9.57  ? 144 VAL A C   1 
ATOM   1135 O  O   . VAL A  1 144 ? 23.008  -8.767  13.036  1.00 10.20 ? 144 VAL A O   1 
ATOM   1136 C  CB  . VAL A  1 144 ? 25.704  -9.888  12.330  1.00 11.34 ? 144 VAL A CB  1 
ATOM   1137 C  CG1 . VAL A  1 144 ? 25.528  -11.320 12.852  1.00 13.21 ? 144 VAL A CG1 1 
ATOM   1138 C  CG2 . VAL A  1 144 ? 27.041  -9.761  11.583  1.00 11.60 ? 144 VAL A CG2 1 
ATOM   1139 N  N   . LEU A  1 145 ? 22.362  -10.549 11.737  1.00 10.41 ? 145 LEU A N   1 
ATOM   1140 C  CA  . LEU A  1 145 ? 21.095  -10.739 12.489  1.00 10.86 ? 145 LEU A CA  1 
ATOM   1141 C  C   . LEU A  1 145 ? 21.377  -11.517 13.768  1.00 11.67 ? 145 LEU A C   1 
ATOM   1142 O  O   . LEU A  1 145 ? 22.164  -12.482 13.703  1.00 11.18 ? 145 LEU A O   1 
ATOM   1143 C  CB  . LEU A  1 145 ? 20.057  -11.416 11.554  1.00 11.86 ? 145 LEU A CB  1 
ATOM   1144 C  CG  . LEU A  1 145 ? 19.864  -10.633 10.248  1.00 11.75 ? 145 LEU A CG  1 
ATOM   1145 C  CD1 . LEU A  1 145 ? 19.180  -11.542 9.258   1.00 13.78 ? 145 LEU A CD1 1 
ATOM   1146 C  CD2 . LEU A  1 145 ? 18.983  -9.401  10.551  1.00 14.15 ? 145 LEU A CD2 1 
ATOM   1147 N  N   . ILE A  1 146 ? 20.745  -11.154 14.851  1.00 9.90  ? 146 ILE A N   1 
ATOM   1148 C  CA  . ILE A  1 146 ? 20.964  -11.766 16.182  1.00 10.96 ? 146 ILE A CA  1 
ATOM   1149 C  C   . ILE A  1 146 ? 19.682  -12.370 16.698  1.00 11.05 ? 146 ILE A C   1 
ATOM   1150 O  O   . ILE A  1 146 ? 18.642  -11.688 16.683  1.00 11.32 ? 146 ILE A O   1 
ATOM   1151 C  CB  . ILE A  1 146 ? 21.482  -10.718 17.165  1.00 10.18 ? 146 ILE A CB  1 
ATOM   1152 C  CG1 . ILE A  1 146 ? 22.843  -10.149 16.655  1.00 11.56 ? 146 ILE A CG1 1 
ATOM   1153 C  CG2 . ILE A  1 146 ? 21.697  -11.305 18.575  1.00 11.46 ? 146 ILE A CG2 1 
ATOM   1154 C  CD1 . ILE A  1 146 ? 23.241  -8.834  17.374  1.00 11.93 ? 146 ILE A CD1 1 
ATOM   1155 N  N   . GLU A  1 147 ? 19.761  -13.626 17.176  1.00 12.72 ? 147 GLU A N   1 
ATOM   1156 C  CA  . GLU A  1 147 ? 18.595  -14.287 17.797  1.00 13.97 ? 147 GLU A CA  1 
ATOM   1157 C  C   . GLU A  1 147 ? 19.030  -14.822 19.171  1.00 13.29 ? 147 GLU A C   1 
ATOM   1158 O  O   . GLU A  1 147 ? 20.219  -14.984 19.461  1.00 13.46 ? 147 GLU A O   1 
ATOM   1159 C  CB  . GLU A  1 147 ? 17.993  -15.412 16.977  1.00 16.22 ? 147 GLU A CB  1 
ATOM   1160 C  CG  . GLU A  1 147 ? 18.968  -16.552 16.750  1.00 15.67 ? 147 GLU A CG  1 
ATOM   1161 C  CD  . GLU A  1 147 ? 18.498  -17.536 15.698  1.00 18.71 ? 147 GLU A CD  1 
ATOM   1162 O  OE1 . GLU A  1 147 ? 17.469  -17.327 14.982  1.00 22.25 ? 147 GLU A OE1 1 
ATOM   1163 O  OE2 . GLU A  1 147 ? 19.240  -18.547 15.505  1.00 23.49 ? 147 GLU A OE2 1 
ATOM   1164 N  N   A MET A  1 148 ? 18.042  -15.014 20.046  0.50 15.11 ? 148 MET A N   1 
ATOM   1165 N  N   B MET A  1 148 ? 18.036  -15.019 20.039  0.50 15.39 ? 148 MET A N   1 
ATOM   1166 C  CA  A MET A  1 148 ? 18.333  -15.675 21.307  0.50 16.60 ? 148 MET A CA  1 
ATOM   1167 C  CA  B MET A  1 148 ? 18.246  -15.724 21.298  0.50 17.35 ? 148 MET A CA  1 
ATOM   1168 C  C   A MET A  1 148 ? 18.706  -17.161 21.071  0.50 17.49 ? 148 MET A C   1 
ATOM   1169 C  C   B MET A  1 148 ? 18.709  -17.171 21.057  0.50 17.76 ? 148 MET A C   1 
ATOM   1170 O  O   A MET A  1 148 ? 18.149  -17.872 20.224  0.50 18.70 ? 148 MET A O   1 
ATOM   1171 O  O   B MET A  1 148 ? 18.171  -17.885 20.213  0.50 18.92 ? 148 MET A O   1 
ATOM   1172 C  CB  A MET A  1 148 ? 17.115  -15.559 22.228  0.50 18.45 ? 148 MET A CB  1 
ATOM   1173 C  CB  B MET A  1 148 ? 16.885  -15.820 21.978  0.50 19.04 ? 148 MET A CB  1 
ATOM   1174 C  CG  A MET A  1 148 ? 17.448  -16.036 23.644  0.50 18.46 ? 148 MET A CG  1 
ATOM   1175 C  CG  B MET A  1 148 ? 16.264  -14.504 22.431  0.50 21.35 ? 148 MET A CG  1 
ATOM   1176 S  SD  A MET A  1 148 ? 16.113  -15.847 24.852  0.50 24.65 ? 148 MET A SD  1 
ATOM   1177 S  SD  B MET A  1 148 ? 14.644  -14.860 23.209  0.50 30.65 ? 148 MET A SD  1 
ATOM   1178 C  CE  A MET A  1 148 ? 15.718  -14.117 24.845  0.50 19.05 ? 148 MET A CE  1 
ATOM   1179 C  CE  B MET A  1 148 ? 13.976  -13.264 23.720  0.50 20.00 ? 148 MET A CE  1 
ATOM   1180 N  N   . GLY A  1 149 ? 19.661  -17.635 21.856  1.00 16.89 ? 149 GLY A N   1 
ATOM   1181 C  CA  . GLY A  1 149 ? 20.118  -19.032 21.763  1.00 17.73 ? 149 GLY A CA  1 
ATOM   1182 C  C   . GLY A  1 149 ? 21.162  -19.218 22.859  1.00 17.26 ? 149 GLY A C   1 
ATOM   1183 O  O   . GLY A  1 149 ? 21.015  -18.759 24.002  1.00 17.60 ? 149 GLY A O   1 
ATOM   1184 N  N   A SER A  1 150 ? 22.253  -19.864 22.445  0.50 18.57 ? 150 SER A N   1 
ATOM   1185 N  N   B SER A  1 150 ? 22.236  -19.917 22.512  0.50 18.47 ? 150 SER A N   1 
ATOM   1186 C  CA  A SER A  1 150 ? 23.435  -20.011 23.260  0.50 18.30 ? 150 SER A CA  1 
ATOM   1187 C  CA  B SER A  1 150 ? 23.274  -20.155 23.479  0.50 18.19 ? 150 SER A CA  1 
ATOM   1188 C  C   A SER A  1 150 ? 24.153  -18.729 23.736  0.50 18.81 ? 150 SER A C   1 
ATOM   1189 C  C   B SER A  1 150 ? 24.122  -18.897 23.722  0.50 18.52 ? 150 SER A C   1 
ATOM   1190 O  O   A SER A  1 150 ? 24.320  -17.746 23.005  0.50 15.43 ? 150 SER A O   1 
ATOM   1191 O  O   B SER A  1 150 ? 24.263  -18.079 22.779  0.50 15.67 ? 150 SER A O   1 
ATOM   1192 C  CB  A SER A  1 150 ? 24.455  -20.870 22.482  0.50 21.55 ? 150 SER A CB  1 
ATOM   1193 C  CB  B SER A  1 150 ? 24.159  -21.276 22.940  0.50 22.44 ? 150 SER A CB  1 
ATOM   1194 O  OG  A SER A  1 150 ? 23.801  -22.015 21.968  0.50 25.73 ? 150 SER A OG  1 
ATOM   1195 O  OG  B SER A  1 150 ? 24.703  -20.840 21.706  0.50 22.63 ? 150 SER A OG  1 
ATOM   1196 N  N   . PHE A  1 151 ? 24.700  -18.767 24.932  1.00 17.68 ? 151 PHE A N   1 
ATOM   1197 C  CA  . PHE A  1 151 ? 25.633  -17.739 25.341  1.00 18.37 ? 151 PHE A CA  1 
ATOM   1198 C  C   . PHE A  1 151 ? 26.756  -17.598 24.283  1.00 19.48 ? 151 PHE A C   1 
ATOM   1199 O  O   . PHE A  1 151 ? 27.351  -18.589 23.781  1.00 19.48 ? 151 PHE A O   1 
ATOM   1200 C  CB  . PHE A  1 151 ? 26.213  -18.090 26.727  1.00 18.10 ? 151 PHE A CB  1 
ATOM   1201 C  CG  . PHE A  1 151 ? 27.159  -17.109 27.219  1.00 17.59 ? 151 PHE A CG  1 
ATOM   1202 C  CD1 . PHE A  1 151 ? 26.739  -15.885 27.771  1.00 18.84 ? 151 PHE A CD1 1 
ATOM   1203 C  CD2 . PHE A  1 151 ? 28.564  -17.339 27.101  1.00 16.33 ? 151 PHE A CD2 1 
ATOM   1204 C  CE1 . PHE A  1 151 ? 27.642  -14.939 28.145  1.00 17.99 ? 151 PHE A CE1 1 
ATOM   1205 C  CE2 . PHE A  1 151 ? 29.456  -16.394 27.564  1.00 17.15 ? 151 PHE A CE2 1 
ATOM   1206 C  CZ  . PHE A  1 151 ? 29.033  -15.196 28.055  1.00 19.04 ? 151 PHE A CZ  1 
ATOM   1207 N  N   . ASN A  1 152 ? 27.080  -16.338 23.994  1.00 15.08 ? 152 ASN A N   1 
ATOM   1208 C  CA  . ASN A  1 152 ? 28.085  -16.036 23.002  1.00 15.34 ? 152 ASN A CA  1 
ATOM   1209 C  C   . ASN A  1 152 ? 29.281  -15.242 23.598  1.00 15.95 ? 152 ASN A C   1 
ATOM   1210 O  O   . ASN A  1 152 ? 29.199  -14.096 23.956  1.00 17.09 ? 152 ASN A O   1 
ATOM   1211 C  CB  . ASN A  1 152 ? 27.375  -15.220 21.868  1.00 14.23 ? 152 ASN A CB  1 
ATOM   1212 C  CG  . ASN A  1 152 ? 28.288  -15.115 20.668  1.00 13.80 ? 152 ASN A CG  1 
ATOM   1213 O  OD1 . ASN A  1 152 ? 29.467  -14.740 20.782  1.00 16.36 ? 152 ASN A OD1 1 
ATOM   1214 N  ND2 . ASN A  1 152 ? 27.726  -15.328 19.530  1.00 14.19 ? 152 ASN A ND2 1 
ATOM   1215 N  N   . PRO A  1 153 ? 30.431  -15.975 23.883  1.00 17.06 ? 153 PRO A N   1 
ATOM   1216 C  CA  . PRO A  1 153 ? 31.499  -15.315 24.553  1.00 18.32 ? 153 PRO A CA  1 
ATOM   1217 C  C   . PRO A  1 153 ? 32.084  -14.095 23.783  1.00 18.11 ? 153 PRO A C   1 
ATOM   1218 O  O   . PRO A  1 153 ? 32.600  -13.115 24.377  1.00 19.84 ? 153 PRO A O   1 
ATOM   1219 C  CB  . PRO A  1 153 ? 32.525  -16.466 24.744  1.00 20.57 ? 153 PRO A CB  1 
ATOM   1220 C  CG  . PRO A  1 153 ? 31.730  -17.729 24.643  1.00 25.63 ? 153 PRO A CG  1 
ATOM   1221 C  CD  . PRO A  1 153 ? 30.543  -17.432 23.720  1.00 19.21 ? 153 PRO A CD  1 
ATOM   1222 N  N   . SER A  1 154 ? 31.994  -14.197 22.452  1.00 18.45 ? 154 SER A N   1 
ATOM   1223 C  CA  . SER A  1 154 ? 32.555  -13.083 21.670  1.00 16.87 ? 154 SER A CA  1 
ATOM   1224 C  C   . SER A  1 154 ? 31.740  -11.807 21.790  1.00 14.20 ? 154 SER A C   1 
ATOM   1225 O  O   . SER A  1 154 ? 32.300  -10.751 21.978  1.00 16.00 ? 154 SER A O   1 
ATOM   1226 C  CB  . SER A  1 154 ? 32.696  -13.493 20.201  1.00 18.76 ? 154 SER A CB  1 
ATOM   1227 O  OG  . SER A  1 154 ? 33.542  -14.624 20.068  1.00 21.21 ? 154 SER A OG  1 
ATOM   1228 N  N   . TYR A  1 155 ? 30.403  -11.950 21.722  1.00 15.03 ? 155 TYR A N   1 
ATOM   1229 C  CA  . TYR A  1 155 ? 29.607  -10.737 21.933  1.00 14.10 ? 155 TYR A CA  1 
ATOM   1230 C  C   . TYR A  1 155 ? 29.786  -10.196 23.365  1.00 16.47 ? 155 TYR A C   1 
ATOM   1231 O  O   . TYR A  1 155 ? 29.708  -9.003  23.582  1.00 16.53 ? 155 TYR A O   1 
ATOM   1232 C  CB  . TYR A  1 155 ? 28.137  -10.988 21.602  1.00 13.15 ? 155 TYR A CB  1 
ATOM   1233 C  CG  . TYR A  1 155 ? 27.858  -10.830 20.125  1.00 14.22 ? 155 TYR A CG  1 
ATOM   1234 C  CD1 . TYR A  1 155 ? 28.194  -11.832 19.228  1.00 14.36 ? 155 TYR A CD1 1 
ATOM   1235 C  CD2 . TYR A  1 155 ? 27.289  -9.668  19.625  1.00 14.89 ? 155 TYR A CD2 1 
ATOM   1236 C  CE1 . TYR A  1 155 ? 27.956  -11.688 17.875  1.00 13.81 ? 155 TYR A CE1 1 
ATOM   1237 C  CE2 . TYR A  1 155 ? 27.047  -9.515  18.274  1.00 13.30 ? 155 TYR A CE2 1 
ATOM   1238 C  CZ  . TYR A  1 155 ? 27.382  -10.528 17.402  1.00 12.03 ? 155 TYR A CZ  1 
ATOM   1239 O  OH  . TYR A  1 155 ? 27.140  -10.373 16.055  1.00 13.58 ? 155 TYR A OH  1 
ATOM   1240 N  N   . ASP A  1 156 ? 30.034  -11.122 24.322  1.00 15.41 ? 156 ASP A N   1 
ATOM   1241 C  CA  . ASP A  1 156 ? 30.289  -10.606 25.662  1.00 17.07 ? 156 ASP A CA  1 
ATOM   1242 C  C   . ASP A  1 156 ? 31.574  -9.773  25.819  1.00 17.58 ? 156 ASP A C   1 
ATOM   1243 O  O   . ASP A  1 156 ? 31.644  -8.953  26.749  1.00 19.24 ? 156 ASP A O   1 
ATOM   1244 C  CB  . ASP A  1 156 ? 30.230  -11.737 26.667  1.00 20.66 ? 156 ASP A CB  1 
ATOM   1245 C  CG  . ASP A  1 156 ? 29.181  -11.440 27.764  1.00 22.75 ? 156 ASP A CG  1 
ATOM   1246 O  OD1 . ASP A  1 156 ? 28.032  -10.955 27.499  1.00 19.22 ? 156 ASP A OD1 1 
ATOM   1247 O  OD2 . ASP A  1 156 ? 29.571  -11.516 28.957  1.00 26.40 ? 156 ASP A OD2 1 
ATOM   1248 N  N   . LYS A  1 157 ? 32.502  -9.861  24.851  1.00 15.69 ? 157 LYS A N   1 
ATOM   1249 C  CA  . LYS A  1 157 ? 33.626  -8.929  24.852  1.00 17.66 ? 157 LYS A CA  1 
ATOM   1250 C  C   . LYS A  1 157 ? 33.193  -7.496  24.654  1.00 19.84 ? 157 LYS A C   1 
ATOM   1251 O  O   . LYS A  1 157 ? 33.882  -6.561  25.128  1.00 21.23 ? 157 LYS A O   1 
ATOM   1252 C  CB  . LYS A  1 157 ? 34.740  -9.329  23.873  1.00 19.52 ? 157 LYS A CB  1 
ATOM   1253 C  CG  . LYS A  1 157 ? 35.237  -10.784 24.106  1.00 20.27 ? 157 LYS A CG  1 
ATOM   1254 C  CD  . LYS A  1 157 ? 36.221  -11.304 23.038  1.00 22.07 ? 157 LYS A CD  1 
ATOM   1255 C  CE  . LYS A  1 157 ? 36.564  -12.759 23.328  1.00 25.94 ? 157 LYS A CE  1 
ATOM   1256 N  NZ  . LYS A  1 157 ? 37.413  -13.345 22.249  1.00 26.20 ? 157 LYS A NZ  1 
ATOM   1257 N  N   . ILE A  1 158 ? 31.999  -7.318  24.090  1.00 18.60 ? 158 ILE A N   1 
ATOM   1258 C  CA  . ILE A  1 158 ? 31.417  -5.988  24.055  1.00 18.68 ? 158 ILE A CA  1 
ATOM   1259 C  C   . ILE A  1 158 ? 30.478  -5.814  25.243  1.00 17.09 ? 158 ILE A C   1 
ATOM   1260 O  O   . ILE A  1 158 ? 30.570  -4.793  25.984  1.00 17.66 ? 158 ILE A O   1 
ATOM   1261 C  CB  . ILE A  1 158 ? 30.593  -5.738  22.755  1.00 21.55 ? 158 ILE A CB  1 
ATOM   1262 C  CG1 . ILE A  1 158 ? 31.458  -5.990  21.502  1.00 24.25 ? 158 ILE A CG1 1 
ATOM   1263 C  CG2 . ILE A  1 158 ? 29.960  -4.322  22.796  1.00 18.72 ? 158 ILE A CG2 1 
ATOM   1264 C  CD1 . ILE A  1 158 ? 30.659  -6.064  20.212  1.00 25.19 ? 158 ILE A CD1 1 
ATOM   1265 N  N   . PHE A  1 159 ? 29.539  -6.759  25.404  1.00 16.12 ? 159 PHE A N   1 
ATOM   1266 C  CA  . PHE A  1 159 ? 28.458  -6.566  26.397  1.00 17.35 ? 159 PHE A CA  1 
ATOM   1267 C  C   . PHE A  1 159 ? 28.965  -6.429  27.868  1.00 18.55 ? 159 PHE A C   1 
ATOM   1268 O  O   . PHE A  1 159 ? 28.356  -5.717  28.632  1.00 19.45 ? 159 PHE A O   1 
ATOM   1269 C  CB  . PHE A  1 159 ? 27.471  -7.674  26.357  1.00 15.36 ? 159 PHE A CB  1 
ATOM   1270 C  CG  . PHE A  1 159 ? 26.749  -7.798  25.033  1.00 17.83 ? 159 PHE A CG  1 
ATOM   1271 C  CD1 . PHE A  1 159 ? 26.642  -6.724  24.114  1.00 19.64 ? 159 PHE A CD1 1 
ATOM   1272 C  CD2 . PHE A  1 159 ? 26.128  -8.974  24.742  1.00 18.05 ? 159 PHE A CD2 1 
ATOM   1273 C  CE1 . PHE A  1 159 ? 25.906  -6.943  22.888  1.00 17.48 ? 159 PHE A CE1 1 
ATOM   1274 C  CE2 . PHE A  1 159 ? 25.447  -9.163  23.561  1.00 18.26 ? 159 PHE A CE2 1 
ATOM   1275 C  CZ  . PHE A  1 159 ? 25.334  -8.130  22.629  1.00 15.99 ? 159 PHE A CZ  1 
ATOM   1276 N  N   . SER A  1 160 ? 30.147  -6.980  28.151  1.00 18.60 ? 160 SER A N   1 
ATOM   1277 C  CA  . SER A  1 160 ? 30.718  -6.835  29.528  1.00 20.88 ? 160 SER A CA  1 
ATOM   1278 C  C   . SER A  1 160 ? 31.105  -5.397  29.862  1.00 23.80 ? 160 SER A C   1 
ATOM   1279 O  O   . SER A  1 160 ? 31.333  -5.051  31.027  1.00 23.78 ? 160 SER A O   1 
ATOM   1280 C  CB  . SER A  1 160 ? 31.893  -7.808  29.683  1.00 17.50 ? 160 SER A CB  1 
ATOM   1281 O  OG  . SER A  1 160 ? 33.011  -7.364  28.928  1.00 23.24 ? 160 SER A OG  1 
ATOM   1282 N  N   . HIS A  1 161 ? 31.168  -4.520  28.859  1.00 19.82 ? 161 HIS A N   1 
ATOM   1283 C  CA  . HIS A  1 161 ? 31.494  -3.142  29.082  1.00 20.71 ? 161 HIS A CA  1 
ATOM   1284 C  C   . HIS A  1 161 ? 30.264  -2.225  29.134  1.00 19.47 ? 161 HIS A C   1 
ATOM   1285 O  O   . HIS A  1 161 ? 30.409  -1.023  29.405  1.00 20.26 ? 161 HIS A O   1 
ATOM   1286 C  CB  . HIS A  1 161 ? 32.518  -2.631  28.083  1.00 20.52 ? 161 HIS A CB  1 
ATOM   1287 C  CG  . HIS A  1 161 ? 33.830  -3.363  28.147  1.00 23.26 ? 161 HIS A CG  1 
ATOM   1288 N  ND1 . HIS A  1 161 ? 34.846  -2.971  28.939  1.00 26.99 ? 161 HIS A ND1 1 
ATOM   1289 C  CD2 . HIS A  1 161 ? 34.260  -4.515  27.498  1.00 24.64 ? 161 HIS A CD2 1 
ATOM   1290 C  CE1 . HIS A  1 161 ? 35.879  -3.821  28.793  1.00 22.72 ? 161 HIS A CE1 1 
ATOM   1291 N  NE2 . HIS A  1 161 ? 35.518  -4.765  27.910  1.00 28.66 ? 161 HIS A NE2 1 
ATOM   1292 N  N   . LEU A  1 162 ? 29.056  -2.771  28.865  1.00 18.28 ? 162 LEU A N   1 
ATOM   1293 C  CA  . LEU A  1 162 ? 27.918  -1.907  28.795  1.00 18.42 ? 162 LEU A CA  1 
ATOM   1294 C  C   . LEU A  1 162 ? 27.682  -1.070  30.082  1.00 23.29 ? 162 LEU A C   1 
ATOM   1295 O  O   . LEU A  1 162 ? 27.186  0.045   29.991  1.00 18.52 ? 162 LEU A O   1 
ATOM   1296 C  CB  . LEU A  1 162 ? 26.614  -2.706  28.491  1.00 19.45 ? 162 LEU A CB  1 
ATOM   1297 C  CG  . LEU A  1 162 ? 26.618  -3.267  27.074  1.00 20.09 ? 162 LEU A CG  1 
ATOM   1298 C  CD1 . LEU A  1 162 ? 25.435  -4.244  27.047  1.00 21.56 ? 162 LEU A CD1 1 
ATOM   1299 C  CD2 . LEU A  1 162 ? 26.629  -2.169  25.987  1.00 24.26 ? 162 LEU A CD2 1 
ATOM   1300 N  N   . GLN A  1 163 ? 27.951  -1.630  31.236  1.00 26.46 ? 163 GLN A N   1 
ATOM   1301 C  CA  . GLN A  1 163 ? 27.614  -0.853  32.442  1.00 29.51 ? 163 GLN A CA  1 
ATOM   1302 C  C   . GLN A  1 163 ? 28.487  0.413   32.565  1.00 30.00 ? 163 GLN A C   1 
ATOM   1303 O  O   . GLN A  1 163 ? 28.042  1.440   33.114  1.00 33.03 ? 163 GLN A O   1 
ATOM   1304 C  CB  . GLN A  1 163 ? 27.582  -1.720  33.709  1.00 39.49 ? 163 GLN A CB  1 
ATOM   1305 N  N   . HIS A  1 164 ? 29.670  0.396   31.965  1.00 22.71 ? 164 HIS A N   1 
ATOM   1306 C  CA  . HIS A  1 164 ? 30.450  1.640   31.923  1.00 22.79 ? 164 HIS A CA  1 
ATOM   1307 C  C   . HIS A  1 164 ? 29.972  2.681   30.886  1.00 23.19 ? 164 HIS A C   1 
ATOM   1308 O  O   . HIS A  1 164 ? 30.463  3.784   30.881  1.00 22.45 ? 164 HIS A O   1 
ATOM   1309 C  CB  . HIS A  1 164 ? 31.915  1.396   31.730  1.00 21.36 ? 164 HIS A CB  1 
ATOM   1310 C  CG  . HIS A  1 164 ? 32.515  0.556   32.800  1.00 23.06 ? 164 HIS A CG  1 
ATOM   1311 N  ND1 . HIS A  1 164 ? 33.323  -0.467  32.520  1.00 23.94 ? 164 HIS A ND1 1 
ATOM   1312 C  CD2 . HIS A  1 164 ? 32.396  0.606   34.188  1.00 28.63 ? 164 HIS A CD2 1 
ATOM   1313 C  CE1 . HIS A  1 164 ? 33.718  -1.051  33.662  1.00 26.58 ? 164 HIS A CE1 1 
ATOM   1314 N  NE2 . HIS A  1 164 ? 33.148  -0.392  34.685  1.00 34.32 ? 164 HIS A NE2 1 
ATOM   1315 N  N   . VAL A  1 165 ? 29.014  2.338   29.997  1.00 18.47 ? 165 VAL A N   1 
ATOM   1316 C  CA  . VAL A  1 165 ? 28.571  3.365   29.061  1.00 18.34 ? 165 VAL A CA  1 
ATOM   1317 C  C   . VAL A  1 165 ? 27.053  3.492   29.138  1.00 18.22 ? 165 VAL A C   1 
ATOM   1318 O  O   . VAL A  1 165 ? 26.315  3.748   28.150  1.00 18.79 ? 165 VAL A O   1 
ATOM   1319 C  CB  . VAL A  1 165 ? 28.996  3.082   27.573  1.00 19.57 ? 165 VAL A CB  1 
ATOM   1320 C  CG1 . VAL A  1 165 ? 30.529  3.238   27.393  1.00 20.91 ? 165 VAL A CG1 1 
ATOM   1321 C  CG2 . VAL A  1 165 ? 28.619  1.678   27.117  1.00 17.52 ? 165 VAL A CG2 1 
ATOM   1322 N  N   . LYS A  1 166 ? 26.563  3.463   30.383  1.00 19.44 ? 166 LYS A N   1 
ATOM   1323 C  CA  . LYS A  1 166 ? 25.120  3.493   30.664  1.00 18.85 ? 166 LYS A CA  1 
ATOM   1324 C  C   . LYS A  1 166 ? 24.390  4.752   30.107  1.00 19.85 ? 166 LYS A C   1 
ATOM   1325 O  O   . LYS A  1 166 ? 23.261  4.671   29.622  1.00 21.29 ? 166 LYS A O   1 
ATOM   1326 C  CB  . LYS A  1 166 ? 24.935  3.360   32.211  1.00 23.03 ? 166 LYS A CB  1 
ATOM   1327 C  CG  . LYS A  1 166 ? 23.526  3.274   32.761  1.00 31.30 ? 166 LYS A CG  1 
ATOM   1328 C  CD  . LYS A  1 166 ? 23.522  2.897   34.254  1.00 32.67 ? 166 LYS A CD  1 
ATOM   1329 C  CE  . LYS A  1 166 ? 24.214  1.537   34.464  1.00 34.74 ? 166 LYS A CE  1 
ATOM   1330 N  NZ  . LYS A  1 166 ? 23.604  0.435   33.647  1.00 44.31 ? 166 LYS A NZ  1 
ATOM   1331 N  N   . TYR A  1 167 ? 25.011  5.947   30.235  1.00 16.85 ? 167 TYR A N   1 
ATOM   1332 C  CA  . TYR A  1 167 ? 24.361  7.199   29.885  1.00 17.14 ? 167 TYR A CA  1 
ATOM   1333 C  C   . TYR A  1 167 ? 24.986  7.846   28.651  1.00 17.56 ? 167 TYR A C   1 
ATOM   1334 O  O   . TYR A  1 167 ? 26.179  7.606   28.364  1.00 17.12 ? 167 TYR A O   1 
ATOM   1335 C  CB  . TYR A  1 167 ? 24.393  8.212   31.047  1.00 18.33 ? 167 TYR A CB  1 
ATOM   1336 C  CG  . TYR A  1 167 ? 23.694  7.638   32.288  1.00 18.67 ? 167 TYR A CG  1 
ATOM   1337 C  CD1 . TYR A  1 167 ? 22.309  7.710   32.385  1.00 21.45 ? 167 TYR A CD1 1 
ATOM   1338 C  CD2 . TYR A  1 167 ? 24.431  7.090   33.344  1.00 19.27 ? 167 TYR A CD2 1 
ATOM   1339 C  CE1 . TYR A  1 167 ? 21.645  7.174   33.501  1.00 23.07 ? 167 TYR A CE1 1 
ATOM   1340 C  CE2 . TYR A  1 167 ? 23.785  6.552   34.438  1.00 25.06 ? 167 TYR A CE2 1 
ATOM   1341 C  CZ  . TYR A  1 167 ? 22.395  6.616   34.495  1.00 23.85 ? 167 TYR A CZ  1 
ATOM   1342 O  OH  . TYR A  1 167 ? 21.829  6.125   35.655  1.00 24.14 ? 167 TYR A OH  1 
ATOM   1343 N  N   . LYS A  1 168 ? 24.221  8.704   27.993  1.00 20.31 ? 168 LYS A N   1 
ATOM   1344 C  CA  . LYS A  1 168 ? 24.679  9.369   26.816  1.00 20.85 ? 168 LYS A CA  1 
ATOM   1345 C  C   . LYS A  1 168 ? 25.984  10.151  27.087  1.00 24.57 ? 168 LYS A C   1 
ATOM   1346 O  O   . LYS A  1 168 ? 26.138  10.824  28.132  1.00 21.22 ? 168 LYS A O   1 
ATOM   1347 C  CB  . LYS A  1 168 ? 23.613  10.354  26.375  1.00 20.13 ? 168 LYS A CB  1 
ATOM   1348 C  CG  . LYS A  1 168 ? 24.039  11.052  25.083  1.00 19.60 ? 168 LYS A CG  1 
ATOM   1349 C  CD  . LYS A  1 168 ? 22.863  11.867  24.562  1.00 25.69 ? 168 LYS A CD  1 
ATOM   1350 C  CE  . LYS A  1 168 ? 23.392  12.819  23.498  1.00 33.48 ? 168 LYS A CE  1 
ATOM   1351 N  NZ  . LYS A  1 168 ? 22.299  13.444  22.695  1.00 36.04 ? 168 LYS A NZ  1 
ATOM   1352 N  N   . GLY A  1 169 ? 26.978  10.017  26.212  1.00 23.68 ? 169 GLY A N   1 
ATOM   1353 C  CA  . GLY A  1 169 ? 28.247  10.699  26.467  1.00 24.24 ? 169 GLY A CA  1 
ATOM   1354 C  C   . GLY A  1 169 ? 29.325  9.861   27.104  1.00 24.91 ? 169 GLY A C   1 
ATOM   1355 O  O   . GLY A  1 169 ? 30.495  10.157  26.905  1.00 29.77 ? 169 GLY A O   1 
ATOM   1356 N  N   . GLN A  1 170 ? 28.965  8.835   27.852  1.00 22.52 ? 170 GLN A N   1 
ATOM   1357 C  CA  . GLN A  1 170 ? 29.962  8.041   28.526  1.00 19.28 ? 170 GLN A CA  1 
ATOM   1358 C  C   . GLN A  1 170 ? 30.758  7.165   27.594  1.00 21.82 ? 170 GLN A C   1 
ATOM   1359 O  O   . GLN A  1 170 ? 30.263  6.811   26.478  1.00 19.42 ? 170 GLN A O   1 
ATOM   1360 C  CB  . GLN A  1 170 ? 29.277  7.192   29.614  1.00 18.46 ? 170 GLN A CB  1 
ATOM   1361 C  CG  . GLN A  1 170 ? 28.671  8.032   30.724  1.00 19.35 ? 170 GLN A CG  1 
ATOM   1362 C  CD  . GLN A  1 170 ? 28.148  7.194   31.884  1.00 20.88 ? 170 GLN A CD  1 
ATOM   1363 O  OE1 . GLN A  1 170 ? 27.628  6.138   31.692  1.00 21.29 ? 170 GLN A OE1 1 
ATOM   1364 N  NE2 . GLN A  1 170 ? 28.249  7.721   33.142  1.00 20.66 ? 170 GLN A NE2 1 
ATOM   1365 N  N   A GLU A  1 171 ? 31.984  6.805   27.990  0.50 21.97 ? 171 GLU A N   1 
ATOM   1366 N  N   B GLU A  1 171 ? 31.950  6.779   28.049  0.50 21.37 ? 171 GLU A N   1 
ATOM   1367 C  CA  A GLU A  1 171 ? 32.977  6.177   27.095  0.50 22.34 ? 171 GLU A CA  1 
ATOM   1368 C  CA  B GLU A  1 171 ? 32.881  5.999   27.258  0.50 20.91 ? 171 GLU A CA  1 
ATOM   1369 C  C   A GLU A  1 171 ? 33.802  5.225   27.907  0.50 20.04 ? 171 GLU A C   1 
ATOM   1370 C  C   B GLU A  1 171 ? 33.554  4.947   28.075  0.50 21.17 ? 171 GLU A C   1 
ATOM   1371 O  O   A GLU A  1 171 ? 34.040  5.538   29.104  0.50 20.23 ? 171 GLU A O   1 
ATOM   1372 O  O   B GLU A  1 171 ? 33.543  4.908   29.341  0.50 18.04 ? 171 GLU A O   1 
ATOM   1373 C  CB  A GLU A  1 171 ? 33.877  7.266   26.457  0.50 24.16 ? 171 GLU A CB  1 
ATOM   1374 C  CB  B GLU A  1 171 ? 33.938  6.891   26.557  0.50 23.12 ? 171 GLU A CB  1 
ATOM   1375 C  CG  A GLU A  1 171 ? 33.158  8.131   25.451  0.50 26.16 ? 171 GLU A CG  1 
ATOM   1376 C  CG  B GLU A  1 171 ? 34.787  7.701   27.528  0.50 24.02 ? 171 GLU A CG  1 
ATOM   1377 C  CD  A GLU A  1 171 ? 33.977  9.316   24.946  0.50 27.79 ? 171 GLU A CD  1 
ATOM   1378 C  CD  B GLU A  1 171 ? 35.960  8.422   26.894  0.50 24.87 ? 171 GLU A CD  1 
ATOM   1379 O  OE1 A GLU A  1 171 ? 35.154  9.469   25.315  0.50 28.25 ? 171 GLU A OE1 1 
ATOM   1380 O  OE1 B GLU A  1 171 ? 35.799  8.982   25.780  0.50 26.84 ? 171 GLU A OE1 1 
ATOM   1381 O  OE2 A GLU A  1 171 ? 33.440  10.087  24.147  0.50 25.53 ? 171 GLU A OE2 1 
ATOM   1382 O  OE2 B GLU A  1 171 ? 37.064  8.417   27.524  0.50 21.11 ? 171 GLU A OE2 1 
ATOM   1383 N  N   . ALA A  1 172 ? 34.150  4.049   27.349  1.00 20.01 ? 172 ALA A N   1 
ATOM   1384 C  CA  . ALA A  1 172 ? 34.949  2.986   27.993  1.00 20.14 ? 172 ALA A CA  1 
ATOM   1385 C  C   . ALA A  1 172 ? 35.927  2.473   26.981  1.00 20.03 ? 172 ALA A C   1 
ATOM   1386 O  O   . ALA A  1 172 ? 35.783  2.743   25.771  1.00 20.62 ? 172 ALA A O   1 
ATOM   1387 C  CB  . ALA A  1 172 ? 34.085  1.835   28.472  1.00 21.62 ? 172 ALA A CB  1 
ATOM   1388 N  N   . PHE A  1 173 ? 36.916  1.732   27.450  1.00 23.22 ? 173 PHE A N   1 
ATOM   1389 C  CA  . PHE A  1 173 ? 37.919  1.190   26.546  1.00 22.72 ? 173 PHE A CA  1 
ATOM   1390 C  C   . PHE A  1 173 ? 37.770  -0.315  26.489  1.00 23.09 ? 173 PHE A C   1 
ATOM   1391 O  O   . PHE A  1 173 ? 37.622  -1.012  27.522  1.00 27.04 ? 173 PHE A O   1 
ATOM   1392 C  CB  . PHE A  1 173 ? 39.299  1.691   26.989  1.00 26.86 ? 173 PHE A CB  1 
ATOM   1393 C  CG  . PHE A  1 173 ? 39.580  3.111   26.553  1.00 28.10 ? 173 PHE A CG  1 
ATOM   1394 C  CD1 . PHE A  1 173 ? 39.859  3.430   25.199  1.00 32.15 ? 173 PHE A CD1 1 
ATOM   1395 C  CD2 . PHE A  1 173 ? 39.587  4.132   27.496  1.00 34.98 ? 173 PHE A CD2 1 
ATOM   1396 C  CE1 . PHE A  1 173 ? 40.120  4.748   24.826  1.00 32.49 ? 173 PHE A CE1 1 
ATOM   1397 C  CE2 . PHE A  1 173 ? 39.855  5.449   27.133  1.00 36.39 ? 173 PHE A CE2 1 
ATOM   1398 C  CZ  . PHE A  1 173 ? 40.126  5.758   25.802  1.00 32.85 ? 173 PHE A CZ  1 
ATOM   1399 N  N   . VAL A  1 174 ? 37.759  -0.848  25.270  1.00 19.03 ? 174 VAL A N   1 
ATOM   1400 C  CA  . VAL A  1 174 ? 37.647  -2.219  25.071  1.00 19.33 ? 174 VAL A CA  1 
ATOM   1401 C  C   . VAL A  1 174 ? 38.920  -2.769  24.448  1.00 20.80 ? 174 VAL A C   1 
ATOM   1402 O  O   . VAL A  1 174 ? 39.336  -2.302  23.406  1.00 21.68 ? 174 VAL A O   1 
ATOM   1403 C  CB  . VAL A  1 174 ? 36.480  -2.482  24.093  1.00 18.08 ? 174 VAL A CB  1 
ATOM   1404 C  CG1 . VAL A  1 174 ? 36.356  -3.972  23.961  1.00 18.56 ? 174 VAL A CG1 1 
ATOM   1405 C  CG2 . VAL A  1 174 ? 35.203  -1.836  24.644  1.00 19.96 ? 174 VAL A CG2 1 
ATOM   1406 N  N   . PRO A  1 175 ? 39.594  -3.763  25.094  1.00 19.87 ? 175 PRO A N   1 
ATOM   1407 C  CA  . PRO A  1 175 ? 40.841  -4.368  24.499  1.00 22.05 ? 175 PRO A CA  1 
ATOM   1408 C  C   . PRO A  1 175 ? 40.567  -5.028  23.179  1.00 21.83 ? 175 PRO A C   1 
ATOM   1409 O  O   . PRO A  1 175 ? 39.545  -5.644  23.039  1.00 20.74 ? 175 PRO A O   1 
ATOM   1410 C  CB  . PRO A  1 175 ? 41.183  -5.467  25.505  1.00 24.04 ? 175 PRO A CB  1 
ATOM   1411 C  CG  . PRO A  1 175 ? 40.515  -5.004  26.750  1.00 24.14 ? 175 PRO A CG  1 
ATOM   1412 C  CD  . PRO A  1 175 ? 39.163  -4.497  26.273  1.00 21.62 ? 175 PRO A CD  1 
ATOM   1413 N  N   . GLY A  1 176 ? 41.438  -4.866  22.215  1.00 23.13 ? 176 GLY A N   1 
ATOM   1414 C  CA  . GLY A  1 176 ? 41.209  -5.504  20.965  1.00 21.25 ? 176 GLY A CA  1 
ATOM   1415 C  C   . GLY A  1 176 ? 40.872  -6.970  21.100  1.00 22.14 ? 176 GLY A C   1 
ATOM   1416 O  O   . GLY A  1 176 ? 41.467  -7.731  21.905  1.00 23.97 ? 176 GLY A O   1 
ATOM   1417 N  N   . PHE A  1 177 ? 39.942  -7.439  20.265  1.00 18.93 ? 177 PHE A N   1 
ATOM   1418 C  CA  . PHE A  1 177 ? 39.653  -8.832  20.009  1.00 18.58 ? 177 PHE A CA  1 
ATOM   1419 C  C   . PHE A  1 177 ? 39.302  -9.112  18.525  1.00 15.99 ? 177 PHE A C   1 
ATOM   1420 O  O   . PHE A  1 177 ? 39.321  -8.129  17.785  1.00 15.53 ? 177 PHE A O   1 
ATOM   1421 C  CB  . PHE A  1 177 ? 38.531  -9.336  20.921  1.00 19.76 ? 177 PHE A CB  1 
ATOM   1422 C  CG  . PHE A  1 177 ? 37.137  -8.751  20.614  1.00 19.02 ? 177 PHE A CG  1 
ATOM   1423 C  CD1 . PHE A  1 177 ? 36.806  -7.478  21.028  1.00 18.33 ? 177 PHE A CD1 1 
ATOM   1424 C  CD2 . PHE A  1 177 ? 36.203  -9.504  19.888  1.00 20.34 ? 177 PHE A CD2 1 
ATOM   1425 C  CE1 . PHE A  1 177 ? 35.513  -6.923  20.731  1.00 20.93 ? 177 PHE A CE1 1 
ATOM   1426 C  CE2 . PHE A  1 177 ? 34.959  -8.968  19.561  1.00 20.72 ? 177 PHE A CE2 1 
ATOM   1427 C  CZ  . PHE A  1 177 ? 34.597  -7.693  20.005  1.00 18.31 ? 177 PHE A CZ  1 
ATOM   1428 N  N   . ASN A  1 178 ? 39.128  -10.363 18.138  1.00 17.34 ? 178 ASN A N   1 
ATOM   1429 C  CA  . ASN A  1 178 ? 38.903  -10.697 16.736  1.00 17.12 ? 178 ASN A CA  1 
ATOM   1430 C  C   . ASN A  1 178 ? 37.411  -10.382 16.384  1.00 17.37 ? 178 ASN A C   1 
ATOM   1431 O  O   . ASN A  1 178 ? 36.501  -11.191 16.666  1.00 15.95 ? 178 ASN A O   1 
ATOM   1432 C  CB  . ASN A  1 178 ? 39.304  -12.148 16.442  1.00 18.92 ? 178 ASN A CB  1 
ATOM   1433 C  CG  . ASN A  1 178 ? 39.087  -12.519 15.006  1.00 22.61 ? 178 ASN A CG  1 
ATOM   1434 O  OD1 . ASN A  1 178 ? 38.800  -11.676 14.162  1.00 18.77 ? 178 ASN A OD1 1 
ATOM   1435 N  ND2 . ASN A  1 178 ? 39.186  -13.764 14.710  1.00 23.12 ? 178 ASN A ND2 1 
ATOM   1436 N  N   . ILE A  1 179 ? 37.243  -9.239  15.711  1.00 14.36 ? 179 ILE A N   1 
ATOM   1437 C  CA  . ILE A  1 179 ? 35.836  -8.869  15.342  1.00 14.54 ? 179 ILE A CA  1 
ATOM   1438 C  C   . ILE A  1 179 ? 35.239  -9.938  14.432  1.00 14.60 ? 179 ILE A C   1 
ATOM   1439 O  O   . ILE A  1 179 ? 33.979  -10.030 14.376  1.00 13.57 ? 179 ILE A O   1 
ATOM   1440 C  CB  . ILE A  1 179 ? 35.878  -7.514  14.625  1.00 13.78 ? 179 ILE A CB  1 
ATOM   1441 C  CG1 . ILE A  1 179 ? 36.489  -6.406  15.508  1.00 13.78 ? 179 ILE A CG1 1 
ATOM   1442 C  CG2 . ILE A  1 179 ? 34.479  -7.089  14.180  1.00 15.03 ? 179 ILE A CG2 1 
ATOM   1443 C  CD1 . ILE A  1 179 ? 35.848  -6.254  16.902  1.00 16.56 ? 179 ILE A CD1 1 
ATOM   1444 N  N   . GLU A  1 180 ? 35.989  -10.750 13.652  1.00 15.17 ? 180 GLU A N   1 
ATOM   1445 C  CA  . GLU A  1 180 ? 35.358  -11.770 12.871  1.00 14.75 ? 180 GLU A CA  1 
ATOM   1446 C  C   . GLU A  1 180 ? 34.561  -12.819 13.741  1.00 14.31 ? 180 GLU A C   1 
ATOM   1447 O  O   . GLU A  1 180 ? 33.689  -13.494 13.208  1.00 15.90 ? 180 GLU A O   1 
ATOM   1448 C  CB  . GLU A  1 180 ? 36.385  -12.457 11.950  1.00 17.99 ? 180 GLU A CB  1 
ATOM   1449 C  CG  . GLU A  1 180 ? 35.789  -13.127 10.715  1.00 21.28 ? 180 GLU A CG  1 
ATOM   1450 C  CD  . GLU A  1 180 ? 36.840  -13.748 9.833   1.00 24.71 ? 180 GLU A CD  1 
ATOM   1451 O  OE1 . GLU A  1 180 ? 38.015  -13.458 10.058  1.00 27.19 ? 180 GLU A OE1 1 
ATOM   1452 O  OE2 . GLU A  1 180 ? 36.390  -14.546 9.023   1.00 28.44 ? 180 GLU A OE2 1 
ATOM   1453 N  N   . GLU A  1 181 ? 34.882  -12.862 15.069  1.00 15.33 ? 181 GLU A N   1 
ATOM   1454 C  CA  . GLU A  1 181 ? 34.122  -13.754 15.926  1.00 16.95 ? 181 GLU A CA  1 
ATOM   1455 C  C   . GLU A  1 181 ? 32.639  -13.332 16.071  1.00 14.24 ? 181 GLU A C   1 
ATOM   1456 O  O   . GLU A  1 181 ? 31.801  -14.127 16.476  1.00 15.71 ? 181 GLU A O   1 
ATOM   1457 C  CB  . GLU A  1 181 ? 34.709  -13.746 17.321  1.00 18.02 ? 181 GLU A CB  1 
ATOM   1458 C  CG  . GLU A  1 181 ? 36.137  -14.337 17.445  1.00 20.34 ? 181 GLU A CG  1 
ATOM   1459 C  CD  . GLU A  1 181 ? 36.768  -14.084 18.807  1.00 23.86 ? 181 GLU A CD  1 
ATOM   1460 O  OE1 . GLU A  1 181 ? 36.112  -13.608 19.792  1.00 26.33 ? 181 GLU A OE1 1 
ATOM   1461 O  OE2 . GLU A  1 181 ? 38.002  -14.375 18.916  1.00 25.86 ? 181 GLU A OE2 1 
ATOM   1462 N  N   . LEU A  1 182 ? 32.346  -12.080 15.677  1.00 13.22 ? 182 LEU A N   1 
ATOM   1463 C  CA  . LEU A  1 182 ? 30.933  -11.609 15.761  1.00 12.11 ? 182 LEU A CA  1 
ATOM   1464 C  C   . LEU A  1 182 ? 30.169  -11.929 14.522  1.00 12.42 ? 182 LEU A C   1 
ATOM   1465 O  O   . LEU A  1 182 ? 28.943  -11.767 14.528  1.00 13.39 ? 182 LEU A O   1 
ATOM   1466 C  CB  . LEU A  1 182 ? 30.936  -10.098 15.842  1.00 12.82 ? 182 LEU A CB  1 
ATOM   1467 C  CG  . LEU A  1 182 ? 31.714  -9.534  17.007  1.00 12.04 ? 182 LEU A CG  1 
ATOM   1468 C  CD1 . LEU A  1 182 ? 31.635  -8.026  17.116  1.00 12.84 ? 182 LEU A CD1 1 
ATOM   1469 C  CD2 . LEU A  1 182 ? 31.212  -10.090 18.341  1.00 15.36 ? 182 LEU A CD2 1 
ATOM   1470 N  N   . LEU A  1 183 ? 30.812  -12.422 13.484  1.00 12.20 ? 183 LEU A N   1 
ATOM   1471 C  CA  . LEU A  1 183 ? 30.125  -12.854 12.265  1.00 13.05 ? 183 LEU A CA  1 
ATOM   1472 C  C   . LEU A  1 183 ? 29.527  -14.219 12.347  1.00 15.11 ? 183 LEU A C   1 
ATOM   1473 O  O   . LEU A  1 183 ? 30.069  -15.058 13.076  1.00 15.82 ? 183 LEU A O   1 
ATOM   1474 C  CB  . LEU A  1 183 ? 31.105  -12.756 11.027  1.00 13.45 ? 183 LEU A CB  1 
ATOM   1475 C  CG  . LEU A  1 183 ? 31.811  -11.404 10.901  1.00 14.87 ? 183 LEU A CG  1 
ATOM   1476 C  CD1 . LEU A  1 183 ? 32.710  -11.389 9.655   1.00 17.55 ? 183 LEU A CD1 1 
ATOM   1477 C  CD2 . LEU A  1 183 ? 30.770  -10.302 10.719  1.00 14.63 ? 183 LEU A CD2 1 
ATOM   1478 N  N   . PRO A  1 184 ? 28.485  -14.529 11.613  1.00 13.48 ? 184 PRO A N   1 
ATOM   1479 C  CA  . PRO A  1 184 ? 27.831  -15.788 11.633  1.00 14.69 ? 184 PRO A CA  1 
ATOM   1480 C  C   . PRO A  1 184 ? 28.582  -16.832 10.812  1.00 15.70 ? 184 PRO A C   1 
ATOM   1481 O  O   . PRO A  1 184 ? 29.652  -16.561 10.219  1.00 15.95 ? 184 PRO A O   1 
ATOM   1482 C  CB  . PRO A  1 184 ? 26.439  -15.449 11.057  1.00 15.62 ? 184 PRO A CB  1 
ATOM   1483 C  CG  . PRO A  1 184 ? 26.767  -14.387 9.979   1.00 14.58 ? 184 PRO A CG  1 
ATOM   1484 C  CD  . PRO A  1 184 ? 27.813  -13.567 10.705  1.00 14.34 ? 184 PRO A CD  1 
ATOM   1485 N  N   . GLU A  1 185 ? 27.980  -18.027 10.852  1.00 17.86 ? 185 GLU A N   1 
ATOM   1486 C  CA  . GLU A  1 185 ? 28.461  -19.105 10.010  1.00 19.09 ? 185 GLU A CA  1 
ATOM   1487 C  C   . GLU A  1 185 ? 28.210  -18.825 8.542   1.00 21.21 ? 185 GLU A C   1 
ATOM   1488 O  O   . GLU A  1 185 ? 27.211  -18.181 8.202   1.00 18.87 ? 185 GLU A O   1 
ATOM   1489 C  CB  . GLU A  1 185 ? 27.607  -20.375 10.408  1.00 23.10 ? 185 GLU A CB  1 
ATOM   1490 C  CG  . GLU A  1 185 ? 27.986  -20.874 11.806  1.00 32.28 ? 185 GLU A CG  1 
ATOM   1491 C  CD  . GLU A  1 185 ? 29.481  -21.125 11.906  1.00 42.34 ? 185 GLU A CD  1 
ATOM   1492 O  OE1 . GLU A  1 185 ? 29.934  -22.097 11.249  1.00 42.22 ? 185 GLU A OE1 1 
ATOM   1493 O  OE2 . GLU A  1 185 ? 30.209  -20.332 12.574  1.00 44.13 ? 185 GLU A OE2 1 
ATOM   1494 N  N   . ARG A  1 186 ? 29.110  -19.292 7.660   1.00 17.74 ? 186 ARG A N   1 
ATOM   1495 C  CA  . ARG A  1 186 ? 28.903  -19.273 6.242   1.00 20.01 ? 186 ARG A CA  1 
ATOM   1496 C  C   . ARG A  1 186 ? 28.621  -17.826 5.780   1.00 16.05 ? 186 ARG A C   1 
ATOM   1497 O  O   . ARG A  1 186 ? 27.632  -17.539 5.103   1.00 16.69 ? 186 ARG A O   1 
ATOM   1498 C  CB  . ARG A  1 186 ? 27.802  -20.244 5.781   1.00 22.02 ? 186 ARG A CB  1 
ATOM   1499 C  CG  . ARG A  1 186 ? 28.190  -21.664 6.249   1.00 27.21 ? 186 ARG A CG  1 
ATOM   1500 C  CD  . ARG A  1 186 ? 27.352  -22.784 5.649   1.00 27.88 ? 186 ARG A CD  1 
ATOM   1501 N  NE  . ARG A  1 186 ? 25.926  -22.540 5.645   1.00 32.24 ? 186 ARG A NE  1 
ATOM   1502 C  CZ  . ARG A  1 186 ? 25.112  -22.634 6.695   1.00 39.16 ? 186 ARG A CZ  1 
ATOM   1503 N  NH1 . ARG A  1 186 ? 25.573  -22.959 7.902   1.00 39.49 ? 186 ARG A NH1 1 
ATOM   1504 N  NH2 . ARG A  1 186 ? 23.815  -22.382 6.520   1.00 45.07 ? 186 ARG A NH2 1 
ATOM   1505 N  N   . THR A  1 187 ? 29.604  -17.018 6.107   1.00 14.91 ? 187 THR A N   1 
ATOM   1506 C  CA  . THR A  1 187 ? 29.645  -15.614 5.653   1.00 15.71 ? 187 THR A CA  1 
ATOM   1507 C  C   . THR A  1 187 ? 29.630  -15.511 4.154   1.00 15.78 ? 187 THR A C   1 
ATOM   1508 O  O   . THR A  1 187 ? 29.269  -14.454 3.648   1.00 15.50 ? 187 THR A O   1 
ATOM   1509 C  CB  . THR A  1 187 ? 30.756  -14.735 6.185   1.00 16.12 ? 187 THR A CB  1 
ATOM   1510 O  OG1 . THR A  1 187 ? 31.991  -15.415 6.034   1.00 18.23 ? 187 THR A OG1 1 
ATOM   1511 C  CG2 . THR A  1 187 ? 30.560  -14.457 7.715   1.00 15.99 ? 187 THR A CG2 1 
ATOM   1512 N  N   . ALA A  1 188 ? 30.001  -16.561 3.396   1.00 15.58 ? 188 ALA A N   1 
ATOM   1513 C  CA  . ALA A  1 188 ? 29.811  -16.492 1.935   1.00 16.22 ? 188 ALA A CA  1 
ATOM   1514 C  C   . ALA A  1 188 ? 28.330  -16.263 1.508   1.00 15.39 ? 188 ALA A C   1 
ATOM   1515 O  O   . ALA A  1 188 ? 28.104  -15.891 0.331   1.00 16.33 ? 188 ALA A O   1 
ATOM   1516 C  CB  . ALA A  1 188 ? 30.335  -17.810 1.303   1.00 18.57 ? 188 ALA A CB  1 
ATOM   1517 N  N   . GLU A  1 189 ? 27.371  -16.583 2.426   1.00 15.34 ? 189 GLU A N   1 
ATOM   1518 C  CA  . GLU A  1 189 ? 25.919  -16.544 2.143   1.00 14.74 ? 189 GLU A CA  1 
ATOM   1519 C  C   . GLU A  1 189 ? 25.410  -15.195 2.641   1.00 12.72 ? 189 GLU A C   1 
ATOM   1520 O  O   . GLU A  1 189 ? 25.374  -14.939 3.840   1.00 13.02 ? 189 GLU A O   1 
ATOM   1521 C  CB  . GLU A  1 189 ? 25.108  -17.696 2.770   1.00 16.65 ? 189 GLU A CB  1 
ATOM   1522 C  CG  . GLU A  1 189 ? 25.545  -19.076 2.249   1.00 22.45 ? 189 GLU A CG  1 
ATOM   1523 C  CD  . GLU A  1 189 ? 25.018  -20.214 3.107   1.00 25.61 ? 189 GLU A CD  1 
ATOM   1524 O  OE1 . GLU A  1 189 ? 24.264  -20.019 4.107   1.00 24.68 ? 189 GLU A OE1 1 
ATOM   1525 O  OE2 . GLU A  1 189 ? 25.474  -21.411 2.895   1.00 29.35 ? 189 GLU A OE2 1 
ATOM   1526 N  N   . TYR A  1 190 ? 25.021  -14.348 1.695   1.00 12.02 ? 190 TYR A N   1 
ATOM   1527 C  CA  . TYR A  1 190 ? 24.511  -12.993 2.079   1.00 11.51 ? 190 TYR A CA  1 
ATOM   1528 C  C   . TYR A  1 190 ? 23.557  -12.396 1.075   1.00 11.96 ? 190 TYR A C   1 
ATOM   1529 O  O   . TYR A  1 190 ? 23.464  -12.803 -0.114  1.00 12.53 ? 190 TYR A O   1 
ATOM   1530 C  CB  . TYR A  1 190 ? 25.724  -12.017 2.358   1.00 11.34 ? 190 TYR A CB  1 
ATOM   1531 C  CG  . TYR A  1 190 ? 26.617  -11.860 1.144   1.00 12.14 ? 190 TYR A CG  1 
ATOM   1532 C  CD1 . TYR A  1 190 ? 26.319  -10.965 0.139   1.00 12.24 ? 190 TYR A CD1 1 
ATOM   1533 C  CD2 . TYR A  1 190 ? 27.848  -12.580 1.052   1.00 14.49 ? 190 TYR A CD2 1 
ATOM   1534 C  CE1 . TYR A  1 190 ? 27.156  -10.737 -0.956  1.00 14.07 ? 190 TYR A CE1 1 
ATOM   1535 C  CE2 . TYR A  1 190 ? 28.695  -12.370 -0.065  1.00 13.93 ? 190 TYR A CE2 1 
ATOM   1536 C  CZ  . TYR A  1 190 ? 28.336  -11.466 -1.014  1.00 13.22 ? 190 TYR A CZ  1 
ATOM   1537 O  OH  . TYR A  1 190 ? 29.216  -11.279 -2.110  1.00 14.84 ? 190 TYR A OH  1 
ATOM   1538 N  N   . TYR A  1 191 ? 22.826  -11.380 1.544   1.00 11.73 ? 191 TYR A N   1 
ATOM   1539 C  CA  . TYR A  1 191 ? 21.988  -10.483 0.737   1.00 10.20 ? 191 TYR A CA  1 
ATOM   1540 C  C   . TYR A  1 191 ? 22.731  -9.225  0.468   1.00 11.14 ? 191 TYR A C   1 
ATOM   1541 O  O   . TYR A  1 191 ? 23.477  -8.754  1.341   1.00 12.29 ? 191 TYR A O   1 
ATOM   1542 C  CB  . TYR A  1 191 ? 20.690  -10.098 1.491   1.00 11.87 ? 191 TYR A CB  1 
ATOM   1543 C  CG  . TYR A  1 191 ? 19.887  -11.231 2.076   1.00 10.83 ? 191 TYR A CG  1 
ATOM   1544 C  CD1 . TYR A  1 191 ? 18.812  -11.817 1.341   1.00 11.75 ? 191 TYR A CD1 1 
ATOM   1545 C  CD2 . TYR A  1 191 ? 20.133  -11.666 3.430   1.00 11.20 ? 191 TYR A CD2 1 
ATOM   1546 C  CE1 . TYR A  1 191 ? 18.028  -12.815 1.953   1.00 11.94 ? 191 TYR A CE1 1 
ATOM   1547 C  CE2 . TYR A  1 191 ? 19.359  -12.672 4.017   1.00 11.96 ? 191 TYR A CE2 1 
ATOM   1548 C  CZ  . TYR A  1 191 ? 18.366  -13.218 3.263   1.00 12.60 ? 191 TYR A CZ  1 
ATOM   1549 O  OH  . TYR A  1 191 ? 17.520  -14.238 3.785   1.00 16.49 ? 191 TYR A OH  1 
ATOM   1550 N  N   . ARG A  1 192 ? 22.546  -8.647  -0.706  1.00 11.92 ? 192 ARG A N   1 
ATOM   1551 C  CA  . ARG A  1 192 ? 23.304  -7.455  -1.057  1.00 10.65 ? 192 ARG A CA  1 
ATOM   1552 C  C   . ARG A  1 192 ? 22.365  -6.490  -1.807  1.00 10.94 ? 192 ARG A C   1 
ATOM   1553 O  O   . ARG A  1 192 ? 21.639  -6.891  -2.737  1.00 12.51 ? 192 ARG A O   1 
ATOM   1554 C  CB  . ARG A  1 192 ? 24.415  -7.885  -2.026  1.00 12.75 ? 192 ARG A CB  1 
ATOM   1555 C  CG  . ARG A  1 192 ? 25.060  -6.764  -2.878  1.00 14.21 ? 192 ARG A CG  1 
ATOM   1556 C  CD  . ARG A  1 192 ? 25.923  -5.764  -2.048  1.00 14.52 ? 192 ARG A CD  1 
ATOM   1557 N  NE  . ARG A  1 192 ? 26.903  -6.413  -1.149  1.00 14.76 ? 192 ARG A NE  1 
ATOM   1558 C  CZ  . ARG A  1 192 ? 28.016  -7.030  -1.544  1.00 15.60 ? 192 ARG A CZ  1 
ATOM   1559 N  NH1 . ARG A  1 192 ? 28.373  -7.009  -2.877  1.00 17.65 ? 192 ARG A NH1 1 
ATOM   1560 N  NH2 . ARG A  1 192 ? 28.843  -7.594  -0.632  1.00 15.93 ? 192 ARG A NH2 1 
ATOM   1561 N  N   . TYR A  1 193 ? 22.386  -5.224  -1.371  1.00 9.96  ? 193 TYR A N   1 
ATOM   1562 C  CA  . TYR A  1 193 ? 21.552  -4.198  -2.102  1.00 10.99 ? 193 TYR A CA  1 
ATOM   1563 C  C   . TYR A  1 193 ? 22.151  -2.873  -1.815  1.00 10.77 ? 193 TYR A C   1 
ATOM   1564 O  O   . TYR A  1 193 ? 22.846  -2.622  -0.801  1.00 12.17 ? 193 TYR A O   1 
ATOM   1565 C  CB  . TYR A  1 193 ? 20.059  -4.306  -1.745  1.00 11.18 ? 193 TYR A CB  1 
ATOM   1566 C  CG  . TYR A  1 193 ? 19.673  -3.748  -0.353  1.00 9.20  ? 193 TYR A CG  1 
ATOM   1567 C  CD1 . TYR A  1 193 ? 19.884  -4.514  0.825   1.00 9.50  ? 193 TYR A CD1 1 
ATOM   1568 C  CD2 . TYR A  1 193 ? 19.115  -2.476  -0.226  1.00 10.86 ? 193 TYR A CD2 1 
ATOM   1569 C  CE1 . TYR A  1 193 ? 19.584  -3.996  2.063   1.00 10.32 ? 193 TYR A CE1 1 
ATOM   1570 C  CE2 . TYR A  1 193 ? 18.845  -1.904  0.999   1.00 9.72  ? 193 TYR A CE2 1 
ATOM   1571 C  CZ  . TYR A  1 193 ? 19.059  -2.697  2.149   1.00 10.25 ? 193 TYR A CZ  1 
ATOM   1572 O  OH  . TYR A  1 193 ? 18.756  -2.142  3.342   1.00 9.33  ? 193 TYR A OH  1 
ATOM   1573 N  N   . ARG A  1 194 ? 21.796  -1.894  -2.649  1.00 11.03 ? 194 ARG A N   1 
ATOM   1574 C  CA  . ARG A  1 194 ? 22.171  -0.477  -2.429  1.00 10.42 ? 194 ARG A CA  1 
ATOM   1575 C  C   . ARG A  1 194 ? 21.090  0.241   -1.643  1.00 10.84 ? 194 ARG A C   1 
ATOM   1576 O  O   . ARG A  1 194 ? 19.849  0.205   -1.944  1.00 12.34 ? 194 ARG A O   1 
ATOM   1577 C  CB  . ARG A  1 194 ? 22.262  0.216   -3.816  1.00 14.31 ? 194 ARG A CB  1 
ATOM   1578 C  CG  . ARG A  1 194 ? 23.531  -0.209  -4.529  1.00 20.06 ? 194 ARG A CG  1 
ATOM   1579 C  CD  . ARG A  1 194 ? 23.807  0.743   -5.735  1.00 28.86 ? 194 ARG A CD  1 
ATOM   1580 N  N   . GLY A  1 195 ? 21.496  0.863   -0.521  1.00 9.79  ? 195 GLY A N   1 
ATOM   1581 C  CA  . GLY A  1 195 ? 20.576  1.539   0.349   1.00 10.69 ? 195 GLY A CA  1 
ATOM   1582 C  C   . GLY A  1 195 ? 21.154  2.705   1.029   1.00 9.69  ? 195 GLY A C   1 
ATOM   1583 O  O   . GLY A  1 195 ? 22.000  3.468   0.478   1.00 9.95  ? 195 GLY A O   1 
ATOM   1584 N  N   . SER A  1 196 ? 20.751  2.888   2.263   1.00 9.08  ? 196 SER A N   1 
ATOM   1585 C  CA  . SER A  1 196 ? 21.025  4.133   2.966   1.00 8.98  ? 196 SER A CA  1 
ATOM   1586 C  C   . SER A  1 196 ? 21.458  3.881   4.417   1.00 9.52  ? 196 SER A C   1 
ATOM   1587 O  O   . SER A  1 196 ? 21.253  2.753   4.934   1.00 9.37  ? 196 SER A O   1 
ATOM   1588 C  CB  . SER A  1 196 ? 19.795  5.076   3.026   1.00 9.58  ? 196 SER A CB  1 
ATOM   1589 O  OG  . SER A  1 196 ? 18.828  4.637   4.015   1.00 8.81  ? 196 SER A OG  1 
ATOM   1590 N  N   . LEU A  1 197 ? 22.010  4.894   5.074   1.00 9.58  ? 197 LEU A N   1 
ATOM   1591 C  CA  . LEU A  1 197 ? 22.103  4.920   6.550   1.00 9.40  ? 197 LEU A CA  1 
ATOM   1592 C  C   . LEU A  1 197 ? 20.676  4.727   7.092   1.00 8.94  ? 197 LEU A C   1 
ATOM   1593 O  O   . LEU A  1 197 ? 19.698  5.324   6.531   1.00 9.08  ? 197 LEU A O   1 
ATOM   1594 C  CB  . LEU A  1 197 ? 22.716  6.222   7.077   1.00 11.12 ? 197 LEU A CB  1 
ATOM   1595 C  CG  . LEU A  1 197 ? 24.099  6.523   6.560   1.00 12.20 ? 197 LEU A CG  1 
ATOM   1596 C  CD1 . LEU A  1 197 ? 24.483  7.861   7.127   1.00 13.57 ? 197 LEU A CD1 1 
ATOM   1597 C  CD2 . LEU A  1 197 ? 25.064  5.472   7.066   1.00 11.80 ? 197 LEU A CD2 1 
ATOM   1598 N  N   . THR A  1 198 ? 20.500  4.000   8.180   1.00 9.12  ? 198 THR A N   1 
ATOM   1599 C  CA  . THR A  1 198 ? 19.175  3.825   8.753   1.00 9.67  ? 198 THR A CA  1 
ATOM   1600 C  C   . THR A  1 198 ? 18.852  4.814   9.833   1.00 9.06  ? 198 THR A C   1 
ATOM   1601 O  O   . THR A  1 198 ? 17.824  4.712   10.505  1.00 9.86  ? 198 THR A O   1 
ATOM   1602 C  CB  . THR A  1 198 ? 19.017  2.389   9.299   1.00 9.38  ? 198 THR A CB  1 
ATOM   1603 O  OG1 . THR A  1 198 ? 19.899  2.237   10.424  1.00 9.20  ? 198 THR A OG1 1 
ATOM   1604 C  CG2 . THR A  1 198 ? 19.270  1.283   8.261   1.00 9.40  ? 198 THR A CG2 1 
ATOM   1605 N  N   . THR A  1 199 ? 19.783  5.727   10.060  1.00 9.32  ? 199 THR A N   1 
ATOM   1606 C  CA  . THR A  1 199 ? 19.529  6.836   10.919  1.00 9.64  ? 199 THR A CA  1 
ATOM   1607 C  C   . THR A  1 199 ? 19.885  8.134   10.221  1.00 10.57 ? 199 THR A C   1 
ATOM   1608 O  O   . THR A  1 199 ? 20.568  8.058   9.205   1.00 10.57 ? 199 THR A O   1 
ATOM   1609 C  CB  . THR A  1 199 ? 20.348  6.904   12.227  1.00 11.21 ? 199 THR A CB  1 
ATOM   1610 O  OG1 . THR A  1 199 ? 21.694  7.152   11.907  1.00 14.03 ? 199 THR A OG1 1 
ATOM   1611 C  CG2 . THR A  1 199 ? 20.399  5.553   12.959  1.00 12.22 ? 199 THR A CG2 1 
ATOM   1612 N  N   . PRO A  1 200 ? 19.364  9.252   10.775  1.00 10.12 ? 200 PRO A N   1 
ATOM   1613 C  CA  . PRO A  1 200 ? 19.819  10.519  10.160  1.00 10.85 ? 200 PRO A CA  1 
ATOM   1614 C  C   . PRO A  1 200 ? 21.372  10.518  10.079  1.00 11.35 ? 200 PRO A C   1 
ATOM   1615 O  O   . PRO A  1 200 ? 21.991  10.015  11.030  1.00 13.06 ? 200 PRO A O   1 
ATOM   1616 C  CB  . PRO A  1 200 ? 19.254  11.558  11.173  1.00 10.73 ? 200 PRO A CB  1 
ATOM   1617 C  CG  . PRO A  1 200 ? 17.986  10.938  11.678  1.00 10.19 ? 200 PRO A CG  1 
ATOM   1618 C  CD  . PRO A  1 200 ? 18.416  9.462   11.837  1.00 10.67 ? 200 PRO A CD  1 
ATOM   1619 N  N   . PRO A  1 201 ? 21.896  11.039  9.006   1.00 10.47 ? 201 PRO A N   1 
ATOM   1620 C  CA  . PRO A  1 201 ? 21.210  11.861  7.956   1.00 11.86 ? 201 PRO A CA  1 
ATOM   1621 C  C   . PRO A  1 201 ? 20.567  11.043  6.852   1.00 10.40 ? 201 PRO A C   1 
ATOM   1622 O  O   . PRO A  1 201 ? 20.155  11.576  5.834   1.00 11.43 ? 201 PRO A O   1 
ATOM   1623 C  CB  . PRO A  1 201 ? 22.361  12.708  7.349   1.00 12.81 ? 201 PRO A CB  1 
ATOM   1624 C  CG  . PRO A  1 201 ? 23.631  11.883  7.658   1.00 15.41 ? 201 PRO A CG  1 
ATOM   1625 C  CD  . PRO A  1 201 ? 23.369  11.216  8.979   1.00 12.70 ? 201 PRO A CD  1 
ATOM   1626 N  N   . CYS A  1 202 ? 20.603  9.680   6.930   1.00 10.27 ? 202 CYS A N   1 
ATOM   1627 C  CA  . CYS A  1 202 ? 19.924  8.750   5.977   1.00 9.87  ? 202 CYS A CA  1 
ATOM   1628 C  C   . CYS A  1 202 ? 20.495  8.812   4.562   1.00 9.79  ? 202 CYS A C   1 
ATOM   1629 O  O   . CYS A  1 202 ? 19.792  8.566   3.588   1.00 10.95 ? 202 CYS A O   1 
ATOM   1630 C  CB  . CYS A  1 202 ? 18.403  9.091   5.905   1.00 11.53 ? 202 CYS A CB  1 
ATOM   1631 S  SG  . CYS A  1 202 ? 17.515  8.964   7.470   1.00 11.23 ? 202 CYS A SG  1 
ATOM   1632 N  N   A ASN A  1 203 ? 21.782  9.164   4.458   0.50 10.31 ? 203 ASN A N   1 
ATOM   1633 N  N   B ASN A  1 203 ? 21.785  9.128   4.437   0.50 10.59 ? 203 ASN A N   1 
ATOM   1634 C  CA  A ASN A  1 203 ? 22.396  9.319   3.147   0.50 10.90 ? 203 ASN A CA  1 
ATOM   1635 C  CA  B ASN A  1 203 ? 22.321  9.256   3.088   0.50 11.32 ? 203 ASN A CA  1 
ATOM   1636 C  C   A ASN A  1 203 ? 22.261  8.018   2.350   0.50 10.58 ? 203 ASN A C   1 
ATOM   1637 C  C   B ASN A  1 203 ? 22.255  7.985   2.325   0.50 10.98 ? 203 ASN A C   1 
ATOM   1638 O  O   A ASN A  1 203 ? 22.529  6.924   2.900   0.50 10.32 ? 203 ASN A O   1 
ATOM   1639 O  O   B ASN A  1 203 ? 22.563  6.891   2.857   0.50 10.46 ? 203 ASN A O   1 
ATOM   1640 C  CB  A ASN A  1 203 ? 23.928  9.569   3.311   0.50 12.82 ? 203 ASN A CB  1 
ATOM   1641 C  CB  B ASN A  1 203 ? 23.796  9.681   3.106   0.50 14.57 ? 203 ASN A CB  1 
ATOM   1642 C  CG  A ASN A  1 203 ? 24.248  10.812  4.097   0.50 13.11 ? 203 ASN A CG  1 
ATOM   1643 C  CG  B ASN A  1 203 ? 23.960  10.927  3.864   0.50 14.36 ? 203 ASN A CG  1 
ATOM   1644 O  OD1 A ASN A  1 203 ? 23.459  11.778  4.220   0.50 13.67 ? 203 ASN A OD1 1 
ATOM   1645 O  OD1 B ASN A  1 203 ? 23.644  10.973  5.074   0.50 16.90 ? 203 ASN A OD1 1 
ATOM   1646 N  ND2 A ASN A  1 203 ? 25.439  10.812  4.668   0.50 14.61 ? 203 ASN A ND2 1 
ATOM   1647 N  ND2 B ASN A  1 203 ? 24.311  12.000  3.156   0.50 16.06 ? 203 ASN A ND2 1 
ATOM   1648 N  N   . PRO A  1 204 ? 21.885  8.062   1.046   1.00 10.96 ? 204 PRO A N   1 
ATOM   1649 C  CA  . PRO A  1 204 ? 21.697  6.904   0.237   1.00 11.37 ? 204 PRO A CA  1 
ATOM   1650 C  C   . PRO A  1 204 ? 22.970  6.392   -0.378  1.00 11.09 ? 204 PRO A C   1 
ATOM   1651 O  O   . PRO A  1 204 ? 23.116  6.261   -1.611  1.00 13.85 ? 204 PRO A O   1 
ATOM   1652 C  CB  . PRO A  1 204 ? 20.691  7.343   -0.880  1.00 12.90 ? 204 PRO A CB  1 
ATOM   1653 C  CG  . PRO A  1 204 ? 21.131  8.783   -1.057  1.00 12.18 ? 204 PRO A CG  1 
ATOM   1654 C  CD  . PRO A  1 204 ? 21.393  9.306   0.344   1.00 11.21 ? 204 PRO A CD  1 
ATOM   1655 N  N   . THR A  1 205 ? 23.951  6.195   0.490   1.00 11.78 ? 205 THR A N   1 
ATOM   1656 C  CA  . THR A  1 205 ? 25.340  5.907   -0.014  1.00 11.21 ? 205 THR A CA  1 
ATOM   1657 C  C   . THR A  1 205 ? 25.892  4.602   0.563   1.00 11.05 ? 205 THR A C   1 
ATOM   1658 O  O   . THR A  1 205 ? 27.080  4.397   0.545   1.00 11.64 ? 205 THR A O   1 
ATOM   1659 C  CB  . THR A  1 205 ? 26.205  7.020   0.572   1.00 11.93 ? 205 THR A CB  1 
ATOM   1660 O  OG1 . THR A  1 205 ? 26.015  7.104   1.953   1.00 12.38 ? 205 THR A OG1 1 
ATOM   1661 C  CG2 . THR A  1 205 ? 25.779  8.401   -0.097  1.00 13.73 ? 205 THR A CG2 1 
ATOM   1662 N  N   . VAL A  1 206 ? 24.986  3.681   0.986   1.00 10.02 ? 206 VAL A N   1 
ATOM   1663 C  CA  . VAL A  1 206 ? 25.437  2.406   1.603   1.00 10.28 ? 206 VAL A CA  1 
ATOM   1664 C  C   . VAL A  1 206 ? 25.256  1.247   0.759   1.00 10.24 ? 206 VAL A C   1 
ATOM   1665 O  O   . VAL A  1 206 ? 24.159  0.939   0.294   1.00 10.96 ? 206 VAL A O   1 
ATOM   1666 C  CB  . VAL A  1 206 ? 24.725  2.196   2.977   1.00 9.73  ? 206 VAL A CB  1 
ATOM   1667 C  CG1 . VAL A  1 206 ? 25.138  0.851   3.558   1.00 10.07 ? 206 VAL A CG1 1 
ATOM   1668 C  CG2 . VAL A  1 206 ? 24.994  3.348   3.963   1.00 9.82  ? 206 VAL A CG2 1 
ATOM   1669 N  N   . LEU A  1 207 ? 26.323  0.501   0.555   1.00 10.01 ? 207 LEU A N   1 
ATOM   1670 C  CA  . LEU A  1 207 ? 26.279  -0.858  0.015   1.00 11.03 ? 207 LEU A CA  1 
ATOM   1671 C  C   . LEU A  1 207 ? 26.056  -1.812  1.142   1.00 10.71 ? 207 LEU A C   1 
ATOM   1672 O  O   . LEU A  1 207 ? 26.937  -1.946  1.992   1.00 11.41 ? 207 LEU A O   1 
ATOM   1673 C  CB  . LEU A  1 207 ? 27.550  -1.176  -0.750  1.00 14.29 ? 207 LEU A CB  1 
ATOM   1674 C  CG  . LEU A  1 207 ? 27.384  -2.504  -1.518  1.00 15.66 ? 207 LEU A CG  1 
ATOM   1675 C  CD1 . LEU A  1 207 ? 26.378  -2.372  -2.702  1.00 18.47 ? 207 LEU A CD1 1 
ATOM   1676 C  CD2 . LEU A  1 207 ? 28.735  -2.960  -2.038  1.00 21.17 ? 207 LEU A CD2 1 
ATOM   1677 N  N   . TRP A  1 208 ? 24.860  -2.377  1.219   1.00 9.76  ? 208 TRP A N   1 
ATOM   1678 C  CA  . TRP A  1 208 ? 24.492  -3.299  2.345   1.00 9.69  ? 208 TRP A CA  1 
ATOM   1679 C  C   . TRP A  1 208 ? 24.875  -4.707  2.029   1.00 9.75  ? 208 TRP A C   1 
ATOM   1680 O  O   . TRP A  1 208 ? 24.607  -5.228  0.899   1.00 10.60 ? 208 TRP A O   1 
ATOM   1681 C  CB  . TRP A  1 208 ? 22.978  -3.232  2.616   1.00 10.10 ? 208 TRP A CB  1 
ATOM   1682 C  CG  . TRP A  1 208 ? 22.631  -2.056  3.431   1.00 9.65  ? 208 TRP A CG  1 
ATOM   1683 C  CD1 . TRP A  1 208 ? 22.117  -0.828  2.967   1.00 9.13  ? 208 TRP A CD1 1 
ATOM   1684 C  CD2 . TRP A  1 208 ? 22.756  -1.924  4.841   1.00 9.33  ? 208 TRP A CD2 1 
ATOM   1685 N  NE1 . TRP A  1 208 ? 21.972  0.046   3.998   1.00 9.07  ? 208 TRP A NE1 1 
ATOM   1686 C  CE2 . TRP A  1 208 ? 22.322  -0.600  5.201   1.00 9.17  ? 208 TRP A CE2 1 
ATOM   1687 C  CE3 . TRP A  1 208 ? 23.150  -2.784  5.863   1.00 9.80  ? 208 TRP A CE3 1 
ATOM   1688 C  CZ2 . TRP A  1 208 ? 22.353  -0.133  6.489   1.00 9.33  ? 208 TRP A CZ2 1 
ATOM   1689 C  CZ3 . TRP A  1 208 ? 23.192  -2.309  7.153   1.00 9.28  ? 208 TRP A CZ3 1 
ATOM   1690 C  CH2 . TRP A  1 208 ? 22.841  -0.979  7.484   1.00 9.11  ? 208 TRP A CH2 1 
ATOM   1691 N  N   . THR A  1 209 ? 25.406  -5.382  3.073   1.00 8.54  ? 209 THR A N   1 
ATOM   1692 C  CA  . THR A  1 209 ? 25.646  -6.839  2.989   1.00 9.63  ? 209 THR A CA  1 
ATOM   1693 C  C   . THR A  1 209 ? 24.983  -7.370  4.258   1.00 9.69  ? 209 THR A C   1 
ATOM   1694 O  O   . THR A  1 209 ? 25.490  -7.038  5.376   1.00 10.43 ? 209 THR A O   1 
ATOM   1695 C  CB  . THR A  1 209 ? 27.129  -7.211  2.996   1.00 9.87  ? 209 THR A CB  1 
ATOM   1696 O  OG1 . THR A  1 209 ? 27.711  -6.651  1.787   1.00 10.92 ? 209 THR A OG1 1 
ATOM   1697 C  CG2 . THR A  1 209 ? 27.279  -8.731  2.911   1.00 11.87 ? 209 THR A CG2 1 
ATOM   1698 N  N   . VAL A  1 210 ? 23.908  -8.156  4.099   1.00 9.17  ? 210 VAL A N   1 
ATOM   1699 C  CA  . VAL A  1 210 ? 23.217  -8.703  5.307   1.00 9.48  ? 210 VAL A CA  1 
ATOM   1700 C  C   . VAL A  1 210 ? 23.461  -10.187 5.243   1.00 10.24 ? 210 VAL A C   1 
ATOM   1701 O  O   . VAL A  1 210 ? 23.126  -10.853 4.293   1.00 10.53 ? 210 VAL A O   1 
ATOM   1702 C  CB  . VAL A  1 210 ? 21.690  -8.413  5.288   1.00 9.01  ? 210 VAL A CB  1 
ATOM   1703 C  CG1 . VAL A  1 210 ? 21.091  -9.041  6.571   1.00 9.29  ? 210 VAL A CG1 1 
ATOM   1704 C  CG2 . VAL A  1 210 ? 21.407  -6.953  5.152   1.00 9.70  ? 210 VAL A CG2 1 
ATOM   1705 N  N   . PHE A  1 211 ? 24.207  -10.707 6.235   1.00 10.12 ? 211 PHE A N   1 
ATOM   1706 C  CA  . PHE A  1 211 ? 24.487  -12.169 6.194   1.00 10.89 ? 211 PHE A CA  1 
ATOM   1707 C  C   . PHE A  1 211 ? 23.230  -12.991 6.311   1.00 10.68 ? 211 PHE A C   1 
ATOM   1708 O  O   . PHE A  1 211 ? 22.333  -12.658 7.098   1.00 11.59 ? 211 PHE A O   1 
ATOM   1709 C  CB  . PHE A  1 211 ? 25.544  -12.511 7.253   1.00 10.15 ? 211 PHE A CB  1 
ATOM   1710 C  CG  . PHE A  1 211 ? 26.853  -11.856 6.991   1.00 9.89  ? 211 PHE A CG  1 
ATOM   1711 C  CD1 . PHE A  1 211 ? 27.659  -12.310 5.893   1.00 11.00 ? 211 PHE A CD1 1 
ATOM   1712 C  CD2 . PHE A  1 211 ? 27.379  -10.801 7.824   1.00 10.85 ? 211 PHE A CD2 1 
ATOM   1713 C  CE1 . PHE A  1 211 ? 28.869  -11.651 5.590   1.00 13.20 ? 211 PHE A CE1 1 
ATOM   1714 C  CE2 . PHE A  1 211 ? 28.591  -10.194 7.476   1.00 11.34 ? 211 PHE A CE2 1 
ATOM   1715 C  CZ  . PHE A  1 211 ? 29.331  -10.629 6.380   1.00 11.96 ? 211 PHE A CZ  1 
ATOM   1716 N  N   A ARG A  1 212 ? 23.163  -14.080 5.525   0.50 11.55 ? 212 ARG A N   1 
ATOM   1717 N  N   B ARG A  1 212 ? 23.155  -14.092 5.530   0.50 12.00 ? 212 ARG A N   1 
ATOM   1718 C  CA  A ARG A  1 212 ? 22.006  -14.957 5.551   0.50 12.22 ? 212 ARG A CA  1 
ATOM   1719 C  CA  B ARG A  1 212 ? 21.972  -14.962 5.564   0.50 13.01 ? 212 ARG A CA  1 
ATOM   1720 C  C   A ARG A  1 212 ? 21.727  -15.591 6.943   0.50 11.76 ? 212 ARG A C   1 
ATOM   1721 C  C   B ARG A  1 212 ? 21.718  -15.591 6.956   0.50 12.20 ? 212 ARG A C   1 
ATOM   1722 O  O   A ARG A  1 212 ? 20.562  -15.670 7.329   0.50 13.19 ? 212 ARG A O   1 
ATOM   1723 O  O   B ARG A  1 212 ? 20.559  -15.666 7.358   0.50 13.66 ? 212 ARG A O   1 
ATOM   1724 C  CB  A ARG A  1 212 ? 22.226  -16.074 4.555   0.50 12.76 ? 212 ARG A CB  1 
ATOM   1725 C  CB  B ARG A  1 212 ? 22.099  -16.086 4.539   0.50 14.58 ? 212 ARG A CB  1 
ATOM   1726 C  CG  A ARG A  1 212 ? 21.042  -17.017 4.520   0.50 13.15 ? 212 ARG A CG  1 
ATOM   1727 C  CG  B ARG A  1 212 ? 20.775  -16.823 4.309   0.50 15.31 ? 212 ARG A CG  1 
ATOM   1728 C  CD  A ARG A  1 212 ? 21.456  -18.284 3.789   0.50 13.40 ? 212 ARG A CD  1 
ATOM   1729 C  CD  B ARG A  1 212 ? 21.013  -18.072 3.483   0.50 18.47 ? 212 ARG A CD  1 
ATOM   1730 N  NE  A ARG A  1 212 ? 20.266  -19.169 3.624   0.50 14.97 ? 212 ARG A NE  1 
ATOM   1731 N  NE  B ARG A  1 212 ? 19.729  -18.584 2.975   0.50 20.97 ? 212 ARG A NE  1 
ATOM   1732 C  CZ  A ARG A  1 212 ? 19.949  -20.198 4.413   0.50 18.74 ? 212 ARG A CZ  1 
ATOM   1733 C  CZ  B ARG A  1 212 ? 19.628  -19.647 2.166   0.50 21.81 ? 212 ARG A CZ  1 
ATOM   1734 N  NH1 A ARG A  1 212 ? 20.730  -20.561 5.418   0.50 18.11 ? 212 ARG A NH1 1 
ATOM   1735 N  NH1 B ARG A  1 212 ? 20.731  -20.269 1.825   0.50 23.38 ? 212 ARG A NH1 1 
ATOM   1736 N  NH2 A ARG A  1 212 ? 18.843  -20.888 4.157   0.50 19.11 ? 212 ARG A NH2 1 
ATOM   1737 N  NH2 B ARG A  1 212 ? 18.423  -20.061 1.706   0.50 21.95 ? 212 ARG A NH2 1 
ATOM   1738 N  N   . ASN A  1 213 ? 22.780  -15.991 7.666   1.00 12.05 ? 213 ASN A N   1 
ATOM   1739 C  CA  . ASN A  1 213 ? 22.589  -16.751 8.939   1.00 12.85 ? 213 ASN A CA  1 
ATOM   1740 C  C   . ASN A  1 213 ? 22.725  -15.818 10.121  1.00 12.25 ? 213 ASN A C   1 
ATOM   1741 O  O   . ASN A  1 213 ? 23.681  -15.057 10.154  1.00 13.11 ? 213 ASN A O   1 
ATOM   1742 C  CB  . ASN A  1 213 ? 23.666  -17.866 8.932   1.00 14.83 ? 213 ASN A CB  1 
ATOM   1743 C  CG  . ASN A  1 213 ? 23.493  -18.784 7.731   1.00 16.27 ? 213 ASN A CG  1 
ATOM   1744 O  OD1 . ASN A  1 213 ? 22.378  -19.194 7.381   1.00 21.17 ? 213 ASN A OD1 1 
ATOM   1745 N  ND2 . ASN A  1 213 ? 24.588  -19.021 7.038   1.00 17.93 ? 213 ASN A ND2 1 
ATOM   1746 N  N   . PRO A  1 214 ? 21.834  -16.004 11.133  1.00 12.79 ? 214 PRO A N   1 
ATOM   1747 C  CA  . PRO A  1 214 ? 21.979  -15.221 12.312  1.00 13.31 ? 214 PRO A CA  1 
ATOM   1748 C  C   . PRO A  1 214 ? 23.054  -15.855 13.270  1.00 12.17 ? 214 PRO A C   1 
ATOM   1749 O  O   . PRO A  1 214 ? 23.514  -17.035 13.127  1.00 14.43 ? 214 PRO A O   1 
ATOM   1750 C  CB  . PRO A  1 214 ? 20.629  -15.386 13.008  1.00 14.38 ? 214 PRO A CB  1 
ATOM   1751 C  CG  . PRO A  1 214 ? 20.304  -16.839 12.628  1.00 17.53 ? 214 PRO A CG  1 
ATOM   1752 C  CD  . PRO A  1 214 ? 20.677  -16.924 11.154  1.00 14.47 ? 214 PRO A CD  1 
ATOM   1753 N  N   . VAL A  1 215 ? 23.458  -15.043 14.204  1.00 11.89 ? 215 VAL A N   1 
ATOM   1754 C  CA  . VAL A  1 215 ? 24.225  -15.470 15.388  1.00 12.08 ? 215 VAL A CA  1 
ATOM   1755 C  C   . VAL A  1 215 ? 23.267  -15.623 16.560  1.00 13.74 ? 215 VAL A C   1 
ATOM   1756 O  O   . VAL A  1 215 ? 22.170  -15.075 16.531  1.00 13.58 ? 215 VAL A O   1 
ATOM   1757 C  CB  . VAL A  1 215 ? 25.394  -14.575 15.729  1.00 13.08 ? 215 VAL A CB  1 
ATOM   1758 C  CG1 . VAL A  1 215 ? 26.418  -14.430 14.620  1.00 14.40 ? 215 VAL A CG1 1 
ATOM   1759 C  CG2 . VAL A  1 215 ? 24.922  -13.191 16.158  1.00 13.73 ? 215 VAL A CG2 1 
ATOM   1760 N  N   A GLN A  1 216 ? 23.721  -16.324 17.597  0.50 14.47 ? 216 GLN A N   1 
ATOM   1761 N  N   B GLN A  1 216 ? 23.682  -16.341 17.587  0.50 14.31 ? 216 GLN A N   1 
ATOM   1762 C  CA  A GLN A  1 216 ? 23.009  -16.395 18.876  0.50 14.17 ? 216 GLN A CA  1 
ATOM   1763 C  CA  B GLN A  1 216 ? 22.871  -16.472 18.784  0.50 14.17 ? 216 GLN A CA  1 
ATOM   1764 C  C   A GLN A  1 216 ? 23.678  -15.733 19.996  0.50 15.02 ? 216 GLN A C   1 
ATOM   1765 C  C   B GLN A  1 216 ? 23.585  -15.866 19.963  0.50 14.50 ? 216 GLN A C   1 
ATOM   1766 O  O   A GLN A  1 216 ? 24.894  -15.718 20.123  0.50 14.95 ? 216 GLN A O   1 
ATOM   1767 O  O   B GLN A  1 216 ? 24.788  -15.974 20.060  0.50 14.12 ? 216 GLN A O   1 
ATOM   1768 C  CB  A GLN A  1 216 ? 22.848  -17.876 19.297  0.50 15.60 ? 216 GLN A CB  1 
ATOM   1769 C  CB  B GLN A  1 216 ? 22.640  -18.000 19.042  0.50 15.21 ? 216 GLN A CB  1 
ATOM   1770 C  CG  A GLN A  1 216 ? 21.828  -18.533 18.392  0.50 16.83 ? 216 GLN A CG  1 
ATOM   1771 C  CG  B GLN A  1 216 ? 21.896  -18.769 17.926  0.50 15.21 ? 216 GLN A CG  1 
ATOM   1772 C  CD  A GLN A  1 216 ? 21.646  -20.025 18.544  0.50 20.12 ? 216 GLN A CD  1 
ATOM   1773 C  CD  B GLN A  1 216 ? 22.708  -19.118 16.665  0.50 16.12 ? 216 GLN A CD  1 
ATOM   1774 O  OE1 A GLN A  1 216 ? 21.895  -20.590 19.607  0.50 21.13 ? 216 GLN A OE1 1 
ATOM   1775 O  OE1 B GLN A  1 216 ? 23.879  -19.438 16.750  0.50 19.40 ? 216 GLN A OE1 1 
ATOM   1776 N  NE2 A GLN A  1 216 ? 21.189  -20.665 17.466  0.50 23.01 ? 216 GLN A NE2 1 
ATOM   1777 N  NE2 B GLN A  1 216 ? 22.047  -19.088 15.462  0.50 16.59 ? 216 GLN A NE2 1 
ATOM   1778 N  N   . ILE A  1 217 ? 22.830  -15.201 20.869  1.00 13.88 ? 217 ILE A N   1 
ATOM   1779 C  CA  . ILE A  1 217 ? 23.266  -14.698 22.185  1.00 14.13 ? 217 ILE A CA  1 
ATOM   1780 C  C   . ILE A  1 217 ? 22.289  -15.207 23.227  1.00 13.61 ? 217 ILE A C   1 
ATOM   1781 O  O   . ILE A  1 217 ? 21.186  -15.555 22.873  1.00 13.24 ? 217 ILE A O   1 
ATOM   1782 C  CB  . ILE A  1 217 ? 23.449  -13.118 22.231  1.00 13.54 ? 217 ILE A CB  1 
ATOM   1783 C  CG1 . ILE A  1 217 ? 22.092  -12.316 22.032  1.00 14.75 ? 217 ILE A CG1 1 
ATOM   1784 C  CG2 . ILE A  1 217 ? 24.481  -12.714 21.146  1.00 13.84 ? 217 ILE A CG2 1 
ATOM   1785 C  CD1 . ILE A  1 217 ? 22.226  -10.838 22.259  1.00 14.78 ? 217 ILE A CD1 1 
ATOM   1786 N  N   . SER A  1 218 ? 22.742  -15.270 24.468  1.00 14.73 ? 218 SER A N   1 
ATOM   1787 C  CA  . SER A  1 218 ? 21.790  -15.860 25.410  1.00 15.04 ? 218 SER A CA  1 
ATOM   1788 C  C   . SER A  1 218 ? 20.653  -14.923 25.789  1.00 15.45 ? 218 SER A C   1 
ATOM   1789 O  O   . SER A  1 218 ? 20.703  -13.704 25.579  1.00 15.02 ? 218 SER A O   1 
ATOM   1790 C  CB  . SER A  1 218 ? 22.491  -16.256 26.696  1.00 16.49 ? 218 SER A CB  1 
ATOM   1791 O  OG  . SER A  1 218 ? 22.955  -15.127 27.369  1.00 16.61 ? 218 SER A OG  1 
ATOM   1792 N  N   . GLN A  1 219 ? 19.617  -15.511 26.414  1.00 17.39 ? 219 GLN A N   1 
ATOM   1793 C  CA  . GLN A  1 219 ? 18.564  -14.646 26.902  1.00 18.52 ? 219 GLN A CA  1 
ATOM   1794 C  C   . GLN A  1 219 ? 19.035  -13.581 27.883  1.00 16.43 ? 219 GLN A C   1 
ATOM   1795 O  O   . GLN A  1 219 ? 18.594  -12.450 27.802  1.00 15.93 ? 219 GLN A O   1 
ATOM   1796 C  CB  . GLN A  1 219 ? 17.367  -15.452 27.382  1.00 24.38 ? 219 GLN A CB  1 
ATOM   1797 C  CG  . GLN A  1 219 ? 17.597  -16.160 28.685  1.00 31.72 ? 219 GLN A CG  1 
ATOM   1798 C  CD  . GLN A  1 219 ? 16.268  -16.395 29.392  1.00 43.05 ? 219 GLN A CD  1 
ATOM   1799 O  OE1 . GLN A  1 219 ? 15.417  -17.130 28.879  1.00 43.79 ? 219 GLN A OE1 1 
ATOM   1800 N  NE2 . GLN A  1 219 ? 16.069  -15.753 30.553  1.00 45.55 ? 219 GLN A NE2 1 
ATOM   1801 N  N   . GLU A  1 220 ? 20.008  -13.870 28.737  1.00 15.23 ? 220 GLU A N   1 
ATOM   1802 C  CA  . GLU A  1 220 ? 20.524  -12.932 29.615  1.00 16.81 ? 220 GLU A CA  1 
ATOM   1803 C  C   . GLU A  1 220 ? 21.331  -11.818 28.874  1.00 15.90 ? 220 GLU A C   1 
ATOM   1804 O  O   . GLU A  1 220 ? 21.313  -10.662 29.237  1.00 15.72 ? 220 GLU A O   1 
ATOM   1805 C  CB  . GLU A  1 220 ? 21.434  -13.615 30.701  1.00 18.20 ? 220 GLU A CB  1 
ATOM   1806 C  CG  . GLU A  1 220 ? 20.655  -14.658 31.587  1.00 21.00 ? 220 GLU A CG  1 
ATOM   1807 C  CD  . GLU A  1 220 ? 20.392  -16.030 30.937  1.00 28.39 ? 220 GLU A CD  1 
ATOM   1808 O  OE1 . GLU A  1 220 ? 20.946  -16.435 29.861  1.00 27.01 ? 220 GLU A OE1 1 
ATOM   1809 O  OE2 . GLU A  1 220 ? 19.525  -16.792 31.494  1.00 35.19 ? 220 GLU A OE2 1 
ATOM   1810 N  N   . GLN A  1 221 ? 22.086  -12.246 27.832  1.00 14.79 ? 221 GLN A N   1 
ATOM   1811 C  CA  . GLN A  1 221 ? 22.881  -11.242 27.116  1.00 13.42 ? 221 GLN A CA  1 
ATOM   1812 C  C   . GLN A  1 221 ? 21.905  -10.268 26.359  1.00 14.48 ? 221 GLN A C   1 
ATOM   1813 O  O   . GLN A  1 221 ? 22.110  -9.040  26.403  1.00 13.72 ? 221 GLN A O   1 
ATOM   1814 C  CB  . GLN A  1 221 ? 23.743  -11.892 26.052  1.00 13.15 ? 221 GLN A CB  1 
ATOM   1815 C  CG  . GLN A  1 221 ? 24.972  -12.656 26.646  1.00 14.80 ? 221 GLN A CG  1 
ATOM   1816 C  CD  . GLN A  1 221 ? 25.782  -13.278 25.558  1.00 11.84 ? 221 GLN A CD  1 
ATOM   1817 O  OE1 . GLN A  1 221 ? 25.373  -14.173 24.924  1.00 14.74 ? 221 GLN A OE1 1 
ATOM   1818 N  NE2 . GLN A  1 221 ? 27.008  -12.837 25.456  1.00 16.12 ? 221 GLN A NE2 1 
ATOM   1819 N  N   . LEU A  1 222 ? 20.827  -10.820 25.829  1.00 11.71 ? 222 LEU A N   1 
ATOM   1820 C  CA  . LEU A  1 222 ? 19.884  -9.987  25.057  1.00 14.25 ? 222 LEU A CA  1 
ATOM   1821 C  C   . LEU A  1 222 ? 19.225  -9.027  26.053  1.00 15.15 ? 222 LEU A C   1 
ATOM   1822 O  O   . LEU A  1 222 ? 19.014  -7.860  25.787  1.00 14.05 ? 222 LEU A O   1 
ATOM   1823 C  CB  . LEU A  1 222 ? 18.885  -10.849 24.322  1.00 14.15 ? 222 LEU A CB  1 
ATOM   1824 C  CG  . LEU A  1 222 ? 17.725  -10.062 23.652  1.00 14.37 ? 222 LEU A CG  1 
ATOM   1825 C  CD1 . LEU A  1 222 ? 18.253  -9.095  22.548  1.00 14.75 ? 222 LEU A CD1 1 
ATOM   1826 C  CD2 . LEU A  1 222 ? 16.755  -11.041 23.033  1.00 16.67 ? 222 LEU A CD2 1 
ATOM   1827 N  N   . LEU A  1 223 ? 18.869  -9.546  27.261  1.00 13.82 ? 223 LEU A N   1 
ATOM   1828 C  CA  . LEU A  1 223 ? 18.215  -8.724  28.272  1.00 14.94 ? 223 LEU A CA  1 
ATOM   1829 C  C   . LEU A  1 223 ? 19.141  -7.596  28.704  1.00 14.72 ? 223 LEU A C   1 
ATOM   1830 O  O   . LEU A  1 223 ? 18.729  -6.432  28.902  1.00 16.58 ? 223 LEU A O   1 
ATOM   1831 C  CB  . LEU A  1 223 ? 17.815  -9.571  29.480  1.00 15.91 ? 223 LEU A CB  1 
ATOM   1832 C  CG  . LEU A  1 223 ? 17.047  -8.844  30.586  1.00 18.32 ? 223 LEU A CG  1 
ATOM   1833 C  CD1 . LEU A  1 223 ? 15.742  -8.274  30.050  1.00 20.25 ? 223 LEU A CD1 1 
ATOM   1834 C  CD2 . LEU A  1 223 ? 16.788  -9.774  31.761  1.00 19.04 ? 223 LEU A CD2 1 
ATOM   1835 N  N   . ALA A  1 224 ? 20.437  -7.894  28.866  1.00 14.90 ? 224 ALA A N   1 
ATOM   1836 C  CA  . ALA A  1 224 ? 21.382  -6.875  29.256  1.00 16.32 ? 224 ALA A CA  1 
ATOM   1837 C  C   . ALA A  1 224 ? 21.470  -5.750  28.226  1.00 16.24 ? 224 ALA A C   1 
ATOM   1838 O  O   . ALA A  1 224 ? 21.499  -4.587  28.539  1.00 16.73 ? 224 ALA A O   1 
ATOM   1839 C  CB  . ALA A  1 224 ? 22.804  -7.482  29.492  1.00 18.44 ? 224 ALA A CB  1 
ATOM   1840 N  N   . LEU A  1 225 ? 21.579  -6.156  26.964  1.00 13.75 ? 225 LEU A N   1 
ATOM   1841 C  CA  . LEU A  1 225 ? 21.652  -5.157  25.873  1.00 13.86 ? 225 LEU A CA  1 
ATOM   1842 C  C   . LEU A  1 225 ? 20.385  -4.265  25.897  1.00 15.41 ? 225 LEU A C   1 
ATOM   1843 O  O   . LEU A  1 225 ? 20.521  -3.042  25.751  1.00 17.31 ? 225 LEU A O   1 
ATOM   1844 C  CB  . LEU A  1 225 ? 21.725  -5.895  24.530  1.00 13.31 ? 225 LEU A CB  1 
ATOM   1845 C  CG  . LEU A  1 225 ? 21.852  -4.929  23.327  1.00 13.36 ? 225 LEU A CG  1 
ATOM   1846 C  CD1 . LEU A  1 225 ? 23.108  -4.052  23.426  1.00 16.52 ? 225 LEU A CD1 1 
ATOM   1847 C  CD2 . LEU A  1 225 ? 21.846  -5.809  22.105  1.00 14.16 ? 225 LEU A CD2 1 
ATOM   1848 N  N   . GLU A  1 226 ? 19.196  -4.888  26.087  1.00 13.45 ? 226 GLU A N   1 
ATOM   1849 C  CA  . GLU A  1 226 ? 17.950  -4.117  26.145  1.00 15.34 ? 226 GLU A CA  1 
ATOM   1850 C  C   . GLU A  1 226 ? 17.744  -3.218  27.339  1.00 16.49 ? 226 GLU A C   1 
ATOM   1851 O  O   . GLU A  1 226 ? 16.963  -2.297  27.274  1.00 17.59 ? 226 GLU A O   1 
ATOM   1852 C  CB  . GLU A  1 226 ? 16.785  -5.108  26.057  1.00 13.47 ? 226 GLU A CB  1 
ATOM   1853 C  CG  . GLU A  1 226 ? 16.669  -5.857  24.727  1.00 12.74 ? 226 GLU A CG  1 
ATOM   1854 C  CD  . GLU A  1 226 ? 15.774  -7.076  24.822  1.00 14.53 ? 226 GLU A CD  1 
ATOM   1855 O  OE1 . GLU A  1 226 ? 15.534  -7.550  25.953  1.00 16.91 ? 226 GLU A OE1 1 
ATOM   1856 O  OE2 . GLU A  1 226 ? 15.312  -7.559  23.768  1.00 14.83 ? 226 GLU A OE2 1 
ATOM   1857 N  N   . THR A  1 227 ? 18.446  -3.512  28.433  1.00 15.71 ? 227 THR A N   1 
ATOM   1858 C  CA  . THR A  1 227 ? 18.157  -2.858  29.711  1.00 16.46 ? 227 THR A CA  1 
ATOM   1859 C  C   . THR A  1 227 ? 19.360  -2.049  30.225  1.00 17.48 ? 227 THR A C   1 
ATOM   1860 O  O   . THR A  1 227 ? 19.179  -1.399  31.255  1.00 20.89 ? 227 THR A O   1 
ATOM   1861 C  CB  . THR A  1 227 ? 17.724  -3.876  30.816  1.00 17.50 ? 227 THR A CB  1 
ATOM   1862 O  OG1 . THR A  1 227 ? 18.717  -4.841  31.049  1.00 19.42 ? 227 THR A OG1 1 
ATOM   1863 C  CG2 . THR A  1 227 ? 16.470  -4.562  30.442  1.00 19.61 ? 227 THR A CG2 1 
ATOM   1864 N  N   . ALA A  1 228 ? 20.576  -2.142  29.639  1.00 17.58 ? 228 ALA A N   1 
ATOM   1865 C  CA  . ALA A  1 228 ? 21.750  -1.540  30.249  1.00 18.87 ? 228 ALA A CA  1 
ATOM   1866 C  C   . ALA A  1 228 ? 21.871  -0.066  29.995  1.00 19.88 ? 228 ALA A C   1 
ATOM   1867 O  O   . ALA A  1 228 ? 22.566  0.629   30.754  1.00 23.96 ? 228 ALA A O   1 
ATOM   1868 C  CB  . ALA A  1 228 ? 23.013  -2.309  29.876  1.00 22.85 ? 228 ALA A CB  1 
ATOM   1869 N  N   . LEU A  1 229 ? 21.243  0.479   28.918  1.00 15.72 ? 229 LEU A N   1 
ATOM   1870 C  CA  . LEU A  1 229 ? 21.590  1.827   28.460  1.00 17.39 ? 229 LEU A CA  1 
ATOM   1871 C  C   . LEU A  1 229 ? 20.472  2.775   28.488  1.00 17.21 ? 229 LEU A C   1 
ATOM   1872 O  O   . LEU A  1 229 ? 19.250  2.391   28.324  1.00 15.79 ? 229 LEU A O   1 
ATOM   1873 C  CB  . LEU A  1 229 ? 22.150  1.789   27.029  1.00 14.96 ? 229 LEU A CB  1 
ATOM   1874 C  CG  . LEU A  1 229 ? 23.197  0.645   26.814  1.00 17.43 ? 229 LEU A CG  1 
ATOM   1875 C  CD1 . LEU A  1 229 ? 23.670  0.803   25.374  1.00 21.20 ? 229 LEU A CD1 1 
ATOM   1876 C  CD2 . LEU A  1 229 ? 24.436  0.860   27.701  1.00 18.96 ? 229 LEU A CD2 1 
ATOM   1877 N  N   . TYR A  1 230 ? 20.815  4.044   28.654  1.00 17.16 ? 230 TYR A N   1 
ATOM   1878 C  CA  . TYR A  1 230 ? 19.858  5.133   28.541  1.00 19.55 ? 230 TYR A CA  1 
ATOM   1879 C  C   . TYR A  1 230 ? 20.200  6.072   27.408  1.00 19.01 ? 230 TYR A C   1 
ATOM   1880 O  O   . TYR A  1 230 ? 21.380  6.246   27.094  1.00 20.40 ? 230 TYR A O   1 
ATOM   1881 C  CB  . TYR A  1 230 ? 19.917  5.995   29.848  1.00 20.77 ? 230 TYR A CB  1 
ATOM   1882 C  CG  . TYR A  1 230 ? 19.386  5.263   31.057  1.00 28.02 ? 230 TYR A CG  1 
ATOM   1883 C  CD1 . TYR A  1 230 ? 20.114  4.255   31.685  1.00 28.61 ? 230 TYR A CD1 1 
ATOM   1884 C  CD2 . TYR A  1 230 ? 18.170  5.658   31.616  1.00 30.74 ? 230 TYR A CD2 1 
ATOM   1885 C  CE1 . TYR A  1 230 ? 19.603  3.592   32.804  1.00 37.10 ? 230 TYR A CE1 1 
ATOM   1886 C  CE2 . TYR A  1 230 ? 17.645  5.032   32.738  1.00 32.06 ? 230 TYR A CE2 1 
ATOM   1887 C  CZ  . TYR A  1 230 ? 18.348  4.011   33.341  1.00 33.56 ? 230 TYR A CZ  1 
ATOM   1888 O  OH  . TYR A  1 230 ? 17.757  3.429   34.471  1.00 40.94 ? 230 TYR A OH  1 
ATOM   1889 N  N   . CYS A  1 231 ? 19.225  6.745   26.810  1.00 21.53 ? 231 CYS A N   1 
ATOM   1890 C  CA  . CYS A  1 231 ? 19.587  7.595   25.740  1.00 23.85 ? 231 CYS A CA  1 
ATOM   1891 C  C   . CYS A  1 231 ? 19.783  9.019   26.237  1.00 22.38 ? 231 CYS A C   1 
ATOM   1892 O  O   . CYS A  1 231 ? 20.200  9.915   25.513  1.00 22.17 ? 231 CYS A O   1 
ATOM   1893 C  CB  . CYS A  1 231 ? 18.625  7.429   24.572  1.00 32.15 ? 231 CYS A CB  1 
ATOM   1894 S  SG  . CYS A  1 231 ? 16.897  7.577   24.902  1.00 36.59 ? 231 CYS A SG  1 
ATOM   1895 N  N   . THR A  1 232 ? 19.625  9.166   27.562  1.00 21.73 ? 232 THR A N   1 
ATOM   1896 C  CA  . THR A  1 232 ? 19.783  10.468  28.218  1.00 21.84 ? 232 THR A CA  1 
ATOM   1897 C  C   . THR A  1 232 ? 21.126  10.594  28.990  1.00 22.08 ? 232 THR A C   1 
ATOM   1898 O  O   . THR A  1 232 ? 21.759  9.589   29.372  1.00 19.68 ? 232 THR A O   1 
ATOM   1899 C  CB  . THR A  1 232 ? 18.599  10.691  29.189  1.00 22.70 ? 232 THR A CB  1 
ATOM   1900 O  OG1 . THR A  1 232 ? 18.371  9.490   29.923  1.00 22.52 ? 232 THR A OG1 1 
ATOM   1901 C  CG2 . THR A  1 232 ? 17.331  11.115  28.491  1.00 21.02 ? 232 THR A CG2 1 
ATOM   1902 N  N   . HIS A  1 233 ? 21.528  11.859  29.250  1.00 24.18 ? 233 HIS A N   1 
ATOM   1903 C  CA  . HIS A  1 233 ? 22.723  12.138  30.077  1.00 24.42 ? 233 HIS A CA  1 
ATOM   1904 C  C   . HIS A  1 233 ? 22.465  11.722  31.523  1.00 23.55 ? 233 HIS A C   1 
ATOM   1905 O  O   . HIS A  1 233 ? 21.288  11.682  31.964  1.00 22.64 ? 233 HIS A O   1 
ATOM   1906 C  CB  . HIS A  1 233 ? 23.098  13.617  30.039  1.00 26.39 ? 233 HIS A CB  1 
ATOM   1907 C  CG  . HIS A  1 233 ? 23.781  14.011  28.743  1.00 32.18 ? 233 HIS A CG  1 
ATOM   1908 N  ND1 . HIS A  1 233 ? 23.139  14.687  27.744  1.00 41.65 ? 233 HIS A ND1 1 
ATOM   1909 C  CD2 . HIS A  1 233 ? 25.074  13.755  28.276  1.00 35.03 ? 233 HIS A CD2 1 
ATOM   1910 C  CE1 . HIS A  1 233 ? 23.977  14.847  26.697  1.00 36.06 ? 233 HIS A CE1 1 
ATOM   1911 N  NE2 . HIS A  1 233 ? 25.162  14.273  27.019  1.00 36.24 ? 233 HIS A NE2 1 
ATOM   1912 N  N   . MET A  1 234 ? 23.544  11.349  32.221  1.00 20.87 ? 234 MET A N   1 
ATOM   1913 C  CA  . MET A  1 234 ? 23.458  10.880  33.636  1.00 22.98 ? 234 MET A CA  1 
ATOM   1914 C  C   . MET A  1 234 ? 22.647  11.805  34.542  1.00 27.25 ? 234 MET A C   1 
ATOM   1915 O  O   . MET A  1 234 ? 21.892  11.322  35.396  1.00 24.92 ? 234 MET A O   1 
ATOM   1916 C  CB  . MET A  1 234 ? 24.828  10.639  34.207  1.00 27.03 ? 234 MET A CB  1 
ATOM   1917 C  CG  . MET A  1 234 ? 24.792  9.953   35.581  1.00 25.73 ? 234 MET A CG  1 
ATOM   1918 S  SD  . MET A  1 234 ? 26.489  9.652   36.123  1.00 40.02 ? 234 MET A SD  1 
ATOM   1919 C  CE  . MET A  1 234 ? 26.980  11.367  35.962  1.00 39.17 ? 234 MET A CE  1 
ATOM   1920 N  N   . ASP A  1 235 ? 22.756  13.112  34.325  1.00 29.67 ? 235 ASP A N   1 
ATOM   1921 C  CA  . ASP A  1 235 ? 22.105  14.030  35.255  1.00 34.38 ? 235 ASP A CA  1 
ATOM   1922 C  C   . ASP A  1 235 ? 20.801  14.612  34.702  1.00 33.85 ? 235 ASP A C   1 
ATOM   1923 O  O   . ASP A  1 235 ? 20.276  15.617  35.187  1.00 30.38 ? 235 ASP A O   1 
ATOM   1924 C  CB  . ASP A  1 235 ? 23.104  15.116  35.680  1.00 44.53 ? 235 ASP A CB  1 
ATOM   1925 C  CG  . ASP A  1 235 ? 23.572  15.966  34.511  1.00 53.42 ? 235 ASP A CG  1 
ATOM   1926 O  OD1 . ASP A  1 235 ? 23.003  15.850  33.387  1.00 59.90 ? 235 ASP A OD1 1 
ATOM   1927 O  OD2 . ASP A  1 235 ? 24.518  16.760  34.731  1.00 67.68 ? 235 ASP A OD2 1 
ATOM   1928 N  N   . ASP A  1 236 ? 20.253  13.956  33.689  1.00 29.71 ? 236 ASP A N   1 
ATOM   1929 C  CA  . ASP A  1 236 ? 18.946  14.329  33.158  1.00 28.14 ? 236 ASP A CA  1 
ATOM   1930 C  C   . ASP A  1 236 ? 17.888  13.947  34.177  1.00 27.17 ? 236 ASP A C   1 
ATOM   1931 O  O   . ASP A  1 236 ? 17.767  12.760  34.550  1.00 26.18 ? 236 ASP A O   1 
ATOM   1932 C  CB  . ASP A  1 236 ? 18.666  13.569  31.867  1.00 28.52 ? 236 ASP A CB  1 
ATOM   1933 C  CG  . ASP A  1 236 ? 17.533  14.165  31.087  1.00 29.16 ? 236 ASP A CG  1 
ATOM   1934 O  OD1 . ASP A  1 236 ? 16.525  14.558  31.706  1.00 32.56 ? 236 ASP A OD1 1 
ATOM   1935 O  OD2 . ASP A  1 236 ? 17.649  14.250  29.820  1.00 28.02 ? 236 ASP A OD2 1 
ATOM   1936 N  N   . PRO A  1 237 ? 17.097  14.927  34.674  1.00 28.15 ? 237 PRO A N   1 
ATOM   1937 C  CA  . PRO A  1 237 ? 16.123  14.566  35.697  1.00 26.32 ? 237 PRO A CA  1 
ATOM   1938 C  C   . PRO A  1 237 ? 14.953  13.742  35.114  1.00 27.42 ? 237 PRO A C   1 
ATOM   1939 O  O   . PRO A  1 237 ? 14.047  13.316  35.823  1.00 26.84 ? 237 PRO A O   1 
ATOM   1940 C  CB  . PRO A  1 237 ? 15.608  15.959  36.198  1.00 29.29 ? 237 PRO A CB  1 
ATOM   1941 C  CG  . PRO A  1 237 ? 15.743  16.824  34.995  1.00 30.71 ? 237 PRO A CG  1 
ATOM   1942 C  CD  . PRO A  1 237 ? 16.964  16.338  34.240  1.00 29.04 ? 237 PRO A CD  1 
ATOM   1943 N  N   . SER A  1 238 ? 14.943  13.536  33.797  1.00 27.41 ? 238 SER A N   1 
ATOM   1944 C  CA  . SER A  1 238 ? 13.906  12.685  33.185  1.00 28.41 ? 238 SER A CA  1 
ATOM   1945 C  C   . SER A  1 238 ? 14.481  11.560  32.332  1.00 28.73 ? 238 SER A C   1 
ATOM   1946 O  O   . SER A  1 238 ? 14.477  11.692  31.110  1.00 25.97 ? 238 SER A O   1 
ATOM   1947 C  CB  . SER A  1 238 ? 13.057  13.544  32.266  1.00 31.33 ? 238 SER A CB  1 
ATOM   1948 O  OG  . SER A  1 238 ? 12.322  14.469  33.037  1.00 39.42 ? 238 SER A OG  1 
ATOM   1949 N  N   . PRO A  1 239 ? 14.983  10.510  32.979  1.00 25.70 ? 239 PRO A N   1 
ATOM   1950 C  CA  . PRO A  1 239 ? 15.792  9.580   32.135  1.00 23.85 ? 239 PRO A CA  1 
ATOM   1951 C  C   . PRO A  1 239 ? 14.910  8.771   31.209  1.00 29.81 ? 239 PRO A C   1 
ATOM   1952 O  O   . PRO A  1 239 ? 13.753  8.475   31.554  1.00 25.52 ? 239 PRO A O   1 
ATOM   1953 C  CB  . PRO A  1 239 ? 16.426  8.666   33.133  1.00 24.73 ? 239 PRO A CB  1 
ATOM   1954 C  CG  . PRO A  1 239 ? 15.734  8.879   34.462  1.00 31.75 ? 239 PRO A CG  1 
ATOM   1955 C  CD  . PRO A  1 239 ? 15.118  10.258  34.421  1.00 26.33 ? 239 PRO A CD  1 
ATOM   1956 N  N   . ARG A  1 240 ? 15.480  8.363   30.072  1.00 26.70 ? 240 ARG A N   1 
ATOM   1957 C  CA  . ARG A  1 240 ? 14.784  7.483   29.111  1.00 26.80 ? 240 ARG A CA  1 
ATOM   1958 C  C   . ARG A  1 240 ? 15.668  6.269   28.834  1.00 24.08 ? 240 ARG A C   1 
ATOM   1959 O  O   . ARG A  1 240 ? 16.864  6.377   28.563  1.00 22.77 ? 240 ARG A O   1 
ATOM   1960 C  CB  . ARG A  1 240 ? 14.454  8.152   27.777  1.00 31.24 ? 240 ARG A CB  1 
ATOM   1961 N  N   . GLU A  1 241 ? 15.074  5.111   28.920  1.00 22.21 ? 241 GLU A N   1 
ATOM   1962 C  CA  . GLU A  1 241 ? 15.794  3.873   28.571  1.00 22.97 ? 241 GLU A CA  1 
ATOM   1963 C  C   . GLU A  1 241 ? 16.027  3.780   27.042  1.00 19.68 ? 241 GLU A C   1 
ATOM   1964 O  O   . GLU A  1 241 ? 15.146  4.207   26.246  1.00 22.16 ? 241 GLU A O   1 
ATOM   1965 C  CB  . GLU A  1 241 ? 14.946  2.689   28.999  1.00 26.43 ? 241 GLU A CB  1 
ATOM   1966 C  CG  . GLU A  1 241 ? 14.740  2.557   30.505  1.00 34.54 ? 241 GLU A CG  1 
ATOM   1967 C  CD  . GLU A  1 241 ? 13.697  1.497   30.862  1.00 42.52 ? 241 GLU A CD  1 
ATOM   1968 O  OE1 . GLU A  1 241 ? 12.806  1.188   30.009  1.00 51.35 ? 241 GLU A OE1 1 
ATOM   1969 O  OE2 . GLU A  1 241 ? 13.764  0.989   32.014  1.00 44.13 ? 241 GLU A OE2 1 
ATOM   1970 N  N   . MET A  1 242 ? 17.212  3.309   26.645  1.00 15.58 ? 242 MET A N   1 
ATOM   1971 C  CA  . MET A  1 242 ? 17.503  3.130   25.215  1.00 14.21 ? 242 MET A CA  1 
ATOM   1972 C  C   . MET A  1 242 ? 16.974  1.771   24.806  1.00 13.67 ? 242 MET A C   1 
ATOM   1973 O  O   . MET A  1 242 ? 17.617  0.724   25.012  1.00 13.94 ? 242 MET A O   1 
ATOM   1974 C  CB  . MET A  1 242 ? 19.015  3.204   25.002  1.00 15.86 ? 242 MET A CB  1 
ATOM   1975 C  CG  . MET A  1 242 ? 19.386  3.124   23.506  1.00 15.91 ? 242 MET A CG  1 
ATOM   1976 S  SD  . MET A  1 242 ? 21.143  3.138   23.183  1.00 16.74 ? 242 MET A SD  1 
ATOM   1977 C  CE  . MET A  1 242 ? 21.524  4.795   23.757  1.00 17.07 ? 242 MET A CE  1 
ATOM   1978 N  N   . ILE A  1 243 ? 15.821  1.814   24.155  1.00 12.81 ? 243 ILE A N   1 
ATOM   1979 C  CA  . ILE A  1 243 ? 15.112  0.635   23.676  1.00 13.26 ? 243 ILE A CA  1 
ATOM   1980 C  C   . ILE A  1 243 ? 14.511  0.933   22.292  1.00 11.94 ? 243 ILE A C   1 
ATOM   1981 O  O   . ILE A  1 243 ? 14.331  2.153   21.904  1.00 12.92 ? 243 ILE A O   1 
ATOM   1982 C  CB  . ILE A  1 243 ? 13.969  0.192   24.598  1.00 13.93 ? 243 ILE A CB  1 
ATOM   1983 C  CG1 . ILE A  1 243 ? 13.044  1.332   24.972  1.00 15.35 ? 243 ILE A CG1 1 
ATOM   1984 C  CG2 . ILE A  1 243 ? 14.585  -0.460  25.841  1.00 17.69 ? 243 ILE A CG2 1 
ATOM   1985 C  CD1 . ILE A  1 243 ? 11.782  0.810   25.742  1.00 17.29 ? 243 ILE A CD1 1 
ATOM   1986 N  N   . ASN A  1 244 ? 14.206  -0.099  21.507  1.00 10.23 ? 244 ASN A N   1 
ATOM   1987 C  CA  . ASN A  1 244 ? 13.452  0.099   20.242  1.00 11.12 ? 244 ASN A CA  1 
ATOM   1988 C  C   . ASN A  1 244 ? 14.179  1.106   19.350  1.00 10.41 ? 244 ASN A C   1 
ATOM   1989 O  O   . ASN A  1 244 ? 13.559  1.910   18.632  1.00 11.27 ? 244 ASN A O   1 
ATOM   1990 C  CB  . ASN A  1 244 ? 12.005  0.488   20.486  1.00 12.72 ? 244 ASN A CB  1 
ATOM   1991 C  CG  . ASN A  1 244 ? 11.305  -0.473  21.376  1.00 13.17 ? 244 ASN A CG  1 
ATOM   1992 O  OD1 . ASN A  1 244 ? 11.513  -1.691  21.285  1.00 16.48 ? 244 ASN A OD1 1 
ATOM   1993 N  ND2 . ASN A  1 244 ? 10.517  0.122   22.305  1.00 16.98 ? 244 ASN A ND2 1 
ATOM   1994 N  N   . ASN A  1 245 ? 15.527  0.919   19.261  1.00 9.29  ? 245 ASN A N   1 
ATOM   1995 C  CA  . ASN A  1 245 ? 16.327  1.887   18.480  1.00 10.57 ? 245 ASN A CA  1 
ATOM   1996 C  C   . ASN A  1 245 ? 16.555  1.319   17.110  1.00 9.51  ? 245 ASN A C   1 
ATOM   1997 O  O   . ASN A  1 245 ? 17.700  1.196   16.679  1.00 10.22 ? 245 ASN A O   1 
ATOM   1998 C  CB  . ASN A  1 245 ? 17.619  2.232   19.197  1.00 11.44 ? 245 ASN A CB  1 
ATOM   1999 C  CG  . ASN A  1 245 ? 18.493  1.014   19.493  1.00 11.87 ? 245 ASN A CG  1 
ATOM   2000 O  OD1 . ASN A  1 245 ? 18.057  -0.132  19.503  1.00 12.50 ? 245 ASN A OD1 1 
ATOM   2001 N  ND2 . ASN A  1 245 ? 19.773  1.267   19.783  1.00 12.21 ? 245 ASN A ND2 1 
ATOM   2002 N  N   . PHE A  1 246 ? 15.511  0.982   16.404  1.00 9.23  ? 246 PHE A N   1 
ATOM   2003 C  CA  . PHE A  1 246 ? 15.568  0.487   15.011  1.00 9.29  ? 246 PHE A CA  1 
ATOM   2004 C  C   . PHE A  1 246 ? 14.545  1.323   14.243  1.00 8.88  ? 246 PHE A C   1 
ATOM   2005 O  O   . PHE A  1 246 ? 13.542  1.784   14.778  1.00 9.48  ? 246 PHE A O   1 
ATOM   2006 C  CB  . PHE A  1 246 ? 15.236  -1.049  14.964  1.00 10.03 ? 246 PHE A CB  1 
ATOM   2007 C  CG  . PHE A  1 246 ? 13.838  -1.407  15.458  1.00 9.39  ? 246 PHE A CG  1 
ATOM   2008 C  CD1 . PHE A  1 246 ? 13.625  -1.637  16.848  1.00 9.86  ? 246 PHE A CD1 1 
ATOM   2009 C  CD2 . PHE A  1 246 ? 12.764  -1.540  14.556  1.00 9.78  ? 246 PHE A CD2 1 
ATOM   2010 C  CE1 . PHE A  1 246 ? 12.347  -1.924  17.343  1.00 11.09 ? 246 PHE A CE1 1 
ATOM   2011 C  CE2 . PHE A  1 246 ? 11.473  -1.829  15.022  1.00 11.06 ? 246 PHE A CE2 1 
ATOM   2012 C  CZ  . PHE A  1 246 ? 11.253  -2.011  16.423  1.00 10.55 ? 246 PHE A CZ  1 
ATOM   2013 N  N   . ARG A  1 247 ? 14.850  1.401   12.947  1.00 8.61  ? 247 ARG A N   1 
ATOM   2014 C  CA  . ARG A  1 247 ? 13.917  2.114   12.012  1.00 8.69  ? 247 ARG A CA  1 
ATOM   2015 C  C   . ARG A  1 247 ? 12.910  1.110   11.445  1.00 7.79  ? 247 ARG A C   1 
ATOM   2016 O  O   . ARG A  1 247 ? 13.327  -0.029  11.192  1.00 9.39  ? 247 ARG A O   1 
ATOM   2017 C  CB  . ARG A  1 247 ? 14.719  2.755   10.872  1.00 9.19  ? 247 ARG A CB  1 
ATOM   2018 C  CG  . ARG A  1 247 ? 13.916  3.757   10.028  1.00 8.22  ? 247 ARG A CG  1 
ATOM   2019 C  CD  . ARG A  1 247 ? 14.759  4.208   8.848   1.00 9.72  ? 247 ARG A CD  1 
ATOM   2020 N  NE  . ARG A  1 247 ? 14.110  5.374   8.249   1.00 8.11  ? 247 ARG A NE  1 
ATOM   2021 C  CZ  . ARG A  1 247 ? 14.653  5.990   7.172   1.00 8.88  ? 247 ARG A CZ  1 
ATOM   2022 N  NH1 . ARG A  1 247 ? 15.659  5.445   6.496   1.00 9.50  ? 247 ARG A NH1 1 
ATOM   2023 N  NH2 . ARG A  1 247 ? 14.105  7.138   6.719   1.00 8.93  ? 247 ARG A NH2 1 
ATOM   2024 N  N   . GLN A  1 248 ? 11.651  1.500   11.261  1.00 7.61  ? 248 GLN A N   1 
ATOM   2025 C  CA  . GLN A  1 248 ? 10.762  0.627   10.497  1.00 7.92  ? 248 GLN A CA  1 
ATOM   2026 C  C   . GLN A  1 248 ? 11.209  0.360   9.084   1.00 9.19  ? 248 GLN A C   1 
ATOM   2027 O  O   . GLN A  1 248 ? 11.956  1.192   8.472   1.00 8.82  ? 248 GLN A O   1 
ATOM   2028 C  CB  . GLN A  1 248 ? 9.390   1.311   10.404  1.00 9.01  ? 248 GLN A CB  1 
ATOM   2029 C  CG  . GLN A  1 248 ? 8.736   1.582   11.759  1.00 8.85  ? 248 GLN A CG  1 
ATOM   2030 C  CD  . GLN A  1 248 ? 8.376   0.399   12.564  1.00 10.63 ? 248 GLN A CD  1 
ATOM   2031 O  OE1 . GLN A  1 248 ? 9.146   -0.028  13.401  1.00 10.99 ? 248 GLN A OE1 1 
ATOM   2032 N  NE2 . GLN A  1 248 ? 7.249   -0.229  12.217  1.00 11.15 ? 248 GLN A NE2 1 
ATOM   2033 N  N   . VAL A  1 249 ? 10.827  -0.771  8.507   1.00 8.70  ? 249 VAL A N   1 
ATOM   2034 C  CA  . VAL A  1 249 ? 11.186  -1.085  7.133   1.00 10.00 ? 249 VAL A CA  1 
ATOM   2035 C  C   . VAL A  1 249 ? 10.593  -0.076  6.149   1.00 9.97  ? 249 VAL A C   1 
ATOM   2036 O  O   . VAL A  1 249 ? 9.467   0.455   6.386   1.00 10.24 ? 249 VAL A O   1 
ATOM   2037 C  CB  . VAL A  1 249 ? 10.831  -2.512  6.719   1.00 10.61 ? 249 VAL A CB  1 
ATOM   2038 C  CG1 . VAL A  1 249 ? 11.759  -3.504  7.482   1.00 10.18 ? 249 VAL A CG1 1 
ATOM   2039 C  CG2 . VAL A  1 249 ? 9.384   -2.837  6.889   1.00 13.92 ? 249 VAL A CG2 1 
ATOM   2040 N  N   . GLN A  1 250 ? 11.332  0.181   5.083   1.00 9.48  ? 250 GLN A N   1 
ATOM   2041 C  CA  . GLN A  1 250 ? 10.912  1.190   4.072   1.00 9.79  ? 250 GLN A CA  1 
ATOM   2042 C  C   . GLN A  1 250 ? 10.310  0.450   2.879   1.00 10.72 ? 250 GLN A C   1 
ATOM   2043 O  O   . GLN A  1 250 ? 10.693  -0.618  2.586   1.00 12.56 ? 250 GLN A O   1 
ATOM   2044 C  CB  . GLN A  1 250 ? 12.161  1.960   3.609   1.00 10.66 ? 250 GLN A CB  1 
ATOM   2045 C  CG  . GLN A  1 250 ? 12.977  2.507   4.812   1.00 9.86  ? 250 GLN A CG  1 
ATOM   2046 C  CD  . GLN A  1 250 ? 12.267  3.585   5.495   1.00 9.19  ? 250 GLN A CD  1 
ATOM   2047 O  OE1 . GLN A  1 250 ? 12.041  4.675   4.894   1.00 11.50 ? 250 GLN A OE1 1 
ATOM   2048 N  NE2 . GLN A  1 250 ? 11.925  3.428   6.719   1.00 8.69  ? 250 GLN A NE2 1 
ATOM   2049 N  N   . LYS A  1 251 ? 9.503   1.220   2.126   1.00 9.81  ? 251 LYS A N   1 
ATOM   2050 C  CA  . LYS A  1 251 ? 9.025   0.678   0.852   1.00 11.95 ? 251 LYS A CA  1 
ATOM   2051 C  C   . LYS A  1 251 ? 10.201  0.356   -0.071  1.00 12.85 ? 251 LYS A C   1 
ATOM   2052 O  O   . LYS A  1 251 ? 11.205  1.173   -0.091  1.00 12.22 ? 251 LYS A O   1 
ATOM   2053 C  CB  . LYS A  1 251 ? 8.056   1.665   0.134   1.00 13.29 ? 251 LYS A CB  1 
ATOM   2054 C  CG  . LYS A  1 251 ? 6.656   1.605   0.803   1.00 15.04 ? 251 LYS A CG  1 
ATOM   2055 C  CD  . LYS A  1 251 ? 5.617   2.397   0.156   1.00 16.56 ? 251 LYS A CD  1 
ATOM   2056 C  CE  . LYS A  1 251 ? 4.190   2.124   0.664   1.00 12.24 ? 251 LYS A CE  1 
ATOM   2057 N  NZ  . LYS A  1 251 ? 4.042   2.168   2.171   1.00 10.54 ? 251 LYS A NZ  1 
ATOM   2058 N  N   . PHE A  1 252 ? 10.086  -0.725  -0.845  1.00 13.82 ? 252 PHE A N   1 
ATOM   2059 C  CA  . PHE A  1 252 ? 11.215  -1.099  -1.763  1.00 16.45 ? 252 PHE A CA  1 
ATOM   2060 C  C   . PHE A  1 252 ? 10.545  -1.633  -3.003  1.00 23.09 ? 252 PHE A C   1 
ATOM   2061 O  O   . PHE A  1 252 ? 10.161  -2.783  -3.004  1.00 25.64 ? 252 PHE A O   1 
ATOM   2062 C  CB  . PHE A  1 252 ? 11.997  -2.218  -1.056  1.00 17.13 ? 252 PHE A CB  1 
ATOM   2063 C  CG  . PHE A  1 252 ? 13.276  -2.654  -1.731  1.00 17.43 ? 252 PHE A CG  1 
ATOM   2064 C  CD1 . PHE A  1 252 ? 14.433  -1.893  -1.641  1.00 16.73 ? 252 PHE A CD1 1 
ATOM   2065 C  CD2 . PHE A  1 252 ? 13.342  -3.879  -2.374  1.00 19.46 ? 252 PHE A CD2 1 
ATOM   2066 C  CE1 . PHE A  1 252 ? 15.611  -2.324  -2.229  1.00 18.61 ? 252 PHE A CE1 1 
ATOM   2067 C  CE2 . PHE A  1 252 ? 14.518  -4.316  -2.962  1.00 17.61 ? 252 PHE A CE2 1 
ATOM   2068 C  CZ  . PHE A  1 252 ? 15.655  -3.536  -2.890  1.00 17.77 ? 252 PHE A CZ  1 
ATOM   2069 N  N   . ASP A  1 253 ? 10.349  -0.815  -4.013  1.00 27.27 ? 253 ASP A N   1 
ATOM   2070 C  CA  . ASP A  1 253 ? 9.508   -1.310  -5.158  1.00 27.84 ? 253 ASP A CA  1 
ATOM   2071 C  C   . ASP A  1 253 ? 10.258  -1.251  -6.461  1.00 26.62 ? 253 ASP A C   1 
ATOM   2072 O  O   . ASP A  1 253 ? 11.048  -0.354  -6.678  1.00 25.56 ? 253 ASP A O   1 
ATOM   2073 C  CB  . ASP A  1 253 ? 8.120   -0.599  -5.247  1.00 33.38 ? 253 ASP A CB  1 
ATOM   2074 C  CG  . ASP A  1 253 ? 7.084   -1.339  -6.200  1.00 45.00 ? 253 ASP A CG  1 
ATOM   2075 O  OD1 . ASP A  1 253 ? 6.918   -2.613  -6.142  1.00 46.11 ? 253 ASP A OD1 1 
ATOM   2076 O  OD2 . ASP A  1 253 ? 6.387   -0.621  -6.991  1.00 43.83 ? 253 ASP A OD2 1 
ATOM   2077 N  N   A GLU A  1 254 ? 9.987   -2.256  -7.297  0.50 27.86 ? 254 GLU A N   1 
ATOM   2078 N  N   B GLU A  1 254 ? 9.984   -2.215  -7.342  0.50 27.96 ? 254 GLU A N   1 
ATOM   2079 C  CA  A GLU A  1 254 ? 10.621  -2.409  -8.606  0.50 27.94 ? 254 GLU A CA  1 
ATOM   2080 C  CA  B GLU A  1 254 ? 10.671  -2.315  -8.639  0.50 28.52 ? 254 GLU A CA  1 
ATOM   2081 C  C   A GLU A  1 254 ? 12.136  -2.534  -8.439  0.50 26.27 ? 254 GLU A C   1 
ATOM   2082 C  C   B GLU A  1 254 ? 12.170  -2.499  -8.429  0.50 26.43 ? 254 GLU A C   1 
ATOM   2083 O  O   A GLU A  1 254 ? 12.893  -2.064  -9.265  0.50 28.12 ? 254 GLU A O   1 
ATOM   2084 O  O   B GLU A  1 254 ? 12.963  -2.018  -9.219  0.50 28.61 ? 254 GLU A O   1 
ATOM   2085 C  CB  A GLU A  1 254 ? 10.216  -1.237  -9.497  0.50 29.09 ? 254 GLU A CB  1 
ATOM   2086 C  CB  B GLU A  1 254 ? 10.435  -1.047  -9.459  0.50 29.16 ? 254 GLU A CB  1 
ATOM   2087 C  CG  A GLU A  1 254 ? 8.696   -1.205  -9.638  0.50 30.88 ? 254 GLU A CG  1 
ATOM   2088 C  CG  B GLU A  1 254 ? 8.960   -0.715  -9.623  0.50 34.03 ? 254 GLU A CG  1 
ATOM   2089 C  CD  A GLU A  1 254 ? 8.178   -0.079  -10.510 0.50 33.07 ? 254 GLU A CD  1 
ATOM   2090 C  CD  B GLU A  1 254 ? 8.122   -1.863  -10.191 0.50 39.25 ? 254 GLU A CD  1 
ATOM   2091 O  OE1 A GLU A  1 254 ? 8.976   0.806   -10.852 0.50 32.43 ? 254 GLU A OE1 1 
ATOM   2092 O  OE1 B GLU A  1 254 ? 8.672   -2.936  -10.535 0.50 41.27 ? 254 GLU A OE1 1 
ATOM   2093 O  OE2 A GLU A  1 254 ? 6.970   -0.105  -10.849 0.50 35.32 ? 254 GLU A OE2 1 
ATOM   2094 O  OE2 B GLU A  1 254 ? 6.891   -1.679  -10.314 0.50 43.71 ? 254 GLU A OE2 1 
ATOM   2095 N  N   . ARG A  1 255 ? 12.549  -3.154  -7.332  1.00 25.03 ? 255 ARG A N   1 
ATOM   2096 C  CA  . ARG A  1 255 ? 13.993  -3.381  -7.018  1.00 23.94 ? 255 ARG A CA  1 
ATOM   2097 C  C   . ARG A  1 255 ? 14.206  -4.808  -6.526  1.00 25.31 ? 255 ARG A C   1 
ATOM   2098 O  O   . ARG A  1 255 ? 13.287  -5.430  -5.953  1.00 26.25 ? 255 ARG A O   1 
ATOM   2099 C  CB  . ARG A  1 255 ? 14.525  -2.365  -6.013  1.00 23.33 ? 255 ARG A CB  1 
ATOM   2100 C  CG  . ARG A  1 255 ? 14.518  -0.929  -6.540  1.00 24.66 ? 255 ARG A CG  1 
ATOM   2101 C  CD  . ARG A  1 255 ? 15.016  0.070   -5.487  1.00 24.28 ? 255 ARG A CD  1 
ATOM   2102 N  NE  . ARG A  1 255 ? 16.393  -0.297  -5.225  1.00 27.40 ? 255 ARG A NE  1 
ATOM   2103 C  CZ  . ARG A  1 255 ? 17.055  -0.063  -4.096  1.00 24.89 ? 255 ARG A CZ  1 
ATOM   2104 N  NH1 . ARG A  1 255 ? 16.470  0.573   -3.093  1.00 24.10 ? 255 ARG A NH1 1 
ATOM   2105 N  NH2 . ARG A  1 255 ? 18.315  -0.463  -3.979  1.00 18.90 ? 255 ARG A NH2 1 
ATOM   2106 N  N   . LEU A  1 256 ? 15.432  -5.307  -6.744  1.00 23.51 ? 256 LEU A N   1 
ATOM   2107 C  CA  . LEU A  1 256 ? 15.820  -6.584  -6.273  1.00 22.94 ? 256 LEU A CA  1 
ATOM   2108 C  C   . LEU A  1 256 ? 16.859  -6.422  -5.125  1.00 19.01 ? 256 LEU A C   1 
ATOM   2109 O  O   . LEU A  1 256 ? 17.651  -5.447  -5.035  1.00 20.21 ? 256 LEU A O   1 
ATOM   2110 C  CB  . LEU A  1 256 ? 16.451  -7.390  -7.424  1.00 25.37 ? 256 LEU A CB  1 
ATOM   2111 C  CG  . LEU A  1 256 ? 15.490  -7.721  -8.587  1.00 25.59 ? 256 LEU A CG  1 
ATOM   2112 C  CD1 . LEU A  1 256 ? 16.294  -8.261  -9.758  1.00 27.17 ? 256 LEU A CD1 1 
ATOM   2113 C  CD2 . LEU A  1 256 ? 14.481  -8.802  -8.165  1.00 31.10 ? 256 LEU A CD2 1 
ATOM   2114 N  N   . VAL A  1 257 ? 16.823  -7.457  -4.315  1.00 20.79 ? 257 VAL A N   1 
ATOM   2115 C  CA  . VAL A  1 257 ? 17.963  -7.749  -3.441  1.00 17.21 ? 257 VAL A CA  1 
ATOM   2116 C  C   . VAL A  1 257 ? 18.689  -8.962  -4.008  1.00 16.11 ? 257 VAL A C   1 
ATOM   2117 O  O   . VAL A  1 257 ? 18.056  -10.032 -4.305  1.00 17.91 ? 257 VAL A O   1 
ATOM   2118 C  CB  . VAL A  1 257 ? 17.482  -8.062  -2.015  1.00 16.42 ? 257 VAL A CB  1 
ATOM   2119 C  CG1 . VAL A  1 257 ? 18.556  -8.581  -1.004  1.00 16.15 ? 257 VAL A CG1 1 
ATOM   2120 C  CG2 . VAL A  1 257 ? 16.714  -6.889  -1.451  1.00 18.30 ? 257 VAL A CG2 1 
ATOM   2121 N  N   . TYR A  1 258 ? 19.972  -8.866  -4.185  1.00 15.30 ? 258 TYR A N   1 
ATOM   2122 C  CA  . TYR A  1 258 ? 20.729  -9.916  -4.786  1.00 15.43 ? 258 TYR A CA  1 
ATOM   2123 C  C   . TYR A  1 258 ? 21.230  -10.820 -3.726  1.00 15.14 ? 258 TYR A C   1 
ATOM   2124 O  O   . TYR A  1 258 ? 21.553  -10.377 -2.610  1.00 15.17 ? 258 TYR A O   1 
ATOM   2125 C  CB  . TYR A  1 258 ? 21.851  -9.306  -5.658  1.00 15.02 ? 258 TYR A CB  1 
ATOM   2126 C  CG  . TYR A  1 258 ? 21.295  -8.370  -6.677  1.00 21.06 ? 258 TYR A CG  1 
ATOM   2127 C  CD1 . TYR A  1 258 ? 20.727  -8.876  -7.841  1.00 20.99 ? 258 TYR A CD1 1 
ATOM   2128 C  CD2 . TYR A  1 258 ? 21.225  -7.029  -6.408  1.00 20.55 ? 258 TYR A CD2 1 
ATOM   2129 C  CE1 . TYR A  1 258 ? 20.120  -8.016  -8.773  1.00 25.17 ? 258 TYR A CE1 1 
ATOM   2130 C  CE2 . TYR A  1 258 ? 20.593  -6.155  -7.295  1.00 27.20 ? 258 TYR A CE2 1 
ATOM   2131 C  CZ  . TYR A  1 258 ? 20.072  -6.676  -8.470  1.00 25.56 ? 258 TYR A CZ  1 
ATOM   2132 O  OH  . TYR A  1 258 ? 19.491  -5.773  -9.364  1.00 28.46 ? 258 TYR A OH  1 
ATOM   2133 N  N   . THR A  1 259 ? 21.301  -12.112 -4.001  1.00 15.83 ? 259 THR A N   1 
ATOM   2134 C  CA  . THR A  1 259 ? 21.765  -13.092 -2.997  1.00 14.73 ? 259 THR A CA  1 
ATOM   2135 C  C   . THR A  1 259 ? 22.983  -13.833 -3.525  1.00 14.32 ? 259 THR A C   1 
ATOM   2136 O  O   . THR A  1 259 ? 23.085  -14.191 -4.756  1.00 16.62 ? 259 THR A O   1 
ATOM   2137 C  CB  . THR A  1 259 ? 20.673  -14.071 -2.562  1.00 16.42 ? 259 THR A CB  1 
ATOM   2138 O  OG1 . THR A  1 259 ? 20.222  -14.724 -3.743  1.00 18.18 ? 259 THR A OG1 1 
ATOM   2139 C  CG2 . THR A  1 259 ? 19.471  -13.274 -1.977  1.00 17.00 ? 259 THR A CG2 1 
ATOM   2140 N  N   . SER A  1 260 ? 23.907  -14.197 -2.673  1.00 14.46 ? 260 SER A N   1 
ATOM   2141 C  CA  . SER A  1 260 ? 25.083  -14.956 -3.068  1.00 15.15 ? 260 SER A CA  1 
ATOM   2142 C  C   . SER A  1 260 ? 24.758  -16.428 -3.031  1.00 16.90 ? 260 SER A C   1 
ATOM   2143 O  O   . SER A  1 260 ? 25.631  -17.240 -3.390  1.00 20.49 ? 260 SER A O   1 
ATOM   2144 C  CB  . SER A  1 260 ? 26.271  -14.663 -2.191  1.00 16.74 ? 260 SER A CB  1 
ATOM   2145 O  OG  . SER A  1 260 ? 25.959  -15.147 -0.895  1.00 16.00 ? 260 SER A OG  1 
ATOM   2146 N  N   . PHE A  1 261 ? 23.573  -16.787 -2.625  1.00 17.09 ? 261 PHE A N   1 
ATOM   2147 C  CA  . PHE A  1 261 ? 23.191  -18.208 -2.489  1.00 19.08 ? 261 PHE A CA  1 
ATOM   2148 C  C   . PHE A  1 261 ? 21.947  -18.367 -3.306  1.00 21.44 ? 261 PHE A C   1 
ATOM   2149 O  O   . PHE A  1 261 ? 21.133  -17.435 -3.507  1.00 22.16 ? 261 PHE A O   1 
ATOM   2150 C  CB  . PHE A  1 261 ? 22.942  -18.531 -1.005  1.00 17.76 ? 261 PHE A CB  1 
ATOM   2151 C  CG  . PHE A  1 261 ? 21.938  -17.602 -0.371  1.00 17.62 ? 261 PHE A CG  1 
ATOM   2152 C  CD1 . PHE A  1 261 ? 20.590  -17.878 -0.336  1.00 18.03 ? 261 PHE A CD1 1 
ATOM   2153 C  CD2 . PHE A  1 261 ? 22.393  -16.422 0.185   1.00 16.25 ? 261 PHE A CD2 1 
ATOM   2154 C  CE1 . PHE A  1 261 ? 19.682  -17.031 0.278   1.00 17.19 ? 261 PHE A CE1 1 
ATOM   2155 C  CE2 . PHE A  1 261 ? 21.502  -15.555 0.796   1.00 16.22 ? 261 PHE A CE2 1 
ATOM   2156 C  CZ  . PHE A  1 261 ? 20.153  -15.834 0.837   1.00 17.23 ? 261 PHE A CZ  1 
ATOM   2157 N  N   . SER A  1 262 ? 21.723  -19.558 -3.846  1.00 29.29 ? 262 SER A N   1 
ATOM   2158 C  CA  . SER A  1 262 ? 20.404  -19.734 -4.484  1.00 35.87 ? 262 SER A CA  1 
ATOM   2159 C  C   . SER A  1 262 ? 19.602  -20.670 -3.584  1.00 45.56 ? 262 SER A C   1 
ATOM   2160 O  O   . SER A  1 262 ? 18.521  -20.309 -3.116  1.00 48.98 ? 262 SER A O   1 
ATOM   2161 C  CB  . SER A  1 262 ? 20.487  -20.279 -5.924  1.00 37.93 ? 262 SER A CB  1 
ATOM   2162 O  OG  . SER A  1 262 ? 21.337  -21.400 -5.957  1.00 42.20 ? 262 SER A OG  1 
ATOM   2163 N  N   . GLN A  1 263 ? 20.187  -21.830 -3.291  1.00 48.41 ? 263 GLN A N   1 
ATOM   2164 C  CA  . GLN A  1 263 ? 19.522  -22.898 -2.515  1.00 55.67 ? 263 GLN A CA  1 
ATOM   2165 C  C   . GLN A  1 263 ? 18.767  -22.420 -1.245  1.00 56.37 ? 263 GLN A C   1 
ATOM   2166 O  O   . GLN A  1 263 ? 19.344  -21.810 -0.332  1.00 57.93 ? 263 GLN A O   1 
ATOM   2167 C  CB  . GLN A  1 263 ? 20.542  -23.997 -2.153  1.00 57.52 ? 263 GLN A CB  1 
ATOM   2168 C  CG  . GLN A  1 263 ? 21.257  -24.606 -3.345  1.00 51.91 ? 263 GLN A CG  1 
ATOM   2169 C  CD  . GLN A  1 263 ? 22.003  -25.888 -2.995  1.00 55.30 ? 263 GLN A CD  1 
ATOM   2170 O  OE1 . GLN A  1 263 ? 23.076  -25.876 -2.349  1.00 57.46 ? 263 GLN A OE1 1 
ATOM   2171 N  NE2 . GLN A  1 263 ? 21.448  -27.006 -3.434  1.00 31.05 ? 263 GLN A NE2 1 
ATOM   2172 N  N   . LYS B  1 3   ? -1.174  17.444  -2.145  1.00 41.18 ? 3   LYS B N   1 
ATOM   2173 C  CA  . LYS B  1 3   ? -0.202  16.796  -3.066  1.00 36.04 ? 3   LYS B CA  1 
ATOM   2174 C  C   . LYS B  1 3   ? 0.634   15.748  -2.333  1.00 29.94 ? 3   LYS B C   1 
ATOM   2175 O  O   . LYS B  1 3   ? 1.593   15.260  -2.926  1.00 31.17 ? 3   LYS B O   1 
ATOM   2176 C  CB  . LYS B  1 3   ? 0.754   17.813  -3.686  1.00 43.75 ? 3   LYS B CB  1 
ATOM   2177 C  CG  . LYS B  1 3   ? 1.603   18.554  -2.662  1.00 45.88 ? 3   LYS B CG  1 
ATOM   2178 C  CD  . LYS B  1 3   ? 2.197   19.841  -3.254  1.00 49.79 ? 3   LYS B CD  1 
ATOM   2179 C  CE  . LYS B  1 3   ? 3.190   19.557  -4.385  1.00 49.24 ? 3   LYS B CE  1 
ATOM   2180 N  NZ  . LYS B  1 3   ? 4.457   18.864  -3.975  1.00 43.03 ? 3   LYS B NZ  1 
ATOM   2181 N  N   . TRP B  1 4   ? 0.276   15.396  -1.064  1.00 18.16 ? 4   TRP B N   1 
ATOM   2182 C  CA  . TRP B  1 4   ? 0.924   14.225  -0.455  1.00 14.45 ? 4   TRP B CA  1 
ATOM   2183 C  C   . TRP B  1 4   ? 0.614   13.039  -1.325  1.00 12.86 ? 4   TRP B C   1 
ATOM   2184 O  O   . TRP B  1 4   ? -0.442  12.940  -2.027  1.00 15.29 ? 4   TRP B O   1 
ATOM   2185 C  CB  . TRP B  1 4   ? 0.431   14.026  1.021   1.00 12.56 ? 4   TRP B CB  1 
ATOM   2186 C  CG  . TRP B  1 4   ? -1.081  13.697  1.171   1.00 12.60 ? 4   TRP B CG  1 
ATOM   2187 C  CD1 . TRP B  1 4   ? -2.156  14.545  1.471   1.00 13.39 ? 4   TRP B CD1 1 
ATOM   2188 C  CD2 . TRP B  1 4   ? -1.680  12.348  1.153   1.00 12.89 ? 4   TRP B CD2 1 
ATOM   2189 N  NE1 . TRP B  1 4   ? -3.334  13.834  1.557   1.00 13.35 ? 4   TRP B NE1 1 
ATOM   2190 C  CE2 . TRP B  1 4   ? -3.081  12.515  1.390   1.00 12.43 ? 4   TRP B CE2 1 
ATOM   2191 C  CE3 . TRP B  1 4   ? -1.144  11.065  0.979   1.00 11.45 ? 4   TRP B CE3 1 
ATOM   2192 C  CZ2 . TRP B  1 4   ? -3.918  11.424  1.482   1.00 11.94 ? 4   TRP B CZ2 1 
ATOM   2193 C  CZ3 . TRP B  1 4   ? -2.011  9.975   0.998   1.00 11.29 ? 4   TRP B CZ3 1 
ATOM   2194 C  CH2 . TRP B  1 4   ? -3.355  10.167  1.209   1.00 12.12 ? 4   TRP B CH2 1 
ATOM   2195 N  N   . THR B  1 5   ? 1.563   12.086  -1.271  1.00 11.90 ? 5   THR B N   1 
ATOM   2196 C  CA  . THR B  1 5   ? 1.434   10.863  -2.131  1.00 12.00 ? 5   THR B CA  1 
ATOM   2197 C  C   . THR B  1 5   ? 1.889   9.622   -1.285  1.00 12.73 ? 5   THR B C   1 
ATOM   2198 O  O   . THR B  1 5   ? 2.324   9.790   -0.114  1.00 12.09 ? 5   THR B O   1 
ATOM   2199 C  CB  . THR B  1 5   ? 2.402   10.913  -3.348  1.00 14.36 ? 5   THR B CB  1 
ATOM   2200 O  OG1 . THR B  1 5   ? 3.721   10.970  -2.827  1.00 16.31 ? 5   THR B OG1 1 
ATOM   2201 C  CG2 . THR B  1 5   ? 2.174   12.200  -4.187  1.00 16.04 ? 5   THR B CG2 1 
ATOM   2202 N  N   . TYR B  1 6   ? 1.951   8.455   -1.904  1.00 13.45 ? 6   TYR B N   1 
ATOM   2203 C  CA  . TYR B  1 6   ? 2.579   7.307   -1.285  1.00 12.28 ? 6   TYR B CA  1 
ATOM   2204 C  C   . TYR B  1 6   ? 3.985   6.953   -1.874  1.00 14.13 ? 6   TYR B C   1 
ATOM   2205 O  O   . TYR B  1 6   ? 4.549   5.911   -1.559  1.00 14.49 ? 6   TYR B O   1 
ATOM   2206 C  CB  . TYR B  1 6   ? 1.671   6.106   -1.458  1.00 11.25 ? 6   TYR B CB  1 
ATOM   2207 C  CG  . TYR B  1 6   ? 0.427   6.142   -0.611  1.00 10.90 ? 6   TYR B CG  1 
ATOM   2208 C  CD1 . TYR B  1 6   ? -0.756  6.664   -1.106  1.00 10.39 ? 6   TYR B CD1 1 
ATOM   2209 C  CD2 . TYR B  1 6   ? 0.429   5.630   0.674   1.00 10.55 ? 6   TYR B CD2 1 
ATOM   2210 C  CE1 . TYR B  1 6   ? -1.908  6.682   -0.336  1.00 10.42 ? 6   TYR B CE1 1 
ATOM   2211 C  CE2 . TYR B  1 6   ? -0.714  5.644   1.449   1.00 10.09 ? 6   TYR B CE2 1 
ATOM   2212 C  CZ  . TYR B  1 6   ? -1.878  6.169   0.942   1.00 9.78  ? 6   TYR B CZ  1 
ATOM   2213 O  OH  . TYR B  1 6   ? -3.012  6.181   1.718   1.00 10.53 ? 6   TYR B OH  1 
ATOM   2214 N  N   . PHE B  1 7   ? 4.533   7.817   -2.734  1.00 17.19 ? 7   PHE B N   1 
ATOM   2215 C  CA  . PHE B  1 7   ? 5.794   7.462   -3.372  1.00 20.58 ? 7   PHE B CA  1 
ATOM   2216 C  C   . PHE B  1 7   ? 6.510   8.712   -3.761  1.00 21.64 ? 7   PHE B C   1 
ATOM   2217 O  O   . PHE B  1 7   ? 5.908   9.506   -4.457  1.00 23.08 ? 7   PHE B O   1 
ATOM   2218 C  CB  . PHE B  1 7   ? 5.535   6.688   -4.687  1.00 27.79 ? 7   PHE B CB  1 
ATOM   2219 C  CG  . PHE B  1 7   ? 6.802   6.329   -5.448  1.00 34.35 ? 7   PHE B CG  1 
ATOM   2220 C  CD1 . PHE B  1 7   ? 7.621   5.208   -5.063  1.00 34.80 ? 7   PHE B CD1 1 
ATOM   2221 C  CD2 . PHE B  1 7   ? 7.220   7.114   -6.559  1.00 37.22 ? 7   PHE B CD2 1 
ATOM   2222 C  CE1 . PHE B  1 7   ? 8.812   4.878   -5.757  1.00 36.11 ? 7   PHE B CE1 1 
ATOM   2223 C  CE2 . PHE B  1 7   ? 8.411   6.782   -7.252  1.00 38.29 ? 7   PHE B CE2 1 
ATOM   2224 C  CZ  . PHE B  1 7   ? 9.188   5.669   -6.859  1.00 40.94 ? 7   PHE B CZ  1 
ATOM   2225 N  N   . GLY B  1 8   ? 7.809   8.773   -3.480  1.00 21.70 ? 8   GLY B N   1 
ATOM   2226 C  CA  . GLY B  1 8   ? 8.606   9.905   -3.974  1.00 20.13 ? 8   GLY B CA  1 
ATOM   2227 C  C   . GLY B  1 8   ? 8.792   10.943  -2.896  1.00 22.00 ? 8   GLY B C   1 
ATOM   2228 O  O   . GLY B  1 8   ? 8.550   10.705  -1.712  1.00 21.13 ? 8   GLY B O   1 
ATOM   2229 N  N   . PRO B  1 9   ? 9.120   12.165  -3.273  1.00 21.54 ? 9   PRO B N   1 
ATOM   2230 C  CA  . PRO B  1 9   ? 9.425   13.191  -2.320  1.00 22.18 ? 9   PRO B CA  1 
ATOM   2231 C  C   . PRO B  1 9   ? 8.306   13.640  -1.451  1.00 18.97 ? 9   PRO B C   1 
ATOM   2232 O  O   . PRO B  1 9   ? 8.555   14.137  -0.366  1.00 21.13 ? 9   PRO B O   1 
ATOM   2233 C  CB  . PRO B  1 9   ? 9.889   14.383  -3.172  1.00 22.76 ? 9   PRO B CB  1 
ATOM   2234 C  CG  . PRO B  1 9   ? 9.943   13.875  -4.526  1.00 22.03 ? 9   PRO B CG  1 
ATOM   2235 C  CD  . PRO B  1 9   ? 9.336   12.539  -4.673  1.00 22.34 ? 9   PRO B CD  1 
ATOM   2236 N  N   . ASP B  1 10  ? 7.051   13.429  -1.893  1.00 16.78 ? 10  ASP B N   1 
ATOM   2237 C  CA  . ASP B  1 10  ? 5.904   13.757  -1.108  1.00 18.34 ? 10  ASP B CA  1 
ATOM   2238 C  C   . ASP B  1 10  ? 5.243   12.511  -0.417  1.00 13.79 ? 10  ASP B C   1 
ATOM   2239 O  O   . ASP B  1 10  ? 4.128   12.657  0.104   1.00 14.51 ? 10  ASP B O   1 
ATOM   2240 C  CB  . ASP B  1 10  ? 4.858   14.528  -1.951  1.00 18.31 ? 10  ASP B CB  1 
ATOM   2241 C  CG  . ASP B  1 10  ? 5.465   15.835  -2.516  1.00 23.96 ? 10  ASP B CG  1 
ATOM   2242 O  OD1 . ASP B  1 10  ? 6.123   16.549  -1.710  1.00 25.63 ? 10  ASP B OD1 1 
ATOM   2243 O  OD2 . ASP B  1 10  ? 5.326   16.076  -3.743  1.00 29.65 ? 10  ASP B OD2 1 
ATOM   2244 N  N   . GLY B  1 11  ? 6.061   11.459  -0.357  1.00 12.92 ? 11  GLY B N   1 
ATOM   2245 C  CA  . GLY B  1 11  ? 5.565   10.161  0.252   1.00 11.61 ? 11  GLY B CA  1 
ATOM   2246 C  C   . GLY B  1 11  ? 5.608   10.230  1.772   1.00 10.52 ? 11  GLY B C   1 
ATOM   2247 O  O   . GLY B  1 11  ? 5.808   11.271  2.436   1.00 10.32 ? 11  GLY B O   1 
ATOM   2248 N  N   . GLU B  1 12  ? 5.351   9.047   2.376   1.00 10.18 ? 12  GLU B N   1 
ATOM   2249 C  CA  . GLU B  1 12  ? 4.953   9.009   3.723   1.00 9.19  ? 12  GLU B CA  1 
ATOM   2250 C  C   . GLU B  1 12  ? 5.985   9.467   4.778   1.00 8.95  ? 12  GLU B C   1 
ATOM   2251 O  O   . GLU B  1 12  ? 5.628   9.902   5.842   1.00 9.10  ? 12  GLU B O   1 
ATOM   2252 C  CB  . GLU B  1 12  ? 4.502   7.537   4.070   1.00 9.61  ? 12  GLU B CB  1 
ATOM   2253 C  CG  . GLU B  1 12  ? 5.603   6.523   4.210   1.00 9.83  ? 12  GLU B CG  1 
ATOM   2254 C  CD  . GLU B  1 12  ? 5.038   5.155   4.164   1.00 8.88  ? 12  GLU B CD  1 
ATOM   2255 O  OE1 . GLU B  1 12  ? 4.646   4.654   5.266   1.00 9.69  ? 12  GLU B OE1 1 
ATOM   2256 O  OE2 . GLU B  1 12  ? 4.924   4.619   3.044   1.00 10.86 ? 12  GLU B OE2 1 
ATOM   2257 N  N   . ASN B  1 13  ? 7.302   9.355   4.436   1.00 10.11 ? 13  ASN B N   1 
ATOM   2258 C  CA  . ASN B  1 13  ? 8.316   9.884   5.398   1.00 9.97  ? 13  ASN B CA  1 
ATOM   2259 C  C   . ASN B  1 13  ? 8.334   11.410  5.458   1.00 11.04 ? 13  ASN B C   1 
ATOM   2260 O  O   . ASN B  1 13  ? 8.885   11.968  6.407   1.00 11.87 ? 13  ASN B O   1 
ATOM   2261 C  CB  . ASN B  1 13  ? 9.711   9.342   5.044   1.00 10.51 ? 13  ASN B CB  1 
ATOM   2262 C  CG  . ASN B  1 13  ? 9.883   7.873   5.322   1.00 10.23 ? 13  ASN B CG  1 
ATOM   2263 O  OD1 . ASN B  1 13  ? 8.980   7.209   5.859   1.00 10.90 ? 13  ASN B OD1 1 
ATOM   2264 N  ND2 . ASN B  1 13  ? 11.032  7.378   4.957   1.00 9.41  ? 13  ASN B ND2 1 
ATOM   2265 N  N   . SER B  1 14  ? 7.633   12.000  4.475   1.00 9.23  ? 14  SER B N   1 
ATOM   2266 C  CA  . SER B  1 14  ? 7.527   13.502  4.419   1.00 9.40  ? 14  SER B CA  1 
ATOM   2267 C  C   . SER B  1 14  ? 6.237   14.021  4.869   1.00 9.53  ? 14  SER B C   1 
ATOM   2268 O  O   . SER B  1 14  ? 6.074   15.276  4.982   1.00 11.20 ? 14  SER B O   1 
ATOM   2269 C  CB  . SER B  1 14  ? 7.852   14.016  3.031   1.00 10.48 ? 14  SER B CB  1 
ATOM   2270 O  OG  . SER B  1 14  ? 9.212   13.699  2.707   1.00 11.82 ? 14  SER B OG  1 
ATOM   2271 N  N   . TRP B  1 15  ? 5.223   13.200  5.144   1.00 9.05  ? 15  TRP B N   1 
ATOM   2272 C  CA  . TRP B  1 15  ? 3.915   13.805  5.482   1.00 9.84  ? 15  TRP B CA  1 
ATOM   2273 C  C   . TRP B  1 15  ? 3.970   14.645  6.671   1.00 10.14 ? 15  TRP B C   1 
ATOM   2274 O  O   . TRP B  1 15  ? 3.240   15.672  6.708   1.00 10.92 ? 15  TRP B O   1 
ATOM   2275 C  CB  . TRP B  1 15  ? 2.930   12.637  5.839   1.00 9.41  ? 15  TRP B CB  1 
ATOM   2276 C  CG  . TRP B  1 15  ? 2.571   11.759  4.677   1.00 8.99  ? 15  TRP B CG  1 
ATOM   2277 C  CD1 . TRP B  1 15  ? 2.805   11.914  3.334   1.00 9.84  ? 15  TRP B CD1 1 
ATOM   2278 C  CD2 . TRP B  1 15  ? 1.783   10.491  4.775   1.00 8.98  ? 15  TRP B CD2 1 
ATOM   2279 N  NE1 . TRP B  1 15  ? 2.231   10.851  2.568   1.00 9.75  ? 15  TRP B NE1 1 
ATOM   2280 C  CE2 . TRP B  1 15  ? 1.609   9.981   3.443   1.00 9.23  ? 15  TRP B CE2 1 
ATOM   2281 C  CE3 . TRP B  1 15  ? 1.221   9.783   5.879   1.00 8.23  ? 15  TRP B CE3 1 
ATOM   2282 C  CZ2 . TRP B  1 15  ? 0.890   8.793   3.180   1.00 9.18  ? 15  TRP B CZ2 1 
ATOM   2283 C  CZ3 . TRP B  1 15  ? 0.499   8.614   5.595   1.00 8.76  ? 15  TRP B CZ3 1 
ATOM   2284 C  CH2 . TRP B  1 15  ? 0.414   8.137   4.291   1.00 8.88  ? 15  TRP B CH2 1 
ATOM   2285 N  N   . SER B  1 16  ? 4.775   14.358  7.664   1.00 10.19 ? 16  SER B N   1 
ATOM   2286 C  CA  . SER B  1 16  ? 4.856   15.126  8.900   1.00 11.56 ? 16  SER B CA  1 
ATOM   2287 C  C   . SER B  1 16  ? 5.326   16.591  8.686   1.00 11.18 ? 16  SER B C   1 
ATOM   2288 O  O   . SER B  1 16  ? 5.066   17.404  9.560   1.00 13.49 ? 16  SER B O   1 
ATOM   2289 C  CB  . SER B  1 16  ? 5.868   14.460  9.928   1.00 12.19 ? 16  SER B CB  1 
ATOM   2290 O  OG  . SER B  1 16  ? 7.156   14.539  9.366   1.00 15.28 ? 16  SER B OG  1 
ATOM   2291 N  N   . LYS B  1 17  ? 5.945   16.863  7.526   1.00 11.43 ? 17  LYS B N   1 
ATOM   2292 C  CA  . LYS B  1 17  ? 6.406   18.241  7.226   1.00 11.14 ? 17  LYS B CA  1 
ATOM   2293 C  C   . LYS B  1 17  ? 5.187   19.109  7.144   1.00 12.04 ? 17  LYS B C   1 
ATOM   2294 O  O   . LYS B  1 17  ? 5.309   20.319  7.487   1.00 13.56 ? 17  LYS B O   1 
ATOM   2295 C  CB  . LYS B  1 17  ? 7.200   18.268  5.949   1.00 11.47 ? 17  LYS B CB  1 
ATOM   2296 C  CG  . LYS B  1 17  ? 8.503   17.440  5.927   1.00 13.34 ? 17  LYS B CG  1 
ATOM   2297 C  CD  . LYS B  1 17  ? 9.094   17.504  4.514   1.00 10.65 ? 17  LYS B CD  1 
ATOM   2298 C  CE  . LYS B  1 17  ? 10.235  16.542  4.299   1.00 11.17 ? 17  LYS B CE  1 
ATOM   2299 N  NZ  . LYS B  1 17  ? 10.877  16.639  3.019   1.00 11.70 ? 17  LYS B NZ  1 
ATOM   2300 N  N   . LYS B  1 18  ? 4.068   18.659  6.593   1.00 11.23 ? 18  LYS B N   1 
ATOM   2301 C  CA  . LYS B  1 18  ? 2.839   19.493  6.423   1.00 12.05 ? 18  LYS B CA  1 
ATOM   2302 C  C   . LYS B  1 18  ? 1.720   19.115  7.398   1.00 12.57 ? 18  LYS B C   1 
ATOM   2303 O  O   . LYS B  1 18  ? 0.826   19.905  7.653   1.00 13.38 ? 18  LYS B O   1 
ATOM   2304 C  CB  . LYS B  1 18  ? 2.332   19.279  5.029   1.00 13.42 ? 18  LYS B CB  1 
ATOM   2305 C  CG  . LYS B  1 18  ? 3.237   19.906  3.954   1.00 19.19 ? 18  LYS B CG  1 
ATOM   2306 C  CD  . LYS B  1 18  ? 2.789   19.618  2.503   1.00 23.25 ? 18  LYS B CD  1 
ATOM   2307 C  CE  . LYS B  1 18  ? 3.439   20.610  1.534   1.00 30.81 ? 18  LYS B CE  1 
ATOM   2308 N  NZ  . LYS B  1 18  ? 2.637   20.442  0.273   1.00 32.59 ? 18  LYS B NZ  1 
ATOM   2309 N  N   . TYR B  1 19  ? 1.762   17.872  7.932   1.00 11.66 ? 19  TYR B N   1 
ATOM   2310 C  CA  . TYR B  1 19  ? 0.691   17.304  8.764   1.00 12.59 ? 19  TYR B CA  1 
ATOM   2311 C  C   . TYR B  1 19  ? 1.291   16.817  10.036  1.00 12.15 ? 19  TYR B C   1 
ATOM   2312 O  O   . TYR B  1 19  ? 1.732   15.642  10.156  1.00 11.93 ? 19  TYR B O   1 
ATOM   2313 C  CB  . TYR B  1 19  ? -0.052  16.181  7.974   1.00 11.87 ? 19  TYR B CB  1 
ATOM   2314 C  CG  . TYR B  1 19  ? -0.619  16.617  6.672   1.00 11.47 ? 19  TYR B CG  1 
ATOM   2315 C  CD1 . TYR B  1 19  ? -1.868  17.198  6.610   1.00 13.62 ? 19  TYR B CD1 1 
ATOM   2316 C  CD2 . TYR B  1 19  ? 0.089   16.429  5.498   1.00 11.83 ? 19  TYR B CD2 1 
ATOM   2317 C  CE1 . TYR B  1 19  ? -2.406  17.594  5.409   1.00 15.15 ? 19  TYR B CE1 1 
ATOM   2318 C  CE2 . TYR B  1 19  ? -0.437  16.818  4.289   1.00 13.58 ? 19  TYR B CE2 1 
ATOM   2319 C  CZ  . TYR B  1 19  ? -1.686  17.400  4.255   1.00 16.46 ? 19  TYR B CZ  1 
ATOM   2320 O  OH  . TYR B  1 19  ? -2.226  17.795  3.060   1.00 21.60 ? 19  TYR B OH  1 
ATOM   2321 N  N   . PRO B  1 20  ? 1.445   17.661  11.064  1.00 12.59 ? 20  PRO B N   1 
ATOM   2322 C  CA  . PRO B  1 20  ? 2.203   17.300  12.214  1.00 13.46 ? 20  PRO B CA  1 
ATOM   2323 C  C   . PRO B  1 20  ? 1.694   16.041  12.925  1.00 12.12 ? 20  PRO B C   1 
ATOM   2324 O  O   . PRO B  1 20  ? 2.568   15.336  13.531  1.00 12.65 ? 20  PRO B O   1 
ATOM   2325 C  CB  . PRO B  1 20  ? 2.159   18.522  13.160  1.00 14.92 ? 20  PRO B CB  1 
ATOM   2326 C  CG  . PRO B  1 20  ? 1.839   19.629  12.248  1.00 16.37 ? 20  PRO B CG  1 
ATOM   2327 C  CD  . PRO B  1 20  ? 1.013   19.101  11.073  1.00 13.13 ? 20  PRO B CD  1 
ATOM   2328 N  N   . SER B  1 21  ? 0.395   15.734  12.851  1.00 11.48 ? 21  SER B N   1 
ATOM   2329 C  CA  . SER B  1 21  ? -0.027  14.521  13.604  1.00 11.62 ? 21  SER B CA  1 
ATOM   2330 C  C   . SER B  1 21  ? 0.586   13.262  12.948  1.00 10.81 ? 21  SER B C   1 
ATOM   2331 O  O   . SER B  1 21  ? 0.637   12.246  13.672  1.00 10.34 ? 21  SER B O   1 
ATOM   2332 C  CB  . SER B  1 21  ? -1.554  14.408  13.577  1.00 12.10 ? 21  SER B CB  1 
ATOM   2333 O  OG  . SER B  1 21  ? -2.071  15.484  14.371  1.00 14.20 ? 21  SER B OG  1 
ATOM   2334 N  N   . CYS B  1 22  ? 1.012   13.289  11.710  1.00 10.92 ? 22  CYS B N   1 
ATOM   2335 C  CA  . CYS B  1 22  ? 1.648   12.110  11.095  1.00 10.48 ? 22  CYS B CA  1 
ATOM   2336 C  C   . CYS B  1 22  ? 2.890   11.735  11.807  1.00 11.49 ? 22  CYS B C   1 
ATOM   2337 O  O   . CYS B  1 22  ? 3.373   10.642  11.603  1.00 12.88 ? 22  CYS B O   1 
ATOM   2338 C  CB  . CYS B  1 22  ? 1.826   12.318  9.579   1.00 11.14 ? 22  CYS B CB  1 
ATOM   2339 S  SG  . CYS B  1 22  ? 0.276   12.639  8.699   1.00 11.70 ? 22  CYS B SG  1 
ATOM   2340 N  N   . GLY B  1 23  ? 3.545   12.679  12.536  1.00 11.76 ? 23  GLY B N   1 
ATOM   2341 C  CA  . GLY B  1 23  ? 4.752   12.408  13.354  1.00 13.45 ? 23  GLY B CA  1 
ATOM   2342 C  C   . GLY B  1 23  ? 4.448   12.314  14.793  1.00 13.40 ? 23  GLY B C   1 
ATOM   2343 O  O   . GLY B  1 23  ? 5.388   12.314  15.631  1.00 14.99 ? 23  GLY B O   1 
ATOM   2344 N  N   . GLY B  1 24  ? 3.174   12.241  15.168  1.00 13.35 ? 24  GLY B N   1 
ATOM   2345 C  CA  . GLY B  1 24  ? 2.779   12.209  16.566  1.00 14.24 ? 24  GLY B CA  1 
ATOM   2346 C  C   . GLY B  1 24  ? 2.537   10.798  17.068  1.00 16.29 ? 24  GLY B C   1 
ATOM   2347 O  O   . GLY B  1 24  ? 3.030   9.829   16.484  1.00 17.83 ? 24  GLY B O   1 
ATOM   2348 N  N   . LEU B  1 25  ? 1.823   10.736  18.146  1.00 19.33 ? 25  LEU B N   1 
ATOM   2349 C  CA  . LEU B  1 25  ? 1.662   9.417   18.751  1.00 20.33 ? 25  LEU B CA  1 
ATOM   2350 C  C   . LEU B  1 25  ? 0.430   8.763   18.156  1.00 18.77 ? 25  LEU B C   1 
ATOM   2351 O  O   . LEU B  1 25  ? -0.336  9.345   17.372  1.00 15.77 ? 25  LEU B O   1 
ATOM   2352 C  CB  . LEU B  1 25  ? 1.677   9.484   20.296  1.00 28.24 ? 25  LEU B CB  1 
ATOM   2353 C  CG  . LEU B  1 25  ? 3.033   9.885   20.958  1.00 28.78 ? 25  LEU B CG  1 
ATOM   2354 C  CD1 . LEU B  1 25  ? 2.935   9.878   22.475  1.00 33.82 ? 25  LEU B CD1 1 
ATOM   2355 C  CD2 . LEU B  1 25  ? 4.221   9.062   20.441  1.00 37.29 ? 25  LEU B CD2 1 
ATOM   2356 N  N   . LEU B  1 26  ? 0.280   7.494   18.558  1.00 19.04 ? 26  LEU B N   1 
ATOM   2357 C  CA  . LEU B  1 26  ? -0.916  6.707   18.269  1.00 17.13 ? 26  LEU B CA  1 
ATOM   2358 C  C   . LEU B  1 26  ? -1.147  6.462   16.759  1.00 11.97 ? 26  LEU B C   1 
ATOM   2359 O  O   . LEU B  1 26  ? -2.334  6.337   16.353  1.00 13.21 ? 26  LEU B O   1 
ATOM   2360 C  CB  . LEU B  1 26  ? -2.200  7.275   18.886  1.00 18.85 ? 26  LEU B CB  1 
ATOM   2361 C  CG  . LEU B  1 26  ? -2.221  7.432   20.455  1.00 25.03 ? 26  LEU B CG  1 
ATOM   2362 C  CD1 . LEU B  1 26  ? -3.374  8.341   20.824  1.00 28.37 ? 26  LEU B CD1 1 
ATOM   2363 C  CD2 . LEU B  1 26  ? -2.282  6.119   21.193  1.00 26.69 ? 26  LEU B CD2 1 
ATOM   2364 N  N   . GLN B  1 27  ? -0.088  6.289   16.020  1.00 11.06 ? 27  GLN B N   1 
ATOM   2365 C  CA  . GLN B  1 27  ? -0.267  6.147   14.549  1.00 10.37 ? 27  GLN B CA  1 
ATOM   2366 C  C   . GLN B  1 27  ? -0.639  4.737   14.103  1.00 10.11 ? 27  GLN B C   1 
ATOM   2367 O  O   . GLN B  1 27  ? -0.219  3.746   14.701  1.00 11.93 ? 27  GLN B O   1 
ATOM   2368 C  CB  . GLN B  1 27  ? 0.961   6.655   13.839  1.00 10.67 ? 27  GLN B CB  1 
ATOM   2369 C  CG  . GLN B  1 27  ? 1.183   8.163   14.118  1.00 11.10 ? 27  GLN B CG  1 
ATOM   2370 C  CD  . GLN B  1 27  ? 0.112   8.999   13.431  1.00 8.22  ? 27  GLN B CD  1 
ATOM   2371 O  OE1 . GLN B  1 27  ? 0.129   9.107   12.176  1.00 10.14 ? 27  GLN B OE1 1 
ATOM   2372 N  NE2 . GLN B  1 27  ? -0.777  9.491   14.187  1.00 9.76  ? 27  GLN B NE2 1 
ATOM   2373 N  N   . SER B  1 28  ? -1.403  4.671   13.046  1.00 8.53  ? 28  SER B N   1 
ATOM   2374 C  CA  . SER B  1 28  ? -1.740  3.459   12.363  1.00 8.54  ? 28  SER B CA  1 
ATOM   2375 C  C   . SER B  1 28  ? -1.231  3.464   10.997  1.00 9.90  ? 28  SER B C   1 
ATOM   2376 O  O   . SER B  1 28  ? -0.966  4.520   10.410  1.00 9.72  ? 28  SER B O   1 
ATOM   2377 C  CB  . SER B  1 28  ? -3.278  3.474   12.339  1.00 9.64  ? 28  SER B CB  1 
ATOM   2378 O  OG  . SER B  1 28  ? -3.833  3.315   13.651  1.00 8.97  ? 28  SER B OG  1 
ATOM   2379 N  N   . PRO B  1 29  ? -1.121  2.351   10.297  1.00 7.84  ? 29  PRO B N   1 
ATOM   2380 C  CA  . PRO B  1 29  ? -1.442  0.946   10.791  1.00 8.40  ? 29  PRO B CA  1 
ATOM   2381 C  C   . PRO B  1 29  ? -0.300  0.382   11.606  1.00 8.52  ? 29  PRO B C   1 
ATOM   2382 O  O   . PRO B  1 29  ? 0.741   0.992   11.784  1.00 8.48  ? 29  PRO B O   1 
ATOM   2383 C  CB  . PRO B  1 29  ? -1.658  0.212   9.413   1.00 9.09  ? 29  PRO B CB  1 
ATOM   2384 C  CG  . PRO B  1 29  ? -0.526  0.778   8.586   1.00 8.16  ? 29  PRO B CG  1 
ATOM   2385 C  CD  . PRO B  1 29  ? -0.663  2.271   8.900   1.00 9.87  ? 29  PRO B CD  1 
ATOM   2386 N  N   . ILE B  1 30  ? -0.566  -0.834  12.088  1.00 9.32  ? 30  ILE B N   1 
ATOM   2387 C  CA  . ILE B  1 30  ? 0.419   -1.572  12.908  1.00 9.09  ? 30  ILE B CA  1 
ATOM   2388 C  C   . ILE B  1 30  ? 0.433   -3.029  12.433  1.00 8.63  ? 30  ILE B C   1 
ATOM   2389 O  O   . ILE B  1 30  ? -0.437  -3.536  11.757  1.00 8.81  ? 30  ILE B O   1 
ATOM   2390 C  CB  . ILE B  1 30  ? 0.143   -1.473  14.408  1.00 10.02 ? 30  ILE B CB  1 
ATOM   2391 C  CG1 . ILE B  1 30  ? -1.290  -2.037  14.689  1.00 11.21 ? 30  ILE B CG1 1 
ATOM   2392 C  CG2 . ILE B  1 30  ? 0.265   0.047   14.864  1.00 10.88 ? 30  ILE B CG2 1 
ATOM   2393 C  CD1 . ILE B  1 30  ? -1.534  -2.085  16.162  1.00 14.28 ? 30  ILE B CD1 1 
ATOM   2394 N  N   . ASP B  1 31  ? 1.552   -3.687  12.825  1.00 9.00  ? 31  ASP B N   1 
ATOM   2395 C  CA  . ASP B  1 31  ? 1.708   -5.130  12.717  1.00 10.38 ? 31  ASP B CA  1 
ATOM   2396 C  C   . ASP B  1 31  ? 1.082   -5.823  13.930  1.00 10.75 ? 31  ASP B C   1 
ATOM   2397 O  O   . ASP B  1 31  ? 1.484   -5.589  15.060  1.00 12.48 ? 31  ASP B O   1 
ATOM   2398 C  CB  . ASP B  1 31  ? 3.181   -5.505  12.672  1.00 10.48 ? 31  ASP B CB  1 
ATOM   2399 C  CG  . ASP B  1 31  ? 3.282   -7.020  12.525  1.00 13.72 ? 31  ASP B CG  1 
ATOM   2400 O  OD1 . ASP B  1 31  ? 2.784   -7.626  11.539  1.00 13.31 ? 31  ASP B OD1 1 
ATOM   2401 O  OD2 . ASP B  1 31  ? 3.964   -7.615  13.379  1.00 16.52 ? 31  ASP B OD2 1 
ATOM   2402 N  N   . LEU B  1 32  ? 0.128   -6.705  13.608  1.00 10.02 ? 32  LEU B N   1 
ATOM   2403 C  CA  . LEU B  1 32  ? -0.561  -7.468  14.688  1.00 12.40 ? 32  LEU B CA  1 
ATOM   2404 C  C   . LEU B  1 32  ? 0.235   -8.715  14.988  1.00 12.79 ? 32  LEU B C   1 
ATOM   2405 O  O   . LEU B  1 32  ? 0.206   -9.590  14.153  1.00 15.18 ? 32  LEU B O   1 
ATOM   2406 C  CB  . LEU B  1 32  ? -1.997  -7.810  14.180  1.00 12.44 ? 32  LEU B CB  1 
ATOM   2407 C  CG  . LEU B  1 32  ? -2.769  -6.505  13.828  1.00 13.61 ? 32  LEU B CG  1 
ATOM   2408 C  CD1 . LEU B  1 32  ? -4.096  -6.825  13.074  1.00 15.62 ? 32  LEU B CD1 1 
ATOM   2409 C  CD2 . LEU B  1 32  ? -3.065  -5.629  15.023  1.00 15.23 ? 32  LEU B CD2 1 
ATOM   2410 N  N   . HIS B  1 33  ? 0.945   -8.814  16.105  1.00 12.12 ? 33  HIS B N   1 
ATOM   2411 C  CA  . HIS B  1 33  ? 1.766   -9.984  16.349  1.00 13.00 ? 33  HIS B CA  1 
ATOM   2412 C  C   . HIS B  1 33  ? 1.636   -10.252 17.828  1.00 12.03 ? 33  HIS B C   1 
ATOM   2413 O  O   . HIS B  1 33  ? 1.312   -9.422  18.667  1.00 13.19 ? 33  HIS B O   1 
ATOM   2414 C  CB  . HIS B  1 33  ? 3.229   -9.729  15.911  1.00 15.65 ? 33  HIS B CB  1 
ATOM   2415 C  CG  . HIS B  1 33  ? 3.895   -8.558  16.630  1.00 16.81 ? 33  HIS B CG  1 
ATOM   2416 N  ND1 . HIS B  1 33  ? 3.654   -7.248  16.363  1.00 21.28 ? 33  HIS B ND1 1 
ATOM   2417 C  CD2 . HIS B  1 33  ? 4.822   -8.571  17.682  1.00 14.88 ? 33  HIS B CD2 1 
ATOM   2418 C  CE1 . HIS B  1 33  ? 4.389   -6.483  17.210  1.00 22.84 ? 33  HIS B CE1 1 
ATOM   2419 N  NE2 . HIS B  1 33  ? 5.128   -7.306  17.974  1.00 16.91 ? 33  HIS B NE2 1 
ATOM   2420 N  N   . SER B  1 34  ? 2.015   -11.514 18.180  1.00 13.54 ? 34  SER B N   1 
ATOM   2421 C  CA  . SER B  1 34  ? 1.656   -12.086 19.503  1.00 14.69 ? 34  SER B CA  1 
ATOM   2422 C  C   . SER B  1 34  ? 2.148   -11.251 20.668  1.00 13.90 ? 34  SER B C   1 
ATOM   2423 O  O   . SER B  1 34  ? 1.445   -11.131 21.682  1.00 13.62 ? 34  SER B O   1 
ATOM   2424 C  CB  . SER B  1 34  ? 2.189   -13.537 19.563  1.00 16.34 ? 34  SER B CB  1 
ATOM   2425 O  OG  . SER B  1 34  ? 3.606   -13.496 19.606  1.00 21.48 ? 34  SER B OG  1 
ATOM   2426 N  N   . ASP B  1 35  ? 3.345   -10.641 20.623  1.00 13.89 ? 35  ASP B N   1 
ATOM   2427 C  CA  . ASP B  1 35  ? 3.857   -9.969  21.811  1.00 15.34 ? 35  ASP B CA  1 
ATOM   2428 C  C   . ASP B  1 35  ? 3.079   -8.827  22.309  1.00 15.87 ? 35  ASP B C   1 
ATOM   2429 O  O   . ASP B  1 35  ? 3.178   -8.367  23.456  1.00 18.13 ? 35  ASP B O   1 
ATOM   2430 C  CB  . ASP B  1 35  ? 5.295   -9.399  21.545  1.00 19.71 ? 35  ASP B CB  1 
ATOM   2431 C  CG  . ASP B  1 35  ? 6.184   -10.421 20.897  1.00 19.34 ? 35  ASP B CG  1 
ATOM   2432 O  OD1 . ASP B  1 35  ? 5.905   -10.839 19.758  1.00 20.51 ? 35  ASP B OD1 1 
ATOM   2433 O  OD2 . ASP B  1 35  ? 7.188   -10.869 21.573  1.00 19.74 ? 35  ASP B OD2 1 
ATOM   2434 N  N   . ILE B  1 36  ? 2.218   -8.267  21.443  1.00 15.38 ? 36  ILE B N   1 
ATOM   2435 C  CA  . ILE B  1 36  ? 1.501   -7.110  21.799  1.00 14.88 ? 36  ILE B CA  1 
ATOM   2436 C  C   . ILE B  1 36  ? -0.049  -7.336  21.851  1.00 14.64 ? 36  ILE B C   1 
ATOM   2437 O  O   . ILE B  1 36  ? -0.826  -6.392  22.043  1.00 14.85 ? 36  ILE B O   1 
ATOM   2438 C  CB  . ILE B  1 36  ? 1.762   -5.829  20.896  1.00 17.03 ? 36  ILE B CB  1 
ATOM   2439 C  CG1 . ILE B  1 36  ? 1.667   -6.097  19.409  1.00 19.22 ? 36  ILE B CG1 1 
ATOM   2440 C  CG2 . ILE B  1 36  ? 3.175   -5.245  21.130  1.00 20.69 ? 36  ILE B CG2 1 
ATOM   2441 C  CD1 . ILE B  1 36  ? 0.340   -6.304  18.850  1.00 20.61 ? 36  ILE B CD1 1 
ATOM   2442 N  N   . LEU B  1 37  ? -0.452  -8.580  21.697  1.00 13.46 ? 37  LEU B N   1 
ATOM   2443 C  CA  . LEU B  1 37  ? -1.878  -9.007  21.756  1.00 14.90 ? 37  LEU B CA  1 
ATOM   2444 C  C   . LEU B  1 37  ? -2.282  -9.311  23.176  1.00 17.59 ? 37  LEU B C   1 
ATOM   2445 O  O   . LEU B  1 37  ? -1.532  -9.961  23.891  1.00 18.20 ? 37  LEU B O   1 
ATOM   2446 C  CB  . LEU B  1 37  ? -2.187  -10.162 20.835  1.00 14.61 ? 37  LEU B CB  1 
ATOM   2447 C  CG  . LEU B  1 37  ? -1.902  -9.949  19.313  1.00 14.18 ? 37  LEU B CG  1 
ATOM   2448 C  CD1 . LEU B  1 37  ? -2.205  -11.229 18.572  1.00 16.23 ? 37  LEU B CD1 1 
ATOM   2449 C  CD2 . LEU B  1 37  ? -2.640  -8.749  18.768  1.00 14.36 ? 37  LEU B CD2 1 
ATOM   2450 N  N   . GLN B  1 38  ? -3.482  -8.969  23.567  1.00 14.74 ? 38  GLN B N   1 
ATOM   2451 C  CA  . GLN B  1 38  ? -3.995  -9.416  24.889  1.00 16.67 ? 38  GLN B CA  1 
ATOM   2452 C  C   . GLN B  1 38  ? -5.482  -9.641  24.739  1.00 16.94 ? 38  GLN B C   1 
ATOM   2453 O  O   . GLN B  1 38  ? -6.236  -8.753  24.332  1.00 14.61 ? 38  GLN B O   1 
ATOM   2454 C  CB  . GLN B  1 38  ? -3.800  -8.353  25.931  1.00 18.13 ? 38  GLN B CB  1 
ATOM   2455 C  CG  . GLN B  1 38  ? -4.191  -8.880  27.290  1.00 23.61 ? 38  GLN B CG  1 
ATOM   2456 C  CD  . GLN B  1 38  ? -3.643  -7.995  28.298  1.00 28.64 ? 38  GLN B CD  1 
ATOM   2457 O  OE1 . GLN B  1 38  ? -2.449  -8.088  28.581  1.00 39.82 ? 38  GLN B OE1 1 
ATOM   2458 N  NE2 . GLN B  1 38  ? -4.447  -7.083  28.809  1.00 32.56 ? 38  GLN B NE2 1 
ATOM   2459 N  N   . TYR B  1 39  ? -5.953  -10.819 25.115  1.00 14.21 ? 39  TYR B N   1 
ATOM   2460 C  CA  . TYR B  1 39  ? -7.392  -11.112 25.097  1.00 13.89 ? 39  TYR B CA  1 
ATOM   2461 C  C   . TYR B  1 39  ? -8.133  -10.220 26.080  1.00 12.84 ? 39  TYR B C   1 
ATOM   2462 O  O   . TYR B  1 39  ? -7.662  -9.930  27.236  1.00 14.11 ? 39  TYR B O   1 
ATOM   2463 C  CB  . TYR B  1 39  ? -7.569  -12.582 25.507  1.00 14.78 ? 39  TYR B CB  1 
ATOM   2464 C  CG  . TYR B  1 39  ? -9.014  -12.981 25.688  1.00 13.79 ? 39  TYR B CG  1 
ATOM   2465 C  CD1 . TYR B  1 39  ? -9.935  -12.940 24.651  1.00 15.32 ? 39  TYR B CD1 1 
ATOM   2466 C  CD2 . TYR B  1 39  ? -9.474  -13.377 26.998  1.00 15.80 ? 39  TYR B CD2 1 
ATOM   2467 C  CE1 . TYR B  1 39  ? -11.254 -13.312 24.794  1.00 15.34 ? 39  TYR B CE1 1 
ATOM   2468 C  CE2 . TYR B  1 39  ? -10.806 -13.704 27.155  1.00 16.86 ? 39  TYR B CE2 1 
ATOM   2469 C  CZ  . TYR B  1 39  ? -11.684 -13.715 26.083  1.00 16.25 ? 39  TYR B CZ  1 
ATOM   2470 O  OH  . TYR B  1 39  ? -13.009 -14.041 26.186  1.00 18.46 ? 39  TYR B OH  1 
ATOM   2471 N  N   . ASP B  1 40  ? -9.282  -9.730  25.650  1.00 13.16 ? 40  ASP B N   1 
ATOM   2472 C  CA  . ASP B  1 40  ? -10.101 -8.853  26.517  1.00 14.07 ? 40  ASP B CA  1 
ATOM   2473 C  C   . ASP B  1 40  ? -11.493 -9.404  26.408  1.00 14.64 ? 40  ASP B C   1 
ATOM   2474 O  O   . ASP B  1 40  ? -12.198 -9.179  25.418  1.00 12.39 ? 40  ASP B O   1 
ATOM   2475 C  CB  . ASP B  1 40  ? -9.975  -7.386  26.087  1.00 14.18 ? 40  ASP B CB  1 
ATOM   2476 C  CG  . ASP B  1 40  ? -10.786 -6.470  26.914  1.00 17.60 ? 40  ASP B CG  1 
ATOM   2477 O  OD1 . ASP B  1 40  ? -11.606 -6.942  27.684  1.00 17.11 ? 40  ASP B OD1 1 
ATOM   2478 O  OD2 . ASP B  1 40  ? -10.649 -5.242  26.717  1.00 22.53 ? 40  ASP B OD2 1 
ATOM   2479 N  N   . ALA B  1 41  ? -12.051 -10.068 27.455  1.00 16.06 ? 41  ALA B N   1 
ATOM   2480 C  CA  . ALA B  1 41  ? -13.386 -10.643 27.384  1.00 16.41 ? 41  ALA B CA  1 
ATOM   2481 C  C   . ALA B  1 41  ? -14.515 -9.624  27.305  1.00 15.77 ? 41  ALA B C   1 
ATOM   2482 O  O   . ALA B  1 41  ? -15.681 -9.988  26.934  1.00 18.72 ? 41  ALA B O   1 
ATOM   2483 C  CB  . ALA B  1 41  ? -13.554 -11.525 28.646  1.00 17.72 ? 41  ALA B CB  1 
ATOM   2484 N  N   A SER B  1 42  ? -14.185 -8.337  27.578  0.50 15.82 ? 42  SER B N   1 
ATOM   2485 N  N   B SER B  1 42  ? -14.256 -8.361  27.579  0.50 17.41 ? 42  SER B N   1 
ATOM   2486 C  CA  A SER B  1 42  ? -15.110 -7.193  27.422  0.50 15.48 ? 42  SER B CA  1 
ATOM   2487 C  CA  B SER B  1 42  ? -15.361 -7.477  27.447  0.50 16.84 ? 42  SER B CA  1 
ATOM   2488 C  C   A SER B  1 42  ? -15.361 -6.730  25.964  0.50 14.61 ? 42  SER B C   1 
ATOM   2489 C  C   B SER B  1 42  ? -15.561 -6.995  25.986  0.50 17.33 ? 42  SER B C   1 
ATOM   2490 O  O   A SER B  1 42  ? -16.214 -5.848  25.637  0.50 13.45 ? 42  SER B O   1 
ATOM   2491 O  O   B SER B  1 42  ? -16.537 -6.293  25.686  0.50 17.83 ? 42  SER B O   1 
ATOM   2492 C  CB  A SER B  1 42  ? -14.594 -5.961  28.184  0.50 16.02 ? 42  SER B CB  1 
ATOM   2493 C  CB  B SER B  1 42  ? -15.144 -6.292  28.363  0.50 21.57 ? 42  SER B CB  1 
ATOM   2494 O  OG  A SER B  1 42  ? -13.800 -5.083  27.454  0.50 18.24 ? 42  SER B OG  1 
ATOM   2495 O  OG  B SER B  1 42  ? -14.813 -6.797  29.646  0.50 21.17 ? 42  SER B OG  1 
ATOM   2496 N  N   . LEU B  1 43  ? -14.663 -7.376  25.062  1.00 14.28 ? 43  LEU B N   1 
ATOM   2497 C  CA  . LEU B  1 43  ? -14.871 -7.085  23.592  1.00 14.37 ? 43  LEU B CA  1 
ATOM   2498 C  C   . LEU B  1 43  ? -15.985 -7.958  23.047  1.00 13.26 ? 43  LEU B C   1 
ATOM   2499 O  O   . LEU B  1 43  ? -15.755 -8.994  22.385  1.00 15.65 ? 43  LEU B O   1 
ATOM   2500 C  CB  . LEU B  1 43  ? -13.577 -7.262  22.841  1.00 12.78 ? 43  LEU B CB  1 
ATOM   2501 C  CG  . LEU B  1 43  ? -12.537 -6.269  23.224  1.00 11.40 ? 43  LEU B CG  1 
ATOM   2502 C  CD1 . LEU B  1 43  ? -11.262 -6.601  22.490  1.00 14.21 ? 43  LEU B CD1 1 
ATOM   2503 C  CD2 . LEU B  1 43  ? -12.876 -4.800  22.912  1.00 13.64 ? 43  LEU B CD2 1 
ATOM   2504 N  N   . THR B  1 44  ? -17.213 -7.473  23.294  1.00 14.99 ? 44  THR B N   1 
ATOM   2505 C  CA  . THR B  1 44  ? -18.409 -8.177  22.840  1.00 16.14 ? 44  THR B CA  1 
ATOM   2506 C  C   . THR B  1 44  ? -18.724 -7.919  21.373  1.00 14.51 ? 44  THR B C   1 
ATOM   2507 O  O   . THR B  1 44  ? -18.098 -7.012  20.746  1.00 14.75 ? 44  THR B O   1 
ATOM   2508 C  CB  . THR B  1 44  ? -19.571 -7.725  23.776  1.00 17.77 ? 44  THR B CB  1 
ATOM   2509 O  OG1 . THR B  1 44  ? -19.580 -6.328  23.819  1.00 23.41 ? 44  THR B OG1 1 
ATOM   2510 C  CG2 . THR B  1 44  ? -19.295 -8.246  25.266  1.00 20.24 ? 44  THR B CG2 1 
ATOM   2511 N  N   . PRO B  1 45  ? -19.631 -8.682  20.763  1.00 15.15 ? 45  PRO B N   1 
ATOM   2512 C  CA  . PRO B  1 45  ? -19.824 -8.531  19.317  1.00 14.89 ? 45  PRO B CA  1 
ATOM   2513 C  C   . PRO B  1 45  ? -20.440 -7.201  18.889  1.00 15.79 ? 45  PRO B C   1 
ATOM   2514 O  O   . PRO B  1 45  ? -21.266 -6.612  19.584  1.00 18.14 ? 45  PRO B O   1 
ATOM   2515 C  CB  . PRO B  1 45  ? -20.682 -9.710  18.938  1.00 18.15 ? 45  PRO B CB  1 
ATOM   2516 C  CG  . PRO B  1 45  ? -20.454 -10.743 20.104  1.00 15.07 ? 45  PRO B CG  1 
ATOM   2517 C  CD  . PRO B  1 45  ? -20.350 -9.864  21.293  1.00 15.73 ? 45  PRO B CD  1 
ATOM   2518 N  N   . LEU B  1 46  ? -20.009 -6.726  17.720  1.00 13.50 ? 46  LEU B N   1 
ATOM   2519 C  CA  . LEU B  1 46  ? -20.686 -5.564  17.190  1.00 14.25 ? 46  LEU B CA  1 
ATOM   2520 C  C   . LEU B  1 46  ? -21.901 -6.057  16.404  1.00 12.92 ? 46  LEU B C   1 
ATOM   2521 O  O   . LEU B  1 46  ? -21.965 -7.175  15.874  1.00 14.29 ? 46  LEU B O   1 
ATOM   2522 C  CB  . LEU B  1 46  ? -19.750 -4.864  16.157  1.00 15.07 ? 46  LEU B CB  1 
ATOM   2523 C  CG  . LEU B  1 46  ? -18.510 -4.209  16.790  1.00 18.61 ? 46  LEU B CG  1 
ATOM   2524 C  CD1 . LEU B  1 46  ? -17.637 -3.692  15.642  1.00 17.98 ? 46  LEU B CD1 1 
ATOM   2525 C  CD2 . LEU B  1 46  ? -18.812 -3.145  17.821  1.00 20.74 ? 46  LEU B CD2 1 
ATOM   2526 N  N   . GLU B  1 47  ? -22.854 -5.146  16.305  1.00 15.09 ? 47  GLU B N   1 
ATOM   2527 C  CA  . GLU B  1 47  ? -23.994 -5.375  15.413  1.00 17.08 ? 47  GLU B CA  1 
ATOM   2528 C  C   . GLU B  1 47  ? -24.045 -4.289  14.299  1.00 12.80 ? 47  GLU B C   1 
ATOM   2529 O  O   . GLU B  1 47  ? -23.805 -3.091  14.600  1.00 17.89 ? 47  GLU B O   1 
ATOM   2530 C  CB  . GLU B  1 47  ? -25.321 -5.298  16.229  1.00 18.40 ? 47  GLU B CB  1 
ATOM   2531 C  CG  . GLU B  1 47  ? -25.471 -6.438  17.263  1.00 24.48 ? 47  GLU B CG  1 
ATOM   2532 C  CD  . GLU B  1 47  ? -26.791 -6.324  18.040  1.00 34.08 ? 47  GLU B CD  1 
ATOM   2533 O  OE1 . GLU B  1 47  ? -27.085 -5.269  18.676  1.00 38.41 ? 47  GLU B OE1 1 
ATOM   2534 O  OE2 . GLU B  1 47  ? -27.540 -7.314  18.004  1.00 42.96 ? 47  GLU B OE2 1 
ATOM   2535 N  N   . PHE B  1 48  ? -24.275 -4.772  13.106  1.00 15.27 ? 48  PHE B N   1 
ATOM   2536 C  CA  . PHE B  1 48  ? -24.250 -3.905  11.923  1.00 14.47 ? 48  PHE B CA  1 
ATOM   2537 C  C   . PHE B  1 48  ? -25.661 -3.576  11.490  1.00 16.25 ? 48  PHE B C   1 
ATOM   2538 O  O   . PHE B  1 48  ? -26.350 -4.499  11.019  1.00 21.62 ? 48  PHE B O   1 
ATOM   2539 C  CB  . PHE B  1 48  ? -23.455 -4.567  10.804  1.00 15.70 ? 48  PHE B CB  1 
ATOM   2540 C  CG  . PHE B  1 48  ? -22.140 -5.119  11.315  1.00 15.17 ? 48  PHE B CG  1 
ATOM   2541 C  CD1 . PHE B  1 48  ? -21.116 -4.268  11.625  1.00 14.75 ? 48  PHE B CD1 1 
ATOM   2542 C  CD2 . PHE B  1 48  ? -21.971 -6.509  11.582  1.00 16.06 ? 48  PHE B CD2 1 
ATOM   2543 C  CE1 . PHE B  1 48  ? -19.917 -4.712  12.225  1.00 14.39 ? 48  PHE B CE1 1 
ATOM   2544 C  CE2 . PHE B  1 48  ? -20.785 -6.969  12.137  1.00 16.80 ? 48  PHE B CE2 1 
ATOM   2545 C  CZ  . PHE B  1 48  ? -19.770 -6.069  12.463  1.00 14.71 ? 48  PHE B CZ  1 
ATOM   2546 N  N   . GLN B  1 49  ? -26.051 -2.323  11.688  1.00 15.17 ? 49  GLN B N   1 
ATOM   2547 C  CA  . GLN B  1 49  ? -27.471 -1.895  11.512  1.00 15.35 ? 49  GLN B CA  1 
ATOM   2548 C  C   . GLN B  1 49  ? -27.594 -1.056  10.284  1.00 14.30 ? 49  GLN B C   1 
ATOM   2549 O  O   . GLN B  1 49  ? -26.802 -0.141  10.063  1.00 12.91 ? 49  GLN B O   1 
ATOM   2550 C  CB  . GLN B  1 49  ? -27.924 -1.086  12.701  1.00 15.75 ? 49  GLN B CB  1 
ATOM   2551 C  CG  . GLN B  1 49  ? -27.766 -1.831  14.003  1.00 22.50 ? 49  GLN B CG  1 
ATOM   2552 C  CD  . GLN B  1 49  ? -28.595 -3.063  14.008  1.00 29.03 ? 49  GLN B CD  1 
ATOM   2553 O  OE1 . GLN B  1 49  ? -28.082 -4.221  14.132  1.00 32.88 ? 49  GLN B OE1 1 
ATOM   2554 N  NE2 . GLN B  1 49  ? -29.916 -2.865  13.820  1.00 30.98 ? 49  GLN B NE2 1 
ATOM   2555 N  N   . GLY B  1 50  ? -28.559 -1.332  9.452   1.00 15.36 ? 50  GLY B N   1 
ATOM   2556 C  CA  . GLY B  1 50  ? -28.777 -0.470  8.244   1.00 13.14 ? 50  GLY B CA  1 
ATOM   2557 C  C   . GLY B  1 50  ? -27.711 -0.652  7.195   1.00 14.28 ? 50  GLY B C   1 
ATOM   2558 O  O   . GLY B  1 50  ? -27.562 0.210   6.346   1.00 14.04 ? 50  GLY B O   1 
ATOM   2559 N  N   . TYR B  1 51  ? -26.932 -1.722  7.306   1.00 11.99 ? 51  TYR B N   1 
ATOM   2560 C  CA  . TYR B  1 51  ? -25.978 -2.089  6.229   1.00 10.71 ? 51  TYR B CA  1 
ATOM   2561 C  C   . TYR B  1 51  ? -26.527 -2.546  4.929   1.00 11.25 ? 51  TYR B C   1 
ATOM   2562 O  O   . TYR B  1 51  ? -25.909 -2.592  3.926   1.00 11.72 ? 51  TYR B O   1 
ATOM   2563 C  CB  . TYR B  1 51  ? -24.946 -3.161  6.749   1.00 10.44 ? 51  TYR B CB  1 
ATOM   2564 C  CG  . TYR B  1 51  ? -23.761 -2.593  7.511   1.00 10.94 ? 51  TYR B CG  1 
ATOM   2565 C  CD1 . TYR B  1 51  ? -23.881 -1.642  8.533   1.00 9.93  ? 51  TYR B CD1 1 
ATOM   2566 C  CD2 . TYR B  1 51  ? -22.475 -3.101  7.237   1.00 9.47  ? 51  TYR B CD2 1 
ATOM   2567 C  CE1 . TYR B  1 51  ? -22.811 -1.096  9.257   1.00 10.92 ? 51  TYR B CE1 1 
ATOM   2568 C  CE2 . TYR B  1 51  ? -21.376 -2.537  7.949   1.00 10.89 ? 51  TYR B CE2 1 
ATOM   2569 C  CZ  . TYR B  1 51  ? -21.537 -1.561  8.896   1.00 10.89 ? 51  TYR B CZ  1 
ATOM   2570 O  OH  . TYR B  1 51  ? -20.431 -1.043  9.558   1.00 12.23 ? 51  TYR B OH  1 
ATOM   2571 N  N   . ASN B  1 52  ? -27.779 -3.085  4.964   1.00 11.82 ? 52  ASN B N   1 
ATOM   2572 C  CA  . ASN B  1 52  ? -28.397 -3.592  3.753   1.00 11.80 ? 52  ASN B CA  1 
ATOM   2573 C  C   . ASN B  1 52  ? -29.045 -2.457  2.954   1.00 15.52 ? 52  ASN B C   1 
ATOM   2574 O  O   . ASN B  1 52  ? -30.218 -2.078  3.173   1.00 15.86 ? 52  ASN B O   1 
ATOM   2575 C  CB  . ASN B  1 52  ? -29.481 -4.621  4.159   1.00 13.89 ? 52  ASN B CB  1 
ATOM   2576 C  CG  . ASN B  1 52  ? -30.050 -5.311  2.987   1.00 18.64 ? 52  ASN B CG  1 
ATOM   2577 O  OD1 . ASN B  1 52  ? -29.716 -5.064  1.848   1.00 24.38 ? 52  ASN B OD1 1 
ATOM   2578 N  ND2 . ASN B  1 52  ? -31.066 -6.158  3.272   1.00 21.25 ? 52  ASN B ND2 1 
ATOM   2579 N  N   . LEU B  1 53  ? -28.223 -1.806  2.142   1.00 13.10 ? 53  LEU B N   1 
ATOM   2580 C  CA  . LEU B  1 53  ? -28.689 -0.566  1.483   1.00 12.19 ? 53  LEU B CA  1 
ATOM   2581 C  C   . LEU B  1 53  ? -29.625 -1.039  0.281   1.00 11.06 ? 53  LEU B C   1 
ATOM   2582 O  O   . LEU B  1 53  ? -29.379 -1.979  -0.447  1.00 13.27 ? 53  LEU B O   1 
ATOM   2583 C  CB  . LEU B  1 53  ? -27.478 0.151   0.860   1.00 12.47 ? 53  LEU B CB  1 
ATOM   2584 C  CG  . LEU B  1 53  ? -26.387 0.546   1.885   1.00 12.93 ? 53  LEU B CG  1 
ATOM   2585 C  CD1 . LEU B  1 53  ? -25.290 1.263   1.107   1.00 14.95 ? 53  LEU B CD1 1 
ATOM   2586 C  CD2 . LEU B  1 53  ? -26.886 1.381   3.014   1.00 14.42 ? 53  LEU B CD2 1 
ATOM   2587 N  N   . SER B  1 54  ? -30.677 -0.223  0.111   1.00 12.45 ? 54  SER B N   1 
ATOM   2588 C  CA  . SER B  1 54  ? -31.622 -0.560  -0.946  1.00 13.26 ? 54  SER B CA  1 
ATOM   2589 C  C   . SER B  1 54  ? -30.987 -0.557  -2.384  1.00 12.50 ? 54  SER B C   1 
ATOM   2590 O  O   . SER B  1 54  ? -30.361 0.460   -2.728  1.00 12.77 ? 54  SER B O   1 
ATOM   2591 C  CB  . SER B  1 54  ? -32.740 0.450   -0.915  1.00 13.99 ? 54  SER B CB  1 
ATOM   2592 O  OG  . SER B  1 54  ? -33.622 0.075   -1.980  1.00 15.16 ? 54  SER B OG  1 
ATOM   2593 N  N   . ALA B  1 55  ? -31.212 -1.638  -3.163  1.00 13.96 ? 55  ALA B N   1 
ATOM   2594 C  CA  . ALA B  1 55  ? -30.773 -1.715  -4.561  1.00 15.79 ? 55  ALA B CA  1 
ATOM   2595 C  C   . ALA B  1 55  ? -31.460 -0.698  -5.394  1.00 14.22 ? 55  ALA B C   1 
ATOM   2596 O  O   . ALA B  1 55  ? -31.003 -0.440  -6.521  1.00 16.64 ? 55  ALA B O   1 
ATOM   2597 C  CB  . ALA B  1 55  ? -30.938 -3.128  -5.119  1.00 19.25 ? 55  ALA B CB  1 
ATOM   2598 N  N   . ASN B  1 56  ? -32.533 -0.097  -4.884  1.00 14.41 ? 56  ASN B N   1 
ATOM   2599 C  CA  . ASN B  1 56  ? -33.197 0.940   -5.664  1.00 15.41 ? 56  ASN B CA  1 
ATOM   2600 C  C   . ASN B  1 56  ? -32.697 2.341   -5.386  1.00 14.80 ? 56  ASN B C   1 
ATOM   2601 O  O   . ASN B  1 56  ? -33.122 3.346   -6.059  1.00 15.88 ? 56  ASN B O   1 
ATOM   2602 C  CB  . ASN B  1 56  ? -34.762 0.893   -5.505  1.00 14.00 ? 56  ASN B CB  1 
ATOM   2603 C  CG  . ASN B  1 56  ? -35.340 -0.405  -5.926  1.00 18.59 ? 56  ASN B CG  1 
ATOM   2604 O  OD1 . ASN B  1 56  ? -34.785 -1.133  -6.710  1.00 19.58 ? 56  ASN B OD1 1 
ATOM   2605 N  ND2 . ASN B  1 56  ? -36.555 -0.625  -5.484  1.00 23.07 ? 56  ASN B ND2 1 
ATOM   2606 N  N   . LYS B  1 57  ? -31.812 2.499   -4.399  1.00 14.39 ? 57  LYS B N   1 
ATOM   2607 C  CA  . LYS B  1 57  ? -31.171 3.755   -4.113  1.00 13.03 ? 57  LYS B CA  1 
ATOM   2608 C  C   . LYS B  1 57  ? -29.747 3.676   -4.685  1.00 13.71 ? 57  LYS B C   1 
ATOM   2609 O  O   . LYS B  1 57  ? -29.277 2.583   -5.109  1.00 12.33 ? 57  LYS B O   1 
ATOM   2610 C  CB  . LYS B  1 57  ? -31.079 3.935   -2.603  1.00 14.75 ? 57  LYS B CB  1 
ATOM   2611 C  CG  . LYS B  1 57  ? -32.453 4.436   -2.074  1.00 17.08 ? 57  LYS B CG  1 
ATOM   2612 C  CD  . LYS B  1 57  ? -32.435 4.502   -0.523  1.00 23.09 ? 57  LYS B CD  1 
ATOM   2613 C  CE  . LYS B  1 57  ? -33.137 5.723   0.020   1.00 30.54 ? 57  LYS B CE  1 
ATOM   2614 N  NZ  . LYS B  1 57  ? -33.067 5.887   1.508   1.00 33.58 ? 57  LYS B NZ  1 
ATOM   2615 N  N   . GLN B  1 58  ? -29.109 4.828   -4.784  1.00 13.06 ? 58  GLN B N   1 
ATOM   2616 C  CA  . GLN B  1 58  ? -27.750 4.856   -5.304  1.00 13.60 ? 58  GLN B CA  1 
ATOM   2617 C  C   . GLN B  1 58  ? -26.848 5.718   -4.500  1.00 12.64 ? 58  GLN B C   1 
ATOM   2618 O  O   . GLN B  1 58  ? -27.244 6.684   -3.842  1.00 13.51 ? 58  GLN B O   1 
ATOM   2619 C  CB  . GLN B  1 58  ? -27.669 5.198   -6.762  1.00 19.13 ? 58  GLN B CB  1 
ATOM   2620 C  CG  . GLN B  1 58  ? -28.195 6.510   -7.136  1.00 21.65 ? 58  GLN B CG  1 
ATOM   2621 C  CD  . GLN B  1 58  ? -28.604 6.574   -8.659  1.00 29.77 ? 58  GLN B CD  1 
ATOM   2622 O  OE1 . GLN B  1 58  ? -28.284 5.701   -9.533  1.00 30.32 ? 58  GLN B OE1 1 
ATOM   2623 N  NE2 . GLN B  1 58  ? -29.349 7.631   -8.960  1.00 33.15 ? 58  GLN B NE2 1 
ATOM   2624 N  N   . PHE B  1 59  ? -25.584 5.290   -4.441  1.00 11.80 ? 59  PHE B N   1 
ATOM   2625 C  CA  . PHE B  1 59  ? -24.603 5.901   -3.521  1.00 11.47 ? 59  PHE B CA  1 
ATOM   2626 C  C   . PHE B  1 59  ? -23.409 6.350   -4.311  1.00 9.26  ? 59  PHE B C   1 
ATOM   2627 O  O   . PHE B  1 59  ? -22.972 5.706   -5.271  1.00 9.93  ? 59  PHE B O   1 
ATOM   2628 C  CB  . PHE B  1 59  ? -24.264 4.817   -2.440  1.00 12.07 ? 59  PHE B CB  1 
ATOM   2629 C  CG  . PHE B  1 59  ? -25.483 4.422   -1.705  1.00 11.13 ? 59  PHE B CG  1 
ATOM   2630 C  CD1 . PHE B  1 59  ? -26.348 3.413   -2.196  1.00 11.44 ? 59  PHE B CD1 1 
ATOM   2631 C  CD2 . PHE B  1 59  ? -25.796 5.114   -0.560  1.00 11.35 ? 59  PHE B CD2 1 
ATOM   2632 C  CE1 . PHE B  1 59  ? -27.578 3.220   -1.509  1.00 12.78 ? 59  PHE B CE1 1 
ATOM   2633 C  CE2 . PHE B  1 59  ? -27.036 4.902   0.100   1.00 12.58 ? 59  PHE B CE2 1 
ATOM   2634 C  CZ  . PHE B  1 59  ? -27.864 3.873   -0.332  1.00 11.72 ? 59  PHE B CZ  1 
ATOM   2635 N  N   . LEU B  1 60  ? -22.874 7.464   -3.899  1.00 10.59 ? 60  LEU B N   1 
ATOM   2636 C  CA  . LEU B  1 60  ? -21.805 8.136   -4.679  1.00 11.65 ? 60  LEU B CA  1 
ATOM   2637 C  C   . LEU B  1 60  ? -20.457 7.491   -4.474  1.00 11.36 ? 60  LEU B C   1 
ATOM   2638 O  O   . LEU B  1 60  ? -19.951 7.446   -3.317  1.00 12.47 ? 60  LEU B O   1 
ATOM   2639 C  CB  . LEU B  1 60  ? -21.765 9.586   -4.232  1.00 13.36 ? 60  LEU B CB  1 
ATOM   2640 C  CG  . LEU B  1 60  ? -20.951 10.479  -5.107  1.00 16.04 ? 60  LEU B CG  1 
ATOM   2641 C  CD1 . LEU B  1 60  ? -21.613 10.671  -6.449  1.00 17.68 ? 60  LEU B CD1 1 
ATOM   2642 C  CD2 . LEU B  1 60  ? -20.777 11.867  -4.432  1.00 20.26 ? 60  LEU B CD2 1 
ATOM   2643 N  N   . LEU B  1 61  ? -19.832 7.076   -5.557  1.00 11.69 ? 61  LEU B N   1 
ATOM   2644 C  CA  . LEU B  1 61  ? -18.455 6.559   -5.592  1.00 11.28 ? 61  LEU B CA  1 
ATOM   2645 C  C   . LEU B  1 61  ? -17.553 7.665   -6.096  1.00 14.04 ? 61  LEU B C   1 
ATOM   2646 O  O   . LEU B  1 61  ? -17.899 8.323   -7.080  1.00 13.87 ? 61  LEU B O   1 
ATOM   2647 C  CB  . LEU B  1 61  ? -18.434 5.356   -6.541  1.00 12.34 ? 61  LEU B CB  1 
ATOM   2648 C  CG  . LEU B  1 61  ? -17.159 4.547   -6.552  1.00 11.91 ? 61  LEU B CG  1 
ATOM   2649 C  CD1 . LEU B  1 61  ? -17.001 3.689   -5.274  1.00 13.52 ? 61  LEU B CD1 1 
ATOM   2650 C  CD2 . LEU B  1 61  ? -17.184 3.587   -7.761  1.00 14.35 ? 61  LEU B CD2 1 
ATOM   2651 N  N   . THR B  1 62  ? -16.411 7.920   -5.448  1.00 12.05 ? 62  THR B N   1 
ATOM   2652 C  CA  . THR B  1 62  ? -15.582 9.077   -5.880  1.00 14.27 ? 62  THR B CA  1 
ATOM   2653 C  C   . THR B  1 62  ? -14.131 8.639   -5.812  1.00 13.38 ? 62  THR B C   1 
ATOM   2654 O  O   . THR B  1 62  ? -13.687 7.977   -4.899  1.00 14.87 ? 62  THR B O   1 
ATOM   2655 C  CB  . THR B  1 62  ? -15.654 10.231  -4.892  1.00 19.84 ? 62  THR B CB  1 
ATOM   2656 O  OG1 . THR B  1 62  ? -17.005 10.724  -4.693  1.00 22.55 ? 62  THR B OG1 1 
ATOM   2657 C  CG2 . THR B  1 62  ? -14.682 11.427  -5.332  1.00 21.72 ? 62  THR B CG2 1 
ATOM   2658 N  N   . ASN B  1 63  ? -13.323 9.031   -6.822  1.00 13.02 ? 63  ASN B N   1 
ATOM   2659 C  CA  . ASN B  1 63  ? -11.859 8.948   -6.692  1.00 12.52 ? 63  ASN B CA  1 
ATOM   2660 C  C   . ASN B  1 63  ? -11.380 10.149  -6.076  1.00 12.51 ? 63  ASN B C   1 
ATOM   2661 O  O   . ASN B  1 63  ? -11.606 11.299  -6.605  1.00 12.94 ? 63  ASN B O   1 
ATOM   2662 C  CB  . ASN B  1 63  ? -11.313 8.871   -8.149  1.00 13.40 ? 63  ASN B CB  1 
ATOM   2663 C  CG  . ASN B  1 63  ? -9.843  8.875   -8.214  1.00 11.90 ? 63  ASN B CG  1 
ATOM   2664 O  OD1 . ASN B  1 63  ? -9.163  9.454   -7.345  1.00 12.51 ? 63  ASN B OD1 1 
ATOM   2665 N  ND2 . ASN B  1 63  ? -9.299  8.259   -9.266  1.00 11.86 ? 63  ASN B ND2 1 
ATOM   2666 N  N   . ASN B  1 64  ? -10.809 10.057  -4.858  1.00 12.89 ? 64  ASN B N   1 
ATOM   2667 C  CA  . ASN B  1 64  ? -10.449 11.288  -4.122  1.00 13.29 ? 64  ASN B CA  1 
ATOM   2668 C  C   . ASN B  1 64  ? -8.983  11.608  -4.326  1.00 15.25 ? 64  ASN B C   1 
ATOM   2669 O  O   . ASN B  1 64  ? -8.448  12.461  -3.571  1.00 15.63 ? 64  ASN B O   1 
ATOM   2670 C  CB  . ASN B  1 64  ? -10.809 11.151  -2.625  1.00 13.28 ? 64  ASN B CB  1 
ATOM   2671 C  CG  . ASN B  1 64  ? -9.973  10.085  -1.916  1.00 14.99 ? 64  ASN B CG  1 
ATOM   2672 O  OD1 . ASN B  1 64  ? -9.049  9.483   -2.453  1.00 13.69 ? 64  ASN B OD1 1 
ATOM   2673 N  ND2 . ASN B  1 64  ? -10.273 9.898   -0.635  1.00 16.32 ? 64  ASN B ND2 1 
ATOM   2674 N  N   . GLY B  1 65  ? -8.316  10.962  -5.295  1.00 13.50 ? 65  GLY B N   1 
ATOM   2675 C  CA  . GLY B  1 65  ? -6.899  11.269  -5.484  1.00 13.79 ? 65  GLY B CA  1 
ATOM   2676 C  C   . GLY B  1 65  ? -5.992  10.366  -4.691  1.00 15.74 ? 65  GLY B C   1 
ATOM   2677 O  O   . GLY B  1 65  ? -4.801  10.352  -4.962  1.00 17.99 ? 65  GLY B O   1 
ATOM   2678 N  N   . HIS B  1 66  ? -6.537  9.609   -3.723  1.00 14.88 ? 66  HIS B N   1 
ATOM   2679 C  CA  . HIS B  1 66  ? -5.738  8.701   -2.847  1.00 15.00 ? 66  HIS B CA  1 
ATOM   2680 C  C   . HIS B  1 66  ? -6.286  7.324   -2.717  1.00 14.62 ? 66  HIS B C   1 
ATOM   2681 O  O   . HIS B  1 66  ? -5.496  6.395   -2.371  1.00 13.07 ? 66  HIS B O   1 
ATOM   2682 C  CB  . HIS B  1 66  ? -5.567  9.357   -1.493  1.00 16.45 ? 66  HIS B CB  1 
ATOM   2683 C  CG  . HIS B  1 66  ? -5.100  10.800  -1.585  1.00 15.71 ? 66  HIS B CG  1 
ATOM   2684 N  ND1 . HIS B  1 66  ? -3.795  11.163  -1.858  1.00 16.45 ? 66  HIS B ND1 1 
ATOM   2685 C  CD2 . HIS B  1 66  ? -5.796  11.880  -1.403  1.00 16.76 ? 66  HIS B CD2 1 
ATOM   2686 C  CE1 . HIS B  1 66  ? -3.766  12.534  -1.837  1.00 14.89 ? 66  HIS B CE1 1 
ATOM   2687 N  NE2 . HIS B  1 66  ? -4.991  12.943  -1.497  1.00 17.59 ? 66  HIS B NE2 1 
ATOM   2688 N  N   . SER B  1 67  ? -7.568  7.135   -3.011  1.00 12.66 ? 67  SER B N   1 
ATOM   2689 C  CA  . SER B  1 67  ? -8.255  5.828   -2.959  1.00 11.80 ? 67  SER B CA  1 
ATOM   2690 C  C   . SER B  1 67  ? -9.521  6.030   -3.769  1.00 13.50 ? 67  SER B C   1 
ATOM   2691 O  O   . SER B  1 67  ? -9.751  7.077   -4.388  1.00 13.42 ? 67  SER B O   1 
ATOM   2692 C  CB  . SER B  1 67  ? -8.598  5.505   -1.472  1.00 13.02 ? 67  SER B CB  1 
ATOM   2693 O  OG  . SER B  1 67  ? -9.181  4.189   -1.394  1.00 12.69 ? 67  SER B OG  1 
ATOM   2694 N  N   . VAL B  1 68  ? -10.307 4.985   -3.796  1.00 12.31 ? 68  VAL B N   1 
ATOM   2695 C  CA  . VAL B  1 68  ? -11.659 5.119   -4.280  1.00 13.13 ? 68  VAL B CA  1 
ATOM   2696 C  C   . VAL B  1 68  ? -12.548 4.995   -3.014  1.00 11.10 ? 68  VAL B C   1 
ATOM   2697 O  O   . VAL B  1 68  ? -12.380 4.033   -2.247  1.00 12.52 ? 68  VAL B O   1 
ATOM   2698 C  CB  . VAL B  1 68  ? -11.928 4.077   -5.371  1.00 13.77 ? 68  VAL B CB  1 
ATOM   2699 C  CG1 . VAL B  1 68  ? -11.726 2.610   -4.960  1.00 14.63 ? 68  VAL B CG1 1 
ATOM   2700 C  CG2 . VAL B  1 68  ? -13.335 4.307   -5.975  1.00 17.60 ? 68  VAL B CG2 1 
ATOM   2701 N  N   . LYS B  1 69  ? -13.491 5.952   -2.909  1.00 12.48 ? 69  LYS B N   1 
ATOM   2702 C  CA  . LYS B  1 69  ? -14.443 5.893   -1.771  1.00 11.59 ? 69  LYS B CA  1 
ATOM   2703 C  C   . LYS B  1 69  ? -15.885 5.832   -2.169  1.00 11.01 ? 69  LYS B C   1 
ATOM   2704 O  O   . LYS B  1 69  ? -16.298 6.409   -3.164  1.00 12.21 ? 69  LYS B O   1 
ATOM   2705 C  CB  . LYS B  1 69  ? -14.162 6.986   -0.768  1.00 14.94 ? 69  LYS B CB  1 
ATOM   2706 C  CG  . LYS B  1 69  ? -14.539 8.347   -1.223  1.00 17.97 ? 69  LYS B CG  1 
ATOM   2707 C  CD  . LYS B  1 69  ? -14.542 9.314   0.010   1.00 17.39 ? 69  LYS B CD  1 
ATOM   2708 C  CE  . LYS B  1 69  ? -15.016 10.548  -0.670  1.00 21.42 ? 69  LYS B CE  1 
ATOM   2709 N  NZ  . LYS B  1 69  ? -14.771 11.713  0.228   1.00 23.63 ? 69  LYS B NZ  1 
ATOM   2710 N  N   . LEU B  1 70  ? -16.681 5.098   -1.404  1.00 8.91  ? 70  LEU B N   1 
ATOM   2711 C  CA  . LEU B  1 70  ? -18.154 5.036   -1.594  1.00 9.21  ? 70  LEU B CA  1 
ATOM   2712 C  C   . LEU B  1 70  ? -18.710 5.761   -0.387  1.00 9.93  ? 70  LEU B C   1 
ATOM   2713 O  O   . LEU B  1 70  ? -18.482 5.361   0.764   1.00 9.84  ? 70  LEU B O   1 
ATOM   2714 C  CB  . LEU B  1 70  ? -18.562 3.596   -1.588  1.00 9.71  ? 70  LEU B CB  1 
ATOM   2715 C  CG  . LEU B  1 70  ? -20.078 3.382   -1.736  1.00 10.51 ? 70  LEU B CG  1 
ATOM   2716 C  CD1 . LEU B  1 70  ? -20.488 3.823   -3.133  1.00 12.50 ? 70  LEU B CD1 1 
ATOM   2717 C  CD2 . LEU B  1 70  ? -20.457 1.915   -1.520  1.00 12.52 ? 70  LEU B CD2 1 
ATOM   2718 N  N   . ASN B  1 71  ? -19.570 6.785   -0.600  1.00 9.89  ? 71  ASN B N   1 
ATOM   2719 C  CA  . ASN B  1 71  ? -20.271 7.491   0.498   1.00 10.78 ? 71  ASN B CA  1 
ATOM   2720 C  C   . ASN B  1 71  ? -21.387 6.585   1.028   1.00 11.83 ? 71  ASN B C   1 
ATOM   2721 O  O   . ASN B  1 71  ? -22.037 5.843   0.258   1.00 13.40 ? 71  ASN B O   1 
ATOM   2722 C  CB  . ASN B  1 71  ? -20.846 8.825   -0.050  1.00 12.15 ? 71  ASN B CB  1 
ATOM   2723 C  CG  . ASN B  1 71  ? -19.837 9.907   -0.191  1.00 16.77 ? 71  ASN B CG  1 
ATOM   2724 O  OD1 . ASN B  1 71  ? -18.659 9.754   0.098   1.00 17.97 ? 71  ASN B OD1 1 
ATOM   2725 N  ND2 . ASN B  1 71  ? -20.330 11.096  -0.627  1.00 20.12 ? 71  ASN B ND2 1 
ATOM   2726 N  N   . LEU B  1 72  ? -21.566 6.616   2.326   1.00 11.35 ? 72  LEU B N   1 
ATOM   2727 C  CA  . LEU B  1 72  ? -22.516 5.783   2.999   1.00 11.24 ? 72  LEU B CA  1 
ATOM   2728 C  C   . LEU B  1 72  ? -23.520 6.682   3.792   1.00 11.40 ? 72  LEU B C   1 
ATOM   2729 O  O   . LEU B  1 72  ? -23.115 7.779   4.224   1.00 12.60 ? 72  LEU B O   1 
ATOM   2730 C  CB  . LEU B  1 72  ? -21.725 4.885   3.985   1.00 10.22 ? 72  LEU B CB  1 
ATOM   2731 C  CG  . LEU B  1 72  ? -20.849 3.848   3.263   1.00 10.33 ? 72  LEU B CG  1 
ATOM   2732 C  CD1 . LEU B  1 72  ? -19.957 3.113   4.279   1.00 9.35  ? 72  LEU B CD1 1 
ATOM   2733 C  CD2 . LEU B  1 72  ? -21.603 2.885   2.385   1.00 11.03 ? 72  LEU B CD2 1 
ATOM   2734 N  N   . PRO B  1 73  ? -24.728 6.153   3.968   1.00 11.19 ? 73  PRO B N   1 
ATOM   2735 C  CA  . PRO B  1 73  ? -25.724 7.000   4.619   1.00 12.40 ? 73  PRO B CA  1 
ATOM   2736 C  C   . PRO B  1 73  ? -25.631 6.929   6.156   1.00 14.44 ? 73  PRO B C   1 
ATOM   2737 O  O   . PRO B  1 73  ? -25.148 5.915   6.681   1.00 13.98 ? 73  PRO B O   1 
ATOM   2738 C  CB  . PRO B  1 73  ? -27.007 6.344   4.176   1.00 12.92 ? 73  PRO B CB  1 
ATOM   2739 C  CG  . PRO B  1 73  ? -26.668 4.809   3.986   1.00 12.49 ? 73  PRO B CG  1 
ATOM   2740 C  CD  . PRO B  1 73  ? -25.270 4.900   3.400   1.00 11.77 ? 73  PRO B CD  1 
ATOM   2741 N  N   . SER B  1 74  ? -25.966 8.011   6.846   1.00 16.23 ? 74  SER B N   1 
ATOM   2742 C  CA  . SER B  1 74  ? -25.825 8.075   8.303   1.00 15.97 ? 74  SER B CA  1 
ATOM   2743 C  C   . SER B  1 74  ? -26.798 7.159   9.020   1.00 17.01 ? 74  SER B C   1 
ATOM   2744 O  O   . SER B  1 74  ? -26.530 6.871   10.223  1.00 15.83 ? 74  SER B O   1 
ATOM   2745 C  CB  . SER B  1 74  ? -26.032 9.486   8.842   1.00 19.45 ? 74  SER B CB  1 
ATOM   2746 O  OG  . SER B  1 74  ? -27.282 10.008  8.405   1.00 24.87 ? 74  SER B OG  1 
ATOM   2747 N  N   . ASP B  1 75  ? -27.849 6.628   8.368   1.00 16.83 ? 75  ASP B N   1 
ATOM   2748 C  CA  . ASP B  1 75  ? -28.685 5.661   9.076   1.00 17.40 ? 75  ASP B CA  1 
ATOM   2749 C  C   . ASP B  1 75  ? -27.983 4.289   9.226   1.00 17.13 ? 75  ASP B C   1 
ATOM   2750 O  O   . ASP B  1 75  ? -28.428 3.466   10.010  1.00 19.78 ? 75  ASP B O   1 
ATOM   2751 C  CB  . ASP B  1 75  ? -30.068 5.524   8.413   1.00 21.87 ? 75  ASP B CB  1 
ATOM   2752 C  CG  . ASP B  1 75  ? -30.018 4.871   7.036   1.00 31.62 ? 75  ASP B CG  1 
ATOM   2753 O  OD1 . ASP B  1 75  ? -29.400 5.449   6.116   1.00 32.54 ? 75  ASP B OD1 1 
ATOM   2754 O  OD2 . ASP B  1 75  ? -30.631 3.792   6.871   1.00 46.32 ? 75  ASP B OD2 1 
ATOM   2755 N  N   . MET B  1 76  ? -26.894 4.059   8.482   1.00 13.38 ? 76  MET B N   1 
ATOM   2756 C  CA  . MET B  1 76  ? -26.070 2.812   8.633   1.00 13.21 ? 76  MET B CA  1 
ATOM   2757 C  C   . MET B  1 76  ? -25.181 3.023   9.867   1.00 12.54 ? 76  MET B C   1 
ATOM   2758 O  O   . MET B  1 76  ? -24.520 4.077   10.023  1.00 13.58 ? 76  MET B O   1 
ATOM   2759 C  CB  . MET B  1 76  ? -25.314 2.683   7.348   1.00 15.10 ? 76  MET B CB  1 
ATOM   2760 C  CG  . MET B  1 76  ? -24.281 1.574   7.404   1.00 15.43 ? 76  MET B CG  1 
ATOM   2761 S  SD  . MET B  1 76  ? -23.586 1.475   5.712   1.00 14.05 ? 76  MET B SD  1 
ATOM   2762 C  CE  . MET B  1 76  ? -22.145 0.528   6.190   1.00 12.85 ? 76  MET B CE  1 
ATOM   2763 N  N   . HIS B  1 77  ? -25.201 2.107   10.822  1.00 12.59 ? 77  HIS B N   1 
ATOM   2764 C  CA  . HIS B  1 77  ? -24.469 2.293   12.025  1.00 13.54 ? 77  HIS B CA  1 
ATOM   2765 C  C   . HIS B  1 77  ? -23.978 1.060   12.680  1.00 13.76 ? 77  HIS B C   1 
ATOM   2766 O  O   . HIS B  1 77  ? -24.419 -0.018  12.322  1.00 13.60 ? 77  HIS B O   1 
ATOM   2767 C  CB  . HIS B  1 77  ? -25.173 3.235   13.025  1.00 20.11 ? 77  HIS B CB  1 
ATOM   2768 C  CG  . HIS B  1 77  ? -26.438 2.701   13.522  1.00 21.05 ? 77  HIS B CG  1 
ATOM   2769 N  ND1 . HIS B  1 77  ? -27.630 2.799   12.823  1.00 21.69 ? 77  HIS B ND1 1 
ATOM   2770 C  CD2 . HIS B  1 77  ? -26.714 2.043   14.698  1.00 22.54 ? 77  HIS B CD2 1 
ATOM   2771 C  CE1 . HIS B  1 77  ? -28.596 2.131   13.530  1.00 23.40 ? 77  HIS B CE1 1 
ATOM   2772 N  NE2 . HIS B  1 77  ? -28.051 1.692   14.677  1.00 25.61 ? 77  HIS B NE2 1 
ATOM   2773 N  N   A ILE B  1 78  ? -23.031 1.234   13.588  0.50 12.72 ? 78  ILE B N   1 
ATOM   2774 N  N   B ILE B  1 78  ? -23.044 1.249   13.595  0.50 13.61 ? 78  ILE B N   1 
ATOM   2775 C  CA  A ILE B  1 78  ? -22.550 0.079   14.415  0.50 13.69 ? 78  ILE B CA  1 
ATOM   2776 C  CA  B ILE B  1 78  ? -22.651 0.097   14.432  0.50 15.41 ? 78  ILE B CA  1 
ATOM   2777 C  C   A ILE B  1 78  ? -23.191 0.240   15.772  0.50 15.76 ? 78  ILE B C   1 
ATOM   2778 C  C   B ILE B  1 78  ? -23.255 0.255   15.781  0.50 16.71 ? 78  ILE B C   1 
ATOM   2779 O  O   A ILE B  1 78  ? -23.179 1.359   16.321  0.50 17.97 ? 78  ILE B O   1 
ATOM   2780 O  O   B ILE B  1 78  ? -23.247 1.352   16.348  0.50 19.05 ? 78  ILE B O   1 
ATOM   2781 C  CB  A ILE B  1 78  ? -20.994 0.174   14.597  0.50 13.84 ? 78  ILE B CB  1 
ATOM   2782 C  CB  B ILE B  1 78  ? -21.139 0.043   14.656  0.50 17.59 ? 78  ILE B CB  1 
ATOM   2783 C  CG1 A ILE B  1 78  ? -20.172 -0.147  13.353  0.50 15.95 ? 78  ILE B CG1 1 
ATOM   2784 C  CG1 B ILE B  1 78  ? -20.412 0.125   13.362  0.50 20.66 ? 78  ILE B CG1 1 
ATOM   2785 C  CG2 A ILE B  1 78  ? -20.478 -0.592  15.859  0.50 12.57 ? 78  ILE B CG2 1 
ATOM   2786 C  CG2 B ILE B  1 78  ? -20.779 -1.254  15.379  0.50 18.22 ? 78  ILE B CG2 1 
ATOM   2787 C  CD1 A ILE B  1 78  ? -18.772 0.458   13.600  0.50 12.77 ? 78  ILE B CD1 1 
ATOM   2788 C  CD1 B ILE B  1 78  ? -20.730 -1.076  12.560  0.50 19.43 ? 78  ILE B CD1 1 
ATOM   2789 N  N   . GLN B  1 79  ? -23.743 -0.875  16.265  1.00 16.33 ? 79  GLN B N   1 
ATOM   2790 C  CA  . GLN B  1 79  ? -24.322 -0.972  17.626  1.00 19.00 ? 79  GLN B CA  1 
ATOM   2791 C  C   . GLN B  1 79  ? -23.300 -1.825  18.436  1.00 20.37 ? 79  GLN B C   1 
ATOM   2792 O  O   . GLN B  1 79  ? -22.776 -2.844  17.964  1.00 21.81 ? 79  GLN B O   1 
ATOM   2793 C  CB  . GLN B  1 79  ? -25.700 -1.665  17.484  1.00 22.63 ? 79  GLN B CB  1 
ATOM   2794 C  CG  . GLN B  1 79  ? -26.522 -2.063  18.729  1.00 31.80 ? 79  GLN B CG  1 
ATOM   2795 C  CD  . GLN B  1 79  ? -26.955 -0.897  19.585  1.00 32.88 ? 79  GLN B CD  1 
ATOM   2796 O  OE1 . GLN B  1 79  ? -27.208 0.215   19.095  1.00 40.02 ? 79  GLN B OE1 1 
ATOM   2797 N  NE2 . GLN B  1 79  ? -27.031 -1.133  20.897  1.00 33.14 ? 79  GLN B NE2 1 
ATOM   2798 N  N   . GLY B  1 80  ? -22.974 -1.345  19.602  1.00 20.13 ? 80  GLY B N   1 
ATOM   2799 C  CA  . GLY B  1 80  ? -22.156 -2.186  20.523  1.00 19.43 ? 80  GLY B CA  1 
ATOM   2800 C  C   . GLY B  1 80  ? -20.946 -1.465  21.036  1.00 19.65 ? 80  GLY B C   1 
ATOM   2801 O  O   . GLY B  1 80  ? -20.377 -1.913  22.052  1.00 23.13 ? 80  GLY B O   1 
ATOM   2802 N  N   . LEU B  1 81  ? -20.577 -0.330  20.439  1.00 19.84 ? 81  LEU B N   1 
ATOM   2803 C  CA  . LEU B  1 81  ? -19.645 0.595   21.086  1.00 18.71 ? 81  LEU B CA  1 
ATOM   2804 C  C   . LEU B  1 81  ? -20.306 1.434   22.169  1.00 22.39 ? 81  LEU B C   1 
ATOM   2805 O  O   . LEU B  1 81  ? -21.523 1.302   22.409  1.00 22.22 ? 81  LEU B O   1 
ATOM   2806 C  CB  . LEU B  1 81  ? -18.838 1.438   20.059  1.00 20.61 ? 81  LEU B CB  1 
ATOM   2807 C  CG  . LEU B  1 81  ? -18.137 0.585   19.016  1.00 22.03 ? 81  LEU B CG  1 
ATOM   2808 C  CD1 . LEU B  1 81  ? -17.654 1.412   17.841  1.00 21.47 ? 81  LEU B CD1 1 
ATOM   2809 C  CD2 . LEU B  1 81  ? -16.928 0.061   19.770  1.00 20.06 ? 81  LEU B CD2 1 
ATOM   2810 N  N   . GLN B  1 82  ? -19.564 2.323   22.790  1.00 23.41 ? 82  GLN B N   1 
ATOM   2811 C  CA  . GLN B  1 82  ? -20.172 3.036   23.896  1.00 29.22 ? 82  GLN B CA  1 
ATOM   2812 C  C   . GLN B  1 82  ? -20.994 4.237   23.449  1.00 29.33 ? 82  GLN B C   1 
ATOM   2813 O  O   . GLN B  1 82  ? -21.686 4.811   24.288  1.00 26.72 ? 82  GLN B O   1 
ATOM   2814 C  CB  . GLN B  1 82  ? -19.082 3.465   24.874  1.00 30.43 ? 82  GLN B CB  1 
ATOM   2815 C  CG  . GLN B  1 82  ? -18.638 2.316   25.811  1.00 33.43 ? 82  GLN B CG  1 
ATOM   2816 C  CD  . GLN B  1 82  ? -17.532 2.775   26.750  1.00 40.10 ? 82  GLN B CD  1 
ATOM   2817 O  OE1 . GLN B  1 82  ? -17.704 2.849   27.990  1.00 38.01 ? 82  GLN B OE1 1 
ATOM   2818 N  NE2 . GLN B  1 82  ? -16.414 3.192   26.155  1.00 38.73 ? 82  GLN B NE2 1 
ATOM   2819 N  N   . SER B  1 83  ? -20.872 4.649   22.162  1.00 23.32 ? 83  SER B N   1 
ATOM   2820 C  CA  . SER B  1 83  ? -21.809 5.548   21.494  1.00 19.46 ? 83  SER B CA  1 
ATOM   2821 C  C   . SER B  1 83  ? -22.157 4.857   20.209  1.00 18.39 ? 83  SER B C   1 
ATOM   2822 O  O   . SER B  1 83  ? -21.477 3.903   19.821  1.00 17.59 ? 83  SER B O   1 
ATOM   2823 C  CB  . SER B  1 83  ? -21.161 6.871   21.166  1.00 23.27 ? 83  SER B CB  1 
ATOM   2824 O  OG  . SER B  1 83  ? -20.736 7.504   22.395  1.00 26.56 ? 83  SER B OG  1 
ATOM   2825 N  N   A ARG B  1 84  ? -23.278 5.260   19.614  0.50 16.29 ? 84  ARG B N   1 
ATOM   2826 N  N   B ARG B  1 84  ? -23.206 5.341   19.565  0.50 17.03 ? 84  ARG B N   1 
ATOM   2827 C  CA  A ARG B  1 84  ? -23.606 4.872   18.240  0.50 17.12 ? 84  ARG B CA  1 
ATOM   2828 C  CA  B ARG B  1 84  ? -23.674 4.796   18.321  0.50 18.13 ? 84  ARG B CA  1 
ATOM   2829 C  C   A ARG B  1 84  ? -22.593 5.555   17.278  0.50 17.01 ? 84  ARG B C   1 
ATOM   2830 C  C   B ARG B  1 84  ? -22.575 5.551   17.289  0.50 17.66 ? 84  ARG B C   1 
ATOM   2831 O  O   A ARG B  1 84  ? -22.298 6.737   17.399  0.50 15.88 ? 84  ARG B O   1 
ATOM   2832 O  O   B ARG B  1 84  ? -22.336 6.740   17.373  0.50 16.18 ? 84  ARG B O   1 
ATOM   2833 C  CB  A ARG B  1 84  ? -25.049 5.255   17.856  0.50 18.65 ? 84  ARG B CB  1 
ATOM   2834 C  CB  B ARG B  1 84  ? -25.098 5.228   18.016  0.50 20.68 ? 84  ARG B CB  1 
ATOM   2835 C  CG  A ARG B  1 84  ? -25.327 5.155   16.340  0.50 18.65 ? 84  ARG B CG  1 
ATOM   2836 C  CG  B ARG B  1 84  ? -25.342 5.546   16.549  0.50 21.88 ? 84  ARG B CG  1 
ATOM   2837 C  CD  A ARG B  1 84  ? -26.777 5.475   15.977  0.50 19.09 ? 84  ARG B CD  1 
ATOM   2838 C  CD  B ARG B  1 84  ? -26.720 6.149   16.331  0.50 23.21 ? 84  ARG B CD  1 
ATOM   2839 N  NE  A ARG B  1 84  ? -26.879 5.725   14.546  0.50 16.24 ? 84  ARG B NE  1 
ATOM   2840 N  NE  B ARG B  1 84  ? -27.786 5.251   16.767  0.50 26.14 ? 84  ARG B NE  1 
ATOM   2841 C  CZ  A ARG B  1 84  ? -27.987 5.700   13.826  0.50 19.52 ? 84  ARG B CZ  1 
ATOM   2842 C  CZ  B ARG B  1 84  ? -28.898 5.019   16.077  0.50 23.64 ? 84  ARG B CZ  1 
ATOM   2843 N  NH1 A ARG B  1 84  ? -29.148 5.380   14.384  0.50 21.09 ? 84  ARG B NH1 1 
ATOM   2844 N  NH1 B ARG B  1 84  ? -29.097 5.618   14.911  0.50 27.62 ? 84  ARG B NH1 1 
ATOM   2845 N  NH2 A ARG B  1 84  ? -27.918 5.972   12.531  0.50 16.59 ? 84  ARG B NH2 1 
ATOM   2846 N  NH2 B ARG B  1 84  ? -29.814 4.186   16.554  0.50 22.77 ? 84  ARG B NH2 1 
ATOM   2847 N  N   . TYR B  1 85  ? -22.015 4.743   16.390  1.00 14.66 ? 85  TYR B N   1 
ATOM   2848 C  CA  . TYR B  1 85  ? -21.122 5.306   15.338  1.00 12.61 ? 85  TYR B CA  1 
ATOM   2849 C  C   . TYR B  1 85  ? -21.849 5.062   14.027  1.00 12.45 ? 85  TYR B C   1 
ATOM   2850 O  O   . TYR B  1 85  ? -22.215 3.967   13.670  1.00 14.61 ? 85  TYR B O   1 
ATOM   2851 C  CB  . TYR B  1 85  ? -19.779 4.613   15.332  1.00 12.32 ? 85  TYR B CB  1 
ATOM   2852 C  CG  . TYR B  1 85  ? -18.884 5.085   16.440  1.00 12.22 ? 85  TYR B CG  1 
ATOM   2853 C  CD1 . TYR B  1 85  ? -19.063 4.634   17.741  1.00 15.54 ? 85  TYR B CD1 1 
ATOM   2854 C  CD2 . TYR B  1 85  ? -17.872 5.995   16.195  1.00 11.69 ? 85  TYR B CD2 1 
ATOM   2855 C  CE1 . TYR B  1 85  ? -18.246 5.067   18.766  1.00 15.43 ? 85  TYR B CE1 1 
ATOM   2856 C  CE2 . TYR B  1 85  ? -17.048 6.436   17.211  1.00 13.32 ? 85  TYR B CE2 1 
ATOM   2857 C  CZ  . TYR B  1 85  ? -17.242 5.967   18.496  1.00 14.50 ? 85  TYR B CZ  1 
ATOM   2858 O  OH  . TYR B  1 85  ? -16.426 6.399   19.518  1.00 18.72 ? 85  TYR B OH  1 
ATOM   2859 N  N   . SER B  1 86  ? -22.027 6.139   13.305  1.00 13.12 ? 86  SER B N   1 
ATOM   2860 C  CA  . SER B  1 86  ? -22.697 6.081   12.003  1.00 12.37 ? 86  SER B CA  1 
ATOM   2861 C  C   . SER B  1 86  ? -21.698 6.127   10.840  1.00 9.94  ? 86  SER B C   1 
ATOM   2862 O  O   . SER B  1 86  ? -20.656 6.726   10.897  1.00 10.31 ? 86  SER B O   1 
ATOM   2863 C  CB  . SER B  1 86  ? -23.703 7.270   11.825  1.00 15.07 ? 86  SER B CB  1 
ATOM   2864 O  OG  . SER B  1 86  ? -24.734 7.180   12.849  1.00 16.96 ? 86  SER B OG  1 
ATOM   2865 N  N   . ALA B  1 87  ? -22.092 5.376   9.823   1.00 10.17 ? 87  ALA B N   1 
ATOM   2866 C  CA  . ALA B  1 87  ? -21.213 5.256   8.600   1.00 10.72 ? 87  ALA B CA  1 
ATOM   2867 C  C   . ALA B  1 87  ? -21.070 6.562   7.879   1.00 11.07 ? 87  ALA B C   1 
ATOM   2868 O  O   . ALA B  1 87  ? -22.027 7.409   7.888   1.00 12.83 ? 87  ALA B O   1 
ATOM   2869 C  CB  . ALA B  1 87  ? -21.664 4.203   7.644   1.00 12.29 ? 87  ALA B CB  1 
ATOM   2870 N  N   . THR B  1 88  ? -19.885 6.819   7.341   1.00 9.47  ? 88  THR B N   1 
ATOM   2871 C  CA  . THR B  1 88  ? -19.677 7.984   6.434   1.00 9.60  ? 88  THR B CA  1 
ATOM   2872 C  C   . THR B  1 88  ? -19.153 7.572   5.084   1.00 9.96  ? 88  THR B C   1 
ATOM   2873 O  O   . THR B  1 88  ? -19.586 8.060   4.022   1.00 10.03 ? 88  THR B O   1 
ATOM   2874 C  CB  . THR B  1 88  ? -18.867 9.101   7.128   1.00 10.24 ? 88  THR B CB  1 
ATOM   2875 O  OG1 . THR B  1 88  ? -18.751 10.208  6.150   1.00 14.88 ? 88  THR B OG1 1 
ATOM   2876 C  CG2 . THR B  1 88  ? -17.472 8.706   7.556   1.00 10.27 ? 88  THR B CG2 1 
ATOM   2877 N  N   . GLN B  1 89  ? -18.189 6.649   5.009   1.00 9.07  ? 89  GLN B N   1 
ATOM   2878 C  CA  . GLN B  1 89  ? -17.705 6.175   3.693   1.00 9.08  ? 89  GLN B CA  1 
ATOM   2879 C  C   . GLN B  1 89  ? -16.900 4.883   3.862   1.00 8.06  ? 89  GLN B C   1 
ATOM   2880 O  O   . GLN B  1 89  ? -16.561 4.561   5.019   1.00 8.43  ? 89  GLN B O   1 
ATOM   2881 C  CB  . GLN B  1 89  ? -16.772 7.241   3.082   1.00 9.42  ? 89  GLN B CB  1 
ATOM   2882 C  CG  . GLN B  1 89  ? -15.587 7.649   3.995   1.00 12.58 ? 89  GLN B CG  1 
ATOM   2883 C  CD  . GLN B  1 89  ? -14.261 7.203   3.468   1.00 12.79 ? 89  GLN B CD  1 
ATOM   2884 O  OE1 . GLN B  1 89  ? -14.142 6.007   3.193   1.00 12.46 ? 89  GLN B OE1 1 
ATOM   2885 N  NE2 . GLN B  1 89  ? -13.298 7.994   3.340   1.00 13.31 ? 89  GLN B NE2 1 
ATOM   2886 N  N   . LEU B  1 90  ? -16.723 4.146   2.784   1.00 6.99  ? 90  LEU B N   1 
ATOM   2887 C  CA  . LEU B  1 90  ? -15.717 3.064   2.773   1.00 7.19  ? 90  LEU B CA  1 
ATOM   2888 C  C   . LEU B  1 90  ? -14.778 3.287   1.658   1.00 8.15  ? 90  LEU B C   1 
ATOM   2889 O  O   . LEU B  1 90  ? -15.058 3.975   0.682   1.00 7.93  ? 90  LEU B O   1 
ATOM   2890 C  CB  . LEU B  1 90  ? -16.418 1.615   2.784   1.00 7.46  ? 90  LEU B CB  1 
ATOM   2891 C  CG  . LEU B  1 90  ? -17.357 1.334   1.606   1.00 7.84  ? 90  LEU B CG  1 
ATOM   2892 C  CD1 . LEU B  1 90  ? -16.653 1.015   0.312   1.00 8.54  ? 90  LEU B CD1 1 
ATOM   2893 C  CD2 . LEU B  1 90  ? -18.267 0.144   1.899   1.00 8.59  ? 90  LEU B CD2 1 
ATOM   2894 N  N   . HIS B  1 91  ? -13.610 2.668   1.752   1.00 7.84  ? 91  HIS B N   1 
ATOM   2895 C  CA  . HIS B  1 91  ? -12.571 2.810   0.694   1.00 7.90  ? 91  HIS B CA  1 
ATOM   2896 C  C   . HIS B  1 91  ? -11.575 1.706   0.852   1.00 7.31  ? 91  HIS B C   1 
ATOM   2897 O  O   . HIS B  1 91  ? -11.663 0.883   1.811   1.00 6.96  ? 91  HIS B O   1 
ATOM   2898 C  CB  . HIS B  1 91  ? -11.835 4.173   0.806   1.00 7.48  ? 91  HIS B CB  1 
ATOM   2899 C  CG  . HIS B  1 91  ? -11.147 4.352   2.089   1.00 6.37  ? 91  HIS B CG  1 
ATOM   2900 N  ND1 . HIS B  1 91  ? -11.706 4.889   3.208   1.00 7.23  ? 91  HIS B ND1 1 
ATOM   2901 C  CD2 . HIS B  1 91  ? -9.877  3.848   2.472   1.00 7.12  ? 91  HIS B CD2 1 
ATOM   2902 C  CE1 . HIS B  1 91  ? -10.829 4.778   4.247   1.00 8.23  ? 91  HIS B CE1 1 
ATOM   2903 N  NE2 . HIS B  1 91  ? -9.711  4.162   3.792   1.00 7.14  ? 91  HIS B NE2 1 
ATOM   2904 N  N   . LEU B  1 92  ? -10.620 1.631   -0.069  1.00 7.66  ? 92  LEU B N   1 
ATOM   2905 C  CA  . LEU B  1 92  ? -9.647  0.516   -0.028  1.00 7.00  ? 92  LEU B CA  1 
ATOM   2906 C  C   . LEU B  1 92  ? -8.228  0.946   -0.115  1.00 6.94  ? 92  LEU B C   1 
ATOM   2907 O  O   . LEU B  1 92  ? -7.936  2.099   -0.513  1.00 8.10  ? 92  LEU B O   1 
ATOM   2908 C  CB  . LEU B  1 92  ? -9.930  -0.486  -1.146  1.00 8.88  ? 92  LEU B CB  1 
ATOM   2909 C  CG  . LEU B  1 92  ? -11.343 -1.172  -1.069  1.00 8.81  ? 92  LEU B CG  1 
ATOM   2910 C  CD1 . LEU B  1 92  ? -12.335 -0.529  -1.949  1.00 12.63 ? 92  LEU B CD1 1 
ATOM   2911 C  CD2 . LEU B  1 92  ? -11.236 -2.653  -1.375  1.00 11.75 ? 92  LEU B CD2 1 
ATOM   2912 N  N   . HIS B  1 93  ? -7.319  0.021   0.164   1.00 7.42  ? 93  HIS B N   1 
ATOM   2913 C  CA  . HIS B  1 93  ? -5.834  0.182   -0.031  1.00 7.58  ? 93  HIS B CA  1 
ATOM   2914 C  C   . HIS B  1 93  ? -5.327  -1.002  -0.690  1.00 8.09  ? 93  HIS B C   1 
ATOM   2915 O  O   . HIS B  1 93  ? -5.813  -2.117  -0.387  1.00 8.41  ? 93  HIS B O   1 
ATOM   2916 C  CB  . HIS B  1 93  ? -5.157  0.353   1.333   1.00 8.16  ? 93  HIS B CB  1 
ATOM   2917 C  CG  . HIS B  1 93  ? -5.705  1.524   2.111   1.00 7.56  ? 93  HIS B CG  1 
ATOM   2918 N  ND1 . HIS B  1 93  ? -5.094  2.813   2.067   1.00 7.75  ? 93  HIS B ND1 1 
ATOM   2919 C  CD2 . HIS B  1 93  ? -6.771  1.624   2.990   1.00 7.01  ? 93  HIS B CD2 1 
ATOM   2920 C  CE1 . HIS B  1 93  ? -5.849  3.651   2.915   1.00 7.58  ? 93  HIS B CE1 1 
ATOM   2921 N  NE2 . HIS B  1 93  ? -6.812  2.950   3.454   1.00 7.49  ? 93  HIS B NE2 1 
ATOM   2922 N  N   . TRP B  1 94  ? -4.372  -0.873  -1.574  1.00 8.05  ? 94  TRP B N   1 
ATOM   2923 C  CA  . TRP B  1 94  ? -3.890  -2.061  -2.361  1.00 7.66  ? 94  TRP B CA  1 
ATOM   2924 C  C   . TRP B  1 94  ? -2.504  -1.766  -2.868  1.00 8.13  ? 94  TRP B C   1 
ATOM   2925 O  O   . TRP B  1 94  ? -1.878  -0.750  -2.583  1.00 8.12  ? 94  TRP B O   1 
ATOM   2926 C  CB  . TRP B  1 94  ? -4.850  -2.311  -3.553  1.00 8.81  ? 94  TRP B CB  1 
ATOM   2927 C  CG  . TRP B  1 94  ? -4.966  -1.106  -4.494  1.00 8.44  ? 94  TRP B CG  1 
ATOM   2928 C  CD1 . TRP B  1 94  ? -4.128  -0.783  -5.539  1.00 8.98  ? 94  TRP B CD1 1 
ATOM   2929 C  CD2 . TRP B  1 94  ? -5.999  -0.083  -4.416  1.00 8.62  ? 94  TRP B CD2 1 
ATOM   2930 N  NE1 . TRP B  1 94  ? -4.606  0.375   -6.142  1.00 9.59  ? 94  TRP B NE1 1 
ATOM   2931 C  CE2 . TRP B  1 94  ? -5.743  0.840   -5.466  1.00 8.46  ? 94  TRP B CE2 1 
ATOM   2932 C  CE3 . TRP B  1 94  ? -7.103  0.170   -3.571  1.00 9.03  ? 94  TRP B CE3 1 
ATOM   2933 C  CZ2 . TRP B  1 94  ? -6.532  1.939   -5.693  1.00 9.22  ? 94  TRP B CZ2 1 
ATOM   2934 C  CZ3 . TRP B  1 94  ? -7.888  1.328   -3.789  1.00 9.77  ? 94  TRP B CZ3 1 
ATOM   2935 C  CH2 . TRP B  1 94  ? -7.613  2.195   -4.863  1.00 9.12  ? 94  TRP B CH2 1 
ATOM   2936 N  N   . GLY B  1 95  ? -1.966  -2.846  -3.489  1.00 8.62  ? 95  GLY B N   1 
ATOM   2937 C  CA  . GLY B  1 95  ? -0.580  -2.855  -4.008  1.00 9.40  ? 95  GLY B CA  1 
ATOM   2938 C  C   . GLY B  1 95  ? -0.490  -2.511  -5.462  1.00 10.32 ? 95  GLY B C   1 
ATOM   2939 O  O   . GLY B  1 95  ? -0.978  -1.498  -5.922  1.00 10.44 ? 95  GLY B O   1 
ATOM   2940 N  N   . ASN B  1 96  ? 0.042   -3.458  -6.257  1.00 10.61 ? 96  ASN B N   1 
ATOM   2941 C  CA  . ASN B  1 96  ? 0.168   -3.167  -7.709  1.00 13.02 ? 96  ASN B CA  1 
ATOM   2942 C  C   . ASN B  1 96  ? 0.178   -4.484  -8.449  1.00 13.54 ? 96  ASN B C   1 
ATOM   2943 O  O   . ASN B  1 96  ? 0.256   -5.480  -7.847  1.00 12.87 ? 96  ASN B O   1 
ATOM   2944 C  CB  . ASN B  1 96  ? 1.439   -2.336  -7.975  1.00 14.58 ? 96  ASN B CB  1 
ATOM   2945 C  CG  . ASN B  1 96  ? 2.704   -3.107  -7.722  1.00 16.83 ? 96  ASN B CG  1 
ATOM   2946 O  OD1 . ASN B  1 96  ? 3.100   -3.899  -8.626  1.00 20.22 ? 96  ASN B OD1 1 
ATOM   2947 N  ND2 . ASN B  1 96  ? 3.334   -2.965  -6.592  1.00 17.73 ? 96  ASN B ND2 1 
ATOM   2948 N  N   . PRO B  1 97  ? 0.094   -4.457  -9.805  1.00 13.43 ? 97  PRO B N   1 
ATOM   2949 C  CA  . PRO B  1 97  ? -0.134  -5.635  -10.538 1.00 15.04 ? 97  PRO B CA  1 
ATOM   2950 C  C   . PRO B  1 97  ? 0.952   -6.700  -10.401 1.00 13.63 ? 97  PRO B C   1 
ATOM   2951 O  O   . PRO B  1 97  ? 0.663   -7.937  -10.501 1.00 17.52 ? 97  PRO B O   1 
ATOM   2952 C  CB  . PRO B  1 97  ? -0.180  -5.114  -11.976 1.00 15.07 ? 97  PRO B CB  1 
ATOM   2953 C  CG  . PRO B  1 97  ? -0.863  -3.809  -11.805 1.00 16.01 ? 97  PRO B CG  1 
ATOM   2954 C  CD  . PRO B  1 97  ? -0.137  -3.271  -10.638 1.00 14.75 ? 97  PRO B CD  1 
ATOM   2955 N  N   . ASN B  1 98  ? 2.162   -6.256  -10.165 1.00 11.47 ? 98  ASN B N   1 
ATOM   2956 C  CA  . ASN B  1 98  ? 3.287   -7.187  -10.113 1.00 16.30 ? 98  ASN B CA  1 
ATOM   2957 C  C   . ASN B  1 98  ? 3.548   -7.524  -8.682  1.00 19.88 ? 98  ASN B C   1 
ATOM   2958 O  O   . ASN B  1 98  ? 4.349   -8.390  -8.380  1.00 26.20 ? 98  ASN B O   1 
ATOM   2959 C  CB  . ASN B  1 98  ? 4.536   -6.522  -10.760 1.00 15.43 ? 98  ASN B CB  1 
ATOM   2960 C  CG  . ASN B  1 98  ? 4.361   -6.231  -12.220 1.00 16.90 ? 98  ASN B CG  1 
ATOM   2961 O  OD1 . ASN B  1 98  ? 4.083   -7.155  -12.970 1.00 16.89 ? 98  ASN B OD1 1 
ATOM   2962 N  ND2 . ASN B  1 98  ? 4.226   -4.980  -12.566 1.00 17.66 ? 98  ASN B ND2 1 
ATOM   2963 N  N   . ASP B  1 99  ? 2.883   -6.866  -7.745  1.00 15.24 ? 99  ASP B N   1 
ATOM   2964 C  CA  . ASP B  1 99  ? 3.125   -7.223  -6.303  1.00 17.99 ? 99  ASP B CA  1 
ATOM   2965 C  C   . ASP B  1 99  ? 1.816   -6.923  -5.511  1.00 13.97 ? 99  ASP B C   1 
ATOM   2966 O  O   . ASP B  1 99  ? 1.605   -5.787  -4.983  1.00 13.01 ? 99  ASP B O   1 
ATOM   2967 C  CB  . ASP B  1 99  ? 4.265   -6.380  -5.710  1.00 22.22 ? 99  ASP B CB  1 
ATOM   2968 C  CG  . ASP B  1 99  ? 4.545   -6.726  -4.190  1.00 26.48 ? 99  ASP B CG  1 
ATOM   2969 O  OD1 . ASP B  1 99  ? 4.112   -7.844  -3.764  1.00 31.38 ? 99  ASP B OD1 1 
ATOM   2970 O  OD2 . ASP B  1 99  ? 5.107   -5.862  -3.510  1.00 35.66 ? 99  ASP B OD2 1 
ATOM   2971 N  N   . PRO B  1 100 ? 0.876   -7.852  -5.565  1.00 12.58 ? 100 PRO B N   1 
ATOM   2972 C  CA  . PRO B  1 100 ? -0.453  -7.643  -4.966  1.00 13.66 ? 100 PRO B CA  1 
ATOM   2973 C  C   . PRO B  1 100 ? -0.444  -7.861  -3.455  1.00 12.34 ? 100 PRO B C   1 
ATOM   2974 O  O   . PRO B  1 100 ? -1.031  -8.799  -2.946  1.00 14.46 ? 100 PRO B O   1 
ATOM   2975 C  CB  . PRO B  1 100 ? -1.413  -8.536  -5.840  1.00 14.45 ? 100 PRO B CB  1 
ATOM   2976 C  CG  . PRO B  1 100 ? -0.482  -9.683  -6.190  1.00 18.15 ? 100 PRO B CG  1 
ATOM   2977 C  CD  . PRO B  1 100 ? 0.874   -9.069  -6.437  1.00 15.87 ? 100 PRO B CD  1 
ATOM   2978 N  N   . HIS B  1 101 ? 0.270   -7.005  -2.739  1.00 12.43 ? 101 HIS B N   1 
ATOM   2979 C  CA  . HIS B  1 101 ? 0.450   -7.127  -1.282  1.00 13.54 ? 101 HIS B CA  1 
ATOM   2980 C  C   . HIS B  1 101 ? 0.372   -5.830  -0.596  1.00 12.83 ? 101 HIS B C   1 
ATOM   2981 O  O   . HIS B  1 101 ? 1.363   -5.451  0.121   1.00 19.01 ? 101 HIS B O   1 
ATOM   2982 C  CB  . HIS B  1 101 ? 1.746   -7.816  -0.890  1.00 17.45 ? 101 HIS B CB  1 
ATOM   2983 C  CG  . HIS B  1 101 ? 1.760   -9.240  -1.324  1.00 23.24 ? 101 HIS B CG  1 
ATOM   2984 N  ND1 . HIS B  1 101 ? 2.190   -9.589  -2.570  1.00 23.65 ? 101 HIS B ND1 1 
ATOM   2985 C  CD2 . HIS B  1 101 ? 1.255   -10.386 -0.724  1.00 26.73 ? 101 HIS B CD2 1 
ATOM   2986 C  CE1 . HIS B  1 101 ? 1.980   -10.938 -2.749  1.00 24.99 ? 101 HIS B CE1 1 
ATOM   2987 N  NE2 . HIS B  1 101 ? 1.455   -11.428 -1.610  1.00 29.51 ? 101 HIS B NE2 1 
ATOM   2988 N  N   . GLY B  1 102 ? -0.791  -5.204  -0.655  1.00 11.10 ? 102 GLY B N   1 
ATOM   2989 C  CA  . GLY B  1 102 ? -0.955  -3.789  -0.247  1.00 10.00 ? 102 GLY B CA  1 
ATOM   2990 C  C   . GLY B  1 102 ? -1.927  -3.562  0.914   1.00 8.86  ? 102 GLY B C   1 
ATOM   2991 O  O   . GLY B  1 102 ? -2.430  -2.454  1.050   1.00 10.03 ? 102 GLY B O   1 
ATOM   2992 N  N   . SER B  1 103 ? -2.160  -4.520  1.809   1.00 9.25  ? 103 SER B N   1 
ATOM   2993 C  CA  . SER B  1 103 ? -2.885  -4.173  3.036   1.00 8.83  ? 103 SER B CA  1 
ATOM   2994 C  C   . SER B  1 103 ? -2.068  -3.156  3.866   1.00 9.07  ? 103 SER B C   1 
ATOM   2995 O  O   . SER B  1 103 ? -0.857  -3.030  3.704   1.00 10.08 ? 103 SER B O   1 
ATOM   2996 C  CB  . SER B  1 103 ? -3.248  -5.480  3.823   1.00 9.47  ? 103 SER B CB  1 
ATOM   2997 O  OG  . SER B  1 103 ? -2.020  -5.968  4.417   1.00 8.91  ? 103 SER B OG  1 
ATOM   2998 N  N   . GLU B  1 104 ? -2.797  -2.480  4.742   1.00 8.52  ? 104 GLU B N   1 
ATOM   2999 C  CA  . GLU B  1 104 ? -2.138  -1.539  5.670   1.00 8.49  ? 104 GLU B CA  1 
ATOM   3000 C  C   . GLU B  1 104 ? -1.718  -2.251  6.941   1.00 7.95  ? 104 GLU B C   1 
ATOM   3001 O  O   . GLU B  1 104 ? -0.539  -2.281  7.280   1.00 9.22  ? 104 GLU B O   1 
ATOM   3002 C  CB  . GLU B  1 104 ? -3.071  -0.414  6.014   1.00 8.28  ? 104 GLU B CB  1 
ATOM   3003 C  CG  . GLU B  1 104 ? -3.515  0.378   4.704   1.00 8.42  ? 104 GLU B CG  1 
ATOM   3004 C  CD  . GLU B  1 104 ? -3.553  1.836   4.977   1.00 7.42  ? 104 GLU B CD  1 
ATOM   3005 O  OE1 . GLU B  1 104 ? -4.521  2.272   5.596   1.00 9.49  ? 104 GLU B OE1 1 
ATOM   3006 O  OE2 . GLU B  1 104 ? -2.607  2.510   4.666   1.00 9.49  ? 104 GLU B OE2 1 
ATOM   3007 N  N   . HIS B  1 105 ? -2.683  -2.890  7.645   1.00 8.72  ? 105 HIS B N   1 
ATOM   3008 C  CA  . HIS B  1 105 ? -2.278  -3.758  8.754   1.00 8.77  ? 105 HIS B CA  1 
ATOM   3009 C  C   . HIS B  1 105 ? -1.637  -4.980  8.219   1.00 8.73  ? 105 HIS B C   1 
ATOM   3010 O  O   . HIS B  1 105 ? -1.965  -5.485  7.146   1.00 9.76  ? 105 HIS B O   1 
ATOM   3011 C  CB  . HIS B  1 105 ? -3.505  -4.077  9.585   1.00 8.75  ? 105 HIS B CB  1 
ATOM   3012 C  CG  . HIS B  1 105 ? -4.078  -2.879  10.289  1.00 8.50  ? 105 HIS B CG  1 
ATOM   3013 N  ND1 . HIS B  1 105 ? -5.000  -2.052  9.704   1.00 8.23  ? 105 HIS B ND1 1 
ATOM   3014 C  CD2 . HIS B  1 105 ? -3.769  -2.352  11.510  1.00 9.06  ? 105 HIS B CD2 1 
ATOM   3015 C  CE1 . HIS B  1 105 ? -5.241  -1.049  10.569  1.00 9.33  ? 105 HIS B CE1 1 
ATOM   3016 N  NE2 . HIS B  1 105 ? -4.477  -1.229  11.675  1.00 9.88  ? 105 HIS B NE2 1 
ATOM   3017 N  N   . THR B  1 106 ? -0.673  -5.506  9.026   1.00 9.29  ? 106 THR B N   1 
ATOM   3018 C  CA  . THR B  1 106 ? -0.037  -6.813  8.727   1.00 9.76  ? 106 THR B CA  1 
ATOM   3019 C  C   . THR B  1 106 ? -0.290  -7.699  9.925   1.00 9.44  ? 106 THR B C   1 
ATOM   3020 O  O   . THR B  1 106 ? -0.625  -7.256  10.997  1.00 11.08 ? 106 THR B O   1 
ATOM   3021 C  CB  . THR B  1 106 ? 1.449   -6.598  8.397   1.00 11.60 ? 106 THR B CB  1 
ATOM   3022 O  OG1 . THR B  1 106 ? 2.089   -5.988  9.561   1.00 11.17 ? 106 THR B OG1 1 
ATOM   3023 C  CG2 . THR B  1 106 ? 1.603   -5.696  7.174   1.00 12.94 ? 106 THR B CG2 1 
ATOM   3024 N  N   . VAL B  1 107 ? -0.154  -9.000  9.625   1.00 11.44 ? 107 VAL B N   1 
ATOM   3025 C  CA  . VAL B  1 107 ? -0.382  -9.982  10.686  1.00 13.40 ? 107 VAL B CA  1 
ATOM   3026 C  C   . VAL B  1 107 ? 0.842   -10.896 10.720  1.00 11.65 ? 107 VAL B C   1 
ATOM   3027 O  O   . VAL B  1 107 ? 1.234   -11.498 9.733   1.00 14.45 ? 107 VAL B O   1 
ATOM   3028 C  CB  . VAL B  1 107 ? -1.696  -10.850 10.444  1.00 13.05 ? 107 VAL B CB  1 
ATOM   3029 C  CG1 . VAL B  1 107 ? -1.807  -11.891 11.611  1.00 17.07 ? 107 VAL B CG1 1 
ATOM   3030 C  CG2 . VAL B  1 107 ? -2.975  -9.973  10.475  1.00 15.12 ? 107 VAL B CG2 1 
ATOM   3031 N  N   . SER B  1 108 ? 1.462   -10.815 11.908  1.00 14.33 ? 108 SER B N   1 
ATOM   3032 C  CA  . SER B  1 108 ? 2.755   -11.580 12.139  1.00 15.08 ? 108 SER B CA  1 
ATOM   3033 C  C   . SER B  1 108 ? 3.729   -11.296 10.964  1.00 15.24 ? 108 SER B C   1 
ATOM   3034 O  O   . SER B  1 108 ? 4.335   -12.176 10.325  1.00 16.94 ? 108 SER B O   1 
ATOM   3035 C  CB  . SER B  1 108 ? 2.464   -13.114 12.279  1.00 16.39 ? 108 SER B CB  1 
ATOM   3036 O  OG  . SER B  1 108 ? 1.742   -13.278 13.433  1.00 18.42 ? 108 SER B OG  1 
ATOM   3037 N  N   . GLY B  1 109 ? 3.820   -10.014 10.600  1.00 14.61 ? 109 GLY B N   1 
ATOM   3038 C  CA  . GLY B  1 109 ? 4.722   -9.495  9.609   1.00 14.73 ? 109 GLY B CA  1 
ATOM   3039 C  C   . GLY B  1 109 ? 4.332   -9.684  8.110   1.00 15.94 ? 109 GLY B C   1 
ATOM   3040 O  O   . GLY B  1 109 ? 5.108   -9.196  7.264   1.00 18.78 ? 109 GLY B O   1 
ATOM   3041 N  N   . GLN B  1 110 ? 3.165   -10.222 7.845   1.00 15.42 ? 110 GLN B N   1 
ATOM   3042 C  CA  . GLN B  1 110 ? 2.771   -10.482 6.423   1.00 17.22 ? 110 GLN B CA  1 
ATOM   3043 C  C   . GLN B  1 110 ? 1.640   -9.520  6.023   1.00 12.03 ? 110 GLN B C   1 
ATOM   3044 O  O   . GLN B  1 110 ? 0.678   -9.321  6.763   1.00 12.58 ? 110 GLN B O   1 
ATOM   3045 C  CB  . GLN B  1 110 ? 2.271   -11.896 6.255   1.00 22.27 ? 110 GLN B CB  1 
ATOM   3046 C  CG  . GLN B  1 110 ? 2.950   -12.965 7.139   1.00 25.62 ? 110 GLN B CG  1 
ATOM   3047 C  CD  . GLN B  1 110 ? 3.965   -13.698 6.341   1.00 37.37 ? 110 GLN B CD  1 
ATOM   3048 O  OE1 . GLN B  1 110 ? 4.666   -13.096 5.519   1.00 30.39 ? 110 GLN B OE1 1 
ATOM   3049 N  NE2 . GLN B  1 110 ? 3.945   -15.022 6.458   1.00 36.97 ? 110 GLN B NE2 1 
ATOM   3050 N  N   . HIS B  1 111 ? 1.822   -9.000  4.823   1.00 13.22 ? 111 HIS B N   1 
ATOM   3051 C  CA  . HIS B  1 111 ? 0.768   -8.238  4.164   1.00 13.04 ? 111 HIS B CA  1 
ATOM   3052 C  C   . HIS B  1 111 ? -0.242  -9.089  3.523   1.00 12.29 ? 111 HIS B C   1 
ATOM   3053 O  O   . HIS B  1 111 ? 0.124   -10.159 2.963   1.00 16.72 ? 111 HIS B O   1 
ATOM   3054 C  CB  . HIS B  1 111 ? 1.250   -7.396  2.947   1.00 15.05 ? 111 HIS B CB  1 
ATOM   3055 C  CG  . HIS B  1 111 ? 1.951   -6.158  3.333   1.00 13.35 ? 111 HIS B CG  1 
ATOM   3056 N  ND1 . HIS B  1 111 ? 1.297   -4.933  3.531   1.00 15.33 ? 111 HIS B ND1 1 
ATOM   3057 C  CD2 . HIS B  1 111 ? 3.296   -5.979  3.732   1.00 15.73 ? 111 HIS B CD2 1 
ATOM   3058 C  CE1 . HIS B  1 111 ? 2.282   -4.028  3.946   1.00 15.30 ? 111 HIS B CE1 1 
ATOM   3059 N  NE2 . HIS B  1 111 ? 3.442   -4.676  4.134   1.00 18.09 ? 111 HIS B NE2 1 
ATOM   3060 N  N   . PHE B  1 112 ? -1.472  -8.673  3.580   1.00 10.81 ? 112 PHE B N   1 
ATOM   3061 C  CA  . PHE B  1 112 ? -2.507  -9.225  2.772   1.00 9.56  ? 112 PHE B CA  1 
ATOM   3062 C  C   . PHE B  1 112 ? -2.590  -8.472  1.405   1.00 8.95  ? 112 PHE B C   1 
ATOM   3063 O  O   . PHE B  1 112 ? -1.856  -7.518  1.216   1.00 9.46  ? 112 PHE B O   1 
ATOM   3064 C  CB  . PHE B  1 112 ? -3.846  -9.184  3.501   1.00 11.68 ? 112 PHE B CB  1 
ATOM   3065 C  CG  . PHE B  1 112 ? -3.929  -10.207 4.617   1.00 13.71 ? 112 PHE B CG  1 
ATOM   3066 C  CD1 . PHE B  1 112 ? -3.268  -9.947  5.796   1.00 15.69 ? 112 PHE B CD1 1 
ATOM   3067 C  CD2 . PHE B  1 112 ? -4.617  -11.384 4.445   1.00 15.47 ? 112 PHE B CD2 1 
ATOM   3068 C  CE1 . PHE B  1 112 ? -3.281  -10.873 6.835   1.00 22.41 ? 112 PHE B CE1 1 
ATOM   3069 C  CE2 . PHE B  1 112 ? -4.567  -12.352 5.501   1.00 17.89 ? 112 PHE B CE2 1 
ATOM   3070 C  CZ  . PHE B  1 112 ? -3.977  -12.025 6.648   1.00 19.44 ? 112 PHE B CZ  1 
ATOM   3071 N  N   . ALA B  1 113 ? -3.386  -8.974  0.475   1.00 8.75  ? 113 ALA B N   1 
ATOM   3072 C  CA  . ALA B  1 113 ? -3.446  -8.375  -0.837  1.00 9.73  ? 113 ALA B CA  1 
ATOM   3073 C  C   . ALA B  1 113 ? -3.924  -6.937  -0.770  1.00 8.72  ? 113 ALA B C   1 
ATOM   3074 O  O   . ALA B  1 113 ? -3.445  -6.062  -1.515  1.00 9.66  ? 113 ALA B O   1 
ATOM   3075 C  CB  . ALA B  1 113 ? -4.307  -9.242  -1.732  1.00 10.26 ? 113 ALA B CB  1 
ATOM   3076 N  N   . ALA B  1 114 ? -4.935  -6.668  0.051   1.00 8.39  ? 114 ALA B N   1 
ATOM   3077 C  CA  . ALA B  1 114 ? -5.610  -5.369  0.047   1.00 7.71  ? 114 ALA B CA  1 
ATOM   3078 C  C   . ALA B  1 114 ? -6.340  -5.263  1.372   1.00 7.34  ? 114 ALA B C   1 
ATOM   3079 O  O   . ALA B  1 114 ? -6.307  -6.183  2.244   1.00 7.67  ? 114 ALA B O   1 
ATOM   3080 C  CB  . ALA B  1 114 ? -6.546  -5.235  -1.143  1.00 7.67  ? 114 ALA B CB  1 
ATOM   3081 N  N   . GLU B  1 115 ? -6.947  -4.079  1.611   1.00 7.41  ? 115 GLU B N   1 
ATOM   3082 C  CA  . GLU B  1 115 ? -7.678  -3.858  2.831   1.00 7.03  ? 115 GLU B CA  1 
ATOM   3083 C  C   . GLU B  1 115 ? -8.825  -2.942  2.599   1.00 7.71  ? 115 GLU B C   1 
ATOM   3084 O  O   . GLU B  1 115 ? -8.665  -1.897  1.866   1.00 8.39  ? 115 GLU B O   1 
ATOM   3085 C  CB  . GLU B  1 115 ? -6.722  -3.292  3.882   1.00 8.01  ? 115 GLU B CB  1 
ATOM   3086 C  CG  . GLU B  1 115 ? -7.276  -3.212  5.326   1.00 8.51  ? 115 GLU B CG  1 
ATOM   3087 C  CD  . GLU B  1 115 ? -6.157  -2.905  6.350   1.00 9.10  ? 115 GLU B CD  1 
ATOM   3088 O  OE1 . GLU B  1 115 ? -5.001  -3.392  6.176   1.00 8.44  ? 115 GLU B OE1 1 
ATOM   3089 O  OE2 . GLU B  1 115 ? -6.462  -2.256  7.391   1.00 9.32  ? 115 GLU B OE2 1 
ATOM   3090 N  N   . LEU B  1 116 ? -9.990  -3.240  3.162   1.00 6.42  ? 116 LEU B N   1 
ATOM   3091 C  CA  . LEU B  1 116 ? -11.188 -2.383  3.117   1.00 6.06  ? 116 LEU B CA  1 
ATOM   3092 C  C   . LEU B  1 116 ? -11.317 -1.689  4.418   1.00 6.47  ? 116 LEU B C   1 
ATOM   3093 O  O   . LEU B  1 116 ? -11.196 -2.311  5.516   1.00 6.80  ? 116 LEU B O   1 
ATOM   3094 C  CB  . LEU B  1 116 ? -12.454 -3.246  2.917   1.00 7.37  ? 116 LEU B CB  1 
ATOM   3095 C  CG  . LEU B  1 116 ? -13.787 -2.518  3.039   1.00 7.23  ? 116 LEU B CG  1 
ATOM   3096 C  CD1 . LEU B  1 116 ? -14.050 -1.656  1.808   1.00 8.67  ? 116 LEU B CD1 1 
ATOM   3097 C  CD2 . LEU B  1 116 ? -14.884 -3.509  3.238   1.00 9.05  ? 116 LEU B CD2 1 
ATOM   3098 N  N   . HIS B  1 117 ? -11.568 -0.376  4.398   1.00 6.23  ? 117 HIS B N   1 
ATOM   3099 C  CA  . HIS B  1 117 ? -11.925 0.401   5.613   1.00 6.10  ? 117 HIS B CA  1 
ATOM   3100 C  C   . HIS B  1 117 ? -13.289 0.931   5.527   1.00 6.73  ? 117 HIS B C   1 
ATOM   3101 O  O   . HIS B  1 117 ? -13.674 1.620   4.557   1.00 7.56  ? 117 HIS B O   1 
ATOM   3102 C  CB  . HIS B  1 117 ? -10.971 1.592   5.719   1.00 6.71  ? 117 HIS B CB  1 
ATOM   3103 C  CG  . HIS B  1 117 ? -9.591  1.108   6.054   1.00 6.37  ? 117 HIS B CG  1 
ATOM   3104 N  ND1 . HIS B  1 117 ? -8.430  1.888   5.844   1.00 6.10  ? 117 HIS B ND1 1 
ATOM   3105 C  CD2 . HIS B  1 117 ? -9.164  -0.074  6.651   1.00 7.36  ? 117 HIS B CD2 1 
ATOM   3106 C  CE1 . HIS B  1 117 ? -7.349  1.187   6.302   1.00 7.61  ? 117 HIS B CE1 1 
ATOM   3107 N  NE2 . HIS B  1 117 ? -7.818  -0.027  6.774   1.00 7.34  ? 117 HIS B NE2 1 
ATOM   3108 N  N   . ILE B  1 118 ? -14.120 0.640   6.568   1.00 7.59  ? 118 ILE B N   1 
ATOM   3109 C  CA  . ILE B  1 118 ? -15.483 1.284   6.604   1.00 7.45  ? 118 ILE B CA  1 
ATOM   3110 C  C   . ILE B  1 118 ? -15.452 2.253   7.732   1.00 8.36  ? 118 ILE B C   1 
ATOM   3111 O  O   . ILE B  1 118 ? -15.287 1.889   8.950   1.00 7.92  ? 118 ILE B O   1 
ATOM   3112 C  CB  . ILE B  1 118 ? -16.573 0.181   6.826   1.00 7.24  ? 118 ILE B CB  1 
ATOM   3113 C  CG1 . ILE B  1 118 ? -16.433 -0.983  5.849   1.00 7.63  ? 118 ILE B CG1 1 
ATOM   3114 C  CG2 . ILE B  1 118 ? -17.967 0.880   6.721   1.00 8.44  ? 118 ILE B CG2 1 
ATOM   3115 C  CD1 . ILE B  1 118 ? -17.502 -2.116  6.081   1.00 10.21 ? 118 ILE B CD1 1 
ATOM   3116 N  N   . VAL B  1 119 ? -15.540 3.541   7.384   1.00 8.31  ? 119 VAL B N   1 
ATOM   3117 C  CA  . VAL B  1 119 ? -15.293 4.636   8.335   1.00 8.81  ? 119 VAL B CA  1 
ATOM   3118 C  C   . VAL B  1 119 ? -16.635 5.110   8.928   1.00 7.98  ? 119 VAL B C   1 
ATOM   3119 O  O   . VAL B  1 119 ? -17.590 5.343   8.177   1.00 9.85  ? 119 VAL B O   1 
ATOM   3120 C  CB  . VAL B  1 119 ? -14.693 5.849   7.559   1.00 9.09  ? 119 VAL B CB  1 
ATOM   3121 C  CG1 . VAL B  1 119 ? -14.339 7.003   8.557   1.00 10.80 ? 119 VAL B CG1 1 
ATOM   3122 C  CG2 . VAL B  1 119 ? -13.411 5.398   6.724   1.00 9.07  ? 119 VAL B CG2 1 
ATOM   3123 N  N   . HIS B  1 120 ? -16.653 5.200   10.261  1.00 8.37  ? 120 HIS B N   1 
ATOM   3124 C  CA  . HIS B  1 120 ? -17.839 5.634   11.032  1.00 8.82  ? 120 HIS B CA  1 
ATOM   3125 C  C   . HIS B  1 120 ? -17.398 6.758   11.942  1.00 10.23 ? 120 HIS B C   1 
ATOM   3126 O  O   . HIS B  1 120 ? -16.235 6.943   12.325  1.00 10.81 ? 120 HIS B O   1 
ATOM   3127 C  CB  . HIS B  1 120 ? -18.397 4.492   11.870  1.00 8.92  ? 120 HIS B CB  1 
ATOM   3128 C  CG  . HIS B  1 120 ? -18.794 3.281   11.131  1.00 8.70  ? 120 HIS B CG  1 
ATOM   3129 N  ND1 . HIS B  1 120 ? -17.817 2.418   10.583  1.00 8.86  ? 120 HIS B ND1 1 
ATOM   3130 C  CD2 . HIS B  1 120 ? -20.028 2.689   10.891  1.00 10.31 ? 120 HIS B CD2 1 
ATOM   3131 C  CE1 . HIS B  1 120 ? -18.439 1.373   10.043  1.00 10.39 ? 120 HIS B CE1 1 
ATOM   3132 N  NE2 . HIS B  1 120 ? -19.808 1.485   10.227  1.00 10.61 ? 120 HIS B NE2 1 
ATOM   3133 N  N   . TYR B  1 121 ? -18.394 7.577   12.350  1.00 11.63 ? 121 TYR B N   1 
ATOM   3134 C  CA  . TYR B  1 121 ? -18.126 8.683   13.279  1.00 12.07 ? 121 TYR B CA  1 
ATOM   3135 C  C   . TYR B  1 121 ? -19.127 8.646   14.445  1.00 12.17 ? 121 TYR B C   1 
ATOM   3136 O  O   . TYR B  1 121 ? -20.198 8.144   14.286  1.00 12.43 ? 121 TYR B O   1 
ATOM   3137 C  CB  . TYR B  1 121 ? -18.177 10.039  12.569  1.00 12.64 ? 121 TYR B CB  1 
ATOM   3138 C  CG  . TYR B  1 121 ? -19.550 10.432  12.065  1.00 12.68 ? 121 TYR B CG  1 
ATOM   3139 C  CD1 . TYR B  1 121 ? -20.043 9.921   10.874  1.00 15.10 ? 121 TYR B CD1 1 
ATOM   3140 C  CD2 . TYR B  1 121 ? -20.349 11.321  12.777  1.00 15.13 ? 121 TYR B CD2 1 
ATOM   3141 C  CE1 . TYR B  1 121 ? -21.293 10.277  10.406  1.00 16.10 ? 121 TYR B CE1 1 
ATOM   3142 C  CE2 . TYR B  1 121 ? -21.603 11.683  12.314  1.00 15.70 ? 121 TYR B CE2 1 
ATOM   3143 C  CZ  . TYR B  1 121 ? -22.070 11.156  11.127  1.00 19.12 ? 121 TYR B CZ  1 
ATOM   3144 O  OH  . TYR B  1 121 ? -23.313 11.500  10.645  1.00 23.72 ? 121 TYR B OH  1 
ATOM   3145 N  N   . ASN B  1 122 ? -18.737 9.236   15.585  1.00 13.01 ? 122 ASN B N   1 
ATOM   3146 C  CA  . ASN B  1 122 ? -19.659 9.271   16.715  1.00 14.62 ? 122 ASN B CA  1 
ATOM   3147 C  C   . ASN B  1 122 ? -20.841 10.267  16.458  1.00 13.69 ? 122 ASN B C   1 
ATOM   3148 O  O   . ASN B  1 122 ? -20.639 11.499  16.610  1.00 15.34 ? 122 ASN B O   1 
ATOM   3149 C  CB  . ASN B  1 122 ? -18.864 9.607   17.971  1.00 16.34 ? 122 ASN B CB  1 
ATOM   3150 C  CG  . ASN B  1 122 ? -19.724 9.531   19.207  1.00 20.02 ? 122 ASN B CG  1 
ATOM   3151 O  OD1 . ASN B  1 122 ? -20.921 9.640   19.158  1.00 19.14 ? 122 ASN B OD1 1 
ATOM   3152 N  ND2 . ASN B  1 122 ? -19.062 9.329   20.341  1.00 23.40 ? 122 ASN B ND2 1 
ATOM   3153 N  N   . SER B  1 123 ? -21.947 9.752   15.962  1.00 17.47 ? 123 SER B N   1 
ATOM   3154 C  CA  . SER B  1 123 ? -23.063 10.635  15.604  1.00 18.94 ? 123 SER B CA  1 
ATOM   3155 C  C   . SER B  1 123 ? -23.906 11.015  16.848  1.00 22.87 ? 123 SER B C   1 
ATOM   3156 O  O   . SER B  1 123 ? -24.783 11.914  16.729  1.00 19.33 ? 123 SER B O   1 
ATOM   3157 C  CB  . SER B  1 123 ? -23.893 9.972   14.522  1.00 17.05 ? 123 SER B CB  1 
ATOM   3158 O  OG  . SER B  1 123 ? -24.262 8.714   14.967  1.00 17.83 ? 123 SER B OG  1 
ATOM   3159 N  N   . ASP B  1 124 ? -23.698 10.347  17.974  1.00 20.58 ? 124 ASP B N   1 
ATOM   3160 C  CA  . ASP B  1 124 ? -24.301 10.816  19.248  1.00 22.22 ? 124 ASP B CA  1 
ATOM   3161 C  C   . ASP B  1 124 ? -23.777 12.178  19.667  1.00 24.08 ? 124 ASP B C   1 
ATOM   3162 O  O   . ASP B  1 124 ? -24.544 13.007  20.178  1.00 21.71 ? 124 ASP B O   1 
ATOM   3163 C  CB  . ASP B  1 124 ? -24.072 9.774   20.362  1.00 21.53 ? 124 ASP B CB  1 
ATOM   3164 C  CG  . ASP B  1 124 ? -24.949 8.516   20.223  1.00 20.49 ? 124 ASP B CG  1 
ATOM   3165 O  OD1 . ASP B  1 124 ? -25.942 8.490   19.424  1.00 26.46 ? 124 ASP B OD1 1 
ATOM   3166 O  OD2 . ASP B  1 124 ? -24.629 7.526   20.906  1.00 24.39 ? 124 ASP B OD2 1 
ATOM   3167 N  N   . LEU B  1 125 ? -22.496 12.416  19.442  1.00 20.93 ? 125 LEU B N   1 
ATOM   3168 C  CA  . LEU B  1 125 ? -21.748 13.655  19.844  1.00 19.96 ? 125 LEU B CA  1 
ATOM   3169 C  C   . LEU B  1 125 ? -21.533 14.684  18.780  1.00 24.49 ? 125 LEU B C   1 
ATOM   3170 O  O   . LEU B  1 125 ? -21.447 15.904  19.065  1.00 24.02 ? 125 LEU B O   1 
ATOM   3171 C  CB  . LEU B  1 125 ? -20.393 13.323  20.472  1.00 20.22 ? 125 LEU B CB  1 
ATOM   3172 C  CG  . LEU B  1 125 ? -20.442 12.394  21.663  1.00 23.03 ? 125 LEU B CG  1 
ATOM   3173 C  CD1 . LEU B  1 125 ? -19.081 12.111  22.198  1.00 21.08 ? 125 LEU B CD1 1 
ATOM   3174 C  CD2 . LEU B  1 125 ? -21.203 13.047  22.813  1.00 23.57 ? 125 LEU B CD2 1 
ATOM   3175 N  N   . TYR B  1 126 ? -21.380 14.238  17.550  1.00 19.98 ? 126 TYR B N   1 
ATOM   3176 C  CA  . TYR B  1 126 ? -21.001 15.106  16.452  1.00 19.47 ? 126 TYR B CA  1 
ATOM   3177 C  C   . TYR B  1 126 ? -21.935 15.034  15.274  1.00 17.52 ? 126 TYR B C   1 
ATOM   3178 O  O   . TYR B  1 126 ? -22.550 14.017  14.974  1.00 19.73 ? 126 TYR B O   1 
ATOM   3179 C  CB  . TYR B  1 126 ? -19.492 14.782  16.031  1.00 19.23 ? 126 TYR B CB  1 
ATOM   3180 C  CG  . TYR B  1 126 ? -18.614 14.715  17.202  1.00 18.91 ? 126 TYR B CG  1 
ATOM   3181 C  CD1 . TYR B  1 126 ? -18.299 15.886  17.923  1.00 24.90 ? 126 TYR B CD1 1 
ATOM   3182 C  CD2 . TYR B  1 126 ? -18.052 13.498  17.626  1.00 19.33 ? 126 TYR B CD2 1 
ATOM   3183 C  CE1 . TYR B  1 126 ? -17.517 15.815  19.058  1.00 21.29 ? 126 TYR B CE1 1 
ATOM   3184 C  CE2 . TYR B  1 126 ? -17.272 13.412  18.724  1.00 21.00 ? 126 TYR B CE2 1 
ATOM   3185 C  CZ  . TYR B  1 126 ? -16.983 14.587  19.434  1.00 23.22 ? 126 TYR B CZ  1 
ATOM   3186 O  OH  . TYR B  1 126 ? -16.212 14.504  20.583  1.00 27.70 ? 126 TYR B OH  1 
ATOM   3187 N  N   . PRO B  1 127 ? -22.043 16.178  14.568  1.00 23.35 ? 127 PRO B N   1 
ATOM   3188 C  CA  . PRO B  1 127 ? -23.016 16.191  13.474  1.00 21.81 ? 127 PRO B CA  1 
ATOM   3189 C  C   . PRO B  1 127 ? -22.496 15.699  12.123  1.00 23.62 ? 127 PRO B C   1 
ATOM   3190 O  O   . PRO B  1 127 ? -23.316 15.436  11.192  1.00 27.19 ? 127 PRO B O   1 
ATOM   3191 C  CB  . PRO B  1 127 ? -23.374 17.681  13.335  1.00 24.40 ? 127 PRO B CB  1 
ATOM   3192 C  CG  . PRO B  1 127 ? -22.226 18.431  13.921  1.00 26.64 ? 127 PRO B CG  1 
ATOM   3193 C  CD  . PRO B  1 127 ? -21.445 17.504  14.839  1.00 25.25 ? 127 PRO B CD  1 
ATOM   3194 N  N   . ASP B  1 128 ? -21.184 15.450  12.007  1.00 19.46 ? 128 ASP B N   1 
ATOM   3195 C  CA  . ASP B  1 128 ? -20.672 14.915  10.753  1.00 17.17 ? 128 ASP B CA  1 
ATOM   3196 C  C   . ASP B  1 128 ? -19.305 14.365  11.038  1.00 20.22 ? 128 ASP B C   1 
ATOM   3197 O  O   . ASP B  1 128 ? -18.731 14.652  12.101  1.00 18.93 ? 128 ASP B O   1 
ATOM   3198 C  CB  . ASP B  1 128 ? -20.560 16.123  9.763   1.00 22.25 ? 128 ASP B CB  1 
ATOM   3199 C  CG  . ASP B  1 128 ? -19.709 17.165  10.302  1.00 25.66 ? 128 ASP B CG  1 
ATOM   3200 O  OD1 . ASP B  1 128 ? -20.122 17.779  11.308  1.00 33.26 ? 128 ASP B OD1 1 
ATOM   3201 O  OD2 . ASP B  1 128 ? -18.604 17.374  9.778   1.00 27.93 ? 128 ASP B OD2 1 
ATOM   3202 N  N   . ALA B  1 129 ? -18.756 13.540  10.125  1.00 17.75 ? 129 ALA B N   1 
ATOM   3203 C  CA  . ALA B  1 129 ? -17.480 12.899  10.339  1.00 17.86 ? 129 ALA B CA  1 
ATOM   3204 C  C   . ALA B  1 129 ? -16.317 13.868  10.368  1.00 16.77 ? 129 ALA B C   1 
ATOM   3205 O  O   . ALA B  1 129 ? -15.384 13.671  11.088  1.00 16.58 ? 129 ALA B O   1 
ATOM   3206 C  CB  . ALA B  1 129 ? -17.275 11.836  9.209   1.00 18.08 ? 129 ALA B CB  1 
ATOM   3207 N  N   A SER B  1 130 ? -16.373 14.946  9.575   0.50 17.45 ? 130 SER B N   1 
ATOM   3208 N  N   B SER B  1 130 ? -16.399 14.936  9.578   0.50 18.08 ? 130 SER B N   1 
ATOM   3209 C  CA  A SER B  1 130 ? -15.229 15.905  9.584   0.50 20.23 ? 130 SER B CA  1 
ATOM   3210 C  CA  B SER B  1 130 ? -15.267 15.877  9.544   0.50 21.64 ? 130 SER B CA  1 
ATOM   3211 C  C   A SER B  1 130 ? -15.072 16.501  10.992  0.50 19.60 ? 130 SER B C   1 
ATOM   3212 C  C   B SER B  1 130 ? -15.077 16.543  10.933  0.50 20.63 ? 130 SER B C   1 
ATOM   3213 O  O   A SER B  1 130 ? -13.977 16.495  11.566  0.50 21.30 ? 130 SER B O   1 
ATOM   3214 O  O   B SER B  1 130 ? -13.947 16.600  11.440  0.50 23.13 ? 130 SER B O   1 
ATOM   3215 C  CB  A SER B  1 130 ? -15.323 17.007  8.492   0.50 21.56 ? 130 SER B CB  1 
ATOM   3216 C  CB  B SER B  1 130 ? -15.372 16.863  8.353   0.50 23.71 ? 130 SER B CB  1 
ATOM   3217 O  OG  A SER B  1 130 ? -14.266 17.972  8.667   0.50 22.29 ? 130 SER B OG  1 
ATOM   3218 O  OG  B SER B  1 130 ? -16.629 17.498  8.319   0.50 27.73 ? 130 SER B OG  1 
ATOM   3219 N  N   . THR B  1 131 ? -16.170 16.955  11.573  1.00 21.37 ? 131 THR B N   1 
ATOM   3220 C  CA  . THR B  1 131 ? -16.100 17.484  12.951  1.00 23.00 ? 131 THR B CA  1 
ATOM   3221 C  C   . THR B  1 131 ? -15.612 16.449  13.931  1.00 22.67 ? 131 THR B C   1 
ATOM   3222 O  O   . THR B  1 131 ? -14.806 16.771  14.820  1.00 24.31 ? 131 THR B O   1 
ATOM   3223 C  CB  . THR B  1 131 ? -17.499 17.906  13.436  1.00 25.92 ? 131 THR B CB  1 
ATOM   3224 O  OG1 . THR B  1 131 ? -17.970 18.961  12.586  1.00 27.86 ? 131 THR B OG1 1 
ATOM   3225 C  CG2 . THR B  1 131 ? -17.496 18.371  14.988  1.00 24.59 ? 131 THR B CG2 1 
ATOM   3226 N  N   . ALA B  1 132 ? -16.098 15.180  13.816  1.00 17.60 ? 132 ALA B N   1 
ATOM   3227 C  CA  . ALA B  1 132 ? -15.722 14.100  14.714  1.00 17.35 ? 132 ALA B CA  1 
ATOM   3228 C  C   . ALA B  1 132 ? -14.209 13.786  14.568  1.00 16.37 ? 132 ALA B C   1 
ATOM   3229 O  O   . ALA B  1 132 ? -13.623 13.214  15.516  1.00 15.38 ? 132 ALA B O   1 
ATOM   3230 C  CB  . ALA B  1 132 ? -16.543 12.821  14.409  1.00 16.68 ? 132 ALA B CB  1 
ATOM   3231 N  N   . SER B  1 133 ? -13.667 14.038  13.373  1.00 17.65 ? 133 SER B N   1 
ATOM   3232 C  CA  . SER B  1 133 ? -12.334 13.486  13.047  1.00 16.95 ? 133 SER B CA  1 
ATOM   3233 C  C   . SER B  1 133 ? -11.270 14.062  13.851  1.00 19.12 ? 133 SER B C   1 
ATOM   3234 O  O   . SER B  1 133 ? -10.139 13.492  13.938  1.00 19.43 ? 133 SER B O   1 
ATOM   3235 C  CB  . SER B  1 133 ? -12.013 13.651  11.570  1.00 20.44 ? 133 SER B CB  1 
ATOM   3236 O  OG  . SER B  1 133 ? -11.753 15.013  11.223  1.00 22.22 ? 133 SER B OG  1 
ATOM   3237 N  N   . ASN B  1 134 ? -11.522 15.180  14.473  1.00 19.89 ? 134 ASN B N   1 
ATOM   3238 C  CA  . ASN B  1 134 ? -10.405 15.679  15.311  1.00 20.95 ? 134 ASN B CA  1 
ATOM   3239 C  C   . ASN B  1 134 ? -10.761 15.686  16.764  1.00 21.68 ? 134 ASN B C   1 
ATOM   3240 O  O   . ASN B  1 134 ? -10.151 16.414  17.528  1.00 26.70 ? 134 ASN B O   1 
ATOM   3241 C  CB  . ASN B  1 134 ? -9.683  16.942  14.806  1.00 29.34 ? 134 ASN B CB  1 
ATOM   3242 C  CG  . ASN B  1 134 ? -10.670 17.975  14.377  1.00 34.83 ? 134 ASN B CG  1 
ATOM   3243 O  OD1 . ASN B  1 134 ? -11.731 18.058  14.975  1.00 38.77 ? 134 ASN B OD1 1 
ATOM   3244 N  ND2 . ASN B  1 134 ? -10.396 18.687  13.297  1.00 43.76 ? 134 ASN B ND2 1 
ATOM   3245 N  N   . LYS B  1 135 ? -11.625 14.762  17.194  1.00 20.56 ? 135 LYS B N   1 
ATOM   3246 C  CA  . LYS B  1 135 ? -12.041 14.619  18.649  1.00 22.53 ? 135 LYS B CA  1 
ATOM   3247 C  C   . LYS B  1 135 ? -11.736 13.253  19.144  1.00 26.35 ? 135 LYS B C   1 
ATOM   3248 O  O   . LYS B  1 135 ? -11.750 12.319  18.352  1.00 20.99 ? 135 LYS B O   1 
ATOM   3249 C  CB  . LYS B  1 135 ? -13.558 14.842  18.775  1.00 28.85 ? 135 LYS B CB  1 
ATOM   3250 C  CG  . LYS B  1 135 ? -14.098 16.014  17.948  1.00 30.92 ? 135 LYS B CG  1 
ATOM   3251 C  CD  . LYS B  1 135 ? -14.318 17.288  18.786  1.00 41.02 ? 135 LYS B CD  1 
ATOM   3252 C  CE  . LYS B  1 135 ? -14.014 18.594  18.033  1.00 45.46 ? 135 LYS B CE  1 
ATOM   3253 N  NZ  . LYS B  1 135 ? -14.454 18.707  16.603  1.00 45.00 ? 135 LYS B NZ  1 
ATOM   3254 N  N   . SER B  1 136 ? -11.534 13.095  20.468  1.00 30.40 ? 136 SER B N   1 
ATOM   3255 C  CA  . SER B  1 136 ? -10.883 11.868  20.943  1.00 28.68 ? 136 SER B CA  1 
ATOM   3256 C  C   . SER B  1 136 ? -11.900 10.740  20.702  1.00 28.58 ? 136 SER B C   1 
ATOM   3257 O  O   . SER B  1 136 ? -13.017 10.939  20.977  1.00 24.20 ? 136 SER B O   1 
ATOM   3258 C  CB  . SER B  1 136 ? -10.517 11.962  22.465  1.00 39.43 ? 136 SER B CB  1 
ATOM   3259 O  OG  . SER B  1 136 ? -11.477 11.298  23.331  1.00 37.03 ? 136 SER B OG  1 
ATOM   3260 N  N   . GLU B  1 137 ? -11.490 9.586   20.169  1.00 27.16 ? 137 GLU B N   1 
ATOM   3261 C  CA  . GLU B  1 137 ? -12.446 8.534   19.747  1.00 28.79 ? 137 GLU B CA  1 
ATOM   3262 C  C   . GLU B  1 137 ? -13.720 9.024   18.966  1.00 23.90 ? 137 GLU B C   1 
ATOM   3263 O  O   . GLU B  1 137 ? -14.817 8.396   19.009  1.00 22.97 ? 137 GLU B O   1 
ATOM   3264 C  CB  . GLU B  1 137 ? -12.824 7.621   20.915  1.00 34.35 ? 137 GLU B CB  1 
ATOM   3265 N  N   . GLY B  1 138 ? -13.558 10.109  18.203  1.00 17.90 ? 138 GLY B N   1 
ATOM   3266 C  CA  . GLY B  1 138 ? -14.538 10.610  17.258  1.00 15.07 ? 138 GLY B CA  1 
ATOM   3267 C  C   . GLY B  1 138 ? -14.834 9.641   16.106  1.00 12.45 ? 138 GLY B C   1 
ATOM   3268 O  O   . GLY B  1 138 ? -15.912 9.689   15.569  1.00 12.97 ? 138 GLY B O   1 
ATOM   3269 N  N   . LEU B  1 139 ? -13.879 8.762   15.740  1.00 10.81 ? 139 LEU B N   1 
ATOM   3270 C  CA  . LEU B  1 139 ? -14.061 7.861   14.570  1.00 10.50 ? 139 LEU B CA  1 
ATOM   3271 C  C   . LEU B  1 139 ? -13.920 6.408   14.989  1.00 10.80 ? 139 LEU B C   1 
ATOM   3272 O  O   . LEU B  1 139 ? -13.194 6.116   15.950  1.00 11.33 ? 139 LEU B O   1 
ATOM   3273 C  CB  . LEU B  1 139 ? -13.028 8.142   13.498  1.00 10.97 ? 139 LEU B CB  1 
ATOM   3274 C  CG  . LEU B  1 139 ? -13.074 9.597   12.979  1.00 11.61 ? 139 LEU B CG  1 
ATOM   3275 C  CD1 . LEU B  1 139 ? -11.922 9.807   11.998  1.00 12.59 ? 139 LEU B CD1 1 
ATOM   3276 C  CD2 . LEU B  1 139 ? -14.423 9.950   12.358  1.00 12.06 ? 139 LEU B CD2 1 
ATOM   3277 N  N   . ALA B  1 140 ? -14.631 5.526   14.306  1.00 10.39 ? 140 ALA B N   1 
ATOM   3278 C  CA  . ALA B  1 140 ? -14.450 4.059   14.496  1.00 9.67  ? 140 ALA B CA  1 
ATOM   3279 C  C   . ALA B  1 140 ? -14.316 3.574   13.046  1.00 9.70  ? 140 ALA B C   1 
ATOM   3280 O  O   . ALA B  1 140 ? -15.218 3.807   12.179  1.00 11.06 ? 140 ALA B O   1 
ATOM   3281 C  CB  . ALA B  1 140 ? -15.623 3.430   15.195  1.00 11.22 ? 140 ALA B CB  1 
ATOM   3282 N  N   . VAL B  1 141 ? -13.188 2.878   12.774  1.00 8.68  ? 141 VAL B N   1 
ATOM   3283 C  CA  . VAL B  1 141 ? -13.031 2.312   11.450  1.00 8.12  ? 141 VAL B CA  1 
ATOM   3284 C  C   . VAL B  1 141 ? -13.014 0.807   11.577  1.00 8.39  ? 141 VAL B C   1 
ATOM   3285 O  O   . VAL B  1 141 ? -12.307 0.280   12.436  1.00 9.99  ? 141 VAL B O   1 
ATOM   3286 C  CB  . VAL B  1 141 ? -11.714 2.847   10.775  1.00 8.32  ? 141 VAL B CB  1 
ATOM   3287 C  CG1 . VAL B  1 141 ? -11.579 2.233   9.362   1.00 9.60  ? 141 VAL B CG1 1 
ATOM   3288 C  CG2 . VAL B  1 141 ? -11.779 4.375   10.627  1.00 8.79  ? 141 VAL B CG2 1 
ATOM   3289 N  N   . LEU B  1 142 ? -13.744 0.134   10.707  1.00 7.92  ? 142 LEU B N   1 
ATOM   3290 C  CA  . LEU B  1 142 ? -13.689 -1.350  10.551  1.00 8.48  ? 142 LEU B CA  1 
ATOM   3291 C  C   . LEU B  1 142 ? -12.767 -1.679  9.451   1.00 8.18  ? 142 LEU B C   1 
ATOM   3292 O  O   . LEU B  1 142 ? -12.881 -1.111  8.352   1.00 9.34  ? 142 LEU B O   1 
ATOM   3293 C  CB  . LEU B  1 142 ? -15.041 -1.959  10.268  1.00 9.12  ? 142 LEU B CB  1 
ATOM   3294 C  CG  . LEU B  1 142 ? -16.225 -1.565  11.145  1.00 10.70 ? 142 LEU B CG  1 
ATOM   3295 C  CD1 . LEU B  1 142 ? -17.468 -2.313  10.624  1.00 12.36 ? 142 LEU B CD1 1 
ATOM   3296 C  CD2 . LEU B  1 142 ? -15.973 -1.870  12.654  1.00 12.81 ? 142 LEU B CD2 1 
ATOM   3297 N  N   . ALA B  1 143 ? -11.820 -2.594  9.669   1.00 8.41  ? 143 ALA B N   1 
ATOM   3298 C  CA  . ALA B  1 143 ? -10.898 -3.019  8.663   1.00 7.80  ? 143 ALA B CA  1 
ATOM   3299 C  C   . ALA B  1 143 ? -11.073 -4.478  8.308   1.00 7.02  ? 143 ALA B C   1 
ATOM   3300 O  O   . ALA B  1 143 ? -11.141 -5.331  9.232   1.00 8.37  ? 143 ALA B O   1 
ATOM   3301 C  CB  . ALA B  1 143 ? -9.437  -2.807  9.131   1.00 9.06  ? 143 ALA B CB  1 
ATOM   3302 N  N   . VAL B  1 144 ? -11.186 -4.767  7.028   1.00 6.90  ? 144 VAL B N   1 
ATOM   3303 C  CA  . VAL B  1 144 ? -11.288 -6.140  6.535   1.00 7.87  ? 144 VAL B CA  1 
ATOM   3304 C  C   . VAL B  1 144 ? -10.026 -6.410  5.715   1.00 7.72  ? 144 VAL B C   1 
ATOM   3305 O  O   . VAL B  1 144 ? -9.754  -5.683  4.723   1.00 7.67  ? 144 VAL B O   1 
ATOM   3306 C  CB  . VAL B  1 144 ? -12.565 -6.338  5.668   1.00 8.17  ? 144 VAL B CB  1 
ATOM   3307 C  CG1 . VAL B  1 144 ? -12.599 -7.784  5.142   1.00 9.48  ? 144 VAL B CG1 1 
ATOM   3308 C  CG2 . VAL B  1 144 ? -13.841 -5.995  6.426   1.00 8.08  ? 144 VAL B CG2 1 
ATOM   3309 N  N   . LEU B  1 145 ? -9.295  -7.434  6.060   1.00 7.97  ? 145 LEU B N   1 
ATOM   3310 C  CA  . LEU B  1 145 ? -8.127  -7.895  5.340   1.00 8.71  ? 145 LEU B CA  1 
ATOM   3311 C  C   . LEU B  1 145 ? -8.589  -8.691  4.149   1.00 7.93  ? 145 LEU B C   1 
ATOM   3312 O  O   . LEU B  1 145 ? -9.568  -9.478  4.227   1.00 8.56  ? 145 LEU B O   1 
ATOM   3313 C  CB  . LEU B  1 145 ? -7.223  -8.719  6.245   1.00 9.46  ? 145 LEU B CB  1 
ATOM   3314 C  CG  . LEU B  1 145 ? -6.764  -7.974  7.498   1.00 10.83 ? 145 LEU B CG  1 
ATOM   3315 C  CD1 . LEU B  1 145 ? -6.171  -8.919  8.528   1.00 12.32 ? 145 LEU B CD1 1 
ATOM   3316 C  CD2 . LEU B  1 145 ? -5.693  -6.973  7.146   1.00 14.73 ? 145 LEU B CD2 1 
ATOM   3317 N  N   . ILE B  1 146 ? -8.005  -8.443  2.989   1.00 8.55  ? 146 ILE B N   1 
ATOM   3318 C  CA  . ILE B  1 146 ? -8.416  -9.058  1.754   1.00 8.01  ? 146 ILE B CA  1 
ATOM   3319 C  C   . ILE B  1 146 ? -7.248  -9.879  1.176   1.00 8.37  ? 146 ILE B C   1 
ATOM   3320 O  O   . ILE B  1 146 ? -6.111  -9.384  1.010   1.00 8.62  ? 146 ILE B O   1 
ATOM   3321 C  CB  . ILE B  1 146 ? -8.829  -8.002  0.703   1.00 8.59  ? 146 ILE B CB  1 
ATOM   3322 C  CG1 . ILE B  1 146 ? -9.987  -7.176  1.224   1.00 9.23  ? 146 ILE B CG1 1 
ATOM   3323 C  CG2 . ILE B  1 146 ? -9.108  -8.672  -0.660  1.00 9.36  ? 146 ILE B CG2 1 
ATOM   3324 C  CD1 . ILE B  1 146 ? -10.260 -5.878  0.405   1.00 10.37 ? 146 ILE B CD1 1 
ATOM   3325 N  N   . GLU B  1 147 ? -7.559  -11.139 0.873   1.00 9.67  ? 147 GLU B N   1 
ATOM   3326 C  CA  . GLU B  1 147 ? -6.527  -12.033 0.305   1.00 10.42 ? 147 GLU B CA  1 
ATOM   3327 C  C   . GLU B  1 147 ? -6.941  -12.439 -1.104  1.00 9.98  ? 147 GLU B C   1 
ATOM   3328 O  O   . GLU B  1 147 ? -8.148  -12.430 -1.435  1.00 10.15 ? 147 GLU B O   1 
ATOM   3329 C  CB  . GLU B  1 147 ? -6.378  -13.275 1.238   1.00 15.50 ? 147 GLU B CB  1 
ATOM   3330 C  CG  . GLU B  1 147 ? -7.384  -14.330 1.179   1.00 19.29 ? 147 GLU B CG  1 
ATOM   3331 C  CD  . GLU B  1 147 ? -7.176  -15.448 2.268   1.00 26.25 ? 147 GLU B CD  1 
ATOM   3332 O  OE1 . GLU B  1 147 ? -6.131  -15.364 2.995   1.00 23.76 ? 147 GLU B OE1 1 
ATOM   3333 O  OE2 . GLU B  1 147 ? -8.122  -16.319 2.428   1.00 30.75 ? 147 GLU B OE2 1 
ATOM   3334 N  N   . MET B  1 148 ? -5.985  -12.783 -1.932  1.00 9.36  ? 148 MET B N   1 
ATOM   3335 C  CA  . MET B  1 148 ? -6.258  -13.291 -3.256  1.00 9.72  ? 148 MET B CA  1 
ATOM   3336 C  C   . MET B  1 148 ? -6.850  -14.705 -3.144  1.00 11.27 ? 148 MET B C   1 
ATOM   3337 O  O   . MET B  1 148 ? -6.296  -15.580 -2.503  1.00 11.87 ? 148 MET B O   1 
ATOM   3338 C  CB  . MET B  1 148 ? -4.953  -13.380 -4.056  1.00 10.53 ? 148 MET B CB  1 
ATOM   3339 C  CG  . MET B  1 148 ? -5.197  -13.629 -5.562  1.00 11.32 ? 148 MET B CG  1 
ATOM   3340 S  SD  . MET B  1 148 ? -3.689  -13.823 -6.502  1.00 14.48 ? 148 MET B SD  1 
ATOM   3341 C  CE  . MET B  1 148 ? -3.149  -12.127 -6.485  1.00 13.40 ? 148 MET B CE  1 
ATOM   3342 N  N   . GLY B  1 149 ? -8.013  -14.855 -3.770  1.00 9.46  ? 149 GLY B N   1 
ATOM   3343 C  CA  . GLY B  1 149 ? -8.763  -16.126 -3.638  1.00 9.60  ? 149 GLY B CA  1 
ATOM   3344 C  C   . GLY B  1 149 ? -9.828  -16.193 -4.696  1.00 8.59  ? 149 GLY B C   1 
ATOM   3345 O  O   . GLY B  1 149 ? -9.656  -15.875 -5.894  1.00 9.64  ? 149 GLY B O   1 
ATOM   3346 N  N   . SER B  1 150 ? -11.001 -16.635 -4.232  1.00 9.50  ? 150 SER B N   1 
ATOM   3347 C  CA  . SER B  1 150 ? -12.219 -16.661 -5.112  1.00 10.60 ? 150 SER B CA  1 
ATOM   3348 C  C   . SER B  1 150 ? -12.751 -15.323 -5.538  1.00 9.55  ? 150 SER B C   1 
ATOM   3349 O  O   . SER B  1 150 ? -12.652 -14.340 -4.750  1.00 10.84 ? 150 SER B O   1 
ATOM   3350 C  CB  . SER B  1 150 ? -13.339 -17.426 -4.422  1.00 9.72  ? 150 SER B CB  1 
ATOM   3351 O  OG  . SER B  1 150 ? -12.933 -18.804 -4.223  1.00 11.51 ? 150 SER B OG  1 
ATOM   3352 N  N   . PHE B  1 151 ? -13.344 -15.321 -6.725  1.00 10.02 ? 151 PHE B N   1 
ATOM   3353 C  CA  . PHE B  1 151 ? -14.135 -14.145 -7.139  1.00 9.99  ? 151 PHE B CA  1 
ATOM   3354 C  C   . PHE B  1 151 ? -15.163 -13.835 -6.130  1.00 10.66 ? 151 PHE B C   1 
ATOM   3355 O  O   . PHE B  1 151 ? -15.815 -14.741 -5.577  1.00 11.53 ? 151 PHE B O   1 
ATOM   3356 C  CB  . PHE B  1 151 ? -14.732 -14.469 -8.485  1.00 10.30 ? 151 PHE B CB  1 
ATOM   3357 C  CG  . PHE B  1 151 ? -15.623 -13.361 -9.006  1.00 10.19 ? 151 PHE B CG  1 
ATOM   3358 C  CD1 . PHE B  1 151 ? -15.011 -12.251 -9.640  1.00 11.57 ? 151 PHE B CD1 1 
ATOM   3359 C  CD2 . PHE B  1 151 ? -16.973 -13.375 -8.867  1.00 10.75 ? 151 PHE B CD2 1 
ATOM   3360 C  CE1 . PHE B  1 151 ? -15.807 -11.126 -10.105 1.00 11.89 ? 151 PHE B CE1 1 
ATOM   3361 C  CE2 . PHE B  1 151 ? -17.773 -12.251 -9.316  1.00 11.70 ? 151 PHE B CE2 1 
ATOM   3362 C  CZ  . PHE B  1 151 ? -17.152 -11.198 -9.944  1.00 10.67 ? 151 PHE B CZ  1 
ATOM   3363 N  N   . ASN B  1 152 ? -15.370 -12.527 -5.819  1.00 9.37  ? 152 ASN B N   1 
ATOM   3364 C  CA  . ASN B  1 152 ? -16.256 -12.111 -4.803  1.00 8.80  ? 152 ASN B CA  1 
ATOM   3365 C  C   . ASN B  1 152 ? -17.337 -11.193 -5.429  1.00 9.73  ? 152 ASN B C   1 
ATOM   3366 O  O   . ASN B  1 152 ? -17.063 -10.013 -5.749  1.00 9.31  ? 152 ASN B O   1 
ATOM   3367 C  CB  . ASN B  1 152 ? -15.447 -11.320 -3.698  1.00 9.11  ? 152 ASN B CB  1 
ATOM   3368 C  CG  . ASN B  1 152 ? -16.256 -11.068 -2.481  1.00 10.44 ? 152 ASN B CG  1 
ATOM   3369 O  OD1 . ASN B  1 152 ? -17.394 -10.573 -2.580  1.00 11.19 ? 152 ASN B OD1 1 
ATOM   3370 N  ND2 . ASN B  1 152 ? -15.716 -11.425 -1.282  1.00 10.69 ? 152 ASN B ND2 1 
ATOM   3371 N  N   . PRO B  1 153 ? -18.554 -11.684 -5.662  1.00 9.64  ? 153 PRO B N   1 
ATOM   3372 C  CA  . PRO B  1 153 ? -19.579 -10.872 -6.346  1.00 9.89  ? 153 PRO B CA  1 
ATOM   3373 C  C   . PRO B  1 153 ? -19.889 -9.643  -5.535  1.00 11.74 ? 153 PRO B C   1 
ATOM   3374 O  O   . PRO B  1 153 ? -20.296 -8.600  -6.138  1.00 12.63 ? 153 PRO B O   1 
ATOM   3375 C  CB  . PRO B  1 153 ? -20.756 -11.825 -6.517  1.00 12.25 ? 153 PRO B CB  1 
ATOM   3376 C  CG  . PRO B  1 153 ? -20.220 -13.176 -6.304  1.00 17.34 ? 153 PRO B CG  1 
ATOM   3377 C  CD  . PRO B  1 153 ? -18.953 -13.097 -5.431  1.00 12.19 ? 153 PRO B CD  1 
ATOM   3378 N  N   . SER B  1 154 ? -19.813 -9.682  -4.226  1.00 10.19 ? 154 SER B N   1 
ATOM   3379 C  CA  . SER B  1 154 ? -20.183 -8.496  -3.425  1.00 10.41 ? 154 SER B CA  1 
ATOM   3380 C  C   . SER B  1 154 ? -19.158 -7.335  -3.626  1.00 10.48 ? 154 SER B C   1 
ATOM   3381 O  O   . SER B  1 154 ? -19.561 -6.164  -3.866  1.00 9.94  ? 154 SER B O   1 
ATOM   3382 C  CB  . SER B  1 154 ? -20.299 -8.851  -1.954  1.00 14.98 ? 154 SER B CB  1 
ATOM   3383 O  OG  . SER B  1 154 ? -21.290 -9.872  -1.795  1.00 18.09 ? 154 SER B OG  1 
ATOM   3384 N  N   . TYR B  1 155 ? -17.837 -7.632  -3.547  1.00 9.52  ? 155 TYR B N   1 
ATOM   3385 C  CA  . TYR B  1 155 ? -16.852 -6.625  -3.880  1.00 9.18  ? 155 TYR B CA  1 
ATOM   3386 C  C   . TYR B  1 155 ? -17.044 -6.175  -5.280  1.00 9.44  ? 155 TYR B C   1 
ATOM   3387 O  O   . TYR B  1 155 ? -16.657 -4.977  -5.577  1.00 9.56  ? 155 TYR B O   1 
ATOM   3388 C  CB  . TYR B  1 155 ? -15.423 -7.092  -3.555  1.00 8.89  ? 155 TYR B CB  1 
ATOM   3389 C  CG  . TYR B  1 155 ? -15.064 -7.000  -2.062  1.00 8.96  ? 155 TYR B CG  1 
ATOM   3390 C  CD1 . TYR B  1 155 ? -15.468 -7.949  -1.130  1.00 8.20  ? 155 TYR B CD1 1 
ATOM   3391 C  CD2 . TYR B  1 155 ? -14.338 -5.877  -1.591  1.00 9.25  ? 155 TYR B CD2 1 
ATOM   3392 C  CE1 . TYR B  1 155 ? -15.253 -7.828  0.220   1.00 10.15 ? 155 TYR B CE1 1 
ATOM   3393 C  CE2 . TYR B  1 155 ? -14.056 -5.783  -0.238  1.00 9.29  ? 155 TYR B CE2 1 
ATOM   3394 C  CZ  . TYR B  1 155 ? -14.498 -6.770  0.650   1.00 10.15 ? 155 TYR B CZ  1 
ATOM   3395 O  OH  . TYR B  1 155 ? -14.217 -6.626  1.985   1.00 10.08 ? 155 TYR B OH  1 
ATOM   3396 N  N   . ASP B  1 156 ? -17.491 -6.996  -6.205  1.00 9.45  ? 156 ASP B N   1 
ATOM   3397 C  CA  . ASP B  1 156 ? -17.561 -6.577  -7.571  1.00 9.26  ? 156 ASP B CA  1 
ATOM   3398 C  C   . ASP B  1 156 ? -18.677 -5.588  -7.708  1.00 9.73  ? 156 ASP B C   1 
ATOM   3399 O  O   . ASP B  1 156 ? -18.663 -4.861  -8.762  1.00 11.39 ? 156 ASP B O   1 
ATOM   3400 C  CB  . ASP B  1 156 ? -17.731 -7.729  -8.583  1.00 11.55 ? 156 ASP B CB  1 
ATOM   3401 C  CG  . ASP B  1 156 ? -16.783 -7.603  -9.766  1.00 11.85 ? 156 ASP B CG  1 
ATOM   3402 O  OD1 . ASP B  1 156 ? -15.583 -7.378  -9.520  1.00 12.46 ? 156 ASP B OD1 1 
ATOM   3403 O  OD2 . ASP B  1 156 ? -17.236 -7.691  -10.924 1.00 16.87 ? 156 ASP B OD2 1 
ATOM   3404 N  N   . LYS B  1 157 ? -19.605 -5.399  -6.793  1.00 10.38 ? 157 LYS B N   1 
ATOM   3405 C  CA  . LYS B  1 157 ? -20.633 -4.343  -6.897  1.00 11.68 ? 157 LYS B CA  1 
ATOM   3406 C  C   . LYS B  1 157 ? -19.866 -3.009  -6.784  1.00 12.48 ? 157 LYS B C   1 
ATOM   3407 O  O   . LYS B  1 157 ? -20.404 -2.034  -7.414  1.00 14.31 ? 157 LYS B O   1 
ATOM   3408 C  CB  . LYS B  1 157 ? -21.692 -4.498  -5.839  1.00 12.03 ? 157 LYS B CB  1 
ATOM   3409 C  CG  . LYS B  1 157 ? -22.496 -5.760  -6.057  1.00 15.08 ? 157 LYS B CG  1 
ATOM   3410 C  CD  . LYS B  1 157 ? -23.466 -6.147  -4.948  1.00 20.98 ? 157 LYS B CD  1 
ATOM   3411 C  CE  . LYS B  1 157 ? -24.246 -7.434  -5.327  1.00 23.57 ? 157 LYS B CE  1 
ATOM   3412 N  NZ  . LYS B  1 157 ? -24.914 -7.929  -4.065  1.00 26.67 ? 157 LYS B NZ  1 
ATOM   3413 N  N   . ILE B  1 158 ? -18.674 -2.917  -6.170  1.00 11.58 ? 158 ILE B N   1 
ATOM   3414 C  CA  . ILE B  1 158 ? -17.870 -1.683  -6.236  1.00 11.86 ? 158 ILE B CA  1 
ATOM   3415 C  C   . ILE B  1 158 ? -16.994 -1.755  -7.466  1.00 11.67 ? 158 ILE B C   1 
ATOM   3416 O  O   . ILE B  1 158 ? -16.944 -0.767  -8.224  1.00 12.03 ? 158 ILE B O   1 
ATOM   3417 C  CB  . ILE B  1 158 ? -17.067 -1.559  -4.972  1.00 11.33 ? 158 ILE B CB  1 
ATOM   3418 C  CG1 . ILE B  1 158 ? -18.034 -1.385  -3.795  1.00 14.43 ? 158 ILE B CG1 1 
ATOM   3419 C  CG2 . ILE B  1 158 ? -16.065 -0.370  -5.030  1.00 12.71 ? 158 ILE B CG2 1 
ATOM   3420 C  CD1 . ILE B  1 158 ? -17.358 -1.588  -2.447  1.00 17.83 ? 158 ILE B CD1 1 
ATOM   3421 N  N   . PHE B  1 159 ? -16.246 -2.855  -7.712  1.00 10.39 ? 159 PHE B N   1 
ATOM   3422 C  CA  . PHE B  1 159 ? -15.195 -2.839  -8.668  1.00 10.63 ? 159 PHE B CA  1 
ATOM   3423 C  C   . PHE B  1 159 ? -15.692 -2.710  -10.080 1.00 12.22 ? 159 PHE B C   1 
ATOM   3424 O  O   . PHE B  1 159 ? -14.919 -2.225  -10.932 1.00 13.97 ? 159 PHE B O   1 
ATOM   3425 C  CB  . PHE B  1 159 ? -14.301 -4.098  -8.583  1.00 10.84 ? 159 PHE B CB  1 
ATOM   3426 C  CG  . PHE B  1 159 ? -13.636 -4.340  -7.261  1.00 11.60 ? 159 PHE B CG  1 
ATOM   3427 C  CD1 . PHE B  1 159 ? -13.300 -3.300  -6.419  1.00 13.53 ? 159 PHE B CD1 1 
ATOM   3428 C  CD2 . PHE B  1 159 ? -13.333 -5.664  -6.862  1.00 13.10 ? 159 PHE B CD2 1 
ATOM   3429 C  CE1 . PHE B  1 159 ? -12.676 -3.558  -5.207  1.00 14.53 ? 159 PHE B CE1 1 
ATOM   3430 C  CE2 . PHE B  1 159 ? -12.713 -5.912  -5.671  1.00 12.55 ? 159 PHE B CE2 1 
ATOM   3431 C  CZ  . PHE B  1 159 ? -12.318 -4.856  -4.847  1.00 13.38 ? 159 PHE B CZ  1 
ATOM   3432 N  N   . SER B  1 160 ? -16.914 -3.090  -10.306 1.00 11.97 ? 160 SER B N   1 
ATOM   3433 C  CA  . SER B  1 160 ? -17.455 -3.012  -11.683 1.00 12.54 ? 160 SER B CA  1 
ATOM   3434 C  C   . SER B  1 160 ? -17.650 -1.580  -12.074 1.00 14.57 ? 160 SER B C   1 
ATOM   3435 O  O   . SER B  1 160 ? -17.822 -1.338  -13.297 1.00 17.01 ? 160 SER B O   1 
ATOM   3436 C  CB  . SER B  1 160 ? -18.780 -3.816  -11.761 1.00 15.01 ? 160 SER B CB  1 
ATOM   3437 O  OG  . SER B  1 160 ? -19.777 -3.236  -10.990 1.00 16.32 ? 160 SER B OG  1 
ATOM   3438 N  N   . HIS B  1 161 ? -17.544 -0.572  -11.173 1.00 13.35 ? 161 HIS B N   1 
ATOM   3439 C  CA  . HIS B  1 161 ? -17.655 0.845   -11.543 1.00 15.04 ? 161 HIS B CA  1 
ATOM   3440 C  C   . HIS B  1 161 ? -16.318 1.560   -11.657 1.00 15.74 ? 161 HIS B C   1 
ATOM   3441 O  O   . HIS B  1 161 ? -16.335 2.817   -11.960 1.00 16.45 ? 161 HIS B O   1 
ATOM   3442 C  CB  . HIS B  1 161 ? -18.509 1.568   -10.534 1.00 15.49 ? 161 HIS B CB  1 
ATOM   3443 C  CG  . HIS B  1 161 ? -19.885 1.072   -10.495 1.00 16.53 ? 161 HIS B CG  1 
ATOM   3444 N  ND1 . HIS B  1 161 ? -20.856 1.609   -11.325 1.00 17.73 ? 161 HIS B ND1 1 
ATOM   3445 C  CD2 . HIS B  1 161 ? -20.487 0.029   -9.803  1.00 17.03 ? 161 HIS B CD2 1 
ATOM   3446 C  CE1 . HIS B  1 161 ? -22.021 0.933   -11.124 1.00 17.26 ? 161 HIS B CE1 1 
ATOM   3447 N  NE2 . HIS B  1 161 ? -21.792 -0.033  -10.182 1.00 18.72 ? 161 HIS B NE2 1 
ATOM   3448 N  N   . LEU B  1 162 ? -15.183 0.847   -11.538 1.00 15.98 ? 162 LEU B N   1 
ATOM   3449 C  CA  . LEU B  1 162 ? -13.865 1.529   -11.416 1.00 18.20 ? 162 LEU B CA  1 
ATOM   3450 C  C   . LEU B  1 162 ? -13.469 2.227   -12.678 1.00 21.42 ? 162 LEU B C   1 
ATOM   3451 O  O   . LEU B  1 162 ? -12.844 3.294   -12.585 1.00 20.01 ? 162 LEU B O   1 
ATOM   3452 C  CB  . LEU B  1 162 ? -12.786 0.539   -11.102 1.00 19.92 ? 162 LEU B CB  1 
ATOM   3453 C  CG  . LEU B  1 162 ? -12.909 -0.029  -9.668  1.00 19.60 ? 162 LEU B CG  1 
ATOM   3454 C  CD1 . LEU B  1 162 ? -11.878 -1.101  -9.569  1.00 22.09 ? 162 LEU B CD1 1 
ATOM   3455 C  CD2 . LEU B  1 162 ? -12.978 1.020   -8.555  1.00 22.36 ? 162 LEU B CD2 1 
ATOM   3456 N  N   . GLN B  1 163 ? -13.914 1.766   -13.846 1.00 18.51 ? 163 GLN B N   1 
ATOM   3457 C  CA  . GLN B  1 163 ? -13.565 2.464   -15.073 1.00 19.15 ? 163 GLN B CA  1 
ATOM   3458 C  C   . GLN B  1 163 ? -14.296 3.790   -15.255 1.00 20.77 ? 163 GLN B C   1 
ATOM   3459 O  O   . GLN B  1 163 ? -14.060 4.522   -16.263 1.00 22.82 ? 163 GLN B O   1 
ATOM   3460 C  CB  . GLN B  1 163 ? -13.719 1.552   -16.318 1.00 24.22 ? 163 GLN B CB  1 
ATOM   3461 C  CG  . GLN B  1 163 ? -12.772 0.317   -16.323 1.00 28.12 ? 163 GLN B CG  1 
ATOM   3462 C  CD  . GLN B  1 163 ? -11.233 0.584   -16.274 1.00 32.05 ? 163 GLN B CD  1 
ATOM   3463 O  OE1 . GLN B  1 163 ? -10.747 1.608   -16.737 1.00 30.16 ? 163 GLN B OE1 1 
ATOM   3464 N  NE2 . GLN B  1 163 ? -10.474 -0.366  -15.689 1.00 29.08 ? 163 GLN B NE2 1 
ATOM   3465 N  N   . HIS B  1 164 ? -15.145 4.156   -14.315 1.00 19.33 ? 164 HIS B N   1 
ATOM   3466 C  CA  . HIS B  1 164 ? -15.960 5.359   -14.351 1.00 17.85 ? 164 HIS B CA  1 
ATOM   3467 C  C   . HIS B  1 164 ? -15.550 6.444   -13.330 1.00 15.88 ? 164 HIS B C   1 
ATOM   3468 O  O   . HIS B  1 164 ? -16.121 7.522   -13.193 1.00 16.83 ? 164 HIS B O   1 
ATOM   3469 C  CB  . HIS B  1 164 ? -17.437 4.933   -14.354 1.00 21.05 ? 164 HIS B CB  1 
ATOM   3470 C  CG  . HIS B  1 164 ? -17.682 3.805   -15.325 1.00 22.37 ? 164 HIS B CG  1 
ATOM   3471 N  ND1 . HIS B  1 164 ? -17.318 3.914   -16.655 1.00 26.01 ? 164 HIS B ND1 1 
ATOM   3472 C  CD2 . HIS B  1 164 ? -18.158 2.510   -15.137 1.00 28.19 ? 164 HIS B CD2 1 
ATOM   3473 C  CE1 . HIS B  1 164 ? -17.568 2.722   -17.264 1.00 26.51 ? 164 HIS B CE1 1 
ATOM   3474 N  NE2 . HIS B  1 164 ? -18.122 1.885   -16.355 1.00 30.25 ? 164 HIS B NE2 1 
ATOM   3475 N  N   . VAL B  1 165 ? -14.543 6.060   -12.507 1.00 14.21 ? 165 VAL B N   1 
ATOM   3476 C  CA  . VAL B  1 165 ? -13.991 6.998   -11.532 1.00 13.52 ? 165 VAL B CA  1 
ATOM   3477 C  C   . VAL B  1 165 ? -12.465 6.913   -11.689 1.00 12.62 ? 165 VAL B C   1 
ATOM   3478 O  O   . VAL B  1 165 ? -11.695 6.989   -10.713 1.00 13.30 ? 165 VAL B O   1 
ATOM   3479 C  CB  . VAL B  1 165 ? -14.462 6.730   -10.068 1.00 13.43 ? 165 VAL B CB  1 
ATOM   3480 C  CG1 . VAL B  1 165 ? -15.919 7.125   -9.924  1.00 15.27 ? 165 VAL B CG1 1 
ATOM   3481 C  CG2 . VAL B  1 165 ? -14.249 5.274   -9.642  1.00 14.54 ? 165 VAL B CG2 1 
ATOM   3482 N  N   . LYS B  1 166 ? -11.962 6.764   -12.928 1.00 11.43 ? 166 LYS B N   1 
ATOM   3483 C  CA  . LYS B  1 166 ? -10.555 6.590   -13.156 1.00 12.66 ? 166 LYS B CA  1 
ATOM   3484 C  C   . LYS B  1 166 ? -9.680  7.724   -12.676 1.00 11.98 ? 166 LYS B C   1 
ATOM   3485 O  O   . LYS B  1 166 ? -8.577  7.516   -12.238 1.00 12.23 ? 166 LYS B O   1 
ATOM   3486 C  CB  . LYS B  1 166 ? -10.253 6.423   -14.673 1.00 16.31 ? 166 LYS B CB  1 
ATOM   3487 C  CG  . LYS B  1 166 ? -10.805 5.107   -15.215 1.00 20.18 ? 166 LYS B CG  1 
ATOM   3488 C  CD  . LYS B  1 166 ? -10.405 4.952   -16.707 1.00 20.99 ? 166 LYS B CD  1 
ATOM   3489 C  CE  . LYS B  1 166 ? -8.904  4.718   -16.822 1.00 21.99 ? 166 LYS B CE  1 
ATOM   3490 N  NZ  . LYS B  1 166 ? -8.608  3.327   -16.266 1.00 18.93 ? 166 LYS B NZ  1 
ATOM   3491 N  N   . TYR B  1 167 ? -10.207 8.973   -12.720 1.00 11.70 ? 167 TYR B N   1 
ATOM   3492 C  CA  . TYR B  1 167 ? -9.370  10.088  -12.363 1.00 11.62 ? 167 TYR B CA  1 
ATOM   3493 C  C   . TYR B  1 167 ? -9.838  10.871  -11.155 1.00 10.93 ? 167 TYR B C   1 
ATOM   3494 O  O   . TYR B  1 167 ? -11.064 10.849  -10.843 1.00 11.15 ? 167 TYR B O   1 
ATOM   3495 C  CB  . TYR B  1 167 ? -9.310  11.041  -13.653 1.00 14.49 ? 167 TYR B CB  1 
ATOM   3496 C  CG  . TYR B  1 167 ? -9.025  10.279  -14.952 1.00 15.35 ? 167 TYR B CG  1 
ATOM   3497 C  CD1 . TYR B  1 167 ? -7.740  9.846   -15.222 1.00 19.00 ? 167 TYR B CD1 1 
ATOM   3498 C  CD2 . TYR B  1 167 ? -10.028 9.972   -15.887 1.00 16.33 ? 167 TYR B CD2 1 
ATOM   3499 C  CE1 . TYR B  1 167 ? -7.442  9.142   -16.365 1.00 14.89 ? 167 TYR B CE1 1 
ATOM   3500 C  CE2 . TYR B  1 167 ? -9.729  9.260   -17.048 1.00 17.77 ? 167 TYR B CE2 1 
ATOM   3501 C  CZ  . TYR B  1 167 ? -8.432  8.849   -17.280 1.00 18.48 ? 167 TYR B CZ  1 
ATOM   3502 O  OH  . TYR B  1 167 ? -8.098  8.143   -18.419 1.00 22.92 ? 167 TYR B OH  1 
ATOM   3503 N  N   . LYS B  1 168 ? -8.871  11.593  -10.552 1.00 11.42 ? 168 LYS B N   1 
ATOM   3504 C  CA  . LYS B  1 168 ? -9.185  12.368  -9.357  1.00 13.80 ? 168 LYS B CA  1 
ATOM   3505 C  C   . LYS B  1 168 ? -10.339 13.279  -9.620  1.00 14.59 ? 168 LYS B C   1 
ATOM   3506 O  O   . LYS B  1 168 ? -10.474 13.985  -10.659 1.00 15.06 ? 168 LYS B O   1 
ATOM   3507 C  CB  . LYS B  1 168 ? -7.989  13.302  -9.054  1.00 15.35 ? 168 LYS B CB  1 
ATOM   3508 C  CG  . LYS B  1 168 ? -8.175  13.977  -7.702  1.00 15.84 ? 168 LYS B CG  1 
ATOM   3509 C  CD  . LYS B  1 168 ? -6.847  14.557  -7.228  1.00 21.82 ? 168 LYS B CD  1 
ATOM   3510 C  CE  . LYS B  1 168 ? -7.053  15.207  -5.852  1.00 26.95 ? 168 LYS B CE  1 
ATOM   3511 N  NZ  . LYS B  1 168 ? -5.800  15.709  -5.142  1.00 30.96 ? 168 LYS B NZ  1 
ATOM   3512 N  N   . GLY B  1 169 ? -11.256 13.240  -8.627  1.00 14.55 ? 169 GLY B N   1 
ATOM   3513 C  CA  . GLY B  1 169 ? -12.466 14.040  -8.634  1.00 16.79 ? 169 GLY B CA  1 
ATOM   3514 C  C   . GLY B  1 169 ? -13.692 13.484  -9.343  1.00 17.89 ? 169 GLY B C   1 
ATOM   3515 O  O   . GLY B  1 169 ? -14.818 14.019  -9.291  1.00 19.18 ? 169 GLY B O   1 
ATOM   3516 N  N   . GLN B  1 170 ? -13.510 12.443  -10.136 1.00 13.86 ? 170 GLN B N   1 
ATOM   3517 C  CA  . GLN B  1 170 ? -14.623 11.856  -10.861 1.00 15.17 ? 170 GLN B CA  1 
ATOM   3518 C  C   . GLN B  1 170 ? -15.548 11.083  -9.859  1.00 15.13 ? 170 GLN B C   1 
ATOM   3519 O  O   . GLN B  1 170 ? -15.066 10.542  -8.833  1.00 15.36 ? 170 GLN B O   1 
ATOM   3520 C  CB  . GLN B  1 170 ? -14.116 10.910  -11.938 1.00 13.61 ? 170 GLN B CB  1 
ATOM   3521 C  CG  . GLN B  1 170 ? -13.404 11.761  -13.040 1.00 15.00 ? 170 GLN B CG  1 
ATOM   3522 C  CD  . GLN B  1 170 ? -13.103 10.919  -14.216 1.00 18.24 ? 170 GLN B CD  1 
ATOM   3523 O  OE1 . GLN B  1 170 ? -12.722 9.719   -14.174 1.00 17.56 ? 170 GLN B OE1 1 
ATOM   3524 N  NE2 . GLN B  1 170 ? -13.209 11.613  -15.377 1.00 21.79 ? 170 GLN B NE2 1 
ATOM   3525 N  N   . GLU B  1 171 ? -16.827 11.092  -10.185 1.00 15.76 ? 171 GLU B N   1 
ATOM   3526 C  CA  . GLU B  1 171 ? -17.950 10.543  -9.376  1.00 16.65 ? 171 GLU B CA  1 
ATOM   3527 C  C   . GLU B  1 171 ? -18.840 9.635   -10.201 1.00 18.52 ? 171 GLU B C   1 
ATOM   3528 O  O   . GLU B  1 171 ? -19.039 9.830   -11.433 1.00 19.01 ? 171 GLU B O   1 
ATOM   3529 C  CB  . GLU B  1 171 ? -18.799 11.711  -8.825  1.00 20.56 ? 171 GLU B CB  1 
ATOM   3530 C  CG  . GLU B  1 171 ? -18.010 12.483  -7.742  1.00 21.68 ? 171 GLU B CG  1 
ATOM   3531 C  CD  . GLU B  1 171 ? -18.685 13.719  -7.096  1.00 28.85 ? 171 GLU B CD  1 
ATOM   3532 O  OE1 . GLU B  1 171 ? -19.767 14.126  -7.528  1.00 34.37 ? 171 GLU B OE1 1 
ATOM   3533 O  OE2 . GLU B  1 171 ? -18.108 14.255  -6.113  1.00 33.05 ? 171 GLU B OE2 1 
ATOM   3534 N  N   . ALA B  1 172 ? -19.323 8.544   -9.620  1.00 15.69 ? 172 ALA B N   1 
ATOM   3535 C  CA  . ALA B  1 172 ? -20.179 7.559   -10.294 1.00 15.26 ? 172 ALA B CA  1 
ATOM   3536 C  C   . ALA B  1 172 ? -21.201 7.172   -9.218  1.00 16.29 ? 172 ALA B C   1 
ATOM   3537 O  O   . ALA B  1 172 ? -20.998 7.442   -8.008  1.00 17.08 ? 172 ALA B O   1 
ATOM   3538 C  CB  . ALA B  1 172 ? -19.467 6.359   -10.889 1.00 14.73 ? 172 ALA B CB  1 
ATOM   3539 N  N   . PHE B  1 173 ? -22.313 6.636   -9.637  1.00 16.09 ? 173 PHE B N   1 
ATOM   3540 C  CA  . PHE B  1 173 ? -23.328 6.078   -8.719  1.00 12.99 ? 173 PHE B CA  1 
ATOM   3541 C  C   . PHE B  1 173 ? -23.334 4.576   -8.692  1.00 15.14 ? 173 PHE B C   1 
ATOM   3542 O  O   . PHE B  1 173 ? -23.261 3.928   -9.755  1.00 19.73 ? 173 PHE B O   1 
ATOM   3543 C  CB  . PHE B  1 173 ? -24.713 6.615   -9.107  1.00 18.51 ? 173 PHE B CB  1 
ATOM   3544 C  CG  . PHE B  1 173 ? -24.976 7.998   -8.551  1.00 20.27 ? 173 PHE B CG  1 
ATOM   3545 C  CD1 . PHE B  1 173 ? -25.064 8.203   -7.183  1.00 23.77 ? 173 PHE B CD1 1 
ATOM   3546 C  CD2 . PHE B  1 173 ? -25.209 9.064   -9.409  1.00 26.01 ? 173 PHE B CD2 1 
ATOM   3547 C  CE1 . PHE B  1 173 ? -25.294 9.450   -6.608  1.00 26.41 ? 173 PHE B CE1 1 
ATOM   3548 C  CE2 . PHE B  1 173 ? -25.476 10.334  -8.863  1.00 26.59 ? 173 PHE B CE2 1 
ATOM   3549 C  CZ  . PHE B  1 173 ? -25.515 10.542  -7.471  1.00 30.31 ? 173 PHE B CZ  1 
ATOM   3550 N  N   . VAL B  1 174 ? -23.415 4.036   -7.491  1.00 12.91 ? 174 VAL B N   1 
ATOM   3551 C  CA  . VAL B  1 174 ? -23.383 2.591   -7.310  1.00 13.39 ? 174 VAL B CA  1 
ATOM   3552 C  C   . VAL B  1 174 ? -24.759 2.232   -6.694  1.00 13.07 ? 174 VAL B C   1 
ATOM   3553 O  O   . VAL B  1 174 ? -25.108 2.800   -5.665  1.00 13.94 ? 174 VAL B O   1 
ATOM   3554 C  CB  . VAL B  1 174 ? -22.260 2.180   -6.325  1.00 12.97 ? 174 VAL B CB  1 
ATOM   3555 C  CG1 . VAL B  1 174 ? -22.358 0.642   -6.052  1.00 14.81 ? 174 VAL B CG1 1 
ATOM   3556 C  CG2 . VAL B  1 174 ? -20.879 2.485   -6.971  1.00 15.94 ? 174 VAL B CG2 1 
ATOM   3557 N  N   . PRO B  1 175 ? -25.523 1.299   -7.296  1.00 11.42 ? 175 PRO B N   1 
ATOM   3558 C  CA  . PRO B  1 175 ? -26.777 0.911   -6.593  1.00 11.29 ? 175 PRO B CA  1 
ATOM   3559 C  C   . PRO B  1 175 ? -26.444 0.319   -5.189  1.00 11.27 ? 175 PRO B C   1 
ATOM   3560 O  O   . PRO B  1 175 ? -25.466 -0.404  -5.002  1.00 11.44 ? 175 PRO B O   1 
ATOM   3561 C  CB  . PRO B  1 175 ? -27.359 -0.156  -7.496  1.00 11.81 ? 175 PRO B CB  1 
ATOM   3562 C  CG  . PRO B  1 175 ? -26.754 0.107   -8.835  1.00 13.24 ? 175 PRO B CG  1 
ATOM   3563 C  CD  . PRO B  1 175 ? -25.339 0.654   -8.592  1.00 12.68 ? 175 PRO B CD  1 
ATOM   3564 N  N   . GLY B  1 176 ? -27.367 0.490   -4.260  1.00 12.37 ? 176 GLY B N   1 
ATOM   3565 C  CA  . GLY B  1 176 ? -27.195 -0.064  -2.901  1.00 11.44 ? 176 GLY B CA  1 
ATOM   3566 C  C   . GLY B  1 176 ? -27.108 -1.585  -3.006  1.00 12.75 ? 176 GLY B C   1 
ATOM   3567 O  O   . GLY B  1 176 ? -27.666 -2.255  -3.861  1.00 12.12 ? 176 GLY B O   1 
ATOM   3568 N  N   . PHE B  1 177 ? -26.322 -2.083  -2.080  1.00 11.70 ? 177 PHE B N   1 
ATOM   3569 C  CA  . PHE B  1 177 ? -26.226 -3.518  -1.819  1.00 12.12 ? 177 PHE B CA  1 
ATOM   3570 C  C   . PHE B  1 177 ? -25.945 -3.660  -0.328  1.00 11.10 ? 177 PHE B C   1 
ATOM   3571 O  O   . PHE B  1 177 ? -25.773 -2.744  0.420   1.00 11.90 ? 177 PHE B O   1 
ATOM   3572 C  CB  . PHE B  1 177 ? -25.149 -4.227  -2.713  1.00 13.54 ? 177 PHE B CB  1 
ATOM   3573 C  CG  . PHE B  1 177 ? -23.770 -3.760  -2.443  1.00 12.29 ? 177 PHE B CG  1 
ATOM   3574 C  CD1 . PHE B  1 177 ? -23.309 -2.588  -2.965  1.00 12.72 ? 177 PHE B CD1 1 
ATOM   3575 C  CD2 . PHE B  1 177 ? -22.924 -4.569  -1.659  1.00 14.53 ? 177 PHE B CD2 1 
ATOM   3576 C  CE1 . PHE B  1 177 ? -22.007 -2.120  -2.730  1.00 14.27 ? 177 PHE B CE1 1 
ATOM   3577 C  CE2 . PHE B  1 177 ? -21.652 -4.151  -1.438  1.00 13.54 ? 177 PHE B CE2 1 
ATOM   3578 C  CZ  . PHE B  1 177 ? -21.153 -2.955  -1.964  1.00 13.86 ? 177 PHE B CZ  1 
ATOM   3579 N  N   . ASN B  1 178 ? -25.934 -4.935  0.094   1.00 12.25 ? 178 ASN B N   1 
ATOM   3580 C  CA  . ASN B  1 178 ? -25.751 -5.237  1.496   1.00 11.91 ? 178 ASN B CA  1 
ATOM   3581 C  C   . ASN B  1 178 ? -24.249 -5.199  1.834   1.00 10.50 ? 178 ASN B C   1 
ATOM   3582 O  O   . ASN B  1 178 ? -23.510 -6.076  1.510   1.00 12.39 ? 178 ASN B O   1 
ATOM   3583 C  CB  . ASN B  1 178 ? -26.391 -6.605  1.862   1.00 13.62 ? 178 ASN B CB  1 
ATOM   3584 C  CG  . ASN B  1 178 ? -26.265 -6.895  3.297   1.00 14.96 ? 178 ASN B CG  1 
ATOM   3585 O  OD1 . ASN B  1 178 ? -25.860 -6.094  4.131   1.00 13.76 ? 178 ASN B OD1 1 
ATOM   3586 N  ND2 . ASN B  1 178 ? -26.626 -8.200  3.639   1.00 18.42 ? 178 ASN B ND2 1 
ATOM   3587 N  N   . ILE B  1 179 ? -23.886 -4.115  2.497   1.00 9.82  ? 179 ILE B N   1 
ATOM   3588 C  CA  . ILE B  1 179 ? -22.486 -3.898  2.896   1.00 10.34 ? 179 ILE B CA  1 
ATOM   3589 C  C   . ILE B  1 179 ? -21.977 -4.964  3.813   1.00 10.39 ? 179 ILE B C   1 
ATOM   3590 O  O   . ILE B  1 179 ? -20.745 -5.204  3.857   1.00 10.98 ? 179 ILE B O   1 
ATOM   3591 C  CB  . ILE B  1 179 ? -22.318 -2.499  3.513   1.00 9.44  ? 179 ILE B CB  1 
ATOM   3592 C  CG1 . ILE B  1 179 ? -22.817 -1.399  2.560   1.00 11.21 ? 179 ILE B CG1 1 
ATOM   3593 C  CG2 . ILE B  1 179 ? -20.848 -2.209  3.887   1.00 10.74 ? 179 ILE B CG2 1 
ATOM   3594 C  CD1 . ILE B  1 179 ? -22.237 -1.376  1.129   1.00 12.44 ? 179 ILE B CD1 1 
ATOM   3595 N  N   . GLU B  1 180 ? -22.882 -5.618  4.570   1.00 10.93 ? 180 GLU B N   1 
ATOM   3596 C  CA  . GLU B  1 180 ? -22.405 -6.675  5.414   1.00 13.05 ? 180 GLU B CA  1 
ATOM   3597 C  C   . GLU B  1 180 ? -21.834 -7.797  4.564   1.00 10.70 ? 180 GLU B C   1 
ATOM   3598 O  O   . GLU B  1 180 ? -21.026 -8.613  5.150   1.00 12.23 ? 180 GLU B O   1 
ATOM   3599 C  CB  . GLU B  1 180 ? -23.550 -7.218  6.259   1.00 15.24 ? 180 GLU B CB  1 
ATOM   3600 C  CG  . GLU B  1 180 ? -23.032 -8.031  7.501   1.00 20.85 ? 180 GLU B CG  1 
ATOM   3601 C  CD  . GLU B  1 180 ? -24.082 -8.229  8.581   1.00 25.88 ? 180 GLU B CD  1 
ATOM   3602 O  OE1 . GLU B  1 180 ? -25.238 -7.749  8.391   1.00 23.87 ? 180 GLU B OE1 1 
ATOM   3603 O  OE2 . GLU B  1 180 ? -23.695 -8.857  9.585   1.00 27.89 ? 180 GLU B OE2 1 
ATOM   3604 N  N   . GLU B  1 181 ? -22.149 -7.957  3.257   1.00 10.93 ? 181 GLU B N   1 
ATOM   3605 C  CA  . GLU B  1 181 ? -21.550 -8.983  2.441   1.00 11.01 ? 181 GLU B CA  1 
ATOM   3606 C  C   . GLU B  1 181 ? -20.073 -8.683  2.174   1.00 11.78 ? 181 GLU B C   1 
ATOM   3607 O  O   . GLU B  1 181 ? -19.362 -9.615  1.724   1.00 13.10 ? 181 GLU B O   1 
ATOM   3608 C  CB  . GLU B  1 181 ? -22.216 -9.024  1.079   1.00 13.47 ? 181 GLU B CB  1 
ATOM   3609 C  CG  . GLU B  1 181 ? -23.649 -9.467  1.084   1.00 16.89 ? 181 GLU B CG  1 
ATOM   3610 C  CD  . GLU B  1 181 ? -24.305 -9.179  -0.266  1.00 22.95 ? 181 GLU B CD  1 
ATOM   3611 O  OE1 . GLU B  1 181 ? -23.649 -8.741  -1.269  1.00 23.45 ? 181 GLU B OE1 1 
ATOM   3612 O  OE2 . GLU B  1 181 ? -25.576 -9.324  -0.375  1.00 24.63 ? 181 GLU B OE2 1 
ATOM   3613 N  N   . LEU B  1 182 ? -19.553 -7.496  2.573   1.00 9.89  ? 182 LEU B N   1 
ATOM   3614 C  CA  . LEU B  1 182 ? -18.098 -7.264  2.416   1.00 9.24  ? 182 LEU B CA  1 
ATOM   3615 C  C   . LEU B  1 182 ? -17.347 -7.730  3.647   1.00 8.95  ? 182 LEU B C   1 
ATOM   3616 O  O   . LEU B  1 182 ? -16.117 -7.726  3.649   1.00 9.91  ? 182 LEU B O   1 
ATOM   3617 C  CB  . LEU B  1 182 ? -17.891 -5.706  2.246   1.00 9.96  ? 182 LEU B CB  1 
ATOM   3618 C  CG  . LEU B  1 182 ? -18.600 -5.069  1.034   1.00 8.55  ? 182 LEU B CG  1 
ATOM   3619 C  CD1 . LEU B  1 182 ? -18.251 -3.575  1.006   1.00 9.43  ? 182 LEU B CD1 1 
ATOM   3620 C  CD2 . LEU B  1 182 ? -18.238 -5.749  -0.253  1.00 10.18 ? 182 LEU B CD2 1 
ATOM   3621 N  N   . LEU B  1 183 ? -18.045 -8.082  4.718   1.00 10.92 ? 183 LEU B N   1 
ATOM   3622 C  CA  . LEU B  1 183 ? -17.370 -8.487  6.008   1.00 11.29 ? 183 LEU B CA  1 
ATOM   3623 C  C   . LEU B  1 183 ? -17.082 -9.999  5.958   1.00 10.05 ? 183 LEU B C   1 
ATOM   3624 O  O   . LEU B  1 183 ? -17.744 -10.747 5.236   1.00 12.27 ? 183 LEU B O   1 
ATOM   3625 C  CB  . LEU B  1 183 ? -18.293 -8.204  7.215   1.00 12.26 ? 183 LEU B CB  1 
ATOM   3626 C  CG  . LEU B  1 183 ? -18.705 -6.722  7.302   1.00 12.72 ? 183 LEU B CG  1 
ATOM   3627 C  CD1 . LEU B  1 183 ? -19.637 -6.469  8.514   1.00 16.76 ? 183 LEU B CD1 1 
ATOM   3628 C  CD2 . LEU B  1 183 ? -17.533 -5.790  7.313   1.00 14.81 ? 183 LEU B CD2 1 
ATOM   3629 N  N   . PRO B  1 184 ? -16.059 -10.405 6.715   1.00 10.73 ? 184 PRO B N   1 
ATOM   3630 C  CA  . PRO B  1 184 ? -15.642 -11.825 6.721   1.00 12.30 ? 184 PRO B CA  1 
ATOM   3631 C  C   . PRO B  1 184 ? -16.530 -12.613 7.653   1.00 14.13 ? 184 PRO B C   1 
ATOM   3632 O  O   . PRO B  1 184 ? -17.484 -12.087 8.236   1.00 15.22 ? 184 PRO B O   1 
ATOM   3633 C  CB  . PRO B  1 184 ? -14.217 -11.723 7.302   1.00 13.78 ? 184 PRO B CB  1 
ATOM   3634 C  CG  . PRO B  1 184 ? -14.257 -10.516 8.215   1.00 12.69 ? 184 PRO B CG  1 
ATOM   3635 C  CD  . PRO B  1 184 ? -15.189 -9.578  7.565   1.00 10.45 ? 184 PRO B CD  1 
ATOM   3636 N  N   A GLU B  1 185 ? -16.178 -13.915 7.710   0.50 15.81 ? 185 GLU B N   1 
ATOM   3637 N  N   B GLU B  1 185 ? -16.160 -13.905 7.738   0.50 15.85 ? 185 GLU B N   1 
ATOM   3638 C  CA  A GLU B  1 185 ? -16.745 -14.870 8.666   0.50 16.63 ? 185 GLU B CA  1 
ATOM   3639 C  CA  B GLU B  1 185 ? -16.801 -14.823 8.669   0.50 16.56 ? 185 GLU B CA  1 
ATOM   3640 C  C   A GLU B  1 185 ? -16.336 -14.514 10.075  0.50 15.21 ? 185 GLU B C   1 
ATOM   3641 C  C   B GLU B  1 185 ? -16.349 -14.508 10.080  0.50 15.36 ? 185 GLU B C   1 
ATOM   3642 O  O   A GLU B  1 185 ? -15.199 -13.988 10.311  0.50 16.60 ? 185 GLU B O   1 
ATOM   3643 O  O   B GLU B  1 185 ? -15.236 -13.949 10.323  0.50 17.09 ? 185 GLU B O   1 
ATOM   3644 C  CB  A GLU B  1 185 ? -16.183 -16.258 8.377   0.50 18.94 ? 185 GLU B CB  1 
ATOM   3645 C  CB  B GLU B  1 185 ? -16.476 -16.270 8.295   0.50 18.65 ? 185 GLU B CB  1 
ATOM   3646 C  CG  A GLU B  1 185 ? -16.584 -16.797 7.019   0.50 23.08 ? 185 GLU B CG  1 
ATOM   3647 C  CG  B GLU B  1 185 ? -17.073 -16.635 6.938   0.50 22.19 ? 185 GLU B CG  1 
ATOM   3648 C  CD  A GLU B  1 185 ? -16.410 -18.304 6.933   0.50 27.62 ? 185 GLU B CD  1 
ATOM   3649 C  CD  B GLU B  1 185 ? -18.602 -16.569 6.906   0.50 26.53 ? 185 GLU B CD  1 
ATOM   3650 O  OE1 A GLU B  1 185 ? -15.256 -18.757 6.968   0.50 31.82 ? 185 GLU B OE1 1 
ATOM   3651 O  OE1 B GLU B  1 185 ? -19.273 -17.494 7.399   0.50 30.96 ? 185 GLU B OE1 1 
ATOM   3652 O  OE2 A GLU B  1 185 ? -17.440 -19.016 6.863   0.50 30.20 ? 185 GLU B OE2 1 
ATOM   3653 O  OE2 B GLU B  1 185 ? -19.153 -15.584 6.388   0.50 28.77 ? 185 GLU B OE2 1 
ATOM   3654 N  N   . ARG B  1 186 ? -17.282 -14.702 10.993  1.00 14.52 ? 186 ARG B N   1 
ATOM   3655 C  CA  . ARG B  1 186 ? -17.022 -14.668 12.428  1.00 15.22 ? 186 ARG B CA  1 
ATOM   3656 C  C   . ARG B  1 186 ? -16.533 -13.268 12.825  1.00 12.99 ? 186 ARG B C   1 
ATOM   3657 O  O   . ARG B  1 186 ? -15.449 -13.018 13.420  1.00 15.18 ? 186 ARG B O   1 
ATOM   3658 C  CB  . ARG B  1 186 ? -16.030 -15.731 12.883  1.00 19.67 ? 186 ARG B CB  1 
ATOM   3659 C  CG  . ARG B  1 186 ? -16.650 -17.134 12.753  1.00 21.96 ? 186 ARG B CG  1 
ATOM   3660 C  CD  . ARG B  1 186 ? -15.651 -18.224 13.279  1.00 25.84 ? 186 ARG B CD  1 
ATOM   3661 N  NE  . ARG B  1 186 ? -14.468 -18.405 12.429  1.00 29.32 ? 186 ARG B NE  1 
ATOM   3662 C  CZ  . ARG B  1 186 ? -14.534 -18.893 11.184  1.00 38.05 ? 186 ARG B CZ  1 
ATOM   3663 N  NH1 . ARG B  1 186 ? -15.723 -19.208 10.645  1.00 41.03 ? 186 ARG B NH1 1 
ATOM   3664 N  NH2 . ARG B  1 186 ? -13.432 -19.037 10.457  1.00 42.12 ? 186 ARG B NH2 1 
ATOM   3665 N  N   . THR B  1 187 ? -17.364 -12.322 12.452  1.00 12.34 ? 187 THR B N   1 
ATOM   3666 C  CA  . THR B  1 187 ? -17.094 -10.976 12.839  1.00 11.14 ? 187 THR B CA  1 
ATOM   3667 C  C   . THR B  1 187 ? -16.946 -10.728 14.323  1.00 11.86 ? 187 THR B C   1 
ATOM   3668 O  O   . THR B  1 187 ? -16.428 -9.695  14.768  1.00 11.83 ? 187 THR B O   1 
ATOM   3669 C  CB  . THR B  1 187 ? -18.081 -9.969  12.231  1.00 11.69 ? 187 THR B CB  1 
ATOM   3670 O  OG1 . THR B  1 187 ? -19.427 -10.372 12.601  1.00 14.39 ? 187 THR B OG1 1 
ATOM   3671 C  CG2 . THR B  1 187 ? -17.923 -9.874  10.686  1.00 13.10 ? 187 THR B CG2 1 
ATOM   3672 N  N   . ALA B  1 188 ? -17.417 -11.656 15.169  1.00 11.93 ? 188 ALA B N   1 
ATOM   3673 C  CA  . ALA B  1 188 ? -17.183 -11.521 16.556  1.00 11.21 ? 188 ALA B CA  1 
ATOM   3674 C  C   . ALA B  1 188 ? -15.724 -11.635 16.968  1.00 10.23 ? 188 ALA B C   1 
ATOM   3675 O  O   . ALA B  1 188 ? -15.438 -11.167 18.050  1.00 12.16 ? 188 ALA B O   1 
ATOM   3676 C  CB  . ALA B  1 188 ? -18.040 -12.538 17.354  1.00 13.43 ? 188 ALA B CB  1 
ATOM   3677 N  N   . GLU B  1 189 ? -14.892 -12.134 16.075  1.00 12.01 ? 189 GLU B N   1 
ATOM   3678 C  CA  . GLU B  1 189 ? -13.442 -12.259 16.364  1.00 11.22 ? 189 GLU B CA  1 
ATOM   3679 C  C   . GLU B  1 189 ? -12.691 -11.075 15.714  1.00 9.69  ? 189 GLU B C   1 
ATOM   3680 O  O   . GLU B  1 189 ? -12.667 -11.004 14.411  1.00 10.07 ? 189 GLU B O   1 
ATOM   3681 C  CB  . GLU B  1 189 ? -12.932 -13.566 15.814  1.00 12.59 ? 189 GLU B CB  1 
ATOM   3682 C  CG  . GLU B  1 189 ? -13.690 -14.731 16.501  1.00 15.20 ? 189 GLU B CG  1 
ATOM   3683 C  CD  . GLU B  1 189 ? -13.247 -16.080 16.058  1.00 21.59 ? 189 GLU B CD  1 
ATOM   3684 O  OE1 . GLU B  1 189 ? -12.071 -16.322 15.737  1.00 21.69 ? 189 GLU B OE1 1 
ATOM   3685 O  OE2 . GLU B  1 189 ? -14.117 -17.021 16.123  1.00 27.11 ? 189 GLU B OE2 1 
ATOM   3686 N  N   . TYR B  1 190 ? -12.166 -10.208 16.536  1.00 9.84  ? 190 TYR B N   1 
ATOM   3687 C  CA  . TYR B  1 190 ? -11.487 -9.007  16.014  1.00 9.14  ? 190 TYR B CA  1 
ATOM   3688 C  C   . TYR B  1 190 ? -10.414 -8.564  16.920  1.00 9.75  ? 190 TYR B C   1 
ATOM   3689 O  O   . TYR B  1 190 ? -10.336 -8.942  18.094  1.00 9.82  ? 190 TYR B O   1 
ATOM   3690 C  CB  . TYR B  1 190 ? -12.498 -7.878  15.709  1.00 8.86  ? 190 TYR B CB  1 
ATOM   3691 C  CG  . TYR B  1 190 ? -13.323 -7.480  16.970  1.00 8.21  ? 190 TYR B CG  1 
ATOM   3692 C  CD1 . TYR B  1 190 ? -12.822 -6.615  17.925  1.00 8.33  ? 190 TYR B CD1 1 
ATOM   3693 C  CD2 . TYR B  1 190 ? -14.584 -7.996  17.171  1.00 9.24  ? 190 TYR B CD2 1 
ATOM   3694 C  CE1 . TYR B  1 190 ? -13.608 -6.205  19.009  1.00 9.15  ? 190 TYR B CE1 1 
ATOM   3695 C  CE2 . TYR B  1 190 ? -15.373 -7.638  18.297  1.00 10.00 ? 190 TYR B CE2 1 
ATOM   3696 C  CZ  . TYR B  1 190 ? -14.874 -6.729  19.187  1.00 10.03 ? 190 TYR B CZ  1 
ATOM   3697 O  OH  . TYR B  1 190 ? -15.626 -6.266  20.299  1.00 11.53 ? 190 TYR B OH  1 
ATOM   3698 N  N   . TYR B  1 191 ? -9.532  -7.697  16.408  1.00 9.33  ? 191 TYR B N   1 
ATOM   3699 C  CA  . TYR B  1 191 ? -8.525  -6.941  17.085  1.00 8.93  ? 191 TYR B CA  1 
ATOM   3700 C  C   . TYR B  1 191 ? -9.035  -5.533  17.276  1.00 9.06  ? 191 TYR B C   1 
ATOM   3701 O  O   . TYR B  1 191 ? -9.668  -4.943  16.380  1.00 9.86  ? 191 TYR B O   1 
ATOM   3702 C  CB  . TYR B  1 191 ? -7.206  -6.854  16.259  1.00 9.54  ? 191 TYR B CB  1 
ATOM   3703 C  CG  . TYR B  1 191 ? -6.614  -8.139  15.700  1.00 9.31  ? 191 TYR B CG  1 
ATOM   3704 C  CD1 . TYR B  1 191 ? -5.634  -8.811  16.447  1.00 10.79 ? 191 TYR B CD1 1 
ATOM   3705 C  CD2 . TYR B  1 191 ? -6.972  -8.630  14.466  1.00 9.71  ? 191 TYR B CD2 1 
ATOM   3706 C  CE1 . TYR B  1 191 ? -5.062  -9.944  15.896  1.00 10.72 ? 191 TYR B CE1 1 
ATOM   3707 C  CE2 . TYR B  1 191 ? -6.385  -9.722  13.877  1.00 11.38 ? 191 TYR B CE2 1 
ATOM   3708 C  CZ  . TYR B  1 191 ? -5.436  -10.394 14.664  1.00 10.15 ? 191 TYR B CZ  1 
ATOM   3709 O  OH  . TYR B  1 191 ? -4.841  -11.541 14.090  1.00 15.33 ? 191 TYR B OH  1 
ATOM   3710 N  N   . ARG B  1 192 ? -8.768  -4.930  18.417  1.00 9.04  ? 192 ARG B N   1 
ATOM   3711 C  CA  . ARG B  1 192 ? -9.216  -3.621  18.760  1.00 9.75  ? 192 ARG B CA  1 
ATOM   3712 C  C   . ARG B  1 192 ? -8.093  -2.828  19.299  1.00 10.94 ? 192 ARG B C   1 
ATOM   3713 O  O   . ARG B  1 192 ? -7.378  -3.264  20.215  1.00 11.05 ? 192 ARG B O   1 
ATOM   3714 C  CB  . ARG B  1 192 ? -10.326 -3.714  19.879  1.00 10.11 ? 192 ARG B CB  1 
ATOM   3715 C  CG  . ARG B  1 192 ? -10.659 -2.394  20.572  1.00 12.42 ? 192 ARG B CG  1 
ATOM   3716 C  CD  . ARG B  1 192 ? -11.323 -1.337  19.661  1.00 12.79 ? 192 ARG B CD  1 
ATOM   3717 N  NE  . ARG B  1 192 ? -12.451 -1.887  18.891  1.00 12.88 ? 192 ARG B NE  1 
ATOM   3718 C  CZ  . ARG B  1 192 ? -13.640 -2.231  19.391  1.00 11.90 ? 192 ARG B CZ  1 
ATOM   3719 N  NH1 . ARG B  1 192 ? -13.903 -2.095  20.683  1.00 14.78 ? 192 ARG B NH1 1 
ATOM   3720 N  NH2 . ARG B  1 192 ? -14.575 -2.725  18.590  1.00 13.47 ? 192 ARG B NH2 1 
ATOM   3721 N  N   . TYR B  1 193 ? -7.848  -1.609  18.839  1.00 9.43  ? 193 TYR B N   1 
ATOM   3722 C  CA  . TYR B  1 193 ? -6.785  -0.744  19.393  1.00 10.84 ? 193 TYR B CA  1 
ATOM   3723 C  C   . TYR B  1 193 ? -7.081  0.706   19.079  1.00 11.04 ? 193 TYR B C   1 
ATOM   3724 O  O   . TYR B  1 193 ? -7.897  0.993   18.166  1.00 10.30 ? 193 TYR B O   1 
ATOM   3725 C  CB  . TYR B  1 193 ? -5.377  -1.213  18.928  1.00 9.69  ? 193 TYR B CB  1 
ATOM   3726 C  CG  . TYR B  1 193 ? -5.026  -0.775  17.480  1.00 8.43  ? 193 TYR B CG  1 
ATOM   3727 C  CD1 . TYR B  1 193 ? -5.433  -1.499  16.374  1.00 9.51  ? 193 TYR B CD1 1 
ATOM   3728 C  CD2 . TYR B  1 193 ? -4.240  0.375   17.251  1.00 9.90  ? 193 TYR B CD2 1 
ATOM   3729 C  CE1 . TYR B  1 193 ? -5.133  -1.102  15.085  1.00 8.16  ? 193 TYR B CE1 1 
ATOM   3730 C  CE2 . TYR B  1 193 ? -3.943  0.777   16.025  1.00 8.37  ? 193 TYR B CE2 1 
ATOM   3731 C  CZ  . TYR B  1 193 ? -4.368  0.075   14.956  1.00 8.60  ? 193 TYR B CZ  1 
ATOM   3732 O  OH  . TYR B  1 193 ? -4.064  0.490   13.665  1.00 9.31  ? 193 TYR B OH  1 
ATOM   3733 N  N   . ARG B  1 194 ? -6.444  1.583   19.828  1.00 12.55 ? 194 ARG B N   1 
ATOM   3734 C  CA  . ARG B  1 194 ? -6.528  3.043   19.610  1.00 12.43 ? 194 ARG B CA  1 
ATOM   3735 C  C   . ARG B  1 194 ? -5.465  3.464   18.713  1.00 10.60 ? 194 ARG B C   1 
ATOM   3736 O  O   . ARG B  1 194 ? -4.272  3.240   18.851  1.00 13.59 ? 194 ARG B O   1 
ATOM   3737 C  CB  . ARG B  1 194 ? -6.221  3.748   20.927  1.00 18.35 ? 194 ARG B CB  1 
ATOM   3738 C  CG  . ARG B  1 194 ? -7.287  3.377   21.917  1.00 25.02 ? 194 ARG B CG  1 
ATOM   3739 C  CD  . ARG B  1 194 ? -8.425  4.409   21.927  1.00 38.81 ? 194 ARG B CD  1 
ATOM   3740 N  N   . GLY B  1 195 ? -5.865  4.101   17.599  1.00 9.85  ? 195 GLY B N   1 
ATOM   3741 C  CA  . GLY B  1 195 ? -4.881  4.598   16.616  1.00 11.34 ? 195 GLY B CA  1 
ATOM   3742 C  C   . GLY B  1 195 ? -5.357  5.835   15.871  1.00 10.81 ? 195 GLY B C   1 
ATOM   3743 O  O   . GLY B  1 195 ? -5.994  6.709   16.442  1.00 11.24 ? 195 GLY B O   1 
ATOM   3744 N  N   . SER B  1 196 ? -5.015  5.897   14.612  1.00 9.34  ? 196 SER B N   1 
ATOM   3745 C  CA  . SER B  1 196 ? -5.134  7.141   13.844  1.00 9.65  ? 196 SER B CA  1 
ATOM   3746 C  C   . SER B  1 196 ? -5.635  6.899   12.490  1.00 8.58  ? 196 SER B C   1 
ATOM   3747 O  O   . SER B  1 196 ? -5.721  5.765   11.963  1.00 9.19  ? 196 SER B O   1 
ATOM   3748 C  CB  . SER B  1 196 ? -3.756  7.864   13.675  1.00 9.16  ? 196 SER B CB  1 
ATOM   3749 O  OG  . SER B  1 196 ? -2.937  7.148   12.708  1.00 8.66  ? 196 SER B OG  1 
ATOM   3750 N  N   . LEU B  1 197 ? -5.979  8.001   11.832  1.00 9.30  ? 197 LEU B N   1 
ATOM   3751 C  CA  . LEU B  1 197 ? -6.120  7.946   10.347  1.00 9.00  ? 197 LEU B CA  1 
ATOM   3752 C  C   . LEU B  1 197 ? -4.796  7.475   9.766   1.00 8.43  ? 197 LEU B C   1 
ATOM   3753 O  O   . LEU B  1 197 ? -3.718  7.900   10.190  1.00 8.87  ? 197 LEU B O   1 
ATOM   3754 C  CB  . LEU B  1 197 ? -6.472  9.366   9.732   1.00 9.10  ? 197 LEU B CB  1 
ATOM   3755 C  CG  . LEU B  1 197 ? -7.748  9.964   10.253  1.00 10.70 ? 197 LEU B CG  1 
ATOM   3756 C  CD1 . LEU B  1 197 ? -7.850  11.377  9.599   1.00 12.04 ? 197 LEU B CD1 1 
ATOM   3757 C  CD2 . LEU B  1 197 ? -8.977  9.101   9.992   1.00 10.37 ? 197 LEU B CD2 1 
ATOM   3758 N  N   . THR B  1 198 ? -4.848  6.651   8.684   1.00 8.06  ? 198 THR B N   1 
ATOM   3759 C  CA  . THR B  1 198 ? -3.626  6.143   8.084   1.00 8.68  ? 198 THR B CA  1 
ATOM   3760 C  C   . THR B  1 198 ? -3.095  7.012   6.946   1.00 8.49  ? 198 THR B C   1 
ATOM   3761 O  O   . THR B  1 198 ? -2.129  6.664   6.278   1.00 9.01  ? 198 THR B O   1 
ATOM   3762 C  CB  . THR B  1 198 ? -3.721  4.721   7.600   1.00 8.09  ? 198 THR B CB  1 
ATOM   3763 O  OG1 . THR B  1 198 ? -4.631  4.708   6.517   1.00 8.04  ? 198 THR B OG1 1 
ATOM   3764 C  CG2 . THR B  1 198 ? -4.151  3.748   8.707   1.00 8.84  ? 198 THR B CG2 1 
ATOM   3765 N  N   . THR B  1 199 ? -3.829  8.151   6.717   1.00 9.30  ? 199 THR B N   1 
ATOM   3766 C  CA  . THR B  1 199 ? -3.414  9.151   5.689   1.00 9.80  ? 199 THR B CA  1 
ATOM   3767 C  C   . THR B  1 199 ? -3.372  10.447  6.441   1.00 9.55  ? 199 THR B C   1 
ATOM   3768 O  O   . THR B  1 199 ? -4.043  10.601  7.412   1.00 10.52 ? 199 THR B O   1 
ATOM   3769 C  CB  . THR B  1 199 ? -4.395  9.284   4.485   1.00 9.60  ? 199 THR B CB  1 
ATOM   3770 O  OG1 . THR B  1 199 ? -5.612  9.845   4.930   1.00 11.75 ? 199 THR B OG1 1 
ATOM   3771 C  CG2 . THR B  1 199 ? -4.741  7.893   3.957   1.00 10.78 ? 199 THR B CG2 1 
ATOM   3772 N  N   . PRO B  1 200 ? -2.696  11.439  5.821   1.00 9.09  ? 200 PRO B N   1 
ATOM   3773 C  CA  . PRO B  1 200 ? -2.879  12.823  6.325   1.00 10.19 ? 200 PRO B CA  1 
ATOM   3774 C  C   . PRO B  1 200 ? -4.380  13.136  6.436   1.00 10.38 ? 200 PRO B C   1 
ATOM   3775 O  O   . PRO B  1 200 ? -5.112  12.740  5.549   1.00 10.88 ? 200 PRO B O   1 
ATOM   3776 C  CB  . PRO B  1 200 ? -2.159  13.609  5.189   1.00 10.07 ? 200 PRO B CB  1 
ATOM   3777 C  CG  . PRO B  1 200 ? -1.019  12.729  4.738   1.00 9.63  ? 200 PRO B CG  1 
ATOM   3778 C  CD  . PRO B  1 200 ? -1.765  11.352  4.668   1.00 9.71  ? 200 PRO B CD  1 
ATOM   3779 N  N   A PRO B  1 201 ? -4.824  13.789  7.519   0.50 9.59  ? 201 PRO B N   1 
ATOM   3780 N  N   B PRO B  1 201 ? -4.732  13.888  7.438   0.50 11.87 ? 201 PRO B N   1 
ATOM   3781 C  CA  A PRO B  1 201 ? -3.992  14.484  8.520   0.50 9.52  ? 201 PRO B CA  1 
ATOM   3782 C  CA  B PRO B  1 201 ? -3.785  14.538  8.372   0.50 11.62 ? 201 PRO B CA  1 
ATOM   3783 C  C   A PRO B  1 201 ? -3.560  13.661  9.713   0.50 9.64  ? 201 PRO B C   1 
ATOM   3784 C  C   B PRO B  1 201 ? -3.353  13.665  9.553   0.50 11.22 ? 201 PRO B C   1 
ATOM   3785 O  O   A PRO B  1 201 ? -3.031  14.109  10.708  0.50 8.27  ? 201 PRO B O   1 
ATOM   3786 O  O   B PRO B  1 201 ? -2.680  14.159  10.433  0.50 10.42 ? 201 PRO B O   1 
ATOM   3787 C  CB  A PRO B  1 201 ? -4.938  15.580  9.007   0.50 9.73  ? 201 PRO B CB  1 
ATOM   3788 C  CB  B PRO B  1 201 ? -4.577  15.754  8.887   0.50 14.02 ? 201 PRO B CB  1 
ATOM   3789 C  CG  A PRO B  1 201 ? -6.292  14.972  8.926   0.50 7.47  ? 201 PRO B CG  1 
ATOM   3790 C  CG  B PRO B  1 201 ? -5.913  15.755  8.204   0.50 14.39 ? 201 PRO B CG  1 
ATOM   3791 C  CD  A PRO B  1 201 ? -6.256  14.144  7.677   0.50 8.92  ? 201 PRO B CD  1 
ATOM   3792 C  CD  B PRO B  1 201 ? -6.076  14.485  7.424   0.50 12.32 ? 201 PRO B CD  1 
ATOM   3793 N  N   . CYS B  1 202 ? -3.741  12.367  9.587   1.00 9.27  ? 202 CYS B N   1 
ATOM   3794 C  CA  . CYS B  1 202 ? -3.191  11.360  10.556  1.00 9.95  ? 202 CYS B CA  1 
ATOM   3795 C  C   . CYS B  1 202 ? -3.736  11.534  11.988  1.00 9.82  ? 202 CYS B C   1 
ATOM   3796 O  O   . CYS B  1 202 ? -3.066  11.179  12.972  1.00 9.97  ? 202 CYS B O   1 
ATOM   3797 C  CB  . CYS B  1 202 ? -1.658  11.354  10.597  1.00 10.62 ? 202 CYS B CB  1 
ATOM   3798 S  SG  . CYS B  1 202 ? -0.852  10.958  9.035   1.00 10.66 ? 202 CYS B SG  1 
ATOM   3799 N  N   . ASN B  1 203 ? -4.937  12.095  12.082  1.00 10.95 ? 203 ASN B N   1 
ATOM   3800 C  CA  . ASN B  1 203 ? -5.482  12.432  13.396  1.00 12.22 ? 203 ASN B CA  1 
ATOM   3801 C  C   . ASN B  1 203 ? -5.494  11.214  14.267  1.00 12.79 ? 203 ASN B C   1 
ATOM   3802 O  O   . ASN B  1 203 ? -6.023  10.178  13.844  1.00 10.07 ? 203 ASN B O   1 
ATOM   3803 C  CB  . ASN B  1 203 ? -6.877  12.995  13.313  1.00 13.64 ? 203 ASN B CB  1 
ATOM   3804 C  CG  . ASN B  1 203 ? -6.971  14.251  12.441  1.00 18.57 ? 203 ASN B CG  1 
ATOM   3805 O  OD1 . ASN B  1 203 ? -5.977  14.863  12.092  1.00 22.14 ? 203 ASN B OD1 1 
ATOM   3806 N  ND2 . ASN B  1 203 ? -8.208  14.630  12.126  1.00 20.93 ? 203 ASN B ND2 1 
ATOM   3807 N  N   . PRO B  1 204 ? -5.071  11.271  15.546  1.00 11.58 ? 204 PRO B N   1 
ATOM   3808 C  CA  . PRO B  1 204 ? -5.046  10.079  16.447  1.00 13.35 ? 204 PRO B CA  1 
ATOM   3809 C  C   . PRO B  1 204 ? -6.408  9.820   17.126  1.00 14.12 ? 204 PRO B C   1 
ATOM   3810 O  O   . PRO B  1 204 ? -6.503  9.829   18.396  1.00 15.80 ? 204 PRO B O   1 
ATOM   3811 C  CB  . PRO B  1 204 ? -3.907  10.384  17.434  1.00 12.06 ? 204 PRO B CB  1 
ATOM   3812 C  CG  . PRO B  1 204 ? -3.938  11.902  17.535  1.00 14.21 ? 204 PRO B CG  1 
ATOM   3813 C  CD  . PRO B  1 204 ? -4.390  12.451  16.145  1.00 12.88 ? 204 PRO B CD  1 
ATOM   3814 N  N   . THR B  1 205 ? -7.465  9.707   16.333  1.00 11.22 ? 205 THR B N   1 
ATOM   3815 C  CA  . THR B  1 205 ? -8.800  9.799   16.842  1.00 12.66 ? 205 THR B CA  1 
ATOM   3816 C  C   . THR B  1 205 ? -9.676  8.660   16.447  1.00 11.05 ? 205 THR B C   1 
ATOM   3817 O  O   . THR B  1 205 ? -10.890 8.710   16.530  1.00 12.94 ? 205 THR B O   1 
ATOM   3818 C  CB  . THR B  1 205 ? -9.470  11.068  16.314  1.00 12.95 ? 205 THR B CB  1 
ATOM   3819 O  OG1 . THR B  1 205 ? -9.327  11.049  14.895  1.00 12.63 ? 205 THR B OG1 1 
ATOM   3820 C  CG2 . THR B  1 205 ? -8.785  12.336  16.899  1.00 15.39 ? 205 THR B CG2 1 
ATOM   3821 N  N   . VAL B  1 206 ? -8.971  7.566   16.071  1.00 9.65  ? 206 VAL B N   1 
ATOM   3822 C  CA  . VAL B  1 206 ? -9.662  6.341   15.597  1.00 11.15 ? 206 VAL B CA  1 
ATOM   3823 C  C   . VAL B  1 206 ? -9.625  5.156   16.565  1.00 10.24 ? 206 VAL B C   1 
ATOM   3824 O  O   . VAL B  1 206 ? -8.599  4.729   16.983  1.00 12.03 ? 206 VAL B O   1 
ATOM   3825 C  CB  . VAL B  1 206 ? -9.063  5.892   14.223  1.00 9.46  ? 206 VAL B CB  1 
ATOM   3826 C  CG1 . VAL B  1 206 ? -9.845  4.665   13.689  1.00 11.35 ? 206 VAL B CG1 1 
ATOM   3827 C  CG2 . VAL B  1 206 ? -9.137  7.011   13.201  1.00 11.07 ? 206 VAL B CG2 1 
ATOM   3828 N  N   . LEU B  1 207 ? -10.781 4.640   16.824  1.00 9.50  ? 207 LEU B N   1 
ATOM   3829 C  CA  . LEU B  1 207 ? -10.945 3.353   17.435  1.00 10.38 ? 207 LEU B CA  1 
ATOM   3830 C  C   . LEU B  1 207 ? -10.947 2.317   16.300  1.00 9.22  ? 207 LEU B C   1 
ATOM   3831 O  O   . LEU B  1 207 ? -11.888 2.225   15.517  1.00 10.18 ? 207 LEU B O   1 
ATOM   3832 C  CB  . LEU B  1 207 ? -12.304 3.295   18.236  1.00 13.37 ? 207 LEU B CB  1 
ATOM   3833 C  CG  . LEU B  1 207 ? -12.375 2.073   19.169  1.00 18.23 ? 207 LEU B CG  1 
ATOM   3834 C  CD1 . LEU B  1 207 ? -11.265 2.080   20.242  1.00 23.73 ? 207 LEU B CD1 1 
ATOM   3835 C  CD2 . LEU B  1 207 ? -13.744 2.149   19.854  1.00 23.55 ? 207 LEU B CD2 1 
ATOM   3836 N  N   . TRP B  1 208 ? -9.889  1.518   16.181  1.00 8.01  ? 208 TRP B N   1 
ATOM   3837 C  CA  . TRP B  1 208 ? -9.790  0.493   15.110  1.00 8.54  ? 208 TRP B CA  1 
ATOM   3838 C  C   . TRP B  1 208 ? -10.354 -0.839  15.499  1.00 8.76  ? 208 TRP B C   1 
ATOM   3839 O  O   . TRP B  1 208 ? -10.120 -1.291  16.662  1.00 10.47 ? 208 TRP B O   1 
ATOM   3840 C  CB  . TRP B  1 208 ? -8.327  0.310   14.785  1.00 9.28  ? 208 TRP B CB  1 
ATOM   3841 C  CG  . TRP B  1 208 ? -7.827  1.376   13.863  1.00 7.85  ? 208 TRP B CG  1 
ATOM   3842 C  CD1 . TRP B  1 208 ? -7.113  2.523   14.191  1.00 8.04  ? 208 TRP B CD1 1 
ATOM   3843 C  CD2 . TRP B  1 208 ? -8.016  1.434   12.418  1.00 7.83  ? 208 TRP B CD2 1 
ATOM   3844 N  NE1 . TRP B  1 208 ? -6.847  3.263   13.068  1.00 8.11  ? 208 TRP B NE1 1 
ATOM   3845 C  CE2 . TRP B  1 208 ? -7.362  2.663   11.970  1.00 7.49  ? 208 TRP B CE2 1 
ATOM   3846 C  CE3 . TRP B  1 208 ? -8.633  0.618   11.485  1.00 7.89  ? 208 TRP B CE3 1 
ATOM   3847 C  CZ2 . TRP B  1 208 ? -7.341  3.036   10.641  1.00 7.94  ? 208 TRP B CZ2 1 
ATOM   3848 C  CZ3 . TRP B  1 208 ? -8.607  1.007   10.149  1.00 8.94  ? 208 TRP B CZ3 1 
ATOM   3849 C  CH2 . TRP B  1 208 ? -7.973  2.185   9.737   1.00 8.05  ? 208 TRP B CH2 1 
ATOM   3850 N  N   . THR B  1 209 ? -11.068 -1.481  14.599  1.00 8.24  ? 209 THR B N   1 
ATOM   3851 C  CA  . THR B  1 209 ? -11.482 -2.899  14.727  1.00 8.15  ? 209 THR B CA  1 
ATOM   3852 C  C   . THR B  1 209 ? -10.998 -3.542  13.498  1.00 8.43  ? 209 THR B C   1 
ATOM   3853 O  O   . THR B  1 209 ? -11.471 -3.194  12.394  1.00 8.96  ? 209 THR B O   1 
ATOM   3854 C  CB  . THR B  1 209 ? -12.995 -2.942  14.829  1.00 8.87  ? 209 THR B CB  1 
ATOM   3855 O  OG1 . THR B  1 209 ? -13.443 -2.230  15.988  1.00 10.03 ? 209 THR B OG1 1 
ATOM   3856 C  CG2 . THR B  1 209 ? -13.566 -4.388  14.986  1.00 10.16 ? 209 THR B CG2 1 
ATOM   3857 N  N   . VAL B  1 210 ? -10.077 -4.486  13.613  1.00 8.65  ? 210 VAL B N   1 
ATOM   3858 C  CA  . VAL B  1 210 ? -9.611  -5.261  12.476  1.00 8.08  ? 210 VAL B CA  1 
ATOM   3859 C  C   . VAL B  1 210 ? -10.176 -6.648  12.599  1.00 8.63  ? 210 VAL B C   1 
ATOM   3860 O  O   . VAL B  1 210 ? -9.886  -7.328  13.627  1.00 8.64  ? 210 VAL B O   1 
ATOM   3861 C  CB  . VAL B  1 210 ? -8.041  -5.300  12.415  1.00 8.96  ? 210 VAL B CB  1 
ATOM   3862 C  CG1 . VAL B  1 210 ? -7.597  -6.034  11.182  1.00 8.87  ? 210 VAL B CG1 1 
ATOM   3863 C  CG2 . VAL B  1 210 ? -7.447  -3.866  12.455  1.00 10.86 ? 210 VAL B CG2 1 
ATOM   3864 N  N   . PHE B  1 211 ? -10.960 -7.133  11.680  1.00 8.26  ? 211 PHE B N   1 
ATOM   3865 C  CA  . PHE B  1 211 ? -11.528 -8.509  11.842  1.00 8.99  ? 211 PHE B CA  1 
ATOM   3866 C  C   . PHE B  1 211 ? -10.438 -9.526  11.685  1.00 8.84  ? 211 PHE B C   1 
ATOM   3867 O  O   . PHE B  1 211 ? -9.440  -9.366  10.956  1.00 9.15  ? 211 PHE B O   1 
ATOM   3868 C  CB  . PHE B  1 211 ? -12.631 -8.674  10.772  1.00 9.83  ? 211 PHE B CB  1 
ATOM   3869 C  CG  . PHE B  1 211 ? -13.812 -7.815  11.115  1.00 8.80  ? 211 PHE B CG  1 
ATOM   3870 C  CD1 . PHE B  1 211 ? -14.588 -8.089  12.247  1.00 9.83  ? 211 PHE B CD1 1 
ATOM   3871 C  CD2 . PHE B  1 211 ? -14.144 -6.714  10.268  1.00 10.90 ? 211 PHE B CD2 1 
ATOM   3872 C  CE1 . PHE B  1 211 ? -15.684 -7.278  12.527  1.00 10.15 ? 211 PHE B CE1 1 
ATOM   3873 C  CE2 . PHE B  1 211 ? -15.220 -5.873  10.554  1.00 10.96 ? 211 PHE B CE2 1 
ATOM   3874 C  CZ  . PHE B  1 211 ? -16.020 -6.129  11.690  1.00 11.83 ? 211 PHE B CZ  1 
ATOM   3875 N  N   . ARG B  1 212 ? -10.554 -10.617 12.478  1.00 8.95  ? 212 ARG B N   1 
ATOM   3876 C  CA  . ARG B  1 212 ? -9.501  -11.655 12.458  1.00 9.16  ? 212 ARG B CA  1 
ATOM   3877 C  C   . ARG B  1 212 ? -9.413  -12.359 11.139  1.00 9.97  ? 212 ARG B C   1 
ATOM   3878 O  O   . ARG B  1 212 ? -8.293  -12.676 10.745  1.00 12.67 ? 212 ARG B O   1 
ATOM   3879 C  CB  . ARG B  1 212 ? -9.880  -12.667 13.564  1.00 9.51  ? 212 ARG B CB  1 
ATOM   3880 C  CG  . ARG B  1 212 ? -8.746  -13.694 13.704  1.00 11.63 ? 212 ARG B CG  1 
ATOM   3881 C  CD  . ARG B  1 212 ? -9.286  -14.835 14.670  1.00 13.70 ? 212 ARG B CD  1 
ATOM   3882 N  NE  . ARG B  1 212 ? -8.157  -15.719 14.961  1.00 15.43 ? 212 ARG B NE  1 
ATOM   3883 C  CZ  . ARG B  1 212 ? -8.178  -16.619 15.933  1.00 18.87 ? 212 ARG B CZ  1 
ATOM   3884 N  NH1 . ARG B  1 212 ? -9.318  -16.971 16.462  1.00 18.28 ? 212 ARG B NH1 1 
ATOM   3885 N  NH2 . ARG B  1 212 ? -7.025  -17.199 16.275  1.00 19.74 ? 212 ARG B NH2 1 
ATOM   3886 N  N   . ASN B  1 213 ? -10.567 -12.611 10.493  1.00 9.30  ? 213 ASN B N   1 
ATOM   3887 C  CA  . ASN B  1 213 ? -10.531 -13.435 9.303   1.00 10.79 ? 213 ASN B CA  1 
ATOM   3888 C  C   . ASN B  1 213 ? -10.596 -12.549 8.053   1.00 10.88 ? 213 ASN B C   1 
ATOM   3889 O  O   . ASN B  1 213 ? -11.372 -11.590 8.015   1.00 10.41 ? 213 ASN B O   1 
ATOM   3890 C  CB  . ASN B  1 213 ? -11.777 -14.369 9.349   1.00 13.08 ? 213 ASN B CB  1 
ATOM   3891 C  CG  . ASN B  1 213 ? -11.707 -15.294 10.580  1.00 14.78 ? 213 ASN B CG  1 
ATOM   3892 O  OD1 . ASN B  1 213 ? -10.657 -15.880 10.807  1.00 22.16 ? 213 ASN B OD1 1 
ATOM   3893 N  ND2 . ASN B  1 213 ? -12.736 -15.347 11.340  1.00 19.05 ? 213 ASN B ND2 1 
ATOM   3894 N  N   . PRO B  1 214 ? -9.832  -12.854 7.030   1.00 10.33 ? 214 PRO B N   1 
ATOM   3895 C  CA  . PRO B  1 214 ? -9.856  -12.157 5.757   1.00 10.78 ? 214 PRO B CA  1 
ATOM   3896 C  C   . PRO B  1 214 ? -11.043 -12.578 4.898   1.00 10.10 ? 214 PRO B C   1 
ATOM   3897 O  O   . PRO B  1 214 ? -11.681 -13.656 5.130   1.00 12.38 ? 214 PRO B O   1 
ATOM   3898 C  CB  . PRO B  1 214 ? -8.508  -12.565 5.129   1.00 11.64 ? 214 PRO B CB  1 
ATOM   3899 C  CG  . PRO B  1 214 ? -8.410  -14.014 5.552   1.00 14.16 ? 214 PRO B CG  1 
ATOM   3900 C  CD  . PRO B  1 214 ? -8.819  -13.968 7.042   1.00 13.02 ? 214 PRO B CD  1 
ATOM   3901 N  N   . VAL B  1 215 ? -11.340 -11.766 3.889   1.00 9.02  ? 215 VAL B N   1 
ATOM   3902 C  CA  . VAL B  1 215 ? -12.152 -12.167 2.803   1.00 8.68  ? 215 VAL B CA  1 
ATOM   3903 C  C   . VAL B  1 215 ? -11.300 -12.417 1.591   1.00 8.71  ? 215 VAL B C   1 
ATOM   3904 O  O   . VAL B  1 215 ? -10.090 -12.098 1.563   1.00 9.93  ? 215 VAL B O   1 
ATOM   3905 C  CB  . VAL B  1 215 ? -13.225 -11.101 2.459   1.00 9.00  ? 215 VAL B CB  1 
ATOM   3906 C  CG1 . VAL B  1 215 ? -14.136 -10.827 3.666   1.00 11.48 ? 215 VAL B CG1 1 
ATOM   3907 C  CG2 . VAL B  1 215 ? -12.641 -9.746  1.895   1.00 8.69  ? 215 VAL B CG2 1 
ATOM   3908 N  N   . GLN B  1 216 ? -11.868 -13.030 0.584   1.00 8.71  ? 216 GLN B N   1 
ATOM   3909 C  CA  . GLN B  1 216 ? -11.152 -13.245 -0.702  1.00 8.61  ? 216 GLN B CA  1 
ATOM   3910 C  C   . GLN B  1 216 ? -11.751 -12.464 -1.861  1.00 7.60  ? 216 GLN B C   1 
ATOM   3911 O  O   . GLN B  1 216 ? -12.999 -12.352 -1.946  1.00 8.81  ? 216 GLN B O   1 
ATOM   3912 C  CB  . GLN B  1 216 ? -11.216 -14.759 -1.150  1.00 10.30 ? 216 GLN B CB  1 
ATOM   3913 C  CG  . GLN B  1 216 ? -10.491 -15.659 -0.129  1.00 10.61 ? 216 GLN B CG  1 
ATOM   3914 C  CD  . GLN B  1 216 ? -10.504 -17.123 -0.579  1.00 14.25 ? 216 GLN B CD  1 
ATOM   3915 O  OE1 . GLN B  1 216 ? -11.054 -17.573 -1.606  1.00 13.08 ? 216 GLN B OE1 1 
ATOM   3916 N  NE2 . GLN B  1 216 ? -9.824  -17.937 0.248   1.00 20.31 ? 216 GLN B NE2 1 
ATOM   3917 N  N   . ILE B  1 217 ? -10.877 -11.948 -2.720  1.00 7.35  ? 217 ILE B N   1 
ATOM   3918 C  CA  . ILE B  1 217 ? -11.296 -11.481 -4.060  1.00 7.39  ? 217 ILE B CA  1 
ATOM   3919 C  C   . ILE B  1 217 ? -10.334 -12.127 -5.048  1.00 7.43  ? 217 ILE B C   1 
ATOM   3920 O  O   . ILE B  1 217 ? -9.239  -12.572 -4.631  1.00 8.41  ? 217 ILE B O   1 
ATOM   3921 C  CB  . ILE B  1 217 ? -11.305 -9.921  -4.183  1.00 8.03  ? 217 ILE B CB  1 
ATOM   3922 C  CG1 . ILE B  1 217 ? -9.919  -9.353  -4.126  1.00 9.14  ? 217 ILE B CG1 1 
ATOM   3923 C  CG2 . ILE B  1 217 ? -12.202 -9.334  -3.088  1.00 8.91  ? 217 ILE B CG2 1 
ATOM   3924 C  CD1 . ILE B  1 217 ? -9.859  -7.785  -4.251  1.00 11.22 ? 217 ILE B CD1 1 
ATOM   3925 N  N   . SER B  1 218 ? -10.707 -12.132 -6.331  1.00 7.65  ? 218 SER B N   1 
ATOM   3926 C  CA  . SER B  1 218 ? -9.822  -12.883 -7.267  1.00 7.57  ? 218 SER B CA  1 
ATOM   3927 C  C   . SER B  1 218 ? -8.690  -12.123 -7.730  1.00 9.40  ? 218 SER B C   1 
ATOM   3928 O  O   . SER B  1 218 ? -8.633  -10.861 -7.626  1.00 9.72  ? 218 SER B O   1 
ATOM   3929 C  CB  . SER B  1 218 ? -10.606 -13.385 -8.442  1.00 8.12  ? 218 SER B CB  1 
ATOM   3930 O  OG  . SER B  1 218 ? -11.043 -12.240 -9.216  1.00 10.56 ? 218 SER B OG  1 
ATOM   3931 N  N   . GLN B  1 219 ? -7.715  -12.787 -8.374  1.00 10.39 ? 219 GLN B N   1 
ATOM   3932 C  CA  . GLN B  1 219 ? -6.588  -12.101 -9.008  1.00 11.45 ? 219 GLN B CA  1 
ATOM   3933 C  C   . GLN B  1 219 ? -7.114  -11.087 -10.049 1.00 11.60 ? 219 GLN B C   1 
ATOM   3934 O  O   . GLN B  1 219 ? -6.550  -9.974  -10.185 1.00 11.17 ? 219 GLN B O   1 
ATOM   3935 C  CB  . GLN B  1 219 ? -5.769  -13.181 -9.763  1.00 14.75 ? 219 GLN B CB  1 
ATOM   3936 C  CG  . GLN B  1 219 ? -4.422  -12.540 -10.198 1.00 22.74 ? 219 GLN B CG  1 
ATOM   3937 C  CD  . GLN B  1 219 ? -4.427  -11.913 -11.565 1.00 25.16 ? 219 GLN B CD  1 
ATOM   3938 O  OE1 . GLN B  1 219 ? -5.254  -12.231 -12.419 1.00 28.50 ? 219 GLN B OE1 1 
ATOM   3939 N  NE2 . GLN B  1 219 ? -3.480  -11.020 -11.781 1.00 24.58 ? 219 GLN B NE2 1 
ATOM   3940 N  N   . GLU B  1 220 ? -8.158  -11.444 -10.779 1.00 11.62 ? 220 GLU B N   1 
ATOM   3941 C  CA  . GLU B  1 220 ? -8.650  -10.506 -11.826 1.00 12.17 ? 220 GLU B CA  1 
ATOM   3942 C  C   . GLU B  1 220 ? -9.268  -9.264  -11.213 1.00 12.00 ? 220 GLU B C   1 
ATOM   3943 O  O   . GLU B  1 220 ? -9.134  -8.141  -11.724 1.00 11.46 ? 220 GLU B O   1 
ATOM   3944 C  CB  . GLU B  1 220 ? -9.644  -11.204 -12.751 1.00 14.63 ? 220 GLU B CB  1 
ATOM   3945 C  CG  . GLU B  1 220 ? -9.045  -12.412 -13.603 1.00 16.10 ? 220 GLU B CG  1 
ATOM   3946 C  CD  . GLU B  1 220 ? -8.789  -13.700 -12.845 1.00 20.05 ? 220 GLU B CD  1 
ATOM   3947 O  OE1 . GLU B  1 220 ? -9.207  -13.949 -11.699 1.00 16.46 ? 220 GLU B OE1 1 
ATOM   3948 O  OE2 . GLU B  1 220 ? -8.083  -14.545 -13.422 1.00 24.19 ? 220 GLU B OE2 1 
ATOM   3949 N  N   . GLN B  1 221 ? -9.925  -9.464  -10.052 1.00 10.32 ? 221 GLN B N   1 
ATOM   3950 C  CA  . GLN B  1 221 ? -10.525 -8.303  -9.350  1.00 8.84  ? 221 GLN B CA  1 
ATOM   3951 C  C   . GLN B  1 221 ? -9.417  -7.432  -8.780  1.00 9.61  ? 221 GLN B C   1 
ATOM   3952 O  O   . GLN B  1 221 ? -9.456  -6.179  -8.949  1.00 10.31 ? 221 GLN B O   1 
ATOM   3953 C  CB  . GLN B  1 221 ? -11.409 -8.759  -8.200  1.00 9.27  ? 221 GLN B CB  1 
ATOM   3954 C  CG  . GLN B  1 221 ? -12.682 -9.376  -8.712  1.00 8.67  ? 221 GLN B CG  1 
ATOM   3955 C  CD  . GLN B  1 221 ? -13.596 -9.843  -7.589  1.00 8.26  ? 221 GLN B CD  1 
ATOM   3956 O  OE1 . GLN B  1 221 ? -13.244 -10.763 -6.817  1.00 9.70  ? 221 GLN B OE1 1 
ATOM   3957 N  NE2 . GLN B  1 221 ? -14.737 -9.169  -7.408  1.00 8.66  ? 221 GLN B NE2 1 
ATOM   3958 N  N   . LEU B  1 222 ? -8.347  -7.996  -8.197  1.00 8.78  ? 222 LEU B N   1 
ATOM   3959 C  CA  . LEU B  1 222 ? -7.206  -7.196  -7.725  1.00 9.12  ? 222 LEU B CA  1 
ATOM   3960 C  C   . LEU B  1 222 ? -6.606  -6.496  -8.931  1.00 10.84 ? 222 LEU B C   1 
ATOM   3961 O  O   . LEU B  1 222 ? -6.196  -5.329  -8.772  1.00 11.08 ? 222 LEU B O   1 
ATOM   3962 C  CB  . LEU B  1 222 ? -6.213  -8.139  -7.090  1.00 10.77 ? 222 LEU B CB  1 
ATOM   3963 C  CG  . LEU B  1 222 ? -6.569  -8.509  -5.685  1.00 10.44 ? 222 LEU B CG  1 
ATOM   3964 C  CD1 . LEU B  1 222 ? -5.869  -9.782  -5.187  1.00 11.62 ? 222 LEU B CD1 1 
ATOM   3965 C  CD2 . LEU B  1 222 ? -6.253  -7.361  -4.705  1.00 11.95 ? 222 LEU B CD2 1 
ATOM   3966 N  N   . LEU B  1 223 ? -6.401  -7.166  -10.094 1.00 11.27 ? 223 LEU B N   1 
ATOM   3967 C  CA  . LEU B  1 223 ? -5.736  -6.509  -11.204 1.00 11.57 ? 223 LEU B CA  1 
ATOM   3968 C  C   . LEU B  1 223 ? -6.618  -5.365  -11.647 1.00 11.17 ? 223 LEU B C   1 
ATOM   3969 O  O   . LEU B  1 223 ? -6.017  -4.279  -12.002 1.00 11.49 ? 223 LEU B O   1 
ATOM   3970 C  CB  . LEU B  1 223 ? -5.573  -7.577  -12.343 1.00 13.49 ? 223 LEU B CB  1 
ATOM   3971 C  CG  . LEU B  1 223 ? -4.832  -6.972  -13.529 1.00 14.70 ? 223 LEU B CG  1 
ATOM   3972 C  CD1 . LEU B  1 223 ? -3.432  -6.607  -13.221 1.00 17.21 ? 223 LEU B CD1 1 
ATOM   3973 C  CD2 . LEU B  1 223 ? -4.814  -8.038  -14.634 1.00 16.20 ? 223 LEU B CD2 1 
ATOM   3974 N  N   . ALA B  1 224 ? -7.945  -5.516  -11.726 1.00 12.14 ? 224 ALA B N   1 
ATOM   3975 C  CA  . ALA B  1 224 ? -8.789  -4.369  -12.079 1.00 12.20 ? 224 ALA B CA  1 
ATOM   3976 C  C   . ALA B  1 224 ? -8.554  -3.244  -11.104 1.00 12.08 ? 224 ALA B C   1 
ATOM   3977 O  O   . ALA B  1 224 ? -8.326  -2.059  -11.527 1.00 14.34 ? 224 ALA B O   1 
ATOM   3978 C  CB  . ALA B  1 224 ? -10.236 -4.773  -12.143 1.00 14.99 ? 224 ALA B CB  1 
ATOM   3979 N  N   . LEU B  1 225 ? -8.627  -3.477  -9.801  1.00 11.74 ? 225 LEU B N   1 
ATOM   3980 C  CA  . LEU B  1 225 ? -8.447  -2.421  -8.843  1.00 10.65 ? 225 LEU B CA  1 
ATOM   3981 C  C   . LEU B  1 225 ? -7.120  -1.748  -8.996  1.00 12.20 ? 225 LEU B C   1 
ATOM   3982 O  O   . LEU B  1 225 ? -7.067  -0.497  -8.847  1.00 13.41 ? 225 LEU B O   1 
ATOM   3983 C  CB  . LEU B  1 225 ? -8.597  -3.106  -7.449  1.00 10.83 ? 225 LEU B CB  1 
ATOM   3984 C  CG  . LEU B  1 225 ? -8.441  -2.144  -6.244  1.00 11.29 ? 225 LEU B CG  1 
ATOM   3985 C  CD1 . LEU B  1 225 ? -9.530  -1.050  -6.261  1.00 11.76 ? 225 LEU B CD1 1 
ATOM   3986 C  CD2 . LEU B  1 225 ? -8.506  -2.957  -4.932  1.00 11.79 ? 225 LEU B CD2 1 
ATOM   3987 N  N   . GLU B  1 226 ? -6.038  -2.511  -9.261  1.00 10.66 ? 226 GLU B N   1 
ATOM   3988 C  CA  . GLU B  1 226 ? -4.684  -2.014  -9.347  1.00 12.46 ? 226 GLU B CA  1 
ATOM   3989 C  C   . GLU B  1 226 ? -4.391  -1.295  -10.700 1.00 11.74 ? 226 GLU B C   1 
ATOM   3990 O  O   . GLU B  1 226 ? -3.322  -0.678  -10.717 1.00 15.98 ? 226 GLU B O   1 
ATOM   3991 C  CB  . GLU B  1 226 ? -3.683  -3.223  -9.199  1.00 12.42 ? 226 GLU B CB  1 
ATOM   3992 C  CG  . GLU B  1 226 ? -3.741  -3.888  -7.779  1.00 11.80 ? 226 GLU B CG  1 
ATOM   3993 C  CD  . GLU B  1 226 ? -3.351  -5.279  -7.838  1.00 13.98 ? 226 GLU B CD  1 
ATOM   3994 O  OE1 . GLU B  1 226 ? -3.105  -5.873  -8.908  1.00 12.55 ? 226 GLU B OE1 1 
ATOM   3995 O  OE2 . GLU B  1 226 ? -3.417  -5.909  -6.785  1.00 13.24 ? 226 GLU B OE2 1 
ATOM   3996 N  N   . THR B  1 227 ? -5.244  -1.427  -11.694 1.00 12.69 ? 227 THR B N   1 
ATOM   3997 C  CA  . THR B  1 227 ? -4.944  -0.764  -12.977 1.00 11.57 ? 227 THR B CA  1 
ATOM   3998 C  C   . THR B  1 227 ? -5.959  0.256   -13.380 1.00 15.38 ? 227 THR B C   1 
ATOM   3999 O  O   . THR B  1 227 ? -5.644  0.983   -14.373 1.00 17.59 ? 227 THR B O   1 
ATOM   4000 C  CB  . THR B  1 227 ? -4.873  -1.822  -14.113 1.00 13.22 ? 227 THR B CB  1 
ATOM   4001 O  OG1 . THR B  1 227 ? -6.076  -2.587  -14.210 1.00 15.23 ? 227 THR B OG1 1 
ATOM   4002 C  CG2 . THR B  1 227 ? -3.673  -2.884  -13.863 1.00 14.84 ? 227 THR B CG2 1 
ATOM   4003 N  N   . ALA B  1 228 ? -7.031  0.406   -12.673 1.00 12.53 ? 228 ALA B N   1 
ATOM   4004 C  CA  . ALA B  1 228 ? -8.116  1.242   -13.192 1.00 13.64 ? 228 ALA B CA  1 
ATOM   4005 C  C   . ALA B  1 228 ? -7.803  2.715   -12.881 1.00 14.14 ? 228 ALA B C   1 
ATOM   4006 O  O   . ALA B  1 228 ? -8.358  3.587   -13.581 1.00 16.11 ? 228 ALA B O   1 
ATOM   4007 C  CB  . ALA B  1 228 ? -9.416  0.842   -12.569 1.00 14.64 ? 228 ALA B CB  1 
ATOM   4008 N  N   . LEU B  1 229 ? -7.171  3.036   -11.783 1.00 12.77 ? 229 LEU B N   1 
ATOM   4009 C  CA  . LEU B  1 229 ? -7.322  4.377   -11.168 1.00 11.16 ? 229 LEU B CA  1 
ATOM   4010 C  C   . LEU B  1 229 ? -6.014  5.120   -11.177 1.00 10.95 ? 229 LEU B C   1 
ATOM   4011 O  O   . LEU B  1 229 ? -4.946  4.570   -11.177 1.00 12.12 ? 229 LEU B O   1 
ATOM   4012 C  CB  . LEU B  1 229 ? -7.793  4.293   -9.679  1.00 13.20 ? 229 LEU B CB  1 
ATOM   4013 C  CG  . LEU B  1 229 ? -9.044  3.415   -9.506  1.00 14.06 ? 229 LEU B CG  1 
ATOM   4014 C  CD1 . LEU B  1 229 ? -9.426  3.263   -8.025  1.00 14.52 ? 229 LEU B CD1 1 
ATOM   4015 C  CD2 . LEU B  1 229 ? -10.201 3.915   -10.362 1.00 16.32 ? 229 LEU B CD2 1 
ATOM   4016 N  N   . TYR B  1 230 ? -6.150  6.445   -11.184 1.00 11.62 ? 230 TYR B N   1 
ATOM   4017 C  CA  . TYR B  1 230 ? -5.091  7.455   -11.189 1.00 12.48 ? 230 TYR B CA  1 
ATOM   4018 C  C   . TYR B  1 230 ? -5.278  8.434   -10.015 1.00 11.42 ? 230 TYR B C   1 
ATOM   4019 O  O   . TYR B  1 230 ? -6.418  8.707   -9.689  1.00 12.56 ? 230 TYR B O   1 
ATOM   4020 C  CB  . TYR B  1 230 ? -5.014  8.149   -12.544 1.00 13.23 ? 230 TYR B CB  1 
ATOM   4021 C  CG  . TYR B  1 230 ? -4.612  7.180   -13.630 1.00 11.71 ? 230 TYR B CG  1 
ATOM   4022 C  CD1 . TYR B  1 230 ? -5.548  6.338   -14.215 1.00 12.90 ? 230 TYR B CD1 1 
ATOM   4023 C  CD2 . TYR B  1 230 ? -3.290  7.076   -14.041 1.00 15.14 ? 230 TYR B CD2 1 
ATOM   4024 C  CE1 . TYR B  1 230 ? -5.185  5.437   -15.197 1.00 13.78 ? 230 TYR B CE1 1 
ATOM   4025 C  CE2 . TYR B  1 230 ? -2.917  6.178   -15.023 1.00 15.59 ? 230 TYR B CE2 1 
ATOM   4026 C  CZ  . TYR B  1 230 ? -3.868  5.361   -15.597 1.00 13.89 ? 230 TYR B CZ  1 
ATOM   4027 O  OH  . TYR B  1 230 ? -3.500  4.465   -16.575 1.00 20.21 ? 230 TYR B OH  1 
ATOM   4028 N  N   . CYS B  1 231 ? -4.196  8.940   -9.434  1.00 13.27 ? 231 CYS B N   1 
ATOM   4029 C  CA  . CYS B  1 231 ? -4.279  9.940   -8.387  1.00 14.89 ? 231 CYS B CA  1 
ATOM   4030 C  C   . CYS B  1 231 ? -4.456  11.318  -8.981  1.00 15.02 ? 231 CYS B C   1 
ATOM   4031 O  O   . CYS B  1 231 ? -4.808  12.267  -8.292  1.00 17.39 ? 231 CYS B O   1 
ATOM   4032 C  CB  . CYS B  1 231 ? -2.953  10.064  -7.671  1.00 18.51 ? 231 CYS B CB  1 
ATOM   4033 S  SG  . CYS B  1 231 ? -2.232  8.543   -7.023  1.00 28.62 ? 231 CYS B SG  1 
ATOM   4034 N  N   . THR B  1 232 ? -4.327  11.404  -10.310 1.00 13.81 ? 232 THR B N   1 
ATOM   4035 C  CA  . THR B  1 232 ? -4.309  12.739  -10.981 1.00 12.71 ? 232 THR B CA  1 
ATOM   4036 C  C   . THR B  1 232 ? -5.586  12.969  -11.730 1.00 12.35 ? 232 THR B C   1 
ATOM   4037 O  O   . THR B  1 232 ? -6.370  12.065  -12.002 1.00 13.32 ? 232 THR B O   1 
ATOM   4038 C  CB  . THR B  1 232 ? -3.096  12.744  -11.971 1.00 13.05 ? 232 THR B CB  1 
ATOM   4039 O  OG1 . THR B  1 232 ? -2.985  11.418  -12.611 1.00 12.81 ? 232 THR B OG1 1 
ATOM   4040 C  CG2 . THR B  1 232 ? -1.835  13.047  -11.228 1.00 14.58 ? 232 THR B CG2 1 
ATOM   4041 N  N   . HIS B  1 233 ? -5.874  14.244  -12.105 1.00 13.39 ? 233 HIS B N   1 
ATOM   4042 C  CA  . HIS B  1 233 ? -6.990  14.578  -12.901 1.00 14.75 ? 233 HIS B CA  1 
ATOM   4043 C  C   . HIS B  1 233 ? -6.910  14.105  -14.319 1.00 14.91 ? 233 HIS B C   1 
ATOM   4044 O  O   . HIS B  1 233 ? -5.806  13.841  -14.816 1.00 15.14 ? 233 HIS B O   1 
ATOM   4045 C  CB  . HIS B  1 233 ? -7.130  16.092  -12.864 1.00 17.63 ? 233 HIS B CB  1 
ATOM   4046 C  CG  . HIS B  1 233 ? -7.571  16.604  -11.524 1.00 20.85 ? 233 HIS B CG  1 
ATOM   4047 N  ND1 . HIS B  1 233 ? -6.735  17.162  -10.590 1.00 27.31 ? 233 HIS B ND1 1 
ATOM   4048 C  CD2 . HIS B  1 233 ? -8.809  16.545  -10.929 1.00 24.93 ? 233 HIS B CD2 1 
ATOM   4049 C  CE1 . HIS B  1 233 ? -7.444  17.499  -9.480  1.00 25.85 ? 233 HIS B CE1 1 
ATOM   4050 N  NE2 . HIS B  1 233 ? -8.711  17.121  -9.694  1.00 27.08 ? 233 HIS B NE2 1 
ATOM   4051 N  N   A MET B  1 234 ? -8.050  13.951  -14.976 0.50 16.03 ? 234 MET B N   1 
ATOM   4052 N  N   B MET B  1 234 ? -8.051  13.958  -14.979 0.50 16.33 ? 234 MET B N   1 
ATOM   4053 C  CA  A MET B  1 234 ? -8.123  13.411  -16.342 0.50 16.13 ? 234 MET B CA  1 
ATOM   4054 C  CA  B MET B  1 234 ? -8.137  13.417  -16.349 0.50 16.71 ? 234 MET B CA  1 
ATOM   4055 C  C   A MET B  1 234 ? -7.200  14.197  -17.282 0.50 16.86 ? 234 MET B C   1 
ATOM   4056 C  C   B MET B  1 234 ? -7.271  14.210  -17.331 0.50 17.12 ? 234 MET B C   1 
ATOM   4057 O  O   A MET B  1 234 ? -6.554  13.608  -18.164 0.50 15.79 ? 234 MET B O   1 
ATOM   4058 O  O   B MET B  1 234 ? -6.743  13.634  -18.301 0.50 16.29 ? 234 MET B O   1 
ATOM   4059 C  CB  A MET B  1 234 ? -9.574  13.438  -16.871 0.50 15.92 ? 234 MET B CB  1 
ATOM   4060 C  CB  B MET B  1 234 ? -9.589  13.414  -16.859 0.50 17.12 ? 234 MET B CB  1 
ATOM   4061 C  CG  A MET B  1 234 ? -9.817  12.886  -18.296 0.50 18.72 ? 234 MET B CG  1 
ATOM   4062 C  CG  B MET B  1 234 ? -9.811  12.889  -18.296 0.50 20.99 ? 234 MET B CG  1 
ATOM   4063 S  SD  A MET B  1 234 ? -11.589 12.589  -18.550 0.50 23.48 ? 234 MET B SD  1 
ATOM   4064 S  SD  B MET B  1 234 ? -11.590 12.737  -18.588 0.50 27.00 ? 234 MET B SD  1 
ATOM   4065 C  CE  A MET B  1 234 ? -11.514 11.975  -20.222 0.50 18.86 ? 234 MET B CE  1 
ATOM   4066 C  CE  B MET B  1 234 ? -12.139 14.374  -18.110 0.50 23.78 ? 234 MET B CE  1 
ATOM   4067 N  N   . ASP B  1 235 ? -7.105  15.501  -17.063 1.00 17.18 ? 235 ASP B N   1 
ATOM   4068 C  CA  . ASP B  1 235 ? -6.269  16.318  -18.017 1.00 17.53 ? 235 ASP B CA  1 
ATOM   4069 C  C   . ASP B  1 235 ? -4.856  16.506  -17.596 1.00 19.59 ? 235 ASP B C   1 
ATOM   4070 O  O   . ASP B  1 235 ? -4.090  17.264  -18.219 1.00 20.35 ? 235 ASP B O   1 
ATOM   4071 C  CB  . ASP B  1 235 ? -6.924  17.653  -18.249 1.00 22.13 ? 235 ASP B CB  1 
ATOM   4072 C  CG  . ASP B  1 235 ? -6.916  18.534  -17.023 1.00 29.74 ? 235 ASP B CG  1 
ATOM   4073 O  OD1 . ASP B  1 235 ? -6.682  18.072  -15.851 1.00 29.83 ? 235 ASP B OD1 1 
ATOM   4074 O  OD2 . ASP B  1 235 ? -7.204  19.742  -17.213 1.00 36.55 ? 235 ASP B OD2 1 
ATOM   4075 N  N   . ASP B  1 236 ? -4.351  15.808  -16.556 1.00 15.91 ? 236 ASP B N   1 
ATOM   4076 C  CA  . ASP B  1 236 ? -3.067  16.093  -16.064 1.00 14.19 ? 236 ASP B CA  1 
ATOM   4077 C  C   . ASP B  1 236 ? -1.976  15.597  -17.062 1.00 16.36 ? 236 ASP B C   1 
ATOM   4078 O  O   . ASP B  1 236 ? -1.970  14.436  -17.472 1.00 15.31 ? 236 ASP B O   1 
ATOM   4079 C  CB  . ASP B  1 236 ? -2.844  15.336  -14.707 1.00 16.56 ? 236 ASP B CB  1 
ATOM   4080 C  CG  . ASP B  1 236 ? -1.677  15.937  -13.946 1.00 17.59 ? 236 ASP B CG  1 
ATOM   4081 O  OD1 . ASP B  1 236 ? -0.578  16.170  -14.498 1.00 17.07 ? 236 ASP B OD1 1 
ATOM   4082 O  OD2 . ASP B  1 236 ? -1.783  16.179  -12.696 1.00 19.81 ? 236 ASP B OD2 1 
ATOM   4083 N  N   . PRO B  1 237 ? -1.023  16.455  -17.503 1.00 15.50 ? 237 PRO B N   1 
ATOM   4084 C  CA  . PRO B  1 237 ? 0.008   16.000  -18.388 1.00 16.32 ? 237 PRO B CA  1 
ATOM   4085 C  C   . PRO B  1 237 ? 1.085   15.082  -17.744 1.00 15.70 ? 237 PRO B C   1 
ATOM   4086 O  O   . PRO B  1 237 ? 1.975   14.525  -18.454 1.00 16.50 ? 237 PRO B O   1 
ATOM   4087 C  CB  . PRO B  1 237 ? 0.610   17.335  -18.892 1.00 17.01 ? 237 PRO B CB  1 
ATOM   4088 C  CG  . PRO B  1 237 ? 0.447   18.238  -17.691 1.00 17.54 ? 237 PRO B CG  1 
ATOM   4089 C  CD  . PRO B  1 237 ? -0.994  17.915  -17.282 1.00 17.45 ? 237 PRO B CD  1 
ATOM   4090 N  N   A SER B  1 238 ? 1.050   14.876  -16.416 0.50 14.86 ? 238 SER B N   1 
ATOM   4091 N  N   B SER B  1 238 ? 1.053   14.934  -16.403 0.50 15.04 ? 238 SER B N   1 
ATOM   4092 C  CA  A SER B  1 238 ? 1.987   13.963  -15.727 0.50 15.15 ? 238 SER B CA  1 
ATOM   4093 C  CA  B SER B  1 238 ? 1.912   14.008  -15.634 0.50 15.47 ? 238 SER B CA  1 
ATOM   4094 C  C   A SER B  1 238 ? 1.220   12.941  -14.907 0.50 14.01 ? 238 SER B C   1 
ATOM   4095 C  C   B SER B  1 238 ? 0.974   13.065  -14.852 0.50 13.95 ? 238 SER B C   1 
ATOM   4096 O  O   A SER B  1 238 ? 1.315   12.988  -13.689 0.50 15.18 ? 238 SER B O   1 
ATOM   4097 O  O   B SER B  1 238 ? 0.729   13.236  -13.638 0.50 14.10 ? 238 SER B O   1 
ATOM   4098 C  CB  A SER B  1 238 ? 2.803   14.723  -14.704 0.50 16.96 ? 238 SER B CB  1 
ATOM   4099 C  CB  B SER B  1 238 ? 2.859   14.773  -14.706 0.50 17.79 ? 238 SER B CB  1 
ATOM   4100 O  OG  A SER B  1 238 ? 3.933   13.953  -14.429 0.50 19.29 ? 238 SER B OG  1 
ATOM   4101 O  OG  B SER B  1 238 ? 3.778   15.509  -15.526 0.50 20.23 ? 238 SER B OG  1 
ATOM   4102 N  N   . PRO B  1 239 ? 0.430   12.074  -15.552 1.00 13.50 ? 239 PRO B N   1 
ATOM   4103 C  CA  . PRO B  1 239 ? -0.440  11.127  -14.794 1.00 13.87 ? 239 PRO B CA  1 
ATOM   4104 C  C   . PRO B  1 239 ? 0.316   10.247  -13.868 1.00 14.73 ? 239 PRO B C   1 
ATOM   4105 O  O   . PRO B  1 239 ? 1.508   9.907   -14.048 1.00 16.19 ? 239 PRO B O   1 
ATOM   4106 C  CB  . PRO B  1 239 ? -1.017  10.229  -15.845 1.00 16.70 ? 239 PRO B CB  1 
ATOM   4107 C  CG  . PRO B  1 239 ? -0.487  10.688  -17.144 1.00 18.33 ? 239 PRO B CG  1 
ATOM   4108 C  CD  . PRO B  1 239 ? 0.417   11.830  -17.008 1.00 14.66 ? 239 PRO B CD  1 
ATOM   4109 N  N   . ARG B  1 240 ? -0.390  9.897   -12.770 1.00 14.50 ? 240 ARG B N   1 
ATOM   4110 C  CA  . ARG B  1 240 ? 0.251   9.003   -11.766 1.00 15.59 ? 240 ARG B CA  1 
ATOM   4111 C  C   . ARG B  1 240 ? -0.776  7.874   -11.447 1.00 13.19 ? 240 ARG B C   1 
ATOM   4112 O  O   . ARG B  1 240 ? -1.895  8.162   -11.136 1.00 14.92 ? 240 ARG B O   1 
ATOM   4113 C  CB  . ARG B  1 240 ? 0.545   9.751   -10.503 1.00 17.04 ? 240 ARG B CB  1 
ATOM   4114 C  CG  . ARG B  1 240 ? 1.668   10.744  -10.723 1.00 23.79 ? 240 ARG B CG  1 
ATOM   4115 C  CD  . ARG B  1 240 ? 2.031   11.463  -9.412  1.00 28.59 ? 240 ARG B CD  1 
ATOM   4116 N  NE  . ARG B  1 240 ? 1.035   12.444  -8.914  1.00 33.73 ? 240 ARG B NE  1 
ATOM   4117 C  CZ  . ARG B  1 240 ? 0.245   12.201  -7.863  1.00 38.29 ? 240 ARG B CZ  1 
ATOM   4118 N  NH1 . ARG B  1 240 ? 0.316   11.003  -7.226  1.00 33.63 ? 240 ARG B NH1 1 
ATOM   4119 N  NH2 . ARG B  1 240 ? -0.631  13.116  -7.460  1.00 35.61 ? 240 ARG B NH2 1 
ATOM   4120 N  N   . GLU B  1 241 ? -0.384  6.639   -11.643 1.00 16.40 ? 241 GLU B N   1 
ATOM   4121 C  CA  . GLU B  1 241 ? -1.187  5.449   -11.269 1.00 15.52 ? 241 GLU B CA  1 
ATOM   4122 C  C   . GLU B  1 241 ? -1.424  5.371   -9.763  1.00 12.96 ? 241 GLU B C   1 
ATOM   4123 O  O   . GLU B  1 241 ? -0.492  5.505   -8.987  1.00 15.39 ? 241 GLU B O   1 
ATOM   4124 C  CB  . GLU B  1 241 ? -0.435  4.234   -11.705 1.00 18.08 ? 241 GLU B CB  1 
ATOM   4125 C  CG  . GLU B  1 241 ? -0.418  4.173   -13.235 1.00 20.24 ? 241 GLU B CG  1 
ATOM   4126 C  CD  . GLU B  1 241 ? 0.375   2.996   -13.721 1.00 27.23 ? 241 GLU B CD  1 
ATOM   4127 O  OE1 . GLU B  1 241 ? 1.309   2.575   -13.019 1.00 34.19 ? 241 GLU B OE1 1 
ATOM   4128 O  OE2 . GLU B  1 241 ? 0.038   2.495   -14.807 1.00 34.04 ? 241 GLU B OE2 1 
ATOM   4129 N  N   . MET B  1 242 ? -2.671  5.068   -9.427  1.00 11.25 ? 242 MET B N   1 
ATOM   4130 C  CA  . MET B  1 242 ? -3.025  4.864   -7.977  1.00 11.53 ? 242 MET B CA  1 
ATOM   4131 C  C   . MET B  1 242 ? -2.767  3.379   -7.586  1.00 10.29 ? 242 MET B C   1 
ATOM   4132 O  O   . MET B  1 242 ? -3.573  2.481   -7.891  1.00 11.37 ? 242 MET B O   1 
ATOM   4133 C  CB  . MET B  1 242 ? -4.465  5.209   -7.813  1.00 12.49 ? 242 MET B CB  1 
ATOM   4134 C  CG  . MET B  1 242 ? -4.878  5.173   -6.309  1.00 12.43 ? 242 MET B CG  1 
ATOM   4135 S  SD  . MET B  1 242 ? -6.564  5.544   -5.998  1.00 12.36 ? 242 MET B SD  1 
ATOM   4136 C  CE  . MET B  1 242 ? -6.570  7.261   -6.530  1.00 11.94 ? 242 MET B CE  1 
ATOM   4137 N  N   . ILE B  1 243 ? -1.549  3.192   -7.137  1.00 9.73  ? 243 ILE B N   1 
ATOM   4138 C  CA  . ILE B  1 243 ? -1.013  1.929   -6.731  1.00 10.53 ? 243 ILE B CA  1 
ATOM   4139 C  C   . ILE B  1 243 ? -0.266  2.089   -5.450  1.00 9.84  ? 243 ILE B C   1 
ATOM   4140 O  O   . ILE B  1 243 ? 0.222   3.206   -5.106  1.00 10.62 ? 243 ILE B O   1 
ATOM   4141 C  CB  . ILE B  1 243 ? -0.090  1.272   -7.853  1.00 11.60 ? 243 ILE B CB  1 
ATOM   4142 C  CG1 . ILE B  1 243 ? 1.055   2.231   -8.199  1.00 13.63 ? 243 ILE B CG1 1 
ATOM   4143 C  CG2 . ILE B  1 243 ? -0.902  0.796   -9.043  1.00 13.08 ? 243 ILE B CG2 1 
ATOM   4144 C  CD1 . ILE B  1 243 ? 2.069   1.625   -9.118  1.00 15.94 ? 243 ILE B CD1 1 
ATOM   4145 N  N   . ASN B  1 244 ? -0.127  0.967   -4.720  1.00 9.14  ? 244 ASN B N   1 
ATOM   4146 C  CA  . ASN B  1 244 ? 0.677   1.003   -3.466  1.00 9.81  ? 244 ASN B CA  1 
ATOM   4147 C  C   . ASN B  1 244 ? 0.246   2.073   -2.505  1.00 9.80  ? 244 ASN B C   1 
ATOM   4148 O  O   . ASN B  1 244 ? 1.069   2.725   -1.934  1.00 9.34  ? 244 ASN B O   1 
ATOM   4149 C  CB  . ASN B  1 244 ? 2.208   1.094   -3.784  1.00 10.71 ? 244 ASN B CB  1 
ATOM   4150 C  CG  . ASN B  1 244 ? 2.618   0.048   -4.753  1.00 13.46 ? 244 ASN B CG  1 
ATOM   4151 O  OD1 . ASN B  1 244 ? 2.233   -1.098  -4.691  1.00 14.79 ? 244 ASN B OD1 1 
ATOM   4152 N  ND2 . ASN B  1 244 ? 3.483   0.480   -5.711  1.00 17.69 ? 244 ASN B ND2 1 
ATOM   4153 N  N   . ASN B  1 245 ? -1.079  2.248   -2.396  1.00 7.99  ? 245 ASN B N   1 
ATOM   4154 C  CA  . ASN B  1 245 ? -1.625  3.315   -1.580  1.00 8.05  ? 245 ASN B CA  1 
ATOM   4155 C  C   . ASN B  1 245 ? -1.887  2.818   -0.141  1.00 8.61  ? 245 ASN B C   1 
ATOM   4156 O  O   . ASN B  1 245 ? -3.007  2.893   0.378   1.00 9.53  ? 245 ASN B O   1 
ATOM   4157 C  CB  . ASN B  1 245 ? -2.897  3.935   -2.209  1.00 8.99  ? 245 ASN B CB  1 
ATOM   4158 C  CG  . ASN B  1 245 ? -4.023  2.926   -2.401  1.00 8.50  ? 245 ASN B CG  1 
ATOM   4159 O  OD1 . ASN B  1 245 ? -3.786  1.721   -2.429  1.00 9.55  ? 245 ASN B OD1 1 
ATOM   4160 N  ND2 . ASN B  1 245 ? -5.228  3.401   -2.596  1.00 9.92  ? 245 ASN B ND2 1 
ATOM   4161 N  N   . PHE B  1 246 ? -0.837  2.346   0.474   1.00 7.72  ? 246 PHE B N   1 
ATOM   4162 C  CA  . PHE B  1 246 ? -0.874  1.909   1.888   1.00 7.58  ? 246 PHE B CA  1 
ATOM   4163 C  C   . PHE B  1 246 ? 0.315   2.515   2.589   1.00 7.73  ? 246 PHE B C   1 
ATOM   4164 O  O   . PHE B  1 246 ? 1.371   2.702   1.991   1.00 8.15  ? 246 PHE B O   1 
ATOM   4165 C  CB  . PHE B  1 246 ? -0.845  0.335   1.938   1.00 9.07  ? 246 PHE B CB  1 
ATOM   4166 C  CG  . PHE B  1 246 ? 0.422   -0.307  1.331   1.00 8.34  ? 246 PHE B CG  1 
ATOM   4167 C  CD1 . PHE B  1 246 ? 0.532   -0.537  -0.026  1.00 9.64  ? 246 PHE B CD1 1 
ATOM   4168 C  CD2 . PHE B  1 246 ? 1.535   -0.640  2.181   1.00 9.89  ? 246 PHE B CD2 1 
ATOM   4169 C  CE1 . PHE B  1 246 ? 1.665   -1.093  -0.578  1.00 9.80  ? 246 PHE B CE1 1 
ATOM   4170 C  CE2 . PHE B  1 246 ? 2.685   -1.176  1.650   1.00 10.18 ? 246 PHE B CE2 1 
ATOM   4171 C  CZ  . PHE B  1 246 ? 2.771   -1.411  0.249   1.00 10.10 ? 246 PHE B CZ  1 
ATOM   4172 N  N   . ARG B  1 247 ? 0.134   2.776   3.852   1.00 7.39  ? 247 ARG B N   1 
ATOM   4173 C  CA  . ARG B  1 247 ? 1.227   3.285   4.744   1.00 8.00  ? 247 ARG B CA  1 
ATOM   4174 C  C   . ARG B  1 247 ? 1.989   2.103   5.344   1.00 7.80  ? 247 ARG B C   1 
ATOM   4175 O  O   . ARG B  1 247 ? 1.365   1.107   5.641   1.00 8.40  ? 247 ARG B O   1 
ATOM   4176 C  CB  . ARG B  1 247 ? 0.610   4.114   5.841   1.00 8.19  ? 247 ARG B CB  1 
ATOM   4177 C  CG  . ARG B  1 247 ? 1.585   5.052   6.570   1.00 7.73  ? 247 ARG B CG  1 
ATOM   4178 C  CD  . ARG B  1 247 ? 0.879   5.728   7.720   1.00 9.03  ? 247 ARG B CD  1 
ATOM   4179 N  NE  . ARG B  1 247 ? 1.689   6.811   8.288   1.00 7.82  ? 247 ARG B NE  1 
ATOM   4180 C  CZ  . ARG B  1 247 ? 1.381   7.501   9.384   1.00 8.10  ? 247 ARG B CZ  1 
ATOM   4181 N  NH1 . ARG B  1 247 ? 0.269   7.238   10.057  1.00 9.31  ? 247 ARG B NH1 1 
ATOM   4182 N  NH2 . ARG B  1 247 ? 2.188   8.464   9.811   1.00 9.03  ? 247 ARG B NH2 1 
ATOM   4183 N  N   . GLN B  1 248 ? 3.311   2.262   5.541   1.00 7.58  ? 248 GLN B N   1 
ATOM   4184 C  CA  . GLN B  1 248 ? 4.076   1.278   6.330   1.00 7.67  ? 248 GLN B CA  1 
ATOM   4185 C  C   . GLN B  1 248 ? 3.522   1.212   7.699   1.00 8.02  ? 248 GLN B C   1 
ATOM   4186 O  O   . GLN B  1 248 ? 2.969   2.168   8.283   1.00 8.26  ? 248 GLN B O   1 
ATOM   4187 C  CB  . GLN B  1 248 ? 5.541   1.687   6.379   1.00 7.29  ? 248 GLN B CB  1 
ATOM   4188 C  CG  . GLN B  1 248 ? 6.214   1.659   4.990   1.00 8.49  ? 248 GLN B CG  1 
ATOM   4189 C  CD  . GLN B  1 248 ? 6.219   0.312   4.315   1.00 9.55  ? 248 GLN B CD  1 
ATOM   4190 O  OE1 . GLN B  1 248 ? 5.354   -0.045  3.508   1.00 10.61 ? 248 GLN B OE1 1 
ATOM   4191 N  NE2 . GLN B  1 248 ? 7.239   -0.478  4.645   1.00 10.69 ? 248 GLN B NE2 1 
ATOM   4192 N  N   . VAL B  1 249 ? 3.723   0.071   8.364   1.00 7.95  ? 249 VAL B N   1 
ATOM   4193 C  CA  . VAL B  1 249 ? 3.335   -0.075  9.805   1.00 8.47  ? 249 VAL B CA  1 
ATOM   4194 C  C   . VAL B  1 249 ? 4.179   0.812   10.715  1.00 8.19  ? 249 VAL B C   1 
ATOM   4195 O  O   . VAL B  1 249 ? 5.306   1.164   10.370  1.00 8.65  ? 249 VAL B O   1 
ATOM   4196 C  CB  . VAL B  1 249 ? 3.377   -1.538  10.309  1.00 9.68  ? 249 VAL B CB  1 
ATOM   4197 C  CG1 . VAL B  1 249 ? 2.270   -2.392  9.595   1.00 9.60  ? 249 VAL B CG1 1 
ATOM   4198 C  CG2 . VAL B  1 249 ? 4.723   -2.164  10.120  1.00 10.57 ? 249 VAL B CG2 1 
ATOM   4199 N  N   . GLN B  1 250 ? 3.554   1.220   11.789  1.00 8.75  ? 250 GLN B N   1 
ATOM   4200 C  CA  . GLN B  1 250 ? 4.125   2.217   12.715  1.00 7.84  ? 250 GLN B CA  1 
ATOM   4201 C  C   . GLN B  1 250 ? 4.625   1.578   13.994  1.00 9.35  ? 250 GLN B C   1 
ATOM   4202 O  O   . GLN B  1 250 ? 4.169   0.492   14.389  1.00 11.95 ? 250 GLN B O   1 
ATOM   4203 C  CB  . GLN B  1 250 ? 2.996   3.199   13.095  1.00 8.73  ? 250 GLN B CB  1 
ATOM   4204 C  CG  . GLN B  1 250 ? 2.310   3.819   11.842  1.00 10.18 ? 250 GLN B CG  1 
ATOM   4205 C  CD  . GLN B  1 250 ? 3.231   4.765   11.090  1.00 9.40  ? 250 GLN B CD  1 
ATOM   4206 O  OE1 . GLN B  1 250 ? 3.684   5.791   11.663  1.00 10.49 ? 250 GLN B OE1 1 
ATOM   4207 N  NE2 . GLN B  1 250 ? 3.560   4.434   9.876   1.00 9.48  ? 250 GLN B NE2 1 
ATOM   4208 N  N   . LYS B  1 251 ? 5.533   2.285   14.658  1.00 9.23  ? 251 LYS B N   1 
ATOM   4209 C  CA  . LYS B  1 251 ? 5.962   1.765   15.982  1.00 10.56 ? 251 LYS B CA  1 
ATOM   4210 C  C   . LYS B  1 251 ? 4.729   1.738   16.941  1.00 11.79 ? 251 LYS B C   1 
ATOM   4211 O  O   . LYS B  1 251 ? 3.789   2.561   16.843  1.00 11.96 ? 251 LYS B O   1 
ATOM   4212 C  CB  . LYS B  1 251 ? 6.985   2.760   16.564  1.00 12.59 ? 251 LYS B CB  1 
ATOM   4213 C  CG  . LYS B  1 251 ? 8.351   2.892   15.920  1.00 14.95 ? 251 LYS B CG  1 
ATOM   4214 C  CD  . LYS B  1 251 ? 9.167   1.742   16.434  1.00 15.02 ? 251 LYS B CD  1 
ATOM   4215 C  CE  . LYS B  1 251 ? 10.664  1.861   16.090  1.00 12.83 ? 251 LYS B CE  1 
ATOM   4216 N  NZ  . LYS B  1 251 ? 10.879  1.818   14.604  1.00 11.99 ? 251 LYS B NZ  1 
ATOM   4217 N  N   A PHE B  1 252 ? 4.744   0.807   17.868  0.50 13.27 ? 252 PHE B N   1 
ATOM   4218 N  N   B PHE B  1 252 ? 4.734   0.787   17.877  0.50 11.74 ? 252 PHE B N   1 
ATOM   4219 C  CA  A PHE B  1 252 ? 3.653   0.706   18.800  0.50 15.02 ? 252 PHE B CA  1 
ATOM   4220 C  CA  B PHE B  1 252 ? 3.623   0.688   18.811  0.50 12.72 ? 252 PHE B CA  1 
ATOM   4221 C  C   A PHE B  1 252 ? 4.152   1.242   20.110  0.50 22.68 ? 252 PHE B C   1 
ATOM   4222 C  C   B PHE B  1 252 ? 3.431   1.827   19.843  0.50 15.58 ? 252 PHE B C   1 
ATOM   4223 O  O   A PHE B  1 252 ? 4.204   0.512   21.103  0.50 19.00 ? 252 PHE B O   1 
ATOM   4224 O  O   B PHE B  1 252 ? 2.328   2.039   20.346  0.50 15.92 ? 252 PHE B O   1 
ATOM   4225 C  CB  A PHE B  1 252 ? 3.118   -0.732  18.953  0.50 16.05 ? 252 PHE B CB  1 
ATOM   4226 C  CB  B PHE B  1 252 ? 3.702   -0.670  19.473  0.50 12.82 ? 252 PHE B CB  1 
ATOM   4227 C  CG  A PHE B  1 252 ? 1.634   -0.801  19.248  0.50 15.96 ? 252 PHE B CG  1 
ATOM   4228 C  CG  B PHE B  1 252 ? 3.621   -1.793  18.491  0.50 15.20 ? 252 PHE B CG  1 
ATOM   4229 C  CD1 A PHE B  1 252 ? 0.772   0.173   18.766  0.50 15.02 ? 252 PHE B CD1 1 
ATOM   4230 C  CD1 B PHE B  1 252 ? 4.769   -2.432  18.028  0.50 16.98 ? 252 PHE B CD1 1 
ATOM   4231 C  CD2 A PHE B  1 252 ? 1.100   -1.837  20.007  0.50 16.61 ? 252 PHE B CD2 1 
ATOM   4232 C  CD2 B PHE B  1 252 ? 2.401   -2.166  17.975  0.50 19.35 ? 252 PHE B CD2 1 
ATOM   4233 C  CE1 A PHE B  1 252 ? -0.585  0.121   19.030  0.50 18.19 ? 252 PHE B CE1 1 
ATOM   4234 C  CE1 B PHE B  1 252 ? 4.675   -3.455  17.097  0.50 15.88 ? 252 PHE B CE1 1 
ATOM   4235 C  CE2 A PHE B  1 252 ? -0.259  -1.894  20.274  0.50 16.52 ? 252 PHE B CE2 1 
ATOM   4236 C  CE2 B PHE B  1 252 ? 2.296   -3.181  17.049  0.50 16.67 ? 252 PHE B CE2 1 
ATOM   4237 C  CZ  A PHE B  1 252 ? -1.101  -0.914  19.786  0.50 17.41 ? 252 PHE B CZ  1 
ATOM   4238 C  CZ  B PHE B  1 252 ? 3.438   -3.828  16.609  0.50 15.67 ? 252 PHE B CZ  1 
ATOM   4239 N  N   . ASP B  1 253 ? 4.510   2.557   20.133  1.00 23.05 ? 253 ASP B N   1 
ATOM   4240 C  CA  . ASP B  1 253 ? 4.485   3.528   21.278  1.00 26.68 ? 253 ASP B CA  1 
ATOM   4241 C  C   . ASP B  1 253 ? 3.910   2.962   22.653  1.00 31.67 ? 253 ASP B C   1 
ATOM   4242 O  O   . ASP B  1 253 ? 3.144   3.689   23.317  1.00 32.96 ? 253 ASP B O   1 
ATOM   4243 C  CB  . ASP B  1 253 ? 3.682   4.809   20.883  1.00 35.15 ? 253 ASP B CB  1 
ATOM   4244 C  CG  . ASP B  1 253 ? 4.249   5.536   19.639  1.00 40.63 ? 253 ASP B CG  1 
ATOM   4245 O  OD1 . ASP B  1 253 ? 5.489   5.527   19.472  1.00 38.56 ? 253 ASP B OD1 1 
ATOM   4246 O  OD2 . ASP B  1 253 ? 3.441   6.111   18.839  1.00 37.19 ? 253 ASP B OD2 1 
ATOM   4247 N  N   . GLU B  1 254 ? 4.255   1.717   23.057  1.00 28.10 ? 254 GLU B N   1 
ATOM   4248 C  CA  . GLU B  1 254 ? 3.746   1.098   24.303  1.00 32.94 ? 254 GLU B CA  1 
ATOM   4249 C  C   . GLU B  1 254 ? 2.252   0.637   24.279  1.00 31.90 ? 254 GLU B C   1 
ATOM   4250 O  O   . GLU B  1 254 ? 1.767   0.093   25.257  1.00 31.58 ? 254 GLU B O   1 
ATOM   4251 C  CB  . GLU B  1 254 ? 3.974   2.033   25.525  1.00 39.06 ? 254 GLU B CB  1 
ATOM   4252 C  CG  . GLU B  1 254 ? 5.311   1.848   26.237  1.00 48.25 ? 254 GLU B CG  1 
ATOM   4253 C  CD  . GLU B  1 254 ? 5.782   3.140   26.875  1.00 57.54 ? 254 GLU B CD  1 
ATOM   4254 O  OE1 . GLU B  1 254 ? 6.069   4.105   26.119  1.00 64.72 ? 254 GLU B OE1 1 
ATOM   4255 O  OE2 . GLU B  1 254 ? 5.862   3.195   28.126  1.00 63.42 ? 254 GLU B OE2 1 
ATOM   4256 N  N   . ARG B  1 255 ? 1.568   0.818   23.158  1.00 26.25 ? 255 ARG B N   1 
ATOM   4257 C  CA  . ARG B  1 255 ? 0.219   0.292   22.993  1.00 20.74 ? 255 ARG B CA  1 
ATOM   4258 C  C   . ARG B  1 255 ? 0.176   -1.291  23.018  1.00 22.95 ? 255 ARG B C   1 
ATOM   4259 O  O   . ARG B  1 255 ? 1.119   -1.979  22.517  1.00 25.03 ? 255 ARG B O   1 
ATOM   4260 C  CB  . ARG B  1 255 ? -0.365  0.818   21.626  1.00 20.19 ? 255 ARG B CB  1 
ATOM   4261 C  CG  . ARG B  1 255 ? -0.748  2.313   21.632  1.00 24.80 ? 255 ARG B CG  1 
ATOM   4262 C  CD  . ARG B  1 255 ? -1.224  2.721   20.229  1.00 20.43 ? 255 ARG B CD  1 
ATOM   4263 N  NE  . ARG B  1 255 ? -0.126  2.819   19.263  1.00 22.76 ? 255 ARG B NE  1 
ATOM   4264 C  CZ  . ARG B  1 255 ? -0.270  3.053   17.960  1.00 21.68 ? 255 ARG B CZ  1 
ATOM   4265 N  NH1 . ARG B  1 255 ? -1.476  3.218   17.441  1.00 14.61 ? 255 ARG B NH1 1 
ATOM   4266 N  NH2 . ARG B  1 255 ? 0.799   3.121   17.176  1.00 17.43 ? 255 ARG B NH2 1 
ATOM   4267 N  N   . LEU B  1 256 ? -0.904  -1.865  23.588  1.00 22.14 ? 256 LEU B N   1 
ATOM   4268 C  CA  . LEU B  1 256 ? -1.313  -3.219  23.210  1.00 22.20 ? 256 LEU B CA  1 
ATOM   4269 C  C   . LEU B  1 256 ? -2.527  -3.211  22.264  1.00 18.97 ? 256 LEU B C   1 
ATOM   4270 O  O   . LEU B  1 256 ? -3.282  -2.218  22.142  1.00 20.77 ? 256 LEU B O   1 
ATOM   4271 C  CB  . LEU B  1 256 ? -1.743  -4.020  24.405  1.00 23.96 ? 256 LEU B CB  1 
ATOM   4272 C  CG  . LEU B  1 256 ? -0.674  -4.056  25.509  1.00 24.75 ? 256 LEU B CG  1 
ATOM   4273 C  CD1 . LEU B  1 256 ? -1.163  -4.996  26.598  1.00 28.52 ? 256 LEU B CD1 1 
ATOM   4274 C  CD2 . LEU B  1 256 ? 0.611   -4.516  24.862  1.00 24.07 ? 256 LEU B CD2 1 
ATOM   4275 N  N   . VAL B  1 257 ? -2.757  -4.365  21.673  1.00 15.36 ? 257 VAL B N   1 
ATOM   4276 C  CA  . VAL B  1 257 ? -3.892  -4.592  20.829  1.00 13.71 ? 257 VAL B CA  1 
ATOM   4277 C  C   . VAL B  1 257 ? -4.711  -5.612  21.563  1.00 13.30 ? 257 VAL B C   1 
ATOM   4278 O  O   . VAL B  1 257 ? -4.204  -6.704  21.963  1.00 15.72 ? 257 VAL B O   1 
ATOM   4279 C  CB  . VAL B  1 257 ? -3.475  -5.122  19.471  1.00 13.40 ? 257 VAL B CB  1 
ATOM   4280 C  CG1 . VAL B  1 257 ? -4.680  -5.549  18.656  1.00 13.81 ? 257 VAL B CG1 1 
ATOM   4281 C  CG2 . VAL B  1 257 ? -2.643  -4.122  18.660  1.00 14.22 ? 257 VAL B CG2 1 
ATOM   4282 N  N   . TYR B  1 258 ? -5.975  -5.366  21.739  1.00 11.81 ? 258 TYR B N   1 
ATOM   4283 C  CA  . TYR B  1 258 ? -6.885  -6.268  22.487  1.00 12.88 ? 258 TYR B CA  1 
ATOM   4284 C  C   . TYR B  1 258 ? -7.645  -7.159  21.549  1.00 12.41 ? 258 TYR B C   1 
ATOM   4285 O  O   . TYR B  1 258 ? -8.065  -6.733  20.435  1.00 13.47 ? 258 TYR B O   1 
ATOM   4286 C  CB  . TYR B  1 258 ? -7.820  -5.439  23.368  1.00 14.38 ? 258 TYR B CB  1 
ATOM   4287 C  CG  . TYR B  1 258 ? -6.978  -4.545  24.250  1.00 18.28 ? 258 TYR B CG  1 
ATOM   4288 C  CD1 . TYR B  1 258 ? -6.398  -5.095  25.425  1.00 22.00 ? 258 TYR B CD1 1 
ATOM   4289 C  CD2 . TYR B  1 258 ? -6.647  -3.220  23.862  1.00 17.18 ? 258 TYR B CD2 1 
ATOM   4290 C  CE1 . TYR B  1 258 ? -5.602  -4.293  26.263  1.00 23.20 ? 258 TYR B CE1 1 
ATOM   4291 C  CE2 . TYR B  1 258 ? -5.850  -2.408  24.702  1.00 20.74 ? 258 TYR B CE2 1 
ATOM   4292 C  CZ  . TYR B  1 258 ? -5.284  -2.977  25.845  1.00 22.78 ? 258 TYR B CZ  1 
ATOM   4293 O  OH  . TYR B  1 258 ? -4.511  -2.095  26.589  1.00 26.73 ? 258 TYR B OH  1 
ATOM   4294 N  N   . THR B  1 259 ? -7.806  -8.411  21.859  1.00 11.57 ? 259 THR B N   1 
ATOM   4295 C  CA  . THR B  1 259 ? -8.469  -9.306  20.993  1.00 11.38 ? 259 THR B CA  1 
ATOM   4296 C  C   . THR B  1 259 ? -9.754  -9.888  21.576  1.00 11.22 ? 259 THR B C   1 
ATOM   4297 O  O   . THR B  1 259 ? -9.792  -10.131 22.829  1.00 12.39 ? 259 THR B O   1 
ATOM   4298 C  CB  . THR B  1 259 ? -7.607  -10.479 20.563  1.00 11.16 ? 259 THR B CB  1 
ATOM   4299 O  OG1 . THR B  1 259 ? -7.139  -11.217 21.736  1.00 13.72 ? 259 THR B OG1 1 
ATOM   4300 C  CG2 . THR B  1 259 ? -6.298  -9.992  19.877  1.00 12.93 ? 259 THR B CG2 1 
ATOM   4301 N  N   . SER B  1 260 ? -10.799 -10.087 20.787  1.00 10.08 ? 260 SER B N   1 
ATOM   4302 C  CA  . SER B  1 260 ? -12.060 -10.618 21.314  1.00 10.59 ? 260 SER B CA  1 
ATOM   4303 C  C   . SER B  1 260 ? -11.959 -12.144 21.299  1.00 11.95 ? 260 SER B C   1 
ATOM   4304 O  O   . SER B  1 260 ? -12.988 -12.780 21.693  1.00 14.85 ? 260 SER B O   1 
ATOM   4305 C  CB  . SER B  1 260 ? -13.232 -10.144 20.398  1.00 10.98 ? 260 SER B CB  1 
ATOM   4306 O  OG  . SER B  1 260 ? -13.069 -10.749 19.140  1.00 11.65 ? 260 SER B OG  1 
ATOM   4307 N  N   . PHE B  1 261 ? -10.822 -12.755 20.915  1.00 12.12 ? 261 PHE B N   1 
ATOM   4308 C  CA  . PHE B  1 261 ? -10.661 -14.193 20.782  1.00 13.59 ? 261 PHE B CA  1 
ATOM   4309 C  C   . PHE B  1 261 ? -9.425  -14.485 21.592  1.00 14.14 ? 261 PHE B C   1 
ATOM   4310 O  O   . PHE B  1 261 ? -8.502  -13.713 21.733  1.00 12.52 ? 261 PHE B O   1 
ATOM   4311 C  CB  . PHE B  1 261 ? -10.500 -14.642 19.320  1.00 14.50 ? 261 PHE B CB  1 
ATOM   4312 C  CG  . PHE B  1 261 ? -9.428  -13.885 18.557  1.00 14.04 ? 261 PHE B CG  1 
ATOM   4313 C  CD1 . PHE B  1 261 ? -9.735  -12.663 17.953  1.00 13.67 ? 261 PHE B CD1 1 
ATOM   4314 C  CD2 . PHE B  1 261 ? -8.107  -14.405 18.412  1.00 16.60 ? 261 PHE B CD2 1 
ATOM   4315 C  CE1 . PHE B  1 261 ? -8.752  -12.002 17.269  1.00 12.80 ? 261 PHE B CE1 1 
ATOM   4316 C  CE2 . PHE B  1 261 ? -7.114  -13.682 17.752  1.00 16.30 ? 261 PHE B CE2 1 
ATOM   4317 C  CZ  . PHE B  1 261 ? -7.464  -12.478 17.142  1.00 14.16 ? 261 PHE B CZ  1 
ATOM   4318 N  N   . SER B  1 262 ? -9.441  -15.675 22.223  1.00 17.21 ? 262 SER B N   1 
ATOM   4319 C  CA  . SER B  1 262 ? -8.326  -15.880 23.144  1.00 23.90 ? 262 SER B CA  1 
ATOM   4320 C  C   . SER B  1 262 ? -7.322  -16.791 22.537  1.00 30.90 ? 262 SER B C   1 
ATOM   4321 O  O   . SER B  1 262 ? -6.200  -16.861 23.022  1.00 36.54 ? 262 SER B O   1 
ATOM   4322 C  CB  . SER B  1 262 ? -8.770  -16.388 24.540  1.00 28.31 ? 262 SER B CB  1 
ATOM   4323 O  OG  . SER B  1 262 ? -9.438  -17.607 24.384  1.00 33.21 ? 262 SER B OG  1 
ATOM   4324 N  N   . GLN B  1 263 ? -7.739  -17.545 21.522  1.00 34.01 ? 263 GLN B N   1 
ATOM   4325 C  CA  . GLN B  1 263 ? -6.864  -18.453 20.761  1.00 36.71 ? 263 GLN B CA  1 
ATOM   4326 C  C   . GLN B  1 263 ? -7.514  -18.627 19.412  1.00 33.00 ? 263 GLN B C   1 
ATOM   4327 O  O   . GLN B  1 263 ? -6.976  -19.259 18.456  1.00 30.31 ? 263 GLN B O   1 
ATOM   4328 C  CB  . GLN B  1 263 ? -6.670  -19.826 21.474  1.00 36.22 ? 263 GLN B CB  1 
ATOM   4329 C  CG  . GLN B  1 263 ? -7.944  -20.627 21.794  1.00 45.63 ? 263 GLN B CG  1 
ATOM   4330 C  CD  . GLN B  1 263 ? -7.683  -21.766 22.788  1.00 48.18 ? 263 GLN B CD  1 
ATOM   4331 O  OE1 . GLN B  1 263 ? -6.759  -22.541 22.625  1.00 57.25 ? 263 GLN B OE1 1 
ATOM   4332 N  NE2 . GLN B  1 263 ? -8.502  -21.861 23.811  1.00 46.84 ? 263 GLN B NE2 1 
ATOM   4333 O  OXT . GLN B  1 263 ? -8.624  -18.091 19.319  1.00 24.43 ? 263 GLN B OXT 1 
ATOM   4334 N  N   . LYS C  1 3   ? 33.912  18.748  -27.237 1.00 46.32 ? 3   LYS C N   1 
ATOM   4335 C  CA  . LYS C  1 3   ? 33.207  17.940  -26.186 1.00 45.57 ? 3   LYS C CA  1 
ATOM   4336 C  C   . LYS C  1 3   ? 31.909  17.274  -26.725 1.00 38.26 ? 3   LYS C C   1 
ATOM   4337 O  O   . LYS C  1 3   ? 31.146  17.834  -27.559 1.00 39.22 ? 3   LYS C O   1 
ATOM   4338 C  CB  . LYS C  1 3   ? 32.970  18.739  -24.903 1.00 50.18 ? 3   LYS C CB  1 
ATOM   4339 C  CG  . LYS C  1 3   ? 32.311  17.997  -23.766 1.00 49.80 ? 3   LYS C CG  1 
ATOM   4340 C  CD  . LYS C  1 3   ? 30.824  18.317  -23.803 1.00 53.98 ? 3   LYS C CD  1 
ATOM   4341 N  N   . TRP C  1 4   ? 31.706  16.068  -26.207 1.00 29.42 ? 4   TRP C N   1 
ATOM   4342 C  CA  . TRP C  1 4   ? 30.831  15.065  -26.782 1.00 19.92 ? 4   TRP C CA  1 
ATOM   4343 C  C   . TRP C  1 4   ? 30.782  13.900  -25.849 1.00 21.42 ? 4   TRP C C   1 
ATOM   4344 O  O   . TRP C  1 4   ? 31.742  13.609  -25.062 1.00 21.18 ? 4   TRP C O   1 
ATOM   4345 C  CB  . TRP C  1 4   ? 31.313  14.644  -28.241 1.00 20.24 ? 4   TRP C CB  1 
ATOM   4346 C  CG  . TRP C  1 4   ? 32.690  13.969  -28.319 1.00 18.41 ? 4   TRP C CG  1 
ATOM   4347 C  CD1 . TRP C  1 4   ? 33.976  14.544  -28.544 1.00 16.87 ? 4   TRP C CD1 1 
ATOM   4348 C  CD2 . TRP C  1 4   ? 32.962  12.565  -28.106 1.00 16.03 ? 4   TRP C CD2 1 
ATOM   4349 N  NE1 . TRP C  1 4   ? 34.953  13.600  -28.492 1.00 17.20 ? 4   TRP C NE1 1 
ATOM   4350 C  CE2 . TRP C  1 4   ? 34.399  12.362  -28.253 1.00 16.81 ? 4   TRP C CE2 1 
ATOM   4351 C  CE3 . TRP C  1 4   ? 32.132  11.446  -27.853 1.00 14.87 ? 4   TRP C CE3 1 
ATOM   4352 C  CZ2 . TRP C  1 4   ? 34.977  11.083  -28.145 1.00 16.62 ? 4   TRP C CZ2 1 
ATOM   4353 C  CZ3 . TRP C  1 4   ? 32.716  10.185  -27.779 1.00 14.79 ? 4   TRP C CZ3 1 
ATOM   4354 C  CH2 . TRP C  1 4   ? 34.091  9.990   -27.880 1.00 15.72 ? 4   TRP C CH2 1 
ATOM   4355 N  N   . THR C  1 5   ? 29.667  13.202  -25.909 1.00 18.02 ? 5   THR C N   1 
ATOM   4356 C  CA  . THR C  1 5   ? 29.398  12.092  -24.990 1.00 18.66 ? 5   THR C CA  1 
ATOM   4357 C  C   . THR C  1 5   ? 28.708  10.959  -25.776 1.00 17.28 ? 5   THR C C   1 
ATOM   4358 O  O   . THR C  1 5   ? 28.470  11.061  -27.021 1.00 17.76 ? 5   THR C O   1 
ATOM   4359 C  CB  . THR C  1 5   ? 28.407  12.508  -23.875 1.00 21.23 ? 5   THR C CB  1 
ATOM   4360 O  OG1 . THR C  1 5   ? 27.123  12.798  -24.491 1.00 22.80 ? 5   THR C OG1 1 
ATOM   4361 C  CG2 . THR C  1 5   ? 28.929  13.781  -23.135 1.00 23.94 ? 5   THR C CG2 1 
ATOM   4362 N  N   . TYR C  1 6   ? 28.335  9.889   -25.076 1.00 20.04 ? 6   TYR C N   1 
ATOM   4363 C  CA  . TYR C  1 6   ? 27.499  8.815   -25.642 1.00 22.12 ? 6   TYR C CA  1 
ATOM   4364 C  C   . TYR C  1 6   ? 26.050  8.858   -25.067 1.00 24.08 ? 6   TYR C C   1 
ATOM   4365 O  O   . TYR C  1 6   ? 25.298  7.842   -25.121 1.00 24.10 ? 6   TYR C O   1 
ATOM   4366 C  CB  . TYR C  1 6   ? 28.111  7.435   -25.447 1.00 19.61 ? 6   TYR C CB  1 
ATOM   4367 C  CG  . TYR C  1 6   ? 29.404  7.136   -26.195 1.00 18.29 ? 6   TYR C CG  1 
ATOM   4368 C  CD1 . TYR C  1 6   ? 30.639  7.322   -25.583 1.00 18.22 ? 6   TYR C CD1 1 
ATOM   4369 C  CD2 . TYR C  1 6   ? 29.391  6.570   -27.459 1.00 15.83 ? 6   TYR C CD2 1 
ATOM   4370 C  CE1 . TYR C  1 6   ? 31.826  7.001   -26.234 1.00 17.98 ? 6   TYR C CE1 1 
ATOM   4371 C  CE2 . TYR C  1 6   ? 30.563  6.242   -28.118 1.00 15.44 ? 6   TYR C CE2 1 
ATOM   4372 C  CZ  . TYR C  1 6   ? 31.774  6.454   -27.506 1.00 16.02 ? 6   TYR C CZ  1 
ATOM   4373 O  OH  . TYR C  1 6   ? 32.923  6.134   -28.193 1.00 18.96 ? 6   TYR C OH  1 
ATOM   4374 N  N   . PHE C  1 7   ? 25.598  10.015  -24.547 1.00 29.49 ? 7   PHE C N   1 
ATOM   4375 C  CA  . PHE C  1 7   ? 24.213  10.111  -24.002 1.00 36.55 ? 7   PHE C CA  1 
ATOM   4376 C  C   . PHE C  1 7   ? 23.644  11.555  -24.043 1.00 41.85 ? 7   PHE C C   1 
ATOM   4377 O  O   . PHE C  1 7   ? 24.201  12.413  -24.737 1.00 34.58 ? 7   PHE C O   1 
ATOM   4378 C  CB  . PHE C  1 7   ? 24.264  9.630   -22.552 1.00 42.30 ? 7   PHE C CB  1 
ATOM   4379 C  CG  . PHE C  1 7   ? 24.843  10.669  -21.650 1.00 39.80 ? 7   PHE C CG  1 
ATOM   4380 C  CD1 . PHE C  1 7   ? 23.994  11.569  -20.989 1.00 42.86 ? 7   PHE C CD1 1 
ATOM   4381 C  CD2 . PHE C  1 7   ? 26.219  10.828  -21.533 1.00 43.11 ? 7   PHE C CD2 1 
ATOM   4382 C  CE1 . PHE C  1 7   ? 24.502  12.598  -20.184 1.00 40.07 ? 7   PHE C CE1 1 
ATOM   4383 C  CE2 . PHE C  1 7   ? 26.735  11.862  -20.748 1.00 38.87 ? 7   PHE C CE2 1 
ATOM   4384 C  CZ  . PHE C  1 7   ? 25.881  12.744  -20.074 1.00 42.32 ? 7   PHE C CZ  1 
ATOM   4385 N  N   . GLY C  1 8   ? 22.576  11.839  -23.261 1.00 42.27 ? 8   GLY C N   1 
ATOM   4386 C  CA  . GLY C  1 8   ? 22.004  13.219  -23.041 1.00 34.76 ? 8   GLY C CA  1 
ATOM   4387 C  C   . GLY C  1 8   ? 22.021  13.918  -24.373 1.00 35.76 ? 8   GLY C C   1 
ATOM   4388 O  O   . GLY C  1 8   ? 21.959  13.218  -25.448 1.00 35.72 ? 8   GLY C O   1 
ATOM   4389 N  N   . PRO C  1 9   ? 22.171  15.250  -24.365 1.00 30.39 ? 9   PRO C N   1 
ATOM   4390 C  CA  . PRO C  1 9   ? 22.093  15.983  -25.610 1.00 29.23 ? 9   PRO C CA  1 
ATOM   4391 C  C   . PRO C  1 9   ? 23.422  16.130  -26.352 1.00 24.72 ? 9   PRO C C   1 
ATOM   4392 O  O   . PRO C  1 9   ? 23.425  16.726  -27.427 1.00 24.67 ? 9   PRO C O   1 
ATOM   4393 C  CB  . PRO C  1 9   ? 21.679  17.402  -25.152 1.00 34.05 ? 9   PRO C CB  1 
ATOM   4394 C  CG  . PRO C  1 9   ? 22.367  17.498  -23.810 1.00 32.53 ? 9   PRO C CG  1 
ATOM   4395 C  CD  . PRO C  1 9   ? 22.107  16.162  -23.187 1.00 32.67 ? 9   PRO C CD  1 
ATOM   4396 N  N   . ASP C  1 10  ? 24.547  15.652  -25.800 1.00 25.25 ? 10  ASP C N   1 
ATOM   4397 C  CA  . ASP C  1 10  ? 25.836  15.776  -26.491 1.00 23.45 ? 10  ASP C CA  1 
ATOM   4398 C  C   . ASP C  1 10  ? 26.247  14.440  -27.073 1.00 21.28 ? 10  ASP C C   1 
ATOM   4399 O  O   . ASP C  1 10  ? 27.384  14.276  -27.507 1.00 19.43 ? 10  ASP C O   1 
ATOM   4400 C  CB  . ASP C  1 10  ? 26.924  16.264  -25.521 1.00 26.47 ? 10  ASP C CB  1 
ATOM   4401 C  CG  . ASP C  1 10  ? 26.712  17.722  -25.125 1.00 31.50 ? 10  ASP C CG  1 
ATOM   4402 O  OD1 . ASP C  1 10  ? 26.340  18.485  -26.033 1.00 34.35 ? 10  ASP C OD1 1 
ATOM   4403 O  OD2 . ASP C  1 10  ? 26.858  18.049  -23.920 1.00 37.20 ? 10  ASP C OD2 1 
ATOM   4404 N  N   . GLY C  1 11  ? 25.278  13.524  -27.140 1.00 21.45 ? 11  GLY C N   1 
ATOM   4405 C  CA  . GLY C  1 11  ? 25.473  12.126  -27.630 1.00 17.49 ? 11  GLY C CA  1 
ATOM   4406 C  C   . GLY C  1 11  ? 25.575  12.025  -29.167 1.00 16.67 ? 11  GLY C C   1 
ATOM   4407 O  O   . GLY C  1 11  ? 25.573  13.024  -29.893 1.00 14.83 ? 11  GLY C O   1 
ATOM   4408 N  N   . GLU C  1 12  ? 25.618  10.765  -29.643 1.00 14.36 ? 12  GLU C N   1 
ATOM   4409 C  CA  . GLU C  1 12  ? 25.989  10.512  -31.010 1.00 13.19 ? 12  GLU C CA  1 
ATOM   4410 C  C   . GLU C  1 12  ? 25.161  11.143  -32.071 1.00 11.91 ? 12  GLU C C   1 
ATOM   4411 O  O   . GLU C  1 12  ? 25.725  11.461  -33.096 1.00 11.01 ? 12  GLU C O   1 
ATOM   4412 C  CB  . GLU C  1 12  ? 26.187  8.987   -31.229 1.00 12.59 ? 12  GLU C CB  1 
ATOM   4413 C  CG  . GLU C  1 12  ? 24.897  8.218   -31.318 1.00 11.61 ? 12  GLU C CG  1 
ATOM   4414 C  CD  . GLU C  1 12  ? 25.153  6.752   -31.106 1.00 11.53 ? 12  GLU C CD  1 
ATOM   4415 O  OE1 . GLU C  1 12  ? 25.398  6.038   -32.101 1.00 11.33 ? 12  GLU C OE1 1 
ATOM   4416 O  OE2 . GLU C  1 12  ? 25.180  6.336   -29.933 1.00 13.61 ? 12  GLU C OE2 1 
ATOM   4417 N  N   . ASN C  1 13  ? 23.857  11.295  -31.847 1.00 11.33 ? 13  ASN C N   1 
ATOM   4418 C  CA  . ASN C  1 13  ? 23.048  11.955  -32.920 1.00 11.48 ? 13  ASN C CA  1 
ATOM   4419 C  C   . ASN C  1 13  ? 23.413  13.449  -33.094 1.00 12.07 ? 13  ASN C C   1 
ATOM   4420 O  O   . ASN C  1 13  ? 23.026  14.015  -34.114 1.00 12.12 ? 13  ASN C O   1 
ATOM   4421 C  CB  . ASN C  1 13  ? 21.590  11.799  -32.582 1.00 10.88 ? 13  ASN C CB  1 
ATOM   4422 C  CG  . ASN C  1 13  ? 21.093  10.366  -32.710 1.00 11.14 ? 13  ASN C CG  1 
ATOM   4423 O  OD1 . ASN C  1 13  ? 21.820  9.462   -33.238 1.00 12.74 ? 13  ASN C OD1 1 
ATOM   4424 N  ND2 . ASN C  1 13  ? 19.897  10.171  -32.267 1.00 10.76 ? 13  ASN C ND2 1 
ATOM   4425 N  N   A SER C  1 14  ? 24.112  13.982  -32.079 0.50 12.07 ? 14  SER C N   1 
ATOM   4426 N  N   B SER C  1 14  ? 24.072  14.071  -32.110 0.50 12.75 ? 14  SER C N   1 
ATOM   4427 C  CA  A SER C  1 14  ? 24.427  15.414  -32.024 0.50 11.93 ? 14  SER C CA  1 
ATOM   4428 C  CA  B SER C  1 14  ? 24.435  15.521  -32.258 0.50 12.13 ? 14  SER C CA  1 
ATOM   4429 C  C   A SER C  1 14  ? 25.827  15.670  -32.501 0.50 12.14 ? 14  SER C C   1 
ATOM   4430 C  C   B SER C  1 14  ? 25.928  15.689  -32.486 0.50 12.85 ? 14  SER C C   1 
ATOM   4431 O  O   A SER C  1 14  ? 26.077  16.843  -32.884 0.50 11.35 ? 14  SER C O   1 
ATOM   4432 O  O   B SER C  1 14  ? 26.421  16.801  -32.588 0.50 12.33 ? 14  SER C O   1 
ATOM   4433 C  CB  A SER C  1 14  ? 24.094  15.955  -30.608 0.50 12.35 ? 14  SER C CB  1 
ATOM   4434 C  CB  B SER C  1 14  ? 24.054  16.265  -30.986 0.50 13.51 ? 14  SER C CB  1 
ATOM   4435 O  OG  A SER C  1 14  ? 22.702  16.100  -30.497 0.50 12.63 ? 14  SER C OG  1 
ATOM   4436 O  OG  B SER C  1 14  ? 24.934  15.768  -30.009 0.50 16.81 ? 14  SER C OG  1 
ATOM   4437 N  N   . TRP C  1 15  ? 26.703  14.631  -32.605 1.00 12.60 ? 15  TRP C N   1 
ATOM   4438 C  CA  . TRP C  1 15  ? 28.095  14.821  -32.978 1.00 12.31 ? 15  TRP C CA  1 
ATOM   4439 C  C   . TRP C  1 15  ? 28.299  15.660  -34.215 1.00 11.60 ? 15  TRP C C   1 
ATOM   4440 O  O   . TRP C  1 15  ? 29.233  16.470  -34.332 1.00 12.76 ? 15  TRP C O   1 
ATOM   4441 C  CB  . TRP C  1 15  ? 28.837  13.500  -33.188 1.00 11.46 ? 15  TRP C CB  1 
ATOM   4442 C  CG  . TRP C  1 15  ? 28.946  12.677  -31.939 1.00 10.46 ? 15  TRP C CG  1 
ATOM   4443 C  CD1 . TRP C  1 15  ? 28.688  13.048  -30.602 1.00 11.94 ? 15  TRP C CD1 1 
ATOM   4444 C  CD2 . TRP C  1 15  ? 29.421  11.299  -31.889 1.00 11.01 ? 15  TRP C CD2 1 
ATOM   4445 N  NE1 . TRP C  1 15  ? 28.962  11.954  -29.752 1.00 11.79 ? 15  TRP C NE1 1 
ATOM   4446 C  CE2 . TRP C  1 15  ? 29.396  10.877  -30.490 1.00 11.37 ? 15  TRP C CE2 1 
ATOM   4447 C  CE3 . TRP C  1 15  ? 29.803  10.367  -32.896 1.00 10.65 ? 15  TRP C CE3 1 
ATOM   4448 C  CZ2 . TRP C  1 15  ? 29.787  9.603   -30.105 1.00 11.48 ? 15  TRP C CZ2 1 
ATOM   4449 C  CZ3 . TRP C  1 15  ? 30.185  9.095   -32.507 1.00 9.50  ? 15  TRP C CZ3 1 
ATOM   4450 C  CH2 . TRP C  1 15  ? 30.211  8.727   -31.121 1.00 11.43 ? 15  TRP C CH2 1 
ATOM   4451 N  N   . SER C  1 16  ? 27.420  15.495  -35.233 1.00 11.61 ? 16  SER C N   1 
ATOM   4452 C  CA  . SER C  1 16  ? 27.659  16.125  -36.546 1.00 12.12 ? 16  SER C CA  1 
ATOM   4453 C  C   . SER C  1 16  ? 27.521  17.671  -36.442 1.00 11.87 ? 16  SER C C   1 
ATOM   4454 O  O   . SER C  1 16  ? 27.963  18.313  -37.379 1.00 12.77 ? 16  SER C O   1 
ATOM   4455 C  CB  . SER C  1 16  ? 26.598  15.615  -37.513 1.00 12.07 ? 16  SER C CB  1 
ATOM   4456 O  OG  . SER C  1 16  ? 25.303  15.984  -37.063 1.00 12.67 ? 16  SER C OG  1 
ATOM   4457 N  N   A LYS C  1 17  ? 26.969  18.198  -35.368 0.50 12.86 ? 17  LYS C N   1 
ATOM   4458 N  N   B LYS C  1 17  ? 26.984  18.197  -35.366 0.50 13.08 ? 17  LYS C N   1 
ATOM   4459 C  CA  A LYS C  1 17  ? 26.920  19.681  -35.238 0.50 13.62 ? 17  LYS C CA  1 
ATOM   4460 C  CA  B LYS C  1 17  ? 26.940  19.675  -35.248 0.50 14.04 ? 17  LYS C CA  1 
ATOM   4461 C  C   A LYS C  1 17  ? 28.345  20.264  -35.190 0.50 14.52 ? 17  LYS C C   1 
ATOM   4462 C  C   B LYS C  1 17  ? 28.349  20.272  -35.187 0.50 15.25 ? 17  LYS C C   1 
ATOM   4463 O  O   A LYS C  1 17  ? 28.704  21.138  -35.989 0.50 14.33 ? 17  LYS C O   1 
ATOM   4464 O  O   B LYS C  1 17  ? 28.699  21.151  -35.985 0.50 16.59 ? 17  LYS C O   1 
ATOM   4465 C  CB  A LYS C  1 17  ? 26.134  20.061  -33.989 0.50 13.78 ? 17  LYS C CB  1 
ATOM   4466 C  CB  B LYS C  1 17  ? 26.073  20.059  -34.058 0.50 13.93 ? 17  LYS C CB  1 
ATOM   4467 C  CG  A LYS C  1 17  ? 24.649  19.721  -33.978 0.50 17.10 ? 17  LYS C CG  1 
ATOM   4468 C  CG  B LYS C  1 17  ? 24.587  19.873  -34.375 0.50 16.55 ? 17  LYS C CG  1 
ATOM   4469 C  CD  A LYS C  1 17  ? 24.155  19.803  -32.523 0.50 17.58 ? 17  LYS C CD  1 
ATOM   4470 C  CD  B LYS C  1 17  ? 23.661  20.266  -33.228 0.50 18.45 ? 17  LYS C CD  1 
ATOM   4471 C  CE  A LYS C  1 17  ? 22.782  19.180  -32.317 0.50 18.61 ? 17  LYS C CE  1 
ATOM   4472 C  CE  B LYS C  1 17  ? 23.736  21.774  -32.994 0.50 17.18 ? 17  LYS C CE  1 
ATOM   4473 N  NZ  A LYS C  1 17  ? 22.279  19.301  -30.918 0.50 18.68 ? 17  LYS C NZ  1 
ATOM   4474 N  NZ  B LYS C  1 17  ? 22.990  21.990  -31.746 0.50 18.80 ? 17  LYS C NZ  1 
ATOM   4475 N  N   . LYS C  1 18  ? 29.173  19.754  -34.296 1.00 13.55 ? 18  LYS C N   1 
ATOM   4476 C  CA  . LYS C  1 18  ? 30.551  20.220  -34.170 1.00 16.57 ? 18  LYS C CA  1 
ATOM   4477 C  C   . LYS C  1 18  ? 31.516  19.448  -35.024 1.00 17.87 ? 18  LYS C C   1 
ATOM   4478 O  O   . LYS C  1 18  ? 32.609  19.943  -35.348 1.00 19.92 ? 18  LYS C O   1 
ATOM   4479 C  CB  . LYS C  1 18  ? 31.001  20.206  -32.730 1.00 20.04 ? 18  LYS C CB  1 
ATOM   4480 C  CG  . LYS C  1 18  ? 30.362  21.241  -31.794 1.00 29.48 ? 18  LYS C CG  1 
ATOM   4481 C  CD  . LYS C  1 18  ? 30.965  22.642  -32.002 1.00 33.90 ? 18  LYS C CD  1 
ATOM   4482 C  CE  . LYS C  1 18  ? 30.083  23.671  -31.335 1.00 37.36 ? 18  LYS C CE  1 
ATOM   4483 N  NZ  . LYS C  1 18  ? 28.719  23.283  -31.836 1.00 37.81 ? 18  LYS C NZ  1 
ATOM   4484 N  N   . TYR C  1 19  ? 31.200  18.224  -35.432 1.00 14.22 ? 19  TYR C N   1 
ATOM   4485 C  CA  . TYR C  1 19  ? 32.141  17.395  -36.168 1.00 13.06 ? 19  TYR C CA  1 
ATOM   4486 C  C   . TYR C  1 19  ? 31.473  16.924  -37.457 1.00 12.93 ? 19  TYR C C   1 
ATOM   4487 O  O   . TYR C  1 19  ? 30.804  15.834  -37.479 1.00 13.36 ? 19  TYR C O   1 
ATOM   4488 C  CB  . TYR C  1 19  ? 32.498  16.131  -35.353 1.00 13.42 ? 19  TYR C CB  1 
ATOM   4489 C  CG  . TYR C  1 19  ? 33.135  16.577  -34.018 1.00 13.72 ? 19  TYR C CG  1 
ATOM   4490 C  CD1 . TYR C  1 19  ? 34.467  16.849  -33.971 1.00 14.44 ? 19  TYR C CD1 1 
ATOM   4491 C  CD2 . TYR C  1 19  ? 32.398  16.600  -32.862 1.00 13.78 ? 19  TYR C CD2 1 
ATOM   4492 C  CE1 . TYR C  1 19  ? 35.069  17.225  -32.749 1.00 15.91 ? 19  TYR C CE1 1 
ATOM   4493 C  CE2 . TYR C  1 19  ? 33.009  16.907  -31.643 1.00 14.70 ? 19  TYR C CE2 1 
ATOM   4494 C  CZ  . TYR C  1 19  ? 34.303  17.235  -31.604 1.00 16.60 ? 19  TYR C CZ  1 
ATOM   4495 O  OH  . TYR C  1 19  ? 34.894  17.580  -30.363 1.00 21.74 ? 19  TYR C OH  1 
ATOM   4496 N  N   . PRO C  1 20  ? 31.513  17.677  -38.520 1.00 12.12 ? 20  PRO C N   1 
ATOM   4497 C  CA  . PRO C  1 20  ? 30.593  17.451  -39.636 1.00 13.82 ? 20  PRO C CA  1 
ATOM   4498 C  C   . PRO C  1 20  ? 30.833  16.045  -40.243 1.00 13.80 ? 20  PRO C C   1 
ATOM   4499 O  O   . PRO C  1 20  ? 29.904  15.520  -40.934 1.00 12.62 ? 20  PRO C O   1 
ATOM   4500 C  CB  . PRO C  1 20  ? 30.907  18.555  -40.687 1.00 14.34 ? 20  PRO C CB  1 
ATOM   4501 C  CG  . PRO C  1 20  ? 31.652  19.591  -39.843 1.00 16.82 ? 20  PRO C CG  1 
ATOM   4502 C  CD  . PRO C  1 20  ? 32.252  18.964  -38.634 1.00 14.08 ? 20  PRO C CD  1 
ATOM   4503 N  N   . SER C  1 21  ? 32.040  15.489  -40.148 1.00 11.45 ? 21  SER C N   1 
ATOM   4504 C  CA  . SER C  1 21  ? 32.236  14.168  -40.801 1.00 11.51 ? 21  SER C CA  1 
ATOM   4505 C  C   . SER C  1 21  ? 31.378  13.104  -40.173 1.00 11.24 ? 21  SER C C   1 
ATOM   4506 O  O   . SER C  1 21  ? 31.133  12.094  -40.789 1.00 11.42 ? 21  SER C O   1 
ATOM   4507 C  CB  . SER C  1 21  ? 33.736  13.747  -40.698 1.00 11.53 ? 21  SER C CB  1 
ATOM   4508 O  OG  . SER C  1 21  ? 34.465  14.609  -41.603 1.00 14.71 ? 21  SER C OG  1 
ATOM   4509 N  N   . CYS C  1 22  ? 30.900  13.311  -38.962 1.00 10.97 ? 22  CYS C N   1 
ATOM   4510 C  CA  . CYS C  1 22  ? 30.031  12.303  -38.321 1.00 11.44 ? 22  CYS C CA  1 
ATOM   4511 C  C   . CYS C  1 22  ? 28.718  12.141  -39.019 1.00 12.82 ? 22  CYS C C   1 
ATOM   4512 O  O   . CYS C  1 22  ? 28.009  11.114  -38.814 1.00 12.54 ? 22  CYS C O   1 
ATOM   4513 C  CB  . CYS C  1 22  ? 29.840  12.698  -36.829 1.00 11.74 ? 22  CYS C CB  1 
ATOM   4514 S  SG  . CYS C  1 22  ? 31.322  12.769  -35.833 1.00 13.61 ? 22  CYS C SG  1 
ATOM   4515 N  N   . GLY C  1 23  ? 28.331  13.098  -39.859 1.00 12.12 ? 23  GLY C N   1 
ATOM   4516 C  CA  . GLY C  1 23  ? 27.096  13.008  -40.722 1.00 12.13 ? 23  GLY C CA  1 
ATOM   4517 C  C   . GLY C  1 23  ? 27.495  12.761  -42.167 1.00 12.02 ? 23  GLY C C   1 
ATOM   4518 O  O   . GLY C  1 23  ? 26.583  12.835  -43.046 1.00 12.05 ? 23  GLY C O   1 
ATOM   4519 N  N   . GLY C  1 24  ? 28.749  12.409  -42.425 1.00 11.45 ? 24  GLY C N   1 
ATOM   4520 C  CA  . GLY C  1 24  ? 29.215  12.220  -43.816 1.00 12.89 ? 24  GLY C CA  1 
ATOM   4521 C  C   . GLY C  1 24  ? 29.290  10.779  -44.267 1.00 14.28 ? 24  GLY C C   1 
ATOM   4522 O  O   . GLY C  1 24  ? 28.574  9.911   -43.739 1.00 14.10 ? 24  GLY C O   1 
ATOM   4523 N  N   . LEU C  1 25  ? 30.073  10.555  -45.284 1.00 14.29 ? 25  LEU C N   1 
ATOM   4524 C  CA  . LEU C  1 25  ? 30.199  9.225   -45.884 1.00 15.54 ? 25  LEU C CA  1 
ATOM   4525 C  C   . LEU C  1 25  ? 31.088  8.327   -45.021 1.00 15.46 ? 25  LEU C C   1 
ATOM   4526 O  O   . LEU C  1 25  ? 31.915  8.746   -44.170 1.00 14.24 ? 25  LEU C O   1 
ATOM   4527 C  CB  . LEU C  1 25  ? 30.802  9.344   -47.319 1.00 18.90 ? 25  LEU C CB  1 
ATOM   4528 C  CG  . LEU C  1 25  ? 30.017  10.316  -48.210 1.00 19.97 ? 25  LEU C CG  1 
ATOM   4529 C  CD1 . LEU C  1 25  ? 30.658  10.338  -49.586 1.00 26.16 ? 25  LEU C CD1 1 
ATOM   4530 C  CD2 . LEU C  1 25  ? 28.602  9.841   -48.260 1.00 25.38 ? 25  LEU C CD2 1 
ATOM   4531 N  N   . LEU C  1 26  ? 30.984  7.050   -45.373 1.00 15.51 ? 26  LEU C N   1 
ATOM   4532 C  CA  . LEU C  1 26  ? 31.935  5.975   -44.959 1.00 14.95 ? 26  LEU C CA  1 
ATOM   4533 C  C   . LEU C  1 26  ? 31.884  5.799   -43.426 1.00 12.29 ? 26  LEU C C   1 
ATOM   4534 O  O   . LEU C  1 26  ? 32.899  5.417   -42.876 1.00 14.57 ? 26  LEU C O   1 
ATOM   4535 C  CB  . LEU C  1 26  ? 33.401  6.228   -45.464 1.00 15.92 ? 26  LEU C CB  1 
ATOM   4536 C  CG  . LEU C  1 26  ? 33.687  6.170   -46.994 1.00 22.47 ? 26  LEU C CG  1 
ATOM   4537 C  CD1 . LEU C  1 26  ? 35.220  6.059   -47.168 1.00 27.44 ? 26  LEU C CD1 1 
ATOM   4538 C  CD2 . LEU C  1 26  ? 32.996  5.066   -47.742 1.00 22.81 ? 26  LEU C CD2 1 
ATOM   4539 N  N   . GLN C  1 27  ? 30.780  6.017   -42.766 1.00 9.64  ? 27  GLN C N   1 
ATOM   4540 C  CA  . GLN C  1 27  ? 30.748  5.940   -41.283 1.00 10.42 ? 27  GLN C CA  1 
ATOM   4541 C  C   . GLN C  1 27  ? 30.775  4.491   -40.753 1.00 11.11 ? 27  GLN C C   1 
ATOM   4542 O  O   . GLN C  1 27  ? 30.171  3.563   -41.324 1.00 13.21 ? 27  GLN C O   1 
ATOM   4543 C  CB  . GLN C  1 27  ? 29.569  6.672   -40.707 1.00 10.10 ? 27  GLN C CB  1 
ATOM   4544 C  CG  . GLN C  1 27  ? 29.676  8.203   -41.025 1.00 10.01 ? 27  GLN C CG  1 
ATOM   4545 C  CD  . GLN C  1 27  ? 30.874  8.852   -40.355 1.00 9.31  ? 27  GLN C CD  1 
ATOM   4546 O  OE1 . GLN C  1 27  ? 30.796  9.050   -39.120 1.00 10.16 ? 27  GLN C OE1 1 
ATOM   4547 N  NE2 . GLN C  1 27  ? 31.948  9.120   -41.086 1.00 10.94 ? 27  GLN C NE2 1 
ATOM   4548 N  N   . SER C  1 28  ? 31.539  4.290   -39.688 1.00 9.52  ? 28  SER C N   1 
ATOM   4549 C  CA  . SER C  1 28  ? 31.620  3.065   -38.905 1.00 9.38  ? 28  SER C CA  1 
ATOM   4550 C  C   . SER C  1 28  ? 31.032  3.285   -37.559 1.00 9.87  ? 28  SER C C   1 
ATOM   4551 O  O   . SER C  1 28  ? 30.930  4.417   -37.088 1.00 10.68 ? 28  SER C O   1 
ATOM   4552 C  CB  . SER C  1 28  ? 33.110  2.754   -38.755 1.00 9.10  ? 28  SER C CB  1 
ATOM   4553 O  OG  . SER C  1 28  ? 33.696  2.478   -40.063 1.00 10.26 ? 28  SER C OG  1 
ATOM   4554 N  N   . PRO C  1 29  ? 30.676  2.208   -36.827 1.00 9.80  ? 29  PRO C N   1 
ATOM   4555 C  CA  . PRO C  1 29  ? 30.824  0.822   -37.205 1.00 8.32  ? 29  PRO C CA  1 
ATOM   4556 C  C   . PRO C  1 29  ? 29.587  0.386   -38.009 1.00 8.46  ? 29  PRO C C   1 
ATOM   4557 O  O   . PRO C  1 29  ? 28.655  1.115   -38.276 1.00 9.91  ? 29  PRO C O   1 
ATOM   4558 C  CB  . PRO C  1 29  ? 30.820  0.137   -35.826 1.00 10.03 ? 29  PRO C CB  1 
ATOM   4559 C  CG  . PRO C  1 29  ? 29.825  0.930   -35.027 1.00 11.53 ? 29  PRO C CG  1 
ATOM   4560 C  CD  . PRO C  1 29  ? 30.076  2.403   -35.474 1.00 10.74 ? 29  PRO C CD  1 
ATOM   4561 N  N   . ILE C  1 30  ? 29.649  -0.896  -38.405 1.00 9.03  ? 30  ILE C N   1 
ATOM   4562 C  CA  . ILE C  1 30  ? 28.638  -1.478  -39.269 1.00 9.29  ? 30  ILE C CA  1 
ATOM   4563 C  C   . ILE C  1 30  ? 28.318  -2.887  -38.782 1.00 9.77  ? 30  ILE C C   1 
ATOM   4564 O  O   . ILE C  1 30  ? 29.082  -3.534  -38.035 1.00 9.87  ? 30  ILE C O   1 
ATOM   4565 C  CB  . ILE C  1 30  ? 29.101  -1.527  -40.728 1.00 9.38  ? 30  ILE C CB  1 
ATOM   4566 C  CG1 . ILE C  1 30  ? 30.345  -2.415  -40.907 1.00 9.86  ? 30  ILE C CG1 1 
ATOM   4567 C  CG2 . ILE C  1 30  ? 29.292  -0.072  -41.229 1.00 10.04 ? 30  ILE C CG2 1 
ATOM   4568 C  CD1 . ILE C  1 30  ? 30.663  -2.646  -42.396 1.00 11.44 ? 30  ILE C CD1 1 
ATOM   4569 N  N   . ASP C  1 31  ? 27.180  -3.405  -39.284 1.00 9.94  ? 31  ASP C N   1 
ATOM   4570 C  CA  . ASP C  1 31  ? 26.839  -4.840  -39.118 1.00 10.98 ? 31  ASP C CA  1 
ATOM   4571 C  C   . ASP C  1 31  ? 27.422  -5.667  -40.194 1.00 11.63 ? 31  ASP C C   1 
ATOM   4572 O  O   . ASP C  1 31  ? 27.296  -5.365  -41.403 1.00 14.12 ? 31  ASP C O   1 
ATOM   4573 C  CB  . ASP C  1 31  ? 25.341  -5.011  -39.275 1.00 12.53 ? 31  ASP C CB  1 
ATOM   4574 C  CG  . ASP C  1 31  ? 24.912  -6.440  -38.974 1.00 14.09 ? 31  ASP C CG  1 
ATOM   4575 O  OD1 . ASP C  1 31  ? 25.380  -7.070  -37.987 1.00 14.41 ? 31  ASP C OD1 1 
ATOM   4576 O  OD2 . ASP C  1 31  ? 24.018  -6.962  -39.741 1.00 19.28 ? 31  ASP C OD2 1 
ATOM   4577 N  N   . LEU C  1 32  ? 28.173  -6.699  -39.827 1.00 12.66 ? 32  LEU C N   1 
ATOM   4578 C  CA  . LEU C  1 32  ? 28.822  -7.627  -40.727 1.00 13.21 ? 32  LEU C CA  1 
ATOM   4579 C  C   . LEU C  1 32  ? 27.918  -8.864  -40.891 1.00 13.12 ? 32  LEU C C   1 
ATOM   4580 O  O   . LEU C  1 32  ? 27.728  -9.602  -39.985 1.00 15.18 ? 32  LEU C O   1 
ATOM   4581 C  CB  . LEU C  1 32  ? 30.131  -8.094  -40.091 1.00 13.86 ? 32  LEU C CB  1 
ATOM   4582 C  CG  . LEU C  1 32  ? 31.061  -6.909  -39.675 1.00 12.55 ? 32  LEU C CG  1 
ATOM   4583 C  CD1 . LEU C  1 32  ? 32.298  -7.348  -38.888 1.00 15.03 ? 32  LEU C CD1 1 
ATOM   4584 C  CD2 . LEU C  1 32  ? 31.501  -6.151  -40.934 1.00 14.78 ? 32  LEU C CD2 1 
ATOM   4585 N  N   . HIS C  1 33  ? 27.337  -9.038  -42.069 1.00 17.75 ? 33  HIS C N   1 
ATOM   4586 C  CA  . HIS C  1 33  ? 26.334  -10.122 -42.265 1.00 18.72 ? 33  HIS C CA  1 
ATOM   4587 C  C   . HIS C  1 33  ? 26.558  -10.727 -43.611 1.00 19.84 ? 33  HIS C C   1 
ATOM   4588 O  O   . HIS C  1 33  ? 27.028  -10.017 -44.476 1.00 19.12 ? 33  HIS C O   1 
ATOM   4589 C  CB  . HIS C  1 33  ? 24.894  -9.638  -42.061 1.00 21.38 ? 33  HIS C CB  1 
ATOM   4590 C  CG  . HIS C  1 33  ? 24.463  -8.582  -42.974 1.00 22.57 ? 33  HIS C CG  1 
ATOM   4591 N  ND1 . HIS C  1 33  ? 23.816  -8.870  -44.136 1.00 27.09 ? 33  HIS C ND1 1 
ATOM   4592 C  CD2 . HIS C  1 33  ? 24.543  -7.197  -42.889 1.00 23.58 ? 33  HIS C CD2 1 
ATOM   4593 C  CE1 . HIS C  1 33  ? 23.562  -7.713  -44.798 1.00 25.83 ? 33  HIS C CE1 1 
ATOM   4594 N  NE2 . HIS C  1 33  ? 23.961  -6.693  -44.028 1.00 27.16 ? 33  HIS C NE2 1 
ATOM   4595 N  N   A SER C  1 34  ? 26.169  -12.000 -43.821 0.50 21.78 ? 34  SER C N   1 
ATOM   4596 N  N   B SER C  1 34  ? 26.118  -11.982 -43.819 0.50 21.57 ? 34  SER C N   1 
ATOM   4597 C  CA  A SER C  1 34  ? 26.583  -12.780 -44.997 0.50 22.10 ? 34  SER C CA  1 
ATOM   4598 C  CA  B SER C  1 34  ? 26.507  -12.794 -44.973 0.50 22.13 ? 34  SER C CA  1 
ATOM   4599 C  C   A SER C  1 34  ? 26.285  -12.171 -46.348 0.50 20.89 ? 34  SER C C   1 
ATOM   4600 C  C   B SER C  1 34  ? 26.267  -12.195 -46.329 0.50 20.69 ? 34  SER C C   1 
ATOM   4601 O  O   A SER C  1 34  ? 27.107  -12.289 -47.252 0.50 24.59 ? 34  SER C O   1 
ATOM   4602 O  O   B SER C  1 34  ? 27.108  -12.347 -47.209 0.50 24.12 ? 34  SER C O   1 
ATOM   4603 C  CB  A SER C  1 34  ? 25.931  -14.149 -44.974 0.50 24.99 ? 34  SER C CB  1 
ATOM   4604 C  CB  B SER C  1 34  ? 25.783  -14.130 -44.936 0.50 24.76 ? 34  SER C CB  1 
ATOM   4605 O  OG  A SER C  1 34  ? 24.540  -13.975 -45.100 0.50 28.14 ? 34  SER C OG  1 
ATOM   4606 O  OG  B SER C  1 34  ? 26.123  -14.835 -43.763 0.50 28.10 ? 34  SER C OG  1 
ATOM   4607 N  N   . ASP C  1 35  ? 25.130  -11.521 -46.488 1.00 22.99 ? 35  ASP C N   1 
ATOM   4608 C  CA  . ASP C  1 35  ? 24.694  -10.946 -47.817 1.00 27.23 ? 35  ASP C CA  1 
ATOM   4609 C  C   . ASP C  1 35  ? 25.594  -9.885  -48.367 1.00 21.35 ? 35  ASP C C   1 
ATOM   4610 O  O   . ASP C  1 35  ? 25.553  -9.519  -49.560 1.00 26.24 ? 35  ASP C O   1 
ATOM   4611 C  CB  . ASP C  1 35  ? 23.258  -10.345 -47.781 1.00 34.00 ? 35  ASP C CB  1 
ATOM   4612 C  CG  . ASP C  1 35  ? 22.164  -11.377 -47.463 1.00 48.74 ? 35  ASP C CG  1 
ATOM   4613 O  OD1 . ASP C  1 35  ? 22.390  -12.601 -47.645 1.00 49.84 ? 35  ASP C OD1 1 
ATOM   4614 O  OD2 . ASP C  1 35  ? 21.056  -10.942 -47.028 1.00 55.75 ? 35  ASP C OD2 1 
ATOM   4615 N  N   . ILE C  1 36  ? 26.484  -9.344  -47.523 1.00 17.79 ? 36  ILE C N   1 
ATOM   4616 C  CA  . ILE C  1 36  ? 27.342  -8.262  -48.000 1.00 17.41 ? 36  ILE C CA  1 
ATOM   4617 C  C   . ILE C  1 36  ? 28.816  -8.662  -47.918 1.00 16.24 ? 36  ILE C C   1 
ATOM   4618 O  O   . ILE C  1 36  ? 29.667  -7.835  -48.237 1.00 18.21 ? 36  ILE C O   1 
ATOM   4619 C  CB  . ILE C  1 36  ? 27.136  -6.931  -47.229 1.00 17.88 ? 36  ILE C CB  1 
ATOM   4620 C  CG1 . ILE C  1 36  ? 27.389  -7.080  -45.692 1.00 19.35 ? 36  ILE C CG1 1 
ATOM   4621 C  CG2 . ILE C  1 36  ? 25.721  -6.368  -47.507 1.00 20.59 ? 36  ILE C CG2 1 
ATOM   4622 C  CD1 . ILE C  1 36  ? 27.544  -5.779  -44.899 1.00 20.02 ? 36  ILE C CD1 1 
ATOM   4623 N  N   . LEU C  1 37  ? 29.084  -9.904  -47.594 1.00 18.86 ? 37  LEU C N   1 
ATOM   4624 C  CA  . LEU C  1 37  ? 30.471  -10.384 -47.594 1.00 17.02 ? 37  LEU C CA  1 
ATOM   4625 C  C   . LEU C  1 37  ? 30.921  -10.900 -48.926 1.00 19.80 ? 37  LEU C C   1 
ATOM   4626 O  O   . LEU C  1 37  ? 30.132  -11.567 -49.695 1.00 24.06 ? 37  LEU C O   1 
ATOM   4627 C  CB  . LEU C  1 37  ? 30.551  -11.520 -46.570 1.00 19.50 ? 37  LEU C CB  1 
ATOM   4628 C  CG  . LEU C  1 37  ? 30.147  -11.227 -45.142 1.00 20.96 ? 37  LEU C CG  1 
ATOM   4629 C  CD1 . LEU C  1 37  ? 30.409  -12.500 -44.345 1.00 22.13 ? 37  LEU C CD1 1 
ATOM   4630 C  CD2 . LEU C  1 37  ? 30.923  -10.019 -44.568 1.00 20.58 ? 37  LEU C CD2 1 
ATOM   4631 N  N   . GLN C  1 38  ? 32.173  -10.656 -49.240 1.00 18.10 ? 38  GLN C N   1 
ATOM   4632 C  CA  . GLN C  1 38  ? 32.783  -11.185 -50.467 1.00 19.19 ? 38  GLN C CA  1 
ATOM   4633 C  C   . GLN C  1 38  ? 34.209  -11.570 -50.226 1.00 18.07 ? 38  GLN C C   1 
ATOM   4634 O  O   . GLN C  1 38  ? 35.001  -10.735 -49.808 1.00 16.48 ? 38  GLN C O   1 
ATOM   4635 C  CB  . GLN C  1 38  ? 32.702  -10.156 -51.620 1.00 21.15 ? 38  GLN C CB  1 
ATOM   4636 C  CG  . GLN C  1 38  ? 33.171  -10.697 -52.989 1.00 25.21 ? 38  GLN C CG  1 
ATOM   4637 C  CD  . GLN C  1 38  ? 32.795  -9.790  -54.140 1.00 28.90 ? 38  GLN C CD  1 
ATOM   4638 O  OE1 . GLN C  1 38  ? 31.645  -9.821  -54.629 1.00 40.91 ? 38  GLN C OE1 1 
ATOM   4639 N  NE2 . GLN C  1 38  ? 33.708  -8.951  -54.541 1.00 27.02 ? 38  GLN C NE2 1 
ATOM   4640 N  N   . TYR C  1 39  ? 34.575  -12.800 -50.546 1.00 19.01 ? 39  TYR C N   1 
ATOM   4641 C  CA  . TYR C  1 39  ? 35.967  -13.194 -50.483 1.00 18.18 ? 39  TYR C CA  1 
ATOM   4642 C  C   . TYR C  1 39  ? 36.861  -12.435 -51.404 1.00 18.02 ? 39  TYR C C   1 
ATOM   4643 O  O   . TYR C  1 39  ? 36.492  -12.150 -52.566 1.00 21.19 ? 39  TYR C O   1 
ATOM   4644 C  CB  . TYR C  1 39  ? 36.062  -14.755 -50.806 1.00 20.18 ? 39  TYR C CB  1 
ATOM   4645 C  CG  . TYR C  1 39  ? 37.506  -15.185 -50.959 1.00 23.82 ? 39  TYR C CG  1 
ATOM   4646 C  CD1 . TYR C  1 39  ? 38.303  -15.376 -49.835 1.00 23.77 ? 39  TYR C CD1 1 
ATOM   4647 C  CD2 . TYR C  1 39  ? 38.041  -15.479 -52.224 1.00 22.09 ? 39  TYR C CD2 1 
ATOM   4648 C  CE1 . TYR C  1 39  ? 39.634  -15.784 -49.975 1.00 30.27 ? 39  TYR C CE1 1 
ATOM   4649 C  CE2 . TYR C  1 39  ? 39.354  -15.894 -52.382 1.00 32.26 ? 39  TYR C CE2 1 
ATOM   4650 C  CZ  . TYR C  1 39  ? 40.148  -16.043 -51.255 1.00 31.58 ? 39  TYR C CZ  1 
ATOM   4651 O  OH  . TYR C  1 39  ? 41.475  -16.442 -51.472 1.00 27.89 ? 39  TYR C OH  1 
ATOM   4652 N  N   . ASP C  1 40  ? 38.028  -12.008 -50.907 1.00 18.77 ? 40  ASP C N   1 
ATOM   4653 C  CA  . ASP C  1 40  ? 38.967  -11.187 -51.672 1.00 19.13 ? 40  ASP C CA  1 
ATOM   4654 C  C   . ASP C  1 40  ? 40.351  -11.828 -51.445 1.00 19.03 ? 40  ASP C C   1 
ATOM   4655 O  O   . ASP C  1 40  ? 40.945  -11.781 -50.363 1.00 19.64 ? 40  ASP C O   1 
ATOM   4656 C  CB  . ASP C  1 40  ? 38.863  -9.736  -51.202 1.00 19.73 ? 40  ASP C CB  1 
ATOM   4657 C  CG  . ASP C  1 40  ? 39.793  -8.799  -51.871 1.00 26.60 ? 40  ASP C CG  1 
ATOM   4658 O  OD1 . ASP C  1 40  ? 40.694  -9.190  -52.591 1.00 21.64 ? 40  ASP C OD1 1 
ATOM   4659 O  OD2 . ASP C  1 40  ? 39.620  -7.587  -51.622 1.00 29.76 ? 40  ASP C OD2 1 
ATOM   4660 N  N   . ALA C  1 41  ? 40.903  -12.331 -52.566 1.00 21.23 ? 41  ALA C N   1 
ATOM   4661 C  CA  . ALA C  1 41  ? 42.260  -13.000 -52.569 1.00 21.07 ? 41  ALA C CA  1 
ATOM   4662 C  C   . ALA C  1 41  ? 43.394  -12.093 -52.187 1.00 21.67 ? 41  ALA C C   1 
ATOM   4663 O  O   . ALA C  1 41  ? 44.472  -12.543 -51.780 1.00 21.82 ? 41  ALA C O   1 
ATOM   4664 C  CB  . ALA C  1 41  ? 42.514  -13.517 -53.987 1.00 24.05 ? 41  ALA C CB  1 
ATOM   4665 N  N   . SER C  1 42  ? 43.224  -10.773 -52.357 1.00 21.83 ? 42  SER C N   1 
ATOM   4666 C  CA  . SER C  1 42  ? 44.234  -9.838  -51.977 1.00 19.80 ? 42  SER C CA  1 
ATOM   4667 C  C   . SER C  1 42  ? 44.483  -9.771  -50.439 1.00 20.22 ? 42  SER C C   1 
ATOM   4668 O  O   . SER C  1 42  ? 45.498  -9.095  -49.991 1.00 22.43 ? 42  SER C O   1 
ATOM   4669 C  CB  . SER C  1 42  ? 43.933  -8.454  -52.506 1.00 23.67 ? 42  SER C CB  1 
ATOM   4670 O  OG  . SER C  1 42  ? 42.977  -7.744  -51.658 1.00 23.64 ? 42  SER C OG  1 
ATOM   4671 N  N   . LEU C  1 43  ? 43.547  -10.378 -49.669 1.00 18.29 ? 43  LEU C N   1 
ATOM   4672 C  CA  . LEU C  1 43  ? 43.608  -10.206 -48.223 1.00 19.30 ? 43  LEU C CA  1 
ATOM   4673 C  C   . LEU C  1 43  ? 44.485  -11.258 -47.553 1.00 19.20 ? 43  LEU C C   1 
ATOM   4674 O  O   . LEU C  1 43  ? 43.984  -12.231 -46.938 1.00 20.39 ? 43  LEU C O   1 
ATOM   4675 C  CB  . LEU C  1 43  ? 42.183  -10.179 -47.623 1.00 16.24 ? 43  LEU C CB  1 
ATOM   4676 C  CG  . LEU C  1 43  ? 41.314  -9.019  -48.142 1.00 14.96 ? 43  LEU C CG  1 
ATOM   4677 C  CD1 . LEU C  1 43  ? 39.892  -9.092  -47.531 1.00 16.80 ? 43  LEU C CD1 1 
ATOM   4678 C  CD2 . LEU C  1 43  ? 41.945  -7.658  -47.993 1.00 16.66 ? 43  LEU C CD2 1 
ATOM   4679 N  N   . THR C  1 44  ? 45.801  -11.057 -47.667 1.00 22.05 ? 44  THR C N   1 
ATOM   4680 C  CA  . THR C  1 44  ? 46.754  -12.034 -47.140 1.00 22.52 ? 44  THR C CA  1 
ATOM   4681 C  C   . THR C  1 44  ? 47.006  -11.677 -45.665 1.00 24.76 ? 44  THR C C   1 
ATOM   4682 O  O   . THR C  1 44  ? 46.506  -10.643 -45.165 1.00 21.13 ? 44  THR C O   1 
ATOM   4683 C  CB  . THR C  1 44  ? 48.023  -11.910 -47.987 1.00 25.66 ? 44  THR C CB  1 
ATOM   4684 O  OG1 . THR C  1 44  ? 48.387  -10.526 -48.082 1.00 25.62 ? 44  THR C OG1 1 
ATOM   4685 C  CG2 . THR C  1 44  ? 47.787  -12.454 -49.411 1.00 27.62 ? 44  THR C CG2 1 
ATOM   4686 N  N   . PRO C  1 45  ? 47.761  -12.486 -44.923 1.00 22.35 ? 45  PRO C N   1 
ATOM   4687 C  CA  . PRO C  1 45  ? 47.910  -12.161 -43.473 1.00 23.32 ? 45  PRO C CA  1 
ATOM   4688 C  C   . PRO C  1 45  ? 48.718  -10.912 -43.214 1.00 24.75 ? 45  PRO C C   1 
ATOM   4689 O  O   . PRO C  1 45  ? 49.713  -10.660 -43.869 1.00 26.10 ? 45  PRO C O   1 
ATOM   4690 C  CB  . PRO C  1 45  ? 48.633  -13.378 -42.923 1.00 25.72 ? 45  PRO C CB  1 
ATOM   4691 C  CG  . PRO C  1 45  ? 48.328  -14.493 -43.926 1.00 23.98 ? 45  PRO C CG  1 
ATOM   4692 C  CD  . PRO C  1 45  ? 48.210  -13.858 -45.273 1.00 23.78 ? 45  PRO C CD  1 
ATOM   4693 N  N   . LEU C  1 46  ? 48.321  -10.114 -42.222 1.00 18.87 ? 46  LEU C N   1 
ATOM   4694 C  CA  . LEU C  1 46  ? 49.099  -9.001  -41.783 1.00 21.13 ? 46  LEU C CA  1 
ATOM   4695 C  C   . LEU C  1 46  ? 50.212  -9.564  -40.883 1.00 21.16 ? 46  LEU C C   1 
ATOM   4696 O  O   . LEU C  1 46  ? 50.044  -10.640 -40.314 1.00 23.97 ? 46  LEU C O   1 
ATOM   4697 C  CB  . LEU C  1 46  ? 48.171  -8.139  -40.942 1.00 21.92 ? 46  LEU C CB  1 
ATOM   4698 C  CG  . LEU C  1 46  ? 47.013  -7.521  -41.728 1.00 24.10 ? 46  LEU C CG  1 
ATOM   4699 C  CD1 . LEU C  1 46  ? 46.156  -6.736  -40.759 1.00 25.72 ? 46  LEU C CD1 1 
ATOM   4700 C  CD2 . LEU C  1 46  ? 47.523  -6.698  -42.928 1.00 27.32 ? 46  LEU C CD2 1 
ATOM   4701 N  N   . GLU C  1 47  ? 51.299  -8.810  -40.801 1.00 23.27 ? 47  GLU C N   1 
ATOM   4702 C  CA  . GLU C  1 47  ? 52.344  -9.086  -39.779 1.00 24.18 ? 47  GLU C CA  1 
ATOM   4703 C  C   . GLU C  1 47  ? 52.398  -7.967  -38.767 1.00 23.35 ? 47  GLU C C   1 
ATOM   4704 O  O   . GLU C  1 47  ? 52.372  -6.769  -39.128 1.00 22.61 ? 47  GLU C O   1 
ATOM   4705 C  CB  . GLU C  1 47  ? 53.696  -9.240  -40.476 1.00 28.67 ? 47  GLU C CB  1 
ATOM   4706 C  CG  . GLU C  1 47  ? 53.624  -10.287 -41.580 1.00 39.63 ? 47  GLU C CG  1 
ATOM   4707 N  N   . PHE C  1 48  ? 52.559  -8.353  -37.502 1.00 20.80 ? 48  PHE C N   1 
ATOM   4708 C  CA  . PHE C  1 48  ? 52.538  -7.421  -36.386 1.00 22.48 ? 48  PHE C CA  1 
ATOM   4709 C  C   . PHE C  1 48  ? 53.948  -7.268  -35.894 1.00 23.09 ? 48  PHE C C   1 
ATOM   4710 O  O   . PHE C  1 48  ? 54.443  -8.182  -35.220 1.00 29.19 ? 48  PHE C O   1 
ATOM   4711 C  CB  . PHE C  1 48  ? 51.512  -7.892  -35.298 1.00 24.69 ? 48  PHE C CB  1 
ATOM   4712 C  CG  . PHE C  1 48  ? 50.196  -8.305  -35.926 1.00 23.71 ? 48  PHE C CG  1 
ATOM   4713 C  CD1 . PHE C  1 48  ? 49.349  -7.332  -36.416 1.00 25.67 ? 48  PHE C CD1 1 
ATOM   4714 C  CD2 . PHE C  1 48  ? 49.862  -9.644  -36.103 1.00 23.97 ? 48  PHE C CD2 1 
ATOM   4715 C  CE1 . PHE C  1 48  ? 48.179  -7.706  -37.044 1.00 22.83 ? 48  PHE C CE1 1 
ATOM   4716 C  CE2 . PHE C  1 48  ? 48.703  -10.002 -36.732 1.00 25.61 ? 48  PHE C CE2 1 
ATOM   4717 C  CZ  . PHE C  1 48  ? 47.855  -9.003  -37.213 1.00 20.57 ? 48  PHE C CZ  1 
ATOM   4718 N  N   . GLN C  1 49  ? 54.514  -6.085  -36.154 1.00 20.56 ? 49  GLN C N   1 
ATOM   4719 C  CA  . GLN C  1 49  ? 55.976  -5.797  -35.869 1.00 22.57 ? 49  GLN C CA  1 
ATOM   4720 C  C   . GLN C  1 49  ? 56.156  -4.897  -34.694 1.00 23.26 ? 49  GLN C C   1 
ATOM   4721 O  O   . GLN C  1 49  ? 55.520  -3.906  -34.570 1.00 20.56 ? 49  GLN C O   1 
ATOM   4722 C  CB  . GLN C  1 49  ? 56.614  -5.243  -37.136 1.00 27.35 ? 49  GLN C CB  1 
ATOM   4723 C  CG  . GLN C  1 49  ? 56.561  -6.342  -38.159 1.00 30.56 ? 49  GLN C CG  1 
ATOM   4724 C  CD  . GLN C  1 49  ? 57.367  -6.117  -39.408 1.00 44.80 ? 49  GLN C CD  1 
ATOM   4725 N  N   . GLY C  1 50  ? 57.081  -5.256  -33.781 1.00 20.77 ? 50  GLY C N   1 
ATOM   4726 C  CA  . GLY C  1 50  ? 57.386  -4.357  -32.713 1.00 22.82 ? 50  GLY C CA  1 
ATOM   4727 C  C   . GLY C  1 50  ? 56.297  -4.418  -31.666 1.00 19.38 ? 50  GLY C C   1 
ATOM   4728 O  O   . GLY C  1 50  ? 56.232  -3.527  -30.811 1.00 24.15 ? 50  GLY C O   1 
ATOM   4729 N  N   . TYR C  1 51  ? 55.422  -5.430  -31.704 1.00 21.77 ? 51  TYR C N   1 
ATOM   4730 C  CA  . TYR C  1 51  ? 54.323  -5.508  -30.703 1.00 21.89 ? 51  TYR C CA  1 
ATOM   4731 C  C   . TYR C  1 51  ? 54.749  -5.974  -29.342 1.00 21.79 ? 51  TYR C C   1 
ATOM   4732 O  O   . TYR C  1 51  ? 54.045  -5.838  -28.355 1.00 19.62 ? 51  TYR C O   1 
ATOM   4733 C  CB  . TYR C  1 51  ? 53.180  -6.397  -31.225 1.00 20.71 ? 51  TYR C CB  1 
ATOM   4734 C  CG  . TYR C  1 51  ? 52.137  -5.720  -32.111 1.00 19.43 ? 51  TYR C CG  1 
ATOM   4735 C  CD1 . TYR C  1 51  ? 52.502  -4.851  -33.135 1.00 19.81 ? 51  TYR C CD1 1 
ATOM   4736 C  CD2 . TYR C  1 51  ? 50.782  -5.986  -31.938 1.00 17.46 ? 51  TYR C CD2 1 
ATOM   4737 C  CE1 . TYR C  1 51  ? 51.545  -4.255  -33.945 1.00 19.59 ? 51  TYR C CE1 1 
ATOM   4738 C  CE2 . TYR C  1 51  ? 49.821  -5.397  -32.741 1.00 20.59 ? 51  TYR C CE2 1 
ATOM   4739 C  CZ  . TYR C  1 51  ? 50.205  -4.533  -33.744 1.00 20.69 ? 51  TYR C CZ  1 
ATOM   4740 O  OH  . TYR C  1 51  ? 49.245  -3.947  -34.542 1.00 20.84 ? 51  TYR C OH  1 
ATOM   4741 N  N   . ASN C  1 52  ? 55.960  -6.555  -29.290 1.00 23.28 ? 52  ASN C N   1 
ATOM   4742 C  CA  . ASN C  1 52  ? 56.413  -7.131  -28.000 1.00 29.25 ? 52  ASN C CA  1 
ATOM   4743 C  C   . ASN C  1 52  ? 57.122  -6.046  -27.214 1.00 30.62 ? 52  ASN C C   1 
ATOM   4744 O  O   . ASN C  1 52  ? 58.318  -5.847  -27.398 1.00 32.30 ? 52  ASN C O   1 
ATOM   4745 C  CB  . ASN C  1 52  ? 57.357  -8.317  -28.279 1.00 28.93 ? 52  ASN C CB  1 
ATOM   4746 C  CG  . ASN C  1 52  ? 57.416  -9.292  -27.155 1.00 32.17 ? 52  ASN C CG  1 
ATOM   4747 O  OD1 . ASN C  1 52  ? 57.015  -9.014  -26.009 1.00 29.92 ? 52  ASN C OD1 1 
ATOM   4748 N  ND2 . ASN C  1 52  ? 57.824  -10.501 -27.494 1.00 40.39 ? 52  ASN C ND2 1 
ATOM   4749 N  N   . LEU C  1 53  ? 56.378  -5.339  -26.367 1.00 26.92 ? 53  LEU C N   1 
ATOM   4750 C  CA  . LEU C  1 53  ? 56.923  -4.166  -25.661 1.00 31.15 ? 53  LEU C CA  1 
ATOM   4751 C  C   . LEU C  1 53  ? 57.639  -4.652  -24.354 1.00 31.24 ? 53  LEU C C   1 
ATOM   4752 O  O   . LEU C  1 53  ? 57.091  -5.498  -23.616 1.00 27.86 ? 53  LEU C O   1 
ATOM   4753 C  CB  . LEU C  1 53  ? 55.832  -3.147  -25.394 1.00 26.14 ? 53  LEU C CB  1 
ATOM   4754 C  CG  . LEU C  1 53  ? 54.782  -2.778  -26.506 1.00 27.66 ? 53  LEU C CG  1 
ATOM   4755 C  CD1 . LEU C  1 53  ? 53.756  -1.851  -25.883 1.00 26.44 ? 53  LEU C CD1 1 
ATOM   4756 C  CD2 . LEU C  1 53  ? 55.388  -2.014  -27.669 1.00 27.76 ? 53  LEU C CD2 1 
ATOM   4757 N  N   . SER C  1 54  ? 58.827  -4.088  -24.052 1.00 39.50 ? 54  SER C N   1 
ATOM   4758 C  CA  . SER C  1 54  ? 59.635  -4.499  -22.864 1.00 40.81 ? 54  SER C CA  1 
ATOM   4759 C  C   . SER C  1 54  ? 58.916  -4.252  -21.517 1.00 41.60 ? 54  SER C C   1 
ATOM   4760 O  O   . SER C  1 54  ? 58.347  -3.168  -21.310 1.00 34.11 ? 54  SER C O   1 
ATOM   4761 C  CB  . SER C  1 54  ? 61.003  -3.796  -22.863 1.00 45.95 ? 54  SER C CB  1 
ATOM   4762 O  OG  . SER C  1 54  ? 61.421  -3.486  -24.189 1.00 46.47 ? 54  SER C OG  1 
ATOM   4763 N  N   . ALA C  1 55  ? 58.930  -5.237  -20.611 1.00 42.75 ? 55  ALA C N   1 
ATOM   4764 C  CA  . ALA C  1 55  ? 58.216  -5.097  -19.303 1.00 44.48 ? 55  ALA C CA  1 
ATOM   4765 C  C   . ALA C  1 55  ? 58.793  -3.982  -18.420 1.00 47.55 ? 55  ALA C C   1 
ATOM   4766 O  O   . ALA C  1 55  ? 58.139  -3.544  -17.436 1.00 44.38 ? 55  ALA C O   1 
ATOM   4767 C  CB  . ALA C  1 55  ? 58.158  -6.409  -18.520 1.00 41.41 ? 55  ALA C CB  1 
ATOM   4768 N  N   . ASN C  1 56  ? 59.987  -3.506  -18.781 1.00 46.65 ? 56  ASN C N   1 
ATOM   4769 C  CA  . ASN C  1 56  ? 60.668  -2.483  -17.978 1.00 51.41 ? 56  ASN C CA  1 
ATOM   4770 C  C   . ASN C  1 56  ? 60.492  -1.100  -18.604 1.00 49.26 ? 56  ASN C C   1 
ATOM   4771 O  O   . ASN C  1 56  ? 60.847  -0.081  -17.987 1.00 39.59 ? 56  ASN C O   1 
ATOM   4772 N  N   . LYS C  1 57  ? 59.920  -1.094  -19.826 1.00 44.41 ? 57  LYS C N   1 
ATOM   4773 C  CA  . LYS C  1 57  ? 59.414  0.109   -20.502 1.00 43.46 ? 57  LYS C CA  1 
ATOM   4774 C  C   . LYS C  1 57  ? 57.980  0.356   -20.038 1.00 30.82 ? 57  LYS C C   1 
ATOM   4775 O  O   . LYS C  1 57  ? 57.300  -0.555  -19.530 1.00 33.20 ? 57  LYS C O   1 
ATOM   4776 C  CB  . LYS C  1 57  ? 59.435  -0.059  -22.019 1.00 49.56 ? 57  LYS C CB  1 
ATOM   4777 C  CG  . LYS C  1 57  ? 60.702  0.413   -22.692 1.00 53.90 ? 57  LYS C CG  1 
ATOM   4778 N  N   . GLN C  1 58  ? 57.526  1.618   -20.074 1.00 31.67 ? 58  GLN C N   1 
ATOM   4779 C  CA  . GLN C  1 58  ? 56.164  1.892   -19.660 1.00 29.36 ? 58  GLN C CA  1 
ATOM   4780 C  C   . GLN C  1 58  ? 55.400  2.834   -20.638 1.00 25.94 ? 58  GLN C C   1 
ATOM   4781 O  O   . GLN C  1 58  ? 56.014  3.629   -21.347 1.00 23.30 ? 58  GLN C O   1 
ATOM   4782 C  CB  . GLN C  1 58  ? 56.077  2.403   -18.175 1.00 27.37 ? 58  GLN C CB  1 
ATOM   4783 C  CG  . GLN C  1 58  ? 56.460  3.865   -18.024 1.00 27.55 ? 58  GLN C CG  1 
ATOM   4784 C  CD  . GLN C  1 58  ? 56.469  4.405   -16.577 1.00 23.94 ? 58  GLN C CD  1 
ATOM   4785 O  OE1 . GLN C  1 58  ? 56.039  3.723   -15.611 1.00 29.51 ? 58  GLN C OE1 1 
ATOM   4786 N  NE2 . GLN C  1 58  ? 56.831  5.664   -16.438 1.00 27.05 ? 58  GLN C NE2 1 
ATOM   4787 N  N   . PHE C  1 59  ? 54.045  2.765   -20.537 1.00 26.99 ? 59  PHE C N   1 
ATOM   4788 C  CA  . PHE C  1 59  ? 53.057  3.290   -21.535 1.00 22.44 ? 59  PHE C CA  1 
ATOM   4789 C  C   . PHE C  1 59  ? 51.933  3.988   -20.832 1.00 19.76 ? 59  PHE C C   1 
ATOM   4790 O  O   . PHE C  1 59  ? 51.358  3.431   -19.867 1.00 24.01 ? 59  PHE C O   1 
ATOM   4791 C  CB  . PHE C  1 59  ? 52.664  2.117   -22.490 1.00 23.26 ? 59  PHE C CB  1 
ATOM   4792 C  CG  . PHE C  1 59  ? 53.866  1.510   -23.132 1.00 22.26 ? 59  PHE C CG  1 
ATOM   4793 C  CD1 . PHE C  1 59  ? 54.429  2.116   -24.241 1.00 21.30 ? 59  PHE C CD1 1 
ATOM   4794 C  CD2 . PHE C  1 59  ? 54.536  0.414   -22.520 1.00 22.02 ? 59  PHE C CD2 1 
ATOM   4795 C  CE1 . PHE C  1 59  ? 55.624  1.625   -24.784 1.00 25.13 ? 59  PHE C CE1 1 
ATOM   4796 C  CE2 . PHE C  1 59  ? 55.715  -0.081  -23.058 1.00 23.17 ? 59  PHE C CE2 1 
ATOM   4797 C  CZ  . PHE C  1 59  ? 56.262  0.548   -24.151 1.00 22.09 ? 59  PHE C CZ  1 
ATOM   4798 N  N   . LEU C  1 60  ? 51.626  5.221   -21.269 1.00 18.40 ? 60  LEU C N   1 
ATOM   4799 C  CA  . LEU C  1 60  ? 50.677  6.081   -20.590 1.00 18.93 ? 60  LEU C CA  1 
ATOM   4800 C  C   . LEU C  1 60  ? 49.231  5.555   -20.865 1.00 19.97 ? 60  LEU C C   1 
ATOM   4801 O  O   . LEU C  1 60  ? 48.808  5.427   -22.052 1.00 21.02 ? 60  LEU C O   1 
ATOM   4802 C  CB  . LEU C  1 60  ? 50.835  7.489   -21.158 1.00 17.60 ? 60  LEU C CB  1 
ATOM   4803 C  CG  . LEU C  1 60  ? 50.058  8.575   -20.396 1.00 20.80 ? 60  LEU C CG  1 
ATOM   4804 C  CD1 . LEU C  1 60  ? 50.547  8.681   -18.921 1.00 22.21 ? 60  LEU C CD1 1 
ATOM   4805 C  CD2 . LEU C  1 60  ? 50.115  9.911   -21.120 1.00 21.75 ? 60  LEU C CD2 1 
ATOM   4806 N  N   . LEU C  1 61  ? 48.552  5.188   -19.804 1.00 21.78 ? 61  LEU C N   1 
ATOM   4807 C  CA  . LEU C  1 61  ? 47.125  4.906   -19.751 1.00 20.79 ? 61  LEU C CA  1 
ATOM   4808 C  C   . LEU C  1 61  ? 46.369  6.149   -19.306 1.00 22.97 ? 61  LEU C C   1 
ATOM   4809 O  O   . LEU C  1 61  ? 46.706  6.729   -18.243 1.00 23.04 ? 61  LEU C O   1 
ATOM   4810 C  CB  . LEU C  1 61  ? 46.928  3.830   -18.710 1.00 21.67 ? 61  LEU C CB  1 
ATOM   4811 C  CG  . LEU C  1 61  ? 45.548  3.160   -18.736 1.00 21.60 ? 61  LEU C CG  1 
ATOM   4812 C  CD1 . LEU C  1 61  ? 45.501  2.217   -19.936 1.00 24.91 ? 61  LEU C CD1 1 
ATOM   4813 C  CD2 . LEU C  1 61  ? 45.442  2.337   -17.416 1.00 26.08 ? 61  LEU C CD2 1 
ATOM   4814 N  N   . THR C  1 62  ? 45.300  6.519   -19.990 1.00 18.18 ? 62  THR C N   1 
ATOM   4815 C  CA  . THR C  1 62  ? 44.587  7.757   -19.753 1.00 18.62 ? 62  THR C CA  1 
ATOM   4816 C  C   . THR C  1 62  ? 43.090  7.450   -19.833 1.00 23.44 ? 62  THR C C   1 
ATOM   4817 O  O   . THR C  1 62  ? 42.595  6.825   -20.777 1.00 20.65 ? 62  THR C O   1 
ATOM   4818 C  CB  . THR C  1 62  ? 44.766  8.800   -20.847 1.00 21.01 ? 62  THR C CB  1 
ATOM   4819 O  OG1 . THR C  1 62  ? 46.137  9.181   -20.957 1.00 22.47 ? 62  THR C OG1 1 
ATOM   4820 C  CG2 . THR C  1 62  ? 43.916  10.100  -20.543 1.00 24.67 ? 62  THR C CG2 1 
ATOM   4821 N  N   . ASN C  1 63  ? 42.368  7.861   -18.823 1.00 21.54 ? 63  ASN C N   1 
ATOM   4822 C  CA  . ASN C  1 63  ? 40.954  8.036   -18.973 1.00 18.47 ? 63  ASN C CA  1 
ATOM   4823 C  C   . ASN C  1 63  ? 40.684  9.357   -19.612 1.00 22.36 ? 63  ASN C C   1 
ATOM   4824 O  O   . ASN C  1 63  ? 40.911  10.374  -18.996 1.00 22.06 ? 63  ASN C O   1 
ATOM   4825 C  CB  . ASN C  1 63  ? 40.379  7.929   -17.548 1.00 19.18 ? 63  ASN C CB  1 
ATOM   4826 C  CG  . ASN C  1 63  ? 38.847  8.125   -17.498 1.00 20.42 ? 63  ASN C CG  1 
ATOM   4827 O  OD1 . ASN C  1 63  ? 38.243  8.788   -18.366 1.00 20.66 ? 63  ASN C OD1 1 
ATOM   4828 N  ND2 . ASN C  1 63  ? 38.246  7.706   -16.384 1.00 16.50 ? 63  ASN C ND2 1 
ATOM   4829 N  N   . ASN C  1 64  ? 40.257  9.323   -20.880 1.00 22.97 ? 64  ASN C N   1 
ATOM   4830 C  CA  . ASN C  1 64  ? 39.950  10.502  -21.592 1.00 23.62 ? 64  ASN C CA  1 
ATOM   4831 C  C   . ASN C  1 64  ? 38.529  10.941  -21.496 1.00 21.76 ? 64  ASN C C   1 
ATOM   4832 O  O   . ASN C  1 64  ? 38.106  11.873  -22.269 1.00 25.60 ? 64  ASN C O   1 
ATOM   4833 C  CB  . ASN C  1 64  ? 40.438  10.397  -23.032 1.00 21.10 ? 64  ASN C CB  1 
ATOM   4834 C  CG  . ASN C  1 64  ? 39.699  9.371   -23.830 1.00 23.20 ? 64  ASN C CG  1 
ATOM   4835 O  OD1 . ASN C  1 64  ? 38.596  8.905   -23.444 1.00 23.81 ? 64  ASN C OD1 1 
ATOM   4836 N  ND2 . ASN C  1 64  ? 40.310  8.937   -24.947 1.00 26.79 ? 64  ASN C ND2 1 
ATOM   4837 N  N   . GLY C  1 65  ? 37.756  10.337  -20.583 1.00 19.87 ? 65  GLY C N   1 
ATOM   4838 C  CA  . GLY C  1 65  ? 36.335  10.670  -20.445 1.00 22.72 ? 65  GLY C CA  1 
ATOM   4839 C  C   . GLY C  1 65  ? 35.457  9.893   -21.414 1.00 23.76 ? 65  GLY C C   1 
ATOM   4840 O  O   . GLY C  1 65  ? 34.255  10.036  -21.315 1.00 25.27 ? 65  GLY C O   1 
ATOM   4841 N  N   . HIS C  1 66  ? 36.059  9.169   -22.365 1.00 21.10 ? 66  HIS C N   1 
ATOM   4842 C  CA  . HIS C  1 66  ? 35.271  8.469   -23.421 1.00 21.03 ? 66  HIS C CA  1 
ATOM   4843 C  C   . HIS C  1 66  ? 35.602  7.030   -23.415 1.00 20.13 ? 66  HIS C C   1 
ATOM   4844 O  O   . HIS C  1 66  ? 34.777  6.196   -23.798 1.00 20.97 ? 66  HIS C O   1 
ATOM   4845 C  CB  . HIS C  1 66  ? 35.571  9.071   -24.786 1.00 20.36 ? 66  HIS C CB  1 
ATOM   4846 C  CG  . HIS C  1 66  ? 35.362  10.568  -24.832 1.00 22.16 ? 66  HIS C CG  1 
ATOM   4847 N  ND1 . HIS C  1 66  ? 36.379  11.440  -25.101 1.00 22.94 ? 66  HIS C ND1 1 
ATOM   4848 C  CD2 . HIS C  1 66  ? 34.205  11.326  -24.738 1.00 20.09 ? 66  HIS C CD2 1 
ATOM   4849 C  CE1 . HIS C  1 66  ? 35.875  12.714  -25.138 1.00 22.60 ? 66  HIS C CE1 1 
ATOM   4850 N  NE2 . HIS C  1 66  ? 34.562  12.644  -24.880 1.00 24.46 ? 66  HIS C NE2 1 
ATOM   4851 N  N   . SER C  1 67  ? 36.810  6.698   -23.042 1.00 20.11 ? 67  SER C N   1 
ATOM   4852 C  CA  . SER C  1 67  ? 37.329  5.389   -22.969 1.00 17.45 ? 67  SER C CA  1 
ATOM   4853 C  C   . SER C  1 67  ? 38.569  5.428   -22.063 1.00 19.99 ? 67  SER C C   1 
ATOM   4854 O  O   . SER C  1 67  ? 38.886  6.484   -21.464 1.00 19.77 ? 67  SER C O   1 
ATOM   4855 C  CB  . SER C  1 67  ? 37.693  4.896   -24.420 1.00 18.70 ? 67  SER C CB  1 
ATOM   4856 O  OG  . SER C  1 67  ? 38.128  3.568   -24.476 1.00 19.97 ? 67  SER C OG  1 
ATOM   4857 N  N   . VAL C  1 68  ? 39.204  4.278   -21.969 1.00 18.08 ? 68  VAL C N   1 
ATOM   4858 C  CA  . VAL C  1 68  ? 40.551  4.176   -21.407 1.00 18.36 ? 68  VAL C CA  1 
ATOM   4859 C  C   . VAL C  1 68  ? 41.452  3.828   -22.583 1.00 19.69 ? 68  VAL C C   1 
ATOM   4860 O  O   . VAL C  1 68  ? 41.155  2.866   -23.335 1.00 18.28 ? 68  VAL C O   1 
ATOM   4861 C  CB  . VAL C  1 68  ? 40.564  3.220   -20.207 1.00 19.57 ? 68  VAL C CB  1 
ATOM   4862 C  CG1 . VAL C  1 68  ? 40.361  1.767   -20.627 1.00 19.54 ? 68  VAL C CG1 1 
ATOM   4863 C  CG2 . VAL C  1 68  ? 41.923  3.306   -19.520 1.00 21.93 ? 68  VAL C CG2 1 
ATOM   4864 N  N   . LYS C  1 69  ? 42.527  4.579   -22.744 1.00 19.03 ? 69  LYS C N   1 
ATOM   4865 C  CA  . LYS C  1 69  ? 43.429  4.402   -23.885 1.00 18.25 ? 69  LYS C CA  1 
ATOM   4866 C  C   . LYS C  1 69  ? 44.837  4.236   -23.350 1.00 23.57 ? 69  LYS C C   1 
ATOM   4867 O  O   . LYS C  1 69  ? 45.217  4.784   -22.307 1.00 23.59 ? 69  LYS C O   1 
ATOM   4868 C  CB  . LYS C  1 69  ? 43.321  5.589   -24.811 1.00 23.83 ? 69  LYS C CB  1 
ATOM   4869 C  CG  . LYS C  1 69  ? 43.997  6.853   -24.404 1.00 26.30 ? 69  LYS C CG  1 
ATOM   4870 C  CD  . LYS C  1 69  ? 44.077  7.848   -25.562 1.00 27.85 ? 69  LYS C CD  1 
ATOM   4871 C  CE  . LYS C  1 69  ? 44.412  9.199   -24.962 1.00 32.22 ? 69  LYS C CE  1 
ATOM   4872 N  NZ  . LYS C  1 69  ? 44.635  10.230  -26.011 1.00 26.95 ? 69  LYS C NZ  1 
ATOM   4873 N  N   . LEU C  1 70  ? 45.559  3.389   -24.005 1.00 17.16 ? 70  LEU C N   1 
ATOM   4874 C  CA  . LEU C  1 70  ? 46.973  3.193   -23.789 1.00 19.02 ? 70  LEU C CA  1 
ATOM   4875 C  C   . LEU C  1 70  ? 47.735  3.760   -24.969 1.00 18.23 ? 70  LEU C C   1 
ATOM   4876 O  O   . LEU C  1 70  ? 47.560  3.320   -26.121 1.00 20.15 ? 70  LEU C O   1 
ATOM   4877 C  CB  . LEU C  1 70  ? 47.208  1.686   -23.668 1.00 17.99 ? 70  LEU C CB  1 
ATOM   4878 C  CG  . LEU C  1 70  ? 48.634  1.221   -23.297 1.00 22.62 ? 70  LEU C CG  1 
ATOM   4879 C  CD1 . LEU C  1 70  ? 48.980  1.615   -21.858 1.00 22.62 ? 70  LEU C CD1 1 
ATOM   4880 C  CD2 . LEU C  1 70  ? 48.748  -0.284  -23.496 1.00 19.36 ? 70  LEU C CD2 1 
ATOM   4881 N  N   . ASN C  1 71  ? 48.639  4.716   -24.736 1.00 18.86 ? 71  ASN C N   1 
ATOM   4882 C  CA  . ASN C  1 71  ? 49.498  5.177   -25.785 1.00 20.62 ? 71  ASN C CA  1 
ATOM   4883 C  C   . ASN C  1 71  ? 50.486  4.060   -26.210 1.00 18.20 ? 71  ASN C C   1 
ATOM   4884 O  O   . ASN C  1 71  ? 50.957  3.213   -25.375 1.00 21.17 ? 71  ASN C O   1 
ATOM   4885 C  CB  . ASN C  1 71  ? 50.267  6.409   -25.294 1.00 19.26 ? 71  ASN C CB  1 
ATOM   4886 C  CG  . ASN C  1 71  ? 49.410  7.620   -25.211 1.00 27.69 ? 71  ASN C CG  1 
ATOM   4887 O  OD1 . ASN C  1 71  ? 48.235  7.623   -25.591 1.00 26.57 ? 71  ASN C OD1 1 
ATOM   4888 N  ND2 . ASN C  1 71  ? 50.028  8.733   -24.738 1.00 29.66 ? 71  ASN C ND2 1 
ATOM   4889 N  N   . LEU C  1 72  ? 50.773  3.954   -27.537 1.00 16.45 ? 72  LEU C N   1 
ATOM   4890 C  CA  . LEU C  1 72  ? 51.587  2.900   -28.034 1.00 16.75 ? 72  LEU C CA  1 
ATOM   4891 C  C   . LEU C  1 72  ? 52.775  3.494   -28.852 1.00 17.02 ? 72  LEU C C   1 
ATOM   4892 O  O   . LEU C  1 72  ? 52.635  4.626   -29.410 1.00 18.01 ? 72  LEU C O   1 
ATOM   4893 C  CB  . LEU C  1 72  ? 50.754  2.087   -29.020 1.00 18.06 ? 72  LEU C CB  1 
ATOM   4894 C  CG  . LEU C  1 72  ? 49.733  1.164   -28.283 1.00 18.07 ? 72  LEU C CG  1 
ATOM   4895 C  CD1 . LEU C  1 72  ? 48.911  0.433   -29.399 1.00 19.20 ? 72  LEU C CD1 1 
ATOM   4896 C  CD2 . LEU C  1 72  ? 50.346  0.109   -27.317 1.00 22.49 ? 72  LEU C CD2 1 
ATOM   4897 N  N   . PRO C  1 73  ? 53.942  2.848   -28.932 1.00 21.25 ? 73  PRO C N   1 
ATOM   4898 C  CA  . PRO C  1 73  ? 55.024  3.572   -29.554 1.00 20.95 ? 73  PRO C CA  1 
ATOM   4899 C  C   . PRO C  1 73  ? 55.124  3.446   -31.087 1.00 22.79 ? 73  PRO C C   1 
ATOM   4900 O  O   . PRO C  1 73  ? 54.691  2.430   -31.612 1.00 24.45 ? 73  PRO C O   1 
ATOM   4901 C  CB  . PRO C  1 73  ? 56.266  2.913   -28.849 1.00 20.90 ? 73  PRO C CB  1 
ATOM   4902 C  CG  . PRO C  1 73  ? 55.901  1.394   -28.749 1.00 20.84 ? 73  PRO C CG  1 
ATOM   4903 C  CD  . PRO C  1 73  ? 54.366  1.458   -28.541 1.00 19.06 ? 73  PRO C CD  1 
ATOM   4904 N  N   . SER C  1 74  ? 55.602  4.482   -31.784 1.00 26.36 ? 74  SER C N   1 
ATOM   4905 C  CA  . SER C  1 74  ? 55.507  4.471   -33.264 1.00 25.74 ? 74  SER C CA  1 
ATOM   4906 C  C   . SER C  1 74  ? 56.388  3.438   -33.999 1.00 28.29 ? 74  SER C C   1 
ATOM   4907 O  O   . SER C  1 74  ? 56.208  3.189   -35.184 1.00 28.79 ? 74  SER C O   1 
ATOM   4908 C  CB  . SER C  1 74  ? 55.666  5.895   -33.858 1.00 35.15 ? 74  SER C CB  1 
ATOM   4909 O  OG  . SER C  1 74  ? 56.944  6.427   -33.537 1.00 33.16 ? 74  SER C OG  1 
ATOM   4910 N  N   . ASP C  1 75  ? 57.351  2.815   -33.324 1.00 28.14 ? 75  ASP C N   1 
ATOM   4911 C  CA  . ASP C  1 75  ? 58.096  1.760   -33.971 1.00 26.97 ? 75  ASP C CA  1 
ATOM   4912 C  C   . ASP C  1 75  ? 57.290  0.421   -33.989 1.00 27.95 ? 75  ASP C C   1 
ATOM   4913 O  O   . ASP C  1 75  ? 57.663  -0.527  -34.657 1.00 28.44 ? 75  ASP C O   1 
ATOM   4914 C  CB  . ASP C  1 75  ? 59.465  1.594   -33.282 1.00 32.59 ? 75  ASP C CB  1 
ATOM   4915 C  CG  . ASP C  1 75  ? 59.305  1.119   -31.889 1.00 31.25 ? 75  ASP C CG  1 
ATOM   4916 O  OD1 . ASP C  1 75  ? 59.017  1.972   -31.000 1.00 34.68 ? 75  ASP C OD1 1 
ATOM   4917 O  OD2 . ASP C  1 75  ? 59.427  -0.105  -31.695 1.00 39.35 ? 75  ASP C OD2 1 
ATOM   4918 N  N   . MET C  1 76  ? 56.142  0.353   -33.318 1.00 23.24 ? 76  MET C N   1 
ATOM   4919 C  CA  . MET C  1 76  ? 55.204  -0.767  -33.470 1.00 19.97 ? 76  MET C CA  1 
ATOM   4920 C  C   . MET C  1 76  ? 54.374  -0.584  -34.762 1.00 18.54 ? 76  MET C C   1 
ATOM   4921 O  O   . MET C  1 76  ? 53.963  0.531   -34.972 1.00 20.12 ? 76  MET C O   1 
ATOM   4922 C  CB  . MET C  1 76  ? 54.265  -0.686  -32.284 1.00 22.64 ? 76  MET C CB  1 
ATOM   4923 C  CG  . MET C  1 76  ? 53.247  -1.766  -32.204 1.00 23.48 ? 76  MET C CG  1 
ATOM   4924 S  SD  . MET C  1 76  ? 52.422  -1.605  -30.597 1.00 24.02 ? 76  MET C SD  1 
ATOM   4925 C  CE  . MET C  1 76  ? 50.826  -2.339  -31.022 1.00 20.96 ? 76  MET C CE  1 
ATOM   4926 N  N   . HIS C  1 77  ? 54.323  -1.580  -35.620 1.00 18.48 ? 77  HIS C N   1 
ATOM   4927 C  CA  . HIS C  1 77  ? 53.639  -1.351  -36.927 1.00 19.99 ? 77  HIS C CA  1 
ATOM   4928 C  C   . HIS C  1 77  ? 53.071  -2.583  -37.531 1.00 18.83 ? 77  HIS C C   1 
ATOM   4929 O  O   . HIS C  1 77  ? 53.352  -3.705  -37.160 1.00 18.56 ? 77  HIS C O   1 
ATOM   4930 C  CB  . HIS C  1 77  ? 54.483  -0.552  -37.911 1.00 22.21 ? 77  HIS C CB  1 
ATOM   4931 C  CG  . HIS C  1 77  ? 55.696  -1.278  -38.346 1.00 24.37 ? 77  HIS C CG  1 
ATOM   4932 N  ND1 . HIS C  1 77  ? 56.902  -1.093  -37.757 1.00 25.36 ? 77  HIS C ND1 1 
ATOM   4933 C  CD2 . HIS C  1 77  ? 55.875  -2.252  -39.340 1.00 25.70 ? 77  HIS C CD2 1 
ATOM   4934 C  CE1 . HIS C  1 77  ? 57.805  -1.923  -38.330 1.00 24.07 ? 77  HIS C CE1 1 
ATOM   4935 N  NE2 . HIS C  1 77  ? 57.200  -2.601  -39.341 1.00 24.66 ? 77  HIS C NE2 1 
ATOM   4936 N  N   . ILE C  1 78  ? 52.128  -2.386  -38.472 1.00 19.54 ? 78  ILE C N   1 
ATOM   4937 C  CA  . ILE C  1 78  ? 51.570  -3.473  -39.221 1.00 19.07 ? 78  ILE C CA  1 
ATOM   4938 C  C   . ILE C  1 78  ? 52.282  -3.485  -40.578 1.00 19.43 ? 78  ILE C C   1 
ATOM   4939 O  O   . ILE C  1 78  ? 52.435  -2.442  -41.180 1.00 23.67 ? 78  ILE C O   1 
ATOM   4940 C  CB  . ILE C  1 78  ? 50.064  -3.130  -39.586 1.00 19.45 ? 78  ILE C CB  1 
ATOM   4941 C  CG1 . ILE C  1 78  ? 49.124  -3.076  -38.360 1.00 21.43 ? 78  ILE C CG1 1 
ATOM   4942 C  CG2 . ILE C  1 78  ? 49.534  -4.064  -40.654 1.00 20.80 ? 78  ILE C CG2 1 
ATOM   4943 C  CD1 . ILE C  1 78  ? 47.768  -2.379  -38.693 1.00 19.90 ? 78  ILE C CD1 1 
ATOM   4944 N  N   . GLN C  1 79  ? 52.677  -4.679  -41.020 1.00 22.36 ? 79  GLN C N   1 
ATOM   4945 C  CA  . GLN C  1 79  ? 53.290  -4.924  -42.294 1.00 27.33 ? 79  GLN C CA  1 
ATOM   4946 C  C   . GLN C  1 79  ? 52.298  -5.796  -43.062 1.00 24.01 ? 79  GLN C C   1 
ATOM   4947 O  O   . GLN C  1 79  ? 51.645  -6.698  -42.500 1.00 25.56 ? 79  GLN C O   1 
ATOM   4948 C  CB  . GLN C  1 79  ? 54.576  -5.706  -42.008 1.00 34.61 ? 79  GLN C CB  1 
ATOM   4949 C  CG  . GLN C  1 79  ? 55.187  -6.482  -43.167 1.00 48.11 ? 79  GLN C CG  1 
ATOM   4950 N  N   . GLY C  1 80  ? 52.198  -5.558  -44.348 1.00 24.88 ? 80  GLY C N   1 
ATOM   4951 C  CA  . GLY C  1 80  ? 51.220  -6.280  -45.130 1.00 27.82 ? 80  GLY C CA  1 
ATOM   4952 C  C   . GLY C  1 80  ? 50.266  -5.420  -45.922 1.00 27.68 ? 80  GLY C C   1 
ATOM   4953 O  O   . GLY C  1 80  ? 49.547  -5.951  -46.783 1.00 29.04 ? 80  GLY C O   1 
ATOM   4954 N  N   . LEU C  1 81  ? 50.181  -4.117  -45.604 1.00 26.34 ? 81  LEU C N   1 
ATOM   4955 C  CA  . LEU C  1 81  ? 49.234  -3.245  -46.269 1.00 26.39 ? 81  LEU C CA  1 
ATOM   4956 C  C   . LEU C  1 81  ? 50.020  -2.434  -47.336 1.00 27.34 ? 81  LEU C C   1 
ATOM   4957 O  O   . LEU C  1 81  ? 51.241  -2.580  -47.412 1.00 31.78 ? 81  LEU C O   1 
ATOM   4958 C  CB  . LEU C  1 81  ? 48.504  -2.333  -45.255 1.00 24.47 ? 81  LEU C CB  1 
ATOM   4959 C  CG  . LEU C  1 81  ? 47.569  -2.936  -44.204 1.00 23.53 ? 81  LEU C CG  1 
ATOM   4960 C  CD1 . LEU C  1 81  ? 47.160  -1.976  -43.071 1.00 23.37 ? 81  LEU C CD1 1 
ATOM   4961 C  CD2 . LEU C  1 81  ? 46.314  -3.433  -44.921 1.00 22.90 ? 81  LEU C CD2 1 
ATOM   4962 N  N   . GLN C  1 82  ? 49.346  -1.571  -48.099 1.00 30.80 ? 82  GLN C N   1 
ATOM   4963 C  CA  . GLN C  1 82  ? 50.007  -0.753  -49.153 1.00 33.17 ? 82  GLN C CA  1 
ATOM   4964 C  C   . GLN C  1 82  ? 51.073  0.197   -48.579 1.00 33.10 ? 82  GLN C C   1 
ATOM   4965 O  O   . GLN C  1 82  ? 52.102  0.446   -49.208 1.00 34.10 ? 82  GLN C O   1 
ATOM   4966 C  CB  . GLN C  1 82  ? 48.965  0.067   -49.964 1.00 40.82 ? 82  GLN C CB  1 
ATOM   4967 N  N   . SER C  1 83  ? 50.789  0.789   -47.414 1.00 26.25 ? 83  SER C N   1 
ATOM   4968 C  CA  . SER C  1 83  ? 51.746  1.611   -46.684 1.00 20.58 ? 83  SER C CA  1 
ATOM   4969 C  C   . SER C  1 83  ? 52.025  0.941   -45.367 1.00 20.49 ? 83  SER C C   1 
ATOM   4970 O  O   . SER C  1 83  ? 51.263  0.094   -44.920 1.00 18.59 ? 83  SER C O   1 
ATOM   4971 C  CB  . SER C  1 83  ? 51.221  2.986   -46.396 1.00 21.68 ? 83  SER C CB  1 
ATOM   4972 O  OG  . SER C  1 83  ? 50.877  3.666   -47.618 1.00 26.62 ? 83  SER C OG  1 
ATOM   4973 N  N   . ARG C  1 84  ? 53.082  1.380   -44.691 1.00 19.21 ? 84  ARG C N   1 
ATOM   4974 C  CA  . ARG C  1 84  ? 53.306  1.003   -43.324 1.00 17.70 ? 84  ARG C CA  1 
ATOM   4975 C  C   . ARG C  1 84  ? 52.392  1.842   -42.446 1.00 15.59 ? 84  ARG C C   1 
ATOM   4976 O  O   . ARG C  1 84  ? 52.297  3.069   -42.599 1.00 17.02 ? 84  ARG C O   1 
ATOM   4977 C  CB  . ARG C  1 84  ? 54.739  1.414   -42.895 1.00 17.74 ? 84  ARG C CB  1 
ATOM   4978 C  CG  . ARG C  1 84  ? 54.946  0.993   -41.429 1.00 19.51 ? 84  ARG C CG  1 
ATOM   4979 C  CD  . ARG C  1 84  ? 56.366  1.224   -40.994 1.00 20.83 ? 84  ARG C CD  1 
ATOM   4980 N  NE  . ARG C  1 84  ? 57.225  0.165   -41.494 1.00 20.06 ? 84  ARG C NE  1 
ATOM   4981 C  CZ  . ARG C  1 84  ? 58.515  0.078   -41.203 1.00 24.07 ? 84  ARG C CZ  1 
ATOM   4982 N  NH1 . ARG C  1 84  ? 59.067  0.986   -40.411 1.00 23.68 ? 84  ARG C NH1 1 
ATOM   4983 N  NH2 . ARG C  1 84  ? 59.245  -0.910  -41.696 1.00 23.15 ? 84  ARG C NH2 1 
ATOM   4984 N  N   . TYR C  1 85  ? 51.698  1.147   -41.497 1.00 15.59 ? 85  TYR C N   1 
ATOM   4985 C  CA  . TYR C  1 85  ? 50.874  1.793   -40.479 1.00 15.53 ? 85  TYR C CA  1 
ATOM   4986 C  C   . TYR C  1 85  ? 51.499  1.582   -39.113 1.00 15.50 ? 85  TYR C C   1 
ATOM   4987 O  O   . TYR C  1 85  ? 51.652  0.442   -38.714 1.00 17.92 ? 85  TYR C O   1 
ATOM   4988 C  CB  . TYR C  1 85  ? 49.407  1.233   -40.553 1.00 16.46 ? 85  TYR C CB  1 
ATOM   4989 C  CG  . TYR C  1 85  ? 48.677  1.797   -41.751 1.00 14.38 ? 85  TYR C CG  1 
ATOM   4990 C  CD1 . TYR C  1 85  ? 47.903  2.948   -41.617 1.00 14.27 ? 85  TYR C CD1 1 
ATOM   4991 C  CD2 . TYR C  1 85  ? 48.793  1.175   -43.042 1.00 15.93 ? 85  TYR C CD2 1 
ATOM   4992 C  CE1 . TYR C  1 85  ? 47.167  3.427   -42.693 1.00 15.02 ? 85  TYR C CE1 1 
ATOM   4993 C  CE2 . TYR C  1 85  ? 48.060  1.660   -44.138 1.00 16.28 ? 85  TYR C CE2 1 
ATOM   4994 C  CZ  . TYR C  1 85  ? 47.314  2.807   -43.977 1.00 16.57 ? 85  TYR C CZ  1 
ATOM   4995 O  OH  . TYR C  1 85  ? 46.610  3.287   -45.103 1.00 19.55 ? 85  TYR C OH  1 
ATOM   4996 N  N   . SER C  1 86  ? 51.878  2.688   -38.474 1.00 15.80 ? 86  SER C N   1 
ATOM   4997 C  CA  . SER C  1 86  ? 52.499  2.675   -37.150 1.00 16.53 ? 86  SER C CA  1 
ATOM   4998 C  C   . SER C  1 86  ? 51.475  2.885   -36.028 1.00 15.94 ? 86  SER C C   1 
ATOM   4999 O  O   . SER C  1 86  ? 50.561  3.705   -36.148 1.00 18.78 ? 86  SER C O   1 
ATOM   5000 C  CB  . SER C  1 86  ? 53.632  3.776   -37.134 1.00 19.94 ? 86  SER C CB  1 
ATOM   5001 O  OG  . SER C  1 86  ? 54.628  3.404   -38.106 1.00 19.30 ? 86  SER C OG  1 
ATOM   5002 N  N   . ALA C  1 87  ? 51.716  2.221   -34.887 1.00 17.35 ? 87  ALA C N   1 
ATOM   5003 C  CA  . ALA C  1 87  ? 50.801  2.286   -33.744 1.00 17.43 ? 87  ALA C CA  1 
ATOM   5004 C  C   . ALA C  1 87  ? 50.774  3.685   -33.099 1.00 17.84 ? 87  ALA C C   1 
ATOM   5005 O  O   . ALA C  1 87  ? 51.793  4.407   -33.103 1.00 17.72 ? 87  ALA C O   1 
ATOM   5006 C  CB  . ALA C  1 87  ? 51.111  1.192   -32.756 1.00 18.08 ? 87  ALA C CB  1 
ATOM   5007 N  N   . THR C  1 88  ? 49.626  4.033   -32.515 1.00 15.97 ? 88  THR C N   1 
ATOM   5008 C  CA  . THR C  1 88  ? 49.478  5.302   -31.782 1.00 15.80 ? 88  THR C CA  1 
ATOM   5009 C  C   . THR C  1 88  ? 48.807  5.077   -30.437 1.00 18.03 ? 88  THR C C   1 
ATOM   5010 O  O   . THR C  1 88  ? 49.275  5.624   -29.425 1.00 17.08 ? 88  THR C O   1 
ATOM   5011 C  CB  . THR C  1 88  ? 48.890  6.444   -32.538 1.00 15.33 ? 88  THR C CB  1 
ATOM   5012 O  OG1 . THR C  1 88  ? 48.777  7.572   -31.692 1.00 18.18 ? 88  THR C OG1 1 
ATOM   5013 C  CG2 . THR C  1 88  ? 47.471  6.142   -33.118 1.00 16.23 ? 88  THR C CG2 1 
ATOM   5014 N  N   . GLN C  1 89  ? 47.745  4.255   -30.340 1.00 17.00 ? 89  GLN C N   1 
ATOM   5015 C  CA  . GLN C  1 89  ? 47.060  3.998   -29.030 1.00 15.85 ? 89  GLN C CA  1 
ATOM   5016 C  C   . GLN C  1 89  ? 46.120  2.786   -29.229 1.00 16.49 ? 89  GLN C C   1 
ATOM   5017 O  O   . GLN C  1 89  ? 45.796  2.389   -30.407 1.00 15.85 ? 89  GLN C O   1 
ATOM   5018 C  CB  . GLN C  1 89  ? 46.287  5.220   -28.594 1.00 17.57 ? 89  GLN C CB  1 
ATOM   5019 C  CG  . GLN C  1 89  ? 45.298  5.746   -29.630 1.00 21.78 ? 89  GLN C CG  1 
ATOM   5020 C  CD  . GLN C  1 89  ? 43.900  5.410   -29.171 1.00 16.97 ? 89  GLN C CD  1 
ATOM   5021 O  OE1 . GLN C  1 89  ? 43.652  4.246   -28.859 1.00 20.97 ? 89  GLN C OE1 1 
ATOM   5022 N  NE2 . GLN C  1 89  ? 43.005  6.338   -29.189 1.00 26.07 ? 89  GLN C NE2 1 
ATOM   5023 N  N   . LEU C  1 90  ? 45.800  2.145   -28.108 1.00 15.86 ? 90  LEU C N   1 
ATOM   5024 C  CA  . LEU C  1 90  ? 44.707  1.206   -28.141 1.00 14.21 ? 90  LEU C CA  1 
ATOM   5025 C  C   . LEU C  1 90  ? 43.698  1.634   -27.146 1.00 16.00 ? 90  LEU C C   1 
ATOM   5026 O  O   . LEU C  1 90  ? 44.000  2.446   -26.228 1.00 15.08 ? 90  LEU C O   1 
ATOM   5027 C  CB  . LEU C  1 90  ? 45.130  -0.203  -28.095 1.00 14.18 ? 90  LEU C CB  1 
ATOM   5028 C  CG  . LEU C  1 90  ? 45.893  -0.540  -26.748 1.00 16.04 ? 90  LEU C CG  1 
ATOM   5029 C  CD1 . LEU C  1 90  ? 45.000  -0.659  -25.523 1.00 16.22 ? 90  LEU C CD1 1 
ATOM   5030 C  CD2 . LEU C  1 90  ? 46.426  -1.904  -26.969 1.00 15.34 ? 90  LEU C CD2 1 
ATOM   5031 N  N   . HIS C  1 91  ? 42.456  1.156   -27.293 1.00 14.76 ? 91  HIS C N   1 
ATOM   5032 C  CA  . HIS C  1 91  ? 41.408  1.519   -26.366 1.00 13.63 ? 91  HIS C CA  1 
ATOM   5033 C  C   . HIS C  1 91  ? 40.251  0.533   -26.531 1.00 13.61 ? 91  HIS C C   1 
ATOM   5034 O  O   . HIS C  1 91  ? 40.313  -0.342  -27.383 1.00 14.83 ? 91  HIS C O   1 
ATOM   5035 C  CB  . HIS C  1 91  ? 40.918  2.914   -26.571 1.00 14.34 ? 91  HIS C CB  1 
ATOM   5036 C  CG  . HIS C  1 91  ? 40.307  3.089   -27.926 1.00 14.14 ? 91  HIS C CG  1 
ATOM   5037 N  ND1 . HIS C  1 91  ? 41.035  3.527   -29.010 1.00 14.49 ? 91  HIS C ND1 1 
ATOM   5038 C  CD2 . HIS C  1 91  ? 39.044  2.841   -28.320 1.00 13.15 ? 91  HIS C CD2 1 
ATOM   5039 C  CE1 . HIS C  1 91  ? 40.185  3.534   -30.095 1.00 13.38 ? 91  HIS C CE1 1 
ATOM   5040 N  NE2 . HIS C  1 91  ? 39.022  3.025   -29.696 1.00 11.04 ? 91  HIS C NE2 1 
ATOM   5041 N  N   . LEU C  1 92  ? 39.263  0.649   -25.631 1.00 13.93 ? 92  LEU C N   1 
ATOM   5042 C  CA  . LEU C  1 92  ? 38.116  -0.306  -25.655 1.00 14.96 ? 92  LEU C CA  1 
ATOM   5043 C  C   . LEU C  1 92  ? 36.789  0.395   -25.635 1.00 10.90 ? 92  LEU C C   1 
ATOM   5044 O  O   . LEU C  1 92  ? 36.571  1.581   -25.366 1.00 14.18 ? 92  LEU C O   1 
ATOM   5045 C  CB  . LEU C  1 92  ? 38.157  -1.320  -24.449 1.00 17.91 ? 92  LEU C CB  1 
ATOM   5046 C  CG  . LEU C  1 92  ? 39.384  -2.237  -24.500 1.00 18.37 ? 92  LEU C CG  1 
ATOM   5047 C  CD1 . LEU C  1 92  ? 40.221  -1.806  -23.323 1.00 23.54 ? 92  LEU C CD1 1 
ATOM   5048 C  CD2 . LEU C  1 92  ? 39.086  -3.672  -24.343 1.00 21.53 ? 92  LEU C CD2 1 
ATOM   5049 N  N   . HIS C  1 93  ? 35.829  -0.469  -26.031 1.00 13.78 ? 93  HIS C N   1 
ATOM   5050 C  CA  . HIS C  1 93  ? 34.394  -0.111  -26.012 1.00 11.50 ? 93  HIS C CA  1 
ATOM   5051 C  C   . HIS C  1 93  ? 33.574  -1.205  -25.345 1.00 11.31 ? 93  HIS C C   1 
ATOM   5052 O  O   . HIS C  1 93  ? 33.842  -2.368  -25.589 1.00 13.80 ? 93  HIS C O   1 
ATOM   5053 C  CB  . HIS C  1 93  ? 33.843  0.081   -27.451 1.00 12.50 ? 93  HIS C CB  1 
ATOM   5054 C  CG  . HIS C  1 93  ? 34.580  1.164   -28.211 1.00 9.99  ? 93  HIS C CG  1 
ATOM   5055 N  ND1 . HIS C  1 93  ? 34.239  2.487   -28.239 1.00 11.65 ? 93  HIS C ND1 1 
ATOM   5056 C  CD2 . HIS C  1 93  ? 35.669  1.013   -29.038 1.00 11.77 ? 93  HIS C CD2 1 
ATOM   5057 C  CE1 . HIS C  1 93  ? 35.128  3.129   -29.054 1.00 10.70 ? 93  HIS C CE1 1 
ATOM   5058 N  NE2 . HIS C  1 93  ? 35.971  2.265   -29.518 1.00 10.52 ? 93  HIS C NE2 1 
ATOM   5059 N  N   . TRP C  1 94  ? 32.626  -0.839  -24.489 1.00 11.87 ? 94  TRP C N   1 
ATOM   5060 C  CA  . TRP C  1 94  ? 31.842  -1.850  -23.765 1.00 12.79 ? 94  TRP C CA  1 
ATOM   5061 C  C   . TRP C  1 94  ? 30.434  -1.340  -23.487 1.00 12.83 ? 94  TRP C C   1 
ATOM   5062 O  O   . TRP C  1 94  ? 30.064  -0.189  -23.784 1.00 12.83 ? 94  TRP C O   1 
ATOM   5063 C  CB  . TRP C  1 94  ? 32.522  -2.222  -22.449 1.00 13.34 ? 94  TRP C CB  1 
ATOM   5064 C  CG  . TRP C  1 94  ? 32.821  -1.046  -21.537 1.00 16.20 ? 94  TRP C CG  1 
ATOM   5065 C  CD1 . TRP C  1 94  ? 32.012  -0.531  -20.529 1.00 16.01 ? 94  TRP C CD1 1 
ATOM   5066 C  CD2 . TRP C  1 94  ? 34.027  -0.204  -21.521 1.00 14.39 ? 94  TRP C CD2 1 
ATOM   5067 N  NE1 . TRP C  1 94  ? 32.614  0.538   -19.919 1.00 14.31 ? 94  TRP C NE1 1 
ATOM   5068 C  CE2 . TRP C  1 94  ? 33.820  0.782   -20.459 1.00 15.42 ? 94  TRP C CE2 1 
ATOM   5069 C  CE3 . TRP C  1 94  ? 35.203  -0.170  -22.253 1.00 15.28 ? 94  TRP C CE3 1 
ATOM   5070 C  CZ2 . TRP C  1 94  ? 34.760  1.751   -20.163 1.00 16.46 ? 94  TRP C CZ2 1 
ATOM   5071 C  CZ3 . TRP C  1 94  ? 36.149  0.811   -21.938 1.00 15.49 ? 94  TRP C CZ3 1 
ATOM   5072 C  CH2 . TRP C  1 94  ? 35.925  1.747   -20.919 1.00 17.41 ? 94  TRP C CH2 1 
ATOM   5073 N  N   . GLY C  1 95  ? 29.655  -2.248  -22.876 1.00 13.43 ? 95  GLY C N   1 
ATOM   5074 C  CA  . GLY C  1 95  ? 28.284  -1.968  -22.553 1.00 15.86 ? 95  GLY C CA  1 
ATOM   5075 C  C   . GLY C  1 95  ? 28.096  -1.650  -21.052 1.00 14.43 ? 95  GLY C C   1 
ATOM   5076 O  O   . GLY C  1 95  ? 28.720  -0.722  -20.522 1.00 14.87 ? 95  GLY C O   1 
ATOM   5077 N  N   . ASN C  1 96  ? 27.244  -2.445  -20.394 1.00 17.65 ? 96  ASN C N   1 
ATOM   5078 C  CA  . ASN C  1 96  ? 27.012  -2.129  -18.922 1.00 17.34 ? 96  ASN C CA  1 
ATOM   5079 C  C   . ASN C  1 96  ? 26.550  -3.445  -18.324 1.00 17.61 ? 96  ASN C C   1 
ATOM   5080 O  O   . ASN C  1 96  ? 26.210  -4.390  -19.037 1.00 18.18 ? 96  ASN C O   1 
ATOM   5081 C  CB  . ASN C  1 96  ? 26.000  -0.992  -18.786 1.00 19.24 ? 96  ASN C CB  1 
ATOM   5082 C  CG  . ASN C  1 96  ? 24.609  -1.427  -19.122 1.00 22.31 ? 96  ASN C CG  1 
ATOM   5083 O  OD1 . ASN C  1 96  ? 23.927  -1.978  -18.243 1.00 27.38 ? 96  ASN C OD1 1 
ATOM   5084 N  ND2 . ASN C  1 96  ? 24.155  -1.213  -20.354 1.00 24.22 ? 96  ASN C ND2 1 
ATOM   5085 N  N   . PRO C  1 97  ? 26.539  -3.567  -16.975 1.00 19.14 ? 97  PRO C N   1 
ATOM   5086 C  CA  . PRO C  1 97  ? 26.298  -4.904  -16.459 1.00 19.69 ? 97  PRO C CA  1 
ATOM   5087 C  C   . PRO C  1 97  ? 24.863  -5.395  -16.688 1.00 19.32 ? 97  PRO C C   1 
ATOM   5088 O  O   . PRO C  1 97  ? 24.633  -6.602  -16.692 1.00 20.76 ? 97  PRO C O   1 
ATOM   5089 C  CB  . PRO C  1 97  ? 26.528  -4.710  -14.921 1.00 20.50 ? 97  PRO C CB  1 
ATOM   5090 C  CG  . PRO C  1 97  ? 27.403  -3.545  -14.844 1.00 19.76 ? 97  PRO C CG  1 
ATOM   5091 C  CD  . PRO C  1 97  ? 27.115  -2.633  -15.991 1.00 23.06 ? 97  PRO C CD  1 
ATOM   5092 N  N   . ASN C  1 98  ? 23.934  -4.486  -16.911 1.00 18.84 ? 98  ASN C N   1 
ATOM   5093 C  CA  . ASN C  1 98  ? 22.547  -4.889  -17.213 1.00 20.76 ? 98  ASN C CA  1 
ATOM   5094 C  C   . ASN C  1 98  ? 22.322  -5.291  -18.678 1.00 22.36 ? 98  ASN C C   1 
ATOM   5095 O  O   . ASN C  1 98  ? 21.308  -5.944  -19.002 1.00 24.25 ? 98  ASN C O   1 
ATOM   5096 C  CB  . ASN C  1 98  ? 21.590  -3.797  -16.884 1.00 22.89 ? 98  ASN C CB  1 
ATOM   5097 C  CG  . ASN C  1 98  ? 21.524  -3.574  -15.390 1.00 30.86 ? 98  ASN C CG  1 
ATOM   5098 O  OD1 . ASN C  1 98  ? 21.514  -4.544  -14.616 1.00 30.19 ? 98  ASN C OD1 1 
ATOM   5099 N  ND2 . ASN C  1 98  ? 21.519  -2.328  -14.987 1.00 34.87 ? 98  ASN C ND2 1 
ATOM   5100 N  N   . ASP C  1 99  ? 23.255  -4.914  -19.547 1.00 21.99 ? 99  ASP C N   1 
ATOM   5101 C  CA  . ASP C  1 99  ? 23.165  -5.262  -20.978 1.00 19.05 ? 99  ASP C CA  1 
ATOM   5102 C  C   . ASP C  1 99  ? 24.630  -5.344  -21.487 1.00 16.96 ? 99  ASP C C   1 
ATOM   5103 O  O   . ASP C  1 99  ? 25.149  -4.393  -22.081 1.00 18.40 ? 99  ASP C O   1 
ATOM   5104 C  CB  . ASP C  1 99  ? 22.357  -4.170  -21.681 1.00 17.65 ? 99  ASP C CB  1 
ATOM   5105 C  CG  . ASP C  1 99  ? 21.884  -4.561  -23.104 1.00 21.27 ? 99  ASP C CG  1 
ATOM   5106 O  OD1 . ASP C  1 99  ? 22.129  -5.697  -23.461 1.00 26.20 ? 99  ASP C OD1 1 
ATOM   5107 O  OD2 . ASP C  1 99  ? 21.294  -3.640  -23.763 1.00 24.47 ? 99  ASP C OD2 1 
ATOM   5108 N  N   . PRO C  1 100 ? 25.266  -6.476  -21.273 1.00 16.81 ? 100 PRO C N   1 
ATOM   5109 C  CA  . PRO C  1 100 ? 26.709  -6.494  -21.388 1.00 17.32 ? 100 PRO C CA  1 
ATOM   5110 C  C   . PRO C  1 100 ? 27.092  -6.858  -22.834 1.00 16.54 ? 100 PRO C C   1 
ATOM   5111 O  O   . PRO C  1 100 ? 27.716  -7.842  -23.110 1.00 17.43 ? 100 PRO C O   1 
ATOM   5112 C  CB  . PRO C  1 100 ? 27.132  -7.581  -20.415 1.00 18.65 ? 100 PRO C CB  1 
ATOM   5113 C  CG  . PRO C  1 100 ? 25.972  -8.509  -20.353 1.00 20.70 ? 100 PRO C CG  1 
ATOM   5114 C  CD  . PRO C  1 100 ? 24.796  -7.619  -20.452 1.00 16.67 ? 100 PRO C CD  1 
ATOM   5115 N  N   . HIS C  1 101 ? 26.652  -5.996  -23.767 1.00 16.30 ? 101 HIS C N   1 
ATOM   5116 C  CA  . HIS C  1 101 ? 26.808  -6.279  -25.229 1.00 17.42 ? 101 HIS C CA  1 
ATOM   5117 C  C   . HIS C  1 101 ? 27.146  -4.942  -25.880 1.00 17.94 ? 101 HIS C C   1 
ATOM   5118 O  O   . HIS C  1 101 ? 26.345  -4.390  -26.637 1.00 20.64 ? 101 HIS C O   1 
ATOM   5119 C  CB  . HIS C  1 101 ? 25.480  -6.770  -25.774 1.00 19.82 ? 101 HIS C CB  1 
ATOM   5120 C  CG  . HIS C  1 101 ? 24.937  -7.920  -25.003 1.00 21.18 ? 101 HIS C CG  1 
ATOM   5121 N  ND1 . HIS C  1 101 ? 25.464  -9.160  -25.080 1.00 21.30 ? 101 HIS C ND1 1 
ATOM   5122 C  CD2 . HIS C  1 101 ? 23.904  -7.974  -24.029 1.00 21.00 ? 101 HIS C CD2 1 
ATOM   5123 C  CE1 . HIS C  1 101 ? 24.767  -9.977  -24.226 1.00 25.41 ? 101 HIS C CE1 1 
ATOM   5124 N  NE2 . HIS C  1 101 ? 23.829  -9.247  -23.618 1.00 22.40 ? 101 HIS C NE2 1 
ATOM   5125 N  N   . GLY C  1 102 ? 28.382  -4.500  -25.694 1.00 14.39 ? 102 GLY C N   1 
ATOM   5126 C  CA  . GLY C  1 102 ? 28.822  -3.206  -26.109 1.00 14.53 ? 102 GLY C CA  1 
ATOM   5127 C  C   . GLY C  1 102 ? 29.970  -3.174  -27.120 1.00 13.30 ? 102 GLY C C   1 
ATOM   5128 O  O   . GLY C  1 102 ? 30.636  -2.117  -27.212 1.00 12.69 ? 102 GLY C O   1 
ATOM   5129 N  N   . SER C  1 103 ? 30.099  -4.191  -27.972 1.00 13.75 ? 103 SER C N   1 
ATOM   5130 C  CA  . SER C  1 103 ? 30.951  -4.016  -29.130 1.00 12.84 ? 103 SER C CA  1 
ATOM   5131 C  C   . SER C  1 103 ? 30.388  -2.971  -30.055 1.00 12.64 ? 103 SER C C   1 
ATOM   5132 O  O   . SER C  1 103 ? 29.182  -2.605  -29.993 1.00 13.06 ? 103 SER C O   1 
ATOM   5133 C  CB  . SER C  1 103 ? 31.161  -5.364  -29.880 1.00 12.54 ? 103 SER C CB  1 
ATOM   5134 O  OG  . SER C  1 103 ? 29.911  -5.780  -30.502 1.00 12.40 ? 103 SER C OG  1 
ATOM   5135 N  N   . GLU C  1 104 ? 31.257  -2.494  -30.944 1.00 10.69 ? 104 GLU C N   1 
ATOM   5136 C  CA  . GLU C  1 104 ? 30.832  -1.519  -31.961 1.00 10.34 ? 104 GLU C CA  1 
ATOM   5137 C  C   . GLU C  1 104 ? 30.359  -2.225  -33.220 1.00 10.27 ? 104 GLU C C   1 
ATOM   5138 O  O   . GLU C  1 104 ? 29.236  -2.000  -33.654 1.00 9.73  ? 104 GLU C O   1 
ATOM   5139 C  CB  . GLU C  1 104 ? 31.969  -0.520  -32.247 1.00 10.08 ? 104 GLU C CB  1 
ATOM   5140 C  CG  . GLU C  1 104 ? 32.487  0.211   -30.955 1.00 10.90 ? 104 GLU C CG  1 
ATOM   5141 C  CD  . GLU C  1 104 ? 32.817  1.639   -31.305 1.00 11.08 ? 104 GLU C CD  1 
ATOM   5142 O  OE1 . GLU C  1 104 ? 33.878  1.827   -31.925 1.00 11.84 ? 104 GLU C OE1 1 
ATOM   5143 O  OE2 . GLU C  1 104 ? 31.947  2.486   -31.068 1.00 12.65 ? 104 GLU C OE2 1 
ATOM   5144 N  N   . HIS C  1 105 ? 31.189  -3.010  -33.801 1.00 10.35 ? 105 HIS C N   1 
ATOM   5145 C  CA  . HIS C  1 105 ? 30.711  -3.870  -34.944 1.00 9.99  ? 105 HIS C CA  1 
ATOM   5146 C  C   . HIS C  1 105 ? 29.799  -4.939  -34.433 1.00 10.20 ? 105 HIS C C   1 
ATOM   5147 O  O   . HIS C  1 105 ? 29.977  -5.445  -33.277 1.00 12.25 ? 105 HIS C O   1 
ATOM   5148 C  CB  . HIS C  1 105 ? 31.913  -4.463  -35.624 1.00 10.63 ? 105 HIS C CB  1 
ATOM   5149 C  CG  . HIS C  1 105 ? 32.725  -3.404  -36.360 1.00 10.54 ? 105 HIS C CG  1 
ATOM   5150 N  ND1 . HIS C  1 105 ? 33.762  -2.696  -35.803 1.00 11.43 ? 105 HIS C ND1 1 
ATOM   5151 C  CD2 . HIS C  1 105 ? 32.560  -2.885  -37.643 1.00 10.14 ? 105 HIS C CD2 1 
ATOM   5152 C  CE1 . HIS C  1 105 ? 34.226  -1.802  -36.699 1.00 11.00 ? 105 HIS C CE1 1 
ATOM   5153 N  NE2 . HIS C  1 105 ? 33.474  -1.922  -37.822 1.00 11.73 ? 105 HIS C NE2 1 
ATOM   5154 N  N   . THR C  1 106 ? 28.844  -5.330  -35.221 1.00 9.24  ? 106 THR C N   1 
ATOM   5155 C  CA  . THR C  1 106 ? 28.019  -6.495  -34.905 1.00 10.89 ? 106 THR C CA  1 
ATOM   5156 C  C   . THR C  1 106 ? 28.152  -7.495  -36.005 1.00 11.72 ? 106 THR C C   1 
ATOM   5157 O  O   . THR C  1 106 ? 28.602  -7.224  -37.095 1.00 11.41 ? 106 THR C O   1 
ATOM   5158 C  CB  . THR C  1 106 ? 26.569  -6.063  -34.753 1.00 10.94 ? 106 THR C CB  1 
ATOM   5159 O  OG1 . THR C  1 106 ? 26.122  -5.442  -35.995 1.00 11.99 ? 106 THR C OG1 1 
ATOM   5160 C  CG2 . THR C  1 106 ? 26.322  -5.046  -33.633 1.00 12.30 ? 106 THR C CG2 1 
ATOM   5161 N  N   . VAL C  1 107 ? 27.824  -8.759  -35.687 1.00 11.06 ? 107 VAL C N   1 
ATOM   5162 C  CA  . VAL C  1 107 ? 27.892  -9.806  -36.674 1.00 12.06 ? 107 VAL C CA  1 
ATOM   5163 C  C   . VAL C  1 107 ? 26.516  -10.484 -36.748 1.00 12.54 ? 107 VAL C C   1 
ATOM   5164 O  O   . VAL C  1 107 ? 25.983  -10.925 -35.709 1.00 13.53 ? 107 VAL C O   1 
ATOM   5165 C  CB  . VAL C  1 107 ? 28.947  -10.894 -36.294 1.00 13.28 ? 107 VAL C CB  1 
ATOM   5166 C  CG1 . VAL C  1 107 ? 28.911  -12.070 -37.304 1.00 14.65 ? 107 VAL C CG1 1 
ATOM   5167 C  CG2 . VAL C  1 107 ? 30.378  -10.261 -36.105 1.00 15.61 ? 107 VAL C CG2 1 
ATOM   5168 N  N   . SER C  1 108 ? 25.909  -10.405 -37.927 1.00 13.22 ? 108 SER C N   1 
ATOM   5169 C  CA  . SER C  1 108 ? 24.545  -10.981 -38.101 1.00 14.86 ? 108 SER C CA  1 
ATOM   5170 C  C   . SER C  1 108 ? 23.619  -10.355 -37.092 1.00 14.99 ? 108 SER C C   1 
ATOM   5171 O  O   . SER C  1 108 ? 22.741  -11.039 -36.504 1.00 15.49 ? 108 SER C O   1 
ATOM   5172 C  CB  . SER C  1 108 ? 24.519  -12.521 -38.020 1.00 16.17 ? 108 SER C CB  1 
ATOM   5173 O  OG  . SER C  1 108 ? 25.331  -13.012 -39.058 1.00 20.52 ? 108 SER C OG  1 
ATOM   5174 N  N   . GLY C  1 109 ? 23.824  -9.050  -36.864 1.00 12.95 ? 109 GLY C N   1 
ATOM   5175 C  CA  . GLY C  1 109 ? 22.990  -8.275  -36.012 1.00 14.38 ? 109 GLY C CA  1 
ATOM   5176 C  C   . GLY C  1 109 ? 23.323  -8.365  -34.519 1.00 13.81 ? 109 GLY C C   1 
ATOM   5177 O  O   . GLY C  1 109 ? 22.701  -7.627  -33.716 1.00 16.43 ? 109 GLY C O   1 
ATOM   5178 N  N   . GLN C  1 110 ? 24.294  -9.218  -34.123 1.00 13.53 ? 110 GLN C N   1 
ATOM   5179 C  CA  . GLN C  1 110 ? 24.542  -9.414  -32.722 1.00 14.30 ? 110 GLN C CA  1 
ATOM   5180 C  C   . GLN C  1 110 ? 25.784  -8.623  -32.241 1.00 11.56 ? 110 GLN C C   1 
ATOM   5181 O  O   . GLN C  1 110 ? 26.829  -8.671  -32.891 1.00 12.17 ? 110 GLN C O   1 
ATOM   5182 C  CB  . GLN C  1 110 ? 24.812  -10.895 -32.492 1.00 15.03 ? 110 GLN C CB  1 
ATOM   5183 C  CG  . GLN C  1 110 ? 23.759  -11.811 -33.085 1.00 16.95 ? 110 GLN C CG  1 
ATOM   5184 C  CD  . GLN C  1 110 ? 22.365  -11.399 -32.633 1.00 15.73 ? 110 GLN C CD  1 
ATOM   5185 O  OE1 . GLN C  1 110 ? 22.041  -11.376 -31.457 1.00 18.94 ? 110 GLN C OE1 1 
ATOM   5186 N  NE2 . GLN C  1 110 ? 21.546  -11.063 -33.626 1.00 18.16 ? 110 GLN C NE2 1 
ATOM   5187 N  N   . HIS C  1 111 ? 25.644  -7.941  -31.112 1.00 12.82 ? 111 HIS C N   1 
ATOM   5188 C  CA  . HIS C  1 111 ? 26.818  -7.401  -30.436 1.00 14.29 ? 111 HIS C CA  1 
ATOM   5189 C  C   . HIS C  1 111 ? 27.607  -8.460  -29.710 1.00 14.82 ? 111 HIS C C   1 
ATOM   5190 O  O   . HIS C  1 111 ? 27.045  -9.483  -29.214 1.00 18.30 ? 111 HIS C O   1 
ATOM   5191 C  CB  . HIS C  1 111 ? 26.479  -6.373  -29.379 1.00 15.30 ? 111 HIS C CB  1 
ATOM   5192 C  CG  . HIS C  1 111 ? 25.965  -5.131  -29.944 1.00 13.55 ? 111 HIS C CG  1 
ATOM   5193 N  ND1 . HIS C  1 111 ? 26.726  -3.970  -30.082 1.00 14.22 ? 111 HIS C ND1 1 
ATOM   5194 C  CD2 . HIS C  1 111 ? 24.708  -4.848  -30.473 1.00 15.36 ? 111 HIS C CD2 1 
ATOM   5195 C  CE1 . HIS C  1 111 ? 25.975  -3.042  -30.634 1.00 15.92 ? 111 HIS C CE1 1 
ATOM   5196 N  NE2 . HIS C  1 111 ? 24.711  -3.541  -30.803 1.00 17.93 ? 111 HIS C NE2 1 
ATOM   5197 N  N   . PHE C  1 112 ? 28.886  -8.251  -29.656 1.00 12.92 ? 112 PHE C N   1 
ATOM   5198 C  CA  . PHE C  1 112 ? 29.796  -8.921  -28.695 1.00 13.47 ? 112 PHE C CA  1 
ATOM   5199 C  C   . PHE C  1 112 ? 29.850  -8.103  -27.425 1.00 14.72 ? 112 PHE C C   1 
ATOM   5200 O  O   . PHE C  1 112 ? 29.281  -7.008  -27.330 1.00 14.31 ? 112 PHE C O   1 
ATOM   5201 C  CB  . PHE C  1 112 ? 31.154  -9.149  -29.305 1.00 14.53 ? 112 PHE C CB  1 
ATOM   5202 C  CG  . PHE C  1 112 ? 31.152  -10.292 -30.245 1.00 17.15 ? 112 PHE C CG  1 
ATOM   5203 C  CD1 . PHE C  1 112 ? 30.599  -10.157 -31.565 1.00 19.11 ? 112 PHE C CD1 1 
ATOM   5204 C  CD2 . PHE C  1 112 ? 31.603  -11.553 -29.803 1.00 21.79 ? 112 PHE C CD2 1 
ATOM   5205 C  CE1 . PHE C  1 112 ? 30.544  -11.307 -32.411 1.00 24.24 ? 112 PHE C CE1 1 
ATOM   5206 C  CE2 . PHE C  1 112 ? 31.587  -12.646 -30.654 1.00 23.00 ? 112 PHE C CE2 1 
ATOM   5207 C  CZ  . PHE C  1 112 ? 31.072  -12.537 -31.939 1.00 22.74 ? 112 PHE C CZ  1 
ATOM   5208 N  N   . ALA C  1 113 ? 30.428  -8.679  -26.317 1.00 14.17 ? 113 ALA C N   1 
ATOM   5209 C  CA  . ALA C  1 113 ? 30.469  -7.982  -25.071 1.00 13.29 ? 113 ALA C CA  1 
ATOM   5210 C  C   . ALA C  1 113 ? 31.193  -6.648  -25.093 1.00 11.63 ? 113 ALA C C   1 
ATOM   5211 O  O   . ALA C  1 113 ? 30.787  -5.687  -24.440 1.00 13.99 ? 113 ALA C O   1 
ATOM   5212 C  CB  . ALA C  1 113 ? 31.106  -8.936  -24.004 1.00 14.64 ? 113 ALA C CB  1 
ATOM   5213 N  N   . ALA C  1 114 ? 32.281  -6.617  -25.870 1.00 13.64 ? 114 ALA C N   1 
ATOM   5214 C  CA  . ALA C  1 114 ? 33.209  -5.483  -25.886 1.00 12.96 ? 114 ALA C CA  1 
ATOM   5215 C  C   . ALA C  1 114 ? 34.058  -5.568  -27.130 1.00 12.93 ? 114 ALA C C   1 
ATOM   5216 O  O   . ALA C  1 114 ? 33.963  -6.501  -27.872 1.00 12.76 ? 114 ALA C O   1 
ATOM   5217 C  CB  . ALA C  1 114 ? 34.033  -5.515  -24.599 1.00 14.75 ? 114 ALA C CB  1 
ATOM   5218 N  N   . GLU C  1 115 ? 34.779  -4.483  -27.443 1.00 13.17 ? 115 GLU C N   1 
ATOM   5219 C  CA  . GLU C  1 115 ? 35.617  -4.493  -28.598 1.00 13.91 ? 115 GLU C CA  1 
ATOM   5220 C  C   . GLU C  1 115 ? 36.921  -3.704  -28.255 1.00 11.80 ? 115 GLU C C   1 
ATOM   5221 O  O   . GLU C  1 115 ? 36.865  -2.585  -27.644 1.00 12.48 ? 115 GLU C O   1 
ATOM   5222 C  CB  . GLU C  1 115 ? 34.822  -3.842  -29.756 1.00 12.43 ? 115 GLU C CB  1 
ATOM   5223 C  CG  . GLU C  1 115 ? 35.516  -3.957  -31.150 1.00 12.35 ? 115 GLU C CG  1 
ATOM   5224 C  CD  . GLU C  1 115 ? 34.537  -3.614  -32.245 1.00 12.64 ? 115 GLU C CD  1 
ATOM   5225 O  OE1 . GLU C  1 115 ? 35.038  -3.080  -33.249 1.00 12.20 ? 115 GLU C OE1 1 
ATOM   5226 O  OE2 . GLU C  1 115 ? 33.370  -3.902  -32.120 1.00 12.32 ? 115 GLU C OE2 1 
ATOM   5227 N  N   . LEU C  1 116 ? 38.042  -4.256  -28.710 1.00 13.46 ? 116 LEU C N   1 
ATOM   5228 C  CA  . LEU C  1 116 ? 39.350  -3.566  -28.579 1.00 12.48 ? 116 LEU C CA  1 
ATOM   5229 C  C   . LEU C  1 116 ? 39.761  -2.990  -29.930 1.00 11.20 ? 116 LEU C C   1 
ATOM   5230 O  O   . LEU C  1 116 ? 39.607  -3.704  -30.960 1.00 13.25 ? 116 LEU C O   1 
ATOM   5231 C  CB  . LEU C  1 116 ? 40.379  -4.614  -28.144 1.00 14.57 ? 116 LEU C CB  1 
ATOM   5232 C  CG  . LEU C  1 116 ? 41.859  -4.121  -28.219 1.00 15.20 ? 116 LEU C CG  1 
ATOM   5233 C  CD1 . LEU C  1 116 ? 42.160  -3.203  -27.032 1.00 17.81 ? 116 LEU C CD1 1 
ATOM   5234 C  CD2 . LEU C  1 116 ? 42.819  -5.295  -28.347 1.00 16.30 ? 116 LEU C CD2 1 
ATOM   5235 N  N   . HIS C  1 117 ? 40.249  -1.747  -29.908 1.00 13.20 ? 117 HIS C N   1 
ATOM   5236 C  CA  . HIS C  1 117 ? 40.704  -1.063  -31.165 1.00 11.85 ? 117 HIS C CA  1 
ATOM   5237 C  C   . HIS C  1 117 ? 42.195  -0.799  -30.983 1.00 12.71 ? 117 HIS C C   1 
ATOM   5238 O  O   . HIS C  1 117 ? 42.539  -0.142  -29.982 1.00 13.33 ? 117 HIS C O   1 
ATOM   5239 C  CB  . HIS C  1 117 ? 39.921  0.192   -31.417 1.00 13.77 ? 117 HIS C CB  1 
ATOM   5240 C  CG  . HIS C  1 117 ? 38.536  -0.117  -31.850 1.00 10.43 ? 117 HIS C CG  1 
ATOM   5241 N  ND1 . HIS C  1 117 ? 37.532  0.811   -31.733 1.00 12.35 ? 117 HIS C ND1 1 
ATOM   5242 C  CD2 . HIS C  1 117 ? 38.043  -1.261  -32.489 1.00 13.17 ? 117 HIS C CD2 1 
ATOM   5243 C  CE1 . HIS C  1 117 ? 36.380  0.226   -32.269 1.00 11.45 ? 117 HIS C CE1 1 
ATOM   5244 N  NE2 . HIS C  1 117 ? 36.673  -1.010  -32.721 1.00 10.65 ? 117 HIS C NE2 1 
ATOM   5245 N  N   . ILE C  1 118 ? 42.979  -1.225  -31.929 1.00 13.18 ? 118 ILE C N   1 
ATOM   5246 C  CA  . ILE C  1 118 ? 44.450  -0.895  -31.942 1.00 14.59 ? 118 ILE C CA  1 
ATOM   5247 C  C   . ILE C  1 118 ? 44.668  0.027   -33.121 1.00 12.64 ? 118 ILE C C   1 
ATOM   5248 O  O   . ILE C  1 118 ? 44.527  -0.408  -34.334 1.00 12.96 ? 118 ILE C O   1 
ATOM   5249 C  CB  . ILE C  1 118 ? 45.280  -2.137  -32.068 1.00 13.45 ? 118 ILE C CB  1 
ATOM   5250 C  CG1 . ILE C  1 118 ? 44.876  -3.191  -31.064 1.00 15.79 ? 118 ILE C CG1 1 
ATOM   5251 C  CG2 . ILE C  1 118 ? 46.791  -1.774  -31.796 1.00 16.38 ? 118 ILE C CG2 1 
ATOM   5252 C  CD1 . ILE C  1 118 ? 45.712  -4.490  -31.082 1.00 17.63 ? 118 ILE C CD1 1 
ATOM   5253 N  N   . VAL C  1 119 ? 44.942  1.275   -32.842 1.00 14.16 ? 119 VAL C N   1 
ATOM   5254 C  CA  . VAL C  1 119 ? 44.883  2.381   -33.778 1.00 12.74 ? 119 VAL C CA  1 
ATOM   5255 C  C   . VAL C  1 119 ? 46.247  2.646   -34.335 1.00 16.40 ? 119 VAL C C   1 
ATOM   5256 O  O   . VAL C  1 119 ? 47.246  2.767   -33.558 1.00 15.91 ? 119 VAL C O   1 
ATOM   5257 C  CB  . VAL C  1 119 ? 44.342  3.706   -33.163 1.00 12.54 ? 119 VAL C CB  1 
ATOM   5258 C  CG1 . VAL C  1 119 ? 44.217  4.807   -34.196 1.00 14.90 ? 119 VAL C CG1 1 
ATOM   5259 C  CG2 . VAL C  1 119 ? 43.027  3.472   -32.427 1.00 14.79 ? 119 VAL C CG2 1 
ATOM   5260 N  N   . HIS C  1 120 ? 46.344  2.709   -35.678 1.00 13.82 ? 120 HIS C N   1 
ATOM   5261 C  CA  . HIS C  1 120 ? 47.649  2.945   -36.387 1.00 16.88 ? 120 HIS C CA  1 
ATOM   5262 C  C   . HIS C  1 120 ? 47.477  4.063   -37.375 1.00 15.95 ? 120 HIS C C   1 
ATOM   5263 O  O   . HIS C  1 120 ? 46.371  4.339   -37.836 1.00 15.07 ? 120 HIS C O   1 
ATOM   5264 C  CB  . HIS C  1 120 ? 48.092  1.745   -37.143 1.00 14.73 ? 120 HIS C CB  1 
ATOM   5265 C  CG  . HIS C  1 120 ? 48.222  0.458   -36.373 1.00 16.07 ? 120 HIS C CG  1 
ATOM   5266 N  ND1 . HIS C  1 120 ? 47.145  -0.252  -35.865 1.00 15.03 ? 120 HIS C ND1 1 
ATOM   5267 C  CD2 . HIS C  1 120 ? 49.346  -0.266  -36.044 1.00 16.57 ? 120 HIS C CD2 1 
ATOM   5268 C  CE1 . HIS C  1 120 ? 47.598  -1.371  -35.272 1.00 17.00 ? 120 HIS C CE1 1 
ATOM   5269 N  NE2 . HIS C  1 120 ? 48.951  -1.399  -35.375 1.00 17.37 ? 120 HIS C NE2 1 
ATOM   5270 N  N   . TYR C  1 121 ? 48.587  4.753   -37.703 1.00 14.82 ? 121 TYR C N   1 
ATOM   5271 C  CA  . TYR C  1 121 ? 48.537  5.829   -38.682 1.00 17.17 ? 121 TYR C CA  1 
ATOM   5272 C  C   . TYR C  1 121 ? 49.535  5.528   -39.822 1.00 16.67 ? 121 TYR C C   1 
ATOM   5273 O  O   . TYR C  1 121 ? 50.511  4.762   -39.627 1.00 15.54 ? 121 TYR C O   1 
ATOM   5274 C  CB  . TYR C  1 121 ? 48.801  7.178   -38.022 1.00 18.21 ? 121 TYR C CB  1 
ATOM   5275 C  CG  . TYR C  1 121 ? 50.221  7.427   -37.585 1.00 17.78 ? 121 TYR C CG  1 
ATOM   5276 C  CD1 . TYR C  1 121 ? 50.670  6.855   -36.394 1.00 19.58 ? 121 TYR C CD1 1 
ATOM   5277 C  CD2 . TYR C  1 121 ? 51.077  8.162   -38.389 1.00 18.11 ? 121 TYR C CD2 1 
ATOM   5278 C  CE1 . TYR C  1 121 ? 52.006  7.017   -35.954 1.00 20.82 ? 121 TYR C CE1 1 
ATOM   5279 C  CE2 . TYR C  1 121 ? 52.427  8.360   -37.947 1.00 20.00 ? 121 TYR C CE2 1 
ATOM   5280 C  CZ  . TYR C  1 121 ? 52.843  7.759   -36.751 1.00 21.71 ? 121 TYR C CZ  1 
ATOM   5281 O  OH  . TYR C  1 121 ? 54.172  7.917   -36.266 1.00 23.27 ? 121 TYR C OH  1 
ATOM   5282 N  N   . ASN C  1 122 ? 49.271  6.131   -40.984 1.00 16.41 ? 122 ASN C N   1 
ATOM   5283 C  CA  . ASN C  1 122 ? 50.108  5.909   -42.155 1.00 17.23 ? 122 ASN C CA  1 
ATOM   5284 C  C   . ASN C  1 122 ? 51.376  6.783   -42.042 1.00 17.94 ? 122 ASN C C   1 
ATOM   5285 O  O   . ASN C  1 122 ? 51.358  7.990   -42.265 1.00 19.58 ? 122 ASN C O   1 
ATOM   5286 C  CB  . ASN C  1 122 ? 49.343  6.323   -43.371 1.00 17.74 ? 122 ASN C CB  1 
ATOM   5287 C  CG  . ASN C  1 122 ? 50.024  5.938   -44.639 1.00 18.86 ? 122 ASN C CG  1 
ATOM   5288 O  OD1 . ASN C  1 122 ? 51.275  5.922   -44.684 1.00 18.49 ? 122 ASN C OD1 1 
ATOM   5289 N  ND2 . ASN C  1 122 ? 49.261  5.611   -45.694 1.00 18.78 ? 122 ASN C ND2 1 
ATOM   5290 N  N   . SER C  1 123 ? 52.409  6.085   -41.555 1.00 16.42 ? 123 SER C N   1 
ATOM   5291 C  CA  . SER C  1 123 ? 53.681  6.792   -41.250 1.00 18.20 ? 123 SER C CA  1 
ATOM   5292 C  C   . SER C  1 123 ? 54.537  6.984   -42.500 1.00 19.16 ? 123 SER C C   1 
ATOM   5293 O  O   . SER C  1 123 ? 55.458  7.842   -42.433 1.00 20.08 ? 123 SER C O   1 
ATOM   5294 C  CB  . SER C  1 123 ? 54.429  6.044   -40.164 1.00 17.21 ? 123 SER C CB  1 
ATOM   5295 O  OG  . SER C  1 123 ? 54.595  4.660   -40.361 1.00 17.54 ? 123 SER C OG  1 
ATOM   5296 N  N   . ASP C  1 124 ? 54.230  6.285   -43.579 1.00 18.33 ? 124 ASP C N   1 
ATOM   5297 C  CA  . ASP C  1 124 ? 54.876  6.558   -44.895 1.00 18.19 ? 124 ASP C CA  1 
ATOM   5298 C  C   . ASP C  1 124 ? 54.424  7.898   -45.467 1.00 23.41 ? 124 ASP C C   1 
ATOM   5299 O  O   . ASP C  1 124 ? 55.217  8.593   -46.089 1.00 25.38 ? 124 ASP C O   1 
ATOM   5300 C  CB  . ASP C  1 124 ? 54.602  5.447   -45.897 1.00 18.39 ? 124 ASP C CB  1 
ATOM   5301 C  CG  . ASP C  1 124 ? 55.260  4.173   -45.560 1.00 19.09 ? 124 ASP C CG  1 
ATOM   5302 O  OD1 . ASP C  1 124 ? 56.303  4.198   -44.783 1.00 20.25 ? 124 ASP C OD1 1 
ATOM   5303 O  OD2 . ASP C  1 124 ? 54.876  3.105   -46.068 1.00 19.04 ? 124 ASP C OD2 1 
ATOM   5304 N  N   . LEU C  1 125 ? 53.177  8.263   -45.263 1.00 18.40 ? 125 LEU C N   1 
ATOM   5305 C  CA  . LEU C  1 125 ? 52.635  9.526   -45.760 1.00 21.77 ? 125 LEU C CA  1 
ATOM   5306 C  C   . LEU C  1 125 ? 52.706  10.698  -44.747 1.00 24.08 ? 125 LEU C C   1 
ATOM   5307 O  O   . LEU C  1 125 ? 52.822  11.883  -45.163 1.00 24.88 ? 125 LEU C O   1 
ATOM   5308 C  CB  . LEU C  1 125 ? 51.197  9.342   -46.258 1.00 21.01 ? 125 LEU C CB  1 
ATOM   5309 C  CG  . LEU C  1 125 ? 50.958  8.309   -47.363 1.00 24.26 ? 125 LEU C CG  1 
ATOM   5310 C  CD1 . LEU C  1 125 ? 49.499  8.313   -47.794 1.00 27.48 ? 125 LEU C CD1 1 
ATOM   5311 C  CD2 . LEU C  1 125 ? 51.870  8.548   -48.556 1.00 22.69 ? 125 LEU C CD2 1 
ATOM   5312 N  N   . TYR C  1 126 ? 52.611  10.381  -43.454 1.00 18.34 ? 126 TYR C N   1 
ATOM   5313 C  CA  . TYR C  1 126 ? 52.351  11.424  -42.467 1.00 19.36 ? 126 TYR C CA  1 
ATOM   5314 C  C   . TYR C  1 126 ? 53.273  11.295  -41.268 1.00 20.50 ? 126 TYR C C   1 
ATOM   5315 O  O   . TYR C  1 126 ? 53.616  10.210  -40.878 1.00 21.38 ? 126 TYR C O   1 
ATOM   5316 C  CB  . TYR C  1 126 ? 50.856  11.423  -42.015 1.00 19.66 ? 126 TYR C CB  1 
ATOM   5317 C  CG  . TYR C  1 126 ? 49.919  11.398  -43.200 1.00 20.88 ? 126 TYR C CG  1 
ATOM   5318 C  CD1 . TYR C  1 126 ? 49.851  12.496  -44.096 1.00 22.90 ? 126 TYR C CD1 1 
ATOM   5319 C  CD2 . TYR C  1 126 ? 49.037  10.304  -43.441 1.00 20.63 ? 126 TYR C CD2 1 
ATOM   5320 C  CE1 . TYR C  1 126 ? 49.004  12.460  -45.182 1.00 21.91 ? 126 TYR C CE1 1 
ATOM   5321 C  CE2 . TYR C  1 126 ? 48.194  10.285  -44.542 1.00 21.53 ? 126 TYR C CE2 1 
ATOM   5322 C  CZ  . TYR C  1 126 ? 48.195  11.368  -45.401 1.00 22.56 ? 126 TYR C CZ  1 
ATOM   5323 O  OH  . TYR C  1 126 ? 47.313  11.365  -46.450 1.00 22.24 ? 126 TYR C OH  1 
ATOM   5324 N  N   . PRO C  1 127 ? 53.586  12.451  -40.641 1.00 22.61 ? 127 PRO C N   1 
ATOM   5325 C  CA  . PRO C  1 127 ? 54.551  12.447  -39.546 1.00 23.47 ? 127 PRO C CA  1 
ATOM   5326 C  C   . PRO C  1 127 ? 54.033  11.913  -38.192 1.00 24.08 ? 127 PRO C C   1 
ATOM   5327 O  O   . PRO C  1 127 ? 54.843  11.398  -37.368 1.00 25.22 ? 127 PRO C O   1 
ATOM   5328 C  CB  . PRO C  1 127 ? 54.925  13.936  -39.430 1.00 24.42 ? 127 PRO C CB  1 
ATOM   5329 C  CG  . PRO C  1 127 ? 53.755  14.682  -39.942 1.00 24.33 ? 127 PRO C CG  1 
ATOM   5330 C  CD  . PRO C  1 127 ? 53.177  13.822  -41.021 1.00 24.78 ? 127 PRO C CD  1 
ATOM   5331 N  N   . ASP C  1 128 ? 52.711  11.952  -37.987 1.00 22.12 ? 128 ASP C N   1 
ATOM   5332 C  CA  . ASP C  1 128 ? 52.190  11.528  -36.700 1.00 21.62 ? 128 ASP C CA  1 
ATOM   5333 C  C   . ASP C  1 128 ? 50.702  11.193  -36.886 1.00 20.32 ? 128 ASP C C   1 
ATOM   5334 O  O   . ASP C  1 128 ? 50.096  11.565  -37.945 1.00 20.84 ? 128 ASP C O   1 
ATOM   5335 C  CB  . ASP C  1 128 ? 52.422  12.593  -35.577 1.00 26.95 ? 128 ASP C CB  1 
ATOM   5336 C  CG  . ASP C  1 128 ? 52.104  14.021  -36.009 1.00 34.52 ? 128 ASP C CG  1 
ATOM   5337 O  OD1 . ASP C  1 128 ? 52.950  14.938  -35.842 1.00 38.34 ? 128 ASP C OD1 1 
ATOM   5338 O  OD2 . ASP C  1 128 ? 51.004  14.278  -36.497 1.00 31.28 ? 128 ASP C OD2 1 
ATOM   5339 N  N   . ALA C  1 129 ? 50.103  10.660  -35.818 1.00 21.00 ? 129 ALA C N   1 
ATOM   5340 C  CA  . ALA C  1 129 ? 48.685  10.231  -35.950 1.00 21.52 ? 129 ALA C CA  1 
ATOM   5341 C  C   . ALA C  1 129 ? 47.723  11.432  -36.101 1.00 24.33 ? 129 ALA C C   1 
ATOM   5342 O  O   . ALA C  1 129 ? 46.769  11.366  -36.845 1.00 22.38 ? 129 ALA C O   1 
ATOM   5343 C  CB  . ALA C  1 129 ? 48.279  9.382   -34.741 1.00 23.65 ? 129 ALA C CB  1 
ATOM   5344 N  N   . SER C  1 130 ? 47.969  12.492  -35.346 1.00 24.92 ? 130 SER C N   1 
ATOM   5345 C  CA  . SER C  1 130 ? 47.175  13.707  -35.372 1.00 28.08 ? 130 SER C CA  1 
ATOM   5346 C  C   . SER C  1 130 ? 47.079  14.249  -36.806 1.00 26.75 ? 130 SER C C   1 
ATOM   5347 O  O   . SER C  1 130 ? 45.981  14.530  -37.313 1.00 29.18 ? 130 SER C O   1 
ATOM   5348 C  CB  . SER C  1 130 ? 47.796  14.690  -34.344 1.00 30.35 ? 130 SER C CB  1 
ATOM   5349 O  OG  . SER C  1 130 ? 47.241  15.997  -34.474 1.00 37.79 ? 130 SER C OG  1 
ATOM   5350 N  N   . THR C  1 131 ? 48.233  14.389  -37.481 1.00 26.10 ? 131 THR C N   1 
ATOM   5351 C  CA  . THR C  1 131 ? 48.278  14.896  -38.829 1.00 22.66 ? 131 THR C CA  1 
ATOM   5352 C  C   . THR C  1 131 ? 47.568  13.889  -39.750 1.00 21.77 ? 131 THR C C   1 
ATOM   5353 O  O   . THR C  1 131 ? 46.889  14.268  -40.693 1.00 21.56 ? 131 THR C O   1 
ATOM   5354 C  CB  . THR C  1 131 ? 49.762  15.051  -39.273 1.00 25.35 ? 131 THR C CB  1 
ATOM   5355 O  OG1 . THR C  1 131 ? 50.421  15.902  -38.332 1.00 26.38 ? 131 THR C OG1 1 
ATOM   5356 C  CG2 . THR C  1 131 ? 49.896  15.604  -40.702 1.00 27.69 ? 131 THR C CG2 1 
ATOM   5357 N  N   . ALA C  1 132 ? 47.837  12.606  -39.527 1.00 20.42 ? 132 ALA C N   1 
ATOM   5358 C  CA  . ALA C  1 132 ? 47.220  11.568  -40.425 1.00 19.74 ? 132 ALA C CA  1 
ATOM   5359 C  C   . ALA C  1 132 ? 45.698  11.498  -40.330 1.00 19.99 ? 132 ALA C C   1 
ATOM   5360 O  O   . ALA C  1 132 ? 45.087  11.156  -41.329 1.00 17.95 ? 132 ALA C O   1 
ATOM   5361 C  CB  . ALA C  1 132 ? 47.752  10.209  -40.068 1.00 18.15 ? 132 ALA C CB  1 
ATOM   5362 N  N   . SER C  1 133 ? 45.139  11.879  -39.203 1.00 18.97 ? 133 SER C N   1 
ATOM   5363 C  CA  . SER C  1 133 ? 43.808  11.409  -38.850 1.00 19.39 ? 133 SER C CA  1 
ATOM   5364 C  C   . SER C  1 133 ? 42.752  11.907  -39.801 1.00 18.62 ? 133 SER C C   1 
ATOM   5365 O  O   . SER C  1 133 ? 41.738  11.212  -40.025 1.00 19.68 ? 133 SER C O   1 
ATOM   5366 C  CB  . SER C  1 133 ? 43.501  11.724  -37.365 1.00 21.46 ? 133 SER C CB  1 
ATOM   5367 O  OG  . SER C  1 133 ? 43.435  13.152  -37.214 1.00 23.50 ? 133 SER C OG  1 
ATOM   5368 N  N   . ASN C  1 134 ? 42.929  13.040  -40.434 1.00 17.88 ? 134 ASN C N   1 
ATOM   5369 C  CA  . ASN C  1 134 ? 41.913  13.620  -41.318 1.00 21.07 ? 134 ASN C CA  1 
ATOM   5370 C  C   . ASN C  1 134 ? 42.348  13.597  -42.806 1.00 19.41 ? 134 ASN C C   1 
ATOM   5371 O  O   . ASN C  1 134 ? 41.758  14.312  -43.636 1.00 23.83 ? 134 ASN C O   1 
ATOM   5372 C  CB  . ASN C  1 134 ? 41.469  15.046  -40.871 1.00 23.22 ? 134 ASN C CB  1 
ATOM   5373 C  CG  . ASN C  1 134 ? 42.591  16.066  -41.005 1.00 28.44 ? 134 ASN C CG  1 
ATOM   5374 O  OD1 . ASN C  1 134 ? 43.732  15.703  -41.155 1.00 27.69 ? 134 ASN C OD1 1 
ATOM   5375 N  ND2 . ASN C  1 134 ? 42.237  17.355  -41.009 1.00 30.96 ? 134 ASN C ND2 1 
ATOM   5376 N  N   . LYS C  1 135 ? 43.302  12.735  -43.178 1.00 18.84 ? 135 LYS C N   1 
ATOM   5377 C  CA  . LYS C  1 135 ? 43.903  12.737  -44.489 1.00 21.05 ? 135 LYS C CA  1 
ATOM   5378 C  C   . LYS C  1 135 ? 43.730  11.392  -45.139 1.00 19.60 ? 135 LYS C C   1 
ATOM   5379 O  O   . LYS C  1 135 ? 43.517  10.376  -44.465 1.00 17.84 ? 135 LYS C O   1 
ATOM   5380 C  CB  . LYS C  1 135 ? 45.415  13.067  -44.357 1.00 22.50 ? 135 LYS C CB  1 
ATOM   5381 C  CG  . LYS C  1 135 ? 45.607  14.520  -43.890 1.00 24.08 ? 135 LYS C CG  1 
ATOM   5382 C  CD  . LYS C  1 135 ? 47.036  15.058  -43.894 1.00 27.02 ? 135 LYS C CD  1 
ATOM   5383 C  CE  . LYS C  1 135 ? 47.000  16.476  -43.346 1.00 28.52 ? 135 LYS C CE  1 
ATOM   5384 N  NZ  . LYS C  1 135 ? 46.262  16.676  -42.054 1.00 29.57 ? 135 LYS C NZ  1 
ATOM   5385 N  N   . SER C  1 136 ? 43.816  11.360  -46.464 1.00 20.04 ? 136 SER C N   1 
ATOM   5386 C  CA  . SER C  1 136 ? 43.581  10.198  -47.280 1.00 20.01 ? 136 SER C CA  1 
ATOM   5387 C  C   . SER C  1 136 ? 44.481  9.076   -46.804 1.00 17.04 ? 136 SER C C   1 
ATOM   5388 O  O   . SER C  1 136 ? 45.706  9.256   -46.619 1.00 19.34 ? 136 SER C O   1 
ATOM   5389 C  CB  . SER C  1 136 ? 44.010  10.559  -48.683 1.00 22.40 ? 136 SER C CB  1 
ATOM   5390 O  OG  . SER C  1 136 ? 43.890  9.435   -49.494 1.00 32.11 ? 136 SER C OG  1 
ATOM   5391 N  N   . GLU C  1 137 ? 43.901  7.897   -46.657 1.00 18.75 ? 137 GLU C N   1 
ATOM   5392 C  CA  . GLU C  1 137 ? 44.681  6.731   -46.233 1.00 17.38 ? 137 GLU C CA  1 
ATOM   5393 C  C   . GLU C  1 137 ? 45.381  6.925   -44.929 1.00 16.23 ? 137 GLU C C   1 
ATOM   5394 O  O   . GLU C  1 137 ? 46.400  6.286   -44.698 1.00 16.89 ? 137 GLU C O   1 
ATOM   5395 C  CB  . GLU C  1 137 ? 45.684  6.291   -47.319 1.00 19.94 ? 137 GLU C CB  1 
ATOM   5396 C  CG  . GLU C  1 137 ? 44.974  5.813   -48.582 1.00 26.17 ? 137 GLU C CG  1 
ATOM   5397 C  CD  . GLU C  1 137 ? 45.894  5.421   -49.762 1.00 33.76 ? 137 GLU C CD  1 
ATOM   5398 O  OE1 . GLU C  1 137 ? 47.158  5.577   -49.758 1.00 41.77 ? 137 GLU C OE1 1 
ATOM   5399 O  OE2 . GLU C  1 137 ? 45.305  4.965   -50.744 1.00 34.10 ? 137 GLU C OE2 1 
ATOM   5400 N  N   . GLY C  1 138 ? 44.824  7.735   -44.059 1.00 15.67 ? 138 GLY C N   1 
ATOM   5401 C  CA  . GLY C  1 138 ? 45.517  8.184   -42.842 1.00 17.23 ? 138 GLY C CA  1 
ATOM   5402 C  C   . GLY C  1 138 ? 45.661  7.139   -41.767 1.00 17.53 ? 138 GLY C C   1 
ATOM   5403 O  O   . GLY C  1 138 ? 46.687  7.115   -41.049 1.00 16.46 ? 138 GLY C O   1 
ATOM   5404 N  N   . LEU C  1 139 ? 44.647  6.243   -41.600 1.00 14.44 ? 139 LEU C N   1 
ATOM   5405 C  CA  . LEU C  1 139 ? 44.567  5.382   -40.411 1.00 13.31 ? 139 LEU C CA  1 
ATOM   5406 C  C   . LEU C  1 139 ? 44.213  3.960   -40.763 1.00 13.93 ? 139 LEU C C   1 
ATOM   5407 O  O   . LEU C  1 139 ? 43.578  3.693   -41.820 1.00 14.38 ? 139 LEU C O   1 
ATOM   5408 C  CB  . LEU C  1 139 ? 43.575  5.873   -39.354 1.00 13.12 ? 139 LEU C CB  1 
ATOM   5409 C  CG  . LEU C  1 139 ? 43.752  7.310   -38.945 1.00 13.40 ? 139 LEU C CG  1 
ATOM   5410 C  CD1 . LEU C  1 139 ? 42.546  7.819   -38.157 1.00 16.94 ? 139 LEU C CD1 1 
ATOM   5411 C  CD2 . LEU C  1 139 ? 45.023  7.447   -38.139 1.00 15.59 ? 139 LEU C CD2 1 
ATOM   5412 N  N   . ALA C  1 140 ? 44.607  3.048   -39.897 1.00 12.46 ? 140 ALA C N   1 
ATOM   5413 C  CA  . ALA C  1 140 ? 44.221  1.649   -39.984 1.00 12.99 ? 140 ALA C CA  1 
ATOM   5414 C  C   . ALA C  1 140 ? 43.962  1.208   -38.567 1.00 13.39 ? 140 ALA C C   1 
ATOM   5415 O  O   . ALA C  1 140 ? 44.747  1.410   -37.675 1.00 14.99 ? 140 ALA C O   1 
ATOM   5416 C  CB  . ALA C  1 140 ? 45.270  0.779   -40.631 1.00 14.17 ? 140 ALA C CB  1 
ATOM   5417 N  N   . VAL C  1 141 ? 42.803  0.581   -38.340 1.00 12.57 ? 141 VAL C N   1 
ATOM   5418 C  CA  . VAL C  1 141 ? 42.458  0.129   -36.993 1.00 13.12 ? 141 VAL C CA  1 
ATOM   5419 C  C   . VAL C  1 141 ? 42.245  -1.358  -37.048 1.00 12.38 ? 141 VAL C C   1 
ATOM   5420 O  O   . VAL C  1 141 ? 41.601  -1.921  -37.988 1.00 13.72 ? 141 VAL C O   1 
ATOM   5421 C  CB  . VAL C  1 141 ? 41.246  0.850   -36.442 1.00 12.09 ? 141 VAL C CB  1 
ATOM   5422 C  CG1 . VAL C  1 141 ? 40.948  0.404   -34.982 1.00 14.02 ? 141 VAL C CG1 1 
ATOM   5423 C  CG2 . VAL C  1 141 ? 41.439  2.367   -36.478 1.00 14.02 ? 141 VAL C CG2 1 
ATOM   5424 N  N   . LEU C  1 142 ? 42.771  -2.050  -36.034 1.00 12.05 ? 142 LEU C N   1 
ATOM   5425 C  CA  . LEU C  1 142 ? 42.535  -3.431  -35.864 1.00 12.40 ? 142 LEU C CA  1 
ATOM   5426 C  C   . LEU C  1 142 ? 41.489  -3.602  -34.813 1.00 13.00 ? 142 LEU C C   1 
ATOM   5427 O  O   . LEU C  1 142 ? 41.626  -2.995  -33.717 1.00 13.82 ? 142 LEU C O   1 
ATOM   5428 C  CB  . LEU C  1 142 ? 43.826  -4.211  -35.355 1.00 13.70 ? 142 LEU C CB  1 
ATOM   5429 C  CG  . LEU C  1 142 ? 45.036  -4.018  -36.279 1.00 14.40 ? 142 LEU C CG  1 
ATOM   5430 C  CD1 . LEU C  1 142 ? 46.142  -4.822  -35.570 1.00 19.84 ? 142 LEU C CD1 1 
ATOM   5431 C  CD2 . LEU C  1 142 ? 44.836  -4.665  -37.631 1.00 16.18 ? 142 LEU C CD2 1 
ATOM   5432 N  N   . ALA C  1 143 ? 40.427  -4.392  -35.085 1.00 11.42 ? 143 ALA C N   1 
ATOM   5433 C  CA  . ALA C  1 143 ? 39.347  -4.619  -34.099 1.00 13.13 ? 143 ALA C CA  1 
ATOM   5434 C  C   . ALA C  1 143 ? 39.244  -6.024  -33.684 1.00 12.10 ? 143 ALA C C   1 
ATOM   5435 O  O   . ALA C  1 143 ? 39.254  -6.943  -34.474 1.00 12.54 ? 143 ALA C O   1 
ATOM   5436 C  CB  . ALA C  1 143 ? 37.989  -4.137  -34.685 1.00 13.16 ? 143 ALA C CB  1 
ATOM   5437 N  N   . VAL C  1 144 ? 39.228  -6.162  -32.357 1.00 13.35 ? 144 VAL C N   1 
ATOM   5438 C  CA  . VAL C  1 144 ? 39.070  -7.521  -31.800 1.00 14.01 ? 144 VAL C CA  1 
ATOM   5439 C  C   . VAL C  1 144 ? 37.767  -7.612  -31.008 1.00 14.58 ? 144 VAL C C   1 
ATOM   5440 O  O   . VAL C  1 144 ? 37.514  -6.747  -30.128 1.00 14.21 ? 144 VAL C O   1 
ATOM   5441 C  CB  . VAL C  1 144 ? 40.228  -7.820  -30.810 1.00 15.09 ? 144 VAL C CB  1 
ATOM   5442 C  CG1 . VAL C  1 144 ? 40.073  -9.217  -30.233 1.00 16.78 ? 144 VAL C CG1 1 
ATOM   5443 C  CG2 . VAL C  1 144 ? 41.557  -7.709  -31.506 1.00 15.73 ? 144 VAL C CG2 1 
ATOM   5444 N  N   . LEU C  1 145 ? 36.944  -8.575  -31.446 1.00 15.56 ? 145 LEU C N   1 
ATOM   5445 C  CA  . LEU C  1 145 ? 35.672  -8.788  -30.740 1.00 15.18 ? 145 LEU C CA  1 
ATOM   5446 C  C   . LEU C  1 145 ? 35.915  -9.543  -29.418 1.00 15.51 ? 145 LEU C C   1 
ATOM   5447 O  O   . LEU C  1 145 ? 36.707  -10.499 -29.462 1.00 17.79 ? 145 LEU C O   1 
ATOM   5448 C  CB  . LEU C  1 145 ? 34.622  -9.437  -31.620 1.00 16.51 ? 145 LEU C CB  1 
ATOM   5449 C  CG  . LEU C  1 145 ? 34.411  -8.657  -32.947 1.00 13.49 ? 145 LEU C CG  1 
ATOM   5450 C  CD1 . LEU C  1 145 ? 33.773  -9.586  -33.920 1.00 17.17 ? 145 LEU C CD1 1 
ATOM   5451 C  CD2 . LEU C  1 145 ? 33.458  -7.521  -32.624 1.00 16.10 ? 145 LEU C CD2 1 
ATOM   5452 N  N   . ILE C  1 146 ? 35.242  -9.108  -28.375 1.00 13.30 ? 146 ILE C N   1 
ATOM   5453 C  CA  . ILE C  1 146 ? 35.486  -9.708  -26.960 1.00 13.90 ? 146 ILE C CA  1 
ATOM   5454 C  C   . ILE C  1 146 ? 34.184  -10.350 -26.532 1.00 16.74 ? 146 ILE C C   1 
ATOM   5455 O  O   . ILE C  1 146 ? 33.152  -9.701  -26.526 1.00 15.39 ? 146 ILE C O   1 
ATOM   5456 C  CB  . ILE C  1 146 ? 35.939  -8.663  -25.999 1.00 14.71 ? 146 ILE C CB  1 
ATOM   5457 C  CG1 . ILE C  1 146 ? 37.282  -8.062  -26.514 1.00 16.02 ? 146 ILE C CG1 1 
ATOM   5458 C  CG2 . ILE C  1 146 ? 36.142  -9.329  -24.623 1.00 16.18 ? 146 ILE C CG2 1 
ATOM   5459 C  CD1 . ILE C  1 146 ? 37.665  -6.804  -25.771 1.00 16.19 ? 146 ILE C CD1 1 
ATOM   5460 N  N   . GLU C  1 147 ? 34.261  -11.605 -26.054 1.00 18.83 ? 147 GLU C N   1 
ATOM   5461 C  CA  . GLU C  1 147 ? 33.128  -12.274 -25.412 1.00 22.39 ? 147 GLU C CA  1 
ATOM   5462 C  C   . GLU C  1 147 ? 33.543  -12.812 -24.027 1.00 20.52 ? 147 GLU C C   1 
ATOM   5463 O  O   . GLU C  1 147 ? 34.713  -12.913 -23.720 1.00 21.70 ? 147 GLU C O   1 
ATOM   5464 C  CB  . GLU C  1 147 ? 32.604  -13.408 -26.263 1.00 21.69 ? 147 GLU C CB  1 
ATOM   5465 C  CG  . GLU C  1 147 ? 33.605  -14.509 -26.485 1.00 22.48 ? 147 GLU C CG  1 
ATOM   5466 C  CD  . GLU C  1 147 ? 33.143  -15.533 -27.523 1.00 26.34 ? 147 GLU C CD  1 
ATOM   5467 O  OE1 . GLU C  1 147 ? 32.107  -15.308 -28.219 1.00 29.93 ? 147 GLU C OE1 1 
ATOM   5468 O  OE2 . GLU C  1 147 ? 33.847  -16.597 -27.666 1.00 33.13 ? 147 GLU C OE2 1 
ATOM   5469 N  N   . MET C  1 148 ? 32.521  -13.035 -23.197 1.00 22.22 ? 148 MET C N   1 
ATOM   5470 C  CA  . MET C  1 148 ? 32.712  -13.754 -21.925 1.00 26.80 ? 148 MET C CA  1 
ATOM   5471 C  C   . MET C  1 148 ? 33.243  -15.171 -22.169 1.00 26.22 ? 148 MET C C   1 
ATOM   5472 O  O   . MET C  1 148 ? 32.777  -15.914 -23.049 1.00 24.00 ? 148 MET C O   1 
ATOM   5473 C  CB  . MET C  1 148 ? 31.383  -13.910 -21.181 1.00 30.47 ? 148 MET C CB  1 
ATOM   5474 C  CG  . MET C  1 148 ? 30.823  -12.726 -20.387 1.00 40.22 ? 148 MET C CG  1 
ATOM   5475 S  SD  . MET C  1 148 ? 29.883  -13.284 -18.914 1.00 60.56 ? 148 MET C SD  1 
ATOM   5476 C  CE  . MET C  1 148 ? 28.546  -14.225 -19.674 1.00 48.84 ? 148 MET C CE  1 
ATOM   5477 N  N   . GLY C  1 149 ? 34.230  -15.556 -21.346 1.00 26.95 ? 149 GLY C N   1 
ATOM   5478 C  CA  . GLY C  1 149 ? 34.722  -16.932 -21.321 1.00 29.33 ? 149 GLY C CA  1 
ATOM   5479 C  C   . GLY C  1 149 ? 35.752  -17.084 -20.177 1.00 23.90 ? 149 GLY C C   1 
ATOM   5480 O  O   . GLY C  1 149 ? 35.546  -16.559 -19.087 1.00 26.30 ? 149 GLY C O   1 
ATOM   5481 N  N   . SER C  1 150 ? 36.857  -17.735 -20.535 1.00 30.52 ? 150 SER C N   1 
ATOM   5482 C  CA  . SER C  1 150 ? 38.045  -17.947 -19.714 1.00 30.85 ? 150 SER C CA  1 
ATOM   5483 C  C   . SER C  1 150 ? 38.705  -16.645 -19.330 1.00 34.63 ? 150 SER C C   1 
ATOM   5484 O  O   . SER C  1 150 ? 38.736  -15.703 -20.159 1.00 26.49 ? 150 SER C O   1 
ATOM   5485 C  CB  . SER C  1 150 ? 39.092  -18.727 -20.505 1.00 34.23 ? 150 SER C CB  1 
ATOM   5486 O  OG  . SER C  1 150 ? 38.634  -20.049 -20.744 1.00 42.40 ? 150 SER C OG  1 
ATOM   5487 N  N   . PHE C  1 151 ? 39.266  -16.600 -18.116 1.00 28.51 ? 151 PHE C N   1 
ATOM   5488 C  CA  . PHE C  1 151 ? 40.136  -15.531 -17.667 1.00 29.69 ? 151 PHE C CA  1 
ATOM   5489 C  C   . PHE C  1 151 ? 41.261  -15.289 -18.661 1.00 27.28 ? 151 PHE C C   1 
ATOM   5490 O  O   . PHE C  1 151 ? 41.917  -16.236 -19.159 1.00 31.17 ? 151 PHE C O   1 
ATOM   5491 C  CB  . PHE C  1 151 ? 40.750  -15.859 -16.263 1.00 27.81 ? 151 PHE C CB  1 
ATOM   5492 C  CG  . PHE C  1 151 ? 41.639  -14.779 -15.734 1.00 26.92 ? 151 PHE C CG  1 
ATOM   5493 C  CD1 . PHE C  1 151 ? 41.092  -13.599 -15.263 1.00 25.35 ? 151 PHE C CD1 1 
ATOM   5494 C  CD2 . PHE C  1 151 ? 43.042  -14.913 -15.767 1.00 27.41 ? 151 PHE C CD2 1 
ATOM   5495 C  CE1 . PHE C  1 151 ? 41.911  -12.562 -14.813 1.00 25.12 ? 151 PHE C CE1 1 
ATOM   5496 C  CE2 . PHE C  1 151 ? 43.861  -13.899 -15.290 1.00 27.76 ? 151 PHE C CE2 1 
ATOM   5497 C  CZ  . PHE C  1 151 ? 43.294  -12.719 -14.798 1.00 28.51 ? 151 PHE C CZ  1 
ATOM   5498 N  N   . ASN C  1 152 ? 41.549  -14.010 -18.913 1.00 24.53 ? 152 ASN C N   1 
ATOM   5499 C  CA  . ASN C  1 152 ? 42.587  -13.693 -19.870 1.00 20.72 ? 152 ASN C CA  1 
ATOM   5500 C  C   . ASN C  1 152 ? 43.726  -12.848 -19.263 1.00 21.82 ? 152 ASN C C   1 
ATOM   5501 O  O   . ASN C  1 152 ? 43.579  -11.645 -18.972 1.00 25.24 ? 152 ASN C O   1 
ATOM   5502 C  CB  . ASN C  1 152 ? 41.897  -12.929 -21.095 1.00 22.48 ? 152 ASN C CB  1 
ATOM   5503 C  CG  . ASN C  1 152 ? 42.820  -12.796 -22.268 1.00 25.30 ? 152 ASN C CG  1 
ATOM   5504 O  OD1 . ASN C  1 152 ? 43.959  -12.368 -22.076 1.00 24.47 ? 152 ASN C OD1 1 
ATOM   5505 N  ND2 . ASN C  1 152 ? 42.329  -13.052 -23.526 1.00 24.67 ? 152 ASN C ND2 1 
ATOM   5506 N  N   . PRO C  1 153 ? 44.876  -13.486 -18.975 1.00 24.06 ? 153 PRO C N   1 
ATOM   5507 C  CA  . PRO C  1 153 ? 45.940  -12.784 -18.264 1.00 25.57 ? 153 PRO C CA  1 
ATOM   5508 C  C   . PRO C  1 153 ? 46.530  -11.654 -19.069 1.00 24.42 ? 153 PRO C C   1 
ATOM   5509 O  O   . PRO C  1 153 ? 46.980  -10.670 -18.514 1.00 28.11 ? 153 PRO C O   1 
ATOM   5510 C  CB  . PRO C  1 153 ? 46.971  -13.892 -17.967 1.00 25.10 ? 153 PRO C CB  1 
ATOM   5511 C  CG  . PRO C  1 153 ? 46.466  -15.149 -18.568 1.00 26.52 ? 153 PRO C CG  1 
ATOM   5512 C  CD  . PRO C  1 153 ? 45.182  -14.896 -19.326 1.00 23.82 ? 153 PRO C CD  1 
ATOM   5513 N  N   . SER C  1 154 ? 46.420  -11.733 -20.397 1.00 28.14 ? 154 SER C N   1 
ATOM   5514 C  CA  . SER C  1 154 ? 46.893  -10.651 -21.264 1.00 25.10 ? 154 SER C CA  1 
ATOM   5515 C  C   . SER C  1 154 ? 46.070  -9.366  -21.130 1.00 18.63 ? 154 SER C C   1 
ATOM   5516 O  O   . SER C  1 154 ? 46.631  -8.249  -20.910 1.00 20.97 ? 154 SER C O   1 
ATOM   5517 C  CB  . SER C  1 154 ? 47.011  -11.171 -22.682 1.00 29.67 ? 154 SER C CB  1 
ATOM   5518 O  OG  . SER C  1 154 ? 47.886  -12.298 -22.687 1.00 29.84 ? 154 SER C OG  1 
ATOM   5519 N  N   . TYR C  1 155 ? 44.715  -9.502  -21.218 1.00 20.37 ? 155 TYR C N   1 
ATOM   5520 C  CA  . TYR C  1 155 ? 43.868  -8.360  -20.963 1.00 23.34 ? 155 TYR C CA  1 
ATOM   5521 C  C   . TYR C  1 155 ? 44.017  -7.817  -19.557 1.00 19.89 ? 155 TYR C C   1 
ATOM   5522 O  O   . TYR C  1 155 ? 43.813  -6.588  -19.283 1.00 20.77 ? 155 TYR C O   1 
ATOM   5523 C  CB  . TYR C  1 155 ? 42.392  -8.671  -21.341 1.00 18.13 ? 155 TYR C CB  1 
ATOM   5524 C  CG  . TYR C  1 155 ? 42.211  -8.531  -22.879 1.00 18.28 ? 155 TYR C CG  1 
ATOM   5525 C  CD1 . TYR C  1 155 ? 42.647  -9.559  -23.736 1.00 21.09 ? 155 TYR C CD1 1 
ATOM   5526 C  CD2 . TYR C  1 155 ? 41.598  -7.377  -23.416 1.00 17.48 ? 155 TYR C CD2 1 
ATOM   5527 C  CE1 . TYR C  1 155 ? 42.488  -9.478  -25.155 1.00 19.62 ? 155 TYR C CE1 1 
ATOM   5528 C  CE2 . TYR C  1 155 ? 41.428  -7.289  -24.821 1.00 18.77 ? 155 TYR C CE2 1 
ATOM   5529 C  CZ  . TYR C  1 155 ? 41.840  -8.319  -25.636 1.00 20.41 ? 155 TYR C CZ  1 
ATOM   5530 O  OH  . TYR C  1 155 ? 41.711  -8.097  -27.007 1.00 19.05 ? 155 TYR C OH  1 
ATOM   5531 N  N   . ASP C  1 156 ? 44.377  -8.689  -18.596 1.00 22.94 ? 156 ASP C N   1 
ATOM   5532 C  CA  . ASP C  1 156 ? 44.527  -8.215  -17.261 1.00 27.99 ? 156 ASP C CA  1 
ATOM   5533 C  C   . ASP C  1 156 ? 45.753  -7.289  -17.071 1.00 26.44 ? 156 ASP C C   1 
ATOM   5534 O  O   . ASP C  1 156 ? 45.821  -6.588  -16.031 1.00 25.13 ? 156 ASP C O   1 
ATOM   5535 C  CB  . ASP C  1 156 ? 44.590  -9.385  -16.276 1.00 29.68 ? 156 ASP C CB  1 
ATOM   5536 C  CG  . ASP C  1 156 ? 43.612  -9.230  -15.127 1.00 34.16 ? 156 ASP C CG  1 
ATOM   5537 O  OD1 . ASP C  1 156 ? 42.422  -8.957  -15.391 1.00 30.07 ? 156 ASP C OD1 1 
ATOM   5538 O  OD2 . ASP C  1 156 ? 44.033  -9.379  -13.961 1.00 35.50 ? 156 ASP C OD2 1 
ATOM   5539 N  N   . LYS C  1 157 ? 46.672  -7.293  -18.047 1.00 25.39 ? 157 LYS C N   1 
ATOM   5540 C  CA  . LYS C  1 157 ? 47.840  -6.391  -18.019 1.00 26.11 ? 157 LYS C CA  1 
ATOM   5541 C  C   . LYS C  1 157 ? 47.380  -4.977  -18.183 1.00 30.35 ? 157 LYS C C   1 
ATOM   5542 O  O   . LYS C  1 157 ? 48.098  -4.046  -17.710 1.00 34.79 ? 157 LYS C O   1 
ATOM   5543 C  CB  . LYS C  1 157 ? 48.906  -6.808  -19.024 1.00 30.55 ? 157 LYS C CB  1 
ATOM   5544 C  CG  . LYS C  1 157 ? 49.295  -8.272  -18.821 1.00 29.26 ? 157 LYS C CG  1 
ATOM   5545 C  CD  . LYS C  1 157 ? 50.352  -8.762  -19.785 1.00 31.78 ? 157 LYS C CD  1 
ATOM   5546 C  CE  . LYS C  1 157 ? 51.114  -9.902  -19.155 1.00 35.62 ? 157 LYS C CE  1 
ATOM   5547 N  NZ  . LYS C  1 157 ? 51.264  -10.891 -20.254 1.00 35.67 ? 157 LYS C NZ  1 
ATOM   5548 N  N   . ILE C  1 158 ? 46.169  -4.804  -18.771 1.00 26.77 ? 158 ILE C N   1 
ATOM   5549 C  CA  . ILE C  1 158 ? 45.516  -3.500  -18.773 1.00 25.51 ? 158 ILE C CA  1 
ATOM   5550 C  C   . ILE C  1 158 ? 44.563  -3.314  -17.579 1.00 24.52 ? 158 ILE C C   1 
ATOM   5551 O  O   . ILE C  1 158 ? 44.590  -2.263  -16.868 1.00 24.35 ? 158 ILE C O   1 
ATOM   5552 C  CB  . ILE C  1 158 ? 44.783  -3.267  -20.124 1.00 24.24 ? 158 ILE C CB  1 
ATOM   5553 C  CG1 . ILE C  1 158 ? 45.854  -3.116  -21.191 1.00 26.29 ? 158 ILE C CG1 1 
ATOM   5554 C  CG2 . ILE C  1 158 ? 44.128  -1.889  -20.103 1.00 23.07 ? 158 ILE C CG2 1 
ATOM   5555 C  CD1 . ILE C  1 158 ? 45.317  -3.290  -22.611 1.00 27.80 ? 158 ILE C CD1 1 
ATOM   5556 N  N   . PHE C  1 159 ? 43.610  -4.246  -17.461 1.00 21.88 ? 159 PHE C N   1 
ATOM   5557 C  CA  . PHE C  1 159 ? 42.508  -4.107  -16.546 1.00 24.14 ? 159 PHE C CA  1 
ATOM   5558 C  C   . PHE C  1 159 ? 42.991  -3.967  -15.080 1.00 23.76 ? 159 PHE C C   1 
ATOM   5559 O  O   . PHE C  1 159 ? 42.250  -3.409  -14.281 1.00 25.47 ? 159 PHE C O   1 
ATOM   5560 C  CB  . PHE C  1 159 ? 41.523  -5.285  -16.616 1.00 24.20 ? 159 PHE C CB  1 
ATOM   5561 C  CG  . PHE C  1 159 ? 40.875  -5.505  -17.978 1.00 24.75 ? 159 PHE C CG  1 
ATOM   5562 C  CD1 . PHE C  1 159 ? 40.737  -4.465  -18.966 1.00 25.76 ? 159 PHE C CD1 1 
ATOM   5563 C  CD2 . PHE C  1 159 ? 40.336  -6.745  -18.228 1.00 22.45 ? 159 PHE C CD2 1 
ATOM   5564 C  CE1 . PHE C  1 159 ? 40.078  -4.773  -20.184 1.00 21.60 ? 159 PHE C CE1 1 
ATOM   5565 C  CE2 . PHE C  1 159 ? 39.696  -7.036  -19.433 1.00 26.88 ? 159 PHE C CE2 1 
ATOM   5566 C  CZ  . PHE C  1 159 ? 39.587  -6.053  -20.388 1.00 23.13 ? 159 PHE C CZ  1 
ATOM   5567 N  N   . SER C  1 160 ? 44.215  -4.419  -14.806 1.00 25.69 ? 160 SER C N   1 
ATOM   5568 C  CA  . SER C  1 160 ? 44.766  -4.333  -13.445 1.00 23.97 ? 160 SER C CA  1 
ATOM   5569 C  C   . SER C  1 160 ? 45.207  -2.938  -13.078 1.00 28.62 ? 160 SER C C   1 
ATOM   5570 O  O   . SER C  1 160 ? 45.594  -2.711  -11.913 1.00 23.67 ? 160 SER C O   1 
ATOM   5571 C  CB  . SER C  1 160 ? 45.885  -5.370  -13.282 1.00 28.39 ? 160 SER C CB  1 
ATOM   5572 O  OG  . SER C  1 160 ? 47.069  -4.977  -13.970 1.00 28.46 ? 160 SER C OG  1 
ATOM   5573 N  N   . HIS C  1 161 ? 45.103  -1.967  -13.978 1.00 24.16 ? 161 HIS C N   1 
ATOM   5574 C  CA  . HIS C  1 161 ? 45.400  -0.562  -13.658 1.00 23.73 ? 161 HIS C CA  1 
ATOM   5575 C  C   . HIS C  1 161 ? 44.228  0.344   -13.677 1.00 20.39 ? 161 HIS C C   1 
ATOM   5576 O  O   . HIS C  1 161 ? 44.366  1.597   -13.468 1.00 21.50 ? 161 HIS C O   1 
ATOM   5577 C  CB  . HIS C  1 161 ? 46.555  -0.078  -14.589 1.00 24.27 ? 161 HIS C CB  1 
ATOM   5578 C  CG  . HIS C  1 161 ? 47.818  -0.923  -14.461 1.00 30.91 ? 161 HIS C CG  1 
ATOM   5579 N  ND1 . HIS C  1 161 ? 48.887  -0.529  -13.678 1.00 36.97 ? 161 HIS C ND1 1 
ATOM   5580 C  CD2 . HIS C  1 161 ? 48.108  -2.221  -14.911 1.00 29.77 ? 161 HIS C CD2 1 
ATOM   5581 C  CE1 . HIS C  1 161 ? 49.833  -1.503  -13.702 1.00 35.90 ? 161 HIS C CE1 1 
ATOM   5582 N  NE2 . HIS C  1 161 ? 49.351  -2.548  -14.436 1.00 37.60 ? 161 HIS C NE2 1 
ATOM   5583 N  N   . LEU C  1 162 ? 43.033  -0.226  -13.976 1.00 21.77 ? 162 LEU C N   1 
ATOM   5584 C  CA  . LEU C  1 162 ? 41.883  0.637   -14.131 1.00 21.89 ? 162 LEU C CA  1 
ATOM   5585 C  C   . LEU C  1 162 ? 41.579  1.488   -12.949 1.00 18.98 ? 162 LEU C C   1 
ATOM   5586 O  O   . LEU C  1 162 ? 41.070  2.603   -13.096 1.00 19.38 ? 162 LEU C O   1 
ATOM   5587 C  CB  . LEU C  1 162 ? 40.647  -0.150  -14.601 1.00 23.09 ? 162 LEU C CB  1 
ATOM   5588 C  CG  . LEU C  1 162 ? 40.835  -0.896  -15.915 1.00 26.17 ? 162 LEU C CG  1 
ATOM   5589 C  CD1 . LEU C  1 162 ? 39.627  -1.753  -16.229 1.00 29.15 ? 162 LEU C CD1 1 
ATOM   5590 C  CD2 . LEU C  1 162 ? 41.061  0.180   -16.990 1.00 29.16 ? 162 LEU C CD2 1 
ATOM   5591 N  N   . GLN C  1 163 ? 41.858  0.964   -11.706 1.00 21.02 ? 163 GLN C N   1 
ATOM   5592 C  CA  . GLN C  1 163 ? 41.472  1.736   -10.531 1.00 23.40 ? 163 GLN C CA  1 
ATOM   5593 C  C   . GLN C  1 163 ? 42.426  2.944   -10.274 1.00 19.52 ? 163 GLN C C   1 
ATOM   5594 O  O   . GLN C  1 163 ? 42.181  3.733   -9.334  1.00 25.74 ? 163 GLN C O   1 
ATOM   5595 C  CB  . GLN C  1 163 ? 41.426  0.854   -9.254  1.00 23.07 ? 163 GLN C CB  1 
ATOM   5596 C  CG  . GLN C  1 163 ? 40.408  -0.306  -9.187  1.00 27.24 ? 163 GLN C CG  1 
ATOM   5597 C  CD  . GLN C  1 163 ? 38.953  0.111   -9.335  1.00 27.30 ? 163 GLN C CD  1 
ATOM   5598 O  OE1 . GLN C  1 163 ? 38.468  1.130   -8.791  1.00 27.04 ? 163 GLN C OE1 1 
ATOM   5599 N  NE2 . GLN C  1 163 ? 38.230  -0.669  -10.160 1.00 27.82 ? 163 GLN C NE2 1 
ATOM   5600 N  N   . HIS C  1 164 ? 43.487  3.105   -11.094 1.00 19.17 ? 164 HIS C N   1 
ATOM   5601 C  CA  . HIS C  1 164 ? 44.394  4.252   -11.056 1.00 20.43 ? 164 HIS C CA  1 
ATOM   5602 C  C   . HIS C  1 164 ? 43.989  5.364   -12.005 1.00 23.60 ? 164 HIS C C   1 
ATOM   5603 O  O   . HIS C  1 164 ? 44.488  6.493   -11.945 1.00 22.39 ? 164 HIS C O   1 
ATOM   5604 C  CB  . HIS C  1 164 ? 45.847  3.841   -11.303 1.00 22.90 ? 164 HIS C CB  1 
ATOM   5605 C  CG  . HIS C  1 164 ? 46.293  2.721   -10.400 1.00 22.59 ? 164 HIS C CG  1 
ATOM   5606 N  ND1 . HIS C  1 164 ? 46.304  2.855   -9.044  1.00 25.73 ? 164 HIS C ND1 1 
ATOM   5607 C  CD2 . HIS C  1 164 ? 46.776  1.448   -10.688 1.00 21.92 ? 164 HIS C CD2 1 
ATOM   5608 C  CE1 . HIS C  1 164 ? 46.696  1.683   -8.492  1.00 21.66 ? 164 HIS C CE1 1 
ATOM   5609 N  NE2 . HIS C  1 164 ? 46.979  0.814   -9.487  1.00 23.16 ? 164 HIS C NE2 1 
ATOM   5610 N  N   . VAL C  1 165 ? 43.012  5.059   -12.874 1.00 23.10 ? 165 VAL C N   1 
ATOM   5611 C  CA  . VAL C  1 165 ? 42.484  6.108   -13.774 1.00 22.88 ? 165 VAL C CA  1 
ATOM   5612 C  C   . VAL C  1 165 ? 40.938  6.217   -13.740 1.00 22.31 ? 165 VAL C C   1 
ATOM   5613 O  O   . VAL C  1 165 ? 40.236  6.400   -14.790 1.00 19.86 ? 165 VAL C O   1 
ATOM   5614 C  CB  . VAL C  1 165 ? 43.046  5.918   -15.208 1.00 22.40 ? 165 VAL C CB  1 
ATOM   5615 C  CG1 . VAL C  1 165 ? 44.536  6.257   -15.235 1.00 22.49 ? 165 VAL C CG1 1 
ATOM   5616 C  CG2 . VAL C  1 165 ? 42.778  4.485   -15.685 1.00 21.99 ? 165 VAL C CG2 1 
ATOM   5617 N  N   . LYS C  1 166 ? 40.366  6.183   -12.536 1.00 21.78 ? 166 LYS C N   1 
ATOM   5618 C  CA  . LYS C  1 166 ? 38.916  6.111   -12.460 1.00 20.94 ? 166 LYS C CA  1 
ATOM   5619 C  C   . LYS C  1 166 ? 38.202  7.360   -12.965 1.00 22.86 ? 166 LYS C C   1 
ATOM   5620 O  O   . LYS C  1 166 ? 37.013  7.282   -13.366 1.00 21.01 ? 166 LYS C O   1 
ATOM   5621 C  CB  . LYS C  1 166 ? 38.477  5.817   -10.975 1.00 23.31 ? 166 LYS C CB  1 
ATOM   5622 C  CG  . LYS C  1 166 ? 38.873  4.426   -10.534 1.00 26.27 ? 166 LYS C CG  1 
ATOM   5623 C  CD  . LYS C  1 166 ? 38.425  4.049   -9.106  1.00 26.91 ? 166 LYS C CD  1 
ATOM   5624 C  CE  . LYS C  1 166 ? 36.921  4.114   -8.965  1.00 28.80 ? 166 LYS C CE  1 
ATOM   5625 N  NZ  . LYS C  1 166 ? 36.442  2.801   -9.527  1.00 29.49 ? 166 LYS C NZ  1 
ATOM   5626 N  N   . TYR C  1 167 ? 38.874  8.491   -12.980 1.00 18.97 ? 167 TYR C N   1 
ATOM   5627 C  CA  . TYR C  1 167 ? 38.184  9.742   -13.274 1.00 19.34 ? 167 TYR C CA  1 
ATOM   5628 C  C   . TYR C  1 167 ? 38.726  10.310  -14.594 1.00 17.22 ? 167 TYR C C   1 
ATOM   5629 O  O   . TYR C  1 167 ? 39.924  10.127  -14.860 1.00 20.89 ? 167 TYR C O   1 
ATOM   5630 C  CB  . TYR C  1 167 ? 38.329  10.779  -12.152 1.00 23.86 ? 167 TYR C CB  1 
ATOM   5631 C  CG  . TYR C  1 167 ? 37.697  10.345  -10.884 1.00 26.10 ? 167 TYR C CG  1 
ATOM   5632 C  CD1 . TYR C  1 167 ? 36.313  10.368  -10.711 1.00 26.14 ? 167 TYR C CD1 1 
ATOM   5633 C  CD2 . TYR C  1 167 ? 38.510  9.861   -9.833  1.00 24.61 ? 167 TYR C CD2 1 
ATOM   5634 C  CE1 . TYR C  1 167 ? 35.754  9.936   -9.490  1.00 30.81 ? 167 TYR C CE1 1 
ATOM   5635 C  CE2 . TYR C  1 167 ? 37.961  9.403   -8.643  1.00 26.40 ? 167 TYR C CE2 1 
ATOM   5636 C  CZ  . TYR C  1 167 ? 36.585  9.460   -8.469  1.00 27.82 ? 167 TYR C CZ  1 
ATOM   5637 O  OH  . TYR C  1 167 ? 36.087  9.020   -7.246  1.00 30.15 ? 167 TYR C OH  1 
ATOM   5638 N  N   . LYS C  1 168 ? 37.881  11.138  -15.234 1.00 19.81 ? 168 LYS C N   1 
ATOM   5639 C  CA  . LYS C  1 168 ? 38.274  11.795  -16.459 1.00 19.24 ? 168 LYS C CA  1 
ATOM   5640 C  C   . LYS C  1 168 ? 39.566  12.593  -16.269 1.00 23.97 ? 168 LYS C C   1 
ATOM   5641 O  O   . LYS C  1 168 ? 39.689  13.425  -15.304 1.00 23.21 ? 168 LYS C O   1 
ATOM   5642 C  CB  . LYS C  1 168 ? 37.136  12.730  -16.965 1.00 19.77 ? 168 LYS C CB  1 
ATOM   5643 C  CG  . LYS C  1 168 ? 37.509  13.374  -18.305 1.00 22.27 ? 168 LYS C CG  1 
ATOM   5644 C  CD  . LYS C  1 168 ? 36.386  14.305  -18.730 1.00 25.67 ? 168 LYS C CD  1 
ATOM   5645 C  CE  . LYS C  1 168 ? 36.914  15.063  -19.929 1.00 30.30 ? 168 LYS C CE  1 
ATOM   5646 N  NZ  . LYS C  1 168 ? 36.698  14.314  -21.183 1.00 42.09 ? 168 LYS C NZ  1 
ATOM   5647 N  N   . GLY C  1 169 ? 40.501  12.377  -17.201 1.00 21.83 ? 169 GLY C N   1 
ATOM   5648 C  CA  . GLY C  1 169 ? 41.727  13.139  -17.244 1.00 25.51 ? 169 GLY C CA  1 
ATOM   5649 C  C   . GLY C  1 169 ? 42.812  12.507  -16.440 1.00 22.25 ? 169 GLY C C   1 
ATOM   5650 O  O   . GLY C  1 169 ? 43.972  12.888  -16.582 1.00 26.57 ? 169 GLY C O   1 
ATOM   5651 N  N   . GLN C  1 170 ? 42.495  11.492  -15.615 1.00 20.30 ? 170 GLN C N   1 
ATOM   5652 C  CA  . GLN C  1 170 ? 43.540  10.825  -14.882 1.00 20.92 ? 170 GLN C CA  1 
ATOM   5653 C  C   . GLN C  1 170 ? 44.433  9.954   -15.724 1.00 21.97 ? 170 GLN C C   1 
ATOM   5654 O  O   . GLN C  1 170 ? 43.963  9.293   -16.728 1.00 19.84 ? 170 GLN C O   1 
ATOM   5655 C  CB  . GLN C  1 170 ? 42.961  10.013  -13.693 1.00 22.28 ? 170 GLN C CB  1 
ATOM   5656 C  CG  . GLN C  1 170 ? 42.434  10.925  -12.599 1.00 22.39 ? 170 GLN C CG  1 
ATOM   5657 C  CD  . GLN C  1 170 ? 41.998  10.135  -11.395 1.00 25.38 ? 170 GLN C CD  1 
ATOM   5658 O  OE1 . GLN C  1 170 ? 41.475  9.006   -11.493 1.00 21.16 ? 170 GLN C OE1 1 
ATOM   5659 N  NE2 . GLN C  1 170 ? 42.195  10.731  -10.216 1.00 28.17 ? 170 GLN C NE2 1 
ATOM   5660 N  N   . GLU C  1 171 ? 45.698  9.861   -15.353 1.00 23.59 ? 171 GLU C N   1 
ATOM   5661 C  CA  . GLU C  1 171 ? 46.695  9.051   -16.085 1.00 23.03 ? 171 GLU C CA  1 
ATOM   5662 C  C   . GLU C  1 171 ? 47.472  8.137   -15.180 1.00 24.26 ? 171 GLU C C   1 
ATOM   5663 O  O   . GLU C  1 171 ? 47.714  8.513   -13.995 1.00 23.72 ? 171 GLU C O   1 
ATOM   5664 C  CB  . GLU C  1 171 ? 47.678  9.968   -16.841 1.00 25.43 ? 171 GLU C CB  1 
ATOM   5665 C  CG  . GLU C  1 171 ? 47.003  10.844  -17.909 1.00 28.30 ? 171 GLU C CG  1 
ATOM   5666 C  CD  . GLU C  1 171 ? 47.891  11.971  -18.447 1.00 36.48 ? 171 GLU C CD  1 
ATOM   5667 O  OE1 . GLU C  1 171 ? 48.997  12.100  -17.921 1.00 33.20 ? 171 GLU C OE1 1 
ATOM   5668 O  OE2 . GLU C  1 171 ? 47.464  12.712  -19.395 1.00 42.65 ? 171 GLU C OE2 1 
ATOM   5669 N  N   . ALA C  1 172 ? 47.987  7.063   -15.750 1.00 20.42 ? 172 ALA C N   1 
ATOM   5670 C  CA  . ALA C  1 172 ? 48.845  6.119   -15.032 1.00 24.36 ? 172 ALA C CA  1 
ATOM   5671 C  C   . ALA C  1 172 ? 49.679  5.432   -16.039 1.00 29.72 ? 172 ALA C C   1 
ATOM   5672 O  O   . ALA C  1 172 ? 49.527  5.651   -17.219 1.00 26.79 ? 172 ALA C O   1 
ATOM   5673 C  CB  . ALA C  1 172 ? 48.090  5.126   -14.145 1.00 29.38 ? 172 ALA C CB  1 
ATOM   5674 N  N   . PHE C  1 173 ? 50.653  4.659   -15.596 1.00 29.10 ? 173 PHE C N   1 
ATOM   5675 C  CA  . PHE C  1 173 ? 51.600  4.006   -16.515 1.00 30.67 ? 173 PHE C CA  1 
ATOM   5676 C  C   . PHE C  1 173 ? 51.403  2.519   -16.357 1.00 31.00 ? 173 PHE C C   1 
ATOM   5677 O  O   . PHE C  1 173 ? 51.045  2.060   -15.278 1.00 33.18 ? 173 PHE C O   1 
ATOM   5678 C  CB  . PHE C  1 173 ? 53.065  4.371   -16.235 1.00 31.22 ? 173 PHE C CB  1 
ATOM   5679 C  CG  . PHE C  1 173 ? 53.510  5.719   -16.793 1.00 29.47 ? 173 PHE C CG  1 
ATOM   5680 C  CD1 . PHE C  1 173 ? 53.712  6.810   -15.939 1.00 30.05 ? 173 PHE C CD1 1 
ATOM   5681 C  CD2 . PHE C  1 173 ? 53.712  5.904   -18.173 1.00 29.46 ? 173 PHE C CD2 1 
ATOM   5682 C  CE1 . PHE C  1 173 ? 54.132  8.039   -16.448 1.00 34.64 ? 173 PHE C CE1 1 
ATOM   5683 C  CE2 . PHE C  1 173 ? 54.127  7.141   -18.688 1.00 32.57 ? 173 PHE C CE2 1 
ATOM   5684 C  CZ  . PHE C  1 173 ? 54.326  8.220   -17.817 1.00 33.65 ? 173 PHE C CZ  1 
ATOM   5685 N  N   . VAL C  1 174 ? 51.467  1.830   -17.488 1.00 33.84 ? 174 VAL C N   1 
ATOM   5686 C  CA  . VAL C  1 174 ? 51.357  0.369   -17.555 1.00 33.38 ? 174 VAL C CA  1 
ATOM   5687 C  C   . VAL C  1 174 ? 52.685  -0.149  -18.079 1.00 29.17 ? 174 VAL C C   1 
ATOM   5688 O  O   . VAL C  1 174 ? 53.225  0.390   -19.035 1.00 29.05 ? 174 VAL C O   1 
ATOM   5689 C  CB  . VAL C  1 174 ? 50.309  -0.045  -18.604 1.00 31.14 ? 174 VAL C CB  1 
ATOM   5690 C  CG1 . VAL C  1 174 ? 50.464  -1.525  -19.009 1.00 28.42 ? 174 VAL C CG1 1 
ATOM   5691 C  CG2 . VAL C  1 174 ? 48.922  0.281   -18.076 1.00 38.29 ? 174 VAL C CG2 1 
ATOM   5692 N  N   . PRO C  1 175 ? 53.258  -1.209  -17.424 1.00 31.20 ? 175 PRO C N   1 
ATOM   5693 C  CA  . PRO C  1 175 ? 54.496  -1.793  -17.949 1.00 31.26 ? 175 PRO C CA  1 
ATOM   5694 C  C   . PRO C  1 175 ? 54.302  -2.404  -19.336 1.00 31.27 ? 175 PRO C C   1 
ATOM   5695 O  O   . PRO C  1 175 ? 53.227  -2.924  -19.574 1.00 29.90 ? 175 PRO C O   1 
ATOM   5696 C  CB  . PRO C  1 175 ? 54.826  -2.927  -16.939 1.00 31.53 ? 175 PRO C CB  1 
ATOM   5697 C  CG  . PRO C  1 175 ? 53.902  -2.776  -15.774 1.00 32.42 ? 175 PRO C CG  1 
ATOM   5698 C  CD  . PRO C  1 175 ? 52.773  -1.857  -16.187 1.00 30.35 ? 175 PRO C CD  1 
ATOM   5699 N  N   . GLY C  1 176 ? 55.320  -2.328  -20.204 1.00 31.42 ? 176 GLY C N   1 
ATOM   5700 C  CA  . GLY C  1 176 ? 55.298  -3.050  -21.470 1.00 28.88 ? 176 GLY C CA  1 
ATOM   5701 C  C   . GLY C  1 176 ? 54.834  -4.477  -21.320 1.00 33.83 ? 176 GLY C C   1 
ATOM   5702 O  O   . GLY C  1 176 ? 54.996  -5.119  -20.278 1.00 30.88 ? 176 GLY C O   1 
ATOM   5703 N  N   . PHE C  1 177 ? 54.192  -4.951  -22.381 1.00 29.86 ? 177 PHE C N   1 
ATOM   5704 C  CA  . PHE C  1 177 ? 53.895  -6.382  -22.563 1.00 28.51 ? 177 PHE C CA  1 
ATOM   5705 C  C   . PHE C  1 177 ? 53.712  -6.587  -24.070 1.00 29.10 ? 177 PHE C C   1 
ATOM   5706 O  O   . PHE C  1 177 ? 53.820  -5.625  -24.881 1.00 26.99 ? 177 PHE C O   1 
ATOM   5707 C  CB  . PHE C  1 177 ? 52.713  -6.830  -21.711 1.00 28.11 ? 177 PHE C CB  1 
ATOM   5708 C  CG  . PHE C  1 177 ? 51.363  -6.335  -22.191 1.00 30.32 ? 177 PHE C CG  1 
ATOM   5709 C  CD1 . PHE C  1 177 ? 50.900  -5.038  -21.868 1.00 30.43 ? 177 PHE C CD1 1 
ATOM   5710 C  CD2 . PHE C  1 177 ? 50.521  -7.194  -22.883 1.00 28.61 ? 177 PHE C CD2 1 
ATOM   5711 C  CE1 . PHE C  1 177 ? 49.667  -4.603  -22.312 1.00 37.40 ? 177 PHE C CE1 1 
ATOM   5712 C  CE2 . PHE C  1 177 ? 49.285  -6.752  -23.332 1.00 30.58 ? 177 PHE C CE2 1 
ATOM   5713 C  CZ  . PHE C  1 177 ? 48.864  -5.470  -23.035 1.00 31.67 ? 177 PHE C CZ  1 
ATOM   5714 N  N   . ASN C  1 178 ? 53.536  -7.832  -24.470 1.00 25.28 ? 178 ASN C N   1 
ATOM   5715 C  CA  . ASN C  1 178 ? 53.409  -8.167  -25.882 1.00 24.73 ? 178 ASN C CA  1 
ATOM   5716 C  C   . ASN C  1 178 ? 51.929  -7.973  -26.339 1.00 25.12 ? 178 ASN C C   1 
ATOM   5717 O  O   . ASN C  1 178 ? 51.022  -8.743  -25.990 1.00 24.80 ? 178 ASN C O   1 
ATOM   5718 C  CB  . ASN C  1 178 ? 53.748  -9.622  -26.055 1.00 23.91 ? 178 ASN C CB  1 
ATOM   5719 C  CG  . ASN C  1 178 ? 53.735  -10.035 -27.507 1.00 29.61 ? 178 ASN C CG  1 
ATOM   5720 O  OD1 . ASN C  1 178 ? 53.577  -9.206  -28.419 1.00 26.20 ? 178 ASN C OD1 1 
ATOM   5721 N  ND2 . ASN C  1 178 ? 53.883  -11.325 -27.746 1.00 27.42 ? 178 ASN C ND2 1 
ATOM   5722 N  N   . ILE C  1 179 ? 51.747  -6.901  -27.115 1.00 22.67 ? 179 ILE C N   1 
ATOM   5723 C  CA  . ILE C  1 179 ? 50.392  -6.495  -27.476 1.00 20.87 ? 179 ILE C CA  1 
ATOM   5724 C  C   . ILE C  1 179 ? 49.795  -7.563  -28.353 1.00 23.60 ? 179 ILE C C   1 
ATOM   5725 O  O   . ILE C  1 179 ? 48.559  -7.677  -28.435 1.00 20.22 ? 179 ILE C O   1 
ATOM   5726 C  CB  . ILE C  1 179 ? 50.472  -5.132  -28.148 1.00 20.06 ? 179 ILE C CB  1 
ATOM   5727 C  CG1 . ILE C  1 179 ? 51.069  -4.043  -27.226 1.00 22.45 ? 179 ILE C CG1 1 
ATOM   5728 C  CG2 . ILE C  1 179 ? 49.079  -4.732  -28.705 1.00 21.55 ? 179 ILE C CG2 1 
ATOM   5729 C  CD1 . ILE C  1 179 ? 50.344  -3.741  -25.914 1.00 21.72 ? 179 ILE C CD1 1 
ATOM   5730 N  N   . GLU C  1 180 ? 50.625  -8.361  -28.984 1.00 24.54 ? 180 GLU C N   1 
ATOM   5731 C  CA  . GLU C  1 180 ? 50.110  -9.393  -29.888 1.00 23.81 ? 180 GLU C CA  1 
ATOM   5732 C  C   . GLU C  1 180 ? 49.263  -10.443 -29.105 1.00 27.56 ? 180 GLU C C   1 
ATOM   5733 O  O   . GLU C  1 180 ? 48.409  -11.142 -29.674 1.00 22.97 ? 180 GLU C O   1 
ATOM   5734 C  CB  . GLU C  1 180 ? 51.196  -10.031 -30.723 1.00 25.63 ? 180 GLU C CB  1 
ATOM   5735 C  CG  . GLU C  1 180 ? 50.655  -10.956 -31.773 1.00 30.40 ? 180 GLU C CG  1 
ATOM   5736 C  CD  . GLU C  1 180 ? 51.694  -11.340 -32.806 1.00 32.90 ? 180 GLU C CD  1 
ATOM   5737 O  OE1 . GLU C  1 180 ? 52.898  -11.009 -32.632 1.00 34.06 ? 180 GLU C OE1 1 
ATOM   5738 O  OE2 . GLU C  1 180 ? 51.267  -12.022 -33.757 1.00 31.28 ? 180 GLU C OE2 1 
ATOM   5739 N  N   . GLU C  1 181 ? 49.492  -10.536 -27.795 1.00 21.78 ? 181 GLU C N   1 
ATOM   5740 C  CA  . GLU C  1 181 ? 48.709  -11.457 -26.956 1.00 25.06 ? 181 GLU C CA  1 
ATOM   5741 C  C   . GLU C  1 181 ? 47.205  -11.031 -26.864 1.00 24.80 ? 181 GLU C C   1 
ATOM   5742 O  O   . GLU C  1 181 ? 46.406  -11.743 -26.294 1.00 22.12 ? 181 GLU C O   1 
ATOM   5743 C  CB  . GLU C  1 181 ? 49.279  -11.510 -25.513 1.00 29.57 ? 181 GLU C CB  1 
ATOM   5744 C  CG  . GLU C  1 181 ? 50.657  -12.198 -25.307 1.00 31.92 ? 181 GLU C CG  1 
ATOM   5745 C  CD  . GLU C  1 181 ? 51.256  -11.863 -23.920 1.00 34.95 ? 181 GLU C CD  1 
ATOM   5746 O  OE1 . GLU C  1 181 ? 50.519  -11.381 -23.015 1.00 32.06 ? 181 GLU C OE1 1 
ATOM   5747 O  OE2 . GLU C  1 181 ? 52.506  -12.010 -23.682 1.00 35.00 ? 181 GLU C OE2 1 
ATOM   5748 N  N   . LEU C  1 182 ? 46.884  -9.823  -27.329 1.00 19.29 ? 182 LEU C N   1 
ATOM   5749 C  CA  . LEU C  1 182 ? 45.507  -9.290  -27.226 1.00 19.92 ? 182 LEU C CA  1 
ATOM   5750 C  C   . LEU C  1 182 ? 44.708  -9.750  -28.436 1.00 20.49 ? 182 LEU C C   1 
ATOM   5751 O  O   . LEU C  1 182 ? 43.463  -9.640  -28.418 1.00 20.53 ? 182 LEU C O   1 
ATOM   5752 C  CB  . LEU C  1 182 ? 45.475  -7.764  -27.072 1.00 20.16 ? 182 LEU C CB  1 
ATOM   5753 C  CG  . LEU C  1 182 ? 46.154  -7.134  -25.854 1.00 18.89 ? 182 LEU C CG  1 
ATOM   5754 C  CD1 . LEU C  1 182 ? 46.145  -5.608  -25.923 1.00 22.08 ? 182 LEU C CD1 1 
ATOM   5755 C  CD2 . LEU C  1 182 ? 45.619  -7.630  -24.519 1.00 19.76 ? 182 LEU C CD2 1 
ATOM   5756 N  N   . LEU C  1 183 ? 45.407  -10.249 -29.460 1.00 18.52 ? 183 LEU C N   1 
ATOM   5757 C  CA  . LEU C  1 183 ? 44.792  -10.676 -30.707 1.00 20.66 ? 183 LEU C CA  1 
ATOM   5758 C  C   . LEU C  1 183 ? 44.233  -12.073 -30.580 1.00 23.76 ? 183 LEU C C   1 
ATOM   5759 O  O   . LEU C  1 183 ? 44.731  -12.900 -29.770 1.00 23.93 ? 183 LEU C O   1 
ATOM   5760 C  CB  . LEU C  1 183 ? 45.808  -10.588 -31.887 1.00 22.25 ? 183 LEU C CB  1 
ATOM   5761 C  CG  . LEU C  1 183 ? 46.412  -9.220  -31.996 1.00 21.74 ? 183 LEU C CG  1 
ATOM   5762 C  CD1 . LEU C  1 183 ? 47.309  -9.116  -33.206 1.00 25.27 ? 183 LEU C CD1 1 
ATOM   5763 C  CD2 . LEU C  1 183 ? 45.318  -8.198  -32.087 1.00 23.42 ? 183 LEU C CD2 1 
ATOM   5764 N  N   . PRO C  1 184 ? 43.194  -12.389 -31.346 1.00 20.16 ? 184 PRO C N   1 
ATOM   5765 C  CA  . PRO C  1 184 ? 42.572  -13.695 -31.299 1.00 21.85 ? 184 PRO C CA  1 
ATOM   5766 C  C   . PRO C  1 184 ? 43.355  -14.788 -32.078 1.00 23.30 ? 184 PRO C C   1 
ATOM   5767 O  O   . PRO C  1 184 ? 44.387  -14.508 -32.745 1.00 22.67 ? 184 PRO C O   1 
ATOM   5768 C  CB  . PRO C  1 184 ? 41.190  -13.416 -31.901 1.00 22.71 ? 184 PRO C CB  1 
ATOM   5769 C  CG  . PRO C  1 184 ? 41.532  -12.454 -32.973 1.00 20.42 ? 184 PRO C CG  1 
ATOM   5770 C  CD  . PRO C  1 184 ? 42.467  -11.504 -32.313 1.00 18.59 ? 184 PRO C CD  1 
ATOM   5771 N  N   . GLU C  1 185 ? 42.840  -16.004 -31.978 1.00 27.34 ? 185 GLU C N   1 
ATOM   5772 C  CA  . GLU C  1 185 ? 43.291  -17.109 -32.806 1.00 31.30 ? 185 GLU C CA  1 
ATOM   5773 C  C   . GLU C  1 185 ? 43.052  -16.787 -34.299 1.00 30.52 ? 185 GLU C C   1 
ATOM   5774 O  O   . GLU C  1 185 ? 42.041  -16.104 -34.707 1.00 27.44 ? 185 GLU C O   1 
ATOM   5775 C  CB  . GLU C  1 185 ? 42.565  -18.426 -32.462 1.00 35.56 ? 185 GLU C CB  1 
ATOM   5776 C  CG  . GLU C  1 185 ? 42.597  -18.847 -31.002 1.00 44.17 ? 185 GLU C CG  1 
ATOM   5777 C  CD  . GLU C  1 185 ? 43.916  -19.442 -30.579 1.00 53.10 ? 185 GLU C CD  1 
ATOM   5778 O  OE1 . GLU C  1 185 ? 44.952  -18.745 -30.672 1.00 55.94 ? 185 GLU C OE1 1 
ATOM   5779 O  OE2 . GLU C  1 185 ? 43.907  -20.611 -30.127 1.00 58.92 ? 185 GLU C OE2 1 
ATOM   5780 N  N   . ARG C  1 186 ? 44.019  -17.212 -35.106 1.00 26.06 ? 186 ARG C N   1 
ATOM   5781 C  CA  . ARG C  1 186 ? 43.881  -17.215 -36.567 1.00 26.42 ? 186 ARG C CA  1 
ATOM   5782 C  C   . ARG C  1 186 ? 43.610  -15.816 -37.130 1.00 23.07 ? 186 ARG C C   1 
ATOM   5783 O  O   . ARG C  1 186 ? 42.597  -15.574 -37.879 1.00 26.10 ? 186 ARG C O   1 
ATOM   5784 C  CB  . ARG C  1 186 ? 42.762  -18.134 -36.952 1.00 25.13 ? 186 ARG C CB  1 
ATOM   5785 C  CG  . ARG C  1 186 ? 43.181  -19.579 -36.806 1.00 30.64 ? 186 ARG C CG  1 
ATOM   5786 C  CD  . ARG C  1 186 ? 42.057  -20.510 -37.218 1.00 29.63 ? 186 ARG C CD  1 
ATOM   5787 N  NE  . ARG C  1 186 ? 40.964  -20.459 -36.234 1.00 32.13 ? 186 ARG C NE  1 
ATOM   5788 C  CZ  . ARG C  1 186 ? 41.039  -20.856 -34.947 1.00 34.44 ? 186 ARG C CZ  1 
ATOM   5789 N  NH1 . ARG C  1 186 ? 42.172  -21.339 -34.436 1.00 36.08 ? 186 ARG C NH1 1 
ATOM   5790 N  NH2 . ARG C  1 186 ? 39.962  -20.754 -34.156 1.00 40.61 ? 186 ARG C NH2 1 
ATOM   5791 N  N   . THR C  1 187 ? 44.528  -14.933 -36.775 1.00 23.22 ? 187 THR C N   1 
ATOM   5792 C  CA  . THR C  1 187 ? 44.493  -13.561 -37.262 1.00 20.89 ? 187 THR C CA  1 
ATOM   5793 C  C   . THR C  1 187 ? 44.392  -13.519 -38.795 1.00 22.08 ? 187 THR C C   1 
ATOM   5794 O  O   . THR C  1 187 ? 44.060  -12.486 -39.330 1.00 19.48 ? 187 THR C O   1 
ATOM   5795 C  CB  . THR C  1 187 ? 45.574  -12.656 -36.669 1.00 21.97 ? 187 THR C CB  1 
ATOM   5796 O  OG1 . THR C  1 187 ? 46.860  -13.205 -36.890 1.00 26.90 ? 187 THR C OG1 1 
ATOM   5797 C  CG2 . THR C  1 187 ? 45.354  -12.475 -35.138 1.00 24.13 ? 187 THR C CG2 1 
ATOM   5798 N  N   . ALA C  1 188 ? 44.780  -14.574 -39.520 1.00 18.28 ? 188 ALA C N   1 
ATOM   5799 C  CA  . ALA C  1 188 ? 44.667  -14.520 -41.011 1.00 20.05 ? 188 ALA C CA  1 
ATOM   5800 C  C   . ALA C  1 188 ? 43.190  -14.424 -41.480 1.00 17.61 ? 188 ALA C C   1 
ATOM   5801 O  O   . ALA C  1 188 ? 42.950  -14.039 -42.652 1.00 18.75 ? 188 ALA C O   1 
ATOM   5802 C  CB  . ALA C  1 188 ? 45.394  -15.730 -41.627 1.00 23.13 ? 188 ALA C CB  1 
ATOM   5803 N  N   . GLU C  1 189 ? 42.224  -14.740 -40.606 1.00 19.92 ? 189 GLU C N   1 
ATOM   5804 C  CA  . GLU C  1 189 ? 40.793  -14.660 -40.919 1.00 19.66 ? 189 GLU C CA  1 
ATOM   5805 C  C   . GLU C  1 189 ? 40.240  -13.312 -40.440 1.00 17.19 ? 189 GLU C C   1 
ATOM   5806 O  O   . GLU C  1 189 ? 40.228  -13.018 -39.232 1.00 17.05 ? 189 GLU C O   1 
ATOM   5807 C  CB  . GLU C  1 189 ? 39.912  -15.779 -40.299 1.00 23.58 ? 189 GLU C CB  1 
ATOM   5808 C  CG  . GLU C  1 189 ? 40.332  -17.178 -40.771 1.00 25.41 ? 189 GLU C CG  1 
ATOM   5809 C  CD  . GLU C  1 189 ? 39.690  -18.323 -39.956 1.00 37.58 ? 189 GLU C CD  1 
ATOM   5810 O  OE1 . GLU C  1 189 ? 39.034  -18.100 -38.886 1.00 33.81 ? 189 GLU C OE1 1 
ATOM   5811 O  OE2 . GLU C  1 189 ? 39.892  -19.498 -40.351 1.00 44.69 ? 189 GLU C OE2 1 
ATOM   5812 N  N   . TYR C  1 190 ? 39.897  -12.450 -41.401 1.00 16.48 ? 190 TYR C N   1 
ATOM   5813 C  CA  . TYR C  1 190 ? 39.380  -11.137 -41.004 1.00 15.23 ? 190 TYR C CA  1 
ATOM   5814 C  C   . TYR C  1 190 ? 38.389  -10.591 -42.051 1.00 15.72 ? 190 TYR C C   1 
ATOM   5815 O  O   . TYR C  1 190 ? 38.439  -10.952 -43.161 1.00 15.11 ? 190 TYR C O   1 
ATOM   5816 C  CB  . TYR C  1 190 ? 40.543  -10.179 -40.736 1.00 14.76 ? 190 TYR C CB  1 
ATOM   5817 C  CG  . TYR C  1 190 ? 41.510  -9.995  -41.885 1.00 14.58 ? 190 TYR C CG  1 
ATOM   5818 C  CD1 . TYR C  1 190 ? 41.210  -9.082  -42.942 1.00 15.14 ? 190 TYR C CD1 1 
ATOM   5819 C  CD2 . TYR C  1 190 ? 42.752  -10.715 -41.937 1.00 17.41 ? 190 TYR C CD2 1 
ATOM   5820 C  CE1 . TYR C  1 190 ? 42.113  -8.858  -43.999 1.00 15.73 ? 190 TYR C CE1 1 
ATOM   5821 C  CE2 . TYR C  1 190 ? 43.638  -10.489 -42.999 1.00 15.52 ? 190 TYR C CE2 1 
ATOM   5822 C  CZ  . TYR C  1 190 ? 43.293  -9.640  -44.054 1.00 17.73 ? 190 TYR C CZ  1 
ATOM   5823 O  OH  . TYR C  1 190 ? 44.253  -9.397  -45.034 1.00 18.21 ? 190 TYR C OH  1 
ATOM   5824 N  N   . TYR C  1 191 ? 37.606  -9.583  -41.620 1.00 14.09 ? 191 TYR C N   1 
ATOM   5825 C  CA  . TYR C  1 191 ? 36.788  -8.701  -42.454 1.00 12.48 ? 191 TYR C CA  1 
ATOM   5826 C  C   . TYR C  1 191 ? 37.539  -7.421  -42.709 1.00 12.66 ? 191 TYR C C   1 
ATOM   5827 O  O   . TYR C  1 191 ? 38.269  -6.945  -41.773 1.00 13.13 ? 191 TYR C O   1 
ATOM   5828 C  CB  . TYR C  1 191 ? 35.566  -8.319  -41.675 1.00 13.67 ? 191 TYR C CB  1 
ATOM   5829 C  CG  . TYR C  1 191 ? 34.711  -9.441  -41.149 1.00 13.32 ? 191 TYR C CG  1 
ATOM   5830 C  CD1 . TYR C  1 191 ? 33.660  -9.986  -41.926 1.00 13.47 ? 191 TYR C CD1 1 
ATOM   5831 C  CD2 . TYR C  1 191 ? 34.893  -9.895  -39.815 1.00 13.02 ? 191 TYR C CD2 1 
ATOM   5832 C  CE1 . TYR C  1 191 ? 32.841  -10.960 -41.361 1.00 15.04 ? 191 TYR C CE1 1 
ATOM   5833 C  CE2 . TYR C  1 191 ? 34.036  -10.851 -39.219 1.00 12.85 ? 191 TYR C CE2 1 
ATOM   5834 C  CZ  . TYR C  1 191 ? 33.074  -11.408 -40.014 1.00 14.46 ? 191 TYR C CZ  1 
ATOM   5835 O  OH  . TYR C  1 191 ? 32.224  -12.396 -39.426 1.00 18.77 ? 191 TYR C OH  1 
ATOM   5836 N  N   . ARG C  1 192 ? 37.400  -6.852  -43.900 1.00 13.18 ? 192 ARG C N   1 
ATOM   5837 C  CA  . ARG C  1 192 ? 38.070  -5.617  -44.278 1.00 12.27 ? 192 ARG C CA  1 
ATOM   5838 C  C   . ARG C  1 192 ? 37.130  -4.695  -44.963 1.00 11.78 ? 192 ARG C C   1 
ATOM   5839 O  O   . ARG C  1 192 ? 36.379  -5.107  -45.903 1.00 11.98 ? 192 ARG C O   1 
ATOM   5840 C  CB  . ARG C  1 192 ? 39.145  -5.996  -45.296 1.00 12.91 ? 192 ARG C CB  1 
ATOM   5841 C  CG  . ARG C  1 192 ? 39.765  -4.844  -46.076 1.00 13.57 ? 192 ARG C CG  1 
ATOM   5842 C  CD  . ARG C  1 192 ? 40.608  -3.857  -45.213 1.00 16.13 ? 192 ARG C CD  1 
ATOM   5843 N  NE  . ARG C  1 192 ? 41.537  -4.532  -44.311 1.00 15.70 ? 192 ARG C NE  1 
ATOM   5844 C  CZ  . ARG C  1 192 ? 42.713  -5.027  -44.681 1.00 15.96 ? 192 ARG C CZ  1 
ATOM   5845 N  NH1 . ARG C  1 192 ? 43.107  -4.933  -45.943 1.00 16.71 ? 192 ARG C NH1 1 
ATOM   5846 N  NH2 . ARG C  1 192 ? 43.495  -5.619  -43.789 1.00 16.82 ? 192 ARG C NH2 1 
ATOM   5847 N  N   . TYR C  1 193 ? 37.127  -3.427  -44.558 1.00 10.56 ? 193 TYR C N   1 
ATOM   5848 C  CA  . TYR C  1 193 ? 36.309  -2.413  -45.329 1.00 11.62 ? 193 TYR C CA  1 
ATOM   5849 C  C   . TYR C  1 193 ? 36.896  -1.025  -45.024 1.00 11.03 ? 193 TYR C C   1 
ATOM   5850 O  O   . TYR C  1 193 ? 37.624  -0.859  -44.018 1.00 11.88 ? 193 TYR C O   1 
ATOM   5851 C  CB  . TYR C  1 193 ? 34.825  -2.506  -45.003 1.00 11.07 ? 193 TYR C CB  1 
ATOM   5852 C  CG  . TYR C  1 193 ? 34.457  -1.936  -43.656 1.00 10.12 ? 193 TYR C CG  1 
ATOM   5853 C  CD1 . TYR C  1 193 ? 34.653  -2.667  -42.492 1.00 10.09 ? 193 TYR C CD1 1 
ATOM   5854 C  CD2 . TYR C  1 193 ? 33.908  -0.668  -43.546 1.00 10.44 ? 193 TYR C CD2 1 
ATOM   5855 C  CE1 . TYR C  1 193 ? 34.313  -2.148  -41.253 1.00 9.68  ? 193 TYR C CE1 1 
ATOM   5856 C  CE2 . TYR C  1 193 ? 33.568  -0.141  -42.313 1.00 10.78 ? 193 TYR C CE2 1 
ATOM   5857 C  CZ  . TYR C  1 193 ? 33.772  -0.884  -41.170 1.00 9.28  ? 193 TYR C CZ  1 
ATOM   5858 O  OH  . TYR C  1 193 ? 33.428  -0.359  -39.945 1.00 9.49  ? 193 TYR C OH  1 
ATOM   5859 N  N   . ARG C  1 194 ? 36.613  -0.054  -45.899 1.00 12.57 ? 194 ARG C N   1 
ATOM   5860 C  CA  . ARG C  1 194 ? 36.998  1.312   -45.680 1.00 12.11 ? 194 ARG C CA  1 
ATOM   5861 C  C   . ARG C  1 194 ? 35.894  1.989   -44.885 1.00 12.63 ? 194 ARG C C   1 
ATOM   5862 O  O   . ARG C  1 194 ? 34.703  1.964   -45.252 1.00 13.21 ? 194 ARG C O   1 
ATOM   5863 C  CB  . ARG C  1 194 ? 37.124  2.050   -47.032 1.00 16.09 ? 194 ARG C CB  1 
ATOM   5864 C  CG  . ARG C  1 194 ? 38.280  1.463   -47.828 1.00 18.54 ? 194 ARG C CG  1 
ATOM   5865 N  N   . GLY C  1 195 ? 36.258  2.634   -43.777 1.00 10.40 ? 195 GLY C N   1 
ATOM   5866 C  CA  . GLY C  1 195 ? 35.264  3.337   -42.977 1.00 10.93 ? 195 GLY C CA  1 
ATOM   5867 C  C   . GLY C  1 195 ? 35.856  4.518   -42.251 1.00 11.38 ? 195 GLY C C   1 
ATOM   5868 O  O   . GLY C  1 195 ? 36.709  5.264   -42.814 1.00 11.23 ? 195 GLY C O   1 
ATOM   5869 N  N   . SER C  1 196 ? 35.426  4.717   -40.992 1.00 10.42 ? 196 SER C N   1 
ATOM   5870 C  CA  . SER C  1 196 ? 35.681  6.007   -40.331 1.00 10.24 ? 196 SER C CA  1 
ATOM   5871 C  C   . SER C  1 196 ? 36.091  5.733   -38.916 1.00 10.47 ? 196 SER C C   1 
ATOM   5872 O  O   . SER C  1 196 ? 35.883  4.605   -38.381 1.00 10.55 ? 196 SER C O   1 
ATOM   5873 C  CB  . SER C  1 196 ? 34.407  6.884   -40.334 1.00 11.24 ? 196 SER C CB  1 
ATOM   5874 O  OG  . SER C  1 196 ? 33.477  6.475   -39.351 1.00 10.41 ? 196 SER C OG  1 
ATOM   5875 N  N   . LEU C  1 197 ? 36.620  6.765   -38.282 1.00 10.61 ? 197 LEU C N   1 
ATOM   5876 C  CA  . LEU C  1 197 ? 36.666  6.782   -36.789 1.00 11.70 ? 197 LEU C CA  1 
ATOM   5877 C  C   . LEU C  1 197 ? 35.233  6.584   -36.261 1.00 10.10 ? 197 LEU C C   1 
ATOM   5878 O  O   . LEU C  1 197 ? 34.284  7.164   -36.829 1.00 10.95 ? 197 LEU C O   1 
ATOM   5879 C  CB  . LEU C  1 197 ? 37.259  8.102   -36.265 1.00 12.35 ? 197 LEU C CB  1 
ATOM   5880 C  CG  . LEU C  1 197 ? 38.665  8.398   -36.698 1.00 14.39 ? 197 LEU C CG  1 
ATOM   5881 C  CD1 . LEU C  1 197 ? 39.013  9.756   -36.142 1.00 16.18 ? 197 LEU C CD1 1 
ATOM   5882 C  CD2 . LEU C  1 197 ? 39.560  7.334   -36.095 1.00 15.20 ? 197 LEU C CD2 1 
ATOM   5883 N  N   . THR C  1 198 ? 35.067  5.880   -35.148 1.00 10.38 ? 198 THR C N   1 
ATOM   5884 C  CA  . THR C  1 198 ? 33.740  5.684   -34.589 1.00 10.46 ? 198 THR C CA  1 
ATOM   5885 C  C   . THR C  1 198 ? 33.392  6.675   -33.487 1.00 12.00 ? 198 THR C C   1 
ATOM   5886 O  O   . THR C  1 198 ? 32.331  6.628   -32.863 1.00 11.11 ? 198 THR C O   1 
ATOM   5887 C  CB  . THR C  1 198 ? 33.513  4.289   -34.046 1.00 11.00 ? 198 THR C CB  1 
ATOM   5888 O  OG1 . THR C  1 198 ? 34.419  4.137   -32.929 1.00 11.16 ? 198 THR C OG1 1 
ATOM   5889 C  CG2 . THR C  1 198 ? 33.879  3.123   -35.034 1.00 12.12 ? 198 THR C CG2 1 
ATOM   5890 N  N   . THR C  1 199 ? 34.327  7.603   -33.256 1.00 12.42 ? 199 THR C N   1 
ATOM   5891 C  CA  . THR C  1 199 ? 34.041  8.739   -32.400 1.00 12.34 ? 199 THR C CA  1 
ATOM   5892 C  C   . THR C  1 199 ? 34.379  10.027  -33.145 1.00 12.16 ? 199 THR C C   1 
ATOM   5893 O  O   . THR C  1 199 ? 35.087  9.957   -34.135 1.00 12.66 ? 199 THR C O   1 
ATOM   5894 C  CB  . THR C  1 199 ? 34.891  8.773   -31.080 1.00 13.54 ? 199 THR C CB  1 
ATOM   5895 O  OG1 . THR C  1 199 ? 36.248  9.033   -31.424 1.00 15.91 ? 199 THR C OG1 1 
ATOM   5896 C  CG2 . THR C  1 199 ? 34.942  7.428   -30.362 1.00 14.52 ? 199 THR C CG2 1 
ATOM   5897 N  N   . PRO C  1 200 ? 33.945  11.194  -32.622 1.00 12.97 ? 200 PRO C N   1 
ATOM   5898 C  CA  . PRO C  1 200 ? 34.387  12.449  -33.260 1.00 13.27 ? 200 PRO C CA  1 
ATOM   5899 C  C   . PRO C  1 200 ? 35.918  12.433  -33.296 1.00 13.72 ? 200 PRO C C   1 
ATOM   5900 O  O   . PRO C  1 200 ? 36.578  11.927  -32.334 1.00 15.03 ? 200 PRO C O   1 
ATOM   5901 C  CB  . PRO C  1 200 ? 33.920  13.490  -32.230 1.00 13.62 ? 200 PRO C CB  1 
ATOM   5902 C  CG  . PRO C  1 200 ? 32.621  12.922  -31.695 1.00 14.13 ? 200 PRO C CG  1 
ATOM   5903 C  CD  . PRO C  1 200 ? 33.007  11.444  -31.530 1.00 13.65 ? 200 PRO C CD  1 
ATOM   5904 N  N   . PRO C  1 201 ? 36.489  12.960  -34.342 1.00 12.77 ? 201 PRO C N   1 
ATOM   5905 C  CA  . PRO C  1 201 ? 35.789  13.692  -35.434 1.00 13.77 ? 201 PRO C CA  1 
ATOM   5906 C  C   . PRO C  1 201 ? 35.237  12.870  -36.584 1.00 12.62 ? 201 PRO C C   1 
ATOM   5907 O  O   . PRO C  1 201 ? 34.815  13.419  -37.577 1.00 13.72 ? 201 PRO C O   1 
ATOM   5908 C  CB  . PRO C  1 201 ? 36.850  14.631  -36.020 1.00 14.40 ? 201 PRO C CB  1 
ATOM   5909 C  CG  . PRO C  1 201 ? 38.110  14.333  -35.249 1.00 20.75 ? 201 PRO C CG  1 
ATOM   5910 C  CD  . PRO C  1 201 ? 37.963  13.121  -34.375 1.00 14.38 ? 201 PRO C CD  1 
ATOM   5911 N  N   . CYS C  1 202 ? 35.238  11.539  -36.421 1.00 12.40 ? 202 CYS C N   1 
ATOM   5912 C  CA  . CYS C  1 202 ? 34.511  10.638  -37.399 1.00 11.04 ? 202 CYS C CA  1 
ATOM   5913 C  C   . CYS C  1 202 ? 35.120  10.686  -38.781 1.00 11.17 ? 202 CYS C C   1 
ATOM   5914 O  O   . CYS C  1 202 ? 34.425  10.368  -39.718 1.00 11.83 ? 202 CYS C O   1 
ATOM   5915 C  CB  . CYS C  1 202 ? 32.982  10.921  -37.508 1.00 11.80 ? 202 CYS C CB  1 
ATOM   5916 S  SG  . CYS C  1 202 ? 32.092  10.827  -35.953 1.00 12.33 ? 202 CYS C SG  1 
ATOM   5917 N  N   . ASN C  1 203 ? 36.394  10.995  -38.909 1.00 12.62 ? 203 ASN C N   1 
ATOM   5918 C  CA  . ASN C  1 203 ? 36.956  11.132  -40.242 1.00 13.40 ? 203 ASN C CA  1 
ATOM   5919 C  C   . ASN C  1 203 ? 36.900  9.818   -41.014 1.00 12.62 ? 203 ASN C C   1 
ATOM   5920 O  O   . ASN C  1 203 ? 37.166  8.728   -40.435 1.00 11.74 ? 203 ASN C O   1 
ATOM   5921 C  CB  . ASN C  1 203 ? 38.444  11.552  -40.145 1.00 15.70 ? 203 ASN C CB  1 
ATOM   5922 C  CG  . ASN C  1 203 ? 38.582  12.827  -39.349 1.00 16.90 ? 203 ASN C CG  1 
ATOM   5923 O  OD1 . ASN C  1 203 ? 38.654  12.779  -38.161 1.00 21.88 ? 203 ASN C OD1 1 
ATOM   5924 N  ND2 . ASN C  1 203 ? 38.341  13.937  -39.976 1.00 21.55 ? 203 ASN C ND2 1 
ATOM   5925 N  N   . PRO C  1 204 ? 36.558  9.878   -42.319 1.00 12.06 ? 204 PRO C N   1 
ATOM   5926 C  CA  . PRO C  1 204 ? 36.373  8.681   -43.136 1.00 12.42 ? 204 PRO C CA  1 
ATOM   5927 C  C   . PRO C  1 204 ? 37.692  8.227   -43.713 1.00 12.38 ? 204 PRO C C   1 
ATOM   5928 O  O   . PRO C  1 204 ? 37.809  8.006   -44.945 1.00 15.29 ? 204 PRO C O   1 
ATOM   5929 C  CB  . PRO C  1 204 ? 35.413  9.157   -44.237 1.00 14.97 ? 204 PRO C CB  1 
ATOM   5930 C  CG  . PRO C  1 204 ? 35.848  10.601  -44.416 1.00 13.76 ? 204 PRO C CG  1 
ATOM   5931 C  CD  . PRO C  1 204 ? 36.114  11.119  -43.026 1.00 14.18 ? 204 PRO C CD  1 
ATOM   5932 N  N   . THR C  1 205 ? 38.626  7.976   -42.802 1.00 12.24 ? 205 THR C N   1 
ATOM   5933 C  CA  . THR C  1 205 ? 40.040  7.756   -43.174 1.00 13.51 ? 205 THR C CA  1 
ATOM   5934 C  C   . THR C  1 205 ? 40.618  6.454   -42.677 1.00 15.47 ? 205 THR C C   1 
ATOM   5935 O  O   . THR C  1 205 ? 41.834  6.227   -42.642 1.00 14.98 ? 205 THR C O   1 
ATOM   5936 C  CB  . THR C  1 205 ? 40.898  8.912   -42.597 1.00 13.31 ? 205 THR C CB  1 
ATOM   5937 O  OG1 . THR C  1 205 ? 40.681  8.953   -41.210 1.00 15.58 ? 205 THR C OG1 1 
ATOM   5938 C  CG2 . THR C  1 205 ? 40.518  10.276  -43.317 1.00 18.51 ? 205 THR C CG2 1 
ATOM   5939 N  N   . VAL C  1 206 ? 39.693  5.569   -42.196 1.00 12.13 ? 206 VAL C N   1 
ATOM   5940 C  CA  . VAL C  1 206 ? 40.136  4.316   -41.564 1.00 11.55 ? 206 VAL C CA  1 
ATOM   5941 C  C   . VAL C  1 206 ? 40.007  3.070   -42.413 1.00 11.14 ? 206 VAL C C   1 
ATOM   5942 O  O   . VAL C  1 206 ? 38.917  2.741   -42.880 1.00 13.20 ? 206 VAL C O   1 
ATOM   5943 C  CB  . VAL C  1 206 ? 39.362  4.059   -40.260 1.00 12.43 ? 206 VAL C CB  1 
ATOM   5944 C  CG1 . VAL C  1 206 ? 39.833  2.728   -39.616 1.00 12.14 ? 206 VAL C CG1 1 
ATOM   5945 C  CG2 . VAL C  1 206 ? 39.547  5.174   -39.234 1.00 14.36 ? 206 VAL C CG2 1 
ATOM   5946 N  N   . LEU C  1 207 ? 41.084  2.308   -42.620 1.00 11.42 ? 207 LEU C N   1 
ATOM   5947 C  CA  . LEU C  1 207 ? 41.047  0.953   -43.171 1.00 12.45 ? 207 LEU C CA  1 
ATOM   5948 C  C   . LEU C  1 207 ? 40.782  0.027   -42.009 1.00 12.14 ? 207 LEU C C   1 
ATOM   5949 O  O   . LEU C  1 207 ? 41.657  -0.160  -41.158 1.00 12.45 ? 207 LEU C O   1 
ATOM   5950 C  CB  . LEU C  1 207 ? 42.420  0.648   -43.884 1.00 14.30 ? 207 LEU C CB  1 
ATOM   5951 C  CG  . LEU C  1 207 ? 42.318  -0.588  -44.786 1.00 17.53 ? 207 LEU C CG  1 
ATOM   5952 C  CD1 . LEU C  1 207 ? 41.299  -0.444  -45.968 1.00 20.51 ? 207 LEU C CD1 1 
ATOM   5953 C  CD2 . LEU C  1 207 ? 43.693  -0.989  -45.321 1.00 23.72 ? 207 LEU C CD2 1 
ATOM   5954 N  N   . TRP C  1 208 ? 39.590  -0.523  -41.930 1.00 10.88 ? 208 TRP C N   1 
ATOM   5955 C  CA  . TRP C  1 208 ? 39.217  -1.450  -40.823 1.00 10.84 ? 208 TRP C CA  1 
ATOM   5956 C  C   . TRP C  1 208 ? 39.589  -2.852  -41.116 1.00 10.99 ? 208 TRP C C   1 
ATOM   5957 O  O   . TRP C  1 208 ? 39.390  -3.402  -42.266 1.00 11.72 ? 208 TRP C O   1 
ATOM   5958 C  CB  . TRP C  1 208 ? 37.704  -1.386  -40.673 1.00 10.54 ? 208 TRP C CB  1 
ATOM   5959 C  CG  . TRP C  1 208 ? 37.323  -0.188  -39.840 1.00 10.29 ? 208 TRP C CG  1 
ATOM   5960 C  CD1 . TRP C  1 208 ? 36.814  1.030   -40.284 1.00 9.13  ? 208 TRP C CD1 1 
ATOM   5961 C  CD2 . TRP C  1 208 ? 37.420  -0.070  -38.404 1.00 9.58  ? 208 TRP C CD2 1 
ATOM   5962 N  NE1 . TRP C  1 208 ? 36.648  1.889   -39.249 1.00 11.37 ? 208 TRP C NE1 1 
ATOM   5963 C  CE2 . TRP C  1 208 ? 36.994  1.258   -38.085 1.00 10.65 ? 208 TRP C CE2 1 
ATOM   5964 C  CE3 . TRP C  1 208 ? 37.811  -0.921  -37.368 1.00 11.69 ? 208 TRP C CE3 1 
ATOM   5965 C  CZ2 . TRP C  1 208 ? 36.986  1.765   -36.810 1.00 11.02 ? 208 TRP C CZ2 1 
ATOM   5966 C  CZ3 . TRP C  1 208 ? 37.776  -0.430  -36.044 1.00 11.22 ? 208 TRP C CZ3 1 
ATOM   5967 C  CH2 . TRP C  1 208 ? 37.378  0.905   -35.772 1.00 12.14 ? 208 TRP C CH2 1 
ATOM   5968 N  N   . THR C  1 209 ? 40.120  -3.529  -40.104 1.00 11.51 ? 209 THR C N   1 
ATOM   5969 C  CA  . THR C  1 209 ? 40.361  -4.933  -40.099 1.00 12.02 ? 209 THR C CA  1 
ATOM   5970 C  C   . THR C  1 209 ? 39.707  -5.480  -38.862 1.00 12.71 ? 209 THR C C   1 
ATOM   5971 O  O   . THR C  1 209 ? 40.169  -5.133  -37.736 1.00 12.64 ? 209 THR C O   1 
ATOM   5972 C  CB  . THR C  1 209 ? 41.836  -5.275  -40.085 1.00 12.55 ? 209 THR C CB  1 
ATOM   5973 O  OG1 . THR C  1 209 ? 42.453  -4.691  -41.254 1.00 13.30 ? 209 THR C OG1 1 
ATOM   5974 C  CG2 . THR C  1 209 ? 42.037  -6.806  -40.101 1.00 12.94 ? 209 THR C CG2 1 
ATOM   5975 N  N   . VAL C  1 210 ? 38.637  -6.268  -38.999 1.00 11.61 ? 210 VAL C N   1 
ATOM   5976 C  CA  . VAL C  1 210 ? 37.960  -6.838  -37.858 1.00 11.93 ? 210 VAL C CA  1 
ATOM   5977 C  C   . VAL C  1 210 ? 38.209  -8.314  -37.856 1.00 12.82 ? 210 VAL C C   1 
ATOM   5978 O  O   . VAL C  1 210 ? 37.902  -8.986  -38.842 1.00 11.92 ? 210 VAL C O   1 
ATOM   5979 C  CB  . VAL C  1 210 ? 36.415  -6.648  -37.920 1.00 10.65 ? 210 VAL C CB  1 
ATOM   5980 C  CG1 . VAL C  1 210 ? 35.721  -7.212  -36.684 1.00 13.21 ? 210 VAL C CG1 1 
ATOM   5981 C  CG2 . VAL C  1 210 ? 36.137  -5.120  -38.151 1.00 11.23 ? 210 VAL C CG2 1 
ATOM   5982 N  N   . PHE C  1 211 ? 38.863  -8.827  -36.807 1.00 12.73 ? 211 PHE C N   1 
ATOM   5983 C  CA  . PHE C  1 211 ? 39.152  -10.262 -36.939 1.00 13.26 ? 211 PHE C CA  1 
ATOM   5984 C  C   . PHE C  1 211 ? 37.916  -11.104 -36.825 1.00 14.44 ? 211 PHE C C   1 
ATOM   5985 O  O   . PHE C  1 211 ? 36.982  -10.746 -36.081 1.00 15.90 ? 211 PHE C O   1 
ATOM   5986 C  CB  . PHE C  1 211 ? 40.236  -10.662 -35.885 1.00 13.77 ? 211 PHE C CB  1 
ATOM   5987 C  CG  . PHE C  1 211 ? 41.563  -10.007 -36.121 1.00 13.32 ? 211 PHE C CG  1 
ATOM   5988 C  CD1 . PHE C  1 211 ? 42.389  -10.414 -37.167 1.00 14.98 ? 211 PHE C CD1 1 
ATOM   5989 C  CD2 . PHE C  1 211 ? 41.984  -8.960  -35.296 1.00 15.10 ? 211 PHE C CD2 1 
ATOM   5990 C  CE1 . PHE C  1 211 ? 43.609  -9.709  -37.403 1.00 16.62 ? 211 PHE C CE1 1 
ATOM   5991 C  CE2 . PHE C  1 211 ? 43.148  -8.277  -35.599 1.00 14.17 ? 211 PHE C CE2 1 
ATOM   5992 C  CZ  . PHE C  1 211 ? 43.991  -8.685  -36.579 1.00 15.05 ? 211 PHE C CZ  1 
ATOM   5993 N  N   A ARG C  1 212 ? 37.894  -12.221 -37.541 0.50 14.94 ? 212 ARG C N   1 
ATOM   5994 N  N   B ARG C  1 212 ? 37.894  -12.224 -37.540 0.50 15.12 ? 212 ARG C N   1 
ATOM   5995 C  CA  A ARG C  1 212 ? 36.720  -13.078 -37.555 0.50 15.91 ? 212 ARG C CA  1 
ATOM   5996 C  CA  B ARG C  1 212 ? 36.721  -13.090 -37.559 0.50 16.30 ? 212 ARG C CA  1 
ATOM   5997 C  C   A ARG C  1 212 ? 36.401  -13.686 -36.182 0.50 15.83 ? 212 ARG C C   1 
ATOM   5998 C  C   B ARG C  1 212 ? 36.401  -13.718 -36.197 0.50 16.16 ? 212 ARG C C   1 
ATOM   5999 O  O   A ARG C  1 212 ? 35.246  -13.747 -35.773 0.50 17.36 ? 212 ARG C O   1 
ATOM   6000 O  O   B ARG C  1 212 ? 35.240  -13.844 -35.819 0.50 18.16 ? 212 ARG C O   1 
ATOM   6001 C  CB  A ARG C  1 212 ? 36.922  -14.193 -38.575 0.50 16.18 ? 212 ARG C CB  1 
ATOM   6002 C  CB  B ARG C  1 212 ? 36.921  -14.204 -38.585 0.50 16.80 ? 212 ARG C CB  1 
ATOM   6003 C  CG  A ARG C  1 212 ? 35.754  -15.146 -38.691 0.50 18.85 ? 212 ARG C CG  1 
ATOM   6004 C  CG  B ARG C  1 212 ? 35.709  -15.093 -38.774 0.50 19.83 ? 212 ARG C CG  1 
ATOM   6005 C  CD  A ARG C  1 212 ? 36.277  -16.438 -39.288 0.50 20.74 ? 212 ARG C CD  1 
ATOM   6006 C  CD  B ARG C  1 212 ? 36.066  -16.233 -39.711 0.50 22.26 ? 212 ARG C CD  1 
ATOM   6007 N  NE  A ARG C  1 212 ? 35.186  -17.390 -39.543 0.50 20.19 ? 212 ARG C NE  1 
ATOM   6008 N  NE  B ARG C  1 212 ? 34.839  -16.806 -40.266 0.50 23.10 ? 212 ARG C NE  1 
ATOM   6009 C  CZ  A ARG C  1 212 ? 34.822  -18.378 -38.731 0.50 23.95 ? 212 ARG C CZ  1 
ATOM   6010 C  CZ  B ARG C  1 212 ? 34.787  -17.865 -41.076 0.50 25.38 ? 212 ARG C CZ  1 
ATOM   6011 N  NH1 A ARG C  1 212 ? 35.431  -18.576 -37.589 0.50 25.03 ? 212 ARG C NH1 1 
ATOM   6012 N  NH1 B ARG C  1 212 ? 35.895  -18.496 -41.445 0.50 28.66 ? 212 ARG C NH1 1 
ATOM   6013 N  NH2 A ARG C  1 212 ? 33.818  -19.169 -39.050 0.50 28.03 ? 212 ARG C NH2 1 
ATOM   6014 N  NH2 B ARG C  1 212 ? 33.617  -18.251 -41.557 0.50 23.57 ? 212 ARG C NH2 1 
ATOM   6015 N  N   . ASN C  1 213 ? 37.468  -14.052 -35.466 1.00 16.65 ? 213 ASN C N   1 
ATOM   6016 C  CA  . ASN C  1 213 ? 37.345  -14.781 -34.173 1.00 19.10 ? 213 ASN C CA  1 
ATOM   6017 C  C   . ASN C  1 213 ? 37.485  -13.857 -32.987 1.00 15.91 ? 213 ASN C C   1 
ATOM   6018 O  O   . ASN C  1 213 ? 38.374  -13.058 -32.925 1.00 19.16 ? 213 ASN C O   1 
ATOM   6019 C  CB  . ASN C  1 213 ? 38.401  -15.915 -34.102 1.00 21.24 ? 213 ASN C CB  1 
ATOM   6020 C  CG  . ASN C  1 213 ? 38.306  -16.856 -35.319 1.00 21.39 ? 213 ASN C CG  1 
ATOM   6021 O  OD1 . ASN C  1 213 ? 37.229  -17.413 -35.672 1.00 27.23 ? 213 ASN C OD1 1 
ATOM   6022 N  ND2 . ASN C  1 213 ? 39.443  -17.021 -35.989 1.00 21.45 ? 213 ASN C ND2 1 
ATOM   6023 N  N   . PRO C  1 214 ? 36.595  -14.027 -32.008 1.00 18.18 ? 214 PRO C N   1 
ATOM   6024 C  CA  . PRO C  1 214 ? 36.665  -13.229 -30.821 1.00 18.27 ? 214 PRO C CA  1 
ATOM   6025 C  C   . PRO C  1 214 ? 37.671  -13.785 -29.801 1.00 17.95 ? 214 PRO C C   1 
ATOM   6026 O  O   . PRO C  1 214 ? 38.237  -14.898 -29.986 1.00 22.42 ? 214 PRO C O   1 
ATOM   6027 C  CB  . PRO C  1 214 ? 35.276  -13.360 -30.244 1.00 20.16 ? 214 PRO C CB  1 
ATOM   6028 C  CG  . PRO C  1 214 ? 34.927  -14.758 -30.619 1.00 21.74 ? 214 PRO C CG  1 
ATOM   6029 C  CD  . PRO C  1 214 ? 35.381  -14.862 -32.053 1.00 22.50 ? 214 PRO C CD  1 
ATOM   6030 N  N   . VAL C  1 215 ? 38.033  -12.918 -28.897 1.00 16.67 ? 215 VAL C N   1 
ATOM   6031 C  CA  . VAL C  1 215 ? 38.787  -13.389 -27.683 1.00 18.79 ? 215 VAL C CA  1 
ATOM   6032 C  C   . VAL C  1 215 ? 37.835  -13.433 -26.520 1.00 21.92 ? 215 VAL C C   1 
ATOM   6033 O  O   . VAL C  1 215 ? 36.704  -12.921 -26.590 1.00 19.88 ? 215 VAL C O   1 
ATOM   6034 C  CB  . VAL C  1 215 ? 39.912  -12.443 -27.292 1.00 22.10 ? 215 VAL C CB  1 
ATOM   6035 C  CG1 . VAL C  1 215 ? 40.979  -12.288 -28.367 1.00 21.34 ? 215 VAL C CG1 1 
ATOM   6036 C  CG2 . VAL C  1 215 ? 39.374  -11.101 -26.794 1.00 20.89 ? 215 VAL C CG2 1 
ATOM   6037 N  N   . GLN C  1 216 ? 38.245  -14.095 -25.426 1.00 21.52 ? 216 GLN C N   1 
ATOM   6038 C  CA  . GLN C  1 216 ? 37.456  -14.267 -24.233 1.00 22.48 ? 216 GLN C CA  1 
ATOM   6039 C  C   . GLN C  1 216 ? 38.147  -13.610 -23.080 1.00 21.88 ? 216 GLN C C   1 
ATOM   6040 O  O   . GLN C  1 216 ? 39.407  -13.613 -22.971 1.00 22.35 ? 216 GLN C O   1 
ATOM   6041 C  CB  . GLN C  1 216 ? 37.341  -15.761 -23.916 1.00 22.35 ? 216 GLN C CB  1 
ATOM   6042 C  CG  . GLN C  1 216 ? 36.688  -16.530 -25.006 1.00 26.88 ? 216 GLN C CG  1 
ATOM   6043 C  CD  . GLN C  1 216 ? 35.997  -17.755 -24.477 1.00 39.86 ? 216 GLN C CD  1 
ATOM   6044 O  OE1 . GLN C  1 216 ? 36.432  -18.379 -23.469 1.00 43.43 ? 216 GLN C OE1 1 
ATOM   6045 N  NE2 . GLN C  1 216 ? 34.879  -18.094 -25.110 1.00 42.14 ? 216 GLN C NE2 1 
ATOM   6046 N  N   . ILE C  1 217 ? 37.306  -13.026 -22.254 1.00 20.90 ? 217 ILE C N   1 
ATOM   6047 C  CA  . ILE C  1 217 ? 37.674  -12.519 -20.952 1.00 19.53 ? 217 ILE C CA  1 
ATOM   6048 C  C   . ILE C  1 217 ? 36.659  -13.058 -19.928 1.00 20.35 ? 217 ILE C C   1 
ATOM   6049 O  O   . ILE C  1 217 ? 35.540  -13.468 -20.293 1.00 23.21 ? 217 ILE C O   1 
ATOM   6050 C  CB  . ILE C  1 217 ? 37.822  -10.951 -20.865 1.00 21.19 ? 217 ILE C CB  1 
ATOM   6051 C  CG1 . ILE C  1 217 ? 36.485  -10.209 -21.147 1.00 18.30 ? 217 ILE C CG1 1 
ATOM   6052 C  CG2 . ILE C  1 217 ? 38.933  -10.495 -21.798 1.00 21.52 ? 217 ILE C CG2 1 
ATOM   6053 C  CD1 . ILE C  1 217 ? 36.581  -8.711  -20.781 1.00 23.08 ? 217 ILE C CD1 1 
ATOM   6054 N  N   . SER C  1 218 ? 37.082  -13.141 -18.658 1.00 24.46 ? 218 SER C N   1 
ATOM   6055 C  CA  . SER C  1 218 ? 36.179  -13.759 -17.696 1.00 26.82 ? 218 SER C CA  1 
ATOM   6056 C  C   . SER C  1 218 ? 35.021  -12.849 -17.429 1.00 25.48 ? 218 SER C C   1 
ATOM   6057 O  O   . SER C  1 218 ? 35.119  -11.592 -17.608 1.00 26.11 ? 218 SER C O   1 
ATOM   6058 C  CB  . SER C  1 218 ? 36.889  -14.085 -16.355 1.00 23.58 ? 218 SER C CB  1 
ATOM   6059 O  OG  . SER C  1 218 ? 37.335  -12.922 -15.696 1.00 26.71 ? 218 SER C OG  1 
ATOM   6060 N  N   . GLN C  1 219 ? 33.923  -13.456 -16.955 1.00 27.94 ? 219 GLN C N   1 
ATOM   6061 C  CA  . GLN C  1 219 ? 32.834  -12.647 -16.421 1.00 30.60 ? 219 GLN C CA  1 
ATOM   6062 C  C   . GLN C  1 219 ? 33.333  -11.584 -15.427 1.00 27.61 ? 219 GLN C C   1 
ATOM   6063 O  O   . GLN C  1 219 ? 32.840  -10.459 -15.415 1.00 26.86 ? 219 GLN C O   1 
ATOM   6064 C  CB  . GLN C  1 219 ? 31.720  -13.515 -15.770 1.00 39.16 ? 219 GLN C CB  1 
ATOM   6065 N  N   . GLU C  1 220 ? 34.290  -11.933 -14.550 1.00 29.00 ? 220 GLU C N   1 
ATOM   6066 C  CA  . GLU C  1 220 ? 34.778  -10.972 -13.595 1.00 27.54 ? 220 GLU C CA  1 
ATOM   6067 C  C   . GLU C  1 220 ? 35.544  -9.826  -14.264 1.00 21.03 ? 220 GLU C C   1 
ATOM   6068 O  O   . GLU C  1 220 ? 35.407  -8.707  -13.831 1.00 22.03 ? 220 GLU C O   1 
ATOM   6069 C  CB  . GLU C  1 220 ? 35.659  -11.627 -12.483 1.00 32.35 ? 220 GLU C CB  1 
ATOM   6070 C  CG  . GLU C  1 220 ? 35.000  -12.881 -11.831 1.00 39.13 ? 220 GLU C CG  1 
ATOM   6071 C  CD  . GLU C  1 220 ? 35.156  -14.250 -12.574 1.00 47.27 ? 220 GLU C CD  1 
ATOM   6072 O  OE1 . GLU C  1 220 ? 34.914  -14.433 -13.795 1.00 39.64 ? 220 GLU C OE1 1 
ATOM   6073 O  OE2 . GLU C  1 220 ? 35.514  -15.228 -11.889 1.00 56.04 ? 220 GLU C OE2 1 
ATOM   6074 N  N   . GLN C  1 221 ? 36.360  -10.135 -15.280 1.00 25.38 ? 221 GLN C N   1 
ATOM   6075 C  CA  . GLN C  1 221 ? 37.131  -9.105  -15.999 1.00 20.89 ? 221 GLN C CA  1 
ATOM   6076 C  C   . GLN C  1 221 ? 36.195  -8.199  -16.788 1.00 16.84 ? 221 GLN C C   1 
ATOM   6077 O  O   . GLN C  1 221 ? 36.390  -6.989  -16.722 1.00 20.52 ? 221 GLN C O   1 
ATOM   6078 C  CB  . GLN C  1 221 ? 38.087  -9.726  -16.980 1.00 20.54 ? 221 GLN C CB  1 
ATOM   6079 C  CG  . GLN C  1 221 ? 39.293  -10.387 -16.310 1.00 20.94 ? 221 GLN C CG  1 
ATOM   6080 C  CD  . GLN C  1 221 ? 40.208  -10.952 -17.361 1.00 20.39 ? 221 GLN C CD  1 
ATOM   6081 O  OE1 . GLN C  1 221 ? 39.813  -11.887 -18.064 1.00 21.35 ? 221 GLN C OE1 1 
ATOM   6082 N  NE2 . GLN C  1 221 ? 41.403  -10.365 -17.527 1.00 21.90 ? 221 GLN C NE2 1 
ATOM   6083 N  N   . LEU C  1 222 ? 35.148  -8.800  -17.399 1.00 20.66 ? 222 LEU C N   1 
ATOM   6084 C  CA  . LEU C  1 222 ? 34.137  -7.949  -18.102 1.00 21.51 ? 222 LEU C CA  1 
ATOM   6085 C  C   . LEU C  1 222 ? 33.434  -6.973  -17.169 1.00 17.35 ? 222 LEU C C   1 
ATOM   6086 O  O   . LEU C  1 222 ? 33.317  -5.752  -17.382 1.00 18.16 ? 222 LEU C O   1 
ATOM   6087 C  CB  . LEU C  1 222 ? 33.133  -8.820  -18.821 1.00 21.99 ? 222 LEU C CB  1 
ATOM   6088 C  CG  . LEU C  1 222 ? 32.056  -8.047  -19.600 1.00 20.48 ? 222 LEU C CG  1 
ATOM   6089 C  CD1 . LEU C  1 222 ? 32.668  -7.073  -20.633 1.00 19.57 ? 222 LEU C CD1 1 
ATOM   6090 C  CD2 . LEU C  1 222 ? 31.255  -9.133  -20.303 1.00 21.11 ? 222 LEU C CD2 1 
ATOM   6091 N  N   . LEU C  1 223 ? 32.970  -7.491  -15.988 1.00 21.04 ? 223 LEU C N   1 
ATOM   6092 C  CA  . LEU C  1 223 ? 32.349  -6.676  -14.952 1.00 21.03 ? 223 LEU C CA  1 
ATOM   6093 C  C   . LEU C  1 223 ? 33.234  -5.586  -14.406 1.00 17.29 ? 223 LEU C C   1 
ATOM   6094 O  O   . LEU C  1 223 ? 32.833  -4.435  -14.192 1.00 20.50 ? 223 LEU C O   1 
ATOM   6095 C  CB  . LEU C  1 223 ? 31.979  -7.601  -13.786 1.00 24.82 ? 223 LEU C CB  1 
ATOM   6096 C  CG  . LEU C  1 223 ? 30.888  -7.146  -12.839 1.00 31.23 ? 223 LEU C CG  1 
ATOM   6097 C  CD1 . LEU C  1 223 ? 29.555  -6.855  -13.532 1.00 29.97 ? 223 LEU C CD1 1 
ATOM   6098 C  CD2 . LEU C  1 223 ? 30.722  -8.234  -11.767 1.00 29.03 ? 223 LEU C CD2 1 
ATOM   6099 N  N   . ALA C  1 224 ? 34.486  -5.957  -14.218 1.00 21.22 ? 224 ALA C N   1 
ATOM   6100 C  CA  . ALA C  1 224 ? 35.536  -5.005  -13.746 1.00 23.44 ? 224 ALA C CA  1 
ATOM   6101 C  C   . ALA C  1 224 ? 35.632  -3.813  -14.717 1.00 19.81 ? 224 ALA C C   1 
ATOM   6102 O  O   . ALA C  1 224 ? 35.536  -2.657  -14.343 1.00 23.87 ? 224 ALA C O   1 
ATOM   6103 C  CB  . ALA C  1 224 ? 36.885  -5.770  -13.584 1.00 22.75 ? 224 ALA C CB  1 
ATOM   6104 N  N   . LEU C  1 225 ? 35.697  -4.130  -16.009 1.00 20.75 ? 225 LEU C N   1 
ATOM   6105 C  CA  . LEU C  1 225 ? 35.800  -3.112  -17.060 1.00 19.10 ? 225 LEU C CA  1 
ATOM   6106 C  C   . LEU C  1 225 ? 34.572  -2.236  -17.101 1.00 17.37 ? 225 LEU C C   1 
ATOM   6107 O  O   . LEU C  1 225 ? 34.716  -1.011  -17.202 1.00 20.86 ? 225 LEU C O   1 
ATOM   6108 C  CB  . LEU C  1 225 ? 36.007  -3.857  -18.437 1.00 19.31 ? 225 LEU C CB  1 
ATOM   6109 C  CG  . LEU C  1 225 ? 36.082  -2.905  -19.683 1.00 19.88 ? 225 LEU C CG  1 
ATOM   6110 C  CD1 . LEU C  1 225 ? 37.222  -1.951  -19.566 1.00 20.35 ? 225 LEU C CD1 1 
ATOM   6111 C  CD2 . LEU C  1 225 ? 36.136  -3.691  -20.982 1.00 19.95 ? 225 LEU C CD2 1 
ATOM   6112 N  N   . GLU C  1 226 ? 33.374  -2.826  -17.044 1.00 18.46 ? 226 GLU C N   1 
ATOM   6113 C  CA  . GLU C  1 226 ? 32.127  -2.055  -17.097 1.00 19.90 ? 226 GLU C CA  1 
ATOM   6114 C  C   . GLU C  1 226 ? 31.866  -1.170  -15.878 1.00 19.44 ? 226 GLU C C   1 
ATOM   6115 O  O   . GLU C  1 226 ? 31.043  -0.258  -15.885 1.00 21.46 ? 226 GLU C O   1 
ATOM   6116 C  CB  . GLU C  1 226 ? 30.960  -2.998  -17.235 1.00 20.25 ? 226 GLU C CB  1 
ATOM   6117 C  CG  . GLU C  1 226 ? 30.964  -3.824  -18.516 1.00 19.21 ? 226 GLU C CG  1 
ATOM   6118 C  CD  . GLU C  1 226 ? 30.063  -5.030  -18.453 1.00 19.20 ? 226 GLU C CD  1 
ATOM   6119 O  OE1 . GLU C  1 226 ? 29.713  -5.527  -17.302 1.00 20.27 ? 226 GLU C OE1 1 
ATOM   6120 O  OE2 . GLU C  1 226 ? 29.770  -5.679  -19.472 1.00 20.33 ? 226 GLU C OE2 1 
ATOM   6121 N  N   . THR C  1 227 ? 32.571  -1.488  -14.788 1.00 23.39 ? 227 THR C N   1 
ATOM   6122 C  CA  . THR C  1 227 ? 32.306  -0.792  -13.496 1.00 23.32 ? 227 THR C CA  1 
ATOM   6123 C  C   . THR C  1 227 ? 33.456  -0.005  -12.894 1.00 24.09 ? 227 THR C C   1 
ATOM   6124 O  O   . THR C  1 227 ? 33.262  0.614   -11.857 1.00 24.38 ? 227 THR C O   1 
ATOM   6125 C  CB  . THR C  1 227 ? 31.773  -1.785  -12.423 1.00 23.70 ? 227 THR C CB  1 
ATOM   6126 O  OG1 . THR C  1 227 ? 32.743  -2.832  -12.238 1.00 23.37 ? 227 THR C OG1 1 
ATOM   6127 C  CG2 . THR C  1 227 ? 30.340  -2.327  -12.878 1.00 26.47 ? 227 THR C CG2 1 
ATOM   6128 N  N   . ALA C  1 228 ? 34.595  0.005   -13.553 1.00 22.50 ? 228 ALA C N   1 
ATOM   6129 C  CA  . ALA C  1 228 ? 35.790  0.674   -13.019 1.00 21.47 ? 228 ALA C CA  1 
ATOM   6130 C  C   . ALA C  1 228 ? 35.862  2.159   -13.209 1.00 24.52 ? 228 ALA C C   1 
ATOM   6131 O  O   . ALA C  1 228 ? 36.451  2.839   -12.387 1.00 23.34 ? 228 ALA C O   1 
ATOM   6132 C  CB  . ALA C  1 228 ? 37.065  -0.008  -13.517 1.00 24.13 ? 228 ALA C CB  1 
ATOM   6133 N  N   . LEU C  1 229 ? 35.324  2.717   -14.305 1.00 20.09 ? 229 LEU C N   1 
ATOM   6134 C  CA  . LEU C  1 229 ? 35.547  4.137   -14.663 1.00 19.52 ? 229 LEU C CA  1 
ATOM   6135 C  C   . LEU C  1 229 ? 34.376  5.055   -14.635 1.00 22.56 ? 229 LEU C C   1 
ATOM   6136 O  O   . LEU C  1 229 ? 33.217  4.659   -14.813 1.00 19.82 ? 229 LEU C O   1 
ATOM   6137 C  CB  . LEU C  1 229 ? 36.153  4.215   -16.078 1.00 20.10 ? 229 LEU C CB  1 
ATOM   6138 C  CG  . LEU C  1 229 ? 37.259  3.204   -16.296 1.00 18.94 ? 229 LEU C CG  1 
ATOM   6139 C  CD1 . LEU C  1 229 ? 37.738  3.343   -17.753 1.00 22.56 ? 229 LEU C CD1 1 
ATOM   6140 C  CD2 . LEU C  1 229 ? 38.460  3.447   -15.356 1.00 20.13 ? 229 LEU C CD2 1 
ATOM   6141 N  N   . TYR C  1 230 ? 34.664  6.328   -14.415 1.00 24.42 ? 230 TYR C N   1 
ATOM   6142 C  CA  . TYR C  1 230 ? 33.693  7.348   -14.481 1.00 23.44 ? 230 TYR C CA  1 
ATOM   6143 C  C   . TYR C  1 230 ? 34.109  8.158   -15.679 1.00 22.39 ? 230 TYR C C   1 
ATOM   6144 O  O   . TYR C  1 230 ? 35.256  8.134   -16.036 1.00 25.23 ? 230 TYR C O   1 
ATOM   6145 C  CB  . TYR C  1 230 ? 33.774  8.213   -13.234 1.00 25.74 ? 230 TYR C CB  1 
ATOM   6146 C  CG  . TYR C  1 230 ? 33.344  7.625   -11.913 1.00 33.72 ? 230 TYR C CG  1 
ATOM   6147 C  CD1 . TYR C  1 230 ? 31.982  7.481   -11.593 1.00 34.14 ? 230 TYR C CD1 1 
ATOM   6148 C  CD2 . TYR C  1 230 ? 34.306  7.350   -10.928 1.00 37.35 ? 230 TYR C CD2 1 
ATOM   6149 C  CE1 . TYR C  1 230 ? 31.590  7.016   -10.332 1.00 37.26 ? 230 TYR C CE1 1 
ATOM   6150 C  CE2 . TYR C  1 230 ? 33.938  6.890   -9.651  1.00 40.13 ? 230 TYR C CE2 1 
ATOM   6151 C  CZ  . TYR C  1 230 ? 32.581  6.717   -9.362  1.00 39.24 ? 230 TYR C CZ  1 
ATOM   6152 O  OH  . TYR C  1 230 ? 32.243  6.273   -8.093  1.00 45.09 ? 230 TYR C OH  1 
ATOM   6153 N  N   A CYS C  1 231 ? 33.105  8.828   -16.263 0.50 23.94 ? 231 CYS C N   1 
ATOM   6154 N  N   B CYS C  1 231 ? 33.192  8.896   -16.304 0.50 20.21 ? 231 CYS C N   1 
ATOM   6155 C  CA  A CYS C  1 231 ? 33.200  9.715   -17.424 0.50 27.57 ? 231 CYS C CA  1 
ATOM   6156 C  CA  B CYS C  1 231 ? 33.552  9.755   -17.408 0.50 21.57 ? 231 CYS C CA  1 
ATOM   6157 C  C   A CYS C  1 231 ? 33.573  11.127  -16.939 0.50 27.09 ? 231 CYS C C   1 
ATOM   6158 C  C   B CYS C  1 231 ? 33.571  11.218  -16.931 0.50 21.48 ? 231 CYS C C   1 
ATOM   6159 O  O   A CYS C  1 231 ? 33.974  11.978  -17.729 0.50 26.96 ? 231 CYS C O   1 
ATOM   6160 O  O   B CYS C  1 231 ? 33.708  12.174  -17.679 0.50 17.43 ? 231 CYS C O   1 
ATOM   6161 C  CB  A CYS C  1 231 ? 31.853  9.784   -18.146 0.50 30.04 ? 231 CYS C CB  1 
ATOM   6162 C  CB  B CYS C  1 231 ? 32.555  9.555   -18.562 0.50 19.24 ? 231 CYS C CB  1 
ATOM   6163 S  SG  A CYS C  1 231 ? 31.687  8.725   -19.601 0.50 37.13 ? 231 CYS C SG  1 
ATOM   6164 S  SG  B CYS C  1 231 ? 30.833  9.823   -18.117 0.50 23.66 ? 231 CYS C SG  1 
ATOM   6165 N  N   . THR C  1 232 ? 33.434  11.353  -15.632 1.00 23.41 ? 232 THR C N   1 
ATOM   6166 C  CA  . THR C  1 232 ? 33.523  12.681  -14.997 1.00 23.42 ? 232 THR C CA  1 
ATOM   6167 C  C   . THR C  1 232 ? 34.835  12.874  -14.241 1.00 24.98 ? 232 THR C C   1 
ATOM   6168 O  O   . THR C  1 232 ? 35.536  11.917  -13.948 1.00 21.39 ? 232 THR C O   1 
ATOM   6169 C  CB  . THR C  1 232 ? 32.374  12.877  -14.015 1.00 24.41 ? 232 THR C CB  1 
ATOM   6170 O  OG1 . THR C  1 232 ? 32.159  11.631  -13.294 1.00 25.77 ? 232 THR C OG1 1 
ATOM   6171 C  CG2 . THR C  1 232 ? 31.086  13.320  -14.789 1.00 24.65 ? 232 THR C CG2 1 
ATOM   6172 N  N   . HIS C  1 233 ? 35.140  14.150  -13.966 1.00 27.62 ? 233 HIS C N   1 
ATOM   6173 C  CA  . HIS C  1 233 ? 36.356  14.577  -13.255 1.00 28.23 ? 233 HIS C CA  1 
ATOM   6174 C  C   . HIS C  1 233 ? 36.185  14.232  -11.801 1.00 28.23 ? 233 HIS C C   1 
ATOM   6175 O  O   . HIS C  1 233 ? 35.046  14.160  -11.319 1.00 30.14 ? 233 HIS C O   1 
ATOM   6176 C  CB  . HIS C  1 233 ? 36.521  16.069  -13.450 1.00 30.20 ? 233 HIS C CB  1 
ATOM   6177 C  CG  . HIS C  1 233 ? 37.021  16.437  -14.832 1.00 37.15 ? 233 HIS C CG  1 
ATOM   6178 N  ND1 . HIS C  1 233 ? 38.329  16.352  -15.177 1.00 36.68 ? 233 HIS C ND1 1 
ATOM   6179 C  CD2 . HIS C  1 233 ? 36.340  16.875  -15.981 1.00 37.65 ? 233 HIS C CD2 1 
ATOM   6180 C  CE1 . HIS C  1 233 ? 38.483  16.736  -16.469 1.00 36.42 ? 233 HIS C CE1 1 
ATOM   6181 N  NE2 . HIS C  1 233 ? 37.277  17.044  -16.961 1.00 35.24 ? 233 HIS C NE2 1 
ATOM   6182 N  N   . MET C  1 234 ? 37.296  13.943  -11.111 1.00 34.02 ? 234 MET C N   1 
ATOM   6183 C  CA  . MET C  1 234 ? 37.310  13.626  -9.649  1.00 38.64 ? 234 MET C CA  1 
ATOM   6184 C  C   . MET C  1 234 ? 36.479  14.621  -8.779  1.00 43.41 ? 234 MET C C   1 
ATOM   6185 O  O   . MET C  1 234 ? 35.635  14.231  -7.960  1.00 41.12 ? 234 MET C O   1 
ATOM   6186 C  CB  . MET C  1 234 ? 38.752  13.532  -9.156  1.00 39.36 ? 234 MET C CB  1 
ATOM   6187 C  CG  . MET C  1 234 ? 38.919  12.960  -7.741  1.00 41.65 ? 234 MET C CG  1 
ATOM   6188 S  SD  . MET C  1 234 ? 40.647  12.714  -7.227  1.00 47.19 ? 234 MET C SD  1 
ATOM   6189 C  CE  . MET C  1 234 ? 40.815  10.916  -7.184  1.00 38.41 ? 234 MET C CE  1 
ATOM   6190 N  N   . ASP C  1 235 ? 36.680  15.911  -9.025  1.00 45.30 ? 235 ASP C N   1 
ATOM   6191 C  CA  . ASP C  1 235 ? 35.992  16.983  -8.284  1.00 53.05 ? 235 ASP C CA  1 
ATOM   6192 C  C   . ASP C  1 235 ? 34.448  17.034  -8.448  1.00 50.01 ? 235 ASP C C   1 
ATOM   6193 O  O   . ASP C  1 235 ? 33.763  17.689  -7.647  1.00 53.59 ? 235 ASP C O   1 
ATOM   6194 N  N   . ASP C  1 236 ? 33.911  16.340  -9.464  1.00 39.08 ? 236 ASP C N   1 
ATOM   6195 C  CA  . ASP C  1 236 ? 32.486  16.400  -9.835  1.00 39.22 ? 236 ASP C CA  1 
ATOM   6196 C  C   . ASP C  1 236 ? 31.546  15.824  -8.735  1.00 40.10 ? 236 ASP C C   1 
ATOM   6197 O  O   . ASP C  1 236 ? 31.607  14.617  -8.446  1.00 37.63 ? 236 ASP C O   1 
ATOM   6198 C  CB  . ASP C  1 236 ? 32.257  15.724  -11.220 1.00 34.04 ? 236 ASP C CB  1 
ATOM   6199 C  CG  . ASP C  1 236 ? 30.973  16.182  -11.895 1.00 34.54 ? 236 ASP C CG  1 
ATOM   6200 O  OD1 . ASP C  1 236 ? 29.986  16.463  -11.166 1.00 41.28 ? 236 ASP C OD1 1 
ATOM   6201 O  OD2 . ASP C  1 236 ? 30.925  16.286  -13.175 1.00 37.00 ? 236 ASP C OD2 1 
ATOM   6202 N  N   . PRO C  1 237 ? 30.685  16.701  -8.128  1.00 43.37 ? 237 PRO C N   1 
ATOM   6203 C  CA  . PRO C  1 237 ? 29.675  16.302  -7.123  1.00 41.71 ? 237 PRO C CA  1 
ATOM   6204 C  C   . PRO C  1 237 ? 28.588  15.375  -7.723  1.00 39.02 ? 237 PRO C C   1 
ATOM   6205 O  O   . PRO C  1 237 ? 27.782  14.800  -7.001  1.00 34.56 ? 237 PRO C O   1 
ATOM   6206 C  CB  . PRO C  1 237 ? 29.015  17.648  -6.700  1.00 41.77 ? 237 PRO C CB  1 
ATOM   6207 C  CG  . PRO C  1 237 ? 29.731  18.740  -7.420  1.00 39.42 ? 237 PRO C CG  1 
ATOM   6208 C  CD  . PRO C  1 237 ? 30.499  18.112  -8.550  1.00 41.84 ? 237 PRO C CD  1 
ATOM   6209 N  N   . SER C  1 238 ? 28.593  15.255  -9.043  1.00 37.30 ? 238 SER C N   1 
ATOM   6210 C  CA  . SER C  1 238 ? 27.622  14.450  -9.765  1.00 35.35 ? 238 SER C CA  1 
ATOM   6211 C  C   . SER C  1 238 ? 28.275  13.421  -10.726 1.00 33.06 ? 238 SER C C   1 
ATOM   6212 O  O   . SER C  1 238 ? 28.232  13.613  -11.972 1.00 31.07 ? 238 SER C O   1 
ATOM   6213 C  CB  . SER C  1 238 ? 26.737  15.421  -10.528 1.00 36.92 ? 238 SER C CB  1 
ATOM   6214 O  OG  . SER C  1 238 ? 25.448  14.871  -10.658 1.00 46.82 ? 238 SER C OG  1 
ATOM   6215 N  N   . PRO C  1 239 ? 28.949  12.373  -10.179 1.00 31.40 ? 239 PRO C N   1 
ATOM   6216 C  CA  . PRO C  1 239 ? 29.694  11.426  -11.006 1.00 29.67 ? 239 PRO C CA  1 
ATOM   6217 C  C   . PRO C  1 239 ? 28.865  10.565  -11.946 1.00 31.42 ? 239 PRO C C   1 
ATOM   6218 O  O   . PRO C  1 239 ? 27.767  10.179  -11.622 1.00 32.96 ? 239 PRO C O   1 
ATOM   6219 C  CB  . PRO C  1 239 ? 30.307  10.464  -9.984  1.00 31.41 ? 239 PRO C CB  1 
ATOM   6220 C  CG  . PRO C  1 239 ? 29.471  10.673  -8.761  1.00 29.62 ? 239 PRO C CG  1 
ATOM   6221 C  CD  . PRO C  1 239 ? 29.262  12.120  -8.755  1.00 26.94 ? 239 PRO C CD  1 
ATOM   6222 N  N   . ARG C  1 240 ? 29.415  10.290  -13.101 1.00 28.06 ? 240 ARG C N   1 
ATOM   6223 C  CA  . ARG C  1 240 ? 28.686  9.456   -14.048 1.00 26.54 ? 240 ARG C CA  1 
ATOM   6224 C  C   . ARG C  1 240 ? 29.606  8.294   -14.366 1.00 24.76 ? 240 ARG C C   1 
ATOM   6225 O  O   . ARG C  1 240 ? 30.760  8.488   -14.696 1.00 27.02 ? 240 ARG C O   1 
ATOM   6226 C  CB  . ARG C  1 240 ? 28.294  10.280  -15.282 1.00 32.61 ? 240 ARG C CB  1 
ATOM   6227 C  CG  . ARG C  1 240 ? 27.511  9.491   -16.357 1.00 35.64 ? 240 ARG C CG  1 
ATOM   6228 N  N   . GLU C  1 241 ? 29.042  7.082   -14.385 1.00 23.94 ? 241 GLU C N   1 
ATOM   6229 C  CA  . GLU C  1 241 ? 29.790  5.861   -14.786 1.00 24.18 ? 241 GLU C CA  1 
ATOM   6230 C  C   . GLU C  1 241 ? 30.100  5.838   -16.302 1.00 23.11 ? 241 GLU C C   1 
ATOM   6231 O  O   . GLU C  1 241 ? 29.257  6.246   -17.089 1.00 24.50 ? 241 GLU C O   1 
ATOM   6232 C  CB  . GLU C  1 241 ? 29.024  4.583   -14.493 1.00 29.24 ? 241 GLU C CB  1 
ATOM   6233 C  CG  . GLU C  1 241 ? 28.844  4.358   -13.021 1.00 35.38 ? 241 GLU C CG  1 
ATOM   6234 C  CD  . GLU C  1 241 ? 27.745  3.364   -12.681 1.00 49.05 ? 241 GLU C CD  1 
ATOM   6235 O  OE1 . GLU C  1 241 ? 27.005  2.899   -13.590 1.00 53.21 ? 241 GLU C OE1 1 
ATOM   6236 O  OE2 . GLU C  1 241 ? 27.625  3.062   -11.465 1.00 56.84 ? 241 GLU C OE2 1 
ATOM   6237 N  N   . MET C  1 242 ? 31.290  5.382   -16.660 1.00 20.34 ? 242 MET C N   1 
ATOM   6238 C  CA  . MET C  1 242 ? 31.680  5.196   -18.105 1.00 16.79 ? 242 MET C CA  1 
ATOM   6239 C  C   . MET C  1 242 ? 31.186  3.811   -18.556 1.00 16.20 ? 242 MET C C   1 
ATOM   6240 O  O   . MET C  1 242 ? 31.810  2.809   -18.308 1.00 17.26 ? 242 MET C O   1 
ATOM   6241 C  CB  . MET C  1 242 ? 33.201  5.276   -18.274 1.00 18.25 ? 242 MET C CB  1 
ATOM   6242 C  CG  . MET C  1 242 ? 33.552  5.338   -19.788 1.00 19.45 ? 242 MET C CG  1 
ATOM   6243 S  SD  . MET C  1 242 ? 35.297  5.309   -19.996 1.00 20.05 ? 242 MET C SD  1 
ATOM   6244 C  CE  . MET C  1 242 ? 35.810  6.957   -19.419 1.00 17.51 ? 242 MET C CE  1 
ATOM   6245 N  N   . ILE C  1 243 ? 30.038  3.806   -19.217 1.00 15.90 ? 243 ILE C N   1 
ATOM   6246 C  CA  . ILE C  1 243 ? 29.394  2.623   -19.716 1.00 16.91 ? 243 ILE C CA  1 
ATOM   6247 C  C   . ILE C  1 243 ? 28.870  2.993   -21.118 1.00 15.14 ? 243 ILE C C   1 
ATOM   6248 O  O   . ILE C  1 243 ? 28.635  4.150   -21.437 1.00 15.81 ? 243 ILE C O   1 
ATOM   6249 C  CB  . ILE C  1 243 ? 28.248  2.101   -18.772 1.00 17.61 ? 243 ILE C CB  1 
ATOM   6250 C  CG1 . ILE C  1 243 ? 27.289  3.259   -18.470 1.00 19.63 ? 243 ILE C CG1 1 
ATOM   6251 C  CG2 . ILE C  1 243 ? 28.823  1.438   -17.498 1.00 18.76 ? 243 ILE C CG2 1 
ATOM   6252 C  CD1 . ILE C  1 243 ? 26.080  2.817   -17.630 1.00 20.83 ? 243 ILE C CD1 1 
ATOM   6253 N  N   . ASN C  1 244 ? 28.537  1.901   -21.836 1.00 12.99 ? 244 ASN C N   1 
ATOM   6254 C  CA  . ASN C  1 244 ? 27.866  2.034   -23.156 1.00 15.18 ? 244 ASN C CA  1 
ATOM   6255 C  C   . ASN C  1 244 ? 28.567  3.032   -24.077 1.00 13.01 ? 244 ASN C C   1 
ATOM   6256 O  O   . ASN C  1 244 ? 27.964  3.877   -24.724 1.00 13.98 ? 244 ASN C O   1 
ATOM   6257 C  CB  . ASN C  1 244 ? 26.393  2.425   -22.940 1.00 16.07 ? 244 ASN C CB  1 
ATOM   6258 C  CG  . ASN C  1 244 ? 25.661  1.494   -22.005 1.00 16.60 ? 244 ASN C CG  1 
ATOM   6259 O  OD1 . ASN C  1 244 ? 25.844  0.295   -22.064 1.00 17.62 ? 244 ASN C OD1 1 
ATOM   6260 N  ND2 . ASN C  1 244 ? 24.851  2.092   -21.101 1.00 20.28 ? 244 ASN C ND2 1 
ATOM   6261 N  N   . ASN C  1 245 ? 29.896  2.888   -24.103 1.00 14.43 ? 245 ASN C N   1 
ATOM   6262 C  CA  . ASN C  1 245 ? 30.712  3.870   -24.872 1.00 12.95 ? 245 ASN C CA  1 
ATOM   6263 C  C   . ASN C  1 245 ? 31.030  3.311   -26.257 1.00 13.04 ? 245 ASN C C   1 
ATOM   6264 O  O   . ASN C  1 245 ? 32.184  3.181   -26.634 1.00 14.01 ? 245 ASN C O   1 
ATOM   6265 C  CB  . ASN C  1 245 ? 31.952  4.237   -24.051 1.00 13.67 ? 245 ASN C CB  1 
ATOM   6266 C  CG  . ASN C  1 245 ? 32.842  3.040   -23.736 1.00 15.20 ? 245 ASN C CG  1 
ATOM   6267 O  OD1 . ASN C  1 245 ? 32.473  1.864   -23.734 1.00 16.41 ? 245 ASN C OD1 1 
ATOM   6268 N  ND2 . ASN C  1 245 ? 34.112  3.350   -23.387 1.00 17.56 ? 245 ASN C ND2 1 
ATOM   6269 N  N   . PHE C  1 246 ? 29.949  3.013   -26.959 1.00 12.18 ? 246 PHE C N   1 
ATOM   6270 C  CA  . PHE C  1 246 ? 30.057  2.420   -28.323 1.00 12.23 ? 246 PHE C CA  1 
ATOM   6271 C  C   . PHE C  1 246 ? 29.078  3.232   -29.146 1.00 11.37 ? 246 PHE C C   1 
ATOM   6272 O  O   . PHE C  1 246 ? 28.078  3.752   -28.627 1.00 11.86 ? 246 PHE C O   1 
ATOM   6273 C  CB  . PHE C  1 246 ? 29.731  0.903   -28.372 1.00 11.87 ? 246 PHE C CB  1 
ATOM   6274 C  CG  . PHE C  1 246 ? 28.358  0.575   -27.928 1.00 11.80 ? 246 PHE C CG  1 
ATOM   6275 C  CD1 . PHE C  1 246 ? 28.105  0.388   -26.548 1.00 13.46 ? 246 PHE C CD1 1 
ATOM   6276 C  CD2 . PHE C  1 246 ? 27.272  0.440   -28.831 1.00 13.38 ? 246 PHE C CD2 1 
ATOM   6277 C  CE1 . PHE C  1 246 ? 26.813  0.120   -26.110 1.00 13.99 ? 246 PHE C CE1 1 
ATOM   6278 C  CE2 . PHE C  1 246 ? 26.000  0.184   -28.382 1.00 14.64 ? 246 PHE C CE2 1 
ATOM   6279 C  CZ  . PHE C  1 246 ? 25.736  0.002   -27.018 1.00 13.41 ? 246 PHE C CZ  1 
ATOM   6280 N  N   . ARG C  1 247 ? 29.389  3.344   -30.452 1.00 10.20 ? 247 ARG C N   1 
ATOM   6281 C  CA  . ARG C  1 247 ? 28.471  4.068   -31.383 1.00 10.69 ? 247 ARG C CA  1 
ATOM   6282 C  C   . ARG C  1 247 ? 27.498  3.014   -31.949 1.00 9.47  ? 247 ARG C C   1 
ATOM   6283 O  O   . ARG C  1 247 ? 27.924  1.858   -32.174 1.00 10.46 ? 247 ARG C O   1 
ATOM   6284 C  CB  . ARG C  1 247 ? 29.289  4.705   -32.521 1.00 9.82  ? 247 ARG C CB  1 
ATOM   6285 C  CG  . ARG C  1 247 ? 28.530  5.731   -33.373 1.00 10.30 ? 247 ARG C CG  1 
ATOM   6286 C  CD  . ARG C  1 247 ? 29.348  6.114   -34.583 1.00 10.29 ? 247 ARG C CD  1 
ATOM   6287 N  NE  . ARG C  1 247 ? 28.806  7.307   -35.197 1.00 9.47  ? 247 ARG C NE  1 
ATOM   6288 C  CZ  . ARG C  1 247 ? 29.282  7.847   -36.304 1.00 9.99  ? 247 ARG C CZ  1 
ATOM   6289 N  NH1 . ARG C  1 247 ? 30.321  7.289   -36.907 1.00 11.80 ? 247 ARG C NH1 1 
ATOM   6290 N  NH2 . ARG C  1 247 ? 28.720  8.938   -36.816 1.00 10.28 ? 247 ARG C NH2 1 
ATOM   6291 N  N   . GLN C  1 248 ? 26.266  3.417   -32.191 1.00 9.84  ? 248 GLN C N   1 
ATOM   6292 C  CA  . GLN C  1 248 ? 25.291  2.527   -32.868 1.00 10.01 ? 248 GLN C CA  1 
ATOM   6293 C  C   . GLN C  1 248 ? 25.830  2.243   -34.309 1.00 10.80 ? 248 GLN C C   1 
ATOM   6294 O  O   . GLN C  1 248 ? 26.584  3.047   -34.926 1.00 10.31 ? 248 GLN C O   1 
ATOM   6295 C  CB  . GLN C  1 248 ? 23.937  3.248   -33.011 1.00 11.04 ? 248 GLN C CB  1 
ATOM   6296 C  CG  . GLN C  1 248 ? 23.261  3.573   -31.671 1.00 10.71 ? 248 GLN C CG  1 
ATOM   6297 C  CD  . GLN C  1 248 ? 22.913  2.312   -30.834 1.00 11.97 ? 248 GLN C CD  1 
ATOM   6298 O  OE1 . GLN C  1 248 ? 23.645  1.891   -29.917 1.00 14.04 ? 248 GLN C OE1 1 
ATOM   6299 N  NE2 . GLN C  1 248 ? 21.808  1.651   -31.235 1.00 12.94 ? 248 GLN C NE2 1 
ATOM   6300 N  N   . VAL C  1 249 ? 25.461  1.093   -34.856 1.00 10.01 ? 249 VAL C N   1 
ATOM   6301 C  CA  . VAL C  1 249 ? 25.813  0.775   -36.221 1.00 10.77 ? 249 VAL C CA  1 
ATOM   6302 C  C   . VAL C  1 249 ? 25.243  1.793   -37.254 1.00 10.61 ? 249 VAL C C   1 
ATOM   6303 O  O   . VAL C  1 249 ? 24.106  2.258   -37.044 1.00 10.27 ? 249 VAL C O   1 
ATOM   6304 C  CB  . VAL C  1 249 ? 25.448  -0.678  -36.636 1.00 11.52 ? 249 VAL C CB  1 
ATOM   6305 C  CG1 . VAL C  1 249 ? 26.334  -1.708  -35.881 1.00 12.71 ? 249 VAL C CG1 1 
ATOM   6306 C  CG2 . VAL C  1 249 ? 24.000  -0.947  -36.570 1.00 15.05 ? 249 VAL C CG2 1 
ATOM   6307 N  N   . GLN C  1 250 ? 25.990  1.984   -38.329 1.00 10.44 ? 250 GLN C N   1 
ATOM   6308 C  CA  . GLN C  1 250 ? 25.599  2.939   -39.359 1.00 10.52 ? 250 GLN C CA  1 
ATOM   6309 C  C   . GLN C  1 250 ? 25.012  2.209   -40.540 1.00 11.49 ? 250 GLN C C   1 
ATOM   6310 O  O   . GLN C  1 250 ? 25.382  1.076   -40.805 1.00 12.39 ? 250 GLN C O   1 
ATOM   6311 C  CB  . GLN C  1 250 ? 26.868  3.643   -39.811 1.00 11.09 ? 250 GLN C CB  1 
ATOM   6312 C  CG  . GLN C  1 250 ? 27.653  4.267   -38.597 1.00 10.67 ? 250 GLN C CG  1 
ATOM   6313 C  CD  . GLN C  1 250 ? 26.970  5.403   -37.961 1.00 10.46 ? 250 GLN C CD  1 
ATOM   6314 O  OE1 . GLN C  1 250 ? 26.705  6.455   -38.668 1.00 10.91 ? 250 GLN C OE1 1 
ATOM   6315 N  NE2 . GLN C  1 250 ? 26.571  5.253   -36.718 1.00 10.76 ? 250 GLN C NE2 1 
ATOM   6316 N  N   . LYS C  1 251 ? 24.183  2.953   -41.301 1.00 10.70 ? 251 LYS C N   1 
ATOM   6317 C  CA  . LYS C  1 251 ? 23.735  2.341   -42.590 1.00 10.34 ? 251 LYS C CA  1 
ATOM   6318 C  C   . LYS C  1 251 ? 24.936  2.069   -43.458 1.00 12.04 ? 251 LYS C C   1 
ATOM   6319 O  O   . LYS C  1 251 ? 25.905  2.865   -43.467 1.00 11.67 ? 251 LYS C O   1 
ATOM   6320 C  CB  . LYS C  1 251 ? 22.746  3.244   -43.283 1.00 11.20 ? 251 LYS C CB  1 
ATOM   6321 C  CG  . LYS C  1 251 ? 21.353  3.189   -42.585 1.00 12.10 ? 251 LYS C CG  1 
ATOM   6322 C  CD  . LYS C  1 251 ? 20.404  4.207   -43.116 1.00 12.38 ? 251 LYS C CD  1 
ATOM   6323 C  CE  . LYS C  1 251 ? 18.900  3.894   -42.820 1.00 11.18 ? 251 LYS C CE  1 
ATOM   6324 N  NZ  . LYS C  1 251 ? 18.727  3.960   -41.319 1.00 10.92 ? 251 LYS C NZ  1 
ATOM   6325 N  N   . PHE C  1 252 ? 24.829  0.995   -44.237 1.00 12.50 ? 252 PHE C N   1 
ATOM   6326 C  CA  . PHE C  1 252 ? 25.940  0.528   -45.114 1.00 13.73 ? 252 PHE C CA  1 
ATOM   6327 C  C   . PHE C  1 252 ? 25.223  -0.037  -46.343 1.00 17.53 ? 252 PHE C C   1 
ATOM   6328 O  O   . PHE C  1 252 ? 24.831  -1.190  -46.327 1.00 20.98 ? 252 PHE C O   1 
ATOM   6329 C  CB  . PHE C  1 252 ? 26.715  -0.551  -44.411 1.00 14.19 ? 252 PHE C CB  1 
ATOM   6330 C  CG  . PHE C  1 252 ? 28.004  -0.982  -45.074 1.00 13.11 ? 252 PHE C CG  1 
ATOM   6331 C  CD1 . PHE C  1 252 ? 29.159  -0.172  -44.992 1.00 13.48 ? 252 PHE C CD1 1 
ATOM   6332 C  CD2 . PHE C  1 252 ? 28.077  -2.248  -45.692 1.00 16.29 ? 252 PHE C CD2 1 
ATOM   6333 C  CE1 . PHE C  1 252 ? 30.380  -0.621  -45.533 1.00 13.50 ? 252 PHE C CE1 1 
ATOM   6334 C  CE2 . PHE C  1 252 ? 29.310  -2.656  -46.224 1.00 14.39 ? 252 PHE C CE2 1 
ATOM   6335 C  CZ  . PHE C  1 252 ? 30.423  -1.828  -46.147 1.00 14.13 ? 252 PHE C CZ  1 
ATOM   6336 N  N   . ASP C  1 253 ? 25.087  0.776   -47.352 1.00 19.91 ? 253 ASP C N   1 
ATOM   6337 C  CA  . ASP C  1 253 ? 24.199  0.469   -48.500 1.00 22.38 ? 253 ASP C CA  1 
ATOM   6338 C  C   . ASP C  1 253 ? 24.960  0.367   -49.765 1.00 19.53 ? 253 ASP C C   1 
ATOM   6339 O  O   . ASP C  1 253 ? 25.771  1.205   -50.066 1.00 21.84 ? 253 ASP C O   1 
ATOM   6340 C  CB  . ASP C  1 253 ? 23.250  1.641   -48.748 1.00 28.82 ? 253 ASP C CB  1 
ATOM   6341 N  N   . GLU C  1 254 ? 24.634  -0.663  -50.529 1.00 20.47 ? 254 GLU C N   1 
ATOM   6342 C  CA  . GLU C  1 254 ? 25.310  -0.911  -51.789 1.00 21.97 ? 254 GLU C CA  1 
ATOM   6343 C  C   . GLU C  1 254 ? 26.847  -0.965  -51.639 1.00 19.18 ? 254 GLU C C   1 
ATOM   6344 O  O   . GLU C  1 254 ? 27.580  -0.450  -52.504 1.00 21.50 ? 254 GLU C O   1 
ATOM   6345 C  CB  . GLU C  1 254 ? 24.919  0.164   -52.843 1.00 25.34 ? 254 GLU C CB  1 
ATOM   6346 C  CG  . GLU C  1 254 ? 23.421  0.115   -53.204 1.00 29.69 ? 254 GLU C CG  1 
ATOM   6347 C  CD  . GLU C  1 254 ? 23.038  -1.187  -53.882 1.00 40.42 ? 254 GLU C CD  1 
ATOM   6348 O  OE1 . GLU C  1 254 ? 23.717  -1.561  -54.879 1.00 44.06 ? 254 GLU C OE1 1 
ATOM   6349 O  OE2 . GLU C  1 254 ? 22.071  -1.858  -53.434 1.00 46.22 ? 254 GLU C OE2 1 
ATOM   6350 N  N   . ARG C  1 255 ? 27.294  -1.563  -50.540 1.00 17.97 ? 255 ARG C N   1 
ATOM   6351 C  CA  . ARG C  1 255 ? 28.694  -1.727  -50.333 1.00 16.57 ? 255 ARG C CA  1 
ATOM   6352 C  C   . ARG C  1 255 ? 28.943  -3.132  -49.856 1.00 15.09 ? 255 ARG C C   1 
ATOM   6353 O  O   . ARG C  1 255 ? 28.060  -3.796  -49.243 1.00 17.62 ? 255 ARG C O   1 
ATOM   6354 C  CB  . ARG C  1 255 ? 29.253  -0.755  -49.285 1.00 15.16 ? 255 ARG C CB  1 
ATOM   6355 C  CG  . ARG C  1 255 ? 29.147  0.690   -49.738 1.00 16.32 ? 255 ARG C CG  1 
ATOM   6356 C  CD  . ARG C  1 255 ? 29.763  1.679   -48.756 1.00 17.42 ? 255 ARG C CD  1 
ATOM   6357 N  NE  . ARG C  1 255 ? 31.137  1.262   -48.512 1.00 19.01 ? 255 ARG C NE  1 
ATOM   6358 C  CZ  . ARG C  1 255 ? 31.851  1.573   -47.438 1.00 16.46 ? 255 ARG C CZ  1 
ATOM   6359 N  NH1 . ARG C  1 255 ? 31.334  2.331   -46.482 1.00 18.02 ? 255 ARG C NH1 1 
ATOM   6360 N  NH2 . ARG C  1 255 ? 33.092  1.124   -47.329 1.00 14.05 ? 255 ARG C NH2 1 
ATOM   6361 N  N   . LEU C  1 256 ? 30.197  -3.590  -50.087 1.00 16.20 ? 256 LEU C N   1 
ATOM   6362 C  CA  . LEU C  1 256 ? 30.586  -4.884  -49.611 1.00 17.25 ? 256 LEU C CA  1 
ATOM   6363 C  C   . LEU C  1 256 ? 31.612  -4.807  -48.420 1.00 14.57 ? 256 LEU C C   1 
ATOM   6364 O  O   . LEU C  1 256 ? 32.331  -3.832  -48.251 1.00 15.11 ? 256 LEU C O   1 
ATOM   6365 C  CB  . LEU C  1 256 ? 31.257  -5.682  -50.742 1.00 20.35 ? 256 LEU C CB  1 
ATOM   6366 C  CG  . LEU C  1 256 ? 30.332  -5.985  -51.940 1.00 23.19 ? 256 LEU C CG  1 
ATOM   6367 C  CD1 . LEU C  1 256 ? 31.187  -6.385  -53.131 1.00 22.43 ? 256 LEU C CD1 1 
ATOM   6368 C  CD2 . LEU C  1 256 ? 29.428  -7.154  -51.613 1.00 23.91 ? 256 LEU C CD2 1 
ATOM   6369 N  N   . VAL C  1 257 ? 31.639  -5.895  -47.657 1.00 16.32 ? 257 VAL C N   1 
ATOM   6370 C  CA  . VAL C  1 257 ? 32.743  -6.111  -46.701 1.00 15.27 ? 257 VAL C CA  1 
ATOM   6371 C  C   . VAL C  1 257 ? 33.546  -7.283  -47.262 1.00 15.18 ? 257 VAL C C   1 
ATOM   6372 O  O   . VAL C  1 257 ? 33.010  -8.364  -47.604 1.00 15.97 ? 257 VAL C O   1 
ATOM   6373 C  CB  . VAL C  1 257 ? 32.244  -6.433  -45.312 1.00 14.72 ? 257 VAL C CB  1 
ATOM   6374 C  CG1 . VAL C  1 257 ? 33.379  -6.882  -44.354 1.00 16.54 ? 257 VAL C CG1 1 
ATOM   6375 C  CG2 . VAL C  1 257 ? 31.495  -5.286  -44.723 1.00 17.43 ? 257 VAL C CG2 1 
ATOM   6376 N  N   . TYR C  1 258 ? 34.840  -7.138  -47.395 1.00 12.99 ? 258 TYR C N   1 
ATOM   6377 C  CA  . TYR C  1 258 ? 35.667  -8.149  -48.051 1.00 14.60 ? 258 TYR C CA  1 
ATOM   6378 C  C   . TYR C  1 258 ? 36.217  -9.057  -46.991 1.00 13.88 ? 258 TYR C C   1 
ATOM   6379 O  O   . TYR C  1 258 ? 36.523  -8.648  -45.816 1.00 16.07 ? 258 TYR C O   1 
ATOM   6380 C  CB  . TYR C  1 258 ? 36.773  -7.454  -48.916 1.00 15.96 ? 258 TYR C CB  1 
ATOM   6381 C  CG  . TYR C  1 258 ? 36.137  -6.575  -49.924 1.00 19.53 ? 258 TYR C CG  1 
ATOM   6382 C  CD1 . TYR C  1 258 ? 35.654  -7.133  -51.135 1.00 20.09 ? 258 TYR C CD1 1 
ATOM   6383 C  CD2 . TYR C  1 258 ? 36.003  -5.192  -49.681 1.00 18.43 ? 258 TYR C CD2 1 
ATOM   6384 C  CE1 . TYR C  1 258 ? 35.017  -6.326  -52.080 1.00 21.81 ? 258 TYR C CE1 1 
ATOM   6385 C  CE2 . TYR C  1 258 ? 35.364  -4.384  -50.600 1.00 25.81 ? 258 TYR C CE2 1 
ATOM   6386 C  CZ  . TYR C  1 258 ? 34.865  -4.933  -51.820 1.00 22.59 ? 258 TYR C CZ  1 
ATOM   6387 O  OH  . TYR C  1 258 ? 34.172  -4.057  -52.732 1.00 25.10 ? 258 TYR C OH  1 
ATOM   6388 N  N   . THR C  1 259 ? 36.316  -10.350 -47.294 1.00 15.21 ? 259 THR C N   1 
ATOM   6389 C  CA  . THR C  1 259 ? 36.769  -11.255 -46.269 1.00 15.30 ? 259 THR C CA  1 
ATOM   6390 C  C   . THR C  1 259 ? 37.969  -12.039 -46.766 1.00 16.26 ? 259 THR C C   1 
ATOM   6391 O  O   . THR C  1 259 ? 38.104  -12.357 -47.971 1.00 17.97 ? 259 THR C O   1 
ATOM   6392 C  CB  . THR C  1 259 ? 35.666  -12.275 -45.912 1.00 16.10 ? 259 THR C CB  1 
ATOM   6393 O  OG1 . THR C  1 259 ? 35.279  -13.023 -47.114 1.00 17.99 ? 259 THR C OG1 1 
ATOM   6394 C  CG2 . THR C  1 259 ? 34.462  -11.582 -45.309 1.00 18.50 ? 259 THR C CG2 1 
ATOM   6395 N  N   . SER C  1 260 ? 38.856  -12.387 -45.813 1.00 15.95 ? 260 SER C N   1 
ATOM   6396 C  CA  . SER C  1 260 ? 40.087  -13.085 -46.212 1.00 17.41 ? 260 SER C CA  1 
ATOM   6397 C  C   . SER C  1 260 ? 39.799  -14.562 -46.243 1.00 19.37 ? 260 SER C C   1 
ATOM   6398 O  O   . SER C  1 260 ? 40.704  -15.369 -46.656 1.00 23.62 ? 260 SER C O   1 
ATOM   6399 C  CB  . SER C  1 260 ? 41.207  -12.792 -45.236 1.00 16.74 ? 260 SER C CB  1 
ATOM   6400 O  OG  . SER C  1 260 ? 40.824  -13.276 -43.955 1.00 17.27 ? 260 SER C OG  1 
ATOM   6401 N  N   . PHE C  1 261 ? 38.616  -14.932 -45.801 1.00 18.53 ? 261 PHE C N   1 
ATOM   6402 C  CA  . PHE C  1 261 ? 38.223  -16.319 -45.652 1.00 21.38 ? 261 PHE C CA  1 
ATOM   6403 C  C   . PHE C  1 261 ? 37.111  -16.528 -46.579 1.00 22.84 ? 261 PHE C C   1 
ATOM   6404 O  O   . PHE C  1 261 ? 36.340  -15.616 -46.898 1.00 25.03 ? 261 PHE C O   1 
ATOM   6405 C  CB  . PHE C  1 261 ? 37.820  -16.653 -44.188 1.00 23.19 ? 261 PHE C CB  1 
ATOM   6406 C  CG  . PHE C  1 261 ? 36.783  -15.710 -43.630 1.00 23.06 ? 261 PHE C CG  1 
ATOM   6407 C  CD1 . PHE C  1 261 ? 37.181  -14.578 -42.994 1.00 21.48 ? 261 PHE C CD1 1 
ATOM   6408 C  CD2 . PHE C  1 261 ? 35.427  -15.991 -43.720 1.00 22.29 ? 261 PHE C CD2 1 
ATOM   6409 C  CE1 . PHE C  1 261 ? 36.233  -13.731 -42.447 1.00 20.72 ? 261 PHE C CE1 1 
ATOM   6410 C  CE2 . PHE C  1 261 ? 34.463  -15.140 -43.205 1.00 26.73 ? 261 PHE C CE2 1 
ATOM   6411 C  CZ  . PHE C  1 261 ? 34.880  -13.971 -42.561 1.00 21.85 ? 261 PHE C CZ  1 
ATOM   6412 N  N   . SER C  1 262 ? 36.989  -17.773 -47.033 1.00 29.52 ? 262 SER C N   1 
ATOM   6413 C  CA  . SER C  1 262 ? 35.815  -18.055 -47.817 1.00 40.26 ? 262 SER C CA  1 
ATOM   6414 C  C   . SER C  1 262 ? 34.740  -18.842 -47.086 1.00 49.57 ? 262 SER C C   1 
ATOM   6415 O  O   . SER C  1 262 ? 33.550  -18.464 -47.085 1.00 56.79 ? 262 SER C O   1 
ATOM   6416 C  CB  . SER C  1 262 ? 36.186  -18.780 -49.089 1.00 44.39 ? 262 SER C CB  1 
ATOM   6417 O  OG  . SER C  1 262 ? 34.989  -19.347 -49.582 1.00 46.61 ? 262 SER C OG  1 
ATOM   6418 N  N   . GLN C  1 263 ? 35.153  -19.964 -46.516 1.00 44.49 ? 263 GLN C N   1 
ATOM   6419 C  CA  . GLN C  1 263 ? 34.206  -20.941 -45.963 1.00 50.50 ? 263 GLN C CA  1 
ATOM   6420 C  C   . GLN C  1 263 ? 33.825  -20.613 -44.497 1.00 53.59 ? 263 GLN C C   1 
ATOM   6421 O  O   . GLN C  1 263 ? 34.567  -19.906 -43.793 1.00 53.02 ? 263 GLN C O   1 
ATOM   6422 C  CB  . GLN C  1 263 ? 34.760  -22.384 -46.134 1.00 42.65 ? 263 GLN C CB  1 
ATOM   6423 C  CG  . GLN C  1 263 ? 36.181  -22.634 -45.579 1.00 41.77 ? 263 GLN C CG  1 
ATOM   6424 C  CD  . GLN C  1 263 ? 36.781  -23.997 -45.985 1.00 41.19 ? 263 GLN C CD  1 
ATOM   6425 O  OE1 . GLN C  1 263 ? 37.961  -24.305 -45.682 1.00 39.54 ? 263 GLN C OE1 1 
ATOM   6426 N  NE2 . GLN C  1 263 ? 35.972  -24.826 -46.659 1.00 25.30 ? 263 GLN C NE2 1 
ATOM   6427 N  N   . LYS D  1 3   ? 14.004  19.647  -45.605 1.00 34.92 ? 3   LYS D N   1 
ATOM   6428 C  CA  . LYS D  1 3   ? 14.605  18.721  -46.602 1.00 32.32 ? 3   LYS D CA  1 
ATOM   6429 C  C   . LYS D  1 3   ? 15.414  17.604  -45.921 1.00 30.76 ? 3   LYS D C   1 
ATOM   6430 O  O   . LYS D  1 3   ? 16.348  17.050  -46.533 1.00 28.60 ? 3   LYS D O   1 
ATOM   6431 C  CB  . LYS D  1 3   ? 15.513  19.495  -47.557 1.00 38.05 ? 3   LYS D CB  1 
ATOM   6432 C  CG  . LYS D  1 3   ? 16.399  20.536  -46.872 1.00 43.98 ? 3   LYS D CG  1 
ATOM   6433 C  CD  . LYS D  1 3   ? 17.237  21.310  -47.897 1.00 46.99 ? 3   LYS D CD  1 
ATOM   6434 C  CE  . LYS D  1 3   ? 18.326  20.419  -48.488 1.00 44.91 ? 3   LYS D CE  1 
ATOM   6435 N  NZ  . LYS D  1 3   ? 19.479  20.311  -47.544 1.00 36.65 ? 3   LYS D NZ  1 
ATOM   6436 N  N   . TRP D  1 4   ? 15.041  17.236  -44.664 1.00 18.72 ? 4   TRP D N   1 
ATOM   6437 C  CA  . TRP D  1 4   ? 15.674  16.036  -44.110 1.00 16.66 ? 4   TRP D CA  1 
ATOM   6438 C  C   . TRP D  1 4   ? 15.382  14.830  -44.994 1.00 14.85 ? 4   TRP D C   1 
ATOM   6439 O  O   . TRP D  1 4   ? 14.326  14.733  -45.663 1.00 16.84 ? 4   TRP D O   1 
ATOM   6440 C  CB  . TRP D  1 4   ? 15.182  15.848  -42.665 1.00 14.56 ? 4   TRP D CB  1 
ATOM   6441 C  CG  . TRP D  1 4   ? 13.739  15.550  -42.481 1.00 13.36 ? 4   TRP D CG  1 
ATOM   6442 C  CD1 . TRP D  1 4   ? 12.676  16.449  -42.207 1.00 13.69 ? 4   TRP D CD1 1 
ATOM   6443 C  CD2 . TRP D  1 4   ? 13.124  14.211  -42.479 1.00 13.29 ? 4   TRP D CD2 1 
ATOM   6444 N  NE1 . TRP D  1 4   ? 11.515  15.782  -42.104 1.00 15.10 ? 4   TRP D NE1 1 
ATOM   6445 C  CE2 . TRP D  1 4   ? 11.718  14.417  -42.229 1.00 12.69 ? 4   TRP D CE2 1 
ATOM   6446 C  CE3 . TRP D  1 4   ? 13.632  12.918  -42.644 1.00 12.60 ? 4   TRP D CE3 1 
ATOM   6447 C  CZ2 . TRP D  1 4   ? 10.827  13.370  -42.133 1.00 13.65 ? 4   TRP D CZ2 1 
ATOM   6448 C  CZ3 . TRP D  1 4   ? 12.717  11.837  -42.550 1.00 11.90 ? 4   TRP D CZ3 1 
ATOM   6449 C  CH2 . TRP D  1 4   ? 11.363  12.092  -42.319 1.00 12.21 ? 4   TRP D CH2 1 
ATOM   6450 N  N   . THR D  1 5   ? 16.293  13.881  -44.902 1.00 13.52 ? 5   THR D N   1 
ATOM   6451 C  CA  . THR D  1 5   ? 16.211  12.640  -45.695 1.00 14.07 ? 5   THR D CA  1 
ATOM   6452 C  C   . THR D  1 5   ? 16.709  11.443  -44.875 1.00 15.41 ? 5   THR D C   1 
ATOM   6453 O  O   . THR D  1 5   ? 17.088  11.612  -43.671 1.00 12.88 ? 5   THR D O   1 
ATOM   6454 C  CB  . THR D  1 5   ? 17.177  12.658  -46.934 1.00 16.53 ? 5   THR D CB  1 
ATOM   6455 O  OG1 . THR D  1 5   ? 18.497  12.681  -46.422 1.00 17.66 ? 5   THR D OG1 1 
ATOM   6456 C  CG2 . THR D  1 5   ? 16.969  13.870  -47.846 1.00 17.06 ? 5   THR D CG2 1 
ATOM   6457 N  N   . TYR D  1 6   ? 16.781  10.242  -45.481 1.00 12.50 ? 6   TYR D N   1 
ATOM   6458 C  CA  . TYR D  1 6   ? 17.323  9.066   -44.819 1.00 13.42 ? 6   TYR D CA  1 
ATOM   6459 C  C   . TYR D  1 6   ? 18.700  8.670   -45.389 1.00 13.91 ? 6   TYR D C   1 
ATOM   6460 O  O   . TYR D  1 6   ? 19.250  7.607   -45.100 1.00 14.73 ? 6   TYR D O   1 
ATOM   6461 C  CB  . TYR D  1 6   ? 16.389  7.873   -44.971 1.00 11.93 ? 6   TYR D CB  1 
ATOM   6462 C  CG  . TYR D  1 6   ? 15.146  7.928   -44.121 1.00 10.95 ? 6   TYR D CG  1 
ATOM   6463 C  CD1 . TYR D  1 6   ? 15.146  7.442   -42.820 1.00 11.49 ? 6   TYR D CD1 1 
ATOM   6464 C  CD2 . TYR D  1 6   ? 13.965  8.447   -44.628 1.00 11.12 ? 6   TYR D CD2 1 
ATOM   6465 C  CE1 . TYR D  1 6   ? 14.005  7.481   -42.042 1.00 10.67 ? 6   TYR D CE1 1 
ATOM   6466 C  CE2 . TYR D  1 6   ? 12.817  8.490   -43.859 1.00 10.96 ? 6   TYR D CE2 1 
ATOM   6467 C  CZ  . TYR D  1 6   ? 12.843  8.007   -42.568 1.00 10.00 ? 6   TYR D CZ  1 
ATOM   6468 O  OH  . TYR D  1 6   ? 11.706  8.044   -41.790 1.00 11.20 ? 6   TYR D OH  1 
ATOM   6469 N  N   . PHE D  1 7   ? 19.288  9.526   -46.228 1.00 16.37 ? 7   PHE D N   1 
ATOM   6470 C  CA  . PHE D  1 7   ? 20.555  9.157   -46.896 1.00 20.81 ? 7   PHE D CA  1 
ATOM   6471 C  C   . PHE D  1 7   ? 21.291  10.435  -47.244 1.00 21.91 ? 7   PHE D C   1 
ATOM   6472 O  O   . PHE D  1 7   ? 20.641  11.352  -47.735 1.00 26.49 ? 7   PHE D O   1 
ATOM   6473 C  CB  . PHE D  1 7   ? 20.265  8.367   -48.188 1.00 29.75 ? 7   PHE D CB  1 
ATOM   6474 C  CG  . PHE D  1 7   ? 21.510  7.944   -48.919 1.00 36.20 ? 7   PHE D CG  1 
ATOM   6475 C  CD1 . PHE D  1 7   ? 22.272  6.845   -48.477 1.00 38.08 ? 7   PHE D CD1 1 
ATOM   6476 C  CD2 . PHE D  1 7   ? 21.959  8.685   -50.032 1.00 42.31 ? 7   PHE D CD2 1 
ATOM   6477 C  CE1 . PHE D  1 7   ? 23.442  6.457   -49.139 1.00 38.96 ? 7   PHE D CE1 1 
ATOM   6478 C  CE2 . PHE D  1 7   ? 23.130  8.306   -50.693 1.00 44.54 ? 7   PHE D CE2 1 
ATOM   6479 C  CZ  . PHE D  1 7   ? 23.860  7.192   -50.252 1.00 45.42 ? 7   PHE D CZ  1 
ATOM   6480 N  N   . GLY D  1 8   ? 22.611  10.433  -47.082 1.00 20.41 ? 8   GLY D N   1 
ATOM   6481 C  CA  . GLY D  1 8   ? 23.359  11.627  -47.581 1.00 19.78 ? 8   GLY D CA  1 
ATOM   6482 C  C   . GLY D  1 8   ? 23.557  12.664  -46.500 1.00 24.57 ? 8   GLY D C   1 
ATOM   6483 O  O   . GLY D  1 8   ? 23.265  12.458  -45.313 1.00 22.87 ? 8   GLY D O   1 
ATOM   6484 N  N   . PRO D  1 9   ? 24.027  13.845  -46.911 1.00 21.89 ? 9   PRO D N   1 
ATOM   6485 C  CA  . PRO D  1 9   ? 24.304  14.907  -45.989 1.00 23.60 ? 9   PRO D CA  1 
ATOM   6486 C  C   . PRO D  1 9   ? 23.199  15.282  -45.091 1.00 19.00 ? 9   PRO D C   1 
ATOM   6487 O  O   . PRO D  1 9   ? 23.490  15.817  -44.041 1.00 20.51 ? 9   PRO D O   1 
ATOM   6488 C  CB  . PRO D  1 9   ? 24.691  16.109  -46.900 1.00 23.33 ? 9   PRO D CB  1 
ATOM   6489 C  CG  . PRO D  1 9   ? 24.366  15.683  -48.265 1.00 25.58 ? 9   PRO D CG  1 
ATOM   6490 C  CD  . PRO D  1 9   ? 24.332  14.171  -48.323 1.00 23.62 ? 9   PRO D CD  1 
ATOM   6491 N  N   . ASP D  1 10  ? 21.903  15.121  -45.456 1.00 17.27 ? 10  ASP D N   1 
ATOM   6492 C  CA  . ASP D  1 10  ? 20.764  15.512  -44.649 1.00 17.84 ? 10  ASP D CA  1 
ATOM   6493 C  C   . ASP D  1 10  ? 20.056  14.293  -43.994 1.00 14.52 ? 10  ASP D C   1 
ATOM   6494 O  O   . ASP D  1 10  ? 18.964  14.445  -43.524 1.00 14.05 ? 10  ASP D O   1 
ATOM   6495 C  CB  . ASP D  1 10  ? 19.733  16.295  -45.468 1.00 18.16 ? 10  ASP D CB  1 
ATOM   6496 C  CG  . ASP D  1 10  ? 20.364  17.574  -46.093 1.00 23.99 ? 10  ASP D CG  1 
ATOM   6497 O  OD1 . ASP D  1 10  ? 21.049  18.346  -45.394 1.00 26.77 ? 10  ASP D OD1 1 
ATOM   6498 O  OD2 . ASP D  1 10  ? 20.255  17.711  -47.316 1.00 27.33 ? 10  ASP D OD2 1 
ATOM   6499 N  N   . GLY D  1 11  ? 20.810  13.218  -43.959 1.00 14.02 ? 11  GLY D N   1 
ATOM   6500 C  CA  . GLY D  1 11  ? 20.309  11.929  -43.343 1.00 11.49 ? 11  GLY D CA  1 
ATOM   6501 C  C   . GLY D  1 11  ? 20.396  12.001  -41.827 1.00 11.26 ? 11  GLY D C   1 
ATOM   6502 O  O   . GLY D  1 11  ? 20.535  13.043  -41.173 1.00 10.56 ? 11  GLY D O   1 
ATOM   6503 N  N   . GLU D  1 12  ? 20.120  10.876  -41.214 1.00 10.48 ? 12  GLU D N   1 
ATOM   6504 C  CA  . GLU D  1 12  ? 19.732  10.817  -39.835 1.00 10.08 ? 12  GLU D CA  1 
ATOM   6505 C  C   . GLU D  1 12  ? 20.783  11.276  -38.808 1.00 9.67  ? 12  GLU D C   1 
ATOM   6506 O  O   . GLU D  1 12  ? 20.363  11.775  -37.804 1.00 9.51  ? 12  GLU D O   1 
ATOM   6507 C  CB  . GLU D  1 12  ? 19.261  9.374   -39.448 1.00 9.98  ? 12  GLU D CB  1 
ATOM   6508 C  CG  . GLU D  1 12  ? 20.348  8.348   -39.255 1.00 9.29  ? 12  GLU D CG  1 
ATOM   6509 C  CD  . GLU D  1 12  ? 19.692  6.938   -39.314 1.00 10.23 ? 12  GLU D CD  1 
ATOM   6510 O  OE1 . GLU D  1 12  ? 19.332  6.487   -38.245 1.00 11.11 ? 12  GLU D OE1 1 
ATOM   6511 O  OE2 . GLU D  1 12  ? 19.584  6.415   -40.447 1.00 11.65 ? 12  GLU D OE2 1 
ATOM   6512 N  N   . ASN D  1 13  ? 22.065  11.163  -39.136 1.00 10.18 ? 13  ASN D N   1 
ATOM   6513 C  CA  . ASN D  1 13  ? 23.022  11.695  -38.179 1.00 9.96  ? 13  ASN D CA  1 
ATOM   6514 C  C   . ASN D  1 13  ? 23.048  13.210  -38.216 1.00 11.84 ? 13  ASN D C   1 
ATOM   6515 O  O   . ASN D  1 13  ? 23.687  13.737  -37.313 1.00 12.26 ? 13  ASN D O   1 
ATOM   6516 C  CB  . ASN D  1 13  ? 24.404  11.157  -38.553 1.00 9.91  ? 13  ASN D CB  1 
ATOM   6517 C  CG  . ASN D  1 13  ? 24.575  9.648   -38.239 1.00 9.56  ? 13  ASN D CG  1 
ATOM   6518 O  OD1 . ASN D  1 13  ? 23.657  9.015   -37.777 1.00 11.46 ? 13  ASN D OD1 1 
ATOM   6519 N  ND2 . ASN D  1 13  ? 25.747  9.149   -38.534 1.00 11.26 ? 13  ASN D ND2 1 
ATOM   6520 N  N   . SER D  1 14  ? 22.381  13.838  -39.178 1.00 11.25 ? 14  SER D N   1 
ATOM   6521 C  CA  . SER D  1 14  ? 22.341  15.311  -39.261 1.00 10.10 ? 14  SER D CA  1 
ATOM   6522 C  C   . SER D  1 14  ? 21.036  15.833  -38.827 1.00 10.36 ? 14  SER D C   1 
ATOM   6523 O  O   . SER D  1 14  ? 20.875  17.068  -38.731 1.00 11.63 ? 14  SER D O   1 
ATOM   6524 C  CB  . SER D  1 14  ? 22.663  15.754  -40.687 1.00 11.49 ? 14  SER D CB  1 
ATOM   6525 O  OG  . SER D  1 14  ? 24.004  15.413  -40.893 1.00 14.10 ? 14  SER D OG  1 
ATOM   6526 N  N   . TRP D  1 15  ? 20.020  15.030  -38.544 1.00 9.32  ? 15  TRP D N   1 
ATOM   6527 C  CA  . TRP D  1 15  ? 18.726  15.659  -38.185 1.00 10.01 ? 15  TRP D CA  1 
ATOM   6528 C  C   . TRP D  1 15  ? 18.759  16.584  -36.982 1.00 9.67  ? 15  TRP D C   1 
ATOM   6529 O  O   . TRP D  1 15  ? 18.008  17.563  -36.969 1.00 10.58 ? 15  TRP D O   1 
ATOM   6530 C  CB  . TRP D  1 15  ? 17.680  14.527  -37.819 1.00 10.11 ? 15  TRP D CB  1 
ATOM   6531 C  CG  . TRP D  1 15  ? 17.312  13.612  -38.964 1.00 9.84  ? 15  TRP D CG  1 
ATOM   6532 C  CD1 . TRP D  1 15  ? 17.551  13.789  -40.285 1.00 9.78  ? 15  TRP D CD1 1 
ATOM   6533 C  CD2 . TRP D  1 15  ? 16.539  12.380  -38.838 1.00 10.17 ? 15  TRP D CD2 1 
ATOM   6534 N  NE1 . TRP D  1 15  ? 16.982  12.725  -41.017 1.00 11.10 ? 15  TRP D NE1 1 
ATOM   6535 C  CE2 . TRP D  1 15  ? 16.361  11.866  -40.162 1.00 8.84  ? 15  TRP D CE2 1 
ATOM   6536 C  CE3 . TRP D  1 15  ? 15.976  11.700  -37.743 1.00 9.30  ? 15  TRP D CE3 1 
ATOM   6537 C  CZ2 . TRP D  1 15  ? 15.664  10.670  -40.413 1.00 10.39 ? 15  TRP D CZ2 1 
ATOM   6538 C  CZ3 . TRP D  1 15  ? 15.263  10.510  -38.003 1.00 9.91  ? 15  TRP D CZ3 1 
ATOM   6539 C  CH2 . TRP D  1 15  ? 15.114  10.036  -39.321 1.00 8.81  ? 15  TRP D CH2 1 
ATOM   6540 N  N   . SER D  1 16  ? 19.614  16.299  -36.027 1.00 10.67 ? 16  SER D N   1 
ATOM   6541 C  CA  . SER D  1 16  ? 19.634  17.101  -34.754 1.00 10.99 ? 16  SER D CA  1 
ATOM   6542 C  C   . SER D  1 16  ? 20.177  18.472  -35.079 1.00 12.74 ? 16  SER D C   1 
ATOM   6543 O  O   . SER D  1 16  ? 19.994  19.305  -34.226 1.00 13.59 ? 16  SER D O   1 
ATOM   6544 C  CB  . SER D  1 16  ? 20.609  16.466  -33.797 1.00 12.64 ? 16  SER D CB  1 
ATOM   6545 O  OG  . SER D  1 16  ? 21.890  16.460  -34.371 1.00 16.50 ? 16  SER D OG  1 
ATOM   6546 N  N   . LYS D  1 17  ? 20.737  18.736  -36.231 1.00 11.79 ? 17  LYS D N   1 
ATOM   6547 C  CA  . LYS D  1 17  ? 21.252  20.087  -36.503 1.00 12.35 ? 17  LYS D CA  1 
ATOM   6548 C  C   . LYS D  1 17  ? 20.077  20.991  -36.648 1.00 13.72 ? 17  LYS D C   1 
ATOM   6549 O  O   . LYS D  1 17  ? 20.186  22.255  -36.368 1.00 14.38 ? 17  LYS D O   1 
ATOM   6550 C  CB  . LYS D  1 17  ? 21.997  20.133  -37.809 1.00 12.29 ? 17  LYS D CB  1 
ATOM   6551 C  CG  . LYS D  1 17  ? 23.268  19.306  -37.825 1.00 12.79 ? 17  LYS D CG  1 
ATOM   6552 C  CD  . LYS D  1 17  ? 23.824  19.309  -39.270 1.00 12.01 ? 17  LYS D CD  1 
ATOM   6553 C  CE  . LYS D  1 17  ? 24.977  18.329  -39.410 1.00 10.66 ? 17  LYS D CE  1 
ATOM   6554 N  NZ  . LYS D  1 17  ? 25.707  18.534  -40.737 1.00 13.75 ? 17  LYS D NZ  1 
ATOM   6555 N  N   . LYS D  1 18  ? 18.939  20.555  -37.131 1.00 11.81 ? 18  LYS D N   1 
ATOM   6556 C  CA  . LYS D  1 18  ? 17.659  21.369  -37.262 1.00 12.17 ? 18  LYS D CA  1 
ATOM   6557 C  C   . LYS D  1 18  ? 16.565  21.032  -36.259 1.00 13.29 ? 18  LYS D C   1 
ATOM   6558 O  O   . LYS D  1 18  ? 15.636  21.762  -36.101 1.00 15.01 ? 18  LYS D O   1 
ATOM   6559 C  CB  . LYS D  1 18  ? 17.072  21.247  -38.672 1.00 15.50 ? 18  LYS D CB  1 
ATOM   6560 C  CG  . LYS D  1 18  ? 17.986  21.840  -39.783 1.00 21.10 ? 18  LYS D CG  1 
ATOM   6561 C  CD  . LYS D  1 18  ? 17.409  21.579  -41.163 1.00 21.99 ? 18  LYS D CD  1 
ATOM   6562 C  CE  . LYS D  1 18  ? 18.200  22.376  -42.229 1.00 27.25 ? 18  LYS D CE  1 
ATOM   6563 N  NZ  . LYS D  1 18  ? 17.743  21.879  -43.607 1.00 31.93 ? 18  LYS D NZ  1 
ATOM   6564 N  N   . TYR D  1 19  ? 16.600  19.811  -35.765 1.00 11.96 ? 19  TYR D N   1 
ATOM   6565 C  CA  . TYR D  1 19  ? 15.546  19.285  -34.943 1.00 12.71 ? 19  TYR D CA  1 
ATOM   6566 C  C   . TYR D  1 19  ? 16.125  18.796  -33.672 1.00 13.12 ? 19  TYR D C   1 
ATOM   6567 O  O   . TYR D  1 19  ? 16.558  17.623  -33.596 1.00 12.79 ? 19  TYR D O   1 
ATOM   6568 C  CB  . TYR D  1 19  ? 14.851  18.102  -35.723 1.00 12.30 ? 19  TYR D CB  1 
ATOM   6569 C  CG  . TYR D  1 19  ? 14.222  18.503  -37.007 1.00 11.26 ? 19  TYR D CG  1 
ATOM   6570 C  CD1 . TYR D  1 19  ? 13.037  19.204  -37.027 1.00 14.23 ? 19  TYR D CD1 1 
ATOM   6571 C  CD2 . TYR D  1 19  ? 14.897  18.286  -38.238 1.00 12.12 ? 19  TYR D CD2 1 
ATOM   6572 C  CE1 . TYR D  1 19  ? 12.482  19.600  -38.240 1.00 16.45 ? 19  TYR D CE1 1 
ATOM   6573 C  CE2 . TYR D  1 19  ? 14.333  18.669  -39.451 1.00 13.20 ? 19  TYR D CE2 1 
ATOM   6574 C  CZ  . TYR D  1 19  ? 13.139  19.331  -39.403 1.00 15.61 ? 19  TYR D CZ  1 
ATOM   6575 O  OH  . TYR D  1 19  ? 12.603  19.718  -40.644 1.00 20.16 ? 19  TYR D OH  1 
ATOM   6576 N  N   . PRO D  1 20  ? 16.275  19.660  -32.656 1.00 12.86 ? 20  PRO D N   1 
ATOM   6577 C  CA  . PRO D  1 20  ? 17.075  19.269  -31.503 1.00 12.26 ? 20  PRO D CA  1 
ATOM   6578 C  C   . PRO D  1 20  ? 16.558  18.001  -30.748 1.00 11.62 ? 20  PRO D C   1 
ATOM   6579 O  O   . PRO D  1 20  ? 17.436  17.326  -30.150 1.00 12.66 ? 20  PRO D O   1 
ATOM   6580 C  CB  . PRO D  1 20  ? 16.962  20.480  -30.516 1.00 13.79 ? 20  PRO D CB  1 
ATOM   6581 C  CG  . PRO D  1 20  ? 16.188  21.455  -31.276 1.00 15.66 ? 20  PRO D CG  1 
ATOM   6582 C  CD  . PRO D  1 20  ? 15.738  21.042  -32.626 1.00 12.68 ? 20  PRO D CD  1 
ATOM   6583 N  N   . SER D  1 21  ? 15.233  17.693  -30.798 1.00 13.34 ? 21  SER D N   1 
ATOM   6584 C  CA  . SER D  1 21  ? 14.810  16.497  -30.061 1.00 13.23 ? 21  SER D CA  1 
ATOM   6585 C  C   . SER D  1 21  ? 15.372  15.228  -30.714 1.00 11.79 ? 21  SER D C   1 
ATOM   6586 O  O   . SER D  1 21  ? 15.455  14.251  -30.007 1.00 12.39 ? 21  SER D O   1 
ATOM   6587 C  CB  . SER D  1 21  ? 13.315  16.363  -30.026 1.00 12.73 ? 21  SER D CB  1 
ATOM   6588 O  OG  . SER D  1 21  ? 12.729  17.488  -29.314 1.00 15.48 ? 21  SER D OG  1 
ATOM   6589 N  N   . CYS D  1 22  ? 15.811  15.235  -31.959 1.00 11.67 ? 22  CYS D N   1 
ATOM   6590 C  CA  . CYS D  1 22  ? 16.458  14.057  -32.559 1.00 11.63 ? 22  CYS D CA  1 
ATOM   6591 C  C   . CYS D  1 22  ? 17.748  13.746  -31.908 1.00 13.72 ? 22  CYS D C   1 
ATOM   6592 O  O   . CYS D  1 22  ? 18.244  12.642  -32.068 1.00 13.92 ? 22  CYS D O   1 
ATOM   6593 C  CB  . CYS D  1 22  ? 16.632  14.275  -34.067 1.00 13.28 ? 22  CYS D CB  1 
ATOM   6594 S  SG  . CYS D  1 22  ? 15.096  14.592  -34.974 1.00 12.38 ? 22  CYS D SG  1 
ATOM   6595 N  N   . GLY D  1 23  ? 18.368  14.696  -31.157 1.00 13.32 ? 23  GLY D N   1 
ATOM   6596 C  CA  . GLY D  1 23  ? 19.587  14.458  -30.351 1.00 14.42 ? 23  GLY D CA  1 
ATOM   6597 C  C   . GLY D  1 23  ? 19.326  14.345  -28.848 1.00 15.52 ? 23  GLY D C   1 
ATOM   6598 O  O   . GLY D  1 23  ? 20.298  14.332  -28.007 1.00 17.30 ? 23  GLY D O   1 
ATOM   6599 N  N   . GLY D  1 24  ? 18.067  14.311  -28.476 1.00 14.43 ? 24  GLY D N   1 
ATOM   6600 C  CA  . GLY D  1 24  ? 17.627  14.273  -27.052 1.00 17.54 ? 24  GLY D CA  1 
ATOM   6601 C  C   . GLY D  1 24  ? 17.434  12.847  -26.546 1.00 18.98 ? 24  GLY D C   1 
ATOM   6602 O  O   . GLY D  1 24  ? 17.815  11.858  -27.147 1.00 20.51 ? 24  GLY D O   1 
ATOM   6603 N  N   . LEU D  1 25  ? 16.814  12.756  -25.426 1.00 19.34 ? 25  LEU D N   1 
ATOM   6604 C  CA  . LEU D  1 25  ? 16.635  11.443  -24.803 1.00 20.19 ? 25  LEU D CA  1 
ATOM   6605 C  C   . LEU D  1 25  ? 15.407  10.751  -25.388 1.00 17.12 ? 25  LEU D C   1 
ATOM   6606 O  O   . LEU D  1 25  ? 14.555  11.373  -26.130 1.00 17.12 ? 25  LEU D O   1 
ATOM   6607 C  CB  . LEU D  1 25  ? 16.572  11.548  -23.256 1.00 24.39 ? 25  LEU D CB  1 
ATOM   6608 C  CG  . LEU D  1 25  ? 17.848  12.149  -22.575 1.00 23.92 ? 25  LEU D CG  1 
ATOM   6609 C  CD1 . LEU D  1 25  ? 17.521  12.418  -21.103 1.00 30.15 ? 25  LEU D CD1 1 
ATOM   6610 C  CD2 . LEU D  1 25  ? 19.068  11.229  -22.763 1.00 29.01 ? 25  LEU D CD2 1 
ATOM   6611 N  N   . LEU D  1 26  ? 15.313  9.441   -25.037 1.00 17.38 ? 26  LEU D N   1 
ATOM   6612 C  CA  . LEU D  1 26  ? 14.065  8.627   -25.255 1.00 16.71 ? 26  LEU D CA  1 
ATOM   6613 C  C   . LEU D  1 26  ? 13.728  8.482   -26.747 1.00 12.02 ? 26  LEU D C   1 
ATOM   6614 O  O   . LEU D  1 26  ? 12.529  8.500   -27.124 1.00 13.68 ? 26  LEU D O   1 
ATOM   6615 C  CB  . LEU D  1 26  ? 12.814  9.206   -24.590 1.00 20.41 ? 26  LEU D CB  1 
ATOM   6616 C  CG  . LEU D  1 26  ? 12.807  9.360   -23.028 1.00 28.93 ? 26  LEU D CG  1 
ATOM   6617 C  CD1 . LEU D  1 26  ? 11.392  9.644   -22.497 1.00 33.33 ? 26  LEU D CD1 1 
ATOM   6618 C  CD2 . LEU D  1 26  ? 13.533  8.213   -22.302 1.00 30.24 ? 26  LEU D CD2 1 
ATOM   6619 N  N   . GLN D  1 27  ? 14.779  8.350   -27.510 1.00 11.52 ? 27  GLN D N   1 
ATOM   6620 C  CA  . GLN D  1 27  ? 14.514  8.173   -29.001 1.00 10.63 ? 27  GLN D CA  1 
ATOM   6621 C  C   . GLN D  1 27  ? 14.088  6.755   -29.390 1.00 10.71 ? 27  GLN D C   1 
ATOM   6622 O  O   . GLN D  1 27  ? 14.520  5.754   -28.797 1.00 12.81 ? 27  GLN D O   1 
ATOM   6623 C  CB  . GLN D  1 27  ? 15.747  8.604   -29.804 1.00 10.88 ? 27  GLN D CB  1 
ATOM   6624 C  CG  . GLN D  1 27  ? 16.059  10.130  -29.581 1.00 11.88 ? 27  GLN D CG  1 
ATOM   6625 C  CD  . GLN D  1 27  ? 14.976  10.980  -30.177 1.00 10.91 ? 27  GLN D CD  1 
ATOM   6626 O  OE1 . GLN D  1 27  ? 14.968  11.126  -31.449 1.00 10.90 ? 27  GLN D OE1 1 
ATOM   6627 N  NE2 . GLN D  1 27  ? 14.066  11.540  -29.407 1.00 10.97 ? 27  GLN D NE2 1 
ATOM   6628 N  N   . SER D  1 28  ? 13.366  6.702   -30.466 1.00 9.58  ? 28  SER D N   1 
ATOM   6629 C  CA  . SER D  1 28  ? 12.925  5.441   -31.098 1.00 9.15  ? 28  SER D CA  1 
ATOM   6630 C  C   . SER D  1 28  ? 13.459  5.410   -32.518 1.00 10.87 ? 28  SER D C   1 
ATOM   6631 O  O   . SER D  1 28  ? 13.770  6.457   -33.096 1.00 10.43 ? 28  SER D O   1 
ATOM   6632 C  CB  . SER D  1 28  ? 11.418  5.463   -31.183 1.00 9.55  ? 28  SER D CB  1 
ATOM   6633 O  OG  . SER D  1 28  ? 10.895  5.384   -29.854 1.00 9.51  ? 28  SER D OG  1 
ATOM   6634 N  N   . PRO D  1 29  ? 13.593  4.246   -33.171 1.00 8.52  ? 29  PRO D N   1 
ATOM   6635 C  CA  . PRO D  1 29  ? 13.207  2.910   -32.629 1.00 9.00  ? 29  PRO D CA  1 
ATOM   6636 C  C   . PRO D  1 29  ? 14.362  2.351   -31.838 1.00 9.99  ? 29  PRO D C   1 
ATOM   6637 O  O   . PRO D  1 29  ? 15.395  2.953   -31.689 1.00 9.84  ? 29  PRO D O   1 
ATOM   6638 C  CB  . PRO D  1 29  ? 12.994  2.135   -34.005 1.00 9.60  ? 29  PRO D CB  1 
ATOM   6639 C  CG  . PRO D  1 29  ? 14.102  2.682   -34.863 1.00 8.60  ? 29  PRO D CG  1 
ATOM   6640 C  CD  . PRO D  1 29  ? 14.123  4.157   -34.572 1.00 9.46  ? 29  PRO D CD  1 
ATOM   6641 N  N   . ILE D  1 30  ? 14.126  1.158   -31.321 1.00 9.17  ? 30  ILE D N   1 
ATOM   6642 C  CA  . ILE D  1 30  ? 15.081  0.422   -30.497 1.00 10.15 ? 30  ILE D CA  1 
ATOM   6643 C  C   . ILE D  1 30  ? 15.074  -1.029  -30.921 1.00 9.38  ? 30  ILE D C   1 
ATOM   6644 O  O   . ILE D  1 30  ? 14.176  -1.552  -31.623 1.00 9.87  ? 30  ILE D O   1 
ATOM   6645 C  CB  . ILE D  1 30  ? 14.762  0.546   -28.984 1.00 10.75 ? 30  ILE D CB  1 
ATOM   6646 C  CG1 . ILE D  1 30  ? 13.329  -0.020  -28.732 1.00 10.78 ? 30  ILE D CG1 1 
ATOM   6647 C  CG2 . ILE D  1 30  ? 14.959  2.047   -28.519 1.00 11.31 ? 30  ILE D CG2 1 
ATOM   6648 C  CD1 . ILE D  1 30  ? 13.059  -0.122  -27.244 1.00 13.81 ? 30  ILE D CD1 1 
ATOM   6649 N  N   . ASP D  1 31  ? 16.158  -1.706  -30.479 1.00 10.12 ? 31  ASP D N   1 
ATOM   6650 C  CA  . ASP D  1 31  ? 16.275  -3.182  -30.596 1.00 11.03 ? 31  ASP D CA  1 
ATOM   6651 C  C   . ASP D  1 31  ? 15.642  -3.870  -29.422 1.00 12.25 ? 31  ASP D C   1 
ATOM   6652 O  O   . ASP D  1 31  ? 16.049  -3.631  -28.297 1.00 14.51 ? 31  ASP D O   1 
ATOM   6653 C  CB  . ASP D  1 31  ? 17.700  -3.564  -30.703 1.00 13.05 ? 31  ASP D CB  1 
ATOM   6654 C  CG  . ASP D  1 31  ? 17.843  -5.085  -30.810 1.00 14.73 ? 31  ASP D CG  1 
ATOM   6655 O  OD1 . ASP D  1 31  ? 17.289  -5.714  -31.736 1.00 13.32 ? 31  ASP D OD1 1 
ATOM   6656 O  OD2 . ASP D  1 31  ? 18.488  -5.721  -29.947 1.00 16.83 ? 31  ASP D OD2 1 
ATOM   6657 N  N   . LEU D  1 32  ? 14.704  -4.728  -29.656 1.00 11.20 ? 32  LEU D N   1 
ATOM   6658 C  CA  . LEU D  1 32  ? 14.005  -5.499  -28.613 1.00 11.70 ? 32  LEU D CA  1 
ATOM   6659 C  C   . LEU D  1 32  ? 14.760  -6.800  -28.327 1.00 13.58 ? 32  LEU D C   1 
ATOM   6660 O  O   . LEU D  1 32  ? 14.755  -7.676  -29.179 1.00 13.70 ? 32  LEU D O   1 
ATOM   6661 C  CB  . LEU D  1 32  ? 12.588  -5.766  -29.129 1.00 13.75 ? 32  LEU D CB  1 
ATOM   6662 C  CG  . LEU D  1 32  ? 11.832  -4.504  -29.505 1.00 14.00 ? 32  LEU D CG  1 
ATOM   6663 C  CD1 . LEU D  1 32  ? 10.484  -4.867  -30.185 1.00 13.77 ? 32  LEU D CD1 1 
ATOM   6664 C  CD2 . LEU D  1 32  ? 11.598  -3.597  -28.260 1.00 16.19 ? 32  LEU D CD2 1 
ATOM   6665 N  N   . HIS D  1 33  ? 15.477  -6.864  -27.212 1.00 12.69 ? 33  HIS D N   1 
ATOM   6666 C  CA  . HIS D  1 33  ? 16.301  -8.077  -26.940 1.00 12.22 ? 33  HIS D CA  1 
ATOM   6667 C  C   . HIS D  1 33  ? 16.185  -8.379  -25.490 1.00 13.85 ? 33  HIS D C   1 
ATOM   6668 O  O   . HIS D  1 33  ? 15.879  -7.512  -24.654 1.00 13.99 ? 33  HIS D O   1 
ATOM   6669 C  CB  . HIS D  1 33  ? 17.782  -7.911  -27.417 1.00 14.28 ? 33  HIS D CB  1 
ATOM   6670 C  CG  . HIS D  1 33  ? 18.516  -6.791  -26.712 1.00 15.06 ? 33  HIS D CG  1 
ATOM   6671 N  ND1 . HIS D  1 33  ? 18.371  -5.543  -27.086 1.00 17.51 ? 33  HIS D ND1 1 
ATOM   6672 C  CD2 . HIS D  1 33  ? 19.390  -6.739  -25.584 1.00 15.42 ? 33  HIS D CD2 1 
ATOM   6673 C  CE1 . HIS D  1 33  ? 19.129  -4.713  -26.315 1.00 22.10 ? 33  HIS D CE1 1 
ATOM   6674 N  NE2 . HIS D  1 33  ? 19.739  -5.459  -25.403 1.00 18.02 ? 33  HIS D NE2 1 
ATOM   6675 N  N   . SER D  1 34  ? 16.474  -9.652  -25.160 1.00 14.18 ? 34  SER D N   1 
ATOM   6676 C  CA  . SER D  1 34  ? 16.129  -10.196 -23.819 1.00 15.92 ? 34  SER D CA  1 
ATOM   6677 C  C   . SER D  1 34  ? 16.627  -9.382  -22.647 1.00 16.15 ? 34  SER D C   1 
ATOM   6678 O  O   . SER D  1 34  ? 15.877  -9.218  -21.681 1.00 15.33 ? 34  SER D O   1 
ATOM   6679 C  CB  . SER D  1 34  ? 16.632  -11.647 -23.759 1.00 18.46 ? 34  SER D CB  1 
ATOM   6680 O  OG  . SER D  1 34  ? 18.021  -11.665 -23.774 1.00 24.17 ? 34  SER D OG  1 
ATOM   6681 N  N   . ASP D  1 35  ? 17.841  -8.861  -22.676 1.00 14.86 ? 35  ASP D N   1 
ATOM   6682 C  CA  . ASP D  1 35  ? 18.394  -8.195  -21.498 1.00 16.80 ? 35  ASP D CA  1 
ATOM   6683 C  C   . ASP D  1 35  ? 17.621  -7.023  -21.016 1.00 15.80 ? 35  ASP D C   1 
ATOM   6684 O  O   . ASP D  1 35  ? 17.702  -6.630  -19.855 1.00 17.89 ? 35  ASP D O   1 
ATOM   6685 C  CB  . ASP D  1 35  ? 19.825  -7.699  -21.756 1.00 19.95 ? 35  ASP D CB  1 
ATOM   6686 C  CG  . ASP D  1 35  ? 20.706  -8.724  -22.426 1.00 22.55 ? 35  ASP D CG  1 
ATOM   6687 O  OD1 . ASP D  1 35  ? 21.716  -9.116  -21.812 1.00 21.13 ? 35  ASP D OD1 1 
ATOM   6688 O  OD2 . ASP D  1 35  ? 20.433  -9.097  -23.586 1.00 22.22 ? 35  ASP D OD2 1 
ATOM   6689 N  N   . ILE D  1 36  ? 16.854  -6.372  -21.935 1.00 14.81 ? 36  ILE D N   1 
ATOM   6690 C  CA  . ILE D  1 36  ? 16.124  -5.199  -21.579 1.00 13.77 ? 36  ILE D CA  1 
ATOM   6691 C  C   . ILE D  1 36  ? 14.632  -5.405  -21.518 1.00 14.66 ? 36  ILE D C   1 
ATOM   6692 O  O   . ILE D  1 36  ? 13.877  -4.382  -21.345 1.00 16.44 ? 36  ILE D O   1 
ATOM   6693 C  CB  . ILE D  1 36  ? 16.544  -3.926  -22.418 1.00 17.30 ? 36  ILE D CB  1 
ATOM   6694 C  CG1 . ILE D  1 36  ? 16.413  -4.157  -23.946 1.00 20.56 ? 36  ILE D CG1 1 
ATOM   6695 C  CG2 . ILE D  1 36  ? 17.985  -3.537  -22.056 1.00 20.39 ? 36  ILE D CG2 1 
ATOM   6696 C  CD1 . ILE D  1 36  ? 15.033  -4.456  -24.416 1.00 18.89 ? 36  ILE D CD1 1 
ATOM   6697 N  N   . LEU D  1 37  ? 14.146  -6.660  -21.578 1.00 13.78 ? 37  LEU D N   1 
ATOM   6698 C  CA  . LEU D  1 37  ? 12.722  -6.958  -21.526 1.00 14.01 ? 37  LEU D CA  1 
ATOM   6699 C  C   . LEU D  1 37  ? 12.299  -7.288  -20.088 1.00 16.55 ? 37  LEU D C   1 
ATOM   6700 O  O   . LEU D  1 37  ? 13.056  -8.013  -19.378 1.00 18.02 ? 37  LEU D O   1 
ATOM   6701 C  CB  . LEU D  1 37  ? 12.357  -8.139  -22.385 1.00 15.01 ? 37  LEU D CB  1 
ATOM   6702 C  CG  . LEU D  1 37  ? 12.658  -7.917  -23.891 1.00 16.66 ? 37  LEU D CG  1 
ATOM   6703 C  CD1 . LEU D  1 37  ? 12.256  -9.177  -24.632 1.00 18.79 ? 37  LEU D CD1 1 
ATOM   6704 C  CD2 . LEU D  1 37  ? 11.920  -6.736  -24.483 1.00 14.85 ? 37  LEU D CD2 1 
ATOM   6705 N  N   . GLN D  1 38  ? 11.134  -6.816  -19.681 1.00 13.55 ? 38  GLN D N   1 
ATOM   6706 C  CA  . GLN D  1 38  ? 10.647  -7.182  -18.325 1.00 15.36 ? 38  GLN D CA  1 
ATOM   6707 C  C   . GLN D  1 38  ? 9.180   -7.315  -18.411 1.00 13.05 ? 38  GLN D C   1 
ATOM   6708 O  O   . GLN D  1 38  ? 8.451   -6.408  -18.880 1.00 13.03 ? 38  GLN D O   1 
ATOM   6709 C  CB  . GLN D  1 38  ? 10.985  -6.066  -17.416 1.00 19.01 ? 38  GLN D CB  1 
ATOM   6710 C  CG  . GLN D  1 38  ? 10.531  -6.433  -16.036 1.00 21.97 ? 38  GLN D CG  1 
ATOM   6711 C  CD  . GLN D  1 38  ? 11.177  -5.585  -15.036 1.00 29.38 ? 38  GLN D CD  1 
ATOM   6712 O  OE1 . GLN D  1 38  ? 12.382  -5.718  -14.821 1.00 31.70 ? 38  GLN D OE1 1 
ATOM   6713 N  NE2 . GLN D  1 38  ? 10.446  -4.617  -14.508 1.00 30.07 ? 38  GLN D NE2 1 
ATOM   6714 N  N   . TYR D  1 39  ? 8.633   -8.453  -17.961 1.00 14.67 ? 39  TYR D N   1 
ATOM   6715 C  CA  . TYR D  1 39  ? 7.207   -8.740  -17.967 1.00 13.86 ? 39  TYR D CA  1 
ATOM   6716 C  C   . TYR D  1 39  ? 6.511   -7.760  -16.973 1.00 13.61 ? 39  TYR D C   1 
ATOM   6717 O  O   . TYR D  1 39  ? 7.067   -7.548  -15.884 1.00 14.71 ? 39  TYR D O   1 
ATOM   6718 C  CB  . TYR D  1 39  ? 6.981   -10.181 -17.449 1.00 14.76 ? 39  TYR D CB  1 
ATOM   6719 C  CG  . TYR D  1 39  ? 5.509   -10.451 -17.194 1.00 15.36 ? 39  TYR D CG  1 
ATOM   6720 C  CD1 . TYR D  1 39  ? 4.595   -10.468 -18.243 1.00 16.35 ? 39  TYR D CD1 1 
ATOM   6721 C  CD2 . TYR D  1 39  ? 5.027   -10.650 -15.907 1.00 15.74 ? 39  TYR D CD2 1 
ATOM   6722 C  CE1 . TYR D  1 39  ? 3.250   -10.698 -18.019 1.00 15.47 ? 39  TYR D CE1 1 
ATOM   6723 C  CE2 . TYR D  1 39  ? 3.682   -10.880 -15.674 1.00 15.30 ? 39  TYR D CE2 1 
ATOM   6724 C  CZ  . TYR D  1 39  ? 2.798   -10.903 -16.734 1.00 16.10 ? 39  TYR D CZ  1 
ATOM   6725 O  OH  . TYR D  1 39  ? 1.459   -11.131 -16.510 1.00 20.41 ? 39  TYR D OH  1 
ATOM   6726 N  N   . ASP D  1 40  ? 5.336   -7.198  -17.371 1.00 13.13 ? 40  ASP D N   1 
ATOM   6727 C  CA  . ASP D  1 40  ? 4.599   -6.261  -16.484 1.00 14.19 ? 40  ASP D CA  1 
ATOM   6728 C  C   . ASP D  1 40  ? 3.190   -6.708  -16.613 1.00 15.09 ? 40  ASP D C   1 
ATOM   6729 O  O   . ASP D  1 40  ? 2.509   -6.636  -17.669 1.00 13.77 ? 40  ASP D O   1 
ATOM   6730 C  CB  . ASP D  1 40  ? 4.833   -4.852  -17.044 1.00 15.75 ? 40  ASP D CB  1 
ATOM   6731 C  CG  . ASP D  1 40  ? 4.099   -3.778  -16.259 1.00 22.08 ? 40  ASP D CG  1 
ATOM   6732 O  OD1 . ASP D  1 40  ? 3.324   -4.095  -15.347 1.00 18.07 ? 40  ASP D OD1 1 
ATOM   6733 O  OD2 . ASP D  1 40  ? 4.280   -2.588  -16.633 1.00 25.32 ? 40  ASP D OD2 1 
ATOM   6734 N  N   . ALA D  1 41  ? 2.666   -7.181  -15.444 1.00 12.05 ? 41  ALA D N   1 
ATOM   6735 C  CA  . ALA D  1 41  ? 1.277   -7.617  -15.367 1.00 15.20 ? 41  ALA D CA  1 
ATOM   6736 C  C   . ALA D  1 41  ? 0.212   -6.470  -15.538 1.00 14.02 ? 41  ALA D C   1 
ATOM   6737 O  O   . ALA D  1 41  ? -0.933  -6.732  -15.829 1.00 15.91 ? 41  ALA D O   1 
ATOM   6738 C  CB  . ALA D  1 41  ? 1.030   -8.343  -14.037 1.00 16.25 ? 41  ALA D CB  1 
ATOM   6739 N  N   . SER D  1 42  ? 0.695   -5.239  -15.516 1.00 15.72 ? 42  SER D N   1 
ATOM   6740 C  CA  . SER D  1 42  ? -0.217  -4.095  -15.690 1.00 18.24 ? 42  SER D CA  1 
ATOM   6741 C  C   . SER D  1 42  ? -0.558  -3.926  -17.161 1.00 20.49 ? 42  SER D C   1 
ATOM   6742 O  O   . SER D  1 42  ? -1.450  -3.082  -17.500 1.00 19.99 ? 42  SER D O   1 
ATOM   6743 C  CB  . SER D  1 42  ? 0.357   -2.806  -15.070 1.00 21.95 ? 42  SER D CB  1 
ATOM   6744 O  OG  . SER D  1 42  ? 1.298   -2.242  -15.976 1.00 25.34 ? 42  SER D OG  1 
ATOM   6745 N  N   . LEU D  1 43  ? 0.162   -4.643  -18.060 1.00 15.99 ? 43  LEU D N   1 
ATOM   6746 C  CA  . LEU D  1 43  ? -0.090  -4.487  -19.508 1.00 17.84 ? 43  LEU D CA  1 
ATOM   6747 C  C   . LEU D  1 43  ? -1.222  -5.346  -20.002 1.00 15.46 ? 43  LEU D C   1 
ATOM   6748 O  O   . LEU D  1 43  ? -1.088  -6.452  -20.528 1.00 17.39 ? 43  LEU D O   1 
ATOM   6749 C  CB  . LEU D  1 43  ? 1.193   -4.765  -20.287 1.00 16.45 ? 43  LEU D CB  1 
ATOM   6750 C  CG  . LEU D  1 43  ? 2.280   -3.789  -19.998 1.00 17.67 ? 43  LEU D CG  1 
ATOM   6751 C  CD1 . LEU D  1 43  ? 3.470   -4.250  -20.806 1.00 15.38 ? 43  LEU D CD1 1 
ATOM   6752 C  CD2 . LEU D  1 43  ? 2.008   -2.309  -20.317 1.00 20.19 ? 43  LEU D CD2 1 
ATOM   6753 N  N   . THR D  1 44  ? -2.457  -4.788  -19.879 1.00 16.85 ? 44  THR D N   1 
ATOM   6754 C  CA  . THR D  1 44  ? -3.648  -5.505  -20.221 1.00 17.30 ? 44  THR D CA  1 
ATOM   6755 C  C   . THR D  1 44  ? -3.996  -5.271  -21.702 1.00 16.41 ? 44  THR D C   1 
ATOM   6756 O  O   . THR D  1 44  ? -3.377  -4.385  -22.330 1.00 15.63 ? 44  THR D O   1 
ATOM   6757 C  CB  . THR D  1 44  ? -4.800  -4.921  -19.324 1.00 16.71 ? 44  THR D CB  1 
ATOM   6758 O  OG1 . THR D  1 44  ? -4.767  -3.497  -19.405 1.00 21.05 ? 44  THR D OG1 1 
ATOM   6759 C  CG2 . THR D  1 44  ? -4.467  -5.287  -17.852 1.00 22.82 ? 44  THR D CG2 1 
ATOM   6760 N  N   . PRO D  1 45  ? -4.958  -5.996  -22.248 1.00 18.07 ? 45  PRO D N   1 
ATOM   6761 C  CA  . PRO D  1 45  ? -5.161  -5.964  -23.719 1.00 19.58 ? 45  PRO D CA  1 
ATOM   6762 C  C   . PRO D  1 45  ? -5.755  -4.644  -24.177 1.00 21.35 ? 45  PRO D C   1 
ATOM   6763 O  O   . PRO D  1 45  ? -6.598  -4.060  -23.507 1.00 23.48 ? 45  PRO D O   1 
ATOM   6764 C  CB  . PRO D  1 45  ? -6.123  -7.091  -23.964 1.00 21.92 ? 45  PRO D CB  1 
ATOM   6765 C  CG  . PRO D  1 45  ? -5.890  -8.047  -22.803 1.00 19.39 ? 45  PRO D CG  1 
ATOM   6766 C  CD  . PRO D  1 45  ? -5.567  -7.188  -21.621 1.00 19.57 ? 45  PRO D CD  1 
ATOM   6767 N  N   . LEU D  1 46  ? -5.214  -4.120  -25.284 1.00 19.57 ? 46  LEU D N   1 
ATOM   6768 C  CA  . LEU D  1 46  ? -5.849  -2.954  -25.865 1.00 18.57 ? 46  LEU D CA  1 
ATOM   6769 C  C   . LEU D  1 46  ? -7.083  -3.337  -26.570 1.00 17.12 ? 46  LEU D C   1 
ATOM   6770 O  O   . LEU D  1 46  ? -7.270  -4.444  -27.098 1.00 17.59 ? 46  LEU D O   1 
ATOM   6771 C  CB  . LEU D  1 46  ? -4.920  -2.358  -26.920 1.00 21.41 ? 46  LEU D CB  1 
ATOM   6772 C  CG  . LEU D  1 46  ? -3.664  -1.756  -26.344 1.00 20.84 ? 46  LEU D CG  1 
ATOM   6773 C  CD1 . LEU D  1 46  ? -2.819  -1.301  -27.537 1.00 21.98 ? 46  LEU D CD1 1 
ATOM   6774 C  CD2 . LEU D  1 46  ? -3.970  -0.624  -25.371 1.00 23.39 ? 46  LEU D CD2 1 
ATOM   6775 N  N   . GLU D  1 47  ? -8.011  -2.351  -26.608 1.00 19.69 ? 47  GLU D N   1 
ATOM   6776 C  CA  . GLU D  1 47  ? -9.180  -2.495  -27.444 1.00 21.28 ? 47  GLU D CA  1 
ATOM   6777 C  C   . GLU D  1 47  ? -9.233  -1.496  -28.669 1.00 16.74 ? 47  GLU D C   1 
ATOM   6778 O  O   . GLU D  1 47  ? -8.858  -0.283  -28.533 1.00 19.89 ? 47  GLU D O   1 
ATOM   6779 C  CB  . GLU D  1 47  ? -10.545 -2.553  -26.686 1.00 27.61 ? 47  GLU D CB  1 
ATOM   6780 C  CG  . GLU D  1 47  ? -10.877 -4.010  -26.232 1.00 33.17 ? 47  GLU D CG  1 
ATOM   6781 C  CD  . GLU D  1 47  ? -12.011 -4.168  -25.200 1.00 43.95 ? 47  GLU D CD  1 
ATOM   6782 O  OE1 . GLU D  1 47  ? -12.622 -3.162  -24.754 1.00 47.19 ? 47  GLU D OE1 1 
ATOM   6783 O  OE2 . GLU D  1 47  ? -12.298 -5.340  -24.821 1.00 52.67 ? 47  GLU D OE2 1 
ATOM   6784 N  N   . PHE D  1 48  ? -9.566  -2.069  -29.794 1.00 18.85 ? 48  PHE D N   1 
ATOM   6785 C  CA  . PHE D  1 48  ? -9.534  -1.313  -31.081 1.00 18.46 ? 48  PHE D CA  1 
ATOM   6786 C  C   . PHE D  1 48  ? -10.946 -0.953  -31.473 1.00 22.22 ? 48  PHE D C   1 
ATOM   6787 O  O   . PHE D  1 48  ? -11.640 -1.802  -31.978 1.00 25.86 ? 48  PHE D O   1 
ATOM   6788 C  CB  . PHE D  1 48  ? -8.815  -2.137  -32.185 1.00 18.91 ? 48  PHE D CB  1 
ATOM   6789 C  CG  . PHE D  1 48  ? -7.466  -2.636  -31.707 1.00 17.53 ? 48  PHE D CG  1 
ATOM   6790 C  CD1 . PHE D  1 48  ? -6.427  -1.781  -31.455 1.00 15.10 ? 48  PHE D CD1 1 
ATOM   6791 C  CD2 . PHE D  1 48  ? -7.312  -4.030  -31.395 1.00 18.78 ? 48  PHE D CD2 1 
ATOM   6792 C  CE1 . PHE D  1 48  ? -5.233  -2.217  -30.904 1.00 16.77 ? 48  PHE D CE1 1 
ATOM   6793 C  CE2 . PHE D  1 48  ? -6.097  -4.496  -30.878 1.00 18.49 ? 48  PHE D CE2 1 
ATOM   6794 C  CZ  . PHE D  1 48  ? -5.065  -3.595  -30.642 1.00 16.44 ? 48  PHE D CZ  1 
ATOM   6795 N  N   . GLN D  1 49  ? -11.284 0.338   -31.369 1.00 18.06 ? 49  GLN D N   1 
ATOM   6796 C  CA  . GLN D  1 49  ? -12.680 0.800   -31.536 1.00 21.76 ? 49  GLN D CA  1 
ATOM   6797 C  C   . GLN D  1 49  ? -12.780 1.647   -32.802 1.00 18.09 ? 49  GLN D C   1 
ATOM   6798 O  O   . GLN D  1 49  ? -11.956 2.568   -33.005 1.00 17.95 ? 49  GLN D O   1 
ATOM   6799 C  CB  . GLN D  1 49  ? -13.087 1.664   -30.380 1.00 23.03 ? 49  GLN D CB  1 
ATOM   6800 C  CG  . GLN D  1 49  ? -13.138 0.952   -29.027 1.00 28.25 ? 49  GLN D CG  1 
ATOM   6801 C  CD  . GLN D  1 49  ? -13.944 -0.364  -29.054 1.00 36.32 ? 49  GLN D CD  1 
ATOM   6802 O  OE1 . GLN D  1 49  ? -13.397 -1.475  -29.006 1.00 40.21 ? 49  GLN D OE1 1 
ATOM   6803 N  NE2 . GLN D  1 49  ? -15.250 -0.238  -29.150 1.00 40.01 ? 49  GLN D NE2 1 
ATOM   6804 N  N   . GLY D  1 50  ? -13.803 1.386   -33.580 1.00 19.34 ? 50  GLY D N   1 
ATOM   6805 C  CA  . GLY D  1 50  ? -14.038 2.145   -34.787 1.00 18.58 ? 50  GLY D CA  1 
ATOM   6806 C  C   . GLY D  1 50  ? -12.930 1.913   -35.823 1.00 16.06 ? 50  GLY D C   1 
ATOM   6807 O  O   . GLY D  1 50  ? -12.821 2.719   -36.743 1.00 16.96 ? 50  GLY D O   1 
ATOM   6808 N  N   . TYR D  1 51  ? -12.257 0.751   -35.736 1.00 15.86 ? 51  TYR D N   1 
ATOM   6809 C  CA  . TYR D  1 51  ? -11.276 0.372   -36.800 1.00 13.24 ? 51  TYR D CA  1 
ATOM   6810 C  C   . TYR D  1 51  ? -11.883 -0.105  -38.085 1.00 13.72 ? 51  TYR D C   1 
ATOM   6811 O  O   . TYR D  1 51  ? -11.292 -0.157  -39.161 1.00 14.38 ? 51  TYR D O   1 
ATOM   6812 C  CB  . TYR D  1 51  ? -10.267 -0.721  -36.279 1.00 13.81 ? 51  TYR D CB  1 
ATOM   6813 C  CG  . TYR D  1 51  ? -9.084  -0.093  -35.533 1.00 12.62 ? 51  TYR D CG  1 
ATOM   6814 C  CD1 . TYR D  1 51  ? -9.225  0.871   -34.552 1.00 14.32 ? 51  TYR D CD1 1 
ATOM   6815 C  CD2 . TYR D  1 51  ? -7.766  -0.619  -35.750 1.00 13.80 ? 51  TYR D CD2 1 
ATOM   6816 C  CE1 . TYR D  1 51  ? -8.174  1.385   -33.860 1.00 13.79 ? 51  TYR D CE1 1 
ATOM   6817 C  CE2 . TYR D  1 51  ? -6.693  -0.072  -35.077 1.00 11.61 ? 51  TYR D CE2 1 
ATOM   6818 C  CZ  . TYR D  1 51  ? -6.835  0.915   -34.135 1.00 13.21 ? 51  TYR D CZ  1 
ATOM   6819 O  OH  . TYR D  1 51  ? -5.682  1.343   -33.627 1.00 14.24 ? 51  TYR D OH  1 
ATOM   6820 N  N   . ASN D  1 52  ? -13.125 -0.550  -37.971 1.00 15.88 ? 52  ASN D N   1 
ATOM   6821 C  CA  . ASN D  1 52  ? -13.822 -1.065  -39.135 1.00 16.29 ? 52  ASN D CA  1 
ATOM   6822 C  C   . ASN D  1 52  ? -14.372 0.092   -39.945 1.00 19.13 ? 52  ASN D C   1 
ATOM   6823 O  O   . ASN D  1 52  ? -15.489 0.546   -39.695 1.00 19.37 ? 52  ASN D O   1 
ATOM   6824 C  CB  . ASN D  1 52  ? -14.954 -2.003  -38.714 1.00 19.17 ? 52  ASN D CB  1 
ATOM   6825 C  CG  . ASN D  1 52  ? -15.499 -2.815  -39.873 1.00 22.23 ? 52  ASN D CG  1 
ATOM   6826 O  OD1 . ASN D  1 52  ? -15.160 -2.571  -41.031 1.00 23.93 ? 52  ASN D OD1 1 
ATOM   6827 N  ND2 . ASN D  1 52  ? -16.348 -3.789  -39.565 1.00 27.56 ? 52  ASN D ND2 1 
ATOM   6828 N  N   . LEU D  1 53  ? -13.613 0.576   -40.901 1.00 16.23 ? 53  LEU D N   1 
ATOM   6829 C  CA  . LEU D  1 53  ? -14.059 1.745   -41.724 1.00 16.09 ? 53  LEU D CA  1 
ATOM   6830 C  C   . LEU D  1 53  ? -14.999 1.336   -42.826 1.00 19.01 ? 53  LEU D C   1 
ATOM   6831 O  O   . LEU D  1 53  ? -14.778 0.318   -43.499 1.00 18.49 ? 53  LEU D O   1 
ATOM   6832 C  CB  . LEU D  1 53  ? -12.806 2.452   -42.326 1.00 15.97 ? 53  LEU D CB  1 
ATOM   6833 C  CG  . LEU D  1 53  ? -11.738 2.859   -41.285 1.00 15.84 ? 53  LEU D CG  1 
ATOM   6834 C  CD1 . LEU D  1 53  ? -10.595 3.608   -41.992 1.00 16.83 ? 53  LEU D CD1 1 
ATOM   6835 C  CD2 . LEU D  1 53  ? -12.282 3.649   -40.126 1.00 16.68 ? 53  LEU D CD2 1 
ATOM   6836 N  N   . SER D  1 54  ? -16.015 2.154   -43.055 1.00 15.37 ? 54  SER D N   1 
ATOM   6837 C  CA  . SER D  1 54  ? -16.977 1.820   -44.065 1.00 17.83 ? 54  SER D CA  1 
ATOM   6838 C  C   . SER D  1 54  ? -16.369 1.788   -45.477 1.00 17.24 ? 54  SER D C   1 
ATOM   6839 O  O   . SER D  1 54  ? -15.754 2.767   -45.902 1.00 16.68 ? 54  SER D O   1 
ATOM   6840 C  CB  . SER D  1 54  ? -18.138 2.838   -44.043 1.00 20.36 ? 54  SER D CB  1 
ATOM   6841 O  OG  . SER D  1 54  ? -19.070 2.458   -45.073 1.00 22.50 ? 54  SER D OG  1 
ATOM   6842 N  N   . ALA D  1 55  ? -16.655 0.744   -46.226 1.00 19.28 ? 55  ALA D N   1 
ATOM   6843 C  CA  . ALA D  1 55  ? -16.281 0.671   -47.660 1.00 20.81 ? 55  ALA D CA  1 
ATOM   6844 C  C   . ALA D  1 55  ? -16.967 1.700   -48.511 1.00 19.65 ? 55  ALA D C   1 
ATOM   6845 O  O   . ALA D  1 55  ? -16.574 1.911   -49.665 1.00 22.35 ? 55  ALA D O   1 
ATOM   6846 C  CB  . ALA D  1 55  ? -16.498 -0.751  -48.255 1.00 24.45 ? 55  ALA D CB  1 
ATOM   6847 N  N   . ASN D  1 56  ? -17.980 2.417   -47.997 1.00 20.31 ? 56  ASN D N   1 
ATOM   6848 C  CA  . ASN D  1 56  ? -18.615 3.525   -48.757 1.00 20.03 ? 56  ASN D CA  1 
ATOM   6849 C  C   . ASN D  1 56  ? -18.112 4.893   -48.423 1.00 20.78 ? 56  ASN D C   1 
ATOM   6850 O  O   . ASN D  1 56  ? -18.604 5.891   -48.972 1.00 23.07 ? 56  ASN D O   1 
ATOM   6851 C  CB  . ASN D  1 56  ? -20.185 3.568   -48.573 1.00 23.54 ? 56  ASN D CB  1 
ATOM   6852 C  CG  . ASN D  1 56  ? -20.858 2.347   -49.140 1.00 35.11 ? 56  ASN D CG  1 
ATOM   6853 O  OD1 . ASN D  1 56  ? -20.593 1.939   -50.287 1.00 37.84 ? 56  ASN D OD1 1 
ATOM   6854 N  ND2 . ASN D  1 56  ? -21.715 1.721   -48.322 1.00 34.67 ? 56  ASN D ND2 1 
ATOM   6855 N  N   . LYS D  1 57  ? -17.152 4.936   -47.490 1.00 18.04 ? 57  LYS D N   1 
ATOM   6856 C  CA  . LYS D  1 57  ? -16.434 6.161   -47.179 1.00 17.71 ? 57  LYS D CA  1 
ATOM   6857 C  C   . LYS D  1 57  ? -15.039 6.067   -47.774 1.00 16.99 ? 57  LYS D C   1 
ATOM   6858 O  O   . LYS D  1 57  ? -14.631 4.945   -48.228 1.00 18.68 ? 57  LYS D O   1 
ATOM   6859 C  CB  . LYS D  1 57  ? -16.369 6.374   -45.673 1.00 18.70 ? 57  LYS D CB  1 
ATOM   6860 C  CG  . LYS D  1 57  ? -17.745 6.701   -45.048 1.00 21.55 ? 57  LYS D CG  1 
ATOM   6861 C  CD  . LYS D  1 57  ? -17.546 7.093   -43.577 1.00 27.90 ? 57  LYS D CD  1 
ATOM   6862 C  CE  . LYS D  1 57  ? -18.709 7.860   -42.944 1.00 31.93 ? 57  LYS D CE  1 
ATOM   6863 N  NZ  . LYS D  1 57  ? -18.517 7.915   -41.463 1.00 34.25 ? 57  LYS D NZ  1 
ATOM   6864 N  N   . GLN D  1 58  ? -14.414 7.247   -47.906 1.00 16.74 ? 58  GLN D N   1 
ATOM   6865 C  CA  . GLN D  1 58  ? -13.069 7.264   -48.531 1.00 17.48 ? 58  GLN D CA  1 
ATOM   6866 C  C   . GLN D  1 58  ? -12.160 8.024   -47.649 1.00 15.19 ? 58  GLN D C   1 
ATOM   6867 O  O   . GLN D  1 58  ? -12.534 8.920   -46.964 1.00 17.46 ? 58  GLN D O   1 
ATOM   6868 C  CB  . GLN D  1 58  ? -12.989 7.738   -49.981 1.00 23.56 ? 58  GLN D CB  1 
ATOM   6869 C  CG  . GLN D  1 58  ? -14.083 8.545   -50.527 1.00 30.98 ? 58  GLN D CG  1 
ATOM   6870 C  CD  . GLN D  1 58  ? -13.734 8.949   -51.958 1.00 30.66 ? 58  GLN D CD  1 
ATOM   6871 O  OE1 . GLN D  1 58  ? -13.350 8.094   -52.798 1.00 29.85 ? 58  GLN D OE1 1 
ATOM   6872 N  NE2 . GLN D  1 58  ? -13.840 10.270  -52.234 1.00 36.50 ? 58  GLN D NE2 1 
ATOM   6873 N  N   . PHE D  1 59  ? -10.891 7.565   -47.673 1.00 14.33 ? 59  PHE D N   1 
ATOM   6874 C  CA  . PHE D  1 59  ? -9.845  8.084   -46.800 1.00 14.85 ? 59  PHE D CA  1 
ATOM   6875 C  C   . PHE D  1 59  ? -8.663  8.489   -47.667 1.00 11.83 ? 59  PHE D C   1 
ATOM   6876 O  O   . PHE D  1 59  ? -8.301  7.832   -48.658 1.00 13.39 ? 59  PHE D O   1 
ATOM   6877 C  CB  . PHE D  1 59  ? -9.477  6.996   -45.785 1.00 14.89 ? 59  PHE D CB  1 
ATOM   6878 C  CG  . PHE D  1 59  ? -10.664 6.640   -44.944 1.00 13.76 ? 59  PHE D CG  1 
ATOM   6879 C  CD1 . PHE D  1 59  ? -11.624 5.696   -45.424 1.00 15.16 ? 59  PHE D CD1 1 
ATOM   6880 C  CD2 . PHE D  1 59  ? -10.983 7.452   -43.870 1.00 14.53 ? 59  PHE D CD2 1 
ATOM   6881 C  CE1 . PHE D  1 59  ? -12.819 5.492   -44.677 1.00 14.68 ? 59  PHE D CE1 1 
ATOM   6882 C  CE2 . PHE D  1 59  ? -12.115 7.215   -43.129 1.00 15.10 ? 59  PHE D CE2 1 
ATOM   6883 C  CZ  . PHE D  1 59  ? -13.053 6.262   -43.539 1.00 14.06 ? 59  PHE D CZ  1 
ATOM   6884 N  N   . LEU D  1 60  ? -8.069  9.606   -47.297 1.00 13.86 ? 60  LEU D N   1 
ATOM   6885 C  CA  . LEU D  1 60  ? -6.971  10.216  -48.100 1.00 14.18 ? 60  LEU D CA  1 
ATOM   6886 C  C   . LEU D  1 60  ? -5.621  9.569   -47.923 1.00 12.91 ? 60  LEU D C   1 
ATOM   6887 O  O   . LEU D  1 60  ? -5.063  9.544   -46.813 1.00 14.02 ? 60  LEU D O   1 
ATOM   6888 C  CB  . LEU D  1 60  ? -6.861  11.670  -47.680 1.00 16.65 ? 60  LEU D CB  1 
ATOM   6889 C  CG  . LEU D  1 60  ? -6.094  12.578  -48.602 1.00 19.87 ? 60  LEU D CG  1 
ATOM   6890 C  CD1 . LEU D  1 60  ? -6.753  12.590  -49.968 1.00 19.51 ? 60  LEU D CD1 1 
ATOM   6891 C  CD2 . LEU D  1 60  ? -6.103  13.994  -48.001 1.00 24.20 ? 60  LEU D CD2 1 
ATOM   6892 N  N   . LEU D  1 61  ? -5.072  9.092   -49.007 1.00 13.28 ? 61  LEU D N   1 
ATOM   6893 C  CA  . LEU D  1 61  ? -3.689  8.579   -49.035 1.00 13.01 ? 61  LEU D CA  1 
ATOM   6894 C  C   . LEU D  1 61  ? -2.809  9.664   -49.608 1.00 14.53 ? 61  LEU D C   1 
ATOM   6895 O  O   . LEU D  1 61  ? -3.203  10.301  -50.646 1.00 15.78 ? 61  LEU D O   1 
ATOM   6896 C  CB  . LEU D  1 61  ? -3.716  7.357   -49.923 1.00 13.27 ? 61  LEU D CB  1 
ATOM   6897 C  CG  . LEU D  1 61  ? -2.511  6.492   -49.992 1.00 13.58 ? 61  LEU D CG  1 
ATOM   6898 C  CD1 . LEU D  1 61  ? -2.351  5.645   -48.706 1.00 13.94 ? 61  LEU D CD1 1 
ATOM   6899 C  CD2 . LEU D  1 61  ? -2.514  5.559   -51.203 1.00 16.24 ? 61  LEU D CD2 1 
ATOM   6900 N  N   . THR D  1 62  ? -1.628  9.883   -49.025 1.00 13.56 ? 62  THR D N   1 
ATOM   6901 C  CA  . THR D  1 62  ? -0.777  10.999  -49.449 1.00 14.00 ? 62  THR D CA  1 
ATOM   6902 C  C   . THR D  1 62  ? 0.680   10.444  -49.415 1.00 14.38 ? 62  THR D C   1 
ATOM   6903 O  O   . THR D  1 62  ? 1.102   9.765   -48.464 1.00 15.19 ? 62  THR D O   1 
ATOM   6904 C  CB  . THR D  1 62  ? -0.811  12.146  -48.453 1.00 18.09 ? 62  THR D CB  1 
ATOM   6905 O  OG1 . THR D  1 62  ? -2.156  12.654  -48.235 1.00 24.64 ? 62  THR D OG1 1 
ATOM   6906 C  CG2 . THR D  1 62  ? 0.026   13.350  -48.972 1.00 21.25 ? 62  THR D CG2 1 
ATOM   6907 N  N   . ASN D  1 63  ? 1.466   10.833  -50.409 1.00 13.87 ? 63  ASN D N   1 
ATOM   6908 C  CA  . ASN D  1 63  ? 2.944   10.759  -50.318 1.00 14.44 ? 63  ASN D CA  1 
ATOM   6909 C  C   . ASN D  1 63  ? 3.486   12.008  -49.714 1.00 14.62 ? 63  ASN D C   1 
ATOM   6910 O  O   . ASN D  1 63  ? 3.337   13.124  -50.270 1.00 14.21 ? 63  ASN D O   1 
ATOM   6911 C  CB  . ASN D  1 63  ? 3.426   10.547  -51.771 1.00 15.38 ? 63  ASN D CB  1 
ATOM   6912 C  CG  . ASN D  1 63  ? 4.952   10.588  -51.913 1.00 12.81 ? 63  ASN D CG  1 
ATOM   6913 O  OD1 . ASN D  1 63  ? 5.650   11.109  -51.018 1.00 13.41 ? 63  ASN D OD1 1 
ATOM   6914 N  ND2 . ASN D  1 63  ? 5.463   9.964   -52.919 1.00 13.60 ? 63  ASN D ND2 1 
ATOM   6915 N  N   . ASN D  1 64  ? 4.008   11.940  -48.499 1.00 13.80 ? 64  ASN D N   1 
ATOM   6916 C  CA  . ASN D  1 64  ? 4.404   13.142  -47.806 1.00 15.55 ? 64  ASN D CA  1 
ATOM   6917 C  C   . ASN D  1 64  ? 5.857   13.495  -48.020 1.00 15.80 ? 64  ASN D C   1 
ATOM   6918 O  O   . ASN D  1 64  ? 6.430   14.350  -47.275 1.00 18.81 ? 64  ASN D O   1 
ATOM   6919 C  CB  . ASN D  1 64  ? 4.021   13.031  -46.324 1.00 16.05 ? 64  ASN D CB  1 
ATOM   6920 C  CG  . ASN D  1 64  ? 4.794   11.960  -45.564 1.00 17.34 ? 64  ASN D CG  1 
ATOM   6921 O  OD1 . ASN D  1 64  ? 5.742   11.328  -46.057 1.00 14.04 ? 64  ASN D OD1 1 
ATOM   6922 N  ND2 . ASN D  1 64  ? 4.432   11.825  -44.285 1.00 18.00 ? 64  ASN D ND2 1 
ATOM   6923 N  N   . GLY D  1 65  ? 6.467   12.749  -48.936 1.00 15.52 ? 65  GLY D N   1 
ATOM   6924 C  CA  . GLY D  1 65  ? 7.893   12.919  -49.190 1.00 15.75 ? 65  GLY D CA  1 
ATOM   6925 C  C   . GLY D  1 65  ? 8.799   12.065  -48.298 1.00 17.34 ? 65  GLY D C   1 
ATOM   6926 O  O   . GLY D  1 65  ? 10.019  12.090  -48.520 1.00 19.07 ? 65  GLY D O   1 
ATOM   6927 N  N   . HIS D  1 66  ? 8.232   11.312  -47.330 1.00 14.95 ? 66  HIS D N   1 
ATOM   6928 C  CA  . HIS D  1 66  ? 9.031   10.449  -46.397 1.00 13.93 ? 66  HIS D CA  1 
ATOM   6929 C  C   . HIS D  1 66  ? 8.455   9.073   -46.251 1.00 12.69 ? 66  HIS D C   1 
ATOM   6930 O  O   . HIS D  1 66  ? 9.222   8.161   -45.852 1.00 13.34 ? 66  HIS D O   1 
ATOM   6931 C  CB  . HIS D  1 66  ? 9.109   11.153  -45.015 1.00 15.42 ? 66  HIS D CB  1 
ATOM   6932 C  CG  . HIS D  1 66  ? 9.564   12.622  -45.118 1.00 18.45 ? 66  HIS D CG  1 
ATOM   6933 N  ND1 . HIS D  1 66  ? 10.849  12.950  -45.420 1.00 19.64 ? 66  HIS D ND1 1 
ATOM   6934 C  CD2 . HIS D  1 66  ? 8.891   13.769  -44.919 1.00 19.70 ? 66  HIS D CD2 1 
ATOM   6935 C  CE1 . HIS D  1 66  ? 10.949  14.320  -45.433 1.00 18.73 ? 66  HIS D CE1 1 
ATOM   6936 N  NE2 . HIS D  1 66  ? 9.760   14.802  -45.100 1.00 19.14 ? 66  HIS D NE2 1 
ATOM   6937 N  N   . SER D  1 67  ? 7.178   8.909   -46.522 1.00 12.83 ? 67  SER D N   1 
ATOM   6938 C  CA  . SER D  1 67  ? 6.473   7.636   -46.485 1.00 12.62 ? 67  SER D CA  1 
ATOM   6939 C  C   . SER D  1 67  ? 5.165   7.847   -47.271 1.00 12.78 ? 67  SER D C   1 
ATOM   6940 O  O   . SER D  1 67  ? 4.962   8.869   -47.895 1.00 14.60 ? 67  SER D O   1 
ATOM   6941 C  CB  . SER D  1 67  ? 6.113   7.384   -45.018 1.00 13.03 ? 67  SER D CB  1 
ATOM   6942 O  OG  . SER D  1 67  ? 5.503   6.102   -44.856 1.00 13.45 ? 67  SER D OG  1 
ATOM   6943 N  N   . VAL D  1 68  ? 4.374   6.805   -47.301 1.00 11.81 ? 68  VAL D N   1 
ATOM   6944 C  CA  . VAL D  1 68  ? 3.001   6.932   -47.783 1.00 14.01 ? 68  VAL D CA  1 
ATOM   6945 C  C   . VAL D  1 68  ? 2.133   6.893   -46.492 1.00 12.85 ? 68  VAL D C   1 
ATOM   6946 O  O   . VAL D  1 68  ? 2.283   5.972   -45.711 1.00 12.52 ? 68  VAL D O   1 
ATOM   6947 C  CB  . VAL D  1 68  ? 2.716   5.874   -48.850 1.00 14.87 ? 68  VAL D CB  1 
ATOM   6948 C  CG1 . VAL D  1 68  ? 2.896   4.438   -48.374 1.00 15.48 ? 68  VAL D CG1 1 
ATOM   6949 C  CG2 . VAL D  1 68  ? 1.267   6.062   -49.348 1.00 16.03 ? 68  VAL D CG2 1 
ATOM   6950 N  N   . LYS D  1 69  ? 1.176   7.810   -46.407 1.00 13.24 ? 69  LYS D N   1 
ATOM   6951 C  CA  . LYS D  1 69  ? 0.268   7.830   -45.248 1.00 12.95 ? 69  LYS D CA  1 
ATOM   6952 C  C   . LYS D  1 69  ? -1.188  7.849   -45.607 1.00 11.38 ? 69  LYS D C   1 
ATOM   6953 O  O   . LYS D  1 69  ? -1.549  8.326   -46.677 1.00 12.73 ? 69  LYS D O   1 
ATOM   6954 C  CB  . LYS D  1 69  ? 0.613   9.009   -44.321 1.00 16.34 ? 69  LYS D CB  1 
ATOM   6955 C  CG  . LYS D  1 69  ? 0.138   10.301  -44.768 1.00 17.32 ? 69  LYS D CG  1 
ATOM   6956 C  CD  . LYS D  1 69  ? 0.215   11.348  -43.597 1.00 18.72 ? 69  LYS D CD  1 
ATOM   6957 C  CE  . LYS D  1 69  ? -0.175  12.633  -44.309 1.00 21.58 ? 69  LYS D CE  1 
ATOM   6958 N  NZ  . LYS D  1 69  ? 0.035   13.688  -43.282 1.00 22.96 ? 69  LYS D NZ  1 
ATOM   6959 N  N   . LEU D  1 70  ? -1.992  7.136   -44.849 1.00 9.57  ? 70  LEU D N   1 
ATOM   6960 C  CA  . LEU D  1 70  ? -3.422  7.116   -45.021 1.00 9.79  ? 70  LEU D CA  1 
ATOM   6961 C  C   . LEU D  1 70  ? -3.967  7.841   -43.795 1.00 10.76 ? 70  LEU D C   1 
ATOM   6962 O  O   . LEU D  1 70  ? -3.709  7.473   -42.642 1.00 10.91 ? 70  LEU D O   1 
ATOM   6963 C  CB  . LEU D  1 70  ? -3.875  5.647   -44.982 1.00 10.95 ? 70  LEU D CB  1 
ATOM   6964 C  CG  . LEU D  1 70  ? -5.346  5.484   -45.110 1.00 10.34 ? 70  LEU D CG  1 
ATOM   6965 C  CD1 . LEU D  1 70  ? -5.786  5.959   -46.541 1.00 12.32 ? 70  LEU D CD1 1 
ATOM   6966 C  CD2 . LEU D  1 70  ? -5.750  4.009   -44.894 1.00 13.88 ? 70  LEU D CD2 1 
ATOM   6967 N  N   . ASN D  1 71  ? -4.786  8.849   -44.059 1.00 11.92 ? 71  ASN D N   1 
ATOM   6968 C  CA  . ASN D  1 71  ? -5.467  9.569   -42.992 1.00 11.77 ? 71  ASN D CA  1 
ATOM   6969 C  C   . ASN D  1 71  ? -6.570  8.709   -42.417 1.00 12.70 ? 71  ASN D C   1 
ATOM   6970 O  O   . ASN D  1 71  ? -7.285  8.008   -43.156 1.00 15.14 ? 71  ASN D O   1 
ATOM   6971 C  CB  . ASN D  1 71  ? -6.053  10.923  -43.509 1.00 14.29 ? 71  ASN D CB  1 
ATOM   6972 C  CG  . ASN D  1 71  ? -5.043  11.994  -43.666 1.00 18.66 ? 71  ASN D CG  1 
ATOM   6973 O  OD1 . ASN D  1 71  ? -3.868  11.837  -43.371 1.00 22.32 ? 71  ASN D OD1 1 
ATOM   6974 N  ND2 . ASN D  1 71  ? -5.541  13.201  -44.103 1.00 20.49 ? 71  ASN D ND2 1 
ATOM   6975 N  N   . LEU D  1 72  ? -6.701  8.775   -41.101 1.00 12.07 ? 72  LEU D N   1 
ATOM   6976 C  CA  . LEU D  1 72  ? -7.710  8.022   -40.360 1.00 12.52 ? 72  LEU D CA  1 
ATOM   6977 C  C   . LEU D  1 72  ? -8.660  8.951   -39.602 1.00 14.26 ? 72  LEU D C   1 
ATOM   6978 O  O   . LEU D  1 72  ? -8.249  10.028  -39.246 1.00 14.80 ? 72  LEU D O   1 
ATOM   6979 C  CB  . LEU D  1 72  ? -7.041  7.043   -39.393 1.00 11.20 ? 72  LEU D CB  1 
ATOM   6980 C  CG  . LEU D  1 72  ? -6.108  6.015   -40.036 1.00 11.53 ? 72  LEU D CG  1 
ATOM   6981 C  CD1 . LEU D  1 72  ? -5.254  5.324   -38.984 1.00 11.21 ? 72  LEU D CD1 1 
ATOM   6982 C  CD2 . LEU D  1 72  ? -6.903  4.999   -40.842 1.00 12.42 ? 72  LEU D CD2 1 
ATOM   6983 N  N   . PRO D  1 73  ? -9.882  8.504   -39.388 1.00 14.13 ? 73  PRO D N   1 
ATOM   6984 C  CA  . PRO D  1 73  ? -10.880 9.383   -38.679 1.00 15.75 ? 73  PRO D CA  1 
ATOM   6985 C  C   . PRO D  1 73  ? -10.720 9.377   -37.171 1.00 17.54 ? 73  PRO D C   1 
ATOM   6986 O  O   . PRO D  1 73  ? -10.349 8.293   -36.589 1.00 16.90 ? 73  PRO D O   1 
ATOM   6987 C  CB  . PRO D  1 73  ? -12.188 8.764   -39.159 1.00 16.03 ? 73  PRO D CB  1 
ATOM   6988 C  CG  . PRO D  1 73  ? -11.877 7.225   -39.187 1.00 14.71 ? 73  PRO D CG  1 
ATOM   6989 C  CD  . PRO D  1 73  ? -10.473 7.244   -39.877 1.00 14.24 ? 73  PRO D CD  1 
ATOM   6990 N  N   . SER D  1 74  ? -11.038 10.493  -36.482 1.00 18.53 ? 74  SER D N   1 
ATOM   6991 C  CA  . SER D  1 74  ? -10.854 10.538  -35.044 1.00 18.73 ? 74  SER D CA  1 
ATOM   6992 C  C   . SER D  1 74  ? -11.857 9.669   -34.248 1.00 18.55 ? 74  SER D C   1 
ATOM   6993 O  O   . SER D  1 74  ? -11.610 9.412   -33.039 1.00 24.36 ? 74  SER D O   1 
ATOM   6994 C  CB  . SER D  1 74  ? -10.776 12.018  -34.566 1.00 23.38 ? 74  SER D CB  1 
ATOM   6995 O  OG  . SER D  1 74  ? -12.009 12.678  -34.864 1.00 23.45 ? 74  SER D OG  1 
ATOM   6996 N  N   . ASP D  1 75  ? -12.909 9.208   -34.905 1.00 19.93 ? 75  ASP D N   1 
ATOM   6997 C  CA  . ASP D  1 75  ? -13.848 8.318   -34.218 1.00 25.00 ? 75  ASP D CA  1 
ATOM   6998 C  C   . ASP D  1 75  ? -13.152 6.963   -33.971 1.00 23.25 ? 75  ASP D C   1 
ATOM   6999 O  O   . ASP D  1 75  ? -13.556 6.217   -33.061 1.00 21.88 ? 75  ASP D O   1 
ATOM   7000 C  CB  . ASP D  1 75  ? -15.228 8.268   -34.936 1.00 31.48 ? 75  ASP D CB  1 
ATOM   7001 C  CG  . ASP D  1 75  ? -15.287 7.301   -36.104 1.00 42.17 ? 75  ASP D CG  1 
ATOM   7002 O  OD1 . ASP D  1 75  ? -14.857 7.603   -37.252 1.00 42.14 ? 75  ASP D OD1 1 
ATOM   7003 O  OD2 . ASP D  1 75  ? -15.845 6.201   -35.883 1.00 52.46 ? 75  ASP D OD2 1 
ATOM   7004 N  N   . MET D  1 76  ? -12.110 6.643   -34.751 1.00 18.37 ? 76  MET D N   1 
ATOM   7005 C  CA  . MET D  1 76  ? -11.284 5.440   -34.507 1.00 18.20 ? 76  MET D CA  1 
ATOM   7006 C  C   . MET D  1 76  ? -10.332 5.684   -33.338 1.00 15.29 ? 76  MET D C   1 
ATOM   7007 O  O   . MET D  1 76  ? -9.684  6.685   -33.205 1.00 14.34 ? 76  MET D O   1 
ATOM   7008 C  CB  . MET D  1 76  ? -10.605 5.137   -35.868 1.00 17.91 ? 76  MET D CB  1 
ATOM   7009 C  CG  . MET D  1 76  ? -9.630  3.983   -35.784 1.00 17.34 ? 76  MET D CG  1 
ATOM   7010 S  SD  . MET D  1 76  ? -8.894  3.817   -37.472 1.00 17.15 ? 76  MET D SD  1 
ATOM   7011 C  CE  . MET D  1 76  ? -7.427  2.836   -37.060 1.00 13.93 ? 76  MET D CE  1 
ATOM   7012 N  N   . HIS D  1 77  ? -10.313 4.711   -32.380 1.00 15.26 ? 77  HIS D N   1 
ATOM   7013 C  CA  . HIS D  1 77  ? -9.549  4.934   -31.167 1.00 15.33 ? 77  HIS D CA  1 
ATOM   7014 C  C   . HIS D  1 77  ? -9.072  3.706   -30.477 1.00 14.06 ? 77  HIS D C   1 
ATOM   7015 O  O   . HIS D  1 77  ? -9.652  2.666   -30.807 1.00 16.77 ? 77  HIS D O   1 
ATOM   7016 C  CB  . HIS D  1 77  ? -10.312 5.838   -30.160 1.00 20.11 ? 77  HIS D CB  1 
ATOM   7017 C  CG  . HIS D  1 77  ? -11.633 5.265   -29.641 1.00 23.43 ? 77  HIS D CG  1 
ATOM   7018 N  ND1 . HIS D  1 77  ? -12.774 5.295   -30.360 1.00 26.62 ? 77  HIS D ND1 1 
ATOM   7019 C  CD2 . HIS D  1 77  ? -11.973 4.681   -28.414 1.00 27.88 ? 77  HIS D CD2 1 
ATOM   7020 C  CE1 . HIS D  1 77  ? -13.799 4.719   -29.654 1.00 27.99 ? 77  HIS D CE1 1 
ATOM   7021 N  NE2 . HIS D  1 77  ? -13.315 4.372   -28.463 1.00 27.58 ? 77  HIS D NE2 1 
ATOM   7022 N  N   . ILE D  1 78  ? -8.119  3.907   -29.579 1.00 15.60 ? 78  ILE D N   1 
ATOM   7023 C  CA  . ILE D  1 78  ? -7.687  2.810   -28.710 1.00 17.22 ? 78  ILE D CA  1 
ATOM   7024 C  C   . ILE D  1 78  ? -8.158  3.128   -27.275 1.00 21.12 ? 78  ILE D C   1 
ATOM   7025 O  O   . ILE D  1 78  ? -7.919  4.250   -26.762 1.00 20.31 ? 78  ILE D O   1 
ATOM   7026 C  CB  . ILE D  1 78  ? -6.187  2.642   -28.666 1.00 18.16 ? 78  ILE D CB  1 
ATOM   7027 C  CG1 . ILE D  1 78  ? -5.571  2.152   -29.966 1.00 20.59 ? 78  ILE D CG1 1 
ATOM   7028 C  CG2 . ILE D  1 78  ? -5.838  1.609   -27.622 1.00 23.11 ? 78  ILE D CG2 1 
ATOM   7029 C  CD1 . ILE D  1 78  ? -4.123  2.710   -29.983 1.00 24.53 ? 78  ILE D CD1 1 
ATOM   7030 N  N   . GLN D  1 79  ? -8.541  2.043   -26.615 1.00 24.58 ? 79  GLN D N   1 
ATOM   7031 C  CA  . GLN D  1 79  ? -8.849  2.000   -25.172 1.00 30.66 ? 79  GLN D CA  1 
ATOM   7032 C  C   . GLN D  1 79  ? -7.901  1.055   -24.405 1.00 29.41 ? 79  GLN D C   1 
ATOM   7033 O  O   . GLN D  1 79  ? -7.408  0.034   -24.978 1.00 28.52 ? 79  GLN D O   1 
ATOM   7034 C  CB  . GLN D  1 79  ? -10.310 1.567   -24.987 1.00 36.09 ? 79  GLN D CB  1 
ATOM   7035 C  CG  . GLN D  1 79  ? -11.358 2.672   -25.256 1.00 44.96 ? 79  GLN D CG  1 
ATOM   7036 C  CD  . GLN D  1 79  ? -11.156 4.001   -24.467 1.00 52.20 ? 79  GLN D CD  1 
ATOM   7037 O  OE1 . GLN D  1 79  ? -10.765 4.017   -23.288 1.00 58.35 ? 79  GLN D OE1 1 
ATOM   7038 N  NE2 . GLN D  1 79  ? -11.458 5.120   -25.127 1.00 53.44 ? 79  GLN D NE2 1 
ATOM   7039 N  N   . GLY D  1 80  ? -7.531  1.424   -23.166 1.00 30.06 ? 80  GLY D N   1 
ATOM   7040 C  CA  . GLY D  1 80  ? -6.579  0.634   -22.392 1.00 23.90 ? 80  GLY D CA  1 
ATOM   7041 C  C   . GLY D  1 80  ? -5.500  1.438   -21.782 1.00 28.99 ? 80  GLY D C   1 
ATOM   7042 O  O   . GLY D  1 80  ? -4.969  1.024   -20.789 1.00 30.98 ? 80  GLY D O   1 
ATOM   7043 N  N   . LEU D  1 81  ? -5.160  2.624   -22.335 1.00 19.93 ? 81  LEU D N   1 
ATOM   7044 C  CA  . LEU D  1 81  ? -3.978  3.339   -21.859 1.00 22.93 ? 81  LEU D CA  1 
ATOM   7045 C  C   . LEU D  1 81  ? -4.396  4.354   -20.802 1.00 20.23 ? 81  LEU D C   1 
ATOM   7046 O  O   . LEU D  1 81  ? -5.553  4.410   -20.461 1.00 22.22 ? 81  LEU D O   1 
ATOM   7047 C  CB  . LEU D  1 81  ? -3.350  4.050   -23.073 1.00 20.96 ? 81  LEU D CB  1 
ATOM   7048 C  CG  . LEU D  1 81  ? -3.060  3.030   -24.216 1.00 21.99 ? 81  LEU D CG  1 
ATOM   7049 C  CD1 . LEU D  1 81  ? -2.803  3.808   -25.505 1.00 23.86 ? 81  LEU D CD1 1 
ATOM   7050 C  CD2 . LEU D  1 81  ? -1.821  2.252   -23.759 1.00 20.71 ? 81  LEU D CD2 1 
ATOM   7051 N  N   . GLN D  1 82  ? -3.472  5.186   -20.326 1.00 21.15 ? 82  GLN D N   1 
ATOM   7052 C  CA  . GLN D  1 82  ? -3.890  6.149   -19.244 1.00 20.35 ? 82  GLN D CA  1 
ATOM   7053 C  C   . GLN D  1 82  ? -4.907  7.226   -19.690 1.00 24.94 ? 82  GLN D C   1 
ATOM   7054 O  O   . GLN D  1 82  ? -5.515  7.833   -18.838 1.00 22.42 ? 82  GLN D O   1 
ATOM   7055 C  CB  . GLN D  1 82  ? -2.613  6.752   -18.637 1.00 21.45 ? 82  GLN D CB  1 
ATOM   7056 C  CG  . GLN D  1 82  ? -2.209  8.105   -19.254 1.00 24.43 ? 82  GLN D CG  1 
ATOM   7057 C  CD  . GLN D  1 82  ? -1.707  8.022   -20.719 1.00 28.75 ? 82  GLN D CD  1 
ATOM   7058 O  OE1 . GLN D  1 82  ? -1.372  6.928   -21.250 1.00 27.92 ? 82  GLN D OE1 1 
ATOM   7059 N  NE2 . GLN D  1 82  ? -1.662  9.184   -21.384 1.00 29.94 ? 82  GLN D NE2 1 
ATOM   7060 N  N   . SER D  1 83  ? -5.138  7.393   -21.013 1.00 22.19 ? 83  SER D N   1 
ATOM   7061 C  CA  . SER D  1 83  ? -6.100  8.366   -21.669 1.00 21.03 ? 83  SER D CA  1 
ATOM   7062 C  C   . SER D  1 83  ? -6.658  7.713   -22.970 1.00 20.94 ? 83  SER D C   1 
ATOM   7063 O  O   . SER D  1 83  ? -5.961  6.755   -23.489 1.00 20.71 ? 83  SER D O   1 
ATOM   7064 C  CB  . SER D  1 83  ? -5.308  9.612   -22.095 1.00 19.61 ? 83  SER D CB  1 
ATOM   7065 O  OG  . SER D  1 83  ? -4.716  10.297  -20.958 1.00 20.03 ? 83  SER D OG  1 
ATOM   7066 N  N   . ARG D  1 84  ? -7.764  8.171   -23.565 1.00 19.19 ? 84  ARG D N   1 
ATOM   7067 C  CA  . ARG D  1 84  ? -8.287  7.779   -24.907 1.00 20.57 ? 84  ARG D CA  1 
ATOM   7068 C  C   . ARG D  1 84  ? -7.315  8.386   -25.961 1.00 18.04 ? 84  ARG D C   1 
ATOM   7069 O  O   . ARG D  1 84  ? -6.952  9.580   -25.861 1.00 18.39 ? 84  ARG D O   1 
ATOM   7070 C  CB  . ARG D  1 84  ? -9.694  8.305   -25.282 1.00 20.14 ? 84  ARG D CB  1 
ATOM   7071 C  CG  . ARG D  1 84  ? -10.067 8.036   -26.745 1.00 27.94 ? 84  ARG D CG  1 
ATOM   7072 C  CD  . ARG D  1 84  ? -11.514 8.427   -27.082 1.00 30.55 ? 84  ARG D CD  1 
ATOM   7073 N  NE  . ARG D  1 84  ? -11.632 8.526   -28.534 1.00 33.49 ? 84  ARG D NE  1 
ATOM   7074 C  CZ  . ARG D  1 84  ? -12.761 8.512   -29.238 1.00 39.82 ? 84  ARG D CZ  1 
ATOM   7075 N  NH1 . ARG D  1 84  ? -13.950 8.476   -28.585 1.00 40.47 ? 84  ARG D NH1 1 
ATOM   7076 N  NH2 . ARG D  1 84  ? -12.708 8.562   -30.591 1.00 32.16 ? 84  ARG D NH2 1 
ATOM   7077 N  N   . TYR D  1 85  ? -6.867  7.552   -26.912 1.00 14.85 ? 85  TYR D N   1 
ATOM   7078 C  CA  . TYR D  1 85  ? -6.031  7.964   -27.982 1.00 14.35 ? 85  TYR D CA  1 
ATOM   7079 C  C   . TYR D  1 85  ? -6.850  7.680   -29.246 1.00 15.23 ? 85  TYR D C   1 
ATOM   7080 O  O   . TYR D  1 85  ? -7.316  6.619   -29.554 1.00 16.56 ? 85  TYR D O   1 
ATOM   7081 C  CB  . TYR D  1 85  ? -4.708  7.213   -27.982 1.00 13.51 ? 85  TYR D CB  1 
ATOM   7082 C  CG  . TYR D  1 85  ? -3.724  7.718   -26.949 1.00 11.51 ? 85  TYR D CG  1 
ATOM   7083 C  CD1 . TYR D  1 85  ? -3.768  7.274   -25.629 1.00 13.87 ? 85  TYR D CD1 1 
ATOM   7084 C  CD2 . TYR D  1 85  ? -2.746  8.636   -27.296 1.00 12.58 ? 85  TYR D CD2 1 
ATOM   7085 C  CE1 . TYR D  1 85  ? -2.862  7.736   -24.689 1.00 14.21 ? 85  TYR D CE1 1 
ATOM   7086 C  CE2 . TYR D  1 85  ? -1.836  9.101   -26.368 1.00 12.63 ? 85  TYR D CE2 1 
ATOM   7087 C  CZ  . TYR D  1 85  ? -1.893  8.650   -25.068 1.00 15.50 ? 85  TYR D CZ  1 
ATOM   7088 O  OH  . TYR D  1 85  ? -0.978  9.130   -24.160 1.00 16.83 ? 85  TYR D OH  1 
ATOM   7089 N  N   . SER D  1 86  ? -6.997  8.749   -30.069 1.00 14.04 ? 86  SER D N   1 
ATOM   7090 C  CA  . SER D  1 86  ? -7.750  8.694   -31.304 1.00 14.94 ? 86  SER D CA  1 
ATOM   7091 C  C   . SER D  1 86  ? -6.802  8.638   -32.550 1.00 11.63 ? 86  SER D C   1 
ATOM   7092 O  O   . SER D  1 86  ? -5.748  9.281   -32.525 1.00 12.38 ? 86  SER D O   1 
ATOM   7093 C  CB  . SER D  1 86  ? -8.607  9.965   -31.466 1.00 16.65 ? 86  SER D CB  1 
ATOM   7094 O  OG  . SER D  1 86  ? -9.471  10.061  -30.309 1.00 18.76 ? 86  SER D OG  1 
ATOM   7095 N  N   . ALA D  1 87  ? -7.193  7.822   -33.491 1.00 12.73 ? 87  ALA D N   1 
ATOM   7096 C  CA  . ALA D  1 87  ? -6.389  7.663   -34.742 1.00 13.62 ? 87  ALA D CA  1 
ATOM   7097 C  C   . ALA D  1 87  ? -6.199  8.998   -35.435 1.00 13.76 ? 87  ALA D C   1 
ATOM   7098 O  O   . ALA D  1 87  ? -7.157  9.845   -35.489 1.00 14.16 ? 87  ALA D O   1 
ATOM   7099 C  CB  . ALA D  1 87  ? -7.008  6.675   -35.656 1.00 13.23 ? 87  ALA D CB  1 
ATOM   7100 N  N   . THR D  1 88  ? -5.049  9.151   -36.072 1.00 12.48 ? 88  THR D N   1 
ATOM   7101 C  CA  . THR D  1 88  ? -4.794  10.259  -37.013 1.00 12.66 ? 88  THR D CA  1 
ATOM   7102 C  C   . THR D  1 88  ? -4.310  9.783   -38.400 1.00 12.40 ? 88  THR D C   1 
ATOM   7103 O  O   . THR D  1 88  ? -4.761  10.268  -39.460 1.00 13.01 ? 88  THR D O   1 
ATOM   7104 C  CB  . THR D  1 88  ? -3.907  11.319  -36.353 1.00 14.13 ? 88  THR D CB  1 
ATOM   7105 O  OG1 . THR D  1 88  ? -3.688  12.389  -37.324 1.00 15.94 ? 88  THR D OG1 1 
ATOM   7106 C  CG2 . THR D  1 88  ? -2.587  10.803  -35.849 1.00 14.90 ? 88  THR D CG2 1 
ATOM   7107 N  N   . GLN D  1 89  ? -3.396  8.818   -38.424 1.00 12.41 ? 89  GLN D N   1 
ATOM   7108 C  CA  . GLN D  1 89  ? -2.956  8.323   -39.740 1.00 10.32 ? 89  GLN D CA  1 
ATOM   7109 C  C   . GLN D  1 89  ? -2.181  7.023   -39.513 1.00 9.13  ? 89  GLN D C   1 
ATOM   7110 O  O   . GLN D  1 89  ? -1.795  6.681   -38.389 1.00 10.47 ? 89  GLN D O   1 
ATOM   7111 C  CB  . GLN D  1 89  ? -1.993  9.371   -40.396 1.00 11.31 ? 89  GLN D CB  1 
ATOM   7112 C  CG  . GLN D  1 89  ? -0.795  9.756   -39.576 1.00 14.30 ? 89  GLN D CG  1 
ATOM   7113 C  CD  . GLN D  1 89  ? 0.504   9.228   -40.076 1.00 15.42 ? 89  GLN D CD  1 
ATOM   7114 O  OE1 . GLN D  1 89  ? 0.562   8.039   -40.352 1.00 16.63 ? 89  GLN D OE1 1 
ATOM   7115 N  NE2 . GLN D  1 89  ? 1.463   10.016  -40.238 1.00 15.69 ? 89  GLN D NE2 1 
ATOM   7116 N  N   . LEU D  1 90  ? -2.013  6.273   -40.622 1.00 8.45  ? 90  LEU D N   1 
ATOM   7117 C  CA  . LEU D  1 90  ? -1.015  5.172   -40.585 1.00 9.15  ? 90  LEU D CA  1 
ATOM   7118 C  C   . LEU D  1 90  ? -0.063  5.343   -41.774 1.00 8.00  ? 90  LEU D C   1 
ATOM   7119 O  O   . LEU D  1 90  ? -0.393  5.996   -42.769 1.00 10.06 ? 90  LEU D O   1 
ATOM   7120 C  CB  . LEU D  1 90  ? -1.714  3.746   -40.550 1.00 9.39  ? 90  LEU D CB  1 
ATOM   7121 C  CG  . LEU D  1 90  ? -2.673  3.446   -41.673 1.00 8.45  ? 90  LEU D CG  1 
ATOM   7122 C  CD1 . LEU D  1 90  ? -2.026  3.094   -43.025 1.00 11.03 ? 90  LEU D CD1 1 
ATOM   7123 C  CD2 . LEU D  1 90  ? -3.577  2.275   -41.332 1.00 10.80 ? 90  LEU D CD2 1 
ATOM   7124 N  N   . HIS D  1 91  ? 1.084   4.696   -41.663 1.00 9.16  ? 91  HIS D N   1 
ATOM   7125 C  CA  . HIS D  1 91  ? 2.094   4.786   -42.714 1.00 9.18  ? 91  HIS D CA  1 
ATOM   7126 C  C   . HIS D  1 91  ? 3.050   3.613   -42.520 1.00 7.85  ? 91  HIS D C   1 
ATOM   7127 O  O   . HIS D  1 91  ? 2.970   2.851   -41.532 1.00 8.32  ? 91  HIS D O   1 
ATOM   7128 C  CB  . HIS D  1 91  ? 2.858   6.125   -42.671 1.00 8.27  ? 91  HIS D CB  1 
ATOM   7129 C  CG  . HIS D  1 91  ? 3.588   6.304   -41.338 1.00 7.18  ? 91  HIS D CG  1 
ATOM   7130 N  ND1 . HIS D  1 91  ? 3.034   6.908   -40.269 1.00 8.78  ? 91  HIS D ND1 1 
ATOM   7131 C  CD2 . HIS D  1 91  ? 4.817   5.795   -40.906 1.00 8.94  ? 91  HIS D CD2 1 
ATOM   7132 C  CE1 . HIS D  1 91  ? 3.908   6.844   -39.245 1.00 8.51  ? 91  HIS D CE1 1 
ATOM   7133 N  NE2 . HIS D  1 91  ? 5.001   6.171   -39.634 1.00 8.95  ? 91  HIS D NE2 1 
ATOM   7134 N  N   . LEU D  1 92  ? 4.020   3.504   -43.459 1.00 8.30  ? 92  LEU D N   1 
ATOM   7135 C  CA  . LEU D  1 92  ? 4.953   2.386   -43.430 1.00 8.76  ? 92  LEU D CA  1 
ATOM   7136 C  C   . LEU D  1 92  ? 6.399   2.806   -43.545 1.00 8.10  ? 92  LEU D C   1 
ATOM   7137 O  O   . LEU D  1 92  ? 6.728   3.927   -43.933 1.00 9.20  ? 92  LEU D O   1 
ATOM   7138 C  CB  . LEU D  1 92  ? 4.650   1.409   -44.583 1.00 10.64 ? 92  LEU D CB  1 
ATOM   7139 C  CG  . LEU D  1 92  ? 3.254   0.707   -44.423 1.00 10.80 ? 92  LEU D CG  1 
ATOM   7140 C  CD1 . LEU D  1 92  ? 2.291   1.381   -45.319 1.00 14.92 ? 92  LEU D CD1 1 
ATOM   7141 C  CD2 . LEU D  1 92  ? 3.386   -0.746  -44.617 1.00 13.86 ? 92  LEU D CD2 1 
ATOM   7142 N  N   . HIS D  1 93  ? 7.272   1.881   -43.232 1.00 8.40  ? 93  HIS D N   1 
ATOM   7143 C  CA  . HIS D  1 93  ? 8.765   2.047   -43.411 1.00 8.50  ? 93  HIS D CA  1 
ATOM   7144 C  C   . HIS D  1 93  ? 9.277   0.793   -44.051 1.00 8.27  ? 93  HIS D C   1 
ATOM   7145 O  O   . HIS D  1 93  ? 8.729   -0.295  -43.752 1.00 8.35  ? 93  HIS D O   1 
ATOM   7146 C  CB  . HIS D  1 93  ? 9.424   2.190   -42.043 1.00 8.28  ? 93  HIS D CB  1 
ATOM   7147 C  CG  . HIS D  1 93  ? 8.974   3.384   -41.286 1.00 8.72  ? 93  HIS D CG  1 
ATOM   7148 N  ND1 . HIS D  1 93  ? 9.545   4.668   -41.400 1.00 8.57  ? 93  HIS D ND1 1 
ATOM   7149 C  CD2 . HIS D  1 93  ? 7.896   3.527   -40.463 1.00 7.34  ? 93  HIS D CD2 1 
ATOM   7150 C  CE1 . HIS D  1 93  ? 8.827   5.548   -40.568 1.00 7.82  ? 93  HIS D CE1 1 
ATOM   7151 N  NE2 . HIS D  1 93  ? 7.854   4.882   -40.002 1.00 7.91  ? 93  HIS D NE2 1 
ATOM   7152 N  N   . TRP D  1 94  ? 10.230  0.919   -44.969 1.00 8.24  ? 94  TRP D N   1 
ATOM   7153 C  CA  . TRP D  1 94  ? 10.697  -0.285  -45.749 1.00 7.73  ? 94  TRP D CA  1 
ATOM   7154 C  C   . TRP D  1 94  ? 12.128  -0.005  -46.169 1.00 7.98  ? 94  TRP D C   1 
ATOM   7155 O  O   . TRP D  1 94  ? 12.749  1.050   -45.968 1.00 8.63  ? 94  TRP D O   1 
ATOM   7156 C  CB  . TRP D  1 94  ? 9.746   -0.555  -46.938 1.00 9.18  ? 94  TRP D CB  1 
ATOM   7157 C  CG  . TRP D  1 94  ? 9.667   0.668   -47.896 1.00 8.43  ? 94  TRP D CG  1 
ATOM   7158 C  CD1 . TRP D  1 94  ? 10.494  0.943   -48.930 1.00 9.45  ? 94  TRP D CD1 1 
ATOM   7159 C  CD2 . TRP D  1 94  ? 8.621   1.710   -47.863 1.00 9.28  ? 94  TRP D CD2 1 
ATOM   7160 N  NE1 . TRP D  1 94  ? 10.067  2.094   -49.584 1.00 10.61 ? 94  TRP D NE1 1 
ATOM   7161 C  CE2 . TRP D  1 94  ? 8.902   2.598   -48.948 1.00 9.88  ? 94  TRP D CE2 1 
ATOM   7162 C  CE3 . TRP D  1 94  ? 7.535   2.028   -46.965 1.00 9.64  ? 94  TRP D CE3 1 
ATOM   7163 C  CZ2 . TRP D  1 94  ? 8.107   3.701   -49.199 1.00 10.67 ? 94  TRP D CZ2 1 
ATOM   7164 C  CZ3 . TRP D  1 94  ? 6.784   3.141   -47.239 1.00 9.65  ? 94  TRP D CZ3 1 
ATOM   7165 C  CH2 . TRP D  1 94  ? 7.084   3.979   -48.306 1.00 10.68 ? 94  TRP D CH2 1 
ATOM   7166 N  N   . GLY D  1 95  ? 12.656  -1.082  -46.791 1.00 9.27  ? 95  GLY D N   1 
ATOM   7167 C  CA  . GLY D  1 95  ? 14.047  -1.135  -47.252 1.00 10.06 ? 95  GLY D CA  1 
ATOM   7168 C  C   . GLY D  1 95  ? 14.131  -0.876  -48.754 1.00 9.87  ? 95  GLY D C   1 
ATOM   7169 O  O   . GLY D  1 95  ? 13.661  0.153   -49.268 1.00 10.10 ? 95  GLY D O   1 
ATOM   7170 N  N   . ASN D  1 96  ? 14.708  -1.836  -49.509 1.00 11.09 ? 96  ASN D N   1 
ATOM   7171 C  CA  . ASN D  1 96  ? 14.790  -1.623  -50.954 1.00 13.63 ? 96  ASN D CA  1 
ATOM   7172 C  C   . ASN D  1 96  ? 14.940  -2.999  -51.583 1.00 13.96 ? 96  ASN D C   1 
ATOM   7173 O  O   . ASN D  1 96  ? 15.119  -3.977  -50.858 1.00 14.02 ? 96  ASN D O   1 
ATOM   7174 C  CB  . ASN D  1 96  ? 16.023  -0.695  -51.260 1.00 15.72 ? 96  ASN D CB  1 
ATOM   7175 C  CG  . ASN D  1 96  ? 17.335  -1.411  -51.044 1.00 17.17 ? 96  ASN D CG  1 
ATOM   7176 O  OD1 . ASN D  1 96  ? 17.789  -2.166  -51.945 1.00 23.22 ? 96  ASN D OD1 1 
ATOM   7177 N  ND2 . ASN D  1 96  ? 17.948  -1.188  -49.940 1.00 16.55 ? 96  ASN D ND2 1 
ATOM   7178 N  N   . PRO D  1 97  ? 14.876  -3.082  -52.948 1.00 15.30 ? 97  PRO D N   1 
ATOM   7179 C  CA  . PRO D  1 97  ? 14.819  -4.394  -53.540 1.00 18.79 ? 97  PRO D CA  1 
ATOM   7180 C  C   . PRO D  1 97  ? 16.075  -5.243  -53.244 1.00 18.11 ? 97  PRO D C   1 
ATOM   7181 O  O   . PRO D  1 97  ? 15.964  -6.474  -53.031 1.00 22.77 ? 97  PRO D O   1 
ATOM   7182 C  CB  . PRO D  1 97  ? 14.597  -4.068  -55.017 1.00 20.55 ? 97  PRO D CB  1 
ATOM   7183 C  CG  . PRO D  1 97  ? 14.004  -2.698  -55.055 1.00 20.73 ? 97  PRO D CG  1 
ATOM   7184 C  CD  . PRO D  1 97  ? 14.582  -2.031  -53.880 1.00 14.85 ? 97  PRO D CD  1 
ATOM   7185 N  N   . ASN D  1 98  ? 17.227  -4.609  -53.061 1.00 17.92 ? 98  ASN D N   1 
ATOM   7186 C  CA  . ASN D  1 98  ? 18.477  -5.325  -52.743 1.00 21.53 ? 98  ASN D CA  1 
ATOM   7187 C  C   . ASN D  1 98  ? 18.668  -5.631  -51.269 1.00 24.40 ? 98  ASN D C   1 
ATOM   7188 O  O   . ASN D  1 98  ? 19.631  -6.302  -50.867 1.00 24.70 ? 98  ASN D O   1 
ATOM   7189 C  CB  . ASN D  1 98  ? 19.684  -4.479  -53.200 1.00 24.66 ? 98  ASN D CB  1 
ATOM   7190 C  CG  . ASN D  1 98  ? 19.658  -4.197  -54.709 1.00 30.08 ? 98  ASN D CG  1 
ATOM   7191 O  OD1 . ASN D  1 98  ? 19.002  -4.911  -55.491 1.00 35.84 ? 98  ASN D OD1 1 
ATOM   7192 N  ND2 . ASN D  1 98  ? 20.346  -3.141  -55.112 1.00 34.26 ? 98  ASN D ND2 1 
ATOM   7193 N  N   . ASP D  1 99  ? 17.850  -4.997  -50.438 1.00 18.63 ? 99  ASP D N   1 
ATOM   7194 C  CA  . ASP D  1 99  ? 18.000  -5.232  -49.018 1.00 18.00 ? 99  ASP D CA  1 
ATOM   7195 C  C   . ASP D  1 99  ? 16.569  -5.069  -48.387 1.00 15.44 ? 99  ASP D C   1 
ATOM   7196 O  O   . ASP D  1 99  ? 16.214  -3.972  -47.910 1.00 13.42 ? 99  ASP D O   1 
ATOM   7197 C  CB  . ASP D  1 99  ? 19.019  -4.271  -48.367 1.00 19.04 ? 99  ASP D CB  1 
ATOM   7198 C  CG  . ASP D  1 99  ? 19.144  -4.475  -46.848 1.00 23.25 ? 99  ASP D CG  1 
ATOM   7199 O  OD1 . ASP D  1 99  ? 18.837  -5.589  -46.363 1.00 25.22 ? 99  ASP D OD1 1 
ATOM   7200 O  OD2 . ASP D  1 99  ? 19.450  -3.497  -46.115 1.00 31.42 ? 99  ASP D OD2 1 
ATOM   7201 N  N   . PRO D  1 100 ? 15.706  -6.062  -48.452 1.00 14.74 ? 100 PRO D N   1 
ATOM   7202 C  CA  . PRO D  1 100 ? 14.281  -5.914  -48.095 1.00 14.71 ? 100 PRO D CA  1 
ATOM   7203 C  C   . PRO D  1 100 ? 14.170  -6.141  -46.586 1.00 13.30 ? 100 PRO D C   1 
ATOM   7204 O  O   . PRO D  1 100 ? 13.537  -7.068  -46.100 1.00 15.68 ? 100 PRO D O   1 
ATOM   7205 C  CB  . PRO D  1 100 ? 13.570  -6.970  -48.950 1.00 18.98 ? 100 PRO D CB  1 
ATOM   7206 C  CG  . PRO D  1 100 ? 14.664  -8.027  -49.044 1.00 17.83 ? 100 PRO D CG  1 
ATOM   7207 C  CD  . PRO D  1 100 ? 15.989  -7.405  -49.070 1.00 18.01 ? 100 PRO D CD  1 
ATOM   7208 N  N   . HIS D  1 101 ? 14.854  -5.293  -45.806 1.00 13.48 ? 101 HIS D N   1 
ATOM   7209 C  CA  . HIS D  1 101 ? 14.950  -5.440  -44.332 1.00 14.06 ? 101 HIS D CA  1 
ATOM   7210 C  C   . HIS D  1 101 ? 14.901  -4.069  -43.699 1.00 12.51 ? 101 HIS D C   1 
ATOM   7211 O  O   . HIS D  1 101 ? 15.893  -3.616  -43.020 1.00 15.94 ? 101 HIS D O   1 
ATOM   7212 C  CB  . HIS D  1 101 ? 16.270  -6.158  -44.014 1.00 15.74 ? 101 HIS D CB  1 
ATOM   7213 C  CG  . HIS D  1 101 ? 16.303  -7.569  -44.601 1.00 18.99 ? 101 HIS D CG  1 
ATOM   7214 N  ND1 . HIS D  1 101 ? 17.007  -7.884  -45.703 1.00 22.01 ? 101 HIS D ND1 1 
ATOM   7215 C  CD2 . HIS D  1 101 ? 15.687  -8.731  -44.179 1.00 21.28 ? 101 HIS D CD2 1 
ATOM   7216 C  CE1 . HIS D  1 101 ? 16.810  -9.202  -46.015 1.00 22.67 ? 101 HIS D CE1 1 
ATOM   7217 N  NE2 . HIS D  1 101 ? 16.057  -9.732  -45.061 1.00 25.35 ? 101 HIS D NE2 1 
ATOM   7218 N  N   . GLY D  1 102 ? 13.761  -3.426  -43.869 1.00 10.36 ? 102 GLY D N   1 
ATOM   7219 C  CA  . GLY D  1 102 ? 13.588  -2.044  -43.463 1.00 10.48 ? 102 GLY D CA  1 
ATOM   7220 C  C   . GLY D  1 102 ? 12.648  -1.754  -42.347 1.00 9.11  ? 102 GLY D C   1 
ATOM   7221 O  O   . GLY D  1 102 ? 12.151  -0.620  -42.264 1.00 11.25 ? 102 GLY D O   1 
ATOM   7222 N  N   . SER D  1 103 ? 12.384  -2.724  -41.487 1.00 9.71  ? 103 SER D N   1 
ATOM   7223 C  CA  . SER D  1 103 ? 11.666  -2.329  -40.266 1.00 8.97  ? 103 SER D CA  1 
ATOM   7224 C  C   . SER D  1 103 ? 12.515  -1.348  -39.431 1.00 8.95  ? 103 SER D C   1 
ATOM   7225 O  O   . SER D  1 103 ? 13.733  -1.286  -39.565 1.00 11.21 ? 103 SER D O   1 
ATOM   7226 C  CB  . SER D  1 103 ? 11.307  -3.516  -39.395 1.00 9.74  ? 103 SER D CB  1 
ATOM   7227 O  OG  . SER D  1 103 ? 12.510  -4.119  -38.792 1.00 9.10  ? 103 SER D OG  1 
ATOM   7228 N  N   . GLU D  1 104 ? 11.789  -0.562  -38.620 1.00 8.80  ? 104 GLU D N   1 
ATOM   7229 C  CA  . GLU D  1 104 ? 12.484  0.328   -37.668 1.00 8.48  ? 104 GLU D CA  1 
ATOM   7230 C  C   . GLU D  1 104 ? 12.922  -0.361  -36.389 1.00 7.93  ? 104 GLU D C   1 
ATOM   7231 O  O   . GLU D  1 104 ? 14.077  -0.369  -36.064 1.00 8.47  ? 104 GLU D O   1 
ATOM   7232 C  CB  . GLU D  1 104 ? 11.588  1.534   -37.362 1.00 8.71  ? 104 GLU D CB  1 
ATOM   7233 C  CG  . GLU D  1 104 ? 11.193  2.236   -38.661 1.00 9.64  ? 104 GLU D CG  1 
ATOM   7234 C  CD  . GLU D  1 104 ? 11.117  3.713   -38.434 1.00 9.98  ? 104 GLU D CD  1 
ATOM   7235 O  OE1 . GLU D  1 104 ? 10.129  4.181   -37.845 1.00 10.23 ? 104 GLU D OE1 1 
ATOM   7236 O  OE2 . GLU D  1 104 ? 12.114  4.382   -38.780 1.00 10.48 ? 104 GLU D OE2 1 
ATOM   7237 N  N   . HIS D  1 105 ? 11.948  -0.952  -35.706 1.00 8.67  ? 105 HIS D N   1 
ATOM   7238 C  CA  . HIS D  1 105 ? 12.278  -1.816  -34.579 1.00 9.12  ? 105 HIS D CA  1 
ATOM   7239 C  C   . HIS D  1 105 ? 12.906  -3.056  -35.110 1.00 9.48  ? 105 HIS D C   1 
ATOM   7240 O  O   . HIS D  1 105 ? 12.583  -3.613  -36.144 1.00 10.28 ? 105 HIS D O   1 
ATOM   7241 C  CB  . HIS D  1 105 ? 11.040  -2.090  -33.764 1.00 9.00  ? 105 HIS D CB  1 
ATOM   7242 C  CG  . HIS D  1 105 ? 10.525  -0.858  -33.074 1.00 9.97  ? 105 HIS D CG  1 
ATOM   7243 N  ND1 . HIS D  1 105 ? 9.581   -0.060  -33.641 1.00 9.35  ? 105 HIS D ND1 1 
ATOM   7244 C  CD2 . HIS D  1 105 ? 10.844  -0.289  -31.829 1.00 9.13  ? 105 HIS D CD2 1 
ATOM   7245 C  CE1 . HIS D  1 105 ? 9.374   1.013   -32.782 1.00 9.48  ? 105 HIS D CE1 1 
ATOM   7246 N  NE2 . HIS D  1 105 ? 10.127  0.866   -31.714 1.00 10.77 ? 105 HIS D NE2 1 
ATOM   7247 N  N   . THR D  1 106 ? 13.847  -3.572  -34.303 1.00 9.61  ? 106 THR D N   1 
ATOM   7248 C  CA  . THR D  1 106 ? 14.494  -4.871  -34.624 1.00 10.29 ? 106 THR D CA  1 
ATOM   7249 C  C   . THR D  1 106 ? 14.233  -5.796  -33.423 1.00 11.80 ? 106 THR D C   1 
ATOM   7250 O  O   . THR D  1 106 ? 13.968  -5.324  -32.317 1.00 11.14 ? 106 THR D O   1 
ATOM   7251 C  CB  . THR D  1 106 ? 15.956  -4.718  -34.909 1.00 10.47 ? 106 THR D CB  1 
ATOM   7252 O  OG1 . THR D  1 106 ? 16.605  -4.080  -33.756 1.00 11.68 ? 106 THR D OG1 1 
ATOM   7253 C  CG2 . THR D  1 106 ? 16.195  -3.865  -36.137 1.00 11.77 ? 106 THR D CG2 1 
ATOM   7254 N  N   . VAL D  1 107 ? 14.312  -7.105  -33.670 1.00 10.85 ? 107 VAL D N   1 
ATOM   7255 C  CA  . VAL D  1 107 ? 14.097  -8.076  -32.600 1.00 13.30 ? 107 VAL D CA  1 
ATOM   7256 C  C   . VAL D  1 107 ? 15.344  -8.936  -32.543 1.00 13.19 ? 107 VAL D C   1 
ATOM   7257 O  O   . VAL D  1 107 ? 15.733  -9.527  -33.553 1.00 13.86 ? 107 VAL D O   1 
ATOM   7258 C  CB  . VAL D  1 107 ? 12.837  -8.992  -32.827 1.00 12.69 ? 107 VAL D CB  1 
ATOM   7259 C  CG1 . VAL D  1 107 ? 12.758  -9.957  -31.622 1.00 16.49 ? 107 VAL D CG1 1 
ATOM   7260 C  CG2 . VAL D  1 107 ? 11.571  -8.129  -32.840 1.00 14.64 ? 107 VAL D CG2 1 
ATOM   7261 N  N   . SER D  1 108 ? 16.011  -8.888  -31.388 1.00 12.91 ? 108 SER D N   1 
ATOM   7262 C  CA  . SER D  1 108 ? 17.258  -9.727  -31.131 1.00 14.83 ? 108 SER D CA  1 
ATOM   7263 C  C   . SER D  1 108 ? 18.238  -9.428  -32.294 1.00 14.30 ? 108 SER D C   1 
ATOM   7264 O  O   . SER D  1 108 ? 18.881  -10.324 -32.922 1.00 14.54 ? 108 SER D O   1 
ATOM   7265 C  CB  . SER D  1 108 ? 16.889  -11.216 -31.014 1.00 14.81 ? 108 SER D CB  1 
ATOM   7266 O  OG  . SER D  1 108 ? 16.158  -11.426 -29.863 1.00 17.56 ? 108 SER D OG  1 
ATOM   7267 N  N   . GLY D  1 109 ? 18.320  -8.137  -32.604 1.00 12.19 ? 109 GLY D N   1 
ATOM   7268 C  CA  . GLY D  1 109 ? 19.276  -7.648  -33.647 1.00 14.10 ? 109 GLY D CA  1 
ATOM   7269 C  C   . GLY D  1 109 ? 18.880  -7.821  -35.134 1.00 16.19 ? 109 GLY D C   1 
ATOM   7270 O  O   . GLY D  1 109 ? 19.663  -7.401  -36.038 1.00 19.82 ? 109 GLY D O   1 
ATOM   7271 N  N   A GLN D  1 110 ? 17.646  -8.287  -35.356 0.50 13.21 ? 110 GLN D N   1 
ATOM   7272 N  N   B GLN D  1 110 ? 17.694  -8.316  -35.425 0.50 14.19 ? 110 GLN D N   1 
ATOM   7273 C  CA  A GLN D  1 110 ? 17.103  -8.672  -36.681 0.50 14.06 ? 110 GLN D CA  1 
ATOM   7274 C  CA  B GLN D  1 110 ? 17.357  -8.540  -36.826 0.50 15.53 ? 110 GLN D CA  1 
ATOM   7275 C  C   A GLN D  1 110 ? 16.055  -7.691  -37.172 0.50 11.09 ? 110 GLN D C   1 
ATOM   7276 C  C   B GLN D  1 110 ? 16.181  -7.668  -37.174 0.50 12.10 ? 110 GLN D C   1 
ATOM   7277 O  O   A GLN D  1 110 ? 15.040  -7.475  -36.474 0.50 10.72 ? 110 GLN D O   1 
ATOM   7278 O  O   B GLN D  1 110 ? 15.242  -7.505  -36.401 0.50 11.95 ? 110 GLN D O   1 
ATOM   7279 C  CB  A GLN D  1 110 ? 16.489  -10.089 -36.657 0.50 13.41 ? 110 GLN D CB  1 
ATOM   7280 C  CB  B GLN D  1 110 ? 16.968  -10.007 -37.141 0.50 16.98 ? 110 GLN D CB  1 
ATOM   7281 C  CG  A GLN D  1 110 ? 17.447  -11.166 -36.079 0.50 17.90 ? 110 GLN D CG  1 
ATOM   7282 C  CG  B GLN D  1 110 ? 17.728  -11.087 -36.376 0.50 23.41 ? 110 GLN D CG  1 
ATOM   7283 C  CD  A GLN D  1 110 ? 18.895  -11.011 -36.598 0.50 19.26 ? 110 GLN D CD  1 
ATOM   7284 C  CD  B GLN D  1 110 ? 17.813  -12.408 -37.118 0.50 22.99 ? 110 GLN D CD  1 
ATOM   7285 O  OE1 A GLN D  1 110 ? 19.155  -11.122 -37.786 0.50 17.25 ? 110 GLN D OE1 1 
ATOM   7286 O  OE1 B GLN D  1 110 ? 18.640  -13.251 -36.776 0.50 32.10 ? 110 GLN D OE1 1 
ATOM   7287 N  NE2 A GLN D  1 110 ? 19.847  -10.832 -35.677 0.50 20.00 ? 110 GLN D NE2 1 
ATOM   7288 N  NE2 B GLN D  1 110 ? 17.002  -12.582 -38.154 0.50 28.94 ? 110 GLN D NE2 1 
ATOM   7289 N  N   . HIS D  1 111 ? 16.284  -7.115  -38.377 1.00 11.34 ? 111 HIS D N   1 
ATOM   7290 C  CA  . HIS D  1 111 ? 15.189  -6.347  -39.026 1.00 10.95 ? 111 HIS D CA  1 
ATOM   7291 C  C   . HIS D  1 111 ? 14.182  -7.292  -39.609 1.00 12.20 ? 111 HIS D C   1 
ATOM   7292 O  O   . HIS D  1 111 ? 14.538  -8.439  -40.076 1.00 15.64 ? 111 HIS D O   1 
ATOM   7293 C  CB  . HIS D  1 111 ? 15.684  -5.545  -40.215 1.00 12.77 ? 111 HIS D CB  1 
ATOM   7294 C  CG  . HIS D  1 111 ? 16.434  -4.344  -39.824 1.00 11.76 ? 111 HIS D CG  1 
ATOM   7295 N  ND1 . HIS D  1 111 ? 15.785  -3.105  -39.671 1.00 11.92 ? 111 HIS D ND1 1 
ATOM   7296 C  CD2 . HIS D  1 111 ? 17.778  -4.131  -39.599 1.00 13.17 ? 111 HIS D CD2 1 
ATOM   7297 C  CE1 . HIS D  1 111 ? 16.741  -2.198  -39.324 1.00 14.72 ? 111 HIS D CE1 1 
ATOM   7298 N  NE2 . HIS D  1 111 ? 17.933  -2.819  -39.265 1.00 16.85 ? 111 HIS D NE2 1 
ATOM   7299 N  N   . PHE D  1 112 ? 12.941  -6.866  -39.643 1.00 10.61 ? 112 PHE D N   1 
ATOM   7300 C  CA  . PHE D  1 112 ? 11.901  -7.453  -40.417 1.00 10.16 ? 112 PHE D CA  1 
ATOM   7301 C  C   . PHE D  1 112 ? 11.860  -6.678  -41.795 1.00 9.29  ? 112 PHE D C   1 
ATOM   7302 O  O   . PHE D  1 112 ? 12.598  -5.686  -41.962 1.00 9.63  ? 112 PHE D O   1 
ATOM   7303 C  CB  . PHE D  1 112 ? 10.591  -7.345  -39.661 1.00 11.28 ? 112 PHE D CB  1 
ATOM   7304 C  CG  . PHE D  1 112 ? 10.438  -8.401  -38.611 1.00 12.96 ? 112 PHE D CG  1 
ATOM   7305 C  CD1 . PHE D  1 112 ? 11.049  -8.300  -37.361 1.00 15.37 ? 112 PHE D CD1 1 
ATOM   7306 C  CD2 . PHE D  1 112 ? 9.714   -9.530  -38.900 1.00 16.98 ? 112 PHE D CD2 1 
ATOM   7307 C  CE1 . PHE D  1 112 ? 10.903  -9.311  -36.420 1.00 18.14 ? 112 PHE D CE1 1 
ATOM   7308 C  CE2 . PHE D  1 112 ? 9.563   -10.539 -37.979 1.00 19.84 ? 112 PHE D CE2 1 
ATOM   7309 C  CZ  . PHE D  1 112 ? 10.156  -10.434 -36.737 1.00 16.98 ? 112 PHE D CZ  1 
ATOM   7310 N  N   . ALA D  1 113 ? 11.051  -7.174  -42.741 1.00 9.01  ? 113 ALA D N   1 
ATOM   7311 C  CA  . ALA D  1 113 ? 11.043  -6.580  -44.043 1.00 9.91  ? 113 ALA D CA  1 
ATOM   7312 C  C   . ALA D  1 113 ? 10.601  -5.108  -44.044 1.00 9.91  ? 113 ALA D C   1 
ATOM   7313 O  O   . ALA D  1 113 ? 11.090  -4.284  -44.798 1.00 9.70  ? 113 ALA D O   1 
ATOM   7314 C  CB  . ALA D  1 113 ? 10.186  -7.419  -44.994 1.00 10.02 ? 113 ALA D CB  1 
ATOM   7315 N  N   . ALA D  1 114 ? 9.567   -4.860  -43.254 1.00 8.85  ? 114 ALA D N   1 
ATOM   7316 C  CA  . ALA D  1 114 ? 8.943   -3.525  -43.259 1.00 8.28  ? 114 ALA D CA  1 
ATOM   7317 C  C   . ALA D  1 114 ? 8.205   -3.353  -41.918 1.00 8.02  ? 114 ALA D C   1 
ATOM   7318 O  O   . ALA D  1 114 ? 8.187   -4.276  -41.036 1.00 8.12  ? 114 ALA D O   1 
ATOM   7319 C  CB  . ALA D  1 114 ? 7.995   -3.328  -44.446 1.00 8.80  ? 114 ALA D CB  1 
ATOM   7320 N  N   . GLU D  1 115 ? 7.567   -2.177  -41.718 1.00 8.35  ? 115 GLU D N   1 
ATOM   7321 C  CA  . GLU D  1 115 ? 6.862   -1.944  -40.436 1.00 9.01  ? 115 GLU D CA  1 
ATOM   7322 C  C   . GLU D  1 115 ? 5.712   -0.959  -40.728 1.00 8.61  ? 115 GLU D C   1 
ATOM   7323 O  O   . GLU D  1 115 ? 5.897   0.025   -41.479 1.00 8.90  ? 115 GLU D O   1 
ATOM   7324 C  CB  . GLU D  1 115 ? 7.815   -1.343  -39.409 1.00 8.49  ? 115 GLU D CB  1 
ATOM   7325 C  CG  . GLU D  1 115 ? 7.275   -1.205  -38.010 1.00 10.10 ? 115 GLU D CG  1 
ATOM   7326 C  CD  . GLU D  1 115 ? 8.408   -0.948  -37.050 1.00 9.89  ? 115 GLU D CD  1 
ATOM   7327 O  OE1 . GLU D  1 115 ? 9.555   -1.423  -37.174 1.00 9.52  ? 115 GLU D OE1 1 
ATOM   7328 O  OE2 . GLU D  1 115 ? 8.135   -0.298  -35.976 1.00 9.86  ? 115 GLU D OE2 1 
ATOM   7329 N  N   . LEU D  1 116 ? 4.553   -1.252  -40.155 1.00 8.15  ? 116 LEU D N   1 
ATOM   7330 C  CA  . LEU D  1 116 ? 3.360   -0.366  -40.177 1.00 8.10  ? 116 LEU D CA  1 
ATOM   7331 C  C   . LEU D  1 116 ? 3.219   0.327   -38.870 1.00 9.38  ? 116 LEU D C   1 
ATOM   7332 O  O   . LEU D  1 116 ? 3.409   -0.289  -37.800 1.00 8.62  ? 116 LEU D O   1 
ATOM   7333 C  CB  . LEU D  1 116 ? 2.119   -1.280  -40.353 1.00 8.31  ? 116 LEU D CB  1 
ATOM   7334 C  CG  . LEU D  1 116 ? 0.781   -0.488  -40.258 1.00 8.75  ? 116 LEU D CG  1 
ATOM   7335 C  CD1 . LEU D  1 116 ? 0.513   0.335   -41.446 1.00 9.30  ? 116 LEU D CD1 1 
ATOM   7336 C  CD2 . LEU D  1 116 ? -0.323  -1.461  -40.003 1.00 10.73 ? 116 LEU D CD2 1 
ATOM   7337 N  N   . HIS D  1 117 ? 3.012   1.640   -38.960 1.00 8.49  ? 117 HIS D N   1 
ATOM   7338 C  CA  . HIS D  1 117 ? 2.759   2.455   -37.746 1.00 7.14  ? 117 HIS D CA  1 
ATOM   7339 C  C   . HIS D  1 117 ? 1.341   3.029   -37.857 1.00 7.78  ? 117 HIS D C   1 
ATOM   7340 O  O   . HIS D  1 117 ? 0.983   3.703   -38.849 1.00 8.66  ? 117 HIS D O   1 
ATOM   7341 C  CB  . HIS D  1 117 ? 3.723   3.609   -37.635 1.00 8.23  ? 117 HIS D CB  1 
ATOM   7342 C  CG  . HIS D  1 117 ? 5.114   3.136   -37.292 1.00 7.30  ? 117 HIS D CG  1 
ATOM   7343 N  ND1 . HIS D  1 117 ? 6.231   3.815   -37.603 1.00 7.16  ? 117 HIS D ND1 1 
ATOM   7344 C  CD2 . HIS D  1 117 ? 5.528   1.962   -36.668 1.00 9.77  ? 117 HIS D CD2 1 
ATOM   7345 C  CE1 . HIS D  1 117 ? 7.305   3.117   -37.179 1.00 8.10  ? 117 HIS D CE1 1 
ATOM   7346 N  NE2 . HIS D  1 117 ? 6.869   1.987   -36.608 1.00 7.83  ? 117 HIS D NE2 1 
ATOM   7347 N  N   . ILE D  1 118 ? 0.551   2.773   -36.827 1.00 9.20  ? 118 ILE D N   1 
ATOM   7348 C  CA  . ILE D  1 118 ? -0.829  3.394   -36.725 1.00 9.70  ? 118 ILE D CA  1 
ATOM   7349 C  C   . ILE D  1 118 ? -0.771  4.426   -35.643 1.00 9.41  ? 118 ILE D C   1 
ATOM   7350 O  O   . ILE D  1 118 ? -0.584  4.075   -34.429 1.00 10.41 ? 118 ILE D O   1 
ATOM   7351 C  CB  . ILE D  1 118 ? -1.929  2.333   -36.446 1.00 9.34  ? 118 ILE D CB  1 
ATOM   7352 C  CG1 . ILE D  1 118 ? -1.835  1.211   -37.447 1.00 9.75  ? 118 ILE D CG1 1 
ATOM   7353 C  CG2 . ILE D  1 118 ? -3.280  3.089   -36.566 1.00 11.13 ? 118 ILE D CG2 1 
ATOM   7354 C  CD1 . ILE D  1 118 ? -2.865  0.079   -37.157 1.00 12.21 ? 118 ILE D CD1 1 
ATOM   7355 N  N   . VAL D  1 119 ? -0.788  5.713   -36.034 1.00 9.50  ? 119 VAL D N   1 
ATOM   7356 C  CA  . VAL D  1 119 ? -0.541  6.856   -35.147 1.00 10.27 ? 119 VAL D CA  1 
ATOM   7357 C  C   . VAL D  1 119 ? -1.881  7.375   -34.561 1.00 9.59  ? 119 VAL D C   1 
ATOM   7358 O  O   . VAL D  1 119 ? -2.822  7.553   -35.273 1.00 10.60 ? 119 VAL D O   1 
ATOM   7359 C  CB  . VAL D  1 119 ? 0.119   7.958   -35.964 1.00 8.92  ? 119 VAL D CB  1 
ATOM   7360 C  CG1 . VAL D  1 119 ? 0.582   9.093   -34.995 1.00 10.51 ? 119 VAL D CG1 1 
ATOM   7361 C  CG2 . VAL D  1 119 ? 1.372   7.387   -36.692 1.00 9.45  ? 119 VAL D CG2 1 
ATOM   7362 N  N   . HIS D  1 120 ? -1.828  7.535   -33.225 1.00 10.46 ? 120 HIS D N   1 
ATOM   7363 C  CA  . HIS D  1 120 ? -2.944  8.111   -32.442 1.00 10.97 ? 120 HIS D CA  1 
ATOM   7364 C  C   . HIS D  1 120 ? -2.431  9.197   -31.562 1.00 11.25 ? 120 HIS D C   1 
ATOM   7365 O  O   . HIS D  1 120 ? -1.274  9.317   -31.206 1.00 12.80 ? 120 HIS D O   1 
ATOM   7366 C  CB  . HIS D  1 120 ? -3.492  6.989   -31.538 1.00 11.40 ? 120 HIS D CB  1 
ATOM   7367 C  CG  . HIS D  1 120 ? -3.964  5.733   -32.239 1.00 11.15 ? 120 HIS D CG  1 
ATOM   7368 N  ND1 . HIS D  1 120 ? -3.047  4.815   -32.736 1.00 12.42 ? 120 HIS D ND1 1 
ATOM   7369 C  CD2 . HIS D  1 120 ? -5.202  5.170   -32.388 1.00 11.42 ? 120 HIS D CD2 1 
ATOM   7370 C  CE1 . HIS D  1 120 ? -3.728  3.744   -33.216 1.00 11.61 ? 120 HIS D CE1 1 
ATOM   7371 N  NE2 . HIS D  1 120 ? -5.059  3.905   -33.013 1.00 13.40 ? 120 HIS D NE2 1 
ATOM   7372 N  N   . TYR D  1 121 ? -3.377  10.124  -31.214 1.00 12.81 ? 121 TYR D N   1 
ATOM   7373 C  CA  . TYR D  1 121 ? -3.034  11.235  -30.334 1.00 13.00 ? 121 TYR D CA  1 
ATOM   7374 C  C   . TYR D  1 121 ? -4.012  11.223  -29.122 1.00 13.40 ? 121 TYR D C   1 
ATOM   7375 O  O   . TYR D  1 121 ? -5.093  10.693  -29.210 1.00 12.15 ? 121 TYR D O   1 
ATOM   7376 C  CB  . TYR D  1 121 ? -3.170  12.586  -31.125 1.00 13.30 ? 121 TYR D CB  1 
ATOM   7377 C  CG  . TYR D  1 121 ? -4.540  13.026  -31.480 1.00 13.51 ? 121 TYR D CG  1 
ATOM   7378 C  CD1 . TYR D  1 121 ? -5.212  12.522  -32.580 1.00 15.34 ? 121 TYR D CD1 1 
ATOM   7379 C  CD2 . TYR D  1 121 ? -5.186  14.003  -30.724 1.00 14.95 ? 121 TYR D CD2 1 
ATOM   7380 C  CE1 . TYR D  1 121 ? -6.490  12.863  -32.905 1.00 15.58 ? 121 TYR D CE1 1 
ATOM   7381 C  CE2 . TYR D  1 121 ? -6.492  14.326  -31.062 1.00 16.66 ? 121 TYR D CE2 1 
ATOM   7382 C  CZ  . TYR D  1 121 ? -7.125  13.756  -32.126 1.00 18.70 ? 121 TYR D CZ  1 
ATOM   7383 O  OH  . TYR D  1 121 ? -8.384  14.178  -32.453 1.00 22.41 ? 121 TYR D OH  1 
ATOM   7384 N  N   . ASN D  1 122 ? -3.521  11.932  -28.096 1.00 14.00 ? 122 ASN D N   1 
ATOM   7385 C  CA  . ASN D  1 122 ? -4.223  12.047  -26.743 1.00 15.50 ? 122 ASN D CA  1 
ATOM   7386 C  C   . ASN D  1 122 ? -5.373  13.072  -26.899 1.00 15.51 ? 122 ASN D C   1 
ATOM   7387 O  O   . ASN D  1 122 ? -5.118  14.279  -26.755 1.00 16.17 ? 122 ASN D O   1 
ATOM   7388 C  CB  . ASN D  1 122 ? -3.230  12.333  -25.658 1.00 15.44 ? 122 ASN D CB  1 
ATOM   7389 C  CG  . ASN D  1 122 ? -3.850  12.190  -24.277 1.00 15.62 ? 122 ASN D CG  1 
ATOM   7390 O  OD1 . ASN D  1 122 ? -5.064  12.318  -24.159 1.00 16.35 ? 122 ASN D OD1 1 
ATOM   7391 N  ND2 . ASN D  1 122 ? -3.012  11.945  -23.294 1.00 19.98 ? 122 ASN D ND2 1 
ATOM   7392 N  N   . SER D  1 123 ? -6.503  12.568  -27.285 1.00 14.88 ? 123 SER D N   1 
ATOM   7393 C  CA  . SER D  1 123 ? -7.684  13.434  -27.474 1.00 16.91 ? 123 SER D CA  1 
ATOM   7394 C  C   . SER D  1 123 ? -8.330  13.826  -26.169 1.00 18.39 ? 123 SER D C   1 
ATOM   7395 O  O   . SER D  1 123 ? -9.220  14.717  -26.153 1.00 21.40 ? 123 SER D O   1 
ATOM   7396 C  CB  . SER D  1 123 ? -8.623  12.868  -28.477 1.00 15.57 ? 123 SER D CB  1 
ATOM   7397 O  OG  . SER D  1 123 ? -9.049  11.490  -28.133 1.00 17.62 ? 123 SER D OG  1 
ATOM   7398 N  N   . ASP D  1 124 ? -7.900  13.247  -25.075 1.00 16.33 ? 124 ASP D N   1 
ATOM   7399 C  CA  . ASP D  1 124 ? -8.461  13.756  -23.757 1.00 18.41 ? 124 ASP D CA  1 
ATOM   7400 C  C   . ASP D  1 124 ? -7.742  15.088  -23.411 1.00 21.03 ? 124 ASP D C   1 
ATOM   7401 O  O   . ASP D  1 124 ? -8.255  15.917  -22.623 1.00 24.16 ? 124 ASP D O   1 
ATOM   7402 C  CB  . ASP D  1 124 ? -8.124  12.791  -22.624 1.00 19.71 ? 124 ASP D CB  1 
ATOM   7403 C  CG  . ASP D  1 124 ? -8.953  11.530  -22.646 1.00 19.34 ? 124 ASP D CG  1 
ATOM   7404 O  OD1 . ASP D  1 124 ? -9.938  11.478  -23.407 1.00 18.46 ? 124 ASP D OD1 1 
ATOM   7405 O  OD2 . ASP D  1 124 ? -8.613  10.600  -21.892 1.00 21.60 ? 124 ASP D OD2 1 
ATOM   7406 N  N   . LEU D  1 125 ? -6.556  15.280  -23.841 1.00 16.64 ? 125 LEU D N   1 
ATOM   7407 C  CA  . LEU D  1 125 ? -5.720  16.371  -23.420 1.00 18.00 ? 125 LEU D CA  1 
ATOM   7408 C  C   . LEU D  1 125 ? -5.660  17.394  -24.556 1.00 19.03 ? 125 LEU D C   1 
ATOM   7409 O  O   . LEU D  1 125 ? -5.557  18.578  -24.307 1.00 20.25 ? 125 LEU D O   1 
ATOM   7410 C  CB  . LEU D  1 125 ? -4.298  15.921  -23.076 1.00 19.35 ? 125 LEU D CB  1 
ATOM   7411 C  CG  . LEU D  1 125 ? -3.998  15.506  -21.617 1.00 22.43 ? 125 LEU D CG  1 
ATOM   7412 C  CD1 . LEU D  1 125 ? -4.873  14.322  -21.206 1.00 24.49 ? 125 LEU D CD1 1 
ATOM   7413 C  CD2 . LEU D  1 125 ? -2.535  15.191  -21.502 1.00 22.83 ? 125 LEU D CD2 1 
ATOM   7414 N  N   . TYR D  1 126 ? -5.676  16.956  -25.828 1.00 17.13 ? 126 TYR D N   1 
ATOM   7415 C  CA  . TYR D  1 126 ? -5.329  17.808  -26.937 1.00 17.39 ? 126 TYR D CA  1 
ATOM   7416 C  C   . TYR D  1 126 ? -6.392  17.785  -28.051 1.00 15.64 ? 126 TYR D C   1 
ATOM   7417 O  O   . TYR D  1 126 ? -7.122  16.824  -28.290 1.00 17.15 ? 126 TYR D O   1 
ATOM   7418 C  CB  . TYR D  1 126 ? -3.983  17.352  -27.547 1.00 15.62 ? 126 TYR D CB  1 
ATOM   7419 C  CG  . TYR D  1 126 ? -2.932  17.360  -26.486 1.00 15.41 ? 126 TYR D CG  1 
ATOM   7420 C  CD1 . TYR D  1 126 ? -2.593  18.554  -25.754 1.00 17.57 ? 126 TYR D CD1 1 
ATOM   7421 C  CD2 . TYR D  1 126 ? -2.283  16.159  -26.084 1.00 16.24 ? 126 TYR D CD2 1 
ATOM   7422 C  CE1 . TYR D  1 126 ? -1.649  18.515  -24.712 1.00 17.03 ? 126 TYR D CE1 1 
ATOM   7423 C  CE2 . TYR D  1 126 ? -1.372  16.087  -25.053 1.00 17.02 ? 126 TYR D CE2 1 
ATOM   7424 C  CZ  . TYR D  1 126 ? -1.039  17.265  -24.341 1.00 17.00 ? 126 TYR D CZ  1 
ATOM   7425 O  OH  . TYR D  1 126 ? -0.107  17.245  -23.314 1.00 17.10 ? 126 TYR D OH  1 
ATOM   7426 N  N   . PRO D  1 127 ? -6.453  18.932  -28.803 1.00 16.49 ? 127 PRO D N   1 
ATOM   7427 C  CA  . PRO D  1 127 ? -7.579  19.027  -29.747 1.00 18.30 ? 127 PRO D CA  1 
ATOM   7428 C  C   . PRO D  1 127 ? -7.341  18.424  -31.089 1.00 19.76 ? 127 PRO D C   1 
ATOM   7429 O  O   . PRO D  1 127 ? -8.260  18.278  -31.867 1.00 22.32 ? 127 PRO D O   1 
ATOM   7430 C  CB  . PRO D  1 127 ? -7.752  20.570  -29.937 1.00 20.99 ? 127 PRO D CB  1 
ATOM   7431 C  CG  . PRO D  1 127 ? -6.406  21.131  -29.572 1.00 18.84 ? 127 PRO D CG  1 
ATOM   7432 C  CD  . PRO D  1 127 ? -5.834  20.221  -28.456 1.00 18.15 ? 127 PRO D CD  1 
ATOM   7433 N  N   . ASP D  1 128 ? -6.110  18.022  -31.343 1.00 17.02 ? 128 ASP D N   1 
ATOM   7434 C  CA  . ASP D  1 128 ? -5.721  17.465  -32.646 1.00 15.43 ? 128 ASP D CA  1 
ATOM   7435 C  C   . ASP D  1 128 ? -4.310  16.935  -32.546 1.00 16.04 ? 128 ASP D C   1 
ATOM   7436 O  O   . ASP D  1 128 ? -3.580  17.206  -31.605 1.00 16.44 ? 128 ASP D O   1 
ATOM   7437 C  CB  . ASP D  1 128 ? -5.802  18.579  -33.745 1.00 19.49 ? 128 ASP D CB  1 
ATOM   7438 C  CG  . ASP D  1 128 ? -4.914  19.722  -33.448 1.00 20.14 ? 128 ASP D CG  1 
ATOM   7439 O  OD1 . ASP D  1 128 ? -5.347  20.756  -32.782 1.00 25.91 ? 128 ASP D OD1 1 
ATOM   7440 O  OD2 . ASP D  1 128 ? -3.806  19.674  -33.894 1.00 22.54 ? 128 ASP D OD2 1 
ATOM   7441 N  N   . ALA D  1 129 ? -3.874  16.166  -33.545 1.00 14.32 ? 129 ALA D N   1 
ATOM   7442 C  CA  . ALA D  1 129 ? -2.639  15.456  -33.434 1.00 13.94 ? 129 ALA D CA  1 
ATOM   7443 C  C   . ALA D  1 129 ? -1.452  16.378  -33.496 1.00 14.13 ? 129 ALA D C   1 
ATOM   7444 O  O   . ALA D  1 129 ? -0.398  16.132  -32.889 1.00 15.25 ? 129 ALA D O   1 
ATOM   7445 C  CB  . ALA D  1 129 ? -2.558  14.364  -34.530 1.00 17.89 ? 129 ALA D CB  1 
ATOM   7446 N  N   . SER D  1 130 ? -1.564  17.398  -34.383 1.00 16.44 ? 130 SER D N   1 
ATOM   7447 C  CA  . SER D  1 130 ? -0.465  18.344  -34.519 1.00 15.93 ? 130 SER D CA  1 
ATOM   7448 C  C   . SER D  1 130 ? -0.195  19.048  -33.173 1.00 15.80 ? 130 SER D C   1 
ATOM   7449 O  O   . SER D  1 130 ? 0.939   19.060  -32.690 1.00 16.68 ? 130 SER D O   1 
ATOM   7450 C  CB  . SER D  1 130 ? -0.731  19.357  -35.653 1.00 18.98 ? 130 SER D CB  1 
ATOM   7451 O  OG  . SER D  1 130 ? 0.423   20.188  -35.757 1.00 27.51 ? 130 SER D OG  1 
ATOM   7452 N  N   . THR D  1 131 ? -1.242  19.491  -32.532 1.00 16.53 ? 131 THR D N   1 
ATOM   7453 C  CA  . THR D  1 131 ? -1.039  20.116  -31.189 1.00 15.47 ? 131 THR D CA  1 
ATOM   7454 C  C   . THR D  1 131 ? -0.471  19.152  -30.112 1.00 16.66 ? 131 THR D C   1 
ATOM   7455 O  O   . THR D  1 131 ? 0.421   19.473  -29.295 1.00 18.00 ? 131 THR D O   1 
ATOM   7456 C  CB  . THR D  1 131 ? -2.359  20.699  -30.700 1.00 18.24 ? 131 THR D CB  1 
ATOM   7457 O  OG1 . THR D  1 131 ? -2.884  21.677  -31.622 1.00 20.61 ? 131 THR D OG1 1 
ATOM   7458 C  CG2 . THR D  1 131 ? -2.191  21.419  -29.302 1.00 20.73 ? 131 THR D CG2 1 
ATOM   7459 N  N   . ALA D  1 132 ? -0.938  17.941  -30.197 1.00 15.86 ? 132 ALA D N   1 
ATOM   7460 C  CA  . ALA D  1 132 ? -0.490  16.885  -29.292 1.00 15.01 ? 132 ALA D CA  1 
ATOM   7461 C  C   . ALA D  1 132 ? 0.960   16.440  -29.461 1.00 14.88 ? 132 ALA D C   1 
ATOM   7462 O  O   . ALA D  1 132 ? 1.678   16.023  -28.556 1.00 14.65 ? 132 ALA D O   1 
ATOM   7463 C  CB  . ALA D  1 132 ? -1.353  15.664  -29.523 1.00 15.63 ? 132 ALA D CB  1 
ATOM   7464 N  N   . SER D  1 133 ? 1.462   16.609  -30.692 1.00 14.70 ? 133 SER D N   1 
ATOM   7465 C  CA  . SER D  1 133 ? 2.679   15.960  -31.050 1.00 14.34 ? 133 SER D CA  1 
ATOM   7466 C  C   . SER D  1 133 ? 3.956   16.349  -30.277 1.00 15.53 ? 133 SER D C   1 
ATOM   7467 O  O   . SER D  1 133 ? 4.890   15.552  -30.135 1.00 15.83 ? 133 SER D O   1 
ATOM   7468 C  CB  . SER D  1 133 ? 2.909   16.185  -32.574 1.00 16.76 ? 133 SER D CB  1 
ATOM   7469 O  OG  . SER D  1 133 ? 3.424   17.476  -32.882 1.00 20.84 ? 133 SER D OG  1 
ATOM   7470 N  N   . ASN D  1 134 ? 4.020   17.587  -29.752 1.00 14.57 ? 134 ASN D N   1 
ATOM   7471 C  CA  . ASN D  1 134 ? 5.169   17.994  -29.001 1.00 16.56 ? 134 ASN D CA  1 
ATOM   7472 C  C   . ASN D  1 134 ? 4.853   18.164  -27.558 1.00 18.36 ? 134 ASN D C   1 
ATOM   7473 O  O   . ASN D  1 134 ? 5.663   18.809  -26.824 1.00 19.63 ? 134 ASN D O   1 
ATOM   7474 C  CB  . ASN D  1 134 ? 5.882   19.282  -29.531 1.00 18.36 ? 134 ASN D CB  1 
ATOM   7475 C  CG  . ASN D  1 134 ? 4.976   20.498  -29.424 1.00 20.80 ? 134 ASN D CG  1 
ATOM   7476 O  OD1 . ASN D  1 134 ? 3.728   20.401  -29.363 1.00 20.53 ? 134 ASN D OD1 1 
ATOM   7477 N  ND2 . ASN D  1 134 ? 5.620   21.684  -29.427 1.00 23.97 ? 134 ASN D ND2 1 
ATOM   7478 N  N   . LYS D  1 135 ? 3.784   17.542  -27.121 1.00 15.07 ? 135 LYS D N   1 
ATOM   7479 C  CA  . LYS D  1 135 ? 3.395   17.744  -25.700 1.00 16.41 ? 135 LYS D CA  1 
ATOM   7480 C  C   . LYS D  1 135 ? 3.291   16.440  -24.939 1.00 17.07 ? 135 LYS D C   1 
ATOM   7481 O  O   . LYS D  1 135 ? 3.277   15.305  -25.497 1.00 16.62 ? 135 LYS D O   1 
ATOM   7482 C  CB  . LYS D  1 135 ? 2.037   18.480  -25.737 1.00 18.01 ? 135 LYS D CB  1 
ATOM   7483 C  CG  . LYS D  1 135 ? 2.194   19.936  -26.266 1.00 17.16 ? 135 LYS D CG  1 
ATOM   7484 C  CD  . LYS D  1 135 ? 0.888   20.713  -26.217 1.00 19.85 ? 135 LYS D CD  1 
ATOM   7485 C  CE  . LYS D  1 135 ? 1.151   22.044  -26.951 1.00 19.40 ? 135 LYS D CE  1 
ATOM   7486 N  NZ  . LYS D  1 135 ? 1.504   21.899  -28.433 1.00 20.62 ? 135 LYS D NZ  1 
ATOM   7487 N  N   . SER D  1 136 ? 3.333   16.570  -23.614 1.00 17.49 ? 136 SER D N   1 
ATOM   7488 C  CA  . SER D  1 136 ? 3.399   15.393  -22.734 1.00 16.19 ? 136 SER D CA  1 
ATOM   7489 C  C   . SER D  1 136 ? 2.248   14.441  -22.958 1.00 14.70 ? 136 SER D C   1 
ATOM   7490 O  O   . SER D  1 136 ? 1.084   14.809  -23.114 1.00 15.15 ? 136 SER D O   1 
ATOM   7491 C  CB  . SER D  1 136 ? 3.256   15.971  -21.314 1.00 18.52 ? 136 SER D CB  1 
ATOM   7492 O  OG  . SER D  1 136 ? 3.587   14.925  -20.382 1.00 25.06 ? 136 SER D OG  1 
ATOM   7493 N  N   . GLU D  1 137 ? 2.616   13.133  -23.028 1.00 14.83 ? 137 GLU D N   1 
ATOM   7494 C  CA  . GLU D  1 137 ? 1.623   12.142  -23.220 1.00 16.51 ? 137 GLU D CA  1 
ATOM   7495 C  C   . GLU D  1 137 ? 0.832   12.262  -24.562 1.00 12.86 ? 137 GLU D C   1 
ATOM   7496 O  O   . GLU D  1 137 ? -0.286  11.876  -24.685 1.00 16.53 ? 137 GLU D O   1 
ATOM   7497 C  CB  . GLU D  1 137 ? 0.621   12.040  -22.022 1.00 20.02 ? 137 GLU D CB  1 
ATOM   7498 C  CG  . GLU D  1 137 ? 1.259   11.901  -20.644 1.00 22.56 ? 137 GLU D CG  1 
ATOM   7499 C  CD  . GLU D  1 137 ? 1.969   10.541  -20.408 1.00 26.35 ? 137 GLU D CD  1 
ATOM   7500 O  OE1 . GLU D  1 137 ? 1.982   9.655   -21.274 1.00 35.08 ? 137 GLU D OE1 1 
ATOM   7501 O  OE2 . GLU D  1 137 ? 2.470   10.300  -19.307 1.00 34.58 ? 137 GLU D OE2 1 
ATOM   7502 N  N   . GLY D  1 138 ? 1.482   12.931  -25.522 1.00 15.58 ? 138 GLY D N   1 
ATOM   7503 C  CA  . GLY D  1 138 ? 0.688   13.385  -26.645 1.00 14.97 ? 138 GLY D CA  1 
ATOM   7504 C  C   . GLY D  1 138 ? 0.261   12.264  -27.654 1.00 11.90 ? 138 GLY D C   1 
ATOM   7505 O  O   . GLY D  1 138 ? -0.773  12.349  -28.260 1.00 12.74 ? 138 GLY D O   1 
ATOM   7506 N  N   . LEU D  1 139 ? 1.129   11.218  -27.801 1.00 11.72 ? 139 LEU D N   1 
ATOM   7507 C  CA  . LEU D  1 139 ? 0.889   10.274  -28.970 1.00 12.33 ? 139 LEU D CA  1 
ATOM   7508 C  C   . LEU D  1 139 ? 1.035   8.814   -28.498 1.00 11.44 ? 139 LEU D C   1 
ATOM   7509 O  O   . LEU D  1 139 ? 1.747   8.561   -27.514 1.00 12.56 ? 139 LEU D O   1 
ATOM   7510 C  CB  . LEU D  1 139 ? 1.936   10.542  -30.104 1.00 13.00 ? 139 LEU D CB  1 
ATOM   7511 C  CG  . LEU D  1 139 ? 1.932   11.970  -30.698 1.00 13.32 ? 139 LEU D CG  1 
ATOM   7512 C  CD1 . LEU D  1 139 ? 3.143   12.065  -31.651 1.00 15.46 ? 139 LEU D CD1 1 
ATOM   7513 C  CD2 . LEU D  1 139 ? 0.555   12.245  -31.318 1.00 14.96 ? 139 LEU D CD2 1 
ATOM   7514 N  N   . ALA D  1 140 ? 0.358   7.935   -29.220 1.00 11.52 ? 140 ALA D N   1 
ATOM   7515 C  CA  . ALA D  1 140 ? 0.520   6.503   -29.010 1.00 10.88 ? 140 ALA D CA  1 
ATOM   7516 C  C   . ALA D  1 140 ? 0.548   5.945   -30.432 1.00 10.59 ? 140 ALA D C   1 
ATOM   7517 O  O   . ALA D  1 140 ? -0.318  6.169   -31.238 1.00 12.14 ? 140 ALA D O   1 
ATOM   7518 C  CB  . ALA D  1 140 ? -0.643  5.930   -28.264 1.00 13.04 ? 140 ALA D CB  1 
ATOM   7519 N  N   . VAL D  1 141 ? 1.585   5.151   -30.691 1.00 10.54 ? 141 VAL D N   1 
ATOM   7520 C  CA  . VAL D  1 141 ? 1.710   4.498   -32.005 1.00 10.96 ? 141 VAL D CA  1 
ATOM   7521 C  C   . VAL D  1 141 ? 1.667   2.965   -31.813 1.00 9.64  ? 141 VAL D C   1 
ATOM   7522 O  O   . VAL D  1 141 ? 2.375   2.466   -30.889 1.00 11.52 ? 141 VAL D O   1 
ATOM   7523 C  CB  . VAL D  1 141 ? 3.031   4.944   -32.678 1.00 9.17  ? 141 VAL D CB  1 
ATOM   7524 C  CG1 . VAL D  1 141 ? 3.130   4.281   -34.098 1.00 10.55 ? 141 VAL D CG1 1 
ATOM   7525 C  CG2 . VAL D  1 141 ? 3.052   6.492   -32.858 1.00 10.12 ? 141 VAL D CG2 1 
ATOM   7526 N  N   . LEU D  1 142 ? 0.957   2.296   -32.667 1.00 9.67  ? 142 LEU D N   1 
ATOM   7527 C  CA  . LEU D  1 142 ? 0.937   0.839   -32.751 1.00 10.19 ? 142 LEU D CA  1 
ATOM   7528 C  C   . LEU D  1 142 ? 1.871   0.466   -33.899 1.00 10.08 ? 142 LEU D C   1 
ATOM   7529 O  O   . LEU D  1 142 ? 1.809   1.029   -34.989 1.00 10.96 ? 142 LEU D O   1 
ATOM   7530 C  CB  . LEU D  1 142 ? -0.442  0.327   -33.092 1.00 11.15 ? 142 LEU D CB  1 
ATOM   7531 C  CG  . LEU D  1 142 ? -1.576  0.706   -32.117 1.00 11.54 ? 142 LEU D CG  1 
ATOM   7532 C  CD1 . LEU D  1 142 ? -2.841  0.011   -32.554 1.00 12.97 ? 142 LEU D CD1 1 
ATOM   7533 C  CD2 . LEU D  1 142 ? -1.263  0.344   -30.650 1.00 13.12 ? 142 LEU D CD2 1 
ATOM   7534 N  N   . ALA D  1 143 ? 2.762   -0.462  -33.610 1.00 10.55 ? 143 ALA D N   1 
ATOM   7535 C  CA  . ALA D  1 143 ? 3.747   -0.957  -34.648 1.00 9.26  ? 143 ALA D CA  1 
ATOM   7536 C  C   . ALA D  1 143 ? 3.487   -2.397  -34.935 1.00 10.35 ? 143 ALA D C   1 
ATOM   7537 O  O   . ALA D  1 143 ? 3.476   -3.247  -34.012 1.00 10.04 ? 143 ALA D O   1 
ATOM   7538 C  CB  . ALA D  1 143 ? 5.165   -0.752  -34.150 1.00 9.45  ? 143 ALA D CB  1 
ATOM   7539 N  N   . VAL D  1 144 ? 3.354   -2.674  -36.214 1.00 9.15  ? 144 VAL D N   1 
ATOM   7540 C  CA  . VAL D  1 144 ? 3.210   -4.084  -36.674 1.00 9.55  ? 144 VAL D CA  1 
ATOM   7541 C  C   . VAL D  1 144 ? 4.451   -4.367  -37.558 1.00 9.27  ? 144 VAL D C   1 
ATOM   7542 O  O   . VAL D  1 144 ? 4.749   -3.709  -38.547 1.00 9.44  ? 144 VAL D O   1 
ATOM   7543 C  CB  . VAL D  1 144 ? 1.993   -4.221  -37.548 1.00 9.22  ? 144 VAL D CB  1 
ATOM   7544 C  CG1 . VAL D  1 144 ? 1.836   -5.681  -38.033 1.00 11.40 ? 144 VAL D CG1 1 
ATOM   7545 C  CG2 . VAL D  1 144 ? 0.709   -3.829  -36.798 1.00 10.67 ? 144 VAL D CG2 1 
ATOM   7546 N  N   . LEU D  1 145 ? 5.221   -5.372  -37.132 1.00 9.73  ? 145 LEU D N   1 
ATOM   7547 C  CA  . LEU D  1 145 ? 6.388   -5.910  -37.881 1.00 9.72  ? 145 LEU D CA  1 
ATOM   7548 C  C   . LEU D  1 145 ? 5.926   -6.706  -39.062 1.00 8.63  ? 145 LEU D C   1 
ATOM   7549 O  O   . LEU D  1 145 ? 4.932   -7.457  -38.925 1.00 9.80  ? 145 LEU D O   1 
ATOM   7550 C  CB  . LEU D  1 145 ? 7.249   -6.780  -36.971 1.00 11.18 ? 145 LEU D CB  1 
ATOM   7551 C  CG  . LEU D  1 145 ? 7.767   -5.994  -35.781 1.00 11.69 ? 145 LEU D CG  1 
ATOM   7552 C  CD1 . LEU D  1 145 ? 8.303   -6.922  -34.680 1.00 14.32 ? 145 LEU D CD1 1 
ATOM   7553 C  CD2 . LEU D  1 145 ? 8.867   -5.051  -36.190 1.00 14.34 ? 145 LEU D CD2 1 
ATOM   7554 N  N   . ILE D  1 146 ? 6.496   -6.477  -40.223 1.00 8.92  ? 146 ILE D N   1 
ATOM   7555 C  CA  . ILE D  1 146 ? 6.046   -7.121  -41.442 1.00 9.33  ? 146 ILE D CA  1 
ATOM   7556 C  C   . ILE D  1 146 ? 7.160   -7.967  -42.015 1.00 9.96  ? 146 ILE D C   1 
ATOM   7557 O  O   . ILE D  1 146 ? 8.277   -7.506  -42.244 1.00 10.11 ? 146 ILE D O   1 
ATOM   7558 C  CB  . ILE D  1 146 ? 5.635   -6.066  -42.478 1.00 8.89  ? 146 ILE D CB  1 
ATOM   7559 C  CG1 . ILE D  1 146 ? 4.450   -5.185  -41.992 1.00 10.95 ? 146 ILE D CG1 1 
ATOM   7560 C  CG2 . ILE D  1 146 ? 5.293   -6.733  -43.818 1.00 9.92  ? 146 ILE D CG2 1 
ATOM   7561 C  CD1 . ILE D  1 146 ? 4.190   -3.952  -42.911 1.00 10.32 ? 146 ILE D CD1 1 
ATOM   7562 N  N   A GLU D  1 147 ? 6.910   -9.288  -42.113 0.50 10.25 ? 147 GLU D N   1 
ATOM   7563 N  N   B GLU D  1 147 ? 6.814   -9.248  -42.251 0.50 10.49 ? 147 GLU D N   1 
ATOM   7564 C  CA  A GLU D  1 147 ? 7.941   -10.198 -42.697 0.50 10.95 ? 147 GLU D CA  1 
ATOM   7565 C  CA  B GLU D  1 147 ? 7.760   -10.251 -42.761 0.50 11.29 ? 147 GLU D CA  1 
ATOM   7566 C  C   A GLU D  1 147 ? 7.509   -10.621 -44.097 0.50 10.23 ? 147 GLU D C   1 
ATOM   7567 C  C   B GLU D  1 147 ? 7.445   -10.542 -44.216 0.50 10.48 ? 147 GLU D C   1 
ATOM   7568 O  O   A GLU D  1 147 ? 6.321   -10.723 -44.381 0.50 9.68  ? 147 GLU D O   1 
ATOM   7569 O  O   B GLU D  1 147 ? 6.283   -10.478 -44.673 0.50 10.46 ? 147 GLU D O   1 
ATOM   7570 C  CB  A GLU D  1 147 ? 8.114   -11.440 -41.796 0.50 12.97 ? 147 GLU D CB  1 
ATOM   7571 C  CB  B GLU D  1 147 ? 7.571   -11.538 -41.951 0.50 12.73 ? 147 GLU D CB  1 
ATOM   7572 C  CG  A GLU D  1 147 ? 7.004   -12.492 -41.920 0.50 17.03 ? 147 GLU D CG  1 
ATOM   7573 C  CG  B GLU D  1 147 ? 8.550   -12.659 -42.273 0.50 15.51 ? 147 GLU D CG  1 
ATOM   7574 C  CD  A GLU D  1 147 ? 7.074   -13.662 -40.858 0.50 17.64 ? 147 GLU D CD  1 
ATOM   7575 C  CD  B GLU D  1 147 ? 8.816   -13.550 -41.049 0.50 20.54 ? 147 GLU D CD  1 
ATOM   7576 O  OE1 A GLU D  1 147 ? 7.987   -13.698 -40.036 0.50 18.76 ? 147 GLU D OE1 1 
ATOM   7577 O  OE1 B GLU D  1 147 ? 8.416   -13.162 -39.935 0.50 24.28 ? 147 GLU D OE1 1 
ATOM   7578 O  OE2 A GLU D  1 147 ? 6.158   -14.531 -40.752 0.50 21.16 ? 147 GLU D OE2 1 
ATOM   7579 O  OE2 B GLU D  1 147 ? 9.426   -14.614 -41.193 0.50 23.32 ? 147 GLU D OE2 1 
ATOM   7580 N  N   . MET D  1 148 ? 8.487   -10.873 -44.990 1.00 11.78 ? 148 MET D N   1 
ATOM   7581 C  CA  . MET D  1 148 ? 8.190   -11.435 -46.312 1.00 11.64 ? 148 MET D CA  1 
ATOM   7582 C  C   . MET D  1 148 ? 7.571   -12.833 -46.197 1.00 11.52 ? 148 MET D C   1 
ATOM   7583 O  O   . MET D  1 148 ? 8.182   -13.709 -45.592 1.00 12.32 ? 148 MET D O   1 
ATOM   7584 C  CB  . MET D  1 148 ? 9.484   -11.503 -47.119 1.00 13.69 ? 148 MET D CB  1 
ATOM   7585 C  CG  . MET D  1 148 ? 9.279   -11.860 -48.534 1.00 14.61 ? 148 MET D CG  1 
ATOM   7586 S  SD  . MET D  1 148 ? 10.841  -11.957 -49.512 1.00 16.62 ? 148 MET D SD  1 
ATOM   7587 C  CE  . MET D  1 148 ? 11.366  -10.224 -49.487 1.00 16.32 ? 148 MET D CE  1 
ATOM   7588 N  N   . GLY D  1 149 ? 6.424   -12.985 -46.819 1.00 10.60 ? 149 GLY D N   1 
ATOM   7589 C  CA  . GLY D  1 149 ? 5.656   -14.234 -46.722 1.00 11.24 ? 149 GLY D CA  1 
ATOM   7590 C  C   . GLY D  1 149 ? 4.566   -14.314 -47.760 1.00 10.40 ? 149 GLY D C   1 
ATOM   7591 O  O   . GLY D  1 149 ? 4.774   -14.094 -48.968 1.00 11.50 ? 149 GLY D O   1 
ATOM   7592 N  N   . SER D  1 150 ? 3.393   -14.701 -47.306 1.00 10.48 ? 150 SER D N   1 
ATOM   7593 C  CA  . SER D  1 150 ? 2.205   -14.819 -48.195 1.00 11.41 ? 150 SER D CA  1 
ATOM   7594 C  C   . SER D  1 150 ? 1.626   -13.447 -48.590 1.00 12.35 ? 150 SER D C   1 
ATOM   7595 O  O   . SER D  1 150 ? 1.714   -12.488 -47.794 1.00 12.03 ? 150 SER D O   1 
ATOM   7596 C  CB  . SER D  1 150 ? 1.117   -15.599 -47.507 1.00 12.34 ? 150 SER D CB  1 
ATOM   7597 O  OG  . SER D  1 150 ? 1.569   -16.982 -47.350 1.00 12.31 ? 150 SER D OG  1 
ATOM   7598 N  N   . PHE D  1 151 ? 1.019   -13.425 -49.776 1.00 12.76 ? 151 PHE D N   1 
ATOM   7599 C  CA  . PHE D  1 151 ? 0.228   -12.274 -50.232 1.00 11.60 ? 151 PHE D CA  1 
ATOM   7600 C  C   . PHE D  1 151 ? -0.790  -11.942 -49.175 1.00 11.78 ? 151 PHE D C   1 
ATOM   7601 O  O   . PHE D  1 151 ? -1.483  -12.816 -48.612 1.00 13.27 ? 151 PHE D O   1 
ATOM   7602 C  CB  . PHE D  1 151 ? -0.438  -12.615 -51.538 1.00 11.48 ? 151 PHE D CB  1 
ATOM   7603 C  CG  . PHE D  1 151 ? -1.239  -11.476 -52.069 1.00 12.60 ? 151 PHE D CG  1 
ATOM   7604 C  CD1 . PHE D  1 151 ? -0.618  -10.428 -52.729 1.00 13.12 ? 151 PHE D CD1 1 
ATOM   7605 C  CD2 . PHE D  1 151 ? -2.600  -11.507 -51.926 1.00 14.68 ? 151 PHE D CD2 1 
ATOM   7606 C  CE1 . PHE D  1 151 ? -1.425  -9.322  -53.183 1.00 13.59 ? 151 PHE D CE1 1 
ATOM   7607 C  CE2 . PHE D  1 151 ? -3.404  -10.491 -52.379 1.00 14.50 ? 151 PHE D CE2 1 
ATOM   7608 C  CZ  . PHE D  1 151 ? -2.785  -9.440  -53.052 1.00 13.75 ? 151 PHE D CZ  1 
ATOM   7609 N  N   . ASN D  1 152 ? -0.949  -10.604 -48.882 1.00 10.77 ? 152 ASN D N   1 
ATOM   7610 C  CA  . ASN D  1 152 ? -1.838  -10.162 -47.893 1.00 11.41 ? 152 ASN D CA  1 
ATOM   7611 C  C   . ASN D  1 152 ? -2.875  -9.231  -48.541 1.00 13.66 ? 152 ASN D C   1 
ATOM   7612 O  O   . ASN D  1 152 ? -2.605  -8.089  -48.930 1.00 12.45 ? 152 ASN D O   1 
ATOM   7613 C  CB  . ASN D  1 152 ? -1.021  -9.366  -46.861 1.00 10.71 ? 152 ASN D CB  1 
ATOM   7614 C  CG  . ASN D  1 152 ? -1.803  -9.093  -45.607 1.00 10.87 ? 152 ASN D CG  1 
ATOM   7615 O  OD1 . ASN D  1 152 ? -2.973  -8.573  -45.731 1.00 11.71 ? 152 ASN D OD1 1 
ATOM   7616 N  ND2 . ASN D  1 152 ? -1.263  -9.405  -44.433 1.00 10.54 ? 152 ASN D ND2 1 
ATOM   7617 N  N   . PRO D  1 153 ? -4.138  -9.738  -48.683 1.00 13.54 ? 153 PRO D N   1 
ATOM   7618 C  CA  . PRO D  1 153 ? -5.121  -8.974  -49.421 1.00 13.45 ? 153 PRO D CA  1 
ATOM   7619 C  C   . PRO D  1 153 ? -5.527  -7.702  -48.680 1.00 13.75 ? 153 PRO D C   1 
ATOM   7620 O  O   . PRO D  1 153 ? -5.877  -6.713  -49.339 1.00 16.68 ? 153 PRO D O   1 
ATOM   7621 C  CB  . PRO D  1 153 ? -6.327  -9.935  -49.537 1.00 15.79 ? 153 PRO D CB  1 
ATOM   7622 C  CG  . PRO D  1 153 ? -5.818  -11.281 -49.164 1.00 19.33 ? 153 PRO D CG  1 
ATOM   7623 C  CD  . PRO D  1 153 ? -4.589  -11.086 -48.283 1.00 16.31 ? 153 PRO D CD  1 
ATOM   7624 N  N   . SER D  1 154 ? -5.377  -7.661  -47.381 1.00 12.15 ? 154 SER D N   1 
ATOM   7625 C  CA  . SER D  1 154 ? -5.784  -6.480  -46.613 1.00 13.24 ? 154 SER D CA  1 
ATOM   7626 C  C   . SER D  1 154 ? -4.696  -5.416  -46.803 1.00 13.84 ? 154 SER D C   1 
ATOM   7627 O  O   . SER D  1 154 ? -5.032  -4.226  -47.033 1.00 14.04 ? 154 SER D O   1 
ATOM   7628 C  CB  . SER D  1 154 ? -5.852  -6.839  -45.132 1.00 14.22 ? 154 SER D CB  1 
ATOM   7629 O  OG  . SER D  1 154 ? -6.885  -7.799  -44.888 1.00 18.53 ? 154 SER D OG  1 
ATOM   7630 N  N   . TYR D  1 155 ? -3.387  -5.718  -46.654 1.00 12.30 ? 155 TYR D N   1 
ATOM   7631 C  CA  . TYR D  1 155 ? -2.416  -4.701  -47.013 1.00 12.10 ? 155 TYR D CA  1 
ATOM   7632 C  C   . TYR D  1 155 ? -2.530  -4.263  -48.406 1.00 9.84  ? 155 TYR D C   1 
ATOM   7633 O  O   . TYR D  1 155 ? -2.235  -3.088  -48.780 1.00 11.55 ? 155 TYR D O   1 
ATOM   7634 C  CB  . TYR D  1 155 ? -0.968  -5.163  -46.687 1.00 10.52 ? 155 TYR D CB  1 
ATOM   7635 C  CG  . TYR D  1 155 ? -0.633  -5.029  -45.239 1.00 9.93  ? 155 TYR D CG  1 
ATOM   7636 C  CD1 . TYR D  1 155 ? -1.064  -5.948  -44.263 1.00 9.56  ? 155 TYR D CD1 1 
ATOM   7637 C  CD2 . TYR D  1 155 ? 0.168   -3.923  -44.782 1.00 10.45 ? 155 TYR D CD2 1 
ATOM   7638 C  CE1 . TYR D  1 155 ? -0.787  -5.807  -42.909 1.00 10.86 ? 155 TYR D CE1 1 
ATOM   7639 C  CE2 . TYR D  1 155 ? 0.455   -3.805  -43.451 1.00 10.91 ? 155 TYR D CE2 1 
ATOM   7640 C  CZ  . TYR D  1 155 ? 0.002   -4.726  -42.502 1.00 10.38 ? 155 TYR D CZ  1 
ATOM   7641 O  OH  . TYR D  1 155 ? 0.261   -4.597  -41.168 1.00 11.48 ? 155 TYR D OH  1 
ATOM   7642 N  N   . ASP D  1 156 ? -2.982  -5.102  -49.340 1.00 10.59 ? 156 ASP D N   1 
ATOM   7643 C  CA  . ASP D  1 156 ? -3.118  -4.702  -50.707 1.00 12.26 ? 156 ASP D CA  1 
ATOM   7644 C  C   . ASP D  1 156 ? -4.237  -3.638  -50.925 1.00 11.48 ? 156 ASP D C   1 
ATOM   7645 O  O   . ASP D  1 156 ? -4.195  -2.990  -51.971 1.00 14.78 ? 156 ASP D O   1 
ATOM   7646 C  CB  . ASP D  1 156 ? -3.338  -5.929  -51.664 1.00 14.81 ? 156 ASP D CB  1 
ATOM   7647 C  CG  . ASP D  1 156 ? -2.413  -5.831  -52.892 1.00 18.83 ? 156 ASP D CG  1 
ATOM   7648 O  OD1 . ASP D  1 156 ? -1.173  -5.568  -52.781 1.00 14.99 ? 156 ASP D OD1 1 
ATOM   7649 O  OD2 . ASP D  1 156 ? -3.016  -5.853  -54.038 1.00 20.86 ? 156 ASP D OD2 1 
ATOM   7650 N  N   . LYS D  1 157 ? -5.106  -3.478  -49.943 1.00 13.22 ? 157 LYS D N   1 
ATOM   7651 C  CA  . LYS D  1 157 ? -6.175  -2.407  -50.078 1.00 15.35 ? 157 LYS D CA  1 
ATOM   7652 C  C   . LYS D  1 157 ? -5.463  -1.050  -49.968 1.00 16.58 ? 157 LYS D C   1 
ATOM   7653 O  O   . LYS D  1 157 ? -5.974  -0.097  -50.608 1.00 18.51 ? 157 LYS D O   1 
ATOM   7654 C  CB  . LYS D  1 157 ? -7.187  -2.581  -48.968 1.00 16.23 ? 157 LYS D CB  1 
ATOM   7655 C  CG  . LYS D  1 157 ? -7.984  -3.853  -49.132 1.00 17.35 ? 157 LYS D CG  1 
ATOM   7656 C  CD  . LYS D  1 157 ? -8.882  -4.161  -47.929 1.00 19.65 ? 157 LYS D CD  1 
ATOM   7657 C  CE  . LYS D  1 157 ? -9.627  -5.527  -48.143 1.00 23.99 ? 157 LYS D CE  1 
ATOM   7658 N  NZ  . LYS D  1 157 ? -10.363 -6.099  -46.943 1.00 26.16 ? 157 LYS D NZ  1 
ATOM   7659 N  N   . ILE D  1 158 ? -4.239  -0.973  -49.425 1.00 14.46 ? 158 ILE D N   1 
ATOM   7660 C  CA  . ILE D  1 158 ? -3.406  0.228   -49.455 1.00 13.70 ? 158 ILE D CA  1 
ATOM   7661 C  C   . ILE D  1 158 ? -2.580  0.180   -50.728 1.00 12.70 ? 158 ILE D C   1 
ATOM   7662 O  O   . ILE D  1 158 ? -2.495  1.140   -51.547 1.00 14.09 ? 158 ILE D O   1 
ATOM   7663 C  CB  . ILE D  1 158 ? -2.535  0.335   -48.232 1.00 13.64 ? 158 ILE D CB  1 
ATOM   7664 C  CG1 . ILE D  1 158 ? -3.418  0.497   -46.950 1.00 17.58 ? 158 ILE D CG1 1 
ATOM   7665 C  CG2 . ILE D  1 158 ? -1.564  1.497   -48.388 1.00 13.93 ? 158 ILE D CG2 1 
ATOM   7666 C  CD1 . ILE D  1 158 ? -2.644  0.282   -45.672 1.00 20.87 ? 158 ILE D CD1 1 
ATOM   7667 N  N   . PHE D  1 159 ? -1.832  -0.951  -50.920 1.00 13.14 ? 159 PHE D N   1 
ATOM   7668 C  CA  . PHE D  1 159 ? -0.797  -0.955  -51.911 1.00 13.06 ? 159 PHE D CA  1 
ATOM   7669 C  C   . PHE D  1 159 ? -1.283  -0.788  -53.368 1.00 12.93 ? 159 PHE D C   1 
ATOM   7670 O  O   . PHE D  1 159 ? -0.568  -0.339  -54.248 1.00 14.32 ? 159 PHE D O   1 
ATOM   7671 C  CB  . PHE D  1 159 ? 0.053   -2.272  -51.849 1.00 12.14 ? 159 PHE D CB  1 
ATOM   7672 C  CG  . PHE D  1 159 ? 0.771   -2.528  -50.528 1.00 13.31 ? 159 PHE D CG  1 
ATOM   7673 C  CD1 . PHE D  1 159 ? 1.174   -1.477  -49.697 1.00 15.65 ? 159 PHE D CD1 1 
ATOM   7674 C  CD2 . PHE D  1 159 ? 1.083   -3.846  -50.140 1.00 13.43 ? 159 PHE D CD2 1 
ATOM   7675 C  CE1 . PHE D  1 159 ? 1.865   -1.729  -48.480 1.00 16.03 ? 159 PHE D CE1 1 
ATOM   7676 C  CE2 . PHE D  1 159 ? 1.760   -4.074  -48.972 1.00 12.85 ? 159 PHE D CE2 1 
ATOM   7677 C  CZ  . PHE D  1 159 ? 2.191   -3.026  -48.131 1.00 13.38 ? 159 PHE D CZ  1 
ATOM   7678 N  N   . SER D  1 160 ? -2.527  -1.234  -53.604 1.00 15.06 ? 160 SER D N   1 
ATOM   7679 C  CA  . SER D  1 160 ? -3.031  -1.059  -54.978 1.00 13.98 ? 160 SER D CA  1 
ATOM   7680 C  C   . SER D  1 160 ? -3.204  0.354   -55.431 1.00 15.72 ? 160 SER D C   1 
ATOM   7681 O  O   . SER D  1 160 ? -3.322  0.602   -56.636 1.00 18.19 ? 160 SER D O   1 
ATOM   7682 C  CB  . SER D  1 160 ? -4.374  -1.823  -55.174 1.00 16.45 ? 160 SER D CB  1 
ATOM   7683 O  OG  . SER D  1 160 ? -5.345  -1.216  -54.337 1.00 19.47 ? 160 SER D OG  1 
ATOM   7684 N  N   . HIS D  1 161 ? -3.091  1.291   -54.480 1.00 14.03 ? 161 HIS D N   1 
ATOM   7685 C  CA  . HIS D  1 161 ? -3.217  2.739   -54.776 1.00 14.31 ? 161 HIS D CA  1 
ATOM   7686 C  C   . HIS D  1 161 ? -1.904  3.460   -54.948 1.00 14.25 ? 161 HIS D C   1 
ATOM   7687 O  O   . HIS D  1 161 ? -1.876  4.677   -55.241 1.00 15.82 ? 161 HIS D O   1 
ATOM   7688 C  CB  . HIS D  1 161 ? -4.054  3.470   -53.655 1.00 14.15 ? 161 HIS D CB  1 
ATOM   7689 C  CG  . HIS D  1 161 ? -5.446  2.993   -53.611 1.00 17.27 ? 161 HIS D CG  1 
ATOM   7690 N  ND1 . HIS D  1 161 ? -6.413  3.571   -54.422 1.00 18.57 ? 161 HIS D ND1 1 
ATOM   7691 C  CD2 . HIS D  1 161 ? -6.053  1.948   -52.912 1.00 17.32 ? 161 HIS D CD2 1 
ATOM   7692 C  CE1 . HIS D  1 161 ? -7.599  2.898   -54.227 1.00 18.92 ? 161 HIS D CE1 1 
ATOM   7693 N  NE2 . HIS D  1 161 ? -7.387  1.904   -53.305 1.00 19.07 ? 161 HIS D NE2 1 
ATOM   7694 N  N   . LEU D  1 162 ? -0.785  2.739   -54.767 1.00 15.96 ? 162 LEU D N   1 
ATOM   7695 C  CA  . LEU D  1 162 ? 0.510   3.443   -54.719 1.00 17.76 ? 162 LEU D CA  1 
ATOM   7696 C  C   . LEU D  1 162 ? 0.850   4.171   -55.982 1.00 19.25 ? 162 LEU D C   1 
ATOM   7697 O  O   . LEU D  1 162 ? 1.484   5.267   -55.934 1.00 20.56 ? 162 LEU D O   1 
ATOM   7698 C  CB  . LEU D  1 162 ? 1.602   2.409   -54.364 1.00 20.42 ? 162 LEU D CB  1 
ATOM   7699 C  CG  . LEU D  1 162 ? 1.584   1.714   -53.017 1.00 21.87 ? 162 LEU D CG  1 
ATOM   7700 C  CD1 . LEU D  1 162 ? 2.601   0.556   -53.018 1.00 24.78 ? 162 LEU D CD1 1 
ATOM   7701 C  CD2 . LEU D  1 162 ? 1.831   2.780   -51.961 1.00 24.81 ? 162 LEU D CD2 1 
ATOM   7702 N  N   . GLN D  1 163 ? 0.401   3.645   -57.116 1.00 21.56 ? 163 GLN D N   1 
ATOM   7703 C  CA  . GLN D  1 163 ? 0.706   4.309   -58.363 1.00 22.90 ? 163 GLN D CA  1 
ATOM   7704 C  C   . GLN D  1 163 ? 0.013   5.658   -58.554 1.00 22.43 ? 163 GLN D C   1 
ATOM   7705 O  O   . GLN D  1 163 ? 0.393   6.407   -59.441 1.00 27.97 ? 163 GLN D O   1 
ATOM   7706 C  CB  . GLN D  1 163 ? 0.450   3.415   -59.565 1.00 29.68 ? 163 GLN D CB  1 
ATOM   7707 C  CG  . GLN D  1 163 ? 1.419   2.202   -59.665 1.00 40.85 ? 163 GLN D CG  1 
ATOM   7708 C  CD  . GLN D  1 163 ? 2.952   2.517   -59.703 1.00 46.42 ? 163 GLN D CD  1 
ATOM   7709 O  OE1 . GLN D  1 163 ? 3.422   3.445   -60.410 1.00 50.58 ? 163 GLN D OE1 1 
ATOM   7710 N  NE2 . GLN D  1 163 ? 3.733   1.717   -58.964 1.00 40.32 ? 163 GLN D NE2 1 
ATOM   7711 N  N   . HIS D  1 164 ? -0.912  6.001   -57.661 1.00 19.95 ? 164 HIS D N   1 
ATOM   7712 C  CA  . HIS D  1 164 ? -1.575  7.298   -57.704 1.00 20.34 ? 164 HIS D CA  1 
ATOM   7713 C  C   . HIS D  1 164 ? -0.960  8.342   -56.798 1.00 21.09 ? 164 HIS D C   1 
ATOM   7714 O  O   . HIS D  1 164 ? -1.388  9.517   -56.806 1.00 20.70 ? 164 HIS D O   1 
ATOM   7715 C  CB  . HIS D  1 164 ? -3.059  7.145   -57.387 1.00 22.10 ? 164 HIS D CB  1 
ATOM   7716 C  CG  . HIS D  1 164 ? -3.808  6.287   -58.378 1.00 27.78 ? 164 HIS D CG  1 
ATOM   7717 N  ND1 . HIS D  1 164 ? -4.416  5.140   -58.027 1.00 30.98 ? 164 HIS D ND1 1 
ATOM   7718 C  CD2 . HIS D  1 164 ? -4.032  6.450   -59.744 1.00 35.87 ? 164 HIS D CD2 1 
ATOM   7719 C  CE1 . HIS D  1 164 ? -5.000  4.593   -59.110 1.00 37.00 ? 164 HIS D CE1 1 
ATOM   7720 N  NE2 . HIS D  1 164 ? -4.764  5.396   -60.160 1.00 42.52 ? 164 HIS D NE2 1 
ATOM   7721 N  N   . VAL D  1 165 ? 0.038   7.948   -56.011 1.00 15.28 ? 165 VAL D N   1 
ATOM   7722 C  CA  . VAL D  1 165 ? 0.708   8.844   -55.088 1.00 14.51 ? 165 VAL D CA  1 
ATOM   7723 C  C   . VAL D  1 165 ? 2.238   8.726   -55.276 1.00 15.42 ? 165 VAL D C   1 
ATOM   7724 O  O   . VAL D  1 165 ? 2.998   8.837   -54.273 1.00 14.77 ? 165 VAL D O   1 
ATOM   7725 C  CB  . VAL D  1 165 ? 0.248   8.639   -53.616 1.00 17.09 ? 165 VAL D CB  1 
ATOM   7726 C  CG1 . VAL D  1 165 ? -1.236  8.981   -53.458 1.00 18.94 ? 165 VAL D CG1 1 
ATOM   7727 C  CG2 . VAL D  1 165 ? 0.489   7.205   -53.133 1.00 16.67 ? 165 VAL D CG2 1 
ATOM   7728 N  N   A LYS D  1 166 ? 2.652   8.589   -56.524 0.50 14.05 ? 166 LYS D N   1 
ATOM   7729 N  N   B LYS D  1 166 ? 2.695   8.580   -56.521 0.50 13.84 ? 166 LYS D N   1 
ATOM   7730 C  CA  A LYS D  1 166 ? 4.044   8.356   -56.829 0.50 14.76 ? 166 LYS D CA  1 
ATOM   7731 C  CA  B LYS D  1 166 ? 4.127   8.337   -56.734 0.50 14.43 ? 166 LYS D CA  1 
ATOM   7732 C  C   A LYS D  1 166 ? 4.976   9.454   -56.289 0.50 15.40 ? 166 LYS D C   1 
ATOM   7733 C  C   B LYS D  1 166 ? 5.021   9.472   -56.274 0.50 15.27 ? 166 LYS D C   1 
ATOM   7734 O  O   A LYS D  1 166 ? 6.064   9.160   -55.824 0.50 15.48 ? 166 LYS D O   1 
ATOM   7735 O  O   B LYS D  1 166 ? 6.141   9.219   -55.876 0.50 15.50 ? 166 LYS D O   1 
ATOM   7736 C  CB  A LYS D  1 166 ? 4.212   8.297   -58.333 0.50 17.93 ? 166 LYS D CB  1 
ATOM   7737 C  CB  B LYS D  1 166 ? 4.485   8.062   -58.184 0.50 16.91 ? 166 LYS D CB  1 
ATOM   7738 C  CG  A LYS D  1 166 ? 5.609   7.924   -58.733 0.50 19.61 ? 166 LYS D CG  1 
ATOM   7739 C  CG  B LYS D  1 166 ? 3.804   6.835   -58.751 0.50 17.56 ? 166 LYS D CG  1 
ATOM   7740 C  CD  A LYS D  1 166 ? 5.613   7.530   -60.207 0.50 25.09 ? 166 LYS D CD  1 
ATOM   7741 C  CD  B LYS D  1 166 ? 4.096   6.679   -60.239 0.50 23.97 ? 166 LYS D CD  1 
ATOM   7742 C  CE  A LYS D  1 166 ? 5.227   6.065   -60.398 0.50 30.12 ? 166 LYS D CE  1 
ATOM   7743 C  CE  B LYS D  1 166 ? 5.553   6.265   -60.488 0.50 27.53 ? 166 LYS D CE  1 
ATOM   7744 N  NZ  A LYS D  1 166 ? 5.902   5.133   -59.442 0.50 32.02 ? 166 LYS D NZ  1 
ATOM   7745 N  NZ  B LYS D  1 166 ? 5.835   4.850   -60.074 0.50 30.24 ? 166 LYS D NZ  1 
ATOM   7746 N  N   . TYR D  1 167 ? 4.557   10.724  -56.325 1.00 16.17 ? 167 TYR D N   1 
ATOM   7747 C  CA  . TYR D  1 167 ? 5.496   11.839  -56.059 1.00 13.31 ? 167 TYR D CA  1 
ATOM   7748 C  C   . TYR D  1 167 ? 5.008   12.610  -54.873 1.00 13.28 ? 167 TYR D C   1 
ATOM   7749 O  O   . TYR D  1 167 ? 3.804   12.601  -54.513 1.00 12.92 ? 167 TYR D O   1 
ATOM   7750 C  CB  . TYR D  1 167 ? 5.518   12.739  -57.293 1.00 15.32 ? 167 TYR D CB  1 
ATOM   7751 C  CG  . TYR D  1 167 ? 6.204   12.058  -58.414 1.00 17.58 ? 167 TYR D CG  1 
ATOM   7752 C  CD1 . TYR D  1 167 ? 7.602   11.933  -58.407 1.00 18.49 ? 167 TYR D CD1 1 
ATOM   7753 C  CD2 . TYR D  1 167 ? 5.475   11.608  -59.444 1.00 18.17 ? 167 TYR D CD2 1 
ATOM   7754 C  CE1 . TYR D  1 167 ? 8.213   11.283  -59.467 1.00 20.86 ? 167 TYR D CE1 1 
ATOM   7755 C  CE2 . TYR D  1 167 ? 6.063   10.959  -60.556 1.00 20.56 ? 167 TYR D CE2 1 
ATOM   7756 C  CZ  . TYR D  1 167 ? 7.430   10.814  -60.503 1.00 22.36 ? 167 TYR D CZ  1 
ATOM   7757 O  OH  . TYR D  1 167 ? 7.994   10.196  -61.617 1.00 27.89 ? 167 TYR D OH  1 
ATOM   7758 N  N   . LYS D  1 168 ? 5.993   13.309  -54.271 1.00 13.74 ? 168 LYS D N   1 
ATOM   7759 C  CA  . LYS D  1 168 ? 5.733   14.078  -53.062 1.00 15.99 ? 168 LYS D CA  1 
ATOM   7760 C  C   . LYS D  1 168 ? 4.576   15.008  -53.260 1.00 15.00 ? 168 LYS D C   1 
ATOM   7761 O  O   . LYS D  1 168 ? 4.475   15.776  -54.290 1.00 17.58 ? 168 LYS D O   1 
ATOM   7762 C  CB  . LYS D  1 168 ? 6.953   14.903  -52.631 1.00 16.29 ? 168 LYS D CB  1 
ATOM   7763 C  CG  . LYS D  1 168 ? 6.722   15.633  -51.303 1.00 18.72 ? 168 LYS D CG  1 
ATOM   7764 C  CD  . LYS D  1 168 ? 8.053   16.212  -50.886 1.00 21.85 ? 168 LYS D CD  1 
ATOM   7765 C  CE  . LYS D  1 168 ? 7.936   16.937  -49.547 1.00 25.56 ? 168 LYS D CE  1 
ATOM   7766 N  NZ  . LYS D  1 168 ? 9.195   17.580  -49.027 1.00 28.56 ? 168 LYS D NZ  1 
ATOM   7767 N  N   . GLY D  1 169 ? 3.621   14.954  -52.349 1.00 16.26 ? 169 GLY D N   1 
ATOM   7768 C  CA  . GLY D  1 169 ? 2.493   15.821  -52.398 1.00 17.95 ? 169 GLY D CA  1 
ATOM   7769 C  C   . GLY D  1 169 ? 1.225   15.295  -53.041 1.00 21.89 ? 169 GLY D C   1 
ATOM   7770 O  O   . GLY D  1 169 ? 0.155   15.897  -52.894 1.00 24.83 ? 169 GLY D O   1 
ATOM   7771 N  N   . GLN D  1 170 ? 1.305   14.215  -53.819 1.00 17.49 ? 170 GLN D N   1 
ATOM   7772 C  CA  . GLN D  1 170 ? 0.205   13.617  -54.509 1.00 16.41 ? 170 GLN D CA  1 
ATOM   7773 C  C   . GLN D  1 170 ? -0.723  12.916  -53.475 1.00 18.34 ? 170 GLN D C   1 
ATOM   7774 O  O   . GLN D  1 170 ? -0.251  12.326  -52.471 1.00 16.75 ? 170 GLN D O   1 
ATOM   7775 C  CB  . GLN D  1 170 ? 0.695   12.706  -55.573 1.00 15.63 ? 170 GLN D CB  1 
ATOM   7776 C  CG  . GLN D  1 170 ? 1.381   13.526  -56.679 1.00 17.37 ? 170 GLN D CG  1 
ATOM   7777 C  CD  . GLN D  1 170 ? 1.741   12.717  -57.848 1.00 19.97 ? 170 GLN D CD  1 
ATOM   7778 O  OE1 . GLN D  1 170 ? 2.025   11.548  -57.762 1.00 18.56 ? 170 GLN D OE1 1 
ATOM   7779 N  NE2 . GLN D  1 170 ? 1.782   13.385  -59.039 1.00 23.82 ? 170 GLN D NE2 1 
ATOM   7780 N  N   . GLU D  1 171 ? -2.013  12.920  -53.821 1.00 22.08 ? 171 GLU D N   1 
ATOM   7781 C  CA  . GLU D  1 171 ? -3.071  12.384  -52.953 1.00 19.86 ? 171 GLU D CA  1 
ATOM   7782 C  C   . GLU D  1 171 ? -4.041  11.550  -53.764 1.00 22.91 ? 171 GLU D C   1 
ATOM   7783 O  O   . GLU D  1 171 ? -4.227  11.755  -55.006 1.00 24.90 ? 171 GLU D O   1 
ATOM   7784 C  CB  . GLU D  1 171 ? -3.833  13.538  -52.291 1.00 23.78 ? 171 GLU D CB  1 
ATOM   7785 C  CG  . GLU D  1 171 ? -3.010  14.339  -51.336 1.00 27.59 ? 171 GLU D CG  1 
ATOM   7786 C  CD  . GLU D  1 171 ? -3.744  15.583  -50.803 1.00 35.83 ? 171 GLU D CD  1 
ATOM   7787 O  OE1 . GLU D  1 171 ? -4.830  15.874  -51.317 1.00 37.03 ? 171 GLU D OE1 1 
ATOM   7788 O  OE2 . GLU D  1 171 ? -3.255  16.223  -49.849 1.00 39.01 ? 171 GLU D OE2 1 
ATOM   7789 N  N   . ALA D  1 172 ? -4.613  10.551  -53.134 1.00 19.76 ? 172 ALA D N   1 
ATOM   7790 C  CA  . ALA D  1 172 ? -5.563  9.646   -53.767 1.00 18.55 ? 172 ALA D CA  1 
ATOM   7791 C  C   . ALA D  1 172 ? -6.516  9.186   -52.662 1.00 19.32 ? 172 ALA D C   1 
ATOM   7792 O  O   . ALA D  1 172 ? -6.217  9.290   -51.470 1.00 21.31 ? 172 ALA D O   1 
ATOM   7793 C  CB  . ALA D  1 172 ? -4.931  8.455   -54.379 1.00 19.34 ? 172 ALA D CB  1 
ATOM   7794 N  N   . PHE D  1 173 ? -7.698  8.714   -53.057 1.00 21.03 ? 173 PHE D N   1 
ATOM   7795 C  CA  . PHE D  1 173 ? -8.666  8.250   -52.042 1.00 18.18 ? 173 PHE D CA  1 
ATOM   7796 C  C   . PHE D  1 173 ? -8.747  6.760   -52.071 1.00 17.46 ? 173 PHE D C   1 
ATOM   7797 O  O   . PHE D  1 173 ? -8.702  6.124   -53.129 1.00 21.85 ? 173 PHE D O   1 
ATOM   7798 C  CB  . PHE D  1 173 ? -10.049 8.775   -52.409 1.00 20.89 ? 173 PHE D CB  1 
ATOM   7799 C  CG  . PHE D  1 173 ? -10.296 10.194  -51.917 1.00 21.12 ? 173 PHE D CG  1 
ATOM   7800 C  CD1 . PHE D  1 173 ? -10.291 10.504  -50.524 1.00 23.65 ? 173 PHE D CD1 1 
ATOM   7801 C  CD2 . PHE D  1 173 ? -10.573 11.238  -52.820 1.00 29.20 ? 173 PHE D CD2 1 
ATOM   7802 C  CE1 . PHE D  1 173 ? -10.548 11.781  -50.034 1.00 29.62 ? 173 PHE D CE1 1 
ATOM   7803 C  CE2 . PHE D  1 173 ? -10.817 12.532  -52.319 1.00 28.66 ? 173 PHE D CE2 1 
ATOM   7804 C  CZ  . PHE D  1 173 ? -10.785 12.812  -50.951 1.00 31.22 ? 173 PHE D CZ  1 
ATOM   7805 N  N   . VAL D  1 174 ? -8.780  6.207   -50.865 1.00 14.86 ? 174 VAL D N   1 
ATOM   7806 C  CA  . VAL D  1 174 ? -8.803  4.765   -50.627 1.00 14.96 ? 174 VAL D CA  1 
ATOM   7807 C  C   . VAL D  1 174 ? -10.219 4.486   -50.008 1.00 14.64 ? 174 VAL D C   1 
ATOM   7808 O  O   . VAL D  1 174 ? -10.556 5.076   -48.979 1.00 15.97 ? 174 VAL D O   1 
ATOM   7809 C  CB  . VAL D  1 174 ? -7.671  4.285   -49.663 1.00 14.35 ? 174 VAL D CB  1 
ATOM   7810 C  CG1 . VAL D  1 174 ? -7.822  2.773   -49.348 1.00 16.10 ? 174 VAL D CG1 1 
ATOM   7811 C  CG2 . VAL D  1 174 ? -6.280  4.542   -50.393 1.00 16.96 ? 174 VAL D CG2 1 
ATOM   7812 N  N   . PRO D  1 175 ? -10.993 3.541   -50.553 1.00 15.02 ? 175 PRO D N   1 
ATOM   7813 C  CA  . PRO D  1 175 ? -12.244 3.112   -49.829 1.00 14.32 ? 175 PRO D CA  1 
ATOM   7814 C  C   . PRO D  1 175 ? -11.923 2.557   -48.439 1.00 15.37 ? 175 PRO D C   1 
ATOM   7815 O  O   . PRO D  1 175 ? -10.898 1.909   -48.211 1.00 16.65 ? 175 PRO D O   1 
ATOM   7816 C  CB  . PRO D  1 175 ? -12.748 1.985   -50.727 1.00 16.67 ? 175 PRO D CB  1 
ATOM   7817 C  CG  . PRO D  1 175 ? -12.232 2.318   -52.083 1.00 17.13 ? 175 PRO D CG  1 
ATOM   7818 C  CD  . PRO D  1 175 ? -10.801 2.794   -51.796 1.00 16.30 ? 175 PRO D CD  1 
ATOM   7819 N  N   . GLY D  1 176 ? -12.754 2.828   -47.442 1.00 15.25 ? 176 GLY D N   1 
ATOM   7820 C  CA  . GLY D  1 176 ? -12.615 2.233   -46.125 1.00 14.39 ? 176 GLY D CA  1 
ATOM   7821 C  C   . GLY D  1 176 ? -12.552 0.692   -46.153 1.00 15.65 ? 176 GLY D C   1 
ATOM   7822 O  O   . GLY D  1 176 ? -13.178 0.009   -46.963 1.00 18.08 ? 176 GLY D O   1 
ATOM   7823 N  N   . PHE D  1 177 ? -11.778 0.226   -45.178 1.00 16.03 ? 177 PHE D N   1 
ATOM   7824 C  CA  . PHE D  1 177 ? -11.728 -1.256  -44.915 1.00 15.52 ? 177 PHE D CA  1 
ATOM   7825 C  C   . PHE D  1 177 ? -11.447 -1.398  -43.473 1.00 15.47 ? 177 PHE D C   1 
ATOM   7826 O  O   . PHE D  1 177 ? -11.224 -0.416  -42.708 1.00 15.23 ? 177 PHE D O   1 
ATOM   7827 C  CB  . PHE D  1 177 ? -10.684 -1.953  -45.848 1.00 17.12 ? 177 PHE D CB  1 
ATOM   7828 C  CG  . PHE D  1 177 ? -9.232  -1.535  -45.600 1.00 15.03 ? 177 PHE D CG  1 
ATOM   7829 C  CD1 . PHE D  1 177 ? -8.686  -0.386  -46.180 1.00 15.31 ? 177 PHE D CD1 1 
ATOM   7830 C  CD2 . PHE D  1 177 ? -8.459  -2.351  -44.754 1.00 17.94 ? 177 PHE D CD2 1 
ATOM   7831 C  CE1 . PHE D  1 177 ? -7.357  -0.032  -45.925 1.00 16.19 ? 177 PHE D CE1 1 
ATOM   7832 C  CE2 . PHE D  1 177 ? -7.133  -2.052  -44.524 1.00 16.58 ? 177 PHE D CE2 1 
ATOM   7833 C  CZ  . PHE D  1 177 ? -6.596  -0.917  -45.149 1.00 18.24 ? 177 PHE D CZ  1 
ATOM   7834 N  N   . ASN D  1 178 ? -11.440 -2.635  -43.003 1.00 16.31 ? 178 ASN D N   1 
ATOM   7835 C  CA  . ASN D  1 178 ? -11.313 -2.788  -41.542 1.00 15.48 ? 178 ASN D CA  1 
ATOM   7836 C  C   . ASN D  1 178 ? -9.791  -2.806  -41.244 1.00 14.92 ? 178 ASN D C   1 
ATOM   7837 O  O   . ASN D  1 178 ? -9.092  -3.794  -41.582 1.00 14.42 ? 178 ASN D O   1 
ATOM   7838 C  CB  . ASN D  1 178 ? -11.866 -4.193  -41.165 1.00 17.79 ? 178 ASN D CB  1 
ATOM   7839 C  CG  . ASN D  1 178 ? -11.740 -4.473  -39.736 1.00 16.67 ? 178 ASN D CG  1 
ATOM   7840 O  OD1 . ASN D  1 178 ? -11.387 -3.636  -38.919 1.00 17.20 ? 178 ASN D OD1 1 
ATOM   7841 N  ND2 . ASN D  1 178 ? -12.095 -5.748  -39.351 1.00 25.78 ? 178 ASN D ND2 1 
ATOM   7842 N  N   . ILE D  1 179 ? -9.347  -1.781  -40.583 1.00 14.52 ? 179 ILE D N   1 
ATOM   7843 C  CA  . ILE D  1 179 ? -7.923  -1.644  -40.252 1.00 13.36 ? 179 ILE D CA  1 
ATOM   7844 C  C   . ILE D  1 179 ? -7.435  -2.705  -39.284 1.00 15.65 ? 179 ILE D C   1 
ATOM   7845 O  O   . ILE D  1 179 ? -6.201  -3.013  -39.196 1.00 14.23 ? 179 ILE D O   1 
ATOM   7846 C  CB  . ILE D  1 179 ? -7.712  -0.221  -39.711 1.00 13.47 ? 179 ILE D CB  1 
ATOM   7847 C  CG1 . ILE D  1 179 ? -8.181  0.867   -40.696 1.00 14.08 ? 179 ILE D CG1 1 
ATOM   7848 C  CG2 . ILE D  1 179 ? -6.233  -0.011  -39.261 1.00 13.33 ? 179 ILE D CG2 1 
ATOM   7849 C  CD1 . ILE D  1 179 ? -7.531  0.841   -42.092 1.00 16.11 ? 179 ILE D CD1 1 
ATOM   7850 N  N   A GLU D  1 180 ? -8.340  -3.364  -38.543 0.50 14.92 ? 180 GLU D N   1 
ATOM   7851 N  N   B GLU D  1 180 ? -8.345  -3.351  -38.540 0.50 15.16 ? 180 GLU D N   1 
ATOM   7852 C  CA  A GLU D  1 180 ? -7.863  -4.431  -37.687 0.50 15.02 ? 180 GLU D CA  1 
ATOM   7853 C  CA  B GLU D  1 180 ? -7.931  -4.468  -37.717 0.50 15.64 ? 180 GLU D CA  1 
ATOM   7854 C  C   A GLU D  1 180 ? -7.318  -5.615  -38.501 0.50 12.77 ? 180 GLU D C   1 
ATOM   7855 C  C   B GLU D  1 180 ? -7.319  -5.611  -38.508 0.50 12.98 ? 180 GLU D C   1 
ATOM   7856 O  O   A GLU D  1 180 ? -6.554  -6.404  -37.949 0.50 15.14 ? 180 GLU D O   1 
ATOM   7857 O  O   B GLU D  1 180 ? -6.533  -6.374  -37.947 0.50 15.13 ? 180 GLU D O   1 
ATOM   7858 C  CB  A GLU D  1 180 ? -8.955  -4.956  -36.712 0.50 16.78 ? 180 GLU D CB  1 
ATOM   7859 C  CB  B GLU D  1 180 ? -9.124  -5.052  -36.944 0.50 17.81 ? 180 GLU D CB  1 
ATOM   7860 C  CG  A GLU D  1 180 ? -8.389  -5.692  -35.518 0.50 18.42 ? 180 GLU D CG  1 
ATOM   7861 C  CG  B GLU D  1 180 ? -9.484  -4.251  -35.698 0.50 17.72 ? 180 GLU D CG  1 
ATOM   7862 C  CD  A GLU D  1 180 ? -9.375  -5.829  -34.329 0.50 18.17 ? 180 GLU D CD  1 
ATOM   7863 C  CD  B GLU D  1 180 ? -10.551 -4.958  -34.859 0.50 24.64 ? 180 GLU D CD  1 
ATOM   7864 O  OE1 A GLU D  1 180 ? -10.449 -5.232  -34.278 0.50 20.64 ? 180 GLU D OE1 1 
ATOM   7865 O  OE1 B GLU D  1 180 ? -10.636 -6.191  -34.980 0.50 27.52 ? 180 GLU D OE1 1 
ATOM   7866 O  OE2 A GLU D  1 180 ? -9.053  -6.570  -33.442 0.50 20.41 ? 180 GLU D OE2 1 
ATOM   7867 O  OE2 B GLU D  1 180 ? -11.255 -4.272  -34.073 0.50 27.80 ? 180 GLU D OE2 1 
ATOM   7868 N  N   . GLU D  1 181 ? -7.668  -5.710  -39.785 1.00 13.92 ? 181 GLU D N   1 
ATOM   7869 C  CA  . GLU D  1 181 ? -7.108  -6.745  -40.660 1.00 13.60 ? 181 GLU D CA  1 
ATOM   7870 C  C   . GLU D  1 181 ? -5.637  -6.536  -40.852 1.00 15.59 ? 181 GLU D C   1 
ATOM   7871 O  O   . GLU D  1 181 ? -4.973  -7.451  -41.355 1.00 15.06 ? 181 GLU D O   1 
ATOM   7872 C  CB  . GLU D  1 181 ? -7.739  -6.764  -42.013 1.00 16.34 ? 181 GLU D CB  1 
ATOM   7873 C  CG  . GLU D  1 181 ? -9.185  -7.176  -42.001 1.00 17.19 ? 181 GLU D CG  1 
ATOM   7874 C  CD  . GLU D  1 181 ? -9.861  -6.927  -43.352 1.00 24.02 ? 181 GLU D CD  1 
ATOM   7875 O  OE1 . GLU D  1 181 ? -9.233  -6.595  -44.417 1.00 26.96 ? 181 GLU D OE1 1 
ATOM   7876 O  OE2 . GLU D  1 181 ? -11.125 -7.020  -43.400 1.00 24.40 ? 181 GLU D OE2 1 
ATOM   7877 N  N   . LEU D  1 182 ? -5.117  -5.354  -40.564 1.00 12.38 ? 182 LEU D N   1 
ATOM   7878 C  CA  . LEU D  1 182 ? -3.639  -5.147  -40.692 1.00 11.57 ? 182 LEU D CA  1 
ATOM   7879 C  C   . LEU D  1 182 ? -2.859  -5.585  -39.460 1.00 11.87 ? 182 LEU D C   1 
ATOM   7880 O  O   . LEU D  1 182 ? -1.644  -5.578  -39.491 1.00 11.56 ? 182 LEU D O   1 
ATOM   7881 C  CB  . LEU D  1 182 ? -3.398  -3.631  -40.886 1.00 11.26 ? 182 LEU D CB  1 
ATOM   7882 C  CG  . LEU D  1 182 ? -4.014  -3.007  -42.132 1.00 11.09 ? 182 LEU D CG  1 
ATOM   7883 C  CD1 . LEU D  1 182 ? -3.654  -1.523  -42.159 1.00 12.56 ? 182 LEU D CD1 1 
ATOM   7884 C  CD2 . LEU D  1 182 ? -3.761  -3.695  -43.447 1.00 11.51 ? 182 LEU D CD2 1 
ATOM   7885 N  N   . LEU D  1 183 ? -3.526  -5.918  -38.342 1.00 12.69 ? 183 LEU D N   1 
ATOM   7886 C  CA  . LEU D  1 183 ? -2.899  -6.323  -37.140 1.00 13.48 ? 183 LEU D CA  1 
ATOM   7887 C  C   . LEU D  1 183 ? -2.620  -7.829  -37.143 1.00 12.45 ? 183 LEU D C   1 
ATOM   7888 O  O   . LEU D  1 183 ? -3.291  -8.576  -37.865 1.00 14.81 ? 183 LEU D O   1 
ATOM   7889 C  CB  . LEU D  1 183 ? -3.855  -5.952  -35.957 1.00 15.00 ? 183 LEU D CB  1 
ATOM   7890 C  CG  . LEU D  1 183 ? -4.173  -4.442  -35.779 1.00 15.16 ? 183 LEU D CG  1 
ATOM   7891 C  CD1 . LEU D  1 183 ? -5.045  -4.194  -34.538 1.00 18.85 ? 183 LEU D CD1 1 
ATOM   7892 C  CD2 . LEU D  1 183 ? -2.927  -3.585  -35.584 1.00 16.81 ? 183 LEU D CD2 1 
ATOM   7893 N  N   . PRO D  1 184 ? -1.596  -8.193  -36.350 1.00 11.56 ? 184 PRO D N   1 
ATOM   7894 C  CA  . PRO D  1 184 ? -1.218  -9.608  -36.251 1.00 14.50 ? 184 PRO D CA  1 
ATOM   7895 C  C   . PRO D  1 184 ? -2.082  -10.404 -35.323 1.00 16.35 ? 184 PRO D C   1 
ATOM   7896 O  O   . PRO D  1 184 ? -3.033  -9.876  -34.683 1.00 17.65 ? 184 PRO D O   1 
ATOM   7897 C  CB  . PRO D  1 184 ? 0.224   -9.534  -35.650 1.00 14.75 ? 184 PRO D CB  1 
ATOM   7898 C  CG  . PRO D  1 184 ? 0.155   -8.298  -34.783 1.00 14.83 ? 184 PRO D CG  1 
ATOM   7899 C  CD  . PRO D  1 184 ? -0.714  -7.343  -35.511 1.00 13.21 ? 184 PRO D CD  1 
ATOM   7900 N  N   A GLU D  1 185 ? -1.727  -11.704 -35.272 0.50 16.33 ? 185 GLU D N   1 
ATOM   7901 N  N   B GLU D  1 185 ? -1.754  -11.707 -35.281 0.50 16.25 ? 185 GLU D N   1 
ATOM   7902 C  CA  A GLU D  1 185 ? -2.312  -12.618 -34.314 0.50 17.74 ? 185 GLU D CA  1 
ATOM   7903 C  CA  B GLU D  1 185 ? -2.420  -12.582 -34.352 0.50 17.40 ? 185 GLU D CA  1 
ATOM   7904 C  C   A GLU D  1 185 ? -1.988  -12.178 -32.880 0.50 16.41 ? 185 GLU D C   1 
ATOM   7905 C  C   B GLU D  1 185 ? -1.981  -12.238 -32.912 0.50 16.12 ? 185 GLU D C   1 
ATOM   7906 O  O   A GLU D  1 185 ? -0.918  -11.587 -32.610 0.50 16.70 ? 185 GLU D O   1 
ATOM   7907 O  O   B GLU D  1 185 ? -0.827  -11.740 -32.687 0.50 16.32 ? 185 GLU D O   1 
ATOM   7908 C  CB  A GLU D  1 185 ? -1.764  -14.018 -34.558 0.50 19.88 ? 185 GLU D CB  1 
ATOM   7909 C  CB  B GLU D  1 185 ? -2.122  -14.028 -34.709 0.50 19.37 ? 185 GLU D CB  1 
ATOM   7910 C  CG  A GLU D  1 185 ? -2.091  -14.565 -35.926 0.50 22.16 ? 185 GLU D CG  1 
ATOM   7911 C  CG  B GLU D  1 185 ? -2.557  -14.376 -36.108 0.50 21.36 ? 185 GLU D CG  1 
ATOM   7912 C  CD  A GLU D  1 185 ? -1.555  -15.985 -36.127 0.50 27.69 ? 185 GLU D CD  1 
ATOM   7913 C  CD  B GLU D  1 185 ? -4.051  -14.427 -36.248 0.50 27.58 ? 185 GLU D CD  1 
ATOM   7914 O  OE1 A GLU D  1 185 ? -1.119  -16.613 -35.122 0.50 30.20 ? 185 GLU D OE1 1 
ATOM   7915 O  OE1 B GLU D  1 185 ? -4.640  -15.327 -35.632 0.50 32.07 ? 185 GLU D OE1 1 
ATOM   7916 O  OE2 A GLU D  1 185 ? -1.584  -16.462 -37.294 0.50 31.59 ? 185 GLU D OE2 1 
ATOM   7917 O  OE2 B GLU D  1 185 ? -4.634  -13.592 -36.981 0.50 30.59 ? 185 GLU D OE2 1 
ATOM   7918 N  N   . ARG D  1 186 ? -2.896  -12.479 -31.947 1.00 16.24 ? 186 ARG D N   1 
ATOM   7919 C  CA  . ARG D  1 186 ? -2.588  -12.366 -30.519 1.00 17.76 ? 186 ARG D CA  1 
ATOM   7920 C  C   . ARG D  1 186 ? -2.080  -10.979 -30.159 1.00 16.45 ? 186 ARG D C   1 
ATOM   7921 O  O   . ARG D  1 186 ? -1.006  -10.787 -29.537 1.00 16.40 ? 186 ARG D O   1 
ATOM   7922 C  CB  . ARG D  1 186 ? -1.604  -13.457 -30.072 1.00 21.21 ? 186 ARG D CB  1 
ATOM   7923 C  CG  . ARG D  1 186 ? -2.264  -14.818 -30.208 1.00 26.32 ? 186 ARG D CG  1 
ATOM   7924 C  CD  . ARG D  1 186 ? -1.388  -15.970 -29.700 1.00 33.24 ? 186 ARG D CD  1 
ATOM   7925 N  NE  . ARG D  1 186 ? -0.293  -16.226 -30.644 1.00 37.17 ? 186 ARG D NE  1 
ATOM   7926 C  CZ  . ARG D  1 186 ? -0.464  -16.743 -31.873 1.00 44.98 ? 186 ARG D CZ  1 
ATOM   7927 N  NH1 . ARG D  1 186 ? -1.689  -17.065 -32.320 1.00 42.08 ? 186 ARG D NH1 1 
ATOM   7928 N  NH2 . ARG D  1 186 ? 0.587   -16.913 -32.674 1.00 45.80 ? 186 ARG D NH2 1 
ATOM   7929 N  N   . THR D  1 187 ? -2.925  -9.997  -30.507 1.00 15.36 ? 187 THR D N   1 
ATOM   7930 C  CA  . THR D  1 187 ? -2.563  -8.624  -30.133 1.00 16.01 ? 187 THR D CA  1 
ATOM   7931 C  C   . THR D  1 187 ? -2.427  -8.350  -28.626 1.00 16.56 ? 187 THR D C   1 
ATOM   7932 O  O   . THR D  1 187 ? -1.843  -7.321  -28.230 1.00 14.96 ? 187 THR D O   1 
ATOM   7933 C  CB  . THR D  1 187 ? -3.559  -7.593  -30.774 1.00 14.37 ? 187 THR D CB  1 
ATOM   7934 O  OG1 . THR D  1 187 ? -4.921  -7.914  -30.374 1.00 17.57 ? 187 THR D OG1 1 
ATOM   7935 C  CG2 . THR D  1 187 ? -3.513  -7.627  -32.346 1.00 16.64 ? 187 THR D CG2 1 
ATOM   7936 N  N   . ALA D  1 188 ? -2.918  -9.244  -27.732 1.00 14.65 ? 188 ALA D N   1 
ATOM   7937 C  CA  . ALA D  1 188 ? -2.686  -9.010  -26.337 1.00 14.89 ? 188 ALA D CA  1 
ATOM   7938 C  C   . ALA D  1 188 ? -1.198  -9.148  -25.939 1.00 13.44 ? 188 ALA D C   1 
ATOM   7939 O  O   . ALA D  1 188 ? -0.841  -8.764  -24.882 1.00 15.63 ? 188 ALA D O   1 
ATOM   7940 C  CB  . ALA D  1 188 ? -3.530  -10.022 -25.504 1.00 16.26 ? 188 ALA D CB  1 
ATOM   7941 N  N   . GLU D  1 189 ? -0.428  -9.755  -26.840 1.00 13.53 ? 189 GLU D N   1 
ATOM   7942 C  CA  . GLU D  1 189 ? 1.020   -9.946  -26.597 1.00 12.69 ? 189 GLU D CA  1 
ATOM   7943 C  C   . GLU D  1 189 ? 1.796   -8.836  -27.392 1.00 10.53 ? 189 GLU D C   1 
ATOM   7944 O  O   . GLU D  1 189 ? 1.773   -8.759  -28.649 1.00 13.06 ? 189 GLU D O   1 
ATOM   7945 C  CB  . GLU D  1 189 ? 1.382   -11.274 -27.230 1.00 13.85 ? 189 GLU D CB  1 
ATOM   7946 C  CG  . GLU D  1 189 ? 0.722   -12.421 -26.408 1.00 15.65 ? 189 GLU D CG  1 
ATOM   7947 C  CD  . GLU D  1 189 ? 1.149   -13.787 -26.890 1.00 22.98 ? 189 GLU D CD  1 
ATOM   7948 O  OE1 . GLU D  1 189 ? 2.244   -14.015 -27.323 1.00 22.49 ? 189 GLU D OE1 1 
ATOM   7949 O  OE2 . GLU D  1 189 ? 0.373   -14.765 -26.644 1.00 27.77 ? 189 GLU D OE2 1 
ATOM   7950 N  N   . TYR D  1 190 ? 2.425   -8.012  -26.584 1.00 11.04 ? 190 TYR D N   1 
ATOM   7951 C  CA  . TYR D  1 190 ? 3.110   -6.814  -27.129 1.00 10.53 ? 190 TYR D CA  1 
ATOM   7952 C  C   . TYR D  1 190 ? 4.177   -6.373  -26.274 1.00 10.93 ? 190 TYR D C   1 
ATOM   7953 O  O   . TYR D  1 190 ? 4.260   -6.761  -25.072 1.00 11.46 ? 190 TYR D O   1 
ATOM   7954 C  CB  . TYR D  1 190 ? 2.115   -5.692  -27.405 1.00 11.81 ? 190 TYR D CB  1 
ATOM   7955 C  CG  . TYR D  1 190 ? 1.322   -5.214  -26.145 1.00 10.11 ? 190 TYR D CG  1 
ATOM   7956 C  CD1 . TYR D  1 190 ? 1.897   -4.353  -25.265 1.00 11.59 ? 190 TYR D CD1 1 
ATOM   7957 C  CD2 . TYR D  1 190 ? 0.025   -5.674  -25.950 1.00 11.83 ? 190 TYR D CD2 1 
ATOM   7958 C  CE1 . TYR D  1 190 ? 1.142   -3.889  -24.126 1.00 12.93 ? 190 TYR D CE1 1 
ATOM   7959 C  CE2 . TYR D  1 190 ? -0.688  -5.232  -24.803 1.00 11.72 ? 190 TYR D CE2 1 
ATOM   7960 C  CZ  . TYR D  1 190 ? -0.112  -4.354  -23.972 1.00 13.39 ? 190 TYR D CZ  1 
ATOM   7961 O  OH  . TYR D  1 190 ? -0.814  -3.861  -22.807 1.00 13.88 ? 190 TYR D OH  1 
ATOM   7962 N  N   . TYR D  1 191 ? 5.097   -5.542  -26.800 1.00 9.99  ? 191 TYR D N   1 
ATOM   7963 C  CA  . TYR D  1 191 ? 6.102   -4.814  -26.150 1.00 10.71 ? 191 TYR D CA  1 
ATOM   7964 C  C   . TYR D  1 191 ? 5.635   -3.356  -26.004 1.00 10.23 ? 191 TYR D C   1 
ATOM   7965 O  O   . TYR D  1 191 ? 4.970   -2.812  -26.899 1.00 10.46 ? 191 TYR D O   1 
ATOM   7966 C  CB  . TYR D  1 191 ? 7.384   -4.759  -27.017 1.00 10.84 ? 191 TYR D CB  1 
ATOM   7967 C  CG  . TYR D  1 191 ? 7.924   -6.081  -27.535 1.00 10.53 ? 191 TYR D CG  1 
ATOM   7968 C  CD1 . TYR D  1 191 ? 8.895   -6.772  -26.858 1.00 11.23 ? 191 TYR D CD1 1 
ATOM   7969 C  CD2 . TYR D  1 191 ? 7.498   -6.584  -28.768 1.00 10.53 ? 191 TYR D CD2 1 
ATOM   7970 C  CE1 . TYR D  1 191 ? 9.468   -7.933  -27.354 1.00 11.25 ? 191 TYR D CE1 1 
ATOM   7971 C  CE2 . TYR D  1 191 ? 8.095   -7.760  -29.316 1.00 11.57 ? 191 TYR D CE2 1 
ATOM   7972 C  CZ  . TYR D  1 191 ? 9.043   -8.421  -28.560 1.00 10.61 ? 191 TYR D CZ  1 
ATOM   7973 O  OH  . TYR D  1 191 ? 9.656   -9.536  -29.102 1.00 15.87 ? 191 TYR D OH  1 
ATOM   7974 N  N   . ARG D  1 192 ? 5.957   -2.743  -24.853 1.00 11.42 ? 192 ARG D N   1 
ATOM   7975 C  CA  . ARG D  1 192 ? 5.529   -1.345  -24.542 1.00 11.03 ? 192 ARG D CA  1 
ATOM   7976 C  C   . ARG D  1 192 ? 6.705   -0.606  -23.978 1.00 10.92 ? 192 ARG D C   1 
ATOM   7977 O  O   . ARG D  1 192 ? 7.411   -1.042  -23.066 1.00 12.14 ? 192 ARG D O   1 
ATOM   7978 C  CB  . ARG D  1 192 ? 4.475   -1.490  -23.478 1.00 13.03 ? 192 ARG D CB  1 
ATOM   7979 C  CG  . ARG D  1 192 ? 4.096   -0.160  -22.793 1.00 17.97 ? 192 ARG D CG  1 
ATOM   7980 C  CD  . ARG D  1 192 ? 3.273   0.803   -23.638 1.00 16.42 ? 192 ARG D CD  1 
ATOM   7981 N  NE  . ARG D  1 192 ? 2.177   0.198   -24.395 1.00 16.31 ? 192 ARG D NE  1 
ATOM   7982 C  CZ  . ARG D  1 192 ? 0.990   -0.111  -23.891 1.00 15.84 ? 192 ARG D CZ  1 
ATOM   7983 N  NH1 . ARG D  1 192 ? 0.745   0.071   -22.601 1.00 19.82 ? 192 ARG D NH1 1 
ATOM   7984 N  NH2 . ARG D  1 192 ? 0.052   -0.640  -24.672 1.00 16.18 ? 192 ARG D NH2 1 
ATOM   7985 N  N   . TYR D  1 193 ? 6.942   0.615   -24.542 1.00 11.51 ? 193 TYR D N   1 
ATOM   7986 C  CA  . TYR D  1 193 ? 8.018   1.434   -23.992 1.00 10.99 ? 193 TYR D CA  1 
ATOM   7987 C  C   . TYR D  1 193 ? 7.746   2.929   -24.335 1.00 11.97 ? 193 TYR D C   1 
ATOM   7988 O  O   . TYR D  1 193 ? 6.925   3.232   -25.201 1.00 11.78 ? 193 TYR D O   1 
ATOM   7989 C  CB  . TYR D  1 193 ? 9.390   0.976   -24.480 1.00 11.01 ? 193 TYR D CB  1 
ATOM   7990 C  CG  . TYR D  1 193 ? 9.708   1.389   -25.894 1.00 10.34 ? 193 TYR D CG  1 
ATOM   7991 C  CD1 . TYR D  1 193 ? 9.241   0.656   -26.976 1.00 11.05 ? 193 TYR D CD1 1 
ATOM   7992 C  CD2 . TYR D  1 193 ? 10.476  2.513   -26.148 1.00 11.69 ? 193 TYR D CD2 1 
ATOM   7993 C  CE1 . TYR D  1 193 ? 9.532   1.036   -28.276 1.00 10.45 ? 193 TYR D CE1 1 
ATOM   7994 C  CE2 . TYR D  1 193 ? 10.773  2.901   -27.438 1.00 10.75 ? 193 TYR D CE2 1 
ATOM   7995 C  CZ  . TYR D  1 193 ? 10.301  2.164   -28.498 1.00 10.85 ? 193 TYR D CZ  1 
ATOM   7996 O  OH  . TYR D  1 193 ? 10.617  2.582   -29.771 1.00 10.61 ? 193 TYR D OH  1 
ATOM   7997 N  N   . ARG D  1 194 ? 8.454   3.758   -23.609 1.00 13.06 ? 194 ARG D N   1 
ATOM   7998 C  CA  . ARG D  1 194 ? 8.399   5.221   -23.867 1.00 14.29 ? 194 ARG D CA  1 
ATOM   7999 C  C   . ARG D  1 194 ? 9.461   5.647   -24.771 1.00 11.25 ? 194 ARG D C   1 
ATOM   8000 O  O   . ARG D  1 194 ? 10.625  5.419   -24.617 1.00 14.00 ? 194 ARG D O   1 
ATOM   8001 C  CB  . ARG D  1 194 ? 8.636   5.986   -22.564 1.00 17.46 ? 194 ARG D CB  1 
ATOM   8002 C  CG  . ARG D  1 194 ? 7.667   5.605   -21.490 1.00 23.47 ? 194 ARG D CG  1 
ATOM   8003 C  CD  . ARG D  1 194 ? 6.407   6.353   -21.783 1.00 28.55 ? 194 ARG D CD  1 
ATOM   8004 N  N   . GLY D  1 195 ? 9.008   6.284   -25.885 1.00 11.61 ? 195 GLY D N   1 
ATOM   8005 C  CA  . GLY D  1 195 ? 9.949   6.769   -26.884 1.00 13.25 ? 195 GLY D CA  1 
ATOM   8006 C  C   . GLY D  1 195 ? 9.507   7.992   -27.639 1.00 12.78 ? 195 GLY D C   1 
ATOM   8007 O  O   . GLY D  1 195 ? 8.873   8.900   -27.098 1.00 12.90 ? 195 GLY D O   1 
ATOM   8008 N  N   . SER D  1 196 ? 9.808   8.004   -28.922 1.00 10.10 ? 196 SER D N   1 
ATOM   8009 C  CA  . SER D  1 196 ? 9.698   9.249   -29.693 1.00 10.23 ? 196 SER D CA  1 
ATOM   8010 C  C   . SER D  1 196 ? 9.151   8.989   -31.057 1.00 10.17 ? 196 SER D C   1 
ATOM   8011 O  O   . SER D  1 196 ? 9.060   7.827   -31.564 1.00 10.03 ? 196 SER D O   1 
ATOM   8012 C  CB  . SER D  1 196 ? 11.111  9.894   -29.812 1.00 10.83 ? 196 SER D CB  1 
ATOM   8013 O  OG  . SER D  1 196 ? 11.893  9.177   -30.840 1.00 10.23 ? 196 SER D OG  1 
ATOM   8014 N  N   . LEU D  1 197 ? 8.908   10.078  -31.765 1.00 10.28 ? 197 LEU D N   1 
ATOM   8015 C  CA  . LEU D  1 197 ? 8.693   9.947   -33.208 1.00 10.99 ? 197 LEU D CA  1 
ATOM   8016 C  C   . LEU D  1 197 ? 10.020  9.510   -33.817 1.00 9.20  ? 197 LEU D C   1 
ATOM   8017 O  O   . LEU D  1 197 ? 11.089  9.894   -33.407 1.00 9.95  ? 197 LEU D O   1 
ATOM   8018 C  CB  . LEU D  1 197 ? 8.404   11.373  -33.801 1.00 10.26 ? 197 LEU D CB  1 
ATOM   8019 C  CG  . LEU D  1 197 ? 7.063   12.014  -33.423 1.00 10.14 ? 197 LEU D CG  1 
ATOM   8020 C  CD1 . LEU D  1 197 ? 6.978   13.412  -34.045 1.00 12.92 ? 197 LEU D CD1 1 
ATOM   8021 C  CD2 . LEU D  1 197 ? 5.851   11.187  -33.686 1.00 10.85 ? 197 LEU D CD2 1 
ATOM   8022 N  N   . THR D  1 198 ? 9.933   8.595   -34.832 1.00 8.90  ? 198 THR D N   1 
ATOM   8023 C  CA  . THR D  1 198 ? 11.156  8.116   -35.463 1.00 9.68  ? 198 THR D CA  1 
ATOM   8024 C  C   . THR D  1 198 ? 11.657  8.960   -36.656 1.00 9.18  ? 198 THR D C   1 
ATOM   8025 O  O   . THR D  1 198 ? 12.615  8.575   -37.289 1.00 9.72  ? 198 THR D O   1 
ATOM   8026 C  CB  . THR D  1 198 ? 11.045  6.687   -35.918 1.00 8.74  ? 198 THR D CB  1 
ATOM   8027 O  OG1 . THR D  1 198 ? 10.107  6.657   -36.985 1.00 8.53  ? 198 THR D OG1 1 
ATOM   8028 C  CG2 . THR D  1 198 ? 10.535  5.710   -34.831 1.00 10.23 ? 198 THR D CG2 1 
ATOM   8029 N  N   . THR D  1 199 ? 10.936  10.054  -36.879 1.00 9.20  ? 199 THR D N   1 
ATOM   8030 C  CA  . THR D  1 199 ? 11.356  11.073  -37.887 1.00 9.84  ? 199 THR D CA  1 
ATOM   8031 C  C   . THR D  1 199 ? 11.407  12.409  -37.227 1.00 10.01 ? 199 THR D C   1 
ATOM   8032 O  O   . THR D  1 199 ? 10.735  12.578  -36.209 1.00 10.98 ? 199 THR D O   1 
ATOM   8033 C  CB  . THR D  1 199 ? 10.370  11.199  -39.101 1.00 10.37 ? 199 THR D CB  1 
ATOM   8034 O  OG1 . THR D  1 199 ? 9.172   11.764  -38.612 1.00 12.27 ? 199 THR D OG1 1 
ATOM   8035 C  CG2 . THR D  1 199 ? 10.023  9.805   -39.687 1.00 11.08 ? 199 THR D CG2 1 
ATOM   8036 N  N   . PRO D  1 200 ? 12.128  13.368  -37.858 1.00 9.84  ? 200 PRO D N   1 
ATOM   8037 C  CA  . PRO D  1 200 ? 11.934  14.760  -37.377 1.00 11.09 ? 200 PRO D CA  1 
ATOM   8038 C  C   . PRO D  1 200 ? 10.465  15.079  -37.226 1.00 11.40 ? 200 PRO D C   1 
ATOM   8039 O  O   . PRO D  1 200 ? 9.668   14.671  -38.039 1.00 12.26 ? 200 PRO D O   1 
ATOM   8040 C  CB  . PRO D  1 200 ? 12.598  15.583  -38.512 1.00 10.95 ? 200 PRO D CB  1 
ATOM   8041 C  CG  . PRO D  1 200 ? 13.736  14.659  -38.940 1.00 10.83 ? 200 PRO D CG  1 
ATOM   8042 C  CD  . PRO D  1 200 ? 13.056  13.267  -38.990 1.00 10.65 ? 200 PRO D CD  1 
ATOM   8043 N  N   . PRO D  1 201 ? 10.108  15.832  -36.177 1.00 10.73 ? 201 PRO D N   1 
ATOM   8044 C  CA  . PRO D  1 201 ? 11.024  16.458  -35.180 1.00 11.48 ? 201 PRO D CA  1 
ATOM   8045 C  C   . PRO D  1 201 ? 11.400  15.615  -34.036 1.00 12.09 ? 201 PRO D C   1 
ATOM   8046 O  O   . PRO D  1 201 ? 12.032  16.126  -33.125 1.00 12.62 ? 201 PRO D O   1 
ATOM   8047 C  CB  . PRO D  1 201 ? 10.218  17.653  -34.660 1.00 13.71 ? 201 PRO D CB  1 
ATOM   8048 C  CG  . PRO D  1 201 ? 8.791   17.294  -34.939 1.00 16.95 ? 201 PRO D CG  1 
ATOM   8049 C  CD  . PRO D  1 201 ? 8.711   16.335  -36.082 1.00 13.73 ? 201 PRO D CD  1 
ATOM   8050 N  N   . CYS D  1 202 ? 11.124  14.302  -34.060 1.00 10.53 ? 202 CYS D N   1 
ATOM   8051 C  CA  . CYS D  1 202 ? 11.705  13.353  -33.056 1.00 10.91 ? 202 CYS D CA  1 
ATOM   8052 C  C   . CYS D  1 202 ? 11.150  13.607  -31.632 1.00 11.44 ? 202 CYS D C   1 
ATOM   8053 O  O   . CYS D  1 202 ? 11.833  13.206  -30.686 1.00 11.21 ? 202 CYS D O   1 
ATOM   8054 C  CB  . CYS D  1 202 ? 13.243  13.330  -33.053 1.00 12.09 ? 202 CYS D CB  1 
ATOM   8055 S  SG  . CYS D  1 202 ? 13.969  12.901  -34.621 1.00 11.72 ? 202 CYS D SG  1 
ATOM   8056 N  N   A ASN D  1 203 ? 9.960   14.221  -31.523 0.50 11.31 ? 203 ASN D N   1 
ATOM   8057 N  N   B ASN D  1 203 ? 10.010  14.191  -31.520 0.50 11.06 ? 203 ASN D N   1 
ATOM   8058 C  CA  A ASN D  1 203 ? 9.379   14.574  -30.177 0.50 12.03 ? 203 ASN D CA  1 
ATOM   8059 C  CA  B ASN D  1 203 ? 9.598   14.493  -30.166 0.50 11.86 ? 203 ASN D CA  1 
ATOM   8060 C  C   A ASN D  1 203 ? 9.284   13.334  -29.317 0.50 12.73 ? 203 ASN D C   1 
ATOM   8061 C  C   B ASN D  1 203 ? 9.543   13.243  -29.328 0.50 11.48 ? 203 ASN D C   1 
ATOM   8062 O  O   A ASN D  1 203 ? 8.603   12.374  -29.735 0.50 10.35 ? 203 ASN D O   1 
ATOM   8063 O  O   B ASN D  1 203 ? 9.135   12.213  -29.746 0.50 9.39  ? 203 ASN D O   1 
ATOM   8064 C  CB  A ASN D  1 203 ? 8.002   15.192  -30.278 0.50 12.78 ? 203 ASN D CB  1 
ATOM   8065 C  CB  B ASN D  1 203 ? 8.307   15.210  -30.203 0.50 11.91 ? 203 ASN D CB  1 
ATOM   8066 C  CG  A ASN D  1 203 ? 7.951   16.389  -31.194 0.50 13.33 ? 203 ASN D CG  1 
ATOM   8067 C  CG  B ASN D  1 203 ? 8.338   16.373  -31.114 0.50 13.21 ? 203 ASN D CG  1 
ATOM   8068 O  OD1 A ASN D  1 203 ? 8.962   17.072  -31.428 0.50 14.48 ? 203 ASN D OD1 1 
ATOM   8069 O  OD1 B ASN D  1 203 ? 8.457   16.232  -32.335 0.50 13.76 ? 203 ASN D OD1 1 
ATOM   8070 N  ND2 A ASN D  1 203 ? 6.788   16.612  -31.741 0.50 12.63 ? 203 ASN D ND2 1 
ATOM   8071 N  ND2 B ASN D  1 203 ? 8.200   17.510  -30.547 0.50 12.47 ? 203 ASN D ND2 1 
ATOM   8072 N  N   . PRO D  1 204 ? 9.872   13.365  -28.080 1.00 11.54 ? 204 PRO D N   1 
ATOM   8073 C  CA  . PRO D  1 204 ? 9.813   12.186  -27.153 1.00 12.74 ? 204 PRO D CA  1 
ATOM   8074 C  C   . PRO D  1 204 ? 8.446   12.058  -26.441 1.00 13.50 ? 204 PRO D C   1 
ATOM   8075 O  O   . PRO D  1 204 ? 8.411   12.097  -25.156 1.00 15.13 ? 204 PRO D O   1 
ATOM   8076 C  CB  . PRO D  1 204 ? 10.954  12.441  -26.133 1.00 13.29 ? 204 PRO D CB  1 
ATOM   8077 C  CG  . PRO D  1 204 ? 10.979  13.958  -26.088 1.00 14.12 ? 204 PRO D CG  1 
ATOM   8078 C  CD  . PRO D  1 204 ? 10.747  14.437  -27.518 1.00 13.76 ? 204 PRO D CD  1 
ATOM   8079 N  N   . THR D  1 205 ? 7.396   11.920  -27.194 1.00 11.55 ? 205 THR D N   1 
ATOM   8080 C  CA  . THR D  1 205 ? 6.036   12.021  -26.755 1.00 11.34 ? 205 THR D CA  1 
ATOM   8081 C  C   . THR D  1 205 ? 5.157   10.838  -27.125 1.00 11.19 ? 205 THR D C   1 
ATOM   8082 O  O   . THR D  1 205 ? 3.961   10.898  -27.099 1.00 12.18 ? 205 THR D O   1 
ATOM   8083 C  CB  . THR D  1 205 ? 5.397   13.276  -27.388 1.00 12.65 ? 205 THR D CB  1 
ATOM   8084 O  OG1 . THR D  1 205 ? 5.487   13.163  -28.827 1.00 13.85 ? 205 THR D OG1 1 
ATOM   8085 C  CG2 . THR D  1 205 ? 6.099   14.642  -26.905 1.00 13.15 ? 205 THR D CG2 1 
ATOM   8086 N  N   . VAL D  1 206 ? 5.916   9.743   -27.487 1.00 11.64 ? 206 VAL D N   1 
ATOM   8087 C  CA  . VAL D  1 206 ? 5.210   8.546   -27.961 1.00 12.37 ? 206 VAL D CA  1 
ATOM   8088 C  C   . VAL D  1 206 ? 5.244   7.335   -26.987 1.00 10.72 ? 206 VAL D C   1 
ATOM   8089 O  O   . VAL D  1 206 ? 6.282   6.923   -26.587 1.00 12.98 ? 206 VAL D O   1 
ATOM   8090 C  CB  . VAL D  1 206 ? 5.801   8.073   -29.325 1.00 9.80  ? 206 VAL D CB  1 
ATOM   8091 C  CG1 . VAL D  1 206 ? 4.986   6.858   -29.792 1.00 11.94 ? 206 VAL D CG1 1 
ATOM   8092 C  CG2 . VAL D  1 206 ? 5.676   9.200   -30.408 1.00 13.13 ? 206 VAL D CG2 1 
ATOM   8093 N  N   . LEU D  1 207 ? 4.060   6.904   -26.720 1.00 10.89 ? 207 LEU D N   1 
ATOM   8094 C  CA  . LEU D  1 207 ? 3.936   5.609   -26.031 1.00 13.20 ? 207 LEU D CA  1 
ATOM   8095 C  C   . LEU D  1 207 ? 3.850   4.553   -27.149 1.00 10.63 ? 207 LEU D C   1 
ATOM   8096 O  O   . LEU D  1 207 ? 2.915   4.506   -27.900 1.00 11.55 ? 207 LEU D O   1 
ATOM   8097 C  CB  . LEU D  1 207 ? 2.693   5.659   -25.187 1.00 15.69 ? 207 LEU D CB  1 
ATOM   8098 C  CG  . LEU D  1 207 ? 2.597   4.343   -24.338 1.00 19.18 ? 207 LEU D CG  1 
ATOM   8099 C  CD1 . LEU D  1 207 ? 3.650   4.319   -23.201 1.00 20.68 ? 207 LEU D CD1 1 
ATOM   8100 C  CD2 . LEU D  1 207 ? 1.216   4.306   -23.792 1.00 25.27 ? 207 LEU D CD2 1 
ATOM   8101 N  N   . TRP D  1 208 ? 4.886   3.708   -27.178 1.00 10.41 ? 208 TRP D N   1 
ATOM   8102 C  CA  . TRP D  1 208 ? 4.975   2.690   -28.261 1.00 10.73 ? 208 TRP D CA  1 
ATOM   8103 C  C   . TRP D  1 208 ? 4.402   1.365   -27.827 1.00 10.45 ? 208 TRP D C   1 
ATOM   8104 O  O   . TRP D  1 208 ? 4.714   0.934   -26.694 1.00 12.67 ? 208 TRP D O   1 
ATOM   8105 C  CB  . TRP D  1 208 ? 6.433   2.437   -28.654 1.00 10.92 ? 208 TRP D CB  1 
ATOM   8106 C  CG  . TRP D  1 208 ? 6.963   3.528   -29.554 1.00 9.57  ? 208 TRP D CG  1 
ATOM   8107 C  CD1 . TRP D  1 208 ? 7.697   4.664   -29.205 1.00 11.45 ? 208 TRP D CD1 1 
ATOM   8108 C  CD2 . TRP D  1 208 ? 6.781   3.534   -30.987 1.00 10.50 ? 208 TRP D CD2 1 
ATOM   8109 N  NE1 . TRP D  1 208 ? 7.875   5.417   -30.370 1.00 10.16 ? 208 TRP D NE1 1 
ATOM   8110 C  CE2 . TRP D  1 208 ? 7.345   4.776   -31.468 1.00 9.87  ? 208 TRP D CE2 1 
ATOM   8111 C  CE3 . TRP D  1 208 ? 6.099   2.722   -31.902 1.00 9.97  ? 208 TRP D CE3 1 
ATOM   8112 C  CZ2 . TRP D  1 208 ? 7.334   5.117   -32.844 1.00 10.27 ? 208 TRP D CZ2 1 
ATOM   8113 C  CZ3 . TRP D  1 208 ? 6.112   3.042   -33.256 1.00 10.82 ? 208 TRP D CZ3 1 
ATOM   8114 C  CH2 . TRP D  1 208 ? 6.672   4.237   -33.727 1.00 10.77 ? 208 TRP D CH2 1 
ATOM   8115 N  N   . THR D  1 209 ? 3.666   0.734   -28.708 1.00 9.29  ? 209 THR D N   1 
ATOM   8116 C  CA  . THR D  1 209 ? 3.189   -0.653  -28.541 1.00 10.09 ? 209 THR D CA  1 
ATOM   8117 C  C   . THR D  1 209 ? 3.638   -1.389  -29.793 1.00 9.12  ? 209 THR D C   1 
ATOM   8118 O  O   . THR D  1 209 ? 3.187   -1.036  -30.923 1.00 10.76 ? 209 THR D O   1 
ATOM   8119 C  CB  . THR D  1 209 ? 1.689   -0.697  -28.467 1.00 10.60 ? 209 THR D CB  1 
ATOM   8120 O  OG1 . THR D  1 209 ? 1.314   0.051   -27.274 1.00 11.60 ? 209 THR D OG1 1 
ATOM   8121 C  CG2 . THR D  1 209 ? 1.179   -2.105  -28.229 1.00 11.80 ? 209 THR D CG2 1 
ATOM   8122 N  N   . VAL D  1 210 ? 4.542   -2.317  -29.669 1.00 10.27 ? 210 VAL D N   1 
ATOM   8123 C  CA  . VAL D  1 210 ? 4.979   -3.144  -30.837 1.00 9.81  ? 210 VAL D CA  1 
ATOM   8124 C  C   . VAL D  1 210 ? 4.402   -4.542  -30.635 1.00 9.57  ? 210 VAL D C   1 
ATOM   8125 O  O   . VAL D  1 210 ? 4.711   -5.135  -29.591 1.00 10.17 ? 210 VAL D O   1 
ATOM   8126 C  CB  . VAL D  1 210 ? 6.524   -3.182  -30.875 1.00 9.76  ? 210 VAL D CB  1 
ATOM   8127 C  CG1 . VAL D  1 210 ? 6.948   -4.037  -32.094 1.00 10.82 ? 210 VAL D CG1 1 
ATOM   8128 C  CG2 . VAL D  1 210 ? 7.186   -1.783  -30.879 1.00 10.03 ? 210 VAL D CG2 1 
ATOM   8129 N  N   . PHE D  1 211 ? 3.584   -5.028  -31.529 1.00 10.04 ? 211 PHE D N   1 
ATOM   8130 C  CA  . PHE D  1 211 ? 2.986   -6.369  -31.323 1.00 9.71  ? 211 PHE D CA  1 
ATOM   8131 C  C   . PHE D  1 211 ? 4.116   -7.391  -31.408 1.00 10.72 ? 211 PHE D C   1 
ATOM   8132 O  O   . PHE D  1 211 ? 5.074   -7.328  -32.203 1.00 11.89 ? 211 PHE D O   1 
ATOM   8133 C  CB  . PHE D  1 211 ? 1.856   -6.564  -32.325 1.00 11.89 ? 211 PHE D CB  1 
ATOM   8134 C  CG  . PHE D  1 211 ? 0.710   -5.635  -32.079 1.00 10.95 ? 211 PHE D CG  1 
ATOM   8135 C  CD1 . PHE D  1 211 ? -0.051  -5.778  -30.908 1.00 12.68 ? 211 PHE D CD1 1 
ATOM   8136 C  CD2 . PHE D  1 211 ? 0.420   -4.596  -32.969 1.00 14.56 ? 211 PHE D CD2 1 
ATOM   8137 C  CE1 . PHE D  1 211 ? -1.082  -4.874  -30.622 1.00 12.30 ? 211 PHE D CE1 1 
ATOM   8138 C  CE2 . PHE D  1 211 ? -0.603  -3.705  -32.696 1.00 14.00 ? 211 PHE D CE2 1 
ATOM   8139 C  CZ  . PHE D  1 211 ? -1.383  -3.854  -31.543 1.00 13.59 ? 211 PHE D CZ  1 
ATOM   8140 N  N   . ARG D  1 212 ? 3.944   -8.467  -30.592 1.00 10.83 ? 212 ARG D N   1 
ATOM   8141 C  CA  . ARG D  1 212 ? 4.950   -9.535  -30.577 1.00 11.95 ? 212 ARG D CA  1 
ATOM   8142 C  C   . ARG D  1 212 ? 5.024   -10.257 -31.927 1.00 12.05 ? 212 ARG D C   1 
ATOM   8143 O  O   . ARG D  1 212 ? 6.128   -10.669 -32.386 1.00 13.94 ? 212 ARG D O   1 
ATOM   8144 C  CB  . ARG D  1 212 ? 4.563   -10.516 -29.473 1.00 12.08 ? 212 ARG D CB  1 
ATOM   8145 C  CG  . ARG D  1 212 ? 5.626   -11.642 -29.374 1.00 12.66 ? 212 ARG D CG  1 
ATOM   8146 C  CD  . ARG D  1 212 ? 5.143   -12.691 -28.383 1.00 17.43 ? 212 ARG D CD  1 
ATOM   8147 N  NE  . ARG D  1 212 ? 6.227   -13.607 -28.091 1.00 17.29 ? 212 ARG D NE  1 
ATOM   8148 C  CZ  . ARG D  1 212 ? 6.127   -14.528 -27.158 1.00 20.68 ? 212 ARG D CZ  1 
ATOM   8149 N  NH1 . ARG D  1 212 ? 4.959   -14.717 -26.581 1.00 21.28 ? 212 ARG D NH1 1 
ATOM   8150 N  NH2 . ARG D  1 212 ? 7.223   -15.234 -26.819 1.00 24.23 ? 212 ARG D NH2 1 
ATOM   8151 N  N   . ASN D  1 213 ? 3.891   -10.481 -32.534 1.00 11.46 ? 213 ASN D N   1 
ATOM   8152 C  CA  . ASN D  1 213 ? 3.876   -11.309 -33.734 1.00 12.53 ? 213 ASN D CA  1 
ATOM   8153 C  C   . ASN D  1 213 ? 3.834   -10.460 -34.998 1.00 13.38 ? 213 ASN D C   1 
ATOM   8154 O  O   . ASN D  1 213 ? 3.090   -9.457  -35.067 1.00 11.91 ? 213 ASN D O   1 
ATOM   8155 C  CB  . ASN D  1 213 ? 2.612   -12.209 -33.678 1.00 14.09 ? 213 ASN D CB  1 
ATOM   8156 C  CG  . ASN D  1 213 ? 2.676   -13.212 -32.530 1.00 17.61 ? 213 ASN D CG  1 
ATOM   8157 O  OD1 . ASN D  1 213 ? 3.689   -13.841 -32.305 1.00 21.79 ? 213 ASN D OD1 1 
ATOM   8158 N  ND2 . ASN D  1 213 ? 1.661   -13.163 -31.716 1.00 20.65 ? 213 ASN D ND2 1 
ATOM   8159 N  N   . PRO D  1 214 ? 4.576   -10.819 -36.024 1.00 12.10 ? 214 PRO D N   1 
ATOM   8160 C  CA  . PRO D  1 214 ? 4.533   -10.109 -37.290 1.00 11.85 ? 214 PRO D CA  1 
ATOM   8161 C  C   . PRO D  1 214 ? 3.355   -10.533 -38.152 1.00 10.82 ? 214 PRO D C   1 
ATOM   8162 O  O   . PRO D  1 214 ? 2.700   -11.547 -37.917 1.00 13.30 ? 214 PRO D O   1 
ATOM   8163 C  CB  . PRO D  1 214 ? 5.830   -10.514 -37.998 1.00 11.44 ? 214 PRO D CB  1 
ATOM   8164 C  CG  . PRO D  1 214 ? 5.934   -11.977 -37.588 1.00 13.68 ? 214 PRO D CG  1 
ATOM   8165 C  CD  . PRO D  1 214 ? 5.557   -11.951 -36.077 1.00 13.84 ? 214 PRO D CD  1 
ATOM   8166 N  N   . VAL D  1 215 ? 3.083   -9.759  -39.199 1.00 10.69 ? 215 VAL D N   1 
ATOM   8167 C  CA  . VAL D  1 215 ? 2.198   -10.177 -40.272 1.00 10.02 ? 215 VAL D CA  1 
ATOM   8168 C  C   . VAL D  1 215 ? 3.063   -10.467 -41.467 1.00 9.73  ? 215 VAL D C   1 
ATOM   8169 O  O   . VAL D  1 215 ? 4.266   -10.172 -41.420 1.00 11.33 ? 215 VAL D O   1 
ATOM   8170 C  CB  . VAL D  1 215 ? 1.152   -9.098  -40.625 1.00 10.37 ? 215 VAL D CB  1 
ATOM   8171 C  CG1 . VAL D  1 215 ? 0.249   -8.755  -39.417 1.00 12.47 ? 215 VAL D CG1 1 
ATOM   8172 C  CG2 . VAL D  1 215 ? 1.800   -7.792  -41.206 1.00 10.32 ? 215 VAL D CG2 1 
ATOM   8173 N  N   . GLN D  1 216 ? 2.483   -10.989 -42.544 1.00 9.92  ? 216 GLN D N   1 
ATOM   8174 C  CA  . GLN D  1 216 ? 3.256   -11.301 -43.728 1.00 10.26 ? 216 GLN D CA  1 
ATOM   8175 C  C   . GLN D  1 216 ? 2.669   -10.534 -44.904 1.00 9.42  ? 216 GLN D C   1 
ATOM   8176 O  O   . GLN D  1 216 ? 1.422   -10.372 -45.004 1.00 10.57 ? 216 GLN D O   1 
ATOM   8177 C  CB  . GLN D  1 216 ? 3.127   -12.819 -44.108 1.00 12.25 ? 216 GLN D CB  1 
ATOM   8178 C  CG  . GLN D  1 216 ? 3.942   -13.663 -43.207 1.00 13.50 ? 216 GLN D CG  1 
ATOM   8179 C  CD  . GLN D  1 216 ? 3.842   -15.133 -43.615 1.00 16.11 ? 216 GLN D CD  1 
ATOM   8180 O  OE1 . GLN D  1 216 ? 3.325   -15.573 -44.658 1.00 15.63 ? 216 GLN D OE1 1 
ATOM   8181 N  NE2 . GLN D  1 216 ? 4.359   -15.939 -42.688 1.00 21.08 ? 216 GLN D NE2 1 
ATOM   8182 N  N   . ILE D  1 217 ? 3.490   -10.064 -45.816 1.00 9.08  ? 217 ILE D N   1 
ATOM   8183 C  CA  . ILE D  1 217 ? 3.092   -9.570  -47.159 1.00 9.55  ? 217 ILE D CA  1 
ATOM   8184 C  C   . ILE D  1 217 ? 4.021   -10.279 -48.164 1.00 9.18  ? 217 ILE D C   1 
ATOM   8185 O  O   . ILE D  1 217 ? 5.136   -10.732 -47.776 1.00 10.38 ? 217 ILE D O   1 
ATOM   8186 C  CB  . ILE D  1 217 ? 3.116   -8.032  -47.328 1.00 9.46  ? 217 ILE D CB  1 
ATOM   8187 C  CG1 . ILE D  1 217 ? 4.554   -7.487  -47.297 1.00 11.16 ? 217 ILE D CG1 1 
ATOM   8188 C  CG2 . ILE D  1 217 ? 2.251   -7.368  -46.255 1.00 12.10 ? 217 ILE D CG2 1 
ATOM   8189 C  CD1 . ILE D  1 217 ? 4.578   -5.931  -47.560 1.00 12.63 ? 217 ILE D CD1 1 
ATOM   8190 N  N   . SER D  1 218 ? 3.632   -10.354 -49.446 1.00 9.26  ? 218 SER D N   1 
ATOM   8191 C  CA  . SER D  1 218 ? 4.551   -11.122 -50.341 1.00 9.62  ? 218 SER D CA  1 
ATOM   8192 C  C   . SER D  1 218 ? 5.756   -10.375 -50.837 1.00 10.69 ? 218 SER D C   1 
ATOM   8193 O  O   . SER D  1 218 ? 5.804   -9.117  -50.756 1.00 11.60 ? 218 SER D O   1 
ATOM   8194 C  CB  . SER D  1 218 ? 3.759   -11.649 -51.540 1.00 10.16 ? 218 SER D CB  1 
ATOM   8195 O  OG  . SER D  1 218 ? 3.353   -10.552 -52.388 1.00 11.41 ? 218 SER D OG  1 
ATOM   8196 N  N   A GLN D  1 219 ? 6.666   -11.140 -51.431 0.50 11.73 ? 219 GLN D N   1 
ATOM   8197 N  N   B GLN D  1 219 ? 6.722   -11.073 -51.429 0.50 10.85 ? 219 GLN D N   1 
ATOM   8198 C  CA  A GLN D  1 219 ? 7.769   -10.637 -52.170 0.50 11.91 ? 219 GLN D CA  1 
ATOM   8199 C  CA  B GLN D  1 219 ? 7.819   -10.387 -52.058 0.50 10.63 ? 219 GLN D CA  1 
ATOM   8200 C  C   A GLN D  1 219 ? 7.331   -9.552  -53.158 0.50 11.87 ? 219 GLN D C   1 
ATOM   8201 C  C   B GLN D  1 219 ? 7.266   -9.422  -53.149 0.50 11.00 ? 219 GLN D C   1 
ATOM   8202 O  O   A GLN D  1 219 ? 8.014   -8.512  -53.293 0.50 11.44 ? 219 GLN D O   1 
ATOM   8203 O  O   B GLN D  1 219 ? 7.763   -8.313  -53.352 0.50 10.28 ? 219 GLN D O   1 
ATOM   8204 C  CB  A GLN D  1 219 ? 8.365   -11.774 -52.998 0.50 14.20 ? 219 GLN D CB  1 
ATOM   8205 C  CB  B GLN D  1 219 ? 8.802   -11.384 -52.665 0.50 11.54 ? 219 GLN D CB  1 
ATOM   8206 C  CG  A GLN D  1 219 ? 9.573   -11.324 -53.834 0.50 16.30 ? 219 GLN D CG  1 
ATOM   8207 C  CG  B GLN D  1 219 ? 10.101  -10.759 -53.193 0.50 13.34 ? 219 GLN D CG  1 
ATOM   8208 C  CD  A GLN D  1 219 ? 10.206  -9.941  -53.417 0.50 22.66 ? 219 GLN D CD  1 
ATOM   8209 C  CD  B GLN D  1 219 ? 10.013  -10.262 -54.690 0.50 12.86 ? 219 GLN D CD  1 
ATOM   8210 O  OE1 A GLN D  1 219 ? 10.408  -9.625  -52.240 0.50 27.10 ? 219 GLN D OE1 1 
ATOM   8211 O  OE1 B GLN D  1 219 ? 9.089   -10.660 -55.418 0.50 18.60 ? 219 GLN D OE1 1 
ATOM   8212 N  NE2 A GLN D  1 219 ? 10.485  -9.108  -54.415 0.50 22.40 ? 219 GLN D NE2 1 
ATOM   8213 N  NE2 B GLN D  1 219 ? 11.022  -9.464  -55.142 0.50 17.63 ? 219 GLN D NE2 1 
ATOM   8214 N  N   . GLU D  1 220 ? 6.247   -9.838  -53.897 1.00 12.33 ? 220 GLU D N   1 
ATOM   8215 C  CA  . GLU D  1 220 ? 5.771   -8.942  -54.978 1.00 12.91 ? 220 GLU D CA  1 
ATOM   8216 C  C   . GLU D  1 220 ? 5.123   -7.676  -54.378 1.00 11.76 ? 220 GLU D C   1 
ATOM   8217 O  O   . GLU D  1 220 ? 5.402   -6.585  -54.887 1.00 12.15 ? 220 GLU D O   1 
ATOM   8218 C  CB  . GLU D  1 220 ? 4.752   -9.689  -55.873 1.00 14.30 ? 220 GLU D CB  1 
ATOM   8219 C  CG  . GLU D  1 220 ? 5.466   -10.808 -56.694 1.00 14.85 ? 220 GLU D CG  1 
ATOM   8220 C  CD  . GLU D  1 220 ? 5.653   -12.108 -55.955 1.00 22.43 ? 220 GLU D CD  1 
ATOM   8221 O  OE1 . GLU D  1 220 ? 5.248   -12.313 -54.793 1.00 20.56 ? 220 GLU D OE1 1 
ATOM   8222 O  OE2 . GLU D  1 220 ? 6.176   -13.014 -56.672 1.00 30.10 ? 220 GLU D OE2 1 
ATOM   8223 N  N   . GLN D  1 221 ? 4.472   -7.790  -53.214 1.00 9.85  ? 221 GLN D N   1 
ATOM   8224 C  CA  . GLN D  1 221 ? 3.955   -6.600  -52.536 1.00 9.93  ? 221 GLN D CA  1 
ATOM   8225 C  C   . GLN D  1 221 ? 5.085   -5.754  -52.039 1.00 11.49 ? 221 GLN D C   1 
ATOM   8226 O  O   . GLN D  1 221 ? 5.068   -4.506  -52.223 1.00 12.26 ? 221 GLN D O   1 
ATOM   8227 C  CB  . GLN D  1 221 ? 3.064   -6.972  -51.407 1.00 10.74 ? 221 GLN D CB  1 
ATOM   8228 C  CG  . GLN D  1 221 ? 1.774   -7.637  -51.886 1.00 10.10 ? 221 GLN D CG  1 
ATOM   8229 C  CD  . GLN D  1 221 ? 0.848   -8.016  -50.780 1.00 10.27 ? 221 GLN D CD  1 
ATOM   8230 O  OE1 . GLN D  1 221 ? 1.170   -8.921  -49.941 1.00 10.27 ? 221 GLN D OE1 1 
ATOM   8231 N  NE2 . GLN D  1 221 ? -0.312  -7.311  -50.635 1.00 10.77 ? 221 GLN D NE2 1 
ATOM   8232 N  N   . LEU D  1 222 ? 6.133   -6.345  -51.435 1.00 10.60 ? 222 LEU D N   1 
ATOM   8233 C  CA  . LEU D  1 222 ? 7.247   -5.572  -50.935 1.00 10.99 ? 222 LEU D CA  1 
ATOM   8234 C  C   . LEU D  1 222 ? 7.969   -4.882  -52.097 1.00 11.69 ? 222 LEU D C   1 
ATOM   8235 O  O   . LEU D  1 222 ? 8.373   -3.736  -51.986 1.00 11.37 ? 222 LEU D O   1 
ATOM   8236 C  CB  . LEU D  1 222 ? 8.177   -6.551  -50.226 1.00 12.14 ? 222 LEU D CB  1 
ATOM   8237 C  CG  . LEU D  1 222 ? 7.871   -6.722  -48.799 1.00 13.35 ? 222 LEU D CG  1 
ATOM   8238 C  CD1 . LEU D  1 222 ? 8.609   -7.982  -48.296 1.00 14.15 ? 222 LEU D CD1 1 
ATOM   8239 C  CD2 . LEU D  1 222 ? 8.256   -5.492  -47.889 1.00 14.07 ? 222 LEU D CD2 1 
ATOM   8240 N  N   . LEU D  1 223 ? 8.158   -5.562  -53.263 1.00 11.56 ? 223 LEU D N   1 
ATOM   8241 C  CA  . LEU D  1 223 ? 8.892   -4.973  -54.361 1.00 11.12 ? 223 LEU D CA  1 
ATOM   8242 C  C   . LEU D  1 223 ? 8.046   -3.805  -54.890 1.00 12.23 ? 223 LEU D C   1 
ATOM   8243 O  O   . LEU D  1 223 ? 8.603   -2.774  -55.263 1.00 12.82 ? 223 LEU D O   1 
ATOM   8244 C  CB  . LEU D  1 223 ? 9.130   -6.033  -55.466 1.00 11.90 ? 223 LEU D CB  1 
ATOM   8245 C  CG  . LEU D  1 223 ? 9.788   -5.440  -56.720 1.00 13.56 ? 223 LEU D CG  1 
ATOM   8246 C  CD1 . LEU D  1 223 ? 11.173  -5.024  -56.329 1.00 16.50 ? 223 LEU D CD1 1 
ATOM   8247 C  CD2 . LEU D  1 223 ? 9.963   -6.591  -57.753 1.00 14.66 ? 223 LEU D CD2 1 
ATOM   8248 N  N   . ALA D  1 224 ? 6.751   -3.956  -54.913 1.00 12.34 ? 224 ALA D N   1 
ATOM   8249 C  CA  . ALA D  1 224 ? 5.898   -2.860  -55.396 1.00 12.67 ? 224 ALA D CA  1 
ATOM   8250 C  C   . ALA D  1 224 ? 6.015   -1.644  -54.468 1.00 12.80 ? 224 ALA D C   1 
ATOM   8251 O  O   . ALA D  1 224 ? 6.226   -0.499  -54.920 1.00 15.32 ? 224 ALA D O   1 
ATOM   8252 C  CB  . ALA D  1 224 ? 4.433   -3.328  -55.532 1.00 13.54 ? 224 ALA D CB  1 
ATOM   8253 N  N   . LEU D  1 225 ? 5.941   -1.876  -53.142 1.00 11.92 ? 225 LEU D N   1 
ATOM   8254 C  CA  . LEU D  1 225 ? 6.139   -0.827  -52.172 1.00 11.86 ? 225 LEU D CA  1 
ATOM   8255 C  C   . LEU D  1 225 ? 7.459   -0.155  -52.344 1.00 12.87 ? 225 LEU D C   1 
ATOM   8256 O  O   . LEU D  1 225 ? 7.554   1.103   -52.339 1.00 14.27 ? 225 LEU D O   1 
ATOM   8257 C  CB  . LEU D  1 225 ? 5.926   -1.419  -50.781 1.00 12.53 ? 225 LEU D CB  1 
ATOM   8258 C  CG  . LEU D  1 225 ? 6.104   -0.402  -49.626 1.00 13.49 ? 225 LEU D CG  1 
ATOM   8259 C  CD1 . LEU D  1 225 ? 5.017   0.764   -49.712 1.00 14.66 ? 225 LEU D CD1 1 
ATOM   8260 C  CD2 . LEU D  1 225 ? 5.987   -1.149  -48.295 1.00 14.42 ? 225 LEU D CD2 1 
ATOM   8261 N  N   . GLU D  1 226 ? 8.516   -0.916  -52.476 1.00 11.54 ? 226 GLU D N   1 
ATOM   8262 C  CA  . GLU D  1 226 ? 9.858   -0.438  -52.609 1.00 12.93 ? 226 GLU D CA  1 
ATOM   8263 C  C   . GLU D  1 226 ? 10.171  0.277   -53.891 1.00 13.38 ? 226 GLU D C   1 
ATOM   8264 O  O   . GLU D  1 226 ? 11.225  0.963   -53.900 1.00 16.76 ? 226 GLU D O   1 
ATOM   8265 C  CB  . GLU D  1 226 ? 10.880  -1.653  -52.472 1.00 12.42 ? 226 GLU D CB  1 
ATOM   8266 C  CG  . GLU D  1 226 ? 10.916  -2.256  -51.087 1.00 11.36 ? 226 GLU D CG  1 
ATOM   8267 C  CD  . GLU D  1 226 ? 11.307  -3.692  -51.114 1.00 14.40 ? 226 GLU D CD  1 
ATOM   8268 O  OE1 . GLU D  1 226 ? 11.545  -4.312  -52.187 1.00 13.91 ? 226 GLU D OE1 1 
ATOM   8269 O  OE2 . GLU D  1 226 ? 11.353  -4.267  -50.021 1.00 15.15 ? 226 GLU D OE2 1 
ATOM   8270 N  N   . THR D  1 227 ? 9.357   0.154   -54.898 1.00 12.81 ? 227 THR D N   1 
ATOM   8271 C  CA  . THR D  1 227 ? 9.701   0.774   -56.213 1.00 13.94 ? 227 THR D CA  1 
ATOM   8272 C  C   . THR D  1 227 ? 8.632   1.731   -56.654 1.00 15.43 ? 227 THR D C   1 
ATOM   8273 O  O   . THR D  1 227 ? 8.822   2.380   -57.686 1.00 18.96 ? 227 THR D O   1 
ATOM   8274 C  CB  . THR D  1 227 ? 9.896   -0.301  -57.291 1.00 16.90 ? 227 THR D CB  1 
ATOM   8275 O  OG1 . THR D  1 227 ? 8.704   -1.080  -57.431 1.00 15.93 ? 227 THR D OG1 1 
ATOM   8276 C  CG2 . THR D  1 227 ? 11.131  -1.203  -56.970 1.00 17.68 ? 227 THR D CG2 1 
ATOM   8277 N  N   . ALA D  1 228 ? 7.602   1.915   -55.889 1.00 13.95 ? 228 ALA D N   1 
ATOM   8278 C  CA  . ALA D  1 228 ? 6.451   2.737   -56.353 1.00 14.91 ? 228 ALA D CA  1 
ATOM   8279 C  C   . ALA D  1 228 ? 6.703   4.243   -56.187 1.00 17.18 ? 228 ALA D C   1 
ATOM   8280 O  O   . ALA D  1 228 ? 6.104   5.027   -56.951 1.00 20.45 ? 228 ALA D O   1 
ATOM   8281 C  CB  . ALA D  1 228 ? 5.195   2.372   -55.621 1.00 19.74 ? 228 ALA D CB  1 
ATOM   8282 N  N   . LEU D  1 229 ? 7.414   4.630   -55.178 1.00 14.93 ? 229 LEU D N   1 
ATOM   8283 C  CA  . LEU D  1 229 ? 7.350   6.040   -54.736 1.00 15.63 ? 229 LEU D CA  1 
ATOM   8284 C  C   . LEU D  1 229 ? 8.686   6.774   -54.814 1.00 15.81 ? 229 LEU D C   1 
ATOM   8285 O  O   . LEU D  1 229 ? 9.762   6.173   -54.753 1.00 14.39 ? 229 LEU D O   1 
ATOM   8286 C  CB  . LEU D  1 229 ? 6.894   6.112   -53.282 1.00 15.20 ? 229 LEU D CB  1 
ATOM   8287 C  CG  . LEU D  1 229 ? 5.576   5.286   -52.935 1.00 15.14 ? 229 LEU D CG  1 
ATOM   8288 C  CD1 . LEU D  1 229 ? 5.288   5.220   -51.455 1.00 17.84 ? 229 LEU D CD1 1 
ATOM   8289 C  CD2 . LEU D  1 229 ? 4.398   5.825   -53.769 1.00 18.54 ? 229 LEU D CD2 1 
ATOM   8290 N  N   . TYR D  1 230 ? 8.542   8.121   -54.878 1.00 16.56 ? 230 TYR D N   1 
ATOM   8291 C  CA  . TYR D  1 230 ? 9.630   9.079   -54.843 1.00 17.58 ? 230 TYR D CA  1 
ATOM   8292 C  C   . TYR D  1 230 ? 9.499   10.007  -53.684 1.00 15.16 ? 230 TYR D C   1 
ATOM   8293 O  O   . TYR D  1 230 ? 8.375   10.438  -53.335 1.00 14.65 ? 230 TYR D O   1 
ATOM   8294 C  CB  . TYR D  1 230 ? 9.717   9.859   -56.192 1.00 16.78 ? 230 TYR D CB  1 
ATOM   8295 C  CG  . TYR D  1 230 ? 10.163  8.989   -57.279 1.00 19.77 ? 230 TYR D CG  1 
ATOM   8296 C  CD1 . TYR D  1 230 ? 9.248   8.119   -57.915 1.00 22.89 ? 230 TYR D CD1 1 
ATOM   8297 C  CD2 . TYR D  1 230 ? 11.486  8.930   -57.664 1.00 24.00 ? 230 TYR D CD2 1 
ATOM   8298 C  CE1 . TYR D  1 230 ? 9.631   7.249   -58.888 1.00 27.32 ? 230 TYR D CE1 1 
ATOM   8299 C  CE2 . TYR D  1 230 ? 11.878  8.060   -58.707 1.00 25.11 ? 230 TYR D CE2 1 
ATOM   8300 C  CZ  . TYR D  1 230 ? 10.928  7.234   -59.298 1.00 26.96 ? 230 TYR D CZ  1 
ATOM   8301 O  OH  . TYR D  1 230 ? 11.234  6.337   -60.291 1.00 30.75 ? 230 TYR D OH  1 
ATOM   8302 N  N   . CYS D  1 231 ? 10.626  10.488  -53.129 1.00 18.18 ? 231 CYS D N   1 
ATOM   8303 C  CA  . CYS D  1 231 ? 10.514  11.485  -52.075 1.00 20.01 ? 231 CYS D CA  1 
ATOM   8304 C  C   . CYS D  1 231 ? 10.411  12.892  -52.596 1.00 15.35 ? 231 CYS D C   1 
ATOM   8305 O  O   . CYS D  1 231 ? 10.139  13.799  -51.861 1.00 19.87 ? 231 CYS D O   1 
ATOM   8306 C  CB  . CYS D  1 231 ? 11.738  11.596  -51.143 1.00 24.64 ? 231 CYS D CB  1 
ATOM   8307 S  SG  . CYS D  1 231 ? 12.569  10.102  -50.564 1.00 33.56 ? 231 CYS D SG  1 
ATOM   8308 N  N   . THR D  1 232 ? 10.617  13.004  -53.909 1.00 15.38 ? 232 THR D N   1 
ATOM   8309 C  CA  . THR D  1 232 ? 10.682  14.338  -54.555 1.00 16.55 ? 232 THR D CA  1 
ATOM   8310 C  C   . THR D  1 232 ? 9.359   14.639  -55.284 1.00 15.59 ? 232 THR D C   1 
ATOM   8311 O  O   . THR D  1 232 ? 8.521   13.765  -55.651 1.00 15.38 ? 232 THR D O   1 
ATOM   8312 C  CB  . THR D  1 232 ? 11.856  14.331  -55.559 1.00 18.94 ? 232 THR D CB  1 
ATOM   8313 O  OG1 . THR D  1 232 ? 11.879  13.071  -56.229 1.00 18.31 ? 232 THR D OG1 1 
ATOM   8314 C  CG2 . THR D  1 232 ? 13.230  14.486  -54.817 1.00 20.77 ? 232 THR D CG2 1 
ATOM   8315 N  N   . HIS D  1 233 ? 9.105   15.931  -55.519 1.00 15.53 ? 233 HIS D N   1 
ATOM   8316 C  CA  . HIS D  1 233 ? 8.022   16.359  -56.308 1.00 14.50 ? 233 HIS D CA  1 
ATOM   8317 C  C   . HIS D  1 233 ? 8.209   15.934  -57.748 1.00 15.34 ? 233 HIS D C   1 
ATOM   8318 O  O   . HIS D  1 233 ? 9.319   15.703  -58.251 1.00 16.08 ? 233 HIS D O   1 
ATOM   8319 C  CB  . HIS D  1 233 ? 8.004   17.909  -56.255 1.00 17.46 ? 233 HIS D CB  1 
ATOM   8320 C  CG  . HIS D  1 233 ? 7.471   18.415  -54.965 1.00 21.04 ? 233 HIS D CG  1 
ATOM   8321 N  ND1 . HIS D  1 233 ? 8.273   18.930  -53.972 1.00 26.94 ? 233 HIS D ND1 1 
ATOM   8322 C  CD2 . HIS D  1 233 ? 6.190   18.322  -54.421 1.00 23.09 ? 233 HIS D CD2 1 
ATOM   8323 C  CE1 . HIS D  1 233 ? 7.492   19.196  -52.864 1.00 24.97 ? 233 HIS D CE1 1 
ATOM   8324 N  NE2 . HIS D  1 233 ? 6.232   18.874  -53.159 1.00 28.43 ? 233 HIS D NE2 1 
ATOM   8325 N  N   . MET D  1 234 ? 7.096   15.800  -58.416 1.00 15.74 ? 234 MET D N   1 
ATOM   8326 C  CA  . MET D  1 234 ? 7.091   15.305  -59.796 1.00 16.89 ? 234 MET D CA  1 
ATOM   8327 C  C   . MET D  1 234 ? 8.037   16.101  -60.734 1.00 22.58 ? 234 MET D C   1 
ATOM   8328 O  O   . MET D  1 234 ? 8.726   15.482  -61.590 1.00 21.81 ? 234 MET D O   1 
ATOM   8329 C  CB  . MET D  1 234 ? 5.676   15.341  -60.322 1.00 18.63 ? 234 MET D CB  1 
ATOM   8330 C  CG  . MET D  1 234 ? 5.615   14.672  -61.682 1.00 21.19 ? 234 MET D CG  1 
ATOM   8331 S  SD  . MET D  1 234 ? 3.831   14.628  -62.139 1.00 29.78 ? 234 MET D SD  1 
ATOM   8332 C  CE  . MET D  1 234 ? 4.020   13.609  -63.604 1.00 31.83 ? 234 MET D CE  1 
ATOM   8333 N  N   . ASP D  1 235 ? 8.121   17.416  -60.505 1.00 20.06 ? 235 ASP D N   1 
ATOM   8334 C  CA  . ASP D  1 235 ? 8.929   18.213  -61.431 1.00 24.74 ? 235 ASP D CA  1 
ATOM   8335 C  C   . ASP D  1 235 ? 10.388  18.408  -60.973 1.00 23.30 ? 235 ASP D C   1 
ATOM   8336 O  O   . ASP D  1 235 ? 11.186  19.128  -61.600 1.00 23.74 ? 235 ASP D O   1 
ATOM   8337 C  CB  . ASP D  1 235 ? 8.200   19.544  -61.688 1.00 29.75 ? 235 ASP D CB  1 
ATOM   8338 C  CG  . ASP D  1 235 ? 8.049   20.401  -60.436 1.00 33.94 ? 235 ASP D CG  1 
ATOM   8339 O  OD1 . ASP D  1 235 ? 8.502   20.043  -59.295 1.00 35.67 ? 235 ASP D OD1 1 
ATOM   8340 O  OD2 . ASP D  1 235 ? 7.412   21.464  -60.573 1.00 37.00 ? 235 ASP D OD2 1 
ATOM   8341 N  N   . ASP D  1 236 ? 10.825  17.708  -59.930 1.00 22.05 ? 236 ASP D N   1 
ATOM   8342 C  CA  . ASP D  1 236 ? 12.188  17.847  -59.476 1.00 23.16 ? 236 ASP D CA  1 
ATOM   8343 C  C   . ASP D  1 236 ? 13.168  17.315  -60.516 1.00 24.19 ? 236 ASP D C   1 
ATOM   8344 O  O   . ASP D  1 236 ? 12.991  16.202  -61.017 1.00 21.20 ? 236 ASP D O   1 
ATOM   8345 C  CB  . ASP D  1 236 ? 12.380  17.081  -58.157 1.00 21.97 ? 236 ASP D CB  1 
ATOM   8346 C  CG  . ASP D  1 236 ? 13.613  17.542  -57.381 1.00 24.48 ? 236 ASP D CG  1 
ATOM   8347 O  OD1 . ASP D  1 236 ? 14.671  17.676  -57.994 1.00 24.26 ? 236 ASP D OD1 1 
ATOM   8348 O  OD2 . ASP D  1 236 ? 13.508  17.749  -56.153 1.00 27.20 ? 236 ASP D OD2 1 
ATOM   8349 N  N   . PRO D  1 237 ? 14.154  18.132  -60.935 1.00 24.32 ? 237 PRO D N   1 
ATOM   8350 C  CA  . PRO D  1 237 ? 15.130  17.576  -61.888 1.00 25.46 ? 237 PRO D CA  1 
ATOM   8351 C  C   . PRO D  1 237 ? 16.089  16.562  -61.279 1.00 29.46 ? 237 PRO D C   1 
ATOM   8352 O  O   . PRO D  1 237 ? 16.812  15.891  -62.056 1.00 29.24 ? 237 PRO D O   1 
ATOM   8353 C  CB  . PRO D  1 237 ? 15.928  18.826  -62.338 1.00 27.67 ? 237 PRO D CB  1 
ATOM   8354 C  CG  . PRO D  1 237 ? 15.774  19.790  -61.200 1.00 28.40 ? 237 PRO D CG  1 
ATOM   8355 C  CD  . PRO D  1 237 ? 14.419  19.550  -60.566 1.00 27.17 ? 237 PRO D CD  1 
ATOM   8356 N  N   . SER D  1 238 ? 16.112  16.449  -59.936 1.00 28.42 ? 238 SER D N   1 
ATOM   8357 C  CA  . SER D  1 238 ? 16.954  15.452  -59.295 1.00 28.35 ? 238 SER D CA  1 
ATOM   8358 C  C   . SER D  1 238 ? 16.063  14.496  -58.466 1.00 22.97 ? 238 SER D C   1 
ATOM   8359 O  O   . SER D  1 238 ? 15.969  14.645  -57.288 1.00 25.89 ? 238 SER D O   1 
ATOM   8360 C  CB  . SER D  1 238 ? 18.003  16.116  -58.406 1.00 30.75 ? 238 SER D CB  1 
ATOM   8361 O  OG  . SER D  1 238 ? 18.982  15.129  -58.110 1.00 42.22 ? 238 SER D OG  1 
ATOM   8362 N  N   . PRO D  1 239 ? 15.440  13.555  -59.138 1.00 23.40 ? 239 PRO D N   1 
ATOM   8363 C  CA  . PRO D  1 239 ? 14.530  12.677  -58.346 1.00 24.12 ? 239 PRO D CA  1 
ATOM   8364 C  C   . PRO D  1 239 ? 15.218  11.708  -57.437 1.00 27.16 ? 239 PRO D C   1 
ATOM   8365 O  O   . PRO D  1 239 ? 16.256  11.153  -57.792 1.00 28.36 ? 239 PRO D O   1 
ATOM   8366 C  CB  . PRO D  1 239 ? 13.747  11.928  -59.397 1.00 22.59 ? 239 PRO D CB  1 
ATOM   8367 C  CG  . PRO D  1 239 ? 14.384  12.218  -60.729 1.00 26.36 ? 239 PRO D CG  1 
ATOM   8368 C  CD  . PRO D  1 239 ? 15.337  13.335  -60.574 1.00 25.62 ? 239 PRO D CD  1 
ATOM   8369 N  N   . ARG D  1 240 ? 14.565  11.408  -56.320 1.00 25.94 ? 240 ARG D N   1 
ATOM   8370 C  CA  . ARG D  1 240 ? 15.118  10.463  -55.345 1.00 23.18 ? 240 ARG D CA  1 
ATOM   8371 C  C   . ARG D  1 240 ? 14.000  9.385   -55.087 1.00 23.09 ? 240 ARG D C   1 
ATOM   8372 O  O   . ARG D  1 240 ? 12.879  9.761   -54.723 1.00 20.56 ? 240 ARG D O   1 
ATOM   8373 C  CB  . ARG D  1 240 ? 15.429  11.131  -54.009 1.00 29.27 ? 240 ARG D CB  1 
ATOM   8374 N  N   . GLU D  1 241 ? 14.305  8.089   -55.314 1.00 20.54 ? 241 GLU D N   1 
ATOM   8375 C  CA  . GLU D  1 241 ? 13.455  6.968   -54.860 1.00 19.15 ? 241 GLU D CA  1 
ATOM   8376 C  C   . GLU D  1 241 ? 13.280  6.893   -53.389 1.00 17.30 ? 241 GLU D C   1 
ATOM   8377 O  O   . GLU D  1 241 ? 14.200  7.092   -52.590 1.00 18.73 ? 241 GLU D O   1 
ATOM   8378 C  CB  . GLU D  1 241 ? 14.029  5.674   -55.368 1.00 21.17 ? 241 GLU D CB  1 
ATOM   8379 C  CG  . GLU D  1 241 ? 14.016  5.639   -56.891 1.00 25.73 ? 241 GLU D CG  1 
ATOM   8380 C  CD  . GLU D  1 241 ? 14.900  4.540   -57.370 1.00 29.13 ? 241 GLU D CD  1 
ATOM   8381 O  OE1 . GLU D  1 241 ? 16.124  4.706   -57.188 1.00 38.00 ? 241 GLU D OE1 1 
ATOM   8382 O  OE2 . GLU D  1 241 ? 14.394  3.502   -57.825 1.00 33.96 ? 241 GLU D OE2 1 
ATOM   8383 N  N   . MET D  1 242 ? 12.000  6.659   -53.016 1.00 15.01 ? 242 MET D N   1 
ATOM   8384 C  CA  . MET D  1 242 ? 11.681  6.542   -51.592 1.00 12.86 ? 242 MET D CA  1 
ATOM   8385 C  C   . MET D  1 242 ? 11.951  5.072   -51.105 1.00 12.70 ? 242 MET D C   1 
ATOM   8386 O  O   . MET D  1 242 ? 11.142  4.137   -51.354 1.00 13.03 ? 242 MET D O   1 
ATOM   8387 C  CB  . MET D  1 242 ? 10.241  6.838   -51.358 1.00 13.15 ? 242 MET D CB  1 
ATOM   8388 C  CG  . MET D  1 242 ? 9.916   6.930   -49.810 1.00 15.71 ? 242 MET D CG  1 
ATOM   8389 S  SD  . MET D  1 242 ? 8.186   7.277   -49.491 1.00 13.47 ? 242 MET D SD  1 
ATOM   8390 C  CE  . MET D  1 242 ? 8.171   8.947   -50.133 1.00 13.96 ? 242 MET D CE  1 
ATOM   8391 N  N   . ILE D  1 243 ? 13.171  4.868   -50.608 1.00 11.64 ? 243 ILE D N   1 
ATOM   8392 C  CA  . ILE D  1 243 ? 13.671  3.547   -50.192 1.00 12.33 ? 243 ILE D CA  1 
ATOM   8393 C  C   . ILE D  1 243 ? 14.378  3.774   -48.871 1.00 11.14 ? 243 ILE D C   1 
ATOM   8394 O  O   . ILE D  1 243 ? 14.834  4.897   -48.587 1.00 11.15 ? 243 ILE D O   1 
ATOM   8395 C  CB  . ILE D  1 243 ? 14.642  2.925   -51.201 1.00 13.01 ? 243 ILE D CB  1 
ATOM   8396 C  CG1 . ILE D  1 243 ? 15.740  3.943   -51.605 1.00 14.73 ? 243 ILE D CG1 1 
ATOM   8397 C  CG2 . ILE D  1 243 ? 13.807  2.463   -52.387 1.00 16.04 ? 243 ILE D CG2 1 
ATOM   8398 C  CD1 . ILE D  1 243 ? 16.860  3.297   -52.406 1.00 19.94 ? 243 ILE D CD1 1 
ATOM   8399 N  N   . ASN D  1 244 ? 14.546  2.655   -48.142 1.00 9.36  ? 244 ASN D N   1 
ATOM   8400 C  CA  . ASN D  1 244 ? 15.307  2.686   -46.891 1.00 10.10 ? 244 ASN D CA  1 
ATOM   8401 C  C   . ASN D  1 244 ? 14.882  3.820   -45.952 1.00 9.98  ? 244 ASN D C   1 
ATOM   8402 O  O   . ASN D  1 244 ? 15.729  4.519   -45.350 1.00 9.92  ? 244 ASN D O   1 
ATOM   8403 C  CB  . ASN D  1 244 ? 16.843  2.797   -47.188 1.00 11.15 ? 244 ASN D CB  1 
ATOM   8404 C  CG  . ASN D  1 244 ? 17.308  1.649   -48.039 1.00 14.49 ? 244 ASN D CG  1 
ATOM   8405 O  OD1 . ASN D  1 244 ? 16.791  0.558   -48.015 1.00 14.56 ? 244 ASN D OD1 1 
ATOM   8406 N  ND2 . ASN D  1 244 ? 18.229  2.004   -48.984 1.00 20.85 ? 244 ASN D ND2 1 
ATOM   8407 N  N   . ASN D  1 245 ? 13.586  3.987   -45.813 1.00 8.09  ? 245 ASN D N   1 
ATOM   8408 C  CA  . ASN D  1 245 ? 13.036  5.117   -45.075 1.00 8.29  ? 245 ASN D CA  1 
ATOM   8409 C  C   . ASN D  1 245 ? 12.797  4.651   -43.625 1.00 8.89  ? 245 ASN D C   1 
ATOM   8410 O  O   . ASN D  1 245 ? 11.681  4.750   -43.083 1.00 10.71 ? 245 ASN D O   1 
ATOM   8411 C  CB  . ASN D  1 245 ? 11.727  5.689   -45.681 1.00 8.44  ? 245 ASN D CB  1 
ATOM   8412 C  CG  . ASN D  1 245 ? 10.648  4.707   -45.843 1.00 9.25  ? 245 ASN D CG  1 
ATOM   8413 O  OD1 . ASN D  1 245 ? 10.845  3.503   -45.827 1.00 10.72 ? 245 ASN D OD1 1 
ATOM   8414 N  ND2 . ASN D  1 245 ? 9.416   5.194   -46.030 1.00 10.64 ? 245 ASN D ND2 1 
ATOM   8415 N  N   . PHE D  1 246 ? 13.828  4.123   -42.966 1.00 8.13  ? 246 PHE D N   1 
ATOM   8416 C  CA  . PHE D  1 246 ? 13.788  3.734   -41.556 1.00 7.30  ? 246 PHE D CA  1 
ATOM   8417 C  C   . PHE D  1 246 ? 14.986  4.340   -40.881 1.00 8.26  ? 246 PHE D C   1 
ATOM   8418 O  O   . PHE D  1 246 ? 16.063  4.513   -41.465 1.00 9.57  ? 246 PHE D O   1 
ATOM   8419 C  CB  . PHE D  1 246 ? 13.791  2.183   -41.464 1.00 8.53  ? 246 PHE D CB  1 
ATOM   8420 C  CG  . PHE D  1 246 ? 15.046  1.496   -42.022 1.00 9.12  ? 246 PHE D CG  1 
ATOM   8421 C  CD1 . PHE D  1 246 ? 15.127  1.227   -43.410 1.00 9.60  ? 246 PHE D CD1 1 
ATOM   8422 C  CD2 . PHE D  1 246 ? 16.158  1.197   -41.217 1.00 10.43 ? 246 PHE D CD2 1 
ATOM   8423 C  CE1 . PHE D  1 246 ? 16.254  0.544   -43.914 1.00 10.04 ? 246 PHE D CE1 1 
ATOM   8424 C  CE2 . PHE D  1 246 ? 17.298  0.639   -41.745 1.00 11.07 ? 246 PHE D CE2 1 
ATOM   8425 C  CZ  . PHE D  1 246 ? 17.361  0.328   -43.113 1.00 10.64 ? 246 PHE D CZ  1 
ATOM   8426 N  N   . ARG D  1 247 ? 14.778  4.629   -39.615 1.00 7.98  ? 247 ARG D N   1 
ATOM   8427 C  CA  . ARG D  1 247 ? 15.875  5.147   -38.792 1.00 8.35  ? 247 ARG D CA  1 
ATOM   8428 C  C   . ARG D  1 247 ? 16.655  3.976   -38.134 1.00 8.97  ? 247 ARG D C   1 
ATOM   8429 O  O   . ARG D  1 247 ? 15.995  2.977   -37.793 1.00 8.77  ? 247 ARG D O   1 
ATOM   8430 C  CB  . ARG D  1 247 ? 15.277  6.029   -37.658 1.00 8.24  ? 247 ARG D CB  1 
ATOM   8431 C  CG  . ARG D  1 247 ? 16.292  6.910   -36.905 1.00 8.84  ? 247 ARG D CG  1 
ATOM   8432 C  CD  . ARG D  1 247 ? 15.595  7.612   -35.799 1.00 9.51  ? 247 ARG D CD  1 
ATOM   8433 N  NE  . ARG D  1 247 ? 16.400  8.714   -35.267 1.00 8.87  ? 247 ARG D NE  1 
ATOM   8434 C  CZ  . ARG D  1 247 ? 16.091  9.423   -34.183 1.00 10.44 ? 247 ARG D CZ  1 
ATOM   8435 N  NH1 . ARG D  1 247 ? 14.987  9.157   -33.500 1.00 11.34 ? 247 ARG D NH1 1 
ATOM   8436 N  NH2 . ARG D  1 247 ? 16.889  10.405  -33.779 1.00 9.17  ? 247 ARG D NH2 1 
ATOM   8437 N  N   . GLN D  1 248 ? 17.970  4.117   -37.920 1.00 8.15  ? 248 GLN D N   1 
ATOM   8438 C  CA  . GLN D  1 248 ? 18.684  3.116   -37.108 1.00 8.31  ? 248 GLN D CA  1 
ATOM   8439 C  C   . GLN D  1 248 ? 18.172  3.095   -35.700 1.00 8.39  ? 248 GLN D C   1 
ATOM   8440 O  O   . GLN D  1 248 ? 17.630  4.063   -35.180 1.00 9.48  ? 248 GLN D O   1 
ATOM   8441 C  CB  . GLN D  1 248 ? 20.166  3.500   -37.072 1.00 8.73  ? 248 GLN D CB  1 
ATOM   8442 C  CG  . GLN D  1 248 ? 20.820  3.470   -38.475 1.00 8.61  ? 248 GLN D CG  1 
ATOM   8443 C  CD  . GLN D  1 248 ? 20.870  2.118   -39.130 1.00 9.96  ? 248 GLN D CD  1 
ATOM   8444 O  OE1 . GLN D  1 248 ? 19.959  1.752   -39.862 1.00 11.31 ? 248 GLN D OE1 1 
ATOM   8445 N  NE2 . GLN D  1 248 ? 21.885  1.325   -38.811 1.00 10.51 ? 248 GLN D NE2 1 
ATOM   8446 N  N   . VAL D  1 249 ? 18.370  1.923   -35.076 1.00 9.41  ? 249 VAL D N   1 
ATOM   8447 C  CA  . VAL D  1 249 ? 17.986  1.821   -33.651 1.00 9.67  ? 249 VAL D CA  1 
ATOM   8448 C  C   . VAL D  1 249 ? 18.871  2.762   -32.757 1.00 9.34  ? 249 VAL D C   1 
ATOM   8449 O  O   . VAL D  1 249 ? 19.991  3.074   -33.114 1.00 9.88  ? 249 VAL D O   1 
ATOM   8450 C  CB  . VAL D  1 249 ? 18.017  0.377   -33.102 1.00 9.74  ? 249 VAL D CB  1 
ATOM   8451 C  CG1 . VAL D  1 249 ? 16.927  -0.493  -33.806 1.00 12.08 ? 249 VAL D CG1 1 
ATOM   8452 C  CG2 . VAL D  1 249 ? 19.409  -0.261  -33.221 1.00 11.62 ? 249 VAL D CG2 1 
ATOM   8453 N  N   . GLN D  1 250 ? 18.244  3.179   -31.663 1.00 9.17  ? 250 GLN D N   1 
ATOM   8454 C  CA  . GLN D  1 250 ? 18.816  4.168   -30.723 1.00 10.13 ? 250 GLN D CA  1 
ATOM   8455 C  C   . GLN D  1 250 ? 19.312  3.561   -29.422 1.00 11.26 ? 250 GLN D C   1 
ATOM   8456 O  O   . GLN D  1 250 ? 18.871  2.470   -28.966 1.00 12.23 ? 250 GLN D O   1 
ATOM   8457 C  CB  . GLN D  1 250 ? 17.683  5.125   -30.390 1.00 9.54  ? 250 GLN D CB  1 
ATOM   8458 C  CG  . GLN D  1 250 ? 17.021  5.760   -31.667 1.00 10.54 ? 250 GLN D CG  1 
ATOM   8459 C  CD  . GLN D  1 250 ? 17.954  6.662   -32.427 1.00 9.32  ? 250 GLN D CD  1 
ATOM   8460 O  OE1 . GLN D  1 250 ? 18.375  7.734   -31.856 1.00 11.35 ? 250 GLN D OE1 1 
ATOM   8461 N  NE2 . GLN D  1 250 ? 18.265  6.386   -33.634 1.00 9.49  ? 250 GLN D NE2 1 
ATOM   8462 N  N   . LYS D  1 251 ? 20.196  4.314   -28.778 1.00 11.75 ? 251 LYS D N   1 
ATOM   8463 C  CA  . LYS D  1 251 ? 20.609  3.894   -27.403 1.00 12.47 ? 251 LYS D CA  1 
ATOM   8464 C  C   . LYS D  1 251 ? 19.356  3.836   -26.469 1.00 13.20 ? 251 LYS D C   1 
ATOM   8465 O  O   . LYS D  1 251 ? 18.392  4.603   -26.557 1.00 12.67 ? 251 LYS D O   1 
ATOM   8466 C  CB  . LYS D  1 251 ? 21.503  5.007   -26.839 1.00 13.54 ? 251 LYS D CB  1 
ATOM   8467 C  CG  . LYS D  1 251 ? 22.915  5.042   -27.431 1.00 15.54 ? 251 LYS D CG  1 
ATOM   8468 C  CD  . LYS D  1 251 ? 23.748  3.859   -26.908 1.00 15.86 ? 251 LYS D CD  1 
ATOM   8469 C  CE  . LYS D  1 251 ? 25.228  3.957   -27.325 1.00 13.65 ? 251 LYS D CE  1 
ATOM   8470 N  NZ  . LYS D  1 251 ? 25.451  3.859   -28.801 1.00 12.76 ? 251 LYS D NZ  1 
ATOM   8471 N  N   . PHE D  1 252 ? 19.397  2.878   -25.547 1.00 14.68 ? 252 PHE D N   1 
ATOM   8472 C  CA  . PHE D  1 252 ? 18.315  2.717   -24.570 1.00 16.87 ? 252 PHE D CA  1 
ATOM   8473 C  C   . PHE D  1 252 ? 18.219  3.871   -23.499 1.00 22.47 ? 252 PHE D C   1 
ATOM   8474 O  O   . PHE D  1 252 ? 17.126  4.167   -23.013 1.00 22.55 ? 252 PHE D O   1 
ATOM   8475 C  CB  . PHE D  1 252 ? 18.457  1.368   -23.919 1.00 19.36 ? 252 PHE D CB  1 
ATOM   8476 C  CG  . PHE D  1 252 ? 17.819  0.306   -24.722 1.00 20.60 ? 252 PHE D CG  1 
ATOM   8477 C  CD1 . PHE D  1 252 ? 16.491  -0.020  -24.499 1.00 26.24 ? 252 PHE D CD1 1 
ATOM   8478 C  CD2 . PHE D  1 252 ? 18.498  -0.304  -25.756 1.00 28.57 ? 252 PHE D CD2 1 
ATOM   8479 C  CE1 . PHE D  1 252 ? 15.873  -0.980  -25.264 1.00 29.49 ? 252 PHE D CE1 1 
ATOM   8480 C  CE2 . PHE D  1 252 ? 17.882  -1.264  -26.519 1.00 24.44 ? 252 PHE D CE2 1 
ATOM   8481 C  CZ  . PHE D  1 252 ? 16.560  -1.601  -26.277 1.00 25.06 ? 252 PHE D CZ  1 
ATOM   8482 N  N   . ASP D  1 253 ? 19.327  4.535   -23.123 1.00 22.12 ? 253 ASP D N   1 
ATOM   8483 C  CA  . ASP D  1 253 ? 19.184  5.655   -22.153 1.00 25.25 ? 253 ASP D CA  1 
ATOM   8484 C  C   . ASP D  1 253 ? 18.530  5.114   -20.862 1.00 27.98 ? 253 ASP D C   1 
ATOM   8485 O  O   . ASP D  1 253 ? 17.643  5.802   -20.307 1.00 29.55 ? 253 ASP D O   1 
ATOM   8486 C  CB  . ASP D  1 253 ? 18.324  6.818   -22.682 1.00 28.48 ? 253 ASP D CB  1 
ATOM   8487 C  CG  . ASP D  1 253 ? 18.991  7.563   -23.860 1.00 30.52 ? 253 ASP D CG  1 
ATOM   8488 O  OD1 . ASP D  1 253 ? 20.255  7.500   -23.987 1.00 30.34 ? 253 ASP D OD1 1 
ATOM   8489 O  OD2 . ASP D  1 253 ? 18.214  8.194   -24.657 1.00 27.88 ? 253 ASP D OD2 1 
ATOM   8490 N  N   . GLU D  1 254 ? 18.940  3.922   -20.383 1.00 27.88 ? 254 GLU D N   1 
ATOM   8491 C  CA  . GLU D  1 254 ? 18.323  3.375   -19.135 1.00 32.52 ? 254 GLU D CA  1 
ATOM   8492 C  C   . GLU D  1 254 ? 16.970  2.754   -19.157 1.00 30.59 ? 254 GLU D C   1 
ATOM   8493 O  O   . GLU D  1 254 ? 16.537  2.111   -18.192 1.00 30.35 ? 254 GLU D O   1 
ATOM   8494 C  CB  . GLU D  1 254 ? 18.359  4.445   -18.035 1.00 37.65 ? 254 GLU D CB  1 
ATOM   8495 C  CG  . GLU D  1 254 ? 19.729  5.067   -17.819 1.00 49.01 ? 254 GLU D CG  1 
ATOM   8496 C  CD  . GLU D  1 254 ? 20.531  4.351   -16.749 1.00 57.51 ? 254 GLU D CD  1 
ATOM   8497 O  OE1 . GLU D  1 254 ? 20.933  3.192   -16.981 1.00 53.96 ? 254 GLU D OE1 1 
ATOM   8498 O  OE2 . GLU D  1 254 ? 20.759  4.949   -15.676 1.00 64.43 ? 254 GLU D OE2 1 
ATOM   8499 N  N   . ARG D  1 255 ? 16.253  2.926   -20.264 1.00 22.47 ? 255 ARG D N   1 
ATOM   8500 C  CA  . ARG D  1 255 ? 14.897  2.381   -20.430 1.00 21.18 ? 255 ARG D CA  1 
ATOM   8501 C  C   . ARG D  1 255 ? 14.853  0.863   -20.415 1.00 20.62 ? 255 ARG D C   1 
ATOM   8502 O  O   . ARG D  1 255 ? 15.827  0.193   -20.886 1.00 22.41 ? 255 ARG D O   1 
ATOM   8503 C  CB  . ARG D  1 255 ? 14.257  2.873   -21.792 1.00 22.81 ? 255 ARG D CB  1 
ATOM   8504 C  CG  . ARG D  1 255 ? 13.892  4.352   -21.807 1.00 22.83 ? 255 ARG D CG  1 
ATOM   8505 C  CD  . ARG D  1 255 ? 13.434  4.677   -23.247 1.00 21.36 ? 255 ARG D CD  1 
ATOM   8506 N  NE  . ARG D  1 255 ? 14.540  4.684   -24.187 1.00 19.18 ? 255 ARG D NE  1 
ATOM   8507 C  CZ  . ARG D  1 255 ? 14.411  5.000   -25.489 1.00 18.81 ? 255 ARG D CZ  1 
ATOM   8508 N  NH1 . ARG D  1 255 ? 13.159  5.268   -26.007 1.00 14.06 ? 255 ARG D NH1 1 
ATOM   8509 N  NH2 . ARG D  1 255 ? 15.548  5.089   -26.240 1.00 16.98 ? 255 ARG D NH2 1 
ATOM   8510 N  N   . LEU D  1 256 ? 13.751  0.302   -19.881 1.00 20.95 ? 256 LEU D N   1 
ATOM   8511 C  CA  . LEU D  1 256 ? 13.399  -1.125  -20.113 1.00 19.69 ? 256 LEU D CA  1 
ATOM   8512 C  C   . LEU D  1 256 ? 12.212  -1.106  -21.047 1.00 19.35 ? 256 LEU D C   1 
ATOM   8513 O  O   . LEU D  1 256 ? 11.549  -0.055  -21.325 1.00 21.85 ? 256 LEU D O   1 
ATOM   8514 C  CB  . LEU D  1 256 ? 13.021  -1.870  -18.821 1.00 21.20 ? 256 LEU D CB  1 
ATOM   8515 C  CG  . LEU D  1 256 ? 14.117  -1.820  -17.796 1.00 22.55 ? 256 LEU D CG  1 
ATOM   8516 C  CD1 . LEU D  1 256 ? 13.610  -2.597  -16.567 1.00 26.27 ? 256 LEU D CD1 1 
ATOM   8517 C  CD2 . LEU D  1 256 ? 15.382  -2.485  -18.369 1.00 25.58 ? 256 LEU D CD2 1 
ATOM   8518 N  N   . VAL D  1 257 ? 12.013  -2.241  -21.671 1.00 15.76 ? 257 VAL D N   1 
ATOM   8519 C  CA  . VAL D  1 257 ? 10.838  -2.440  -22.513 1.00 14.71 ? 257 VAL D CA  1 
ATOM   8520 C  C   . VAL D  1 257 ? 10.001  -3.486  -21.814 1.00 14.49 ? 257 VAL D C   1 
ATOM   8521 O  O   . VAL D  1 257 ? 10.501  -4.564  -21.374 1.00 15.95 ? 257 VAL D O   1 
ATOM   8522 C  CB  . VAL D  1 257 ? 11.131  -3.028  -23.939 1.00 15.24 ? 257 VAL D CB  1 
ATOM   8523 C  CG1 . VAL D  1 257 ? 9.859   -3.412  -24.654 1.00 14.66 ? 257 VAL D CG1 1 
ATOM   8524 C  CG2 . VAL D  1 257 ? 11.970  -2.092  -24.775 1.00 15.59 ? 257 VAL D CG2 1 
ATOM   8525 N  N   . TYR D  1 258 ? 8.778   -3.153  -21.589 1.00 12.63 ? 258 TYR D N   1 
ATOM   8526 C  CA  . TYR D  1 258 ? 7.834   -3.990  -20.765 1.00 13.55 ? 258 TYR D CA  1 
ATOM   8527 C  C   . TYR D  1 258 ? 7.026   -4.841  -21.675 1.00 14.69 ? 258 TYR D C   1 
ATOM   8528 O  O   . TYR D  1 258 ? 6.675   -4.464  -22.799 1.00 15.76 ? 258 TYR D O   1 
ATOM   8529 C  CB  . TYR D  1 258 ? 6.941   -3.122  -19.842 1.00 15.04 ? 258 TYR D CB  1 
ATOM   8530 C  CG  . TYR D  1 258 ? 7.794   -2.268  -18.964 1.00 16.10 ? 258 TYR D CG  1 
ATOM   8531 C  CD1 . TYR D  1 258 ? 8.294   -2.781  -17.765 1.00 16.77 ? 258 TYR D CD1 1 
ATOM   8532 C  CD2 . TYR D  1 258 ? 8.202   -0.968  -19.362 1.00 16.80 ? 258 TYR D CD2 1 
ATOM   8533 C  CE1 . TYR D  1 258 ? 9.172   -2.011  -16.979 1.00 20.34 ? 258 TYR D CE1 1 
ATOM   8534 C  CE2 . TYR D  1 258 ? 9.058   -0.231  -18.565 1.00 20.79 ? 258 TYR D CE2 1 
ATOM   8535 C  CZ  . TYR D  1 258 ? 9.517   -0.751  -17.391 1.00 21.02 ? 258 TYR D CZ  1 
ATOM   8536 O  OH  . TYR D  1 258 ? 10.370  0.024   -16.618 1.00 26.58 ? 258 TYR D OH  1 
ATOM   8537 N  N   . THR D  1 259 ? 6.809   -6.122  -21.307 1.00 11.83 ? 259 THR D N   1 
ATOM   8538 C  CA  . THR D  1 259 ? 6.117   -7.059  -22.177 1.00 12.28 ? 259 THR D CA  1 
ATOM   8539 C  C   . THR D  1 259 ? 4.870   -7.502  -21.509 1.00 12.87 ? 259 THR D C   1 
ATOM   8540 O  O   . THR D  1 259 ? 4.812   -7.636  -20.218 1.00 13.24 ? 259 THR D O   1 
ATOM   8541 C  CB  . THR D  1 259 ? 6.927   -8.270  -22.572 1.00 11.36 ? 259 THR D CB  1 
ATOM   8542 O  OG1 . THR D  1 259 ? 7.407   -8.938  -21.387 1.00 14.59 ? 259 THR D OG1 1 
ATOM   8543 C  CG2 . THR D  1 259 ? 8.201   -7.827  -23.261 1.00 13.59 ? 259 THR D CG2 1 
ATOM   8544 N  N   . SER D  1 260 ? 3.843   -7.817  -22.287 1.00 12.43 ? 260 SER D N   1 
ATOM   8545 C  CA  . SER D  1 260 ? 2.591   -8.364  -21.747 1.00 13.61 ? 260 SER D CA  1 
ATOM   8546 C  C   . SER D  1 260 ? 2.645   -9.880  -21.701 1.00 16.52 ? 260 SER D C   1 
ATOM   8547 O  O   . SER D  1 260 ? 1.615   -10.548 -21.353 1.00 20.44 ? 260 SER D O   1 
ATOM   8548 C  CB  . SER D  1 260 ? 1.397   -7.872  -22.551 1.00 16.00 ? 260 SER D CB  1 
ATOM   8549 O  OG  . SER D  1 260 ? 1.494   -8.394  -23.910 1.00 14.72 ? 260 SER D OG  1 
ATOM   8550 N  N   . PHE D  1 261 ? 3.785   -10.458 -22.035 1.00 14.61 ? 261 PHE D N   1 
ATOM   8551 C  CA  . PHE D  1 261 ? 3.925   -11.925 -22.140 1.00 17.27 ? 261 PHE D CA  1 
ATOM   8552 C  C   . PHE D  1 261 ? 5.201   -12.233 -21.429 1.00 21.39 ? 261 PHE D C   1 
ATOM   8553 O  O   . PHE D  1 261 ? 6.054   -11.443 -21.305 1.00 17.21 ? 261 PHE D O   1 
ATOM   8554 C  CB  . PHE D  1 261 ? 3.975   -12.402 -23.615 1.00 17.38 ? 261 PHE D CB  1 
ATOM   8555 C  CG  . PHE D  1 261 ? 5.059   -11.682 -24.434 1.00 16.18 ? 261 PHE D CG  1 
ATOM   8556 C  CD1 . PHE D  1 261 ? 6.373   -12.217 -24.549 1.00 17.72 ? 261 PHE D CD1 1 
ATOM   8557 C  CD2 . PHE D  1 261 ? 4.785   -10.463 -25.090 1.00 17.09 ? 261 PHE D CD2 1 
ATOM   8558 C  CE1 . PHE D  1 261 ? 7.392   -11.577 -25.315 1.00 17.69 ? 261 PHE D CE1 1 
ATOM   8559 C  CE2 . PHE D  1 261 ? 5.841   -9.835  -25.823 1.00 14.11 ? 261 PHE D CE2 1 
ATOM   8560 C  CZ  . PHE D  1 261 ? 7.091   -10.355 -25.959 1.00 16.38 ? 261 PHE D CZ  1 
ATOM   8561 N  N   . SER D  1 262 ? 5.326   -13.453 -20.874 1.00 30.98 ? 262 SER D N   1 
ATOM   8562 C  CA  . SER D  1 262 ? 6.650   -14.031 -20.403 1.00 36.06 ? 262 SER D CA  1 
ATOM   8563 C  C   . SER D  1 262 ? 7.126   -15.028 -21.445 1.00 39.76 ? 262 SER D C   1 
ATOM   8564 O  O   . SER D  1 262 ? 8.314   -15.151 -21.780 1.00 46.30 ? 262 SER D O   1 
ATOM   8565 C  CB  . SER D  1 262 ? 6.523   -14.793 -19.094 1.00 45.14 ? 262 SER D CB  1 
ATOM   8566 O  OG  . SER D  1 262 ? 5.607   -14.190 -18.196 1.00 43.81 ? 262 SER D OG  1 
HETATM 8567 ZN ZN  . ZN  E  2 .   ? 22.991  0.645   12.334  1.00 8.88  ? 301 ZN  A ZN  1 
HETATM 8568 C  C1  . EDO F  3 .   ? 23.994  4.237   14.837  1.00 23.06 ? 302 EDO A C1  1 
HETATM 8569 O  O1  . EDO F  3 .   ? 23.401  5.155   15.782  1.00 20.11 ? 302 EDO A O1  1 
HETATM 8570 C  C2  . EDO F  3 .   ? 25.294  4.728   14.192  1.00 21.37 ? 302 EDO A C2  1 
HETATM 8571 O  O2  . EDO F  3 .   ? 26.170  4.909   15.255  1.00 24.42 ? 302 EDO A O2  1 
HETATM 8572 C  C1  . EDO G  3 .   ? 26.382  -8.800  29.941  1.00 32.06 ? 303 EDO A C1  1 
HETATM 8573 O  O1  . EDO G  3 .   ? 26.117  -9.883  28.999  1.00 29.31 ? 303 EDO A O1  1 
HETATM 8574 C  C2  . EDO G  3 .   ? 27.185  -9.358  31.116  1.00 35.49 ? 303 EDO A C2  1 
HETATM 8575 O  O2  . EDO G  3 .   ? 28.579  -9.253  30.759  1.00 39.43 ? 303 EDO A O2  1 
HETATM 8576 C  C1  . EDO H  3 .   ? 36.359  6.192   14.127  1.00 27.97 ? 304 EDO A C1  1 
HETATM 8577 O  O1  . EDO H  3 .   ? 36.897  4.929   14.521  1.00 28.45 ? 304 EDO A O1  1 
HETATM 8578 C  C2  . EDO H  3 .   ? 37.151  6.801   12.948  1.00 28.48 ? 304 EDO A C2  1 
HETATM 8579 O  O2  . EDO H  3 .   ? 36.906  6.204   11.611  1.00 22.10 ? 304 EDO A O2  1 
HETATM 8580 O  O4  . VD9 I  4 .   ? 23.021  2.585   8.708   1.00 10.06 ? 305 VD9 A O4  1 
HETATM 8581 S  S2  . VD9 I  4 .   ? 23.683  2.401   10.007  1.00 10.52 ? 305 VD9 A S2  1 
HETATM 8582 O  O1  . VD9 I  4 .   ? 24.724  1.322   10.015  1.00 10.60 ? 305 VD9 A O1  1 
HETATM 8583 N  N3  . VD9 I  4 .   ? 22.615  2.141   11.164  1.00 9.33  ? 305 VD9 A N3  1 
HETATM 8584 C  C5  . VD9 I  4 .   ? 24.541  3.890   10.292  1.00 11.41 ? 305 VD9 A C5  1 
HETATM 8585 C  C10 . VD9 I  4 .   ? 25.926  3.926   10.227  1.00 12.97 ? 305 VD9 A C10 1 
HETATM 8586 C  C9  . VD9 I  4 .   ? 26.642  5.126   10.409  1.00 13.90 ? 305 VD9 A C9  1 
HETATM 8587 C  C8  . VD9 I  4 .   ? 25.888  6.249   10.742  1.00 14.99 ? 305 VD9 A C8  1 
HETATM 8588 C  C7  . VD9 I  4 .   ? 24.493  6.282   10.858  1.00 16.96 ? 305 VD9 A C7  1 
HETATM 8589 C  C6  . VD9 I  4 .   ? 23.866  5.031   10.687  1.00 13.38 ? 305 VD9 A C6  1 
HETATM 8590 S  S11 . VD9 I  4 .   ? 26.643  7.858   10.960  1.00 19.79 ? 305 VD9 A S11 1 
HETATM 8591 C  C12 . VD9 I  4 .   ? 28.381  7.643   10.399  1.00 19.68 ? 305 VD9 A C12 1 
HETATM 8592 C  C13 . VD9 I  4 .   ? 28.465  7.459   8.903   1.00 19.55 ? 305 VD9 A C13 1 
HETATM 8593 C  C14 . VD9 I  4 .   ? 29.909  7.231   8.497   1.00 22.60 ? 305 VD9 A C14 1 
HETATM 8594 ZN ZN  . ZN  J  2 .   ? -8.109  3.611   4.868   1.00 7.27  ? 301 ZN  B ZN  1 
HETATM 8595 C  C1  . EDO K  3 .   ? -9.504  7.848   2.974   1.00 15.80 ? 302 EDO B C1  1 
HETATM 8596 O  O1  . EDO K  3 .   ? -10.586 8.161   2.137   1.00 17.83 ? 302 EDO B O1  1 
HETATM 8597 C  C2  . EDO K  3 .   ? -8.475  7.152   2.211   1.00 16.71 ? 302 EDO B C2  1 
HETATM 8598 O  O2  . EDO K  3 .   ? -7.833  8.063   1.245   1.00 15.90 ? 302 EDO B O2  1 
HETATM 8599 C  C1  . EDO L  3 .   ? -16.980 -3.430  23.018  1.00 28.23 ? 303 EDO B C1  1 
HETATM 8600 O  O1  . EDO L  3 .   ? -15.948 -2.430  23.061  1.00 27.79 ? 303 EDO B O1  1 
HETATM 8601 C  C2  . EDO L  3 .   ? -17.452 -3.664  21.569  1.00 24.17 ? 303 EDO B C2  1 
HETATM 8602 O  O2  . EDO L  3 .   ? -16.432 -3.667  20.502  1.00 20.89 ? 303 EDO B O2  1 
HETATM 8603 C  C1  . EDO M  3 .   ? -13.470 -5.950  -12.374 1.00 29.64 ? 304 EDO B C1  1 
HETATM 8604 O  O1  . EDO M  3 .   ? -13.455 -6.916  -11.268 1.00 22.86 ? 304 EDO B O1  1 
HETATM 8605 C  C2  . EDO M  3 .   ? -14.679 -5.854  -13.322 1.00 28.23 ? 304 EDO B C2  1 
HETATM 8606 O  O2  . EDO M  3 .   ? -16.065 -5.791  -12.775 1.00 25.29 ? 304 EDO B O2  1 
HETATM 8607 C  C1  A EDO N  3 .   ? -13.561 11.088  2.575   0.50 24.19 ? 305 EDO B C1  1 
HETATM 8608 C  C1  B EDO N  3 .   ? -13.672 11.586  2.544   0.50 20.60 ? 305 EDO B C1  1 
HETATM 8609 O  O1  A EDO N  3 .   ? -13.890 11.004  3.966   0.50 24.72 ? 305 EDO B O1  1 
HETATM 8610 O  O1  B EDO N  3 .   ? -13.841 10.944  3.812   0.50 21.18 ? 305 EDO B O1  1 
HETATM 8611 C  C2  A EDO N  3 .   ? -12.224 11.801  2.412   0.50 23.63 ? 305 EDO B C2  1 
HETATM 8612 C  C2  B EDO N  3 .   ? -12.204 11.532  2.138   0.50 20.08 ? 305 EDO B C2  1 
HETATM 8613 O  O2  A EDO N  3 .   ? -11.157 10.868  2.616   0.50 19.42 ? 305 EDO B O2  1 
HETATM 8614 O  O2  B EDO N  3 .   ? -12.069 11.952  0.776   0.50 16.17 ? 305 EDO B O2  1 
HETATM 8615 C  C1  . EDO O  3 .   ? -15.363 -13.773 2.833   1.00 37.14 ? 306 EDO B C1  1 
HETATM 8616 O  O1  . EDO O  3 .   ? -15.525 -14.913 3.684   1.00 34.36 ? 306 EDO B O1  1 
HETATM 8617 C  C2  . EDO O  3 .   ? -16.731 -13.280 2.379   1.00 29.93 ? 306 EDO B C2  1 
HETATM 8618 O  O2  . EDO O  3 .   ? -17.405 -12.661 3.481   1.00 23.40 ? 306 EDO B O2  1 
HETATM 8619 C  C1  . EDO P  3 .   ? -3.239  0.869   25.659  1.00 37.12 ? 307 EDO B C1  1 
HETATM 8620 O  O1  . EDO P  3 .   ? -2.715  -0.358  25.170  1.00 27.35 ? 307 EDO B O1  1 
HETATM 8621 C  C2  . EDO P  3 .   ? -3.080  1.943   24.612  1.00 40.98 ? 307 EDO B C2  1 
HETATM 8622 O  O2  . EDO P  3 .   ? -4.378  1.968   24.020  1.00 37.42 ? 307 EDO B O2  1 
HETATM 8623 O  O4  . VD9 Q  4 .   ? -7.605  5.684   8.400   1.00 8.32  ? 308 VD9 B O4  1 
HETATM 8624 S  S2  . VD9 Q  4 .   ? -8.359  5.547   7.176   1.00 8.71  ? 308 VD9 B S2  1 
HETATM 8625 O  O1  . VD9 Q  4 .   ? -9.523  4.735   7.229   1.00 8.70  ? 308 VD9 B O1  1 
HETATM 8626 N  N3  . VD9 Q  4 .   ? -7.484  5.026   5.918   1.00 9.67  ? 308 VD9 B N3  1 
HETATM 8627 C  C5  . VD9 Q  4 .   ? -8.931  7.191   6.830   1.00 10.06 ? 308 VD9 B C5  1 
HETATM 8628 C  C10 . VD9 Q  4 .   ? -8.080  8.269   6.416   1.00 11.35 ? 308 VD9 B C10 1 
HETATM 8629 C  C9  . VD9 Q  4 .   ? -8.585  9.548   6.151   1.00 14.73 ? 308 VD9 B C9  1 
HETATM 8630 C  C8  . VD9 Q  4 .   ? -9.909  9.681   6.322   1.00 10.46 ? 308 VD9 B C8  1 
HETATM 8631 C  C7  . VD9 Q  4 .   ? -10.808 8.788   6.724   1.00 11.73 ? 308 VD9 B C7  1 
HETATM 8632 C  C6  . VD9 Q  4 .   ? -10.318 7.464   6.930   1.00 10.97 ? 308 VD9 B C6  1 
HETATM 8633 S  S11 . VD9 Q  4 .   ? -10.405 11.396  6.038   1.00 17.39 ? 308 VD9 B S11 1 
HETATM 8634 C  C12 . VD9 Q  4 .   ? -12.150 11.467  6.604   1.00 19.55 ? 308 VD9 B C12 1 
HETATM 8635 C  C13 . VD9 Q  4 .   ? -12.161 11.504  8.136   1.00 16.36 ? 308 VD9 B C13 1 
HETATM 8636 C  C14 . VD9 Q  4 .   ? -13.645 11.503  8.515   1.00 17.78 ? 308 VD9 B C14 1 
HETATM 8637 ZN ZN  . ZN  R  2 .   ? 37.459  2.607   -30.901 1.00 12.20 ? 301 ZN  C ZN  1 
HETATM 8638 C  C1  . EDO S  3 .   ? 38.289  6.312   -28.253 1.00 29.50 ? 302 EDO C C1  1 
HETATM 8639 O  O1  . EDO S  3 .   ? 37.577  7.186   -27.352 1.00 31.50 ? 302 EDO C O1  1 
HETATM 8640 C  C2  . EDO S  3 .   ? 39.602  6.900   -28.836 1.00 32.99 ? 302 EDO C C2  1 
HETATM 8641 O  O2  . EDO S  3 .   ? 40.610  6.873   -27.811 1.00 34.34 ? 302 EDO C O2  1 
HETATM 8642 C  C1  . EDO T  3 .   ? 51.504  9.231   -29.979 1.00 26.95 ? 303 EDO C C1  1 
HETATM 8643 O  O1  . EDO T  3 .   ? 51.268  8.599   -31.298 1.00 26.05 ? 303 EDO C O1  1 
HETATM 8644 C  C2  . EDO T  3 .   ? 50.610  8.635   -28.876 1.00 27.39 ? 303 EDO C C2  1 
HETATM 8645 O  O2  . EDO T  3 .   ? 51.150  7.369   -28.435 1.00 26.83 ? 303 EDO C O2  1 
HETATM 8646 O  O4  . VD9 U  4 .   ? 37.576  4.477   -34.591 1.00 12.77 ? 304 VD9 C O4  1 
HETATM 8647 S  S2  . VD9 U  4 .   ? 38.201  4.331   -33.224 1.00 13.33 ? 304 VD9 C S2  1 
HETATM 8648 O  O1  . VD9 U  4 .   ? 39.169  3.273   -33.233 1.00 12.47 ? 304 VD9 C O1  1 
HETATM 8649 N  N3  . VD9 U  4 .   ? 37.055  4.094   -32.118 1.00 12.27 ? 304 VD9 C N3  1 
HETATM 8650 C  C5  . VD9 U  4 .   ? 39.078  5.792   -32.852 1.00 13.46 ? 304 VD9 C C5  1 
HETATM 8651 C  C10 . VD9 U  4 .   ? 40.485  5.766   -32.959 1.00 16.09 ? 304 VD9 C C10 1 
HETATM 8652 C  C9  . VD9 U  4 .   ? 41.136  6.980   -32.741 1.00 17.67 ? 304 VD9 C C9  1 
HETATM 8653 C  C8  . VD9 U  4 .   ? 40.439  8.133   -32.425 1.00 18.13 ? 304 VD9 C C8  1 
HETATM 8654 C  C7  . VD9 U  4 .   ? 39.028  8.168   -32.334 1.00 19.01 ? 304 VD9 C C7  1 
HETATM 8655 C  C6  . VD9 U  4 .   ? 38.362  6.948   -32.558 1.00 17.94 ? 304 VD9 C C6  1 
HETATM 8656 S  S11 . VD9 U  4 .   ? 41.112  9.805   -32.164 1.00 23.81 ? 304 VD9 C S11 1 
HETATM 8657 C  C12 . VD9 U  4 .   ? 42.842  9.504   -32.720 1.00 22.43 ? 304 VD9 C C12 1 
HETATM 8658 C  C13 . VD9 U  4 .   ? 42.892  9.540   -34.230 1.00 20.59 ? 304 VD9 C C13 1 
HETATM 8659 C  C14 . VD9 U  4 .   ? 44.354  9.192   -34.572 1.00 25.80 ? 304 VD9 C C14 1 
HETATM 8660 ZN ZN  . ZN  V  2 .   ? 6.597   5.565   -38.591 1.00 8.38  ? 301 ZN  D ZN  1 
HETATM 8661 C  C1  . EDO W  3 .   ? 5.146   9.799   -40.611 1.00 15.19 ? 302 EDO D C1  1 
HETATM 8662 O  O1  . EDO W  3 .   ? 4.156   10.101  -41.544 1.00 19.70 ? 302 EDO D O1  1 
HETATM 8663 C  C2  . EDO W  3 .   ? 6.269   9.089   -41.290 1.00 18.17 ? 302 EDO D C2  1 
HETATM 8664 O  O2  . EDO W  3 .   ? 6.987   9.896   -42.271 1.00 15.70 ? 302 EDO D O2  1 
HETATM 8665 C  C1  . EDO X  3 .   ? -2.281  -1.157  -20.486 1.00 26.32 ? 303 EDO D C1  1 
HETATM 8666 O  O1  . EDO X  3 .   ? -1.326  -0.060  -20.274 1.00 34.96 ? 303 EDO D O1  1 
HETATM 8667 C  C2  . EDO X  3 .   ? -2.872  -1.141  -21.910 1.00 25.80 ? 303 EDO D C2  1 
HETATM 8668 O  O2  . EDO X  3 .   ? -1.928  -1.518  -22.943 1.00 25.07 ? 303 EDO D O2  1 
HETATM 8669 O  O4  . VD9 Y  4 .   ? 7.175   7.727   -35.109 1.00 10.64 ? 304 VD9 D O4  1 
HETATM 8670 S  S2  . VD9 Y  4 .   ? 6.383   7.568   -36.321 1.00 10.22 ? 304 VD9 D S2  1 
HETATM 8671 O  O1  . VD9 Y  4 .   ? 5.179   6.756   -36.216 1.00 9.82  ? 304 VD9 D O1  1 
HETATM 8672 N  N3  . VD9 Y  4 .   ? 7.315   7.050   -37.527 1.00 9.75  ? 304 VD9 D N3  1 
HETATM 8673 C  C5  . VD9 Y  4 .   ? 5.768   9.218   -36.752 1.00 11.30 ? 304 VD9 D C5  1 
HETATM 8674 C  C10 . VD9 Y  4 .   ? 6.671   10.157  -37.213 1.00 13.67 ? 304 VD9 D C10 1 
HETATM 8675 C  C9  . VD9 Y  4 .   ? 6.273   11.447  -37.522 1.00 14.57 ? 304 VD9 D C9  1 
HETATM 8676 C  C8  . VD9 Y  4 .   ? 4.923   11.704  -37.349 1.00 11.91 ? 304 VD9 D C8  1 
HETATM 8677 C  C7  . VD9 Y  4 .   ? 3.961   10.827  -36.903 1.00 12.94 ? 304 VD9 D C7  1 
HETATM 8678 C  C6  . VD9 Y  4 .   ? 4.403   9.530   -36.662 1.00 12.71 ? 304 VD9 D C6  1 
HETATM 8679 S  S11 . VD9 Y  4 .   ? 4.427   13.398  -37.697 1.00 18.30 ? 304 VD9 D S11 1 
HETATM 8680 C  C12 . VD9 Y  4 .   ? 2.721   13.546  -37.044 1.00 20.58 ? 304 VD9 D C12 1 
HETATM 8681 C  C13 . VD9 Y  4 .   ? 2.516   13.552  -35.515 1.00 19.15 ? 304 VD9 D C13 1 
HETATM 8682 C  C14 . VD9 Y  4 .   ? 1.065   13.713  -35.101 1.00 20.62 ? 304 VD9 D C14 1 
HETATM 8683 O  O   . HOH Z  5 .   ? 16.989  -13.615 30.852  1.00 26.11 ? 401 HOH A O   1 
HETATM 8684 O  O   . HOH Z  5 .   ? 42.335  -0.288  5.683   1.00 33.87 ? 402 HOH A O   1 
HETATM 8685 O  O   . HOH Z  5 .   ? 28.156  3.950   33.431  1.00 32.20 ? 403 HOH A O   1 
HETATM 8686 O  O   . HOH Z  5 .   ? 43.692  -4.289  12.866  1.00 26.37 ? 404 HOH A O   1 
HETATM 8687 O  O   . HOH Z  5 .   ? 45.184  -4.435  7.550   1.00 27.39 ? 405 HOH A O   1 
HETATM 8688 O  O   . HOH Z  5 .   ? 25.114  -21.197 19.138  1.00 38.71 ? 406 HOH A O   1 
HETATM 8689 O  O   . HOH Z  5 .   ? 41.749  5.902   5.302   1.00 26.87 ? 407 HOH A O   1 
HETATM 8690 O  O   . HOH Z  5 .   ? 47.151  -3.670  10.138  1.00 24.66 ? 408 HOH A O   1 
HETATM 8691 O  O   . HOH Z  5 .   ? 42.082  2.196   0.916   1.00 15.22 ? 409 HOH A O   1 
HETATM 8692 O  O   . HOH Z  5 .   ? 31.725  5.656   32.419  1.00 29.22 ? 410 HOH A O   1 
HETATM 8693 O  O   . HOH Z  5 .   ? 12.606  14.622  2.277   1.00 15.01 ? 411 HOH A O   1 
HETATM 8694 O  O   . HOH Z  5 .   ? 39.465  -15.813 17.064  1.00 28.90 ? 412 HOH A O   1 
HETATM 8695 O  O   . HOH Z  5 .   ? 39.957  -1.633  28.958  1.00 37.27 ? 413 HOH A O   1 
HETATM 8696 O  O   . HOH Z  5 .   ? 5.512   20.026  10.713  1.00 22.66 ? 414 HOH A O   1 
HETATM 8697 O  O   . HOH Z  5 .   ? 34.174  -1.285  37.226  1.00 26.27 ? 415 HOH A O   1 
HETATM 8698 O  O   . HOH Z  5 .   ? 17.220  -16.341 -7.673  1.00 30.80 ? 416 HOH A O   1 
HETATM 8699 O  O   . HOH Z  5 .   ? 32.597  7.827   30.730  1.00 24.81 ? 417 HOH A O   1 
HETATM 8700 O  O   . HOH Z  5 .   ? 41.532  -4.437  0.063   1.00 37.09 ? 418 HOH A O   1 
HETATM 8701 O  O   . HOH Z  5 .   ? 28.279  -24.105 8.345   1.00 36.28 ? 419 HOH A O   1 
HETATM 8702 O  O   . HOH Z  5 .   ? 27.576  5.930   35.420  1.00 29.52 ? 420 HOH A O   1 
HETATM 8703 O  O   . HOH Z  5 .   ? 18.421  -15.696 34.062  1.00 29.89 ? 421 HOH A O   1 
HETATM 8704 O  O   . HOH Z  5 .   ? 42.532  2.968   5.096   1.00 34.63 ? 422 HOH A O   1 
HETATM 8705 O  O   . HOH Z  5 .   ? 23.925  -15.451 -11.858 1.00 34.31 ? 423 HOH A O   1 
HETATM 8706 O  O   . HOH Z  5 .   ? 45.390  -6.120  13.307  1.00 37.22 ? 424 HOH A O   1 
HETATM 8707 O  O   . HOH Z  5 .   ? 22.519  -21.990 -0.637  1.00 42.55 ? 425 HOH A O   1 
HETATM 8708 O  O   . HOH Z  5 .   ? 17.656  -6.650  33.530  1.00 34.85 ? 426 HOH A O   1 
HETATM 8709 O  O   . HOH Z  5 .   ? 7.709   -15.904 7.692   1.00 36.00 ? 427 HOH A O   1 
HETATM 8710 O  O   . HOH Z  5 .   ? 36.112  -16.134 13.684  1.00 37.16 ? 428 HOH A O   1 
HETATM 8711 O  O   . HOH Z  5 .   ? 14.758  -12.346 29.464  1.00 20.94 ? 429 HOH A O   1 
HETATM 8712 O  O   . HOH Z  5 .   ? 13.759  21.302  11.575  1.00 30.54 ? 430 HOH A O   1 
HETATM 8713 O  O   . HOH Z  5 .   ? 50.611  -9.436  27.431  1.00 35.41 ? 431 HOH A O   1 
HETATM 8714 O  O   . HOH Z  5 .   ? 21.028  -4.526  32.493  1.00 35.00 ? 432 HOH A O   1 
HETATM 8715 O  O   . HOH Z  5 .   ? 38.396  -15.543 12.289  1.00 33.30 ? 433 HOH A O   1 
HETATM 8716 O  O   . HOH Z  5 .   ? 20.310  -7.297  32.368  1.00 28.26 ? 434 HOH A O   1 
HETATM 8717 O  O   . HOH Z  5 .   ? 42.307  -13.630 12.140  1.00 34.69 ? 435 HOH A O   1 
HETATM 8718 O  O   . HOH Z  5 .   ? 8.818   -6.486  7.552   1.00 19.97 ? 436 HOH A O   1 
HETATM 8719 O  O   . HOH Z  5 .   ? 17.879  3.106   12.848  1.00 11.05 ? 437 HOH A O   1 
HETATM 8720 O  O   . HOH Z  5 .   ? 11.430  5.301   2.287   1.00 12.34 ? 438 HOH A O   1 
HETATM 8721 O  O   . HOH Z  5 .   ? 8.680   2.958   7.393   1.00 9.42  ? 439 HOH A O   1 
HETATM 8722 O  O   . HOH Z  5 .   ? 19.727  -0.577  26.611  1.00 15.90 ? 440 HOH A O   1 
HETATM 8723 O  O   . HOH Z  5 .   ? 8.997   3.969   2.733   1.00 14.21 ? 441 HOH A O   1 
HETATM 8724 O  O   . HOH Z  5 .   ? 19.446  14.220  5.159   1.00 14.29 ? 442 HOH A O   1 
HETATM 8725 O  O   . HOH Z  5 .   ? 10.640  6.222   15.429  1.00 14.39 ? 443 HOH A O   1 
HETATM 8726 O  O   . HOH Z  5 .   ? 12.514  -2.650  11.060  1.00 10.55 ? 444 HOH A O   1 
HETATM 8727 O  O   . HOH Z  5 .   ? 6.044   11.718  7.970   1.00 10.55 ? 445 HOH A O   1 
HETATM 8728 O  O   . HOH Z  5 .   ? 17.740  9.621   0.230   1.00 12.18 ? 446 HOH A O   1 
HETATM 8729 O  O   . HOH Z  5 .   ? 15.297  -6.869  21.152  1.00 13.06 ? 447 HOH A O   1 
HETATM 8730 O  O   . HOH Z  5 .   ? 11.992  7.499   8.705   1.00 11.36 ? 448 HOH A O   1 
HETATM 8731 O  O   . HOH Z  5 .   ? 10.502  -3.287  2.836   1.00 13.96 ? 449 HOH A O   1 
HETATM 8732 O  O   . HOH Z  5 .   ? 18.107  -15.165 6.225   1.00 18.79 ? 450 HOH A O   1 
HETATM 8733 O  O   . HOH Z  5 .   ? 39.284  3.770   19.431  1.00 24.37 ? 451 HOH A O   1 
HETATM 8734 O  O   . HOH Z  5 .   ? 41.137  -10.433 9.744   1.00 20.48 ? 452 HOH A O   1 
HETATM 8735 O  O   . HOH Z  5 .   ? 28.451  -4.190  2.647   1.00 12.59 ? 453 HOH A O   1 
HETATM 8736 O  O   . HOH Z  5 .   ? 31.423  -18.974 4.172   1.00 24.46 ? 454 HOH A O   1 
HETATM 8737 O  O   . HOH Z  5 .   ? 7.384   4.952   11.223  1.00 11.05 ? 455 HOH A O   1 
HETATM 8738 O  O   . HOH Z  5 .   ? 13.674  16.507  11.829  1.00 15.96 ? 456 HOH A O   1 
HETATM 8739 O  O   . HOH Z  5 .   ? 23.920  -16.148 29.728  1.00 25.85 ? 457 HOH A O   1 
HETATM 8740 O  O   . HOH Z  5 .   ? 28.677  2.293   -1.388  1.00 23.45 ? 458 HOH A O   1 
HETATM 8741 O  O   . HOH Z  5 .   ? 30.439  -8.805  -2.601  1.00 21.73 ? 459 HOH A O   1 
HETATM 8742 O  O   . HOH Z  5 .   ? 10.343  4.811   8.831   1.00 12.37 ? 460 HOH A O   1 
HETATM 8743 O  O   . HOH Z  5 .   ? 36.205  -6.955  26.366  1.00 24.62 ? 461 HOH A O   1 
HETATM 8744 O  O   . HOH Z  5 .   ? 14.122  1.829   -2.989  1.00 22.49 ? 462 HOH A O   1 
HETATM 8745 O  O   . HOH Z  5 .   ? 23.057  -12.358 9.749   1.00 12.09 ? 463 HOH A O   1 
HETATM 8746 O  O   . HOH Z  5 .   ? 36.721  -4.451  -0.816  1.00 19.30 ? 464 HOH A O   1 
HETATM 8747 O  O   . HOH Z  5 .   ? 16.623  11.015  -3.072  1.00 27.81 ? 465 HOH A O   1 
HETATM 8748 O  O   . HOH Z  5 .   ? 4.965   -9.263  25.732  1.00 25.79 ? 466 HOH A O   1 
HETATM 8749 O  O   . HOH Z  5 .   ? 17.445  0.188   28.551  1.00 20.43 ? 467 HOH A O   1 
HETATM 8750 O  O   . HOH Z  5 .   ? 17.152  0.756   -0.430  1.00 16.80 ? 468 HOH A O   1 
HETATM 8751 O  O   . HOH Z  5 .   ? 5.614   -12.073 13.349  1.00 20.42 ? 469 HOH A O   1 
HETATM 8752 O  O   . HOH Z  5 .   ? 14.517  -9.971  26.062  1.00 16.76 ? 470 HOH A O   1 
HETATM 8753 O  O   . HOH Z  5 .   ? 16.026  -12.131 26.802  1.00 21.09 ? 471 HOH A O   1 
HETATM 8754 O  O   . HOH Z  5 .   ? 25.717  -15.984 6.642   1.00 14.32 ? 472 HOH A O   1 
HETATM 8755 O  O   . HOH Z  5 .   ? 19.441  9.732   32.402  1.00 22.03 ? 473 HOH A O   1 
HETATM 8756 O  O   . HOH Z  5 .   ? 23.392  3.311   -2.058  1.00 16.10 ? 474 HOH A O   1 
HETATM 8757 O  O   . HOH Z  5 .   ? 13.990  1.629   -0.201  1.00 19.90 ? 475 HOH A O   1 
HETATM 8758 O  O   . HOH Z  5 .   ? 20.955  -2.738  -5.268  1.00 22.60 ? 476 HOH A O   1 
HETATM 8759 O  O   . HOH Z  5 .   ? 12.884  -12.238 16.574  1.00 23.37 ? 477 HOH A O   1 
HETATM 8760 O  O   . HOH Z  5 .   ? 15.165  -13.595 16.762  1.00 17.02 ? 478 HOH A O   1 
HETATM 8761 O  O   . HOH Z  5 .   ? 12.180  -10.562 27.372  1.00 17.87 ? 479 HOH A O   1 
HETATM 8762 O  O   . HOH Z  5 .   ? 11.100  -5.061  0.740   1.00 21.44 ? 480 HOH A O   1 
HETATM 8763 O  O   . HOH Z  5 .   ? 40.030  -12.170 11.763  1.00 24.54 ? 481 HOH A O   1 
HETATM 8764 O  O   . HOH Z  5 .   ? 13.204  14.168  14.077  1.00 21.53 ? 482 HOH A O   1 
HETATM 8765 O  O   . HOH Z  5 .   ? 11.643  7.997   1.714   1.00 13.39 ? 483 HOH A O   1 
HETATM 8766 O  O   . HOH Z  5 .   ? 15.212  -14.456 19.303  1.00 17.64 ? 484 HOH A O   1 
HETATM 8767 O  O   . HOH Z  5 .   ? 7.786   -8.173  11.862  1.00 26.02 ? 485 HOH A O   1 
HETATM 8768 O  O   . HOH Z  5 .   ? 38.643  4.124   11.340  1.00 19.29 ? 486 HOH A O   1 
HETATM 8769 O  O   . HOH Z  5 .   ? 26.209  -18.481 20.654  1.00 21.30 ? 487 HOH A O   1 
HETATM 8770 O  O   . HOH Z  5 .   ? 19.036  11.823  -0.797  1.00 21.91 ? 488 HOH A O   1 
HETATM 8771 O  O   . HOH Z  5 .   ? 32.922  6.811   15.524  1.00 32.18 ? 489 HOH A O   1 
HETATM 8772 O  O   . HOH Z  5 .   ? 7.683   9.167   14.182  1.00 18.96 ? 490 HOH A O   1 
HETATM 8773 O  O   . HOH Z  5 .   ? 29.812  -15.633 -1.799  1.00 22.75 ? 491 HOH A O   1 
HETATM 8774 O  O   . HOH Z  5 .   ? 13.776  -12.608 20.937  1.00 19.17 ? 492 HOH A O   1 
HETATM 8775 O  O   . HOH Z  5 .   ? 20.848  -9.854  31.884  1.00 22.24 ? 493 HOH A O   1 
HETATM 8776 O  O   . HOH Z  5 .   ? 35.431  10.328  9.994   1.00 28.93 ? 494 HOH A O   1 
HETATM 8777 O  O   . HOH Z  5 .   ? 6.249   -2.954  13.409  1.00 18.82 ? 495 HOH A O   1 
HETATM 8778 O  O   . HOH Z  5 .   ? 9.773   -2.641  10.476  1.00 18.31 ? 496 HOH A O   1 
HETATM 8779 O  O   . HOH Z  5 .   ? 24.138  10.464  12.466  1.00 31.17 ? 497 HOH A O   1 
HETATM 8780 O  O   . HOH Z  5 .   ? 33.165  -14.829 3.496   1.00 24.16 ? 498 HOH A O   1 
HETATM 8781 O  O   . HOH Z  5 .   ? 7.449   -1.911  -0.641  1.00 25.31 ? 499 HOH A O   1 
HETATM 8782 O  O   . HOH Z  5 .   ? 25.697  -18.543 12.561  1.00 25.14 ? 500 HOH A O   1 
HETATM 8783 O  O   . HOH Z  5 .   ? 32.041  -16.907 20.866  1.00 35.06 ? 501 HOH A O   1 
HETATM 8784 O  O   . HOH Z  5 .   ? 31.904  -2.928  -5.145  1.00 33.39 ? 502 HOH A O   1 
HETATM 8785 O  O   . HOH Z  5 .   ? 26.168  -17.912 17.358  1.00 22.54 ? 503 HOH A O   1 
HETATM 8786 O  O   . HOH Z  5 .   ? 43.430  -9.542  11.466  1.00 24.35 ? 504 HOH A O   1 
HETATM 8787 O  O   . HOH Z  5 .   ? 13.415  5.101   -0.335  1.00 22.26 ? 505 HOH A O   1 
HETATM 8788 O  O   . HOH Z  5 .   ? 14.336  4.468   -3.924  1.00 21.48 ? 506 HOH A O   1 
HETATM 8789 O  O   . HOH Z  5 .   ? 32.398  -16.905 10.206  1.00 30.73 ? 507 HOH A O   1 
HETATM 8790 O  O   . HOH Z  5 .   ? 27.762  -21.162 24.727  1.00 30.64 ? 508 HOH A O   1 
HETATM 8791 O  O   . HOH Z  5 .   ? 37.325  7.876   9.426   1.00 26.79 ? 509 HOH A O   1 
HETATM 8792 O  O   . HOH Z  5 .   ? 8.249   -10.457 26.425  1.00 30.93 ? 510 HOH A O   1 
HETATM 8793 O  O   . HOH Z  5 .   ? 10.792  -4.515  -5.269  1.00 35.39 ? 511 HOH A O   1 
HETATM 8794 O  O   . HOH Z  5 .   ? 13.190  -14.614 12.897  1.00 33.13 ? 512 HOH A O   1 
HETATM 8795 O  O   . HOH Z  5 .   ? 32.956  5.075   20.160  1.00 23.75 ? 513 HOH A O   1 
HETATM 8796 O  O   . HOH Z  5 .   ? 31.536  -13.225 2.488   1.00 23.40 ? 514 HOH A O   1 
HETATM 8797 O  O   . HOH Z  5 .   ? 7.512   -6.680  2.499   1.00 25.23 ? 515 HOH A O   1 
HETATM 8798 O  O   . HOH Z  5 .   ? 20.667  17.984  7.610   1.00 35.70 ? 516 HOH A O   1 
HETATM 8799 O  O   . HOH Z  5 .   ? 26.547  5.414   -3.753  1.00 26.09 ? 517 HOH A O   1 
HETATM 8800 O  O   . HOH Z  5 .   ? 24.570  -7.663  -7.695  1.00 37.45 ? 518 HOH A O   1 
HETATM 8801 O  O   . HOH Z  5 .   ? 7.908   6.639   15.551  1.00 16.67 ? 519 HOH A O   1 
HETATM 8802 O  O   . HOH Z  5 .   ? 10.889  12.539  20.565  1.00 30.71 ? 520 HOH A O   1 
HETATM 8803 O  O   . HOH Z  5 .   ? 29.217  -14.901 17.100  1.00 21.00 ? 521 HOH A O   1 
HETATM 8804 O  O   . HOH Z  5 .   ? 24.160  -20.873 26.851  1.00 26.93 ? 522 HOH A O   1 
HETATM 8805 O  O   . HOH Z  5 .   ? 28.874  -18.627 20.662  1.00 26.72 ? 523 HOH A O   1 
HETATM 8806 O  O   . HOH Z  5 .   ? 33.930  -13.324 26.640  1.00 26.53 ? 524 HOH A O   1 
HETATM 8807 O  O   . HOH Z  5 .   ? 14.313  -2.084  28.978  1.00 24.88 ? 525 HOH A O   1 
HETATM 8808 O  O   . HOH Z  5 .   ? 21.349  16.176  5.297   1.00 24.44 ? 526 HOH A O   1 
HETATM 8809 O  O   . HOH Z  5 .   ? 9.281   11.430  1.134   1.00 17.13 ? 527 HOH A O   1 
HETATM 8810 O  O   . HOH Z  5 .   ? 6.072   -4.095  -8.187  1.00 34.39 ? 528 HOH A O   1 
HETATM 8811 O  O   . HOH Z  5 .   ? 29.680  11.882  -4.861  1.00 26.77 ? 529 HOH A O   1 
HETATM 8812 O  O   . HOH Z  5 .   ? 33.736  -17.474 2.878   1.00 33.12 ? 530 HOH A O   1 
HETATM 8813 O  O   . HOH Z  5 .   ? 27.372  -5.529  -5.206  1.00 22.17 ? 531 HOH A O   1 
HETATM 8814 O  O   . HOH Z  5 .   ? 26.089  11.105  30.883  1.00 25.07 ? 532 HOH A O   1 
HETATM 8815 O  O   . HOH Z  5 .   ? 39.632  -12.628 19.984  1.00 23.74 ? 533 HOH A O   1 
HETATM 8816 O  O   . HOH Z  5 .   ? 11.354  3.449   19.389  1.00 21.56 ? 534 HOH A O   1 
HETATM 8817 O  O   . HOH Z  5 .   ? 38.256  -7.549  24.461  1.00 26.79 ? 535 HOH A O   1 
HETATM 8818 O  O   . HOH Z  5 .   ? 12.058  -15.313 8.612   1.00 27.70 ? 536 HOH A O   1 
HETATM 8819 O  O   . HOH Z  5 .   ? 30.181  -18.054 -2.612  1.00 32.30 ? 537 HOH A O   1 
HETATM 8820 O  O   . HOH Z  5 .   ? 32.163  -18.304 7.159   1.00 31.83 ? 538 HOH A O   1 
HETATM 8821 O  O   . HOH Z  5 .   ? 10.266  -4.103  19.599  1.00 26.06 ? 539 HOH A O   1 
HETATM 8822 O  O   . HOH Z  5 .   ? 34.027  1.568   -5.813  1.00 32.55 ? 540 HOH A O   1 
HETATM 8823 O  O   . HOH Z  5 .   ? 11.612  9.835   -2.154  1.00 27.76 ? 541 HOH A O   1 
HETATM 8824 O  O   . HOH Z  5 .   ? 6.406   15.796  16.007  1.00 29.99 ? 542 HOH A O   1 
HETATM 8825 O  O   . HOH Z  5 .   ? 19.754  14.016  28.567  1.00 27.22 ? 543 HOH A O   1 
HETATM 8826 O  O   . HOH Z  5 .   ? 32.576  -15.081 28.292  1.00 33.56 ? 544 HOH A O   1 
HETATM 8827 O  O   . HOH Z  5 .   ? 26.680  13.385  24.377  1.00 39.36 ? 545 HOH A O   1 
HETATM 8828 O  O   . HOH Z  5 .   ? 15.127  -15.910 15.171  1.00 23.23 ? 546 HOH A O   1 
HETATM 8829 O  O   . HOH Z  5 .   ? 20.912  4.011   16.503  1.00 17.88 ? 547 HOH A O   1 
HETATM 8830 O  O   . HOH Z  5 .   ? 14.956  7.247   21.038  1.00 29.26 ? 548 HOH A O   1 
HETATM 8831 O  O   . HOH Z  5 .   ? 31.245  -20.959 8.617   1.00 27.76 ? 549 HOH A O   1 
HETATM 8832 O  O   . HOH Z  5 .   ? 17.241  -3.497  -8.283  1.00 34.06 ? 550 HOH A O   1 
HETATM 8833 O  O   . HOH Z  5 .   ? 10.453  -8.940  -8.044  1.00 34.35 ? 551 HOH A O   1 
HETATM 8834 O  O   . HOH Z  5 .   ? 39.840  -12.070 23.012  1.00 33.71 ? 552 HOH A O   1 
HETATM 8835 O  O   . HOH Z  5 .   ? 11.536  -13.018 25.863  1.00 29.17 ? 553 HOH A O   1 
HETATM 8836 O  O   . HOH Z  5 .   ? 14.481  4.669   23.968  1.00 32.41 ? 554 HOH A O   1 
HETATM 8837 O  O   . HOH Z  5 .   ? 23.573  -10.218 32.619  1.00 28.30 ? 555 HOH A O   1 
HETATM 8838 O  O   . HOH Z  5 .   ? 24.571  -11.662 30.398  1.00 28.69 ? 556 HOH A O   1 
HETATM 8839 O  O   . HOH Z  5 .   ? 9.345   -14.321 1.770   1.00 33.09 ? 557 HOH A O   1 
HETATM 8840 O  O   . HOH Z  5 .   ? 32.762  -16.139 12.753  1.00 35.91 ? 558 HOH A O   1 
HETATM 8841 O  O   . HOH Z  5 .   ? 10.080  2.925   22.543  1.00 33.80 ? 559 HOH A O   1 
HETATM 8842 O  O   . HOH Z  5 .   ? 23.581  -21.637 -3.436  1.00 34.41 ? 560 HOH A O   1 
HETATM 8843 O  O   . HOH Z  5 .   ? 12.487  4.543   22.114  1.00 29.07 ? 561 HOH A O   1 
HETATM 8844 O  O   . HOH Z  5 .   ? 33.911  -10.815 28.109  1.00 33.33 ? 562 HOH A O   1 
HETATM 8845 O  O   . HOH Z  5 .   ? 7.392   -0.779  8.214   1.00 32.31 ? 563 HOH A O   1 
HETATM 8846 O  O   . HOH Z  5 .   ? 44.161  -9.802  8.186   1.00 28.63 ? 564 HOH A O   1 
HETATM 8847 O  O   . HOH Z  5 .   ? 41.409  12.199  7.783   1.00 36.30 ? 565 HOH A O   1 
HETATM 8848 O  O   . HOH Z  5 .   ? 15.369  -15.581 2.677   1.00 29.82 ? 566 HOH A O   1 
HETATM 8849 O  O   . HOH Z  5 .   ? 26.665  12.666  6.407   1.00 33.09 ? 567 HOH A O   1 
HETATM 8850 O  O   . HOH Z  5 .   ? 6.710   -9.859  4.547   1.00 26.06 ? 568 HOH A O   1 
HETATM 8851 O  O   . HOH Z  5 .   ? 38.889  -5.726  -3.101  1.00 29.35 ? 569 HOH A O   1 
HETATM 8852 O  O   . HOH Z  5 .   ? 38.261  -13.562 5.637   1.00 28.29 ? 570 HOH A O   1 
HETATM 8853 O  O   . HOH Z  5 .   ? 32.272  -16.745 17.179  1.00 36.68 ? 571 HOH A O   1 
HETATM 8854 O  O   . HOH Z  5 .   ? 7.957   -1.754  15.222  1.00 27.65 ? 572 HOH A O   1 
HETATM 8855 O  O   . HOH Z  5 .   ? 15.902  4.578   21.730  1.00 26.82 ? 573 HOH A O   1 
HETATM 8856 O  O   . HOH Z  5 .   ? 37.319  10.322  23.695  1.00 36.18 ? 574 HOH A O   1 
HETATM 8857 O  O   . HOH Z  5 .   ? 28.128  -21.395 2.090   1.00 37.02 ? 575 HOH A O   1 
HETATM 8858 O  O   . HOH Z  5 .   ? 6.037   -3.533  20.852  1.00 28.14 ? 576 HOH A O   1 
HETATM 8859 O  O   . HOH Z  5 .   ? 36.511  13.705  -1.046  1.00 35.60 ? 577 HOH A O   1 
HETATM 8860 O  O   . HOH Z  5 .   ? 4.151   13.581  19.798  1.00 40.57 ? 578 HOH A O   1 
HETATM 8861 O  O   . HOH Z  5 .   ? 36.931  -15.246 2.103   1.00 43.06 ? 579 HOH A O   1 
HETATM 8862 O  O   . HOH Z  5 .   ? 11.918  5.382   -4.193  1.00 37.13 ? 580 HOH A O   1 
HETATM 8863 O  O   . HOH Z  5 .   ? 30.080  -17.741 18.502  1.00 32.20 ? 581 HOH A O   1 
HETATM 8864 O  O   . HOH Z  5 .   ? 27.252  -18.466 14.674  1.00 40.84 ? 582 HOH A O   1 
HETATM 8865 O  O   . HOH Z  5 .   ? 23.178  7.480   14.500  1.00 28.50 ? 583 HOH A O   1 
HETATM 8866 O  O   . HOH Z  5 .   ? 28.118  8.531   17.061  1.00 32.84 ? 584 HOH A O   1 
HETATM 8867 O  O   . HOH Z  5 .   ? 18.386  -3.135  -5.580  1.00 31.00 ? 585 HOH A O   1 
HETATM 8868 O  O   . HOH Z  5 .   ? 23.995  14.761  4.639   1.00 32.60 ? 586 HOH A O   1 
HETATM 8869 O  O   . HOH Z  5 .   ? 9.251   -10.893 14.165  1.00 32.37 ? 587 HOH A O   1 
HETATM 8870 O  O   . HOH Z  5 .   ? 9.550   -5.266  -1.326  1.00 32.72 ? 588 HOH A O   1 
HETATM 8871 O  O   . HOH Z  5 .   ? 11.497  1.590   -4.079  1.00 34.93 ? 589 HOH A O   1 
HETATM 8872 O  O   . HOH Z  5 .   ? 21.155  11.914  -2.787  1.00 34.66 ? 590 HOH A O   1 
HETATM 8873 O  O   . HOH Z  5 .   ? 43.034  -10.069 19.168  1.00 31.84 ? 591 HOH A O   1 
HETATM 8874 O  O   . HOH Z  5 .   ? 8.473   -0.271  24.475  1.00 29.36 ? 592 HOH A O   1 
HETATM 8875 O  O   . HOH Z  5 .   ? 12.032  2.221   -6.771  1.00 34.59 ? 593 HOH A O   1 
HETATM 8876 O  O   . HOH Z  5 .   ? 23.210  12.416  14.525  1.00 30.45 ? 594 HOH A O   1 
HETATM 8877 O  O   . HOH Z  5 .   ? 11.322  3.914   -0.060  1.00 26.23 ? 595 HOH A O   1 
HETATM 8878 O  O   . HOH Z  5 .   ? 37.522  15.874  3.443   1.00 36.48 ? 596 HOH A O   1 
HETATM 8879 O  O   . HOH Z  5 .   ? 32.685  6.778   12.800  1.00 31.97 ? 597 HOH A O   1 
HETATM 8880 O  O   . HOH Z  5 .   ? 31.554  -20.095 -1.377  1.00 39.48 ? 598 HOH A O   1 
HETATM 8881 O  O   . HOH Z  5 .   ? 29.966  7.045   13.359  1.00 32.94 ? 599 HOH A O   1 
HETATM 8882 O  O   . HOH Z  5 .   ? 27.197  7.737   14.741  1.00 37.48 ? 600 HOH A O   1 
HETATM 8883 O  O   . HOH Z  5 .   ? 8.809   3.068   20.089  1.00 38.69 ? 601 HOH A O   1 
HETATM 8884 O  O   . HOH Z  5 .   ? 13.292  13.671  -1.699  1.00 33.79 ? 602 HOH A O   1 
HETATM 8885 O  O   . HOH Z  5 .   ? 19.345  10.457  -4.419  1.00 34.09 ? 603 HOH A O   1 
HETATM 8886 O  O   . HOH Z  5 .   ? 7.335   -5.739  5.235   1.00 31.03 ? 604 HOH A O   1 
HETATM 8887 O  O   . HOH Z  5 .   ? 26.930  -19.012 -1.086  1.00 37.35 ? 605 HOH A O   1 
HETATM 8888 O  O   . HOH Z  5 .   ? 27.325  -15.962 -5.709  1.00 34.02 ? 606 HOH A O   1 
HETATM 8889 O  O   . HOH Z  5 .   ? 9.488   -5.108  16.720  1.00 31.50 ? 607 HOH A O   1 
HETATM 8890 O  O   . HOH Z  5 .   ? 38.028  10.052  -5.078  1.00 30.00 ? 608 HOH A O   1 
HETATM 8891 O  O   . HOH Z  5 .   ? 19.458  -18.442 26.206  1.00 27.18 ? 609 HOH A O   1 
HETATM 8892 O  O   . HOH Z  5 .   ? 28.284  -4.813  31.402  1.00 33.51 ? 610 HOH A O   1 
HETATM 8893 O  O   . HOH Z  5 .   ? 29.368  -16.831 14.903  1.00 27.47 ? 611 HOH A O   1 
HETATM 8894 O  O   . HOH Z  5 .   ? 23.691  -4.124  -5.607  1.00 42.36 ? 612 HOH A O   1 
HETATM 8895 O  O   . HOH Z  5 .   ? 12.384  4.825   29.790  1.00 36.17 ? 613 HOH A O   1 
HETATM 8896 O  O   . HOH Z  5 .   ? 16.865  -18.573 12.694  1.00 38.06 ? 614 HOH A O   1 
HETATM 8897 O  O   . HOH Z  5 .   ? 35.307  -0.905  30.616  1.00 32.59 ? 615 HOH A O   1 
HETATM 8898 O  O   . HOH Z  5 .   ? 15.630  4.662   -6.673  1.00 37.27 ? 616 HOH A O   1 
HETATM 8899 O  O   . HOH Z  5 .   ? 15.968  13.917  -0.438  1.00 36.26 ? 617 HOH A O   1 
HETATM 8900 O  O   . HOH Z  5 .   ? 39.806  2.948   16.762  1.00 35.60 ? 618 HOH A O   1 
HETATM 8901 O  O   . HOH Z  5 .   ? 26.294  11.788  11.006  1.00 33.73 ? 619 HOH A O   1 
HETATM 8902 O  O   . HOH AA 5 .   ? -31.510 1.751   7.866   1.00 29.73 ? 401 HOH B O   1 
HETATM 8903 O  O   . HOH AA 5 .   ? -17.453 13.212  -3.954  1.00 31.94 ? 402 HOH B O   1 
HETATM 8904 O  O   . HOH AA 5 .   ? -18.709 6.611   23.584  1.00 36.91 ? 403 HOH B O   1 
HETATM 8905 O  O   . HOH AA 5 .   ? -16.823 10.943  4.632   1.00 31.39 ? 404 HOH B O   1 
HETATM 8906 O  O   . HOH AA 5 .   ? -21.046 11.381  6.121   1.00 25.72 ? 405 HOH B O   1 
HETATM 8907 O  O   . HOH AA 5 .   ? -13.186 4.614   -18.695 1.00 43.60 ? 406 HOH B O   1 
HETATM 8908 O  O   . HOH AA 5 .   ? -27.205 3.488   -10.327 1.00 41.83 ? 407 HOH B O   1 
HETATM 8909 O  O   . HOH AA 5 .   ? -29.102 1.085   16.998  1.00 38.62 ? 408 HOH B O   1 
HETATM 8910 O  O   . HOH AA 5 .   ? -29.802 -4.603  -0.736  1.00 20.56 ? 409 HOH B O   1 
HETATM 8911 O  O   . HOH AA 5 .   ? -13.838 -15.157 28.416  1.00 26.08 ? 410 HOH B O   1 
HETATM 8912 O  O   . HOH AA 5 .   ? -30.613 2.043   10.480  1.00 36.23 ? 411 HOH B O   1 
HETATM 8913 O  O   . HOH AA 5 .   ? -16.903 15.975  22.678  1.00 38.26 ? 412 HOH B O   1 
HETATM 8914 O  O   . HOH AA 5 .   ? -27.504 -4.356  8.619   1.00 19.11 ? 413 HOH B O   1 
HETATM 8915 O  O   . HOH AA 5 .   ? 6.102   20.429  -5.400  1.00 29.15 ? 414 HOH B O   1 
HETATM 8916 O  O   . HOH AA 5 .   ? -17.582 -16.552 -6.470  1.00 26.23 ? 415 HOH B O   1 
HETATM 8917 O  O   . HOH AA 5 .   ? -3.793  -17.862 22.361  1.00 26.39 ? 416 HOH B O   1 
HETATM 8918 O  O   . HOH AA 5 .   ? -3.731  19.149  -20.111 1.00 27.43 ? 417 HOH B O   1 
HETATM 8919 O  O   . HOH AA 5 .   ? -16.462 5.318   21.987  1.00 34.25 ? 418 HOH B O   1 
HETATM 8920 O  O   . HOH AA 5 .   ? 7.719   21.513  7.859   1.00 12.05 ? 419 HOH B O   1 
HETATM 8921 O  O   . HOH AA 5 .   ? -21.686 -2.367  -12.728 1.00 28.68 ? 420 HOH B O   1 
HETATM 8922 O  O   . HOH AA 5 .   ? -17.673 -10.178 28.787  1.00 29.57 ? 421 HOH B O   1 
HETATM 8923 O  O   . HOH AA 5 .   ? -7.380  -7.555  28.561  1.00 31.64 ? 422 HOH B O   1 
HETATM 8924 O  O   . HOH AA 5 .   ? -23.118 9.450   6.428   1.00 16.97 ? 423 HOH B O   1 
HETATM 8925 O  O   . HOH AA 5 .   ? 3.497   18.248  -15.590 1.00 35.55 ? 424 HOH B O   1 
HETATM 8926 O  O   . HOH AA 5 .   ? -7.801  -19.772 25.464  1.00 35.87 ? 425 HOH B O   1 
HETATM 8927 O  O   . HOH AA 5 .   ? -12.226 -13.569 -11.321 1.00 16.82 ? 426 HOH B O   1 
HETATM 8928 O  O   . HOH AA 5 .   ? -32.766 -1.680  -8.520  1.00 35.58 ? 427 HOH B O   1 
HETATM 8929 O  O   . HOH AA 5 .   ? 4.073   -14.906 9.961   1.00 33.81 ? 428 HOH B O   1 
HETATM 8930 O  O   . HOH AA 5 .   ? -27.373 6.781   -11.915 1.00 26.03 ? 429 HOH B O   1 
HETATM 8931 O  O   . HOH AA 5 .   ? -35.269 7.012   2.772   1.00 27.51 ? 430 HOH B O   1 
HETATM 8932 O  O   . HOH AA 5 .   ? 6.986   -11.591 17.300  1.00 28.39 ? 431 HOH B O   1 
HETATM 8933 O  O   . HOH AA 5 .   ? 4.503   17.103  3.575   1.00 25.79 ? 432 HOH B O   1 
HETATM 8934 O  O   . HOH AA 5 .   ? -5.560  17.779  -6.998  1.00 48.02 ? 433 HOH B O   1 
HETATM 8935 O  O   . HOH AA 5 .   ? -17.101 11.170  1.937   1.00 26.53 ? 434 HOH B O   1 
HETATM 8936 O  O   . HOH AA 5 .   ? -23.710 -7.715  20.410  1.00 35.53 ? 435 HOH B O   1 
HETATM 8937 O  O   . HOH AA 5 .   ? -5.316  -24.909 23.059  1.00 27.20 ? 436 HOH B O   1 
HETATM 8938 O  O   . HOH AA 5 .   ? -17.733 -3.840  26.878  1.00 32.45 ? 437 HOH B O   1 
HETATM 8939 O  O   . HOH AA 5 .   ? -31.840 5.294   -7.623  1.00 22.90 ? 438 HOH B O   1 
HETATM 8940 O  O   . HOH AA 5 .   ? -15.787 -0.258  -14.920 1.00 25.24 ? 439 HOH B O   1 
HETATM 8941 O  O   . HOH AA 5 .   ? 8.949   16.628  0.894   1.00 17.63 ? 440 HOH B O   1 
HETATM 8942 O  O   . HOH AA 5 .   ? -31.011 2.013   1.827   1.00 28.73 ? 441 HOH B O   1 
HETATM 8943 O  O   . HOH AA 5 .   ? -31.916 -6.563  5.952   1.00 28.13 ? 442 HOH B O   1 
HETATM 8944 O  O   . HOH AA 5 .   ? -6.387  -18.397 -2.148  1.00 28.30 ? 443 HOH B O   1 
HETATM 8945 O  O   . HOH AA 5 .   ? -29.724 -3.252  7.040   1.00 22.94 ? 444 HOH B O   1 
HETATM 8946 O  O   . HOH AA 5 .   ? -34.723 5.531   -5.170  1.00 30.81 ? 445 HOH B O   1 
HETATM 8947 O  O   . HOH AA 5 .   ? -20.491 13.245  7.881   1.00 29.25 ? 446 HOH B O   1 
HETATM 8948 O  O   . HOH AA 5 .   ? -19.375 -0.690  -16.369 1.00 33.98 ? 447 HOH B O   1 
HETATM 8949 O  O   . HOH AA 5 .   ? -32.397 -4.004  -2.037  1.00 28.07 ? 448 HOH B O   1 
HETATM 8950 O  O   . HOH AA 5 .   ? -6.351  -11.594 29.206  1.00 30.18 ? 449 HOH B O   1 
HETATM 8951 O  O   . HOH AA 5 .   ? 4.332   -13.406 22.433  1.00 34.60 ? 450 HOH B O   1 
HETATM 8952 O  O   . HOH AA 5 .   ? -26.492 10.376  5.204   1.00 27.57 ? 451 HOH B O   1 
HETATM 8953 O  O   . HOH AA 5 .   ? -22.763 6.057   -12.480 1.00 25.40 ? 452 HOH B O   1 
HETATM 8954 O  O   . HOH AA 5 .   ? -4.211  -13.025 25.994  1.00 31.43 ? 453 HOH B O   1 
HETATM 8955 O  O   . HOH AA 5 .   ? -1.957  -12.776 24.678  1.00 35.43 ? 454 HOH B O   1 
HETATM 8956 O  O   . HOH AA 5 .   ? -3.171  -12.788 -1.002  1.00 19.64 ? 455 HOH B O   1 
HETATM 8957 O  O   . HOH AA 5 .   ? 3.477   21.395  9.567   1.00 24.75 ? 456 HOH B O   1 
HETATM 8958 O  O   . HOH AA 5 .   ? -0.293  20.920  0.078   1.00 43.75 ? 457 HOH B O   1 
HETATM 8959 O  O   . HOH AA 5 .   ? -23.253 11.321  -1.161  1.00 22.50 ? 458 HOH B O   1 
HETATM 8960 O  O   . HOH AA 5 .   ? -24.133 8.977   -1.650  1.00 19.76 ? 459 HOH B O   1 
HETATM 8961 O  O   . HOH AA 5 .   ? 11.515  14.464  0.014   1.00 31.93 ? 460 HOH B O   1 
HETATM 8962 O  O   . HOH AA 5 .   ? -20.488 -0.179  -14.098 1.00 29.76 ? 461 HOH B O   1 
HETATM 8963 O  O   . HOH AA 5 .   ? -18.055 14.654  7.064   1.00 33.09 ? 462 HOH B O   1 
HETATM 8964 O  O   . HOH AA 5 .   ? 3.909   -16.208 18.254  1.00 35.97 ? 463 HOH B O   1 
HETATM 8965 O  O   . HOH AA 5 .   ? -33.527 3.042   2.504   1.00 31.88 ? 464 HOH B O   1 
HETATM 8966 O  O   . HOH AA 5 .   ? -15.158 15.040  -6.139  1.00 46.91 ? 465 HOH B O   1 
HETATM 8967 O  O   . HOH AA 5 .   ? 8.733   17.574  -3.073  1.00 33.40 ? 466 HOH B O   1 
HETATM 8968 O  O   . HOH AA 5 .   ? -11.546 -19.840 25.013  1.00 36.64 ? 467 HOH B O   1 
HETATM 8969 O  O   . HOH AA 5 .   ? 1.206   22.487  9.610   1.00 35.77 ? 468 HOH B O   1 
HETATM 8970 O  O   . HOH AA 5 .   ? -28.904 9.944   -6.627  1.00 43.64 ? 469 HOH B O   1 
HETATM 8971 O  O   . HOH AA 5 .   ? -24.523 -1.126  -11.786 1.00 25.54 ? 470 HOH B O   1 
HETATM 8972 O  O   . HOH AA 5 .   ? -24.731 8.188   1.115   1.00 26.95 ? 471 HOH B O   1 
HETATM 8973 O  O   . HOH AA 5 .   ? -31.560 -0.007  5.676   1.00 34.41 ? 472 HOH B O   1 
HETATM 8974 O  O   . HOH AA 5 .   ? -10.021 20.251  -8.570  1.00 34.35 ? 473 HOH B O   1 
HETATM 8975 O  O   . HOH AA 5 .   ? -15.826 13.605  6.158   1.00 40.70 ? 474 HOH B O   1 
HETATM 8976 O  O   . HOH AA 5 .   ? -0.117  -13.310 -4.398  1.00 31.66 ? 475 HOH B O   1 
HETATM 8977 O  O   . HOH AA 5 .   ? 2.049   -15.782 16.656  1.00 31.21 ? 476 HOH B O   1 
HETATM 8978 O  O   . HOH AA 5 .   ? -19.240 -16.472 -3.868  1.00 31.19 ? 477 HOH B O   1 
HETATM 8979 O  O   . HOH AA 5 .   ? 5.454   -13.084 15.790  1.00 25.85 ? 478 HOH B O   1 
HETATM 8980 O  O   . HOH AA 5 .   ? -15.729 14.931  -13.550 1.00 42.40 ? 479 HOH B O   1 
HETATM 8981 O  O   . HOH AA 5 .   ? -27.587 8.535   0.459   1.00 41.84 ? 480 HOH B O   1 
HETATM 8982 O  O   . HOH AA 5 .   ? -12.659 -14.360 30.896  1.00 24.02 ? 481 HOH B O   1 
HETATM 8983 O  O   . HOH AA 5 .   ? -10.167 -13.287 30.589  1.00 28.19 ? 482 HOH B O   1 
HETATM 8984 O  O   . HOH AA 5 .   ? 6.580   4.782   13.777  1.00 11.98 ? 483 HOH B O   1 
HETATM 8985 O  O   . HOH AA 5 .   ? 4.254   8.208   7.701   1.00 10.59 ? 484 HOH B O   1 
HETATM 8986 O  O   . HOH AA 5 .   ? 11.036  11.207  8.086   1.00 11.32 ? 485 HOH B O   1 
HETATM 8987 O  O   . HOH AA 5 .   ? -10.222 -9.013  8.249   1.00 10.02 ? 486 HOH B O   1 
HETATM 8988 O  O   . HOH AA 5 .   ? -16.929 -10.444 20.285  1.00 16.71 ? 487 HOH B O   1 
HETATM 8989 O  O   . HOH AA 5 .   ? -1.602  16.643  11.017  1.00 13.38 ? 488 HOH B O   1 
HETATM 8990 O  O   . HOH AA 5 .   ? -2.610  5.049   4.033   1.00 10.70 ? 489 HOH B O   1 
HETATM 8991 O  O   . HOH AA 5 .   ? -30.903 7.234   -4.597  1.00 27.31 ? 490 HOH B O   1 
HETATM 8992 O  O   . HOH AA 5 .   ? -17.737 9.182   -2.566  1.00 19.19 ? 491 HOH B O   1 
HETATM 8993 O  O   . HOH AA 5 .   ? 8.193   4.627   5.193   1.00 11.58 ? 492 HOH B O   1 
HETATM 8994 O  O   . HOH AA 5 .   ? -16.904 -10.808 1.243   1.00 15.21 ? 493 HOH B O   1 
HETATM 8995 O  O   . HOH AA 5 .   ? 1.751   -1.608  5.860   1.00 10.00 ? 494 HOH B O   1 
HETATM 8996 O  O   . HOH AA 5 .   ? -5.742  -12.671 11.889  1.00 18.77 ? 495 HOH B O   1 
HETATM 8997 O  O   . HOH AA 5 .   ? -5.600  1.618   -9.709  1.00 12.17 ? 496 HOH B O   1 
HETATM 8998 O  O   . HOH AA 5 .   ? -13.844 0.280   15.038  1.00 11.90 ? 497 HOH B O   1 
HETATM 8999 O  O   . HOH AA 5 .   ? 6.659   3.297   9.175   1.00 9.05  ? 498 HOH B O   1 
HETATM 9000 O  O   . HOH AA 5 .   ? -13.306 -12.052 11.674  1.00 12.00 ? 499 HOH B O   1 
HETATM 9001 O  O   . HOH AA 5 .   ? -21.703 -8.723  -8.519  1.00 18.30 ? 500 HOH B O   1 
HETATM 9002 O  O   . HOH AA 5 .   ? -5.563  6.443   0.565   1.00 13.61 ? 501 HOH B O   1 
HETATM 9003 O  O   . HOH AA 5 .   ? 3.726   -2.164  13.926  1.00 15.29 ? 502 HOH B O   1 
HETATM 9004 O  O   . HOH AA 5 .   ? -21.848 1.464   18.704  1.00 23.21 ? 503 HOH B O   1 
HETATM 9005 O  O   . HOH AA 5 .   ? -3.951  16.110  -11.111 1.00 18.89 ? 504 HOH B O   1 
HETATM 9006 O  O   . HOH AA 5 .   ? 9.202   7.198   8.566   1.00 18.14 ? 505 HOH B O   1 
HETATM 9007 O  O   . HOH AA 5 .   ? 6.023   -2.412  1.857   1.00 24.00 ? 506 HOH B O   1 
HETATM 9008 O  O   . HOH AA 5 .   ? 4.941   9.180   14.442  1.00 14.92 ? 507 HOH B O   1 
HETATM 9009 O  O   . HOH AA 5 .   ? -13.981 -14.804 5.937   1.00 18.52 ? 508 HOH B O   1 
HETATM 9010 O  O   . HOH AA 5 .   ? 5.206   6.338   1.058   1.00 13.47 ? 509 HOH B O   1 
HETATM 9011 O  O   . HOH AA 5 .   ? -26.192 -9.712  6.101   1.00 27.70 ? 510 HOH B O   1 
HETATM 9012 O  O   . HOH AA 5 .   ? 4.411   6.425   14.177  1.00 12.35 ? 511 HOH B O   1 
HETATM 9013 O  O   . HOH AA 5 .   ? -18.265 -8.145  16.100  1.00 18.99 ? 512 HOH B O   1 
HETATM 9014 O  O   . HOH AA 5 .   ? -8.927  -7.959  -14.447 1.00 17.15 ? 513 HOH B O   1 
HETATM 9015 O  O   . HOH AA 5 .   ? 5.420   5.474   7.705   1.00 11.99 ? 514 HOH B O   1 
HETATM 9016 O  O   . HOH AA 5 .   ? -0.728  11.970  16.231  1.00 15.14 ? 515 HOH B O   1 
HETATM 9017 O  O   . HOH AA 5 .   ? -3.646  2.195   -11.926 1.00 17.61 ? 516 HOH B O   1 
HETATM 9018 O  O   . HOH AA 5 .   ? 5.881   12.237  -4.371  1.00 20.77 ? 517 HOH B O   1 
HETATM 9019 O  O   . HOH AA 5 .   ? 4.821   -5.797  9.001   1.00 24.11 ? 518 HOH B O   1 
HETATM 9020 O  O   . HOH AA 5 .   ? 5.894   -9.420  13.532  1.00 18.45 ? 519 HOH B O   1 
HETATM 9021 O  O   . HOH AA 5 .   ? -25.175 -7.567  12.827  1.00 27.67 ? 520 HOH B O   1 
HETATM 9022 O  O   . HOH AA 5 .   ? -24.586 -2.481  -6.562  1.00 16.92 ? 521 HOH B O   1 
HETATM 9023 O  O   . HOH AA 5 .   ? -4.633  0.319   21.813  1.00 22.08 ? 522 HOH B O   1 
HETATM 9024 O  O   . HOH AA 5 .   ? -20.319 -9.444  15.047  1.00 21.40 ? 523 HOH B O   1 
HETATM 9025 O  O   . HOH AA 5 .   ? -14.735 -14.712 -2.537  1.00 17.98 ? 524 HOH B O   1 
HETATM 9026 O  O   . HOH AA 5 .   ? -19.466 -13.717 14.522  1.00 22.59 ? 525 HOH B O   1 
HETATM 9027 O  O   . HOH AA 5 .   ? -2.877  -5.407  -4.136  1.00 11.91 ? 526 HOH B O   1 
HETATM 9028 O  O   . HOH AA 5 .   ? -4.437  11.390  -15.003 1.00 22.87 ? 527 HOH B O   1 
HETATM 9029 O  O   . HOH AA 5 .   ? -10.390 14.272  -13.428 1.00 20.49 ? 528 HOH B O   1 
HETATM 9030 O  O   . HOH AA 5 .   ? -1.482  14.576  17.029  1.00 24.92 ? 529 HOH B O   1 
HETATM 9031 O  O   . HOH AA 5 .   ? -14.090 -10.894 23.951  1.00 23.32 ? 530 HOH B O   1 
HETATM 9032 O  O   . HOH AA 5 .   ? 7.846   6.037   0.867   1.00 21.78 ? 531 HOH B O   1 
HETATM 9033 O  O   . HOH AA 5 .   ? -22.872 -2.156  -8.690  1.00 17.52 ? 532 HOH B O   1 
HETATM 9034 O  O   . HOH AA 5 .   ? -13.282 7.578   -15.527 1.00 22.01 ? 533 HOH B O   1 
HETATM 9035 O  O   . HOH AA 5 .   ? -21.338 -12.088 15.846  1.00 26.26 ? 534 HOH B O   1 
HETATM 9036 O  O   . HOH AA 5 .   ? 7.885   11.918  14.768  1.00 21.70 ? 535 HOH B O   1 
HETATM 9037 O  O   . HOH AA 5 .   ? 1.640   14.376  -11.357 1.00 32.12 ? 536 HOH B O   1 
HETATM 9038 O  O   . HOH AA 5 .   ? 4.153   -9.326  3.067   1.00 26.35 ? 537 HOH B O   1 
HETATM 9039 O  O   . HOH AA 5 .   ? -0.879  5.727   -4.706  1.00 21.02 ? 538 HOH B O   1 
HETATM 9040 O  O   . HOH AA 5 .   ? 8.737   8.653   2.007   1.00 18.05 ? 539 HOH B O   1 
HETATM 9041 O  O   . HOH AA 5 .   ? -20.981 -5.062  22.039  1.00 25.85 ? 540 HOH B O   1 
HETATM 9042 O  O   . HOH AA 5 .   ? 7.037   -1.094  17.725  1.00 22.63 ? 541 HOH B O   1 
HETATM 9043 O  O   . HOH AA 5 .   ? -1.857  -11.451 -3.278  1.00 19.63 ? 542 HOH B O   1 
HETATM 9044 O  O   . HOH AA 5 .   ? 4.399   -2.109  6.524   1.00 15.24 ? 543 HOH B O   1 
HETATM 9045 O  O   . HOH AA 5 .   ? -19.190 -16.003 15.816  1.00 34.60 ? 544 HOH B O   1 
HETATM 9046 O  O   . HOH AA 5 .   ? -26.996 -6.247  6.619   1.00 18.42 ? 545 HOH B O   1 
HETATM 9047 O  O   . HOH AA 5 .   ? 2.769   -13.371 15.893  1.00 22.31 ? 546 HOH B O   1 
HETATM 9048 O  O   . HOH AA 5 .   ? -3.947  12.550  -18.215 1.00 21.06 ? 547 HOH B O   1 
HETATM 9049 O  O   . HOH AA 5 .   ? -1.258  -0.616  -12.661 1.00 21.51 ? 548 HOH B O   1 
HETATM 9050 O  O   . HOH AA 5 .   ? -12.458 -0.585  22.763  1.00 21.94 ? 549 HOH B O   1 
HETATM 9051 O  O   . HOH AA 5 .   ? -29.638 8.365   6.306   1.00 38.23 ? 550 HOH B O   1 
HETATM 9052 O  O   . HOH AA 5 .   ? -8.217  -5.696  -15.501 1.00 29.49 ? 551 HOH B O   1 
HETATM 9053 O  O   . HOH AA 5 .   ? -0.217  -13.257 22.546  1.00 28.38 ? 552 HOH B O   1 
HETATM 9054 O  O   . HOH AA 5 .   ? -27.119 -3.823  -5.915  1.00 28.86 ? 553 HOH B O   1 
HETATM 9055 O  O   . HOH AA 5 .   ? -7.640  -9.971  -15.984 1.00 21.10 ? 554 HOH B O   1 
HETATM 9056 O  O   . HOH AA 5 .   ? -11.411 -17.345 21.617  1.00 35.45 ? 555 HOH B O   1 
HETATM 9057 O  O   . HOH AA 5 .   ? -20.201 -11.917 8.176   1.00 29.47 ? 556 HOH B O   1 
HETATM 9058 O  O   . HOH AA 5 .   ? -0.814  18.107  0.428   1.00 38.42 ? 557 HOH B O   1 
HETATM 9059 O  O   . HOH AA 5 .   ? -2.980  7.196   -3.776  1.00 21.00 ? 558 HOH B O   1 
HETATM 9060 O  O   . HOH AA 5 .   ? 7.800   -3.328  3.527   1.00 20.76 ? 559 HOH B O   1 
HETATM 9061 O  O   . HOH AA 5 .   ? 4.419   3.251   -5.751  1.00 27.28 ? 560 HOH B O   1 
HETATM 9062 O  O   . HOH AA 5 .   ? -3.431  -8.630  -9.230  1.00 25.63 ? 561 HOH B O   1 
HETATM 9063 O  O   . HOH AA 5 .   ? 5.908   -0.407  -2.399  1.00 29.67 ? 562 HOH B O   1 
HETATM 9064 O  O   . HOH AA 5 .   ? 3.743   3.484   -2.445  1.00 17.69 ? 563 HOH B O   1 
HETATM 9065 O  O   . HOH AA 5 .   ? 7.685   -9.341  15.702  1.00 22.34 ? 564 HOH B O   1 
HETATM 9066 O  O   . HOH AA 5 .   ? -20.927 -10.860 -9.904  1.00 26.73 ? 565 HOH B O   1 
HETATM 9067 O  O   . HOH AA 5 .   ? -17.360 12.912  -12.322 1.00 27.91 ? 566 HOH B O   1 
HETATM 9068 O  O   . HOH AA 5 .   ? -17.547 -14.347 -2.321  1.00 25.29 ? 567 HOH B O   1 
HETATM 9069 O  O   . HOH AA 5 .   ? -27.096 -10.170 1.663   1.00 26.64 ? 568 HOH B O   1 
HETATM 9070 O  O   . HOH AA 5 .   ? 7.306   -11.335 24.174  1.00 30.43 ? 569 HOH B O   1 
HETATM 9071 O  O   . HOH AA 5 .   ? -25.313 15.054  17.420  1.00 35.42 ? 570 HOH B O   1 
HETATM 9072 O  O   . HOH AA 5 .   ? -11.489 -8.350  -14.981 1.00 26.15 ? 571 HOH B O   1 
HETATM 9073 O  O   . HOH AA 5 .   ? -20.766 -11.360 5.557   1.00 37.22 ? 572 HOH B O   1 
HETATM 9074 O  O   . HOH AA 5 .   ? -26.798 9.452   12.207  1.00 34.79 ? 573 HOH B O   1 
HETATM 9075 O  O   . HOH AA 5 .   ? 4.074   11.086  -13.497 1.00 37.73 ? 574 HOH B O   1 
HETATM 9076 O  O   . HOH AA 5 .   ? -23.949 0.747   21.104  1.00 32.39 ? 575 HOH B O   1 
HETATM 9077 O  O   . HOH AA 5 .   ? -7.117  10.369  2.445   1.00 20.11 ? 576 HOH B O   1 
HETATM 9078 O  O   . HOH AA 5 .   ? 0.066   16.693  -11.038 1.00 32.93 ? 577 HOH B O   1 
HETATM 9079 O  O   . HOH AA 5 .   ? 5.595   -8.095  -1.377  1.00 31.90 ? 578 HOH B O   1 
HETATM 9080 O  O   . HOH AA 5 .   ? 4.173   -2.729  -2.949  1.00 37.12 ? 579 HOH B O   1 
HETATM 9081 O  O   . HOH AA 5 .   ? -3.595  15.187  18.444  1.00 33.88 ? 580 HOH B O   1 
HETATM 9082 O  O   . HOH AA 5 .   ? 6.070   -6.050  14.709  1.00 27.67 ? 581 HOH B O   1 
HETATM 9083 O  O   . HOH AA 5 .   ? -20.206 -11.984 0.706   1.00 33.90 ? 582 HOH B O   1 
HETATM 9084 O  O   . HOH AA 5 .   ? -13.449 -11.863 -13.157 1.00 25.70 ? 583 HOH B O   1 
HETATM 9085 O  O   . HOH AA 5 .   ? 3.709   -2.247  22.715  1.00 26.41 ? 584 HOH B O   1 
HETATM 9086 O  O   . HOH AA 5 .   ? -19.659 -16.057 10.297  1.00 27.33 ? 585 HOH B O   1 
HETATM 9087 O  O   . HOH AA 5 .   ? -21.614 -13.589 18.241  1.00 35.38 ? 586 HOH B O   1 
HETATM 9088 O  O   . HOH AA 5 .   ? 0.677   8.116   -4.568  1.00 22.70 ? 587 HOH B O   1 
HETATM 9089 O  O   . HOH AA 5 .   ? -5.747  -15.508 13.261  1.00 29.92 ? 588 HOH B O   1 
HETATM 9090 O  O   . HOH AA 5 .   ? 4.109   14.732  1.698   1.00 27.57 ? 589 HOH B O   1 
HETATM 9091 O  O   . HOH AA 5 .   ? -2.953  -12.983 15.373  1.00 30.81 ? 590 HOH B O   1 
HETATM 9092 O  O   . HOH AA 5 .   ? -5.872  15.306  2.022   1.00 29.86 ? 591 HOH B O   1 
HETATM 9093 O  O   . HOH AA 5 .   ? -17.511 -12.798 21.343  1.00 27.93 ? 592 HOH B O   1 
HETATM 9094 O  O   . HOH AA 5 .   ? -10.352 -10.517 29.738  1.00 24.06 ? 593 HOH B O   1 
HETATM 9095 O  O   . HOH AA 5 .   ? 4.107   10.045  -6.865  1.00 35.24 ? 594 HOH B O   1 
HETATM 9096 O  O   . HOH AA 5 .   ? -3.206  2.560   21.229  1.00 25.22 ? 595 HOH B O   1 
HETATM 9097 O  O   . HOH AA 5 .   ? -10.070 -2.589  24.581  1.00 45.05 ? 596 HOH B O   1 
HETATM 9098 O  O   . HOH AA 5 .   ? -16.394 -12.288 25.740  1.00 24.98 ? 597 HOH B O   1 
HETATM 9099 O  O   . HOH AA 5 .   ? 5.955   2.347   -3.540  1.00 28.81 ? 598 HOH B O   1 
HETATM 9100 O  O   . HOH AA 5 .   ? -16.657 -16.873 16.725  1.00 30.49 ? 599 HOH B O   1 
HETATM 9101 O  O   . HOH AA 5 .   ? -5.861  2.565   -16.818 1.00 29.50 ? 600 HOH B O   1 
HETATM 9102 O  O   . HOH AA 5 .   ? -26.596 -7.129  -1.632  1.00 23.56 ? 601 HOH B O   1 
HETATM 9103 O  O   . HOH AA 5 .   ? -13.137 13.730  -2.996  1.00 42.61 ? 602 HOH B O   1 
HETATM 9104 O  O   . HOH AA 5 .   ? 6.538   0.755   22.127  1.00 36.83 ? 603 HOH B O   1 
HETATM 9105 O  O   . HOH AA 5 .   ? -3.896  13.236  -5.131  1.00 29.10 ? 604 HOH B O   1 
HETATM 9106 O  O   . HOH AA 5 .   ? 2.516   5.023   -5.562  1.00 28.14 ? 605 HOH B O   1 
HETATM 9107 O  O   . HOH AA 5 .   ? -23.479 -9.091  14.458  1.00 37.16 ? 606 HOH B O   1 
HETATM 9108 O  O   . HOH AA 5 .   ? -9.485  16.882  -15.718 1.00 28.92 ? 607 HOH B O   1 
HETATM 9109 O  O   . HOH AA 5 .   ? -4.704  -12.819 22.202  1.00 32.96 ? 608 HOH B O   1 
HETATM 9110 O  O   . HOH AA 5 .   ? 4.281   -6.087  24.733  1.00 30.36 ? 609 HOH B O   1 
HETATM 9111 O  O   . HOH AA 5 .   ? -0.601  -12.739 15.286  1.00 34.40 ? 610 HOH B O   1 
HETATM 9112 O  O   . HOH AA 5 .   ? 1.335   -0.264  -12.452 1.00 30.18 ? 611 HOH B O   1 
HETATM 9113 O  O   . HOH AA 5 .   ? -19.772 -7.591  -11.592 1.00 36.27 ? 612 HOH B O   1 
HETATM 9114 O  O   . HOH AA 5 .   ? -2.762  1.538   -14.509 1.00 29.17 ? 613 HOH B O   1 
HETATM 9115 O  O   . HOH AA 5 .   ? -20.257 -13.267 11.622  1.00 33.00 ? 614 HOH B O   1 
HETATM 9116 O  O   . HOH AA 5 .   ? -14.558 -13.496 24.048  1.00 27.18 ? 615 HOH B O   1 
HETATM 9117 O  O   . HOH AA 5 .   ? -5.632  -11.540 -14.884 1.00 29.01 ? 616 HOH B O   1 
HETATM 9118 O  O   . HOH AA 5 .   ? -3.550  17.320  -0.900  1.00 36.35 ? 617 HOH B O   1 
HETATM 9119 O  O   . HOH AA 5 .   ? -12.330 -17.507 13.291  1.00 32.30 ? 618 HOH B O   1 
HETATM 9120 O  O   . HOH AA 5 .   ? -0.761  -14.268 6.399   1.00 32.19 ? 619 HOH B O   1 
HETATM 9121 O  O   . HOH AA 5 .   ? -10.750 17.141  -18.804 1.00 38.52 ? 620 HOH B O   1 
HETATM 9122 O  O   . HOH AA 5 .   ? -21.545 -6.516  -9.758  1.00 32.58 ? 621 HOH B O   1 
HETATM 9123 O  O   . HOH AA 5 .   ? -14.522 -14.134 0.679   1.00 17.00 ? 622 HOH B O   1 
HETATM 9124 O  O   . HOH AA 5 .   ? -29.236 2.457   5.875   1.00 21.95 ? 623 HOH B O   1 
HETATM 9125 O  O   . HOH AA 5 .   ? -16.693 -14.068 27.958  1.00 25.29 ? 624 HOH B O   1 
HETATM 9126 O  O   . HOH AA 5 .   ? 5.111   -7.284  1.162   1.00 22.35 ? 625 HOH B O   1 
HETATM 9127 O  O   . HOH AA 5 .   ? 1.085   18.102  -13.839 1.00 29.24 ? 626 HOH B O   1 
HETATM 9128 O  O   . HOH AA 5 .   ? 2.711   6.682   16.783  1.00 28.91 ? 627 HOH B O   1 
HETATM 9129 O  O   . HOH AA 5 .   ? -1.953  9.508   -3.160  1.00 26.56 ? 628 HOH B O   1 
HETATM 9130 O  O   . HOH AA 5 .   ? -7.156  6.935   19.090  1.00 24.40 ? 629 HOH B O   1 
HETATM 9131 O  O   . HOH AA 5 .   ? 1.443   13.021  19.576  1.00 35.60 ? 630 HOH B O   1 
HETATM 9132 O  O   . HOH AA 5 .   ? 8.969   6.489   -1.865  1.00 32.34 ? 631 HOH B O   1 
HETATM 9133 O  O   . HOH AA 5 .   ? -2.600  -10.698 -14.943 1.00 30.90 ? 632 HOH B O   1 
HETATM 9134 O  O   . HOH AA 5 .   ? 12.838  11.476  -3.705  1.00 34.82 ? 633 HOH B O   1 
HETATM 9135 O  O   . HOH AA 5 .   ? 6.475   -5.682  11.311  1.00 31.33 ? 634 HOH B O   1 
HETATM 9136 O  O   . HOH AA 5 .   ? -3.066  18.942  10.572  1.00 32.71 ? 635 HOH B O   1 
HETATM 9137 O  O   . HOH AA 5 .   ? 2.330   6.274   -12.361 1.00 35.20 ? 636 HOH B O   1 
HETATM 9138 O  O   . HOH AA 5 .   ? -7.182  13.588  3.963   1.00 31.73 ? 637 HOH B O   1 
HETATM 9139 O  O   . HOH AA 5 .   ? -18.571 -11.902 23.950  1.00 34.64 ? 638 HOH B O   1 
HETATM 9140 O  O   . HOH AA 5 .   ? -1.663  20.637  8.561   1.00 35.73 ? 639 HOH B O   1 
HETATM 9141 O  O   . HOH AA 5 .   ? -26.511 9.120   -2.817  1.00 30.63 ? 640 HOH B O   1 
HETATM 9142 O  O   . HOH AA 5 .   ? -11.104 14.556  -5.036  1.00 40.96 ? 641 HOH B O   1 
HETATM 9143 O  O   . HOH AA 5 .   ? 7.652   1.261   19.797  1.00 30.37 ? 642 HOH B O   1 
HETATM 9144 O  O   . HOH AA 5 .   ? 5.354   15.933  13.605  1.00 27.80 ? 643 HOH B O   1 
HETATM 9145 O  O   . HOH AA 5 .   ? 7.951   -7.138  16.809  1.00 28.80 ? 644 HOH B O   1 
HETATM 9146 O  O   . HOH AA 5 .   ? 4.828   -12.012 24.638  1.00 37.00 ? 645 HOH B O   1 
HETATM 9147 O  O   . HOH AA 5 .   ? -29.096 7.223   -1.792  1.00 30.35 ? 646 HOH B O   1 
HETATM 9148 O  O   . HOH AA 5 .   ? -26.360 8.874   16.652  1.00 31.13 ? 647 HOH B O   1 
HETATM 9149 O  O   . HOH AA 5 .   ? 4.878   -9.711  -12.472 1.00 30.91 ? 648 HOH B O   1 
HETATM 9150 O  O   . HOH AA 5 .   ? -0.857  -13.088 4.305   1.00 42.29 ? 649 HOH B O   1 
HETATM 9151 O  O   . HOH AA 5 .   ? -5.985  11.349  20.694  1.00 33.81 ? 650 HOH B O   1 
HETATM 9152 O  O   . HOH AA 5 .   ? -11.111 -15.926 3.137   1.00 28.60 ? 651 HOH B O   1 
HETATM 9153 O  O   . HOH AA 5 .   ? -19.990 -12.160 -2.331  1.00 34.65 ? 652 HOH B O   1 
HETATM 9154 O  O   . HOH AA 5 .   ? -12.899 -17.397 7.338   1.00 38.96 ? 653 HOH B O   1 
HETATM 9155 O  O   . HOH AA 5 .   ? -9.621  -18.178 12.808  1.00 39.80 ? 654 HOH B O   1 
HETATM 9156 O  O   . HOH AA 5 .   ? -22.836 -4.427  -10.190 1.00 35.04 ? 655 HOH B O   1 
HETATM 9157 O  O   . HOH AA 5 .   ? -17.080 9.934   -14.234 1.00 40.58 ? 656 HOH B O   1 
HETATM 9158 O  O   . HOH AA 5 .   ? -12.797 -9.069  -12.587 1.00 31.54 ? 657 HOH B O   1 
HETATM 9159 O  O   . HOH AA 5 .   ? -23.636 -11.178 5.505   1.00 39.54 ? 658 HOH B O   1 
HETATM 9160 O  O   . HOH AA 5 .   ? -8.777  8.838   20.192  1.00 38.94 ? 659 HOH B O   1 
HETATM 9161 O  O   . HOH AA 5 .   ? -28.911 -6.502  -2.427  1.00 34.79 ? 660 HOH B O   1 
HETATM 9162 O  O   . HOH BA 5 .   ? 32.688  -19.787 -50.014 1.00 30.43 ? 401 HOH C O   1 
HETATM 9163 O  O   . HOH BA 5 .   ? 47.721  -1.413  -10.237 1.00 36.95 ? 402 HOH C O   1 
HETATM 9164 O  O   . HOH BA 5 .   ? 56.179  8.385   -37.705 1.00 28.83 ? 403 HOH C O   1 
HETATM 9165 O  O   . HOH BA 5 .   ? 27.245  25.316  -32.396 1.00 19.19 ? 404 HOH C O   1 
HETATM 9166 O  O   . HOH BA 5 .   ? 46.411  8.158   -11.536 1.00 27.04 ? 405 HOH C O   1 
HETATM 9167 O  O   . HOH BA 5 .   ? 44.511  -14.834 -50.539 1.00 36.97 ? 406 HOH C O   1 
HETATM 9168 O  O   . HOH BA 5 .   ? 35.299  -21.432 -51.157 1.00 22.80 ? 407 HOH C O   1 
HETATM 9169 O  O   . HOH BA 5 .   ? 56.730  4.548   -42.188 1.00 23.38 ? 408 HOH C O   1 
HETATM 9170 O  O   . HOH BA 5 .   ? 56.397  9.146   -40.317 1.00 33.10 ? 409 HOH C O   1 
HETATM 9171 O  O   . HOH BA 5 .   ? 35.631  -13.697 -54.551 1.00 24.06 ? 410 HOH C O   1 
HETATM 9172 O  O   . HOH BA 5 .   ? 41.532  -8.341  -54.985 1.00 23.92 ? 411 HOH C O   1 
HETATM 9173 O  O   . HOH BA 5 .   ? 27.383  16.321  -41.351 1.00 15.91 ? 412 HOH C O   1 
HETATM 9174 O  O   . HOH BA 5 .   ? 52.619  1.228   -13.277 1.00 31.36 ? 413 HOH C O   1 
HETATM 9175 O  O   . HOH BA 5 .   ? 56.468  3.786   -12.958 1.00 25.06 ? 414 HOH C O   1 
HETATM 9176 O  O   . HOH BA 5 .   ? 52.739  4.922   -49.140 1.00 30.42 ? 415 HOH C O   1 
HETATM 9177 O  O   . HOH BA 5 .   ? 58.416  -1.983  -30.009 1.00 32.97 ? 416 HOH C O   1 
HETATM 9178 O  O   . HOH BA 5 .   ? 33.334  22.565  -34.831 1.00 39.78 ? 417 HOH C O   1 
HETATM 9179 O  O   . HOH BA 5 .   ? 43.266  -1.269  -10.863 1.00 39.42 ? 418 HOH C O   1 
HETATM 9180 O  O   . HOH BA 5 .   ? 38.902  2.029   -6.148  1.00 21.68 ? 419 HOH C O   1 
HETATM 9181 O  O   . HOH BA 5 .   ? 46.866  -13.021 -53.211 1.00 23.56 ? 420 HOH C O   1 
HETATM 9182 O  O   . HOH BA 5 .   ? 59.884  -2.136  -35.357 1.00 33.53 ? 421 HOH C O   1 
HETATM 9183 O  O   . HOH BA 5 .   ? 46.362  11.660  -13.270 1.00 38.63 ? 422 HOH C O   1 
HETATM 9184 O  O   . HOH BA 5 .   ? 41.002  3.943   -6.757  1.00 25.04 ? 423 HOH C O   1 
HETATM 9185 O  O   . HOH BA 5 .   ? 61.725  -1.092  -33.066 1.00 29.39 ? 424 HOH C O   1 
HETATM 9186 O  O   . HOH BA 5 .   ? 39.048  -26.706 -44.583 1.00 23.23 ? 425 HOH C O   1 
HETATM 9187 O  O   . HOH BA 5 .   ? 54.677  1.317   -14.849 1.00 33.60 ? 426 HOH C O   1 
HETATM 9188 O  O   . HOH BA 5 .   ? 32.582  -14.617 -51.555 1.00 26.46 ? 427 HOH C O   1 
HETATM 9189 O  O   . HOH BA 5 .   ? 44.164  13.861  -47.856 1.00 30.32 ? 428 HOH C O   1 
HETATM 9190 O  O   . HOH BA 5 .   ? 51.972  5.484   -12.962 1.00 28.40 ? 429 HOH C O   1 
HETATM 9191 O  O   . HOH BA 5 .   ? 22.273  -13.961 -35.668 1.00 36.52 ? 430 HOH C O   1 
HETATM 9192 O  O   . HOH BA 5 .   ? 42.655  -5.707  -54.524 1.00 26.01 ? 431 HOH C O   1 
HETATM 9193 O  O   . HOH BA 5 .   ? 40.518  6.693   -7.465  1.00 31.32 ? 432 HOH C O   1 
HETATM 9194 O  O   . HOH BA 5 .   ? 28.228  27.104  -30.626 1.00 23.99 ? 433 HOH C O   1 
HETATM 9195 O  O   . HOH BA 5 .   ? 61.897  -6.582  -16.953 1.00 36.96 ? 434 HOH C O   1 
HETATM 9196 O  O   . HOH BA 5 .   ? 41.821  -26.199 -44.663 1.00 35.40 ? 435 HOH C O   1 
HETATM 9197 O  O   . HOH BA 5 .   ? 41.865  -10.667 -56.694 1.00 22.39 ? 436 HOH C O   1 
HETATM 9198 O  O   . HOH BA 5 .   ? 48.813  -11.235 -52.979 1.00 23.73 ? 437 HOH C O   1 
HETATM 9199 O  O   . HOH BA 5 .   ? 20.415  -16.158 -50.452 1.00 37.05 ? 438 HOH C O   1 
HETATM 9200 O  O   . HOH BA 5 .   ? 53.566  -3.463  -46.193 1.00 38.75 ? 439 HOH C O   1 
HETATM 9201 O  O   . HOH BA 5 .   ? 20.784  13.597  -35.693 1.00 12.53 ? 440 HOH C O   1 
HETATM 9202 O  O   . HOH BA 5 .   ? 25.279  -1.606  -40.657 1.00 12.68 ? 441 HOH C O   1 
HETATM 9203 O  O   . HOH BA 5 .   ? 26.131  7.023   -41.194 1.00 13.41 ? 442 HOH C O   1 
HETATM 9204 O  O   . HOH BA 5 .   ? 31.881  2.552   -43.765 1.00 16.52 ? 443 HOH C O   1 
HETATM 9205 O  O   . HOH BA 5 .   ? 23.340  4.799   -36.079 1.00 9.92  ? 444 HOH C O   1 
HETATM 9206 O  O   . HOH BA 5 .   ? 32.457  11.353  -43.268 1.00 13.93 ? 445 HOH C O   1 
HETATM 9207 O  O   . HOH BA 5 .   ? 29.674  -4.925  -22.129 1.00 17.33 ? 446 HOH C O   1 
HETATM 9208 O  O   . HOH BA 5 .   ? 26.627  9.388   -34.796 1.00 13.07 ? 447 HOH C O   1 
HETATM 9209 O  O   . HOH BA 5 .   ? 34.102  16.039  -38.334 1.00 14.19 ? 448 HOH C O   1 
HETATM 9210 O  O   . HOH BA 5 .   ? 25.111  8.261   -28.017 1.00 17.24 ? 449 HOH C O   1 
HETATM 9211 O  O   . HOH BA 5 .   ? 22.079  6.896   -32.271 1.00 12.53 ? 450 HOH C O   1 
HETATM 9212 O  O   . HOH BA 5 .   ? 25.887  -3.448  -42.673 1.00 18.56 ? 451 HOH C O   1 
HETATM 9213 O  O   . HOH BA 5 .   ? 28.619  3.386   -43.516 1.00 17.24 ? 452 HOH C O   1 
HETATM 9214 O  O   . HOH BA 5 .   ? 20.169  -10.063 -29.954 1.00 20.64 ? 453 HOH C O   1 
HETATM 9215 O  O   . HOH BA 5 .   ? 43.175  -2.275  -40.425 1.00 14.96 ? 454 HOH C O   1 
HETATM 9216 O  O   . HOH BA 5 .   ? 24.985  6.624   -34.684 1.00 13.03 ? 455 HOH C O   1 
HETATM 9217 O  O   . HOH BA 5 .   ? 27.068  -0.794  -32.323 1.00 11.90 ? 456 HOH C O   1 
HETATM 9218 O  O   . HOH BA 5 .   ? 23.664  5.732   -40.747 1.00 12.98 ? 457 HOH C O   1 
HETATM 9219 O  O   . HOH BA 5 .   ? 32.444  5.006   -30.504 1.00 14.71 ? 458 HOH C O   1 
HETATM 9220 O  O   . HOH BA 5 .   ? 24.226  -0.679  -32.898 1.00 18.43 ? 459 HOH C O   1 
HETATM 9221 O  O   . HOH BA 5 .   ? 28.809  3.669   -46.238 1.00 19.74 ? 460 HOH C O   1 
HETATM 9222 O  O   . HOH BA 5 .   ? 33.781  1.635   -16.592 1.00 17.31 ? 461 HOH C O   1 
HETATM 9223 O  O   . HOH BA 5 .   ? 22.377  11.053  -29.408 1.00 18.95 ? 462 HOH C O   1 
HETATM 9224 O  O   . HOH BA 5 .   ? 23.470  -4.531  -35.932 1.00 20.09 ? 463 HOH C O   1 
HETATM 9225 O  O   . HOH BA 5 .   ? 40.478  -13.907 -36.308 1.00 18.85 ? 464 HOH C O   1 
HETATM 9226 O  O   . HOH BA 5 .   ? 33.347  12.066  -10.929 1.00 25.39 ? 465 HOH C O   1 
HETATM 9227 O  O   . HOH BA 5 .   ? 35.819  -1.069  -48.478 1.00 19.77 ? 466 HOH C O   1 
HETATM 9228 O  O   . HOH BA 5 .   ? 28.299  18.391  -31.734 1.00 18.15 ? 467 HOH C O   1 
HETATM 9229 O  O   . HOH BA 5 .   ? 51.486  -2.393  -43.770 1.00 27.43 ? 468 HOH C O   1 
HETATM 9230 O  O   . HOH BA 5 .   ? 26.397  9.758   -41.824 1.00 14.13 ? 469 HOH C O   1 
HETATM 9231 O  O   . HOH BA 5 .   ? 32.879  -13.350 -37.021 1.00 22.75 ? 470 HOH C O   1 
HETATM 9232 O  O   . HOH BA 5 .   ? 44.832  -13.797 -44.587 1.00 25.30 ? 471 HOH C O   1 
HETATM 9233 O  O   . HOH BA 5 .   ? 45.277  -6.958  -45.606 1.00 22.52 ? 472 HOH C O   1 
HETATM 9234 O  O   . HOH BA 5 .   ? 29.159  6.170   -47.300 1.00 18.91 ? 473 HOH C O   1 
HETATM 9235 O  O   . HOH BA 5 .   ? 38.191  5.120   -45.256 1.00 18.16 ? 474 HOH C O   1 
HETATM 9236 O  O   . HOH BA 5 .   ? 27.421  -10.307 -26.729 1.00 27.43 ? 475 HOH C O   1 
HETATM 9237 O  O   . HOH BA 5 .   ? 22.269  -6.215  -31.529 1.00 22.94 ? 476 HOH C O   1 
HETATM 9238 O  O   . HOH BA 5 .   ? 23.955  13.106  -42.514 1.00 18.40 ? 477 HOH C O   1 
HETATM 9239 O  O   . HOH BA 5 .   ? 46.968  9.092   -27.319 1.00 28.50 ? 478 HOH C O   1 
HETATM 9240 O  O   . HOH BA 5 .   ? 25.602  -2.968  -48.265 1.00 25.37 ? 479 HOH C O   1 
HETATM 9241 O  O   . HOH BA 5 .   ? 28.230  6.907   -43.952 1.00 20.01 ? 480 HOH C O   1 
HETATM 9242 O  O   . HOH BA 5 .   ? 41.215  7.268   -47.020 1.00 24.97 ? 481 HOH C O   1 
HETATM 9243 O  O   . HOH BA 5 .   ? 26.497  -13.470 -34.557 1.00 23.21 ? 482 HOH C O   1 
HETATM 9244 O  O   . HOH BA 5 .   ? 55.710  -7.977  -32.667 1.00 26.92 ? 483 HOH C O   1 
HETATM 9245 O  O   . HOH BA 5 .   ? 22.313  -0.403  -44.156 1.00 23.16 ? 484 HOH C O   1 
HETATM 9246 O  O   . HOH BA 5 .   ? 33.644  13.604  -44.219 1.00 21.58 ? 485 HOH C O   1 
HETATM 9247 O  O   . HOH BA 5 .   ? 38.581  -19.860 -46.210 1.00 39.99 ? 486 HOH C O   1 
HETATM 9248 O  O   . HOH BA 5 .   ? 53.323  6.367   -23.452 1.00 28.54 ? 487 HOH C O   1 
HETATM 9249 O  O   . HOH BA 5 .   ? 31.437  12.810  -46.571 1.00 27.16 ? 488 HOH C O   1 
HETATM 9250 O  O   . HOH BA 5 .   ? 52.907  6.445   -31.519 1.00 21.46 ? 489 HOH C O   1 
HETATM 9251 O  O   . HOH BA 5 .   ? 37.682  -10.352 -33.337 1.00 16.24 ? 490 HOH C O   1 
HETATM 9252 O  O   . HOH BA 5 .   ? 43.700  4.153   -44.489 1.00 22.48 ? 491 HOH C O   1 
HETATM 9253 O  O   . HOH BA 5 .   ? 29.704  -12.438 -23.906 1.00 22.74 ? 492 HOH C O   1 
HETATM 9254 O  O   . HOH BA 5 .   ? 29.725  -11.697 -26.463 1.00 20.38 ? 493 HOH C O   1 
HETATM 9255 O  O   . HOH BA 5 .   ? 58.169  -7.113  -30.899 1.00 30.25 ? 494 HOH C O   1 
HETATM 9256 O  O   . HOH BA 5 .   ? 26.410  3.299   -47.389 1.00 26.01 ? 495 HOH C O   1 
HETATM 9257 O  O   . HOH BA 5 .   ? 20.883  -1.013  -30.088 1.00 21.47 ? 496 HOH C O   1 
HETATM 9258 O  O   . HOH BA 5 .   ? 24.799  -2.114  -23.734 1.00 26.19 ? 497 HOH C O   1 
HETATM 9259 O  O   . HOH BA 5 .   ? 22.531  8.610   -27.897 1.00 20.44 ? 498 HOH C O   1 
HETATM 9260 O  O   . HOH BA 5 .   ? 24.175  -14.414 -47.817 1.00 40.41 ? 499 HOH C O   1 
HETATM 9261 O  O   . HOH BA 5 .   ? 33.168  -1.399  -49.079 1.00 22.87 ? 500 HOH C O   1 
HETATM 9262 O  O   . HOH BA 5 .   ? 48.052  -12.745 -39.412 1.00 27.97 ? 501 HOH C O   1 
HETATM 9263 O  O   . HOH BA 5 .   ? 22.213  -8.804  -39.895 1.00 28.34 ? 502 HOH C O   1 
HETATM 9264 O  O   . HOH BA 5 .   ? 27.582  -12.559 -30.078 1.00 30.88 ? 503 HOH C O   1 
HETATM 9265 O  O   . HOH BA 5 .   ? 22.407  -5.101  -41.193 1.00 26.59 ? 504 HOH C O   1 
HETATM 9266 O  O   . HOH BA 5 .   ? 50.448  -4.511  -16.044 1.00 37.44 ? 505 HOH C O   1 
HETATM 9267 O  O   . HOH BA 5 .   ? 48.143  -10.871 -16.115 1.00 29.65 ? 506 HOH C O   1 
HETATM 9268 O  O   . HOH BA 5 .   ? 35.948  18.037  -38.248 1.00 26.72 ? 507 HOH C O   1 
HETATM 9269 O  O   . HOH BA 5 .   ? 38.541  16.608  -38.989 1.00 28.18 ? 508 HOH C O   1 
HETATM 9270 O  O   . HOH BA 5 .   ? 19.579  -7.646  -17.561 1.00 33.35 ? 509 HOH C O   1 
HETATM 9271 O  O   . HOH BA 5 .   ? 46.949  -16.326 -35.793 1.00 32.78 ? 510 HOH C O   1 
HETATM 9272 O  O   . HOH BA 5 .   ? 26.521  -8.464  -16.014 1.00 29.64 ? 511 HOH C O   1 
HETATM 9273 O  O   . HOH BA 5 .   ? 51.670  10.139  -33.448 1.00 29.34 ? 512 HOH C O   1 
HETATM 9274 O  O   . HOH BA 5 .   ? 26.429  11.484  -45.542 1.00 33.26 ? 513 HOH C O   1 
HETATM 9275 O  O   . HOH BA 5 .   ? 28.139  -10.656 -22.414 1.00 26.08 ? 514 HOH C O   1 
HETATM 9276 O  O   . HOH BA 5 .   ? 39.366  18.115  -41.120 1.00 31.32 ? 515 HOH C O   1 
HETATM 9277 O  O   . HOH BA 5 .   ? 34.083  12.082  -47.865 1.00 27.55 ? 516 HOH C O   1 
HETATM 9278 O  O   . HOH BA 5 .   ? 46.319  -11.183 -40.558 1.00 28.46 ? 517 HOH C O   1 
HETATM 9279 O  O   . HOH BA 5 .   ? 53.695  7.010   -27.882 1.00 28.61 ? 518 HOH C O   1 
HETATM 9280 O  O   . HOH BA 5 .   ? 22.459  0.130   -28.070 1.00 24.25 ? 519 HOH C O   1 
HETATM 9281 O  O   . HOH BA 5 .   ? 54.585  -9.833  -30.986 1.00 34.55 ? 520 HOH C O   1 
HETATM 9282 O  O   . HOH BA 5 .   ? 27.811  16.020  -29.462 1.00 26.46 ? 521 HOH C O   1 
HETATM 9283 O  O   . HOH BA 5 .   ? 39.816  -11.885 -55.202 1.00 27.46 ? 522 HOH C O   1 
HETATM 9284 O  O   . HOH BA 5 .   ? 42.156  -3.952  -48.397 1.00 26.96 ? 523 HOH C O   1 
HETATM 9285 O  O   . HOH BA 5 .   ? 22.910  -11.402 -44.698 1.00 35.36 ? 524 HOH C O   1 
HETATM 9286 O  O   . HOH BA 5 .   ? 26.947  -13.608 -31.977 1.00 34.67 ? 525 HOH C O   1 
HETATM 9287 O  O   . HOH BA 5 .   ? 24.305  -3.657  -44.869 1.00 28.05 ? 526 HOH C O   1 
HETATM 9288 O  O   . HOH BA 5 .   ? 31.530  2.360   -14.530 1.00 24.32 ? 527 HOH C O   1 
HETATM 9289 O  O   . HOH BA 5 .   ? 47.051  7.427   -22.926 1.00 24.37 ? 528 HOH C O   1 
HETATM 9290 O  O   . HOH BA 5 .   ? 48.516  11.360  -24.146 1.00 32.68 ? 529 HOH C O   1 
HETATM 9291 O  O   . HOH BA 5 .   ? 29.207  9.118   -22.524 1.00 30.65 ? 530 HOH C O   1 
HETATM 9292 O  O   . HOH BA 5 .   ? 35.052  -8.116  -11.278 1.00 31.59 ? 531 HOH C O   1 
HETATM 9293 O  O   . HOH BA 5 .   ? 43.757  -12.727 -26.015 1.00 26.76 ? 532 HOH C O   1 
HETATM 9294 O  O   . HOH BA 5 .   ? 30.363  -10.061 -16.556 1.00 30.38 ? 533 HOH C O   1 
HETATM 9295 O  O   . HOH BA 5 .   ? 38.822  13.672  -43.113 1.00 33.47 ? 534 HOH C O   1 
HETATM 9296 O  O   . HOH BA 5 .   ? 38.483  -14.332 -13.502 1.00 37.80 ? 535 HOH C O   1 
HETATM 9297 O  O   . HOH BA 5 .   ? 45.482  -6.031  -48.168 1.00 30.81 ? 536 HOH C O   1 
HETATM 9298 O  O   . HOH BA 5 .   ? 49.791  12.366  -33.021 1.00 32.20 ? 537 HOH C O   1 
HETATM 9299 O  O   . HOH BA 5 .   ? 40.509  -16.415 -30.361 1.00 30.29 ? 538 HOH C O   1 
HETATM 9300 O  O   . HOH BA 5 .   ? 46.498  -3.430  -48.614 1.00 38.46 ? 539 HOH C O   1 
HETATM 9301 O  O   . HOH BA 5 .   ? 46.885  -13.097 -14.802 1.00 43.55 ? 540 HOH C O   1 
HETATM 9302 O  O   . HOH BA 5 .   ? 32.535  0.654   -50.957 1.00 38.37 ? 541 HOH C O   1 
HETATM 9303 O  O   . HOH BA 5 .   ? 29.543  -13.957 -28.171 1.00 31.26 ? 542 HOH C O   1 
HETATM 9304 O  O   . HOH BA 5 .   ? 54.501  9.687   -34.320 1.00 35.72 ? 543 HOH C O   1 
HETATM 9305 O  O   . HOH BA 5 .   ? 33.336  3.998   -10.982 1.00 39.29 ? 544 HOH C O   1 
HETATM 9306 O  O   . HOH BA 5 .   ? 22.778  1.695   -18.976 1.00 32.43 ? 545 HOH C O   1 
HETATM 9307 O  O   . HOH BA 5 .   ? 38.705  12.168  -30.569 1.00 32.86 ? 546 HOH C O   1 
HETATM 9308 O  O   . HOH BA 5 .   ? 40.836  -16.179 -22.401 1.00 31.04 ? 547 HOH C O   1 
HETATM 9309 O  O   . HOH BA 5 .   ? 22.653  -2.713  -50.314 1.00 37.74 ? 548 HOH C O   1 
HETATM 9310 O  O   . HOH BA 5 .   ? 26.804  6.494   -21.186 1.00 32.53 ? 549 HOH C O   1 
HETATM 9311 O  O   . HOH BA 5 .   ? 33.057  16.271  -14.798 1.00 31.68 ? 550 HOH C O   1 
HETATM 9312 O  O   . HOH BA 5 .   ? 38.874  -2.732  -11.491 1.00 31.03 ? 551 HOH C O   1 
HETATM 9313 O  O   . HOH BA 5 .   ? 23.836  -9.013  -29.069 1.00 31.97 ? 552 HOH C O   1 
HETATM 9314 O  O   . HOH BA 5 .   ? 28.634  -7.947  -17.240 1.00 24.21 ? 553 HOH C O   1 
HETATM 9315 O  O   . HOH BA 5 .   ? 46.894  -14.687 -32.239 1.00 32.11 ? 554 HOH C O   1 
HETATM 9316 O  O   . HOH BA 5 .   ? 33.257  9.021   -6.828  1.00 37.04 ? 555 HOH C O   1 
HETATM 9317 O  O   . HOH BA 5 .   ? 29.439  -12.245 -40.912 1.00 40.85 ? 556 HOH C O   1 
HETATM 9318 O  O   . HOH BA 5 .   ? 40.704  -15.604 -25.462 1.00 29.75 ? 557 HOH C O   1 
HETATM 9319 O  O   . HOH BA 5 .   ? 38.697  -2.306  -48.743 1.00 40.70 ? 558 HOH C O   1 
HETATM 9320 O  O   . HOH BA 5 .   ? 24.710  -12.981 -41.552 1.00 29.80 ? 559 HOH C O   1 
HETATM 9321 O  O   . HOH BA 5 .   ? 49.912  -9.184  -46.344 1.00 30.41 ? 560 HOH C O   1 
HETATM 9322 O  O   . HOH BA 5 .   ? 41.682  6.928   -9.933  1.00 31.98 ? 561 HOH C O   1 
HETATM 9323 O  O   . HOH BA 5 .   ? 35.269  6.131   -26.880 1.00 27.40 ? 562 HOH C O   1 
HETATM 9324 O  O   . HOH BA 5 .   ? 25.810  5.470   -24.006 1.00 26.21 ? 563 HOH C O   1 
HETATM 9325 O  O   . HOH BA 5 .   ? 26.100  5.625   -43.447 1.00 23.94 ? 564 HOH C O   1 
HETATM 9326 O  O   . HOH BA 5 .   ? 42.308  16.744  -44.728 1.00 34.80 ? 565 HOH C O   1 
HETATM 9327 O  O   . HOH BA 5 .   ? 32.001  -1.962  -51.913 1.00 34.66 ? 566 HOH C O   1 
HETATM 9328 O  O   . HOH BA 5 .   ? 54.044  5.214   -26.056 1.00 31.40 ? 567 HOH C O   1 
HETATM 9329 O  O   . HOH BA 5 .   ? 26.804  4.088   -50.007 1.00 33.64 ? 568 HOH C O   1 
HETATM 9330 O  O   . HOH BA 5 .   ? 53.327  -10.913 -37.266 1.00 37.35 ? 569 HOH C O   1 
HETATM 9331 O  O   . HOH BA 5 .   ? 26.419  6.703   -14.101 1.00 37.44 ? 570 HOH C O   1 
HETATM 9332 O  O   . HOH BA 5 .   ? 21.924  -3.945  -38.168 1.00 27.42 ? 571 HOH C O   1 
HETATM 9333 O  O   . HOH BA 5 .   ? 45.333  -15.971 -45.664 1.00 33.30 ? 572 HOH C O   1 
HETATM 9334 O  O   . HOH BA 5 .   ? 38.648  -18.766 -16.354 1.00 32.93 ? 573 HOH C O   1 
HETATM 9335 O  O   . HOH BA 5 .   ? 42.327  -10.018 -11.845 1.00 43.10 ? 574 HOH C O   1 
HETATM 9336 O  O   . HOH BA 5 .   ? 42.083  11.098  -26.365 1.00 41.12 ? 575 HOH C O   1 
HETATM 9337 O  O   . HOH BA 5 .   ? 37.679  14.461  -28.825 1.00 33.63 ? 576 HOH C O   1 
HETATM 9338 O  O   . HOH BA 5 .   ? 41.047  14.234  -36.898 1.00 36.39 ? 577 HOH C O   1 
HETATM 9339 O  O   . HOH BA 5 .   ? 40.343  16.883  -36.844 1.00 33.05 ? 578 HOH C O   1 
HETATM 9340 O  O   . HOH BA 5 .   ? 43.638  13.248  -33.987 1.00 44.89 ? 579 HOH C O   1 
HETATM 9341 O  O   . HOH BA 5 .   ? 28.285  15.435  -45.425 1.00 35.36 ? 580 HOH C O   1 
HETATM 9342 O  O   . HOH BA 5 .   ? 30.660  15.629  -44.059 1.00 33.03 ? 581 HOH C O   1 
HETATM 9343 O  O   . HOH BA 5 .   ? 36.124  13.818  -45.771 1.00 35.36 ? 582 HOH C O   1 
HETATM 9344 O  O   . HOH BA 5 .   ? 58.831  -7.531  -34.501 1.00 32.98 ? 583 HOH C O   1 
HETATM 9345 O  O   . HOH BA 5 .   ? 52.637  8.732   -24.039 1.00 31.53 ? 584 HOH C O   1 
HETATM 9346 O  O   . HOH BA 5 .   ? 35.450  19.430  -35.966 1.00 38.83 ? 585 HOH C O   1 
HETATM 9347 O  O   . HOH BA 5 .   ? 39.840  13.695  -12.608 1.00 31.90 ? 586 HOH C O   1 
HETATM 9348 O  O   . HOH BA 5 .   ? 48.240  17.711  -36.747 1.00 37.93 ? 587 HOH C O   1 
HETATM 9349 O  O   . HOH CA 5 .   ? 17.500  -6.526  -56.258 1.00 31.95 ? 401 HOH D O   1 
HETATM 9350 O  O   . HOH CA 5 .   ? 12.462  19.897  -29.475 1.00 31.70 ? 402 HOH D O   1 
HETATM 9351 O  O   . HOH CA 5 .   ? -6.204  5.404   -56.380 1.00 35.78 ? 403 HOH D O   1 
HETATM 9352 O  O   . HOH CA 5 .   ? 8.315   -14.754 -37.786 1.00 35.11 ? 404 HOH D O   1 
HETATM 9353 O  O   . HOH CA 5 .   ? 11.955  -6.856  -52.215 1.00 21.61 ? 405 HOH D O   1 
HETATM 9354 O  O   . HOH CA 5 .   ? -15.358 -2.188  -43.758 1.00 26.53 ? 406 HOH D O   1 
HETATM 9355 O  O   . HOH CA 5 .   ? -6.068  13.636  -37.472 1.00 23.98 ? 407 HOH D O   1 
HETATM 9356 O  O   . HOH CA 5 .   ? 20.021  21.701  -32.955 1.00 28.95 ? 408 HOH D O   1 
HETATM 9357 O  O   . HOH CA 5 .   ? 10.951  13.921  -61.471 1.00 32.94 ? 409 HOH D O   1 
HETATM 9358 O  O   . HOH CA 5 .   ? -1.530  13.255  -38.743 1.00 29.66 ? 410 HOH D O   1 
HETATM 9359 O  O   . HOH CA 5 .   ? -8.231  13.569  -44.387 1.00 26.37 ? 411 HOH D O   1 
HETATM 9360 O  O   . HOH CA 5 .   ? 20.975  18.532  -42.664 1.00 31.18 ? 412 HOH D O   1 
HETATM 9361 O  O   . HOH CA 5 .   ? 6.571   -13.938 -51.035 1.00 13.30 ? 413 HOH D O   1 
HETATM 9362 O  O   . HOH CA 5 .   ? -18.767 5.307   -40.647 1.00 34.97 ? 414 HOH D O   1 
HETATM 9363 O  O   . HOH CA 5 .   ? -5.460  19.648  -21.779 1.00 33.97 ? 415 HOH D O   1 
HETATM 9364 O  O   . HOH CA 5 .   ? -8.188  11.863  -37.067 1.00 21.81 ? 416 HOH D O   1 
HETATM 9365 O  O   . HOH CA 5 .   ? 19.370  18.883  -40.193 1.00 26.01 ? 417 HOH D O   1 
HETATM 9366 O  O   . HOH CA 5 .   ? -10.080 -0.363  -49.609 1.00 21.73 ? 418 HOH D O   1 
HETATM 9367 O  O   . HOH CA 5 .   ? -3.346  -14.605 -49.675 1.00 30.63 ? 419 HOH D O   1 
HETATM 9368 O  O   . HOH CA 5 .   ? -2.208  13.178  -41.554 1.00 28.80 ? 420 HOH D O   1 
HETATM 9369 O  O   . HOH CA 5 .   ? -12.896 8.532   -55.529 1.00 32.88 ? 421 HOH D O   1 
HETATM 9370 O  O   . HOH CA 5 .   ? -6.827  0.201   -56.249 1.00 28.10 ? 422 HOH D O   1 
HETATM 9371 O  O   . HOH CA 5 .   ? 11.042  3.733   -55.299 1.00 17.88 ? 423 HOH D O   1 
HETATM 9372 O  O   . HOH CA 5 .   ? -3.949  24.173  -30.863 1.00 40.28 ? 424 HOH D O   1 
HETATM 9373 O  O   . HOH CA 5 .   ? 14.029  5.889   -60.598 1.00 32.19 ? 425 HOH D O   1 
HETATM 9374 O  O   . HOH CA 5 .   ? 8.832   -10.150 -58.211 1.00 24.96 ? 426 HOH D O   1 
HETATM 9375 O  O   . HOH CA 5 .   ? 7.798   9.191   -24.473 1.00 20.80 ? 427 HOH D O   1 
HETATM 9376 O  O   . HOH CA 5 .   ? 5.785   21.413  -25.665 1.00 22.15 ? 428 HOH D O   1 
HETATM 9377 O  O   . HOH CA 5 .   ? 9.616   -13.435 -55.830 1.00 36.40 ? 429 HOH D O   1 
HETATM 9378 O  O   . HOH CA 5 .   ? 23.777  18.448  -42.840 1.00 20.49 ? 430 HOH D O   1 
HETATM 9379 O  O   . HOH CA 5 .   ? -0.177  0.281   -57.011 1.00 33.25 ? 431 HOH D O   1 
HETATM 9380 O  O   . HOH CA 5 .   ? -17.252 -4.132  -36.858 1.00 34.93 ? 432 HOH D O   1 
HETATM 9381 O  O   . HOH CA 5 .   ? -2.025  -3.976  -55.981 1.00 37.24 ? 433 HOH D O   1 
HETATM 9382 O  O   . HOH CA 5 .   ? 8.056   -16.566 -45.202 1.00 28.22 ? 434 HOH D O   1 
HETATM 9383 O  O   . HOH CA 5 .   ? 18.811  -13.209 -33.079 1.00 29.83 ? 435 HOH D O   1 
HETATM 9384 O  O   . HOH CA 5 .   ? -18.097 -1.582  -45.287 1.00 35.61 ? 436 HOH D O   1 
HETATM 9385 O  O   . HOH CA 5 .   ? -16.638 3.684   -51.957 1.00 37.17 ? 437 HOH D O   1 
HETATM 9386 O  O   . HOH CA 5 .   ? 26.342  16.182  -43.605 1.00 29.73 ? 438 HOH D O   1 
HETATM 9387 O  O   . HOH CA 5 .   ? 8.399   17.595  -27.630 1.00 26.59 ? 439 HOH D O   1 
HETATM 9388 O  O   . HOH CA 5 .   ? -16.168 4.421   -41.189 1.00 23.03 ? 440 HOH D O   1 
HETATM 9389 O  O   . HOH CA 5 .   ? 8.548   21.623  -29.692 1.00 21.44 ? 441 HOH D O   1 
HETATM 9390 O  O   . HOH CA 5 .   ? -9.293  11.139  -45.086 1.00 20.21 ? 442 HOH D O   1 
HETATM 9391 O  O   . HOH CA 5 .   ? -9.537  0.561   -54.842 1.00 30.13 ? 443 HOH D O   1 
HETATM 9392 O  O   . HOH CA 5 .   ? -15.146 -0.550  -35.801 1.00 29.30 ? 444 HOH D O   1 
HETATM 9393 O  O   . HOH CA 5 .   ? -11.644 12.837  -38.211 1.00 28.63 ? 445 HOH D O   1 
HETATM 9394 O  O   . HOH CA 5 .   ? 13.477  1.199   -55.842 1.00 24.24 ? 446 HOH D O   1 
HETATM 9395 O  O   . HOH CA 5 .   ? 11.219  -10.732 -43.796 1.00 24.23 ? 447 HOH D O   1 
HETATM 9396 O  O   . HOH CA 5 .   ? 11.399  22.084  -61.961 1.00 36.53 ? 448 HOH D O   1 
HETATM 9397 O  O   . HOH CA 5 .   ? -8.431  8.640   -55.959 1.00 32.11 ? 449 HOH D O   1 
HETATM 9398 O  O   . HOH CA 5 .   ? 17.105  18.858  -43.224 1.00 47.50 ? 450 HOH D O   1 
HETATM 9399 O  O   . HOH CA 5 .   ? 18.275  23.232  -34.225 1.00 24.26 ? 451 HOH D O   1 
HETATM 9400 O  O   . HOH CA 5 .   ? 13.627  16.511  -26.559 1.00 26.65 ? 452 HOH D O   1 
HETATM 9401 O  O   . HOH CA 5 .   ? 21.296  -1.501  -57.559 1.00 39.97 ? 453 HOH D O   1 
HETATM 9402 O  O   . HOH CA 5 .   ? 3.934   24.191  -28.425 1.00 36.70 ? 454 HOH D O   1 
HETATM 9403 O  O   . HOH CA 5 .   ? 14.604  19.682  -27.964 1.00 34.87 ? 455 HOH D O   1 
HETATM 9404 O  O   . HOH CA 5 .   ? 16.243  24.312  -34.241 1.00 28.86 ? 456 HOH D O   1 
HETATM 9405 O  O   . HOH CA 5 .   ? 7.911   -12.455 -59.467 1.00 37.99 ? 457 HOH D O   1 
HETATM 9406 O  O   . HOH CA 5 .   ? -14.102 12.409  -49.618 1.00 36.37 ? 458 HOH D O   1 
HETATM 9407 O  O   . HOH CA 5 .   ? 14.513  -11.450 -47.611 1.00 30.98 ? 459 HOH D O   1 
HETATM 9408 O  O   . HOH CA 5 .   ? -0.795  23.158  -34.514 1.00 40.54 ? 460 HOH D O   1 
HETATM 9409 O  O   . HOH CA 5 .   ? 12.142  -12.455 -56.599 1.00 30.11 ? 461 HOH D O   1 
HETATM 9410 O  O   . HOH CA 5 .   ? 6.984   -4.189  -58.495 1.00 26.77 ? 462 HOH D O   1 
HETATM 9411 O  O   . HOH CA 5 .   ? 5.061   22.090  -51.926 1.00 36.57 ? 463 HOH D O   1 
HETATM 9412 O  O   . HOH CA 5 .   ? 4.934   9.362   -23.864 1.00 29.59 ? 464 HOH D O   1 
HETATM 9413 O  O   . HOH CA 5 .   ? -16.337 10.231  -54.999 1.00 30.95 ? 465 HOH D O   1 
HETATM 9414 O  O   . HOH CA 5 .   ? -1.125  15.970  -37.811 1.00 38.47 ? 466 HOH D O   1 
HETATM 9415 O  O   . HOH CA 5 .   ? 3.149   -6.749  -58.147 1.00 24.86 ? 467 HOH D O   1 
HETATM 9416 O  O   . HOH CA 5 .   ? 19.850  -11.047 -27.400 1.00 31.42 ? 468 HOH D O   1 
HETATM 9417 O  O   . HOH CA 5 .   ? 5.377   -15.621 -36.472 1.00 38.62 ? 469 HOH D O   1 
HETATM 9418 O  O   . HOH CA 5 .   ? 14.539  -12.542 -54.883 1.00 30.06 ? 470 HOH D O   1 
HETATM 9419 O  O   . HOH CA 5 .   ? 7.010   -8.548  -59.128 1.00 23.42 ? 471 HOH D O   1 
HETATM 9420 O  O   . HOH CA 5 .   ? -16.174 -4.354  -48.351 1.00 46.34 ? 472 HOH D O   1 
HETATM 9421 O  O   . HOH CA 5 .   ? 19.807  1.261   -51.731 1.00 37.43 ? 473 HOH D O   1 
HETATM 9422 O  O   . HOH CA 5 .   ? -9.212  -5.037  -22.654 1.00 34.45 ? 474 HOH D O   1 
HETATM 9423 O  O   . HOH CA 5 .   ? 21.255  6.769   -29.732 1.00 13.23 ? 475 HOH D O   1 
HETATM 9424 O  O   . HOH CA 5 .   ? 18.966  10.098  -35.816 1.00 11.39 ? 476 HOH D O   1 
HETATM 9425 O  O   . HOH CA 5 .   ? 25.750  13.089  -35.470 1.00 12.97 ? 477 HOH D O   1 
HETATM 9426 O  O   . HOH CA 5 .   ? 9.178   8.268   -42.975 1.00 13.69 ? 478 HOH D O   1 
HETATM 9427 O  O   . HOH CA 5 .   ? 13.312  18.595  -32.613 1.00 13.55 ? 479 HOH D O   1 
HETATM 9428 O  O   . HOH CA 5 .   ? 12.085  6.924   -39.505 1.00 10.57 ? 480 HOH D O   1 
HETATM 9429 O  O   . HOH CA 5 .   ? 0.374   -12.733 -37.008 1.00 18.13 ? 481 HOH D O   1 
HETATM 9430 O  O   . HOH CA 5 .   ? 16.368  0.274   -37.479 1.00 9.86  ? 482 HOH D O   1 
HETATM 9431 O  O   . HOH CA 5 .   ? 0.937   2.566   -28.321 1.00 12.90 ? 483 HOH D O   1 
HETATM 9432 O  O   . HOH CA 5 .   ? 11.833  -3.664  -47.341 1.00 14.22 ? 484 HOH D O   1 
HETATM 9433 O  O   . HOH CA 5 .   ? -7.264  -6.915  -51.608 1.00 22.50 ? 485 HOH D O   1 
HETATM 9434 O  O   . HOH CA 5 .   ? 5.802   -6.424  -57.622 1.00 16.98 ? 486 HOH D O   1 
HETATM 9435 O  O   . HOH CA 5 .   ? 20.110  7.445   -35.790 1.00 13.28 ? 487 HOH D O   1 
HETATM 9436 O  O   . HOH CA 5 .   ? 8.672   -10.675 -31.216 1.00 19.44 ? 488 HOH D O   1 
HETATM 9437 O  O   . HOH CA 5 .   ? 4.220   -6.929  -34.907 1.00 11.61 ? 489 HOH D O   1 
HETATM 9438 O  O   . HOH CA 5 .   ? 1.132   -9.888  -31.332 1.00 13.68 ? 490 HOH D O   1 
HETATM 9439 O  O   . HOH CA 5 .   ? 18.353  -0.150  -29.450 1.00 15.00 ? 491 HOH D O   1 
HETATM 9440 O  O   . HOH CA 5 .   ? -12.834 -1.748  -34.343 1.00 22.13 ? 492 HOH D O   1 
HETATM 9441 O  O   . HOH CA 5 .   ? 2.485   9.398   -24.808 1.00 19.73 ? 493 HOH D O   1 
HETATM 9442 O  O   . HOH CA 5 .   ? 1.019   9.475   -59.162 1.00 26.61 ? 494 HOH D O   1 
HETATM 9443 O  O   . HOH CA 5 .   ? 20.659  14.002  -48.010 1.00 23.08 ? 495 HOH D O   1 
HETATM 9444 O  O   . HOH CA 5 .   ? 19.015  16.569  -41.826 1.00 26.54 ? 496 HOH D O   1 
HETATM 9445 O  O   . HOH CA 5 .   ? 14.244  13.940  -27.426 1.00 17.32 ? 497 HOH D O   1 
HETATM 9446 O  O   . HOH CA 5 .   ? -0.140  -12.192 -42.369 1.00 18.74 ? 498 HOH D O   1 
HETATM 9447 O  O   . HOH CA 5 .   ? 19.929  8.131   -42.447 1.00 13.91 ? 499 HOH D O   1 
HETATM 9448 O  O   . HOH CA 5 .   ? 22.839  6.460   -38.267 1.00 11.90 ? 500 HOH D O   1 
HETATM 9449 O  O   . HOH CA 5 .   ? 1.003   -4.975  -54.458 1.00 25.20 ? 501 HOH D O   1 
HETATM 9450 O  O   . HOH CA 5 .   ? 10.929  13.522  -58.642 1.00 22.40 ? 502 HOH D O   1 
HETATM 9451 O  O   . HOH CA 5 .   ? -2.564  -8.775  -41.852 1.00 17.69 ? 503 HOH D O   1 
HETATM 9452 O  O   . HOH CA 5 .   ? -2.280  -7.783  -22.613 1.00 21.31 ? 504 HOH D O   1 
HETATM 9453 O  O   . HOH CA 5 .   ? 19.112  8.462   -29.323 1.00 14.60 ? 505 HOH D O   1 
HETATM 9454 O  O   . HOH CA 5 .   ? -3.492  -5.584  -26.850 1.00 19.40 ? 506 HOH D O   1 
HETATM 9455 O  O   . HOH CA 5 .   ? 21.304  5.162   -34.272 1.00 10.86 ? 507 HOH D O   1 
HETATM 9456 O  O   . HOH CA 5 .   ? 17.853  7.465   -27.193 1.00 22.01 ? 508 HOH D O   1 
HETATM 9457 O  O   . HOH CA 5 .   ? 19.007  -0.275  -36.857 1.00 15.31 ? 509 HOH D O   1 
HETATM 9458 O  O   . HOH CA 5 .   ? 4.658   16.044  -57.048 1.00 19.15 ? 510 HOH D O   1 
HETATM 9459 O  O   . HOH CA 5 .   ? 19.692  11.162  -29.186 1.00 16.98 ? 511 HOH D O   1 
HETATM 9460 O  O   . HOH CA 5 .   ? 23.853  9.043   -35.043 1.00 15.80 ? 512 HOH D O   1 
HETATM 9461 O  O   . HOH CA 5 .   ? -5.774  -6.917  -27.852 1.00 20.44 ? 513 HOH D O   1 
HETATM 9462 O  O   . HOH CA 5 .   ? 0.586   -8.227  -19.020 1.00 22.66 ? 514 HOH D O   1 
HETATM 9463 O  O   . HOH CA 5 .   ? -3.021  -10.506 -39.549 1.00 24.68 ? 515 HOH D O   1 
HETATM 9464 O  O   . HOH CA 5 .   ? 18.518  -7.630  -40.238 1.00 20.84 ? 516 HOH D O   1 
HETATM 9465 O  O   . HOH CA 5 .   ? 19.286  -3.778  -34.418 1.00 25.21 ? 517 HOH D O   1 
HETATM 9466 O  O   . HOH CA 5 .   ? -2.915  11.202  -46.141 1.00 20.93 ? 518 HOH D O   1 
HETATM 9467 O  O   . HOH CA 5 .   ? -0.295  -12.768 -45.480 1.00 16.97 ? 519 HOH D O   1 
HETATM 9468 O  O   . HOH CA 5 .   ? -6.953  11.143  -19.572 1.00 17.99 ? 520 HOH D O   1 
HETATM 9469 O  O   . HOH CA 5 .   ? -10.574 11.711  -26.151 1.00 27.03 ? 521 HOH D O   1 
HETATM 9470 O  O   . HOH CA 5 .   ? -8.508  -0.193  -51.890 1.00 19.01 ? 522 HOH D O   1 
HETATM 9471 O  O   . HOH CA 5 .   ? -2.016  -8.876  -16.910 1.00 23.61 ? 523 HOH D O   1 
HETATM 9472 O  O   . HOH CA 5 .   ? 12.597  -9.791  -46.219 1.00 19.65 ? 524 HOH D O   1 
HETATM 9473 O  O   . HOH CA 5 .   ? 8.927   3.405   -53.048 1.00 13.25 ? 525 HOH D O   1 
HETATM 9474 O  O   . HOH CA 5 .   ? -12.760 -4.247  -47.683 1.00 29.09 ? 526 HOH D O   1 
HETATM 9475 O  O   . HOH CA 5 .   ? 20.472  -7.498  -29.901 1.00 19.33 ? 527 HOH D O   1 
HETATM 9476 O  O   . HOH CA 5 .   ? -5.934  -9.884  -41.896 1.00 31.40 ? 528 HOH D O   1 
HETATM 9477 O  O   . HOH CA 5 .   ? -5.013  -11.227 -28.342 1.00 23.61 ? 529 HOH D O   1 
HETATM 9478 O  O   . HOH CA 5 .   ? -6.569  -9.143  -53.127 1.00 29.20 ? 530 HOH D O   1 
HETATM 9479 O  O   . HOH CA 5 .   ? -14.473 4.826   -37.403 1.00 25.40 ? 531 HOH D O   1 
HETATM 9480 O  O   . HOH CA 5 .   ? -15.997 9.738   -47.516 1.00 26.45 ? 532 HOH D O   1 
HETATM 9481 O  O   . HOH CA 5 .   ? -12.434 -3.790  -36.390 1.00 26.30 ? 533 HOH D O   1 
HETATM 9482 O  O   . HOH CA 5 .   ? 23.478  10.383  -41.602 1.00 20.04 ? 534 HOH D O   1 
HETATM 9483 O  O   . HOH CA 5 .   ? 15.621  9.712   -48.121 1.00 23.15 ? 535 HOH D O   1 
HETATM 9484 O  O   . HOH CA 5 .   ? 18.411  5.219   -45.941 1.00 17.79 ? 536 HOH D O   1 
HETATM 9485 O  O   . HOH CA 5 .   ? 14.058  19.726  -43.022 1.00 37.60 ? 537 HOH D O   1 
HETATM 9486 O  O   . HOH CA 5 .   ? -1.250  -12.430 -39.286 1.00 27.52 ? 538 HOH D O   1 
HETATM 9487 O  O   . HOH CA 5 .   ? 12.612  -2.799  -12.665 1.00 40.56 ? 539 HOH D O   1 
HETATM 9488 O  O   . HOH CA 5 .   ? 10.174  2.497   -21.534 1.00 23.00 ? 540 HOH D O   1 
HETATM 9489 O  O   . HOH CA 5 .   ? -0.271  -10.324 -18.215 1.00 31.88 ? 541 HOH D O   1 
HETATM 9490 O  O   . HOH CA 5 .   ? 9.997   -12.110 -33.174 1.00 30.80 ? 542 HOH D O   1 
HETATM 9491 O  O   . HOH CA 5 .   ? 17.314  -11.366 -27.434 1.00 22.15 ? 543 HOH D O   1 
HETATM 9492 O  O   . HOH CA 5 .   ? 10.472  -10.634 -17.124 1.00 29.66 ? 544 HOH D O   1 
HETATM 9493 O  O   . HOH CA 5 .   ? -6.875  -9.231  -26.797 1.00 33.53 ? 545 HOH D O   1 
HETATM 9494 O  O   . HOH CA 5 .   ? 11.329  17.751  -54.697 1.00 26.36 ? 546 HOH D O   1 
HETATM 9495 O  O   . HOH CA 5 .   ? 13.746  7.517   -48.196 1.00 24.35 ? 547 HOH D O   1 
HETATM 9496 O  O   . HOH CA 5 .   ? -5.646  -9.687  -34.694 1.00 29.15 ? 548 HOH D O   1 
HETATM 9497 O  O   . HOH CA 5 .   ? 18.756  -4.373  -18.322 1.00 34.04 ? 549 HOH D O   1 
HETATM 9498 O  O   . HOH CA 5 .   ? 20.541  -2.097  -50.828 1.00 42.81 ? 550 HOH D O   1 
HETATM 9499 O  O   . HOH CA 5 .   ? 5.775   18.686  -33.264 1.00 29.81 ? 551 HOH D O   1 
HETATM 9500 O  O   . HOH CA 5 .   ? -12.242 -4.813  -44.697 1.00 27.24 ? 552 HOH D O   1 
HETATM 9501 O  O   . HOH CA 5 .   ? 17.115  6.665   -48.950 1.00 26.04 ? 553 HOH D O   1 
HETATM 9502 O  O   . HOH CA 5 .   ? -11.960 11.930  -30.990 1.00 44.05 ? 554 HOH D O   1 
HETATM 9503 O  O   . HOH CA 5 .   ? 19.093  4.775   -49.314 1.00 28.31 ? 555 HOH D O   1 
HETATM 9504 O  O   . HOH CA 5 .   ? -6.175  4.404   -24.476 1.00 27.27 ? 556 HOH D O   1 
HETATM 9505 O  O   . HOH CA 5 .   ? 2.102   -15.288 -29.738 1.00 27.51 ? 557 HOH D O   1 
HETATM 9506 O  O   . HOH CA 5 .   ? 0.671   -11.867 -13.711 1.00 36.25 ? 558 HOH D O   1 
HETATM 9507 O  O   . HOH CA 5 .   ? 23.646  8.214   -45.291 1.00 34.66 ? 559 HOH D O   1 
HETATM 9508 O  O   . HOH CA 5 .   ? -2.694  -0.574  -16.757 1.00 28.34 ? 560 HOH D O   1 
HETATM 9509 O  O   . HOH CA 5 .   ? -5.635  -5.763  -53.965 1.00 32.74 ? 561 HOH D O   1 
HETATM 9510 O  O   . HOH CA 5 .   ? 12.078  1.963   -18.104 1.00 22.92 ? 562 HOH D O   1 
HETATM 9511 O  O   . HOH CA 5 .   ? 8.431   -9.233  -14.188 1.00 33.27 ? 563 HOH D O   1 
HETATM 9512 O  O   . HOH CA 5 .   ? -5.453  -13.598 -32.591 1.00 28.78 ? 564 HOH D O   1 
HETATM 9513 O  O   . HOH CA 5 .   ? 8.982   20.022  -31.976 1.00 24.21 ? 565 HOH D O   1 
HETATM 9514 O  O   . HOH CA 5 .   ? 16.043  15.142  -24.099 1.00 33.07 ? 566 HOH D O   1 
HETATM 9515 O  O   . HOH CA 5 .   ? 27.723  13.135  -47.223 1.00 38.56 ? 567 HOH D O   1 
HETATM 9516 O  O   . HOH CA 5 .   ? 11.716  20.828  -32.676 1.00 25.03 ? 568 HOH D O   1 
HETATM 9517 O  O   . HOH CA 5 .   ? -5.822  -10.977 -31.101 1.00 31.65 ? 569 HOH D O   1 
HETATM 9518 O  O   . HOH CA 5 .   ? -2.949  -12.484 -45.537 1.00 29.36 ? 570 HOH D O   1 
HETATM 9519 O  O   . HOH CA 5 .   ? 18.701  -3.478  -43.115 1.00 25.73 ? 571 HOH D O   1 
HETATM 9520 O  O   . HOH CA 5 .   ? 22.235  -7.288  -27.606 1.00 26.39 ? 572 HOH D O   1 
HETATM 9521 O  O   . HOH CA 5 .   ? -15.315 7.140   -41.018 1.00 28.74 ? 573 HOH D O   1 
HETATM 9522 O  O   . HOH CA 5 .   ? 14.529  -11.982 -34.395 1.00 31.40 ? 574 HOH D O   1 
HETATM 9523 O  O   . HOH CA 5 .   ? 22.743  13.819  -28.736 1.00 24.17 ? 575 HOH D O   1 
HETATM 9524 O  O   . HOH CA 5 .   ? 0.821   13.003  -39.949 1.00 25.08 ? 576 HOH D O   1 
HETATM 9525 O  O   . HOH CA 5 .   ? 3.153   -13.763 -39.622 1.00 26.80 ? 577 HOH D O   1 
HETATM 9526 O  O   . HOH CA 5 .   ? 5.650   -0.186  -57.799 1.00 25.02 ? 578 HOH D O   1 
HETATM 9527 O  O   . HOH CA 5 .   ? 19.007  11.529  -50.299 1.00 34.72 ? 579 HOH D O   1 
HETATM 9528 O  O   . HOH CA 5 .   ? 5.122   -0.866  -14.425 1.00 40.39 ? 580 HOH D O   1 
HETATM 9529 O  O   . HOH CA 5 .   ? -2.504  14.041  -56.551 1.00 30.41 ? 581 HOH D O   1 
HETATM 9530 O  O   . HOH CA 5 .   ? 5.049   -2.442  -59.064 1.00 25.44 ? 582 HOH D O   1 
HETATM 9531 O  O   . HOH CA 5 .   ? 16.742  7.341   -56.522 1.00 32.54 ? 583 HOH D O   1 
HETATM 9532 O  O   . HOH CA 5 .   ? 18.343  0.008   -20.543 1.00 25.35 ? 584 HOH D O   1 
HETATM 9533 O  O   . HOH CA 5 .   ? -2.667  -14.737 -39.440 1.00 33.05 ? 585 HOH D O   1 
HETATM 9534 O  O   . HOH CA 5 .   ? 21.688  1.133   -25.435 1.00 31.97 ? 586 HOH D O   1 
HETATM 9535 O  O   . HOH CA 5 .   ? 11.806  8.883   -47.257 1.00 24.14 ? 587 HOH D O   1 
HETATM 9536 O  O   . HOH CA 5 .   ? 20.404  3.977   -46.999 1.00 28.61 ? 588 HOH D O   1 
HETATM 9537 O  O   . HOH CA 5 .   ? 20.664  -3.934  -28.648 1.00 28.89 ? 589 HOH D O   1 
HETATM 9538 O  O   . HOH CA 5 .   ? -3.288  -9.791  -21.322 1.00 28.02 ? 590 HOH D O   1 
HETATM 9539 O  O   . HOH CA 5 .   ? 22.521  7.747   -42.573 1.00 21.39 ? 591 HOH D O   1 
HETATM 9540 O  O   . HOH CA 5 .   ? 21.009  2.306   -21.248 1.00 34.38 ? 592 HOH D O   1 
HETATM 9541 O  O   . HOH CA 5 .   ? 20.219  1.331   -45.407 1.00 31.22 ? 593 HOH D O   1 
HETATM 9542 O  O   . HOH CA 5 .   ? -11.591 -7.747  -37.037 1.00 38.18 ? 594 HOH D O   1 
HETATM 9543 O  O   . HOH CA 5 .   ? 20.918  9.425   -25.850 1.00 30.14 ? 595 HOH D O   1 
HETATM 9544 O  O   . HOH CA 5 .   ? -6.686  -8.656  -18.332 1.00 26.48 ? 596 HOH D O   1 
HETATM 9545 O  O   . HOH CA 5 .   ? -3.941  -8.716  -18.653 1.00 26.02 ? 597 HOH D O   1 
HETATM 9546 O  O   . HOH CA 5 .   ? 7.351   20.506  -33.776 1.00 34.34 ? 598 HOH D O   1 
HETATM 9547 O  O   . HOH CA 5 .   ? -9.234  -9.010  -37.615 1.00 41.30 ? 599 HOH D O   1 
HETATM 9548 O  O   . HOH CA 5 .   ? 4.202   18.629  -50.578 1.00 38.02 ? 600 HOH D O   1 
HETATM 9549 O  O   . HOH CA 5 .   ? -14.497 10.533  -37.083 1.00 32.92 ? 601 HOH D O   1 
HETATM 9550 O  O   . HOH CA 5 .   ? -9.835  8.526   -20.597 1.00 32.06 ? 602 HOH D O   1 
HETATM 9551 O  O   . HOH CA 5 .   ? -14.392 9.578   -44.903 1.00 28.99 ? 603 HOH D O   1 
HETATM 9552 O  O   . HOH CA 5 .   ? 2.304   1.744   -20.485 1.00 32.35 ? 604 HOH D O   1 
HETATM 9553 O  O   . HOH CA 5 .   ? 13.599  -11.277 -38.558 1.00 46.31 ? 605 HOH D O   1 
HETATM 9554 O  O   . HOH CA 5 .   ? 20.509  0.528   -56.580 1.00 39.59 ? 606 HOH D O   1 
HETATM 9555 O  O   . HOH CA 5 .   ? 11.026  14.883  -48.912 1.00 29.43 ? 607 HOH D O   1 
HETATM 9556 O  O   . HOH CA 5 .   ? 7.495   -4.831  -14.572 1.00 30.13 ? 608 HOH D O   1 
HETATM 9557 O  O   . HOH CA 5 .   ? 16.407  19.605  -57.488 1.00 34.03 ? 609 HOH D O   1 
HETATM 9558 O  O   . HOH CA 5 .   ? 10.078  -10.917 -20.655 1.00 35.86 ? 610 HOH D O   1 
HETATM 9559 O  O   . HOH CA 5 .   ? 1.760   -7.476  -55.818 1.00 25.65 ? 611 HOH D O   1 
HETATM 9560 O  O   . HOH CA 5 .   ? 7.679   12.254  -41.148 1.00 20.73 ? 612 HOH D O   1 
HETATM 9561 O  O   . HOH CA 5 .   ? 22.504  -1.604  -39.943 1.00 23.29 ? 613 HOH D O   1 
HETATM 9562 O  O   . HOH CA 5 .   ? 13.890  -11.185 -20.998 1.00 39.44 ? 614 HOH D O   1 
HETATM 9563 O  O   . HOH CA 5 .   ? 20.763  -0.832  -41.929 1.00 32.72 ? 615 HOH D O   1 
HETATM 9564 O  O   . HOH CA 5 .   ? -8.575  19.305  -26.099 1.00 34.99 ? 616 HOH D O   1 
HETATM 9565 O  O   . HOH CA 5 .   ? -10.575 -4.690  -29.855 1.00 29.71 ? 617 HOH D O   1 
HETATM 9566 O  O   . HOH CA 5 .   ? -11.644 11.364  -46.121 1.00 30.16 ? 618 HOH D O   1 
HETATM 9567 O  O   . HOH CA 5 .   ? 22.234  3.486   -23.524 1.00 26.03 ? 619 HOH D O   1 
HETATM 9568 O  O   . HOH CA 5 .   ? -6.584  -2.556  -21.284 1.00 28.16 ? 620 HOH D O   1 
HETATM 9569 O  O   . HOH CA 5 .   ? -12.593 -7.735  -41.351 1.00 30.43 ? 621 HOH D O   1 
HETATM 9570 O  O   . HOH CA 5 .   ? 13.846  -10.785 -27.683 1.00 42.76 ? 622 HOH D O   1 
HETATM 9571 O  O   . HOH CA 5 .   ? 2.810   14.044  -43.166 1.00 25.28 ? 623 HOH D O   1 
HETATM 9572 O  O   . HOH CA 5 .   ? 12.718  11.472  -46.268 1.00 32.55 ? 624 HOH D O   1 
HETATM 9573 O  O   . HOH CA 5 .   ? 14.147  2.849   -16.622 1.00 35.82 ? 625 HOH D O   1 
HETATM 9574 O  O   . HOH CA 5 .   ? -10.078 15.222  -20.850 1.00 30.80 ? 626 HOH D O   1 
HETATM 9575 O  O   . HOH CA 5 .   ? 19.703  -5.754  -41.964 1.00 24.95 ? 627 HOH D O   1 
HETATM 9576 O  O   . HOH CA 5 .   ? 10.499  3.935   -19.262 1.00 28.24 ? 628 HOH D O   1 
HETATM 9577 O  O   . HOH CA 5 .   ? 5.595   18.826  -59.213 1.00 32.29 ? 629 HOH D O   1 
HETATM 9578 O  O   . HOH CA 5 .   ? 20.988  -3.844  -32.229 1.00 30.23 ? 630 HOH D O   1 
HETATM 9579 O  O   . HOH CA 5 .   ? 1.496   7.508   -22.532 1.00 42.49 ? 631 HOH D O   1 
HETATM 9580 O  O   . HOH CA 5 .   ? 2.182   15.389  -40.106 1.00 35.67 ? 632 HOH D O   1 
HETATM 9581 O  O   . HOH CA 5 .   ? -9.559  15.713  -30.071 1.00 35.79 ? 633 HOH D O   1 
HETATM 9582 O  O   . HOH CA 5 .   ? 1.037   -14.745 -41.753 1.00 30.93 ? 634 HOH D O   1 
HETATM 9583 O  O   . HOH CA 5 .   ? 11.378  6.033   -19.856 1.00 33.88 ? 635 HOH D O   1 
HETATM 9584 O  O   . HOH CA 5 .   ? 6.587   14.315  -41.485 1.00 37.03 ? 636 HOH D O   1 
HETATM 9585 O  O   . HOH CA 5 .   ? 3.771   12.930  -40.878 1.00 30.53 ? 637 HOH D O   1 
HETATM 9586 O  O   . HOH CA 5 .   ? 9.045   17.194  -41.708 1.00 35.15 ? 638 HOH D O   1 
HETATM 9587 O  O   . HOH CA 5 .   ? 1.143   16.836  -37.678 1.00 32.56 ? 639 HOH D O   1 
HETATM 9588 O  O   . HOH CA 5 .   ? 7.526   15.226  -39.533 1.00 38.86 ? 640 HOH D O   1 
HETATM 9589 O  O   . HOH CA 5 .   ? -4.032  10.015  -17.408 1.00 25.18 ? 641 HOH D O   1 
HETATM 9590 O  O   . HOH CA 5 .   ? 21.426  -9.674  -26.106 1.00 32.66 ? 642 HOH D O   1 
HETATM 9591 O  O   . HOH CA 5 .   ? 0.408   19.451  -21.763 1.00 34.91 ? 643 HOH D O   1 
HETATM 9592 O  O   . HOH CA 5 .   ? -5.409  -10.025 -45.135 1.00 34.35 ? 644 HOH D O   1 
HETATM 9593 O  O   . HOH CA 5 .   ? 8.644   -13.762 -29.627 1.00 40.79 ? 645 HOH D O   1 
HETATM 9594 O  O   . HOH CA 5 .   ? -2.496  -14.187 -26.210 1.00 36.09 ? 646 HOH D O   1 
# 
